uniProtId	entrezGeneId	mutagenesis	GObiolProcess	GObiolProcessId	GOmolFunction	GOmolFunctionId	GOcellComponent	GOcellComponentId	extUniProtIds	dbSNP	mutPolyFlag
A0AVK6	79733	<ul><li>R->A at 156: Loss of DNA-binding and inhibition of E2F1-dependent activation</li><li>R->A at 314: Loss of DNA-binding and inhibition of E2F1-dependent activation</li></ul>			DNA-binding	GO:0003677			<li>Q01094</li><li>Q90977</li><li>Q27368</li>		1
A0AVT1	55236	<ul><li>C->A,S at 625: Impairs ubiquitin activation</li></ul>							<li>P69326</li><li>P08565</li><li>P69322</li><li>P69323</li><li>P69324</li><li>P69325</li><li>P68196</li><li>O46543</li><li>P68197</li><li>Q05550</li><li>P68198</li><li>P68199</li><li>P19848</li><li>P42739</li><li>P68195</li><li>Q867C2</li><li>P62991</li><li>P62990</li><li>P61863</li><li>P61864</li><li>P61862</li><li>Q867C4</li><li>Q867C3</li><li>P23398</li><li>P68204</li><li>P84589</li><li>Q865C5</li><li>P42740</li><li>P68201</li><li>Q8MKD1</li><li>P14792</li><li>P63049</li><li>P0C072</li><li>P63051</li><li>P69308</li><li>P69309</li><li>P20685</li><li>P15174</li><li>P62976</li><li>P62977</li><li>P62974</li><li>P62975</li><li>P62972</li><li>P13117</li><li>P14624</li><li>P62973</li><li>P46574</li><li>P69310</li><li>P69313</li><li>P69314</li><li>P69311</li><li>P08618</li><li>P69312</li><li>P69317</li><li>P69318</li><li>P69315</li><li>P0C014</li><li>P69316</li><li>P59263</li><li>P69319</li><li>P49634</li><li>P49635</li><li>Q9Y848</li><li>P22589</li><li>P62988</li><li>P62989</li><li>P69321</li><li>P23324</li><li>P69320</li><li>P59669</li>		1
A6H8Y1	55814	<ul><li>S->A at 390: Not phosphorylated by CSNK2A1; when associated with A-426; A-431; A-437 and A-446. CK2 treatment constituvely activates for U6 transcription; when associated with A-426; A-431; A-437 and A-446</li><li>S->A at 426: Not phosphorylated by CSNK2A1; when associated with A-390; A-431; A-437 and A-446. CK2 treatment constituvely activates for U6 transcription; when associated with A-390; A-431; A-437 and A-446</li><li>S->A at 431: Not phosphorylated by CSNK2A1; when associated with A-390; A-426; A-437 and A-446. CK2 treatment constituvely activates for U6 transcription; when associated with A-390; A-426; A-437 and A-446</li><li>T->A at 437: Not phosphorylated by CSNK2A1; when associated with A-390; A-426; A-431 and A-446. CK2 treatment constituvely activates for U6 transcription; when associated with A-390; A-426; A-431 and A-446</li><li>S->A at 446: Not phosphorylated by CSNK2A1; when associated with A-390; A-426; A-431 and A-437. CK2 treatment constituvely activates for U6 transcription; when associated with A-390; A-426; A-431 and A-437</li></ul>	transcription	GO:0006350					<li>Q65ZV5</li><li>P33674</li><li>P21868</li><li>P43893</li><li>O51759</li><li>P68399</li><li>P68400</li>		1
A7KAX9	9743	<ul><li>Y->A at 173: Loss of binding to phospholipids. Cytoplasmic localization</li><li>R->A at 407: Mild effect on GAP activity and neurite-promotion upon nerve growth factor stimulation</li><li>R->I at 407: Loss of GAP activity</li><li>R->M at 407: Loss of GAP activity. In isoform 1, no inhibitory effect on neurite extension</li><li>K->A at 447: Loss of GAP activity</li></ul>	localization	GO:0051179	binding	GO:0005488			<li>Q92263</li><li>P20936</li><li>Q92211</li><li>P09851</li><li>Q5PEA9</li><li>P74873</li><li>P74851</li><li>P50904</li>		1
A8K4G0	124599	<ul><li>K->L at 158: Abolishes interaction with TYROBP, and strongly reduces activation properties</li><li>Y->F at 188: No effect on interaction with TYROBP, but strongly reduces activation properties</li></ul>							<li>Q95J79</li><li>Q9TU45</li><li>Q8WNQ8</li><li>O43914</li>		1
O00115	1777	<ul><li>C->A at 19: Loss of activity</li><li>N->Q at 86: Reduced N-glycosylation, complete loss of N-glycosylation; when associated with Q-212; Q-266 and Q-290</li><li>C->A at 151: Loss of activity</li><li>C->A at 159: Loss of activity</li><li>N->Q at 212: Reduced N-glycosylation, complete loss of N-glycosylation; when associated with Q-86; Q-266 and Q-290</li><li>N->Q at 266: Reduced N-glycosylation, complete loss of N-glycosylation; when associated with Q-86; Q-212 and Q-290</li><li>C->A at 267: Loss of activity</li><li>N->Q at 290: Reduced N-glycosylation, complete loss of N-glycosylation; when associated with Q-86; Q-212 and Q-266</li><li>H->A,K,N,R,S at 295: Loss of activity, but not of DNA-binding</li><li>C->A at 299: No effect</li><li>C->A at 308: Loss of activity</li><li>C->A at 327: Loss of activity</li><li>C->A at 347: Loss of activity</li></ul>			DNA-binding	GO:0003677					1
O00141	6446	<ul><li>K->M at 127: Abolishes enzymatic activity</li><li>T->A at 256: Low activity</li><li>T->D at 256: Low activity</li><li>T->E at 256: Low activity</li><li>Y->A at 298: Abolishes interaction with NEDD4 and NEDD4L</li><li>S->A at 422: Low activity</li><li>S->D at 422: 10-fold activation</li></ul>							<li>Q5RBF2</li><li>Q96PU5</li><li>P46934</li>		1
O00180	3775	<ul><li>T->A at 161: No effect on channel activity</li></ul>									1
O00187	10747	<ul><li>Y->A at 74: Strongly decreases affinity for MBL2. Decreases affinity for FCN2</li><li>Y->A at 121: Strongly decreases affinity for MBL2, but not for FCN2</li><li>E->A at 124: Decreases affinity for MBL2. Slight decrease in affinity for FCN2</li></ul>							<li>Q15485</li><li>Q66S41</li><li>Q66S50</li><li>Q66S60</li><li>Q66S61</li><li>Q66S62</li><li>Q66S63</li><li>Q66S54</li><li>Q66S65</li><li>Q66S37</li><li>Q66S64</li><li>P11226</li><li>Q66S45</li><li>Q66S58</li>		1
O00204	6820	<ul><li>Missing at 1-23: Loss of the cholesterol sulfotransferase activity</li><li>Missing at 1-18: Increases the cholesterol sulfotransferase activity</li><li>D->A at 19: Increases the cholesterol sulfotransferase activity</li><li>I->A at 20: Loss of the cholesterol sulfotransferase activity</li><li>S->A at 21: Increases the cholesterol sulfotransferase activity</li><li>E->A at 22: Increases the cholesterol sulfotransferase activity</li><li>I->A at 23: Loss of the cholesterol sulfotransferase activity</li></ul>			sulfotransferase activity	GO:0008146					1
O00206	7099	<ul><li>N->A at 526: Abolishes LPS-response and prevents the cell surface expression</li><li>N->A at 575: Abolishes LPS-response and prevents the cell surface expression</li><li>E->R at 697: Abolishes LPS-response</li><li>R->E at 710: Abolishes LPS-response</li><li>D->K at 711: Abolishes LPS-response</li><li>P->H,R,E at 714: Abolishes MYD88-binding and LPS-response</li></ul>			binding	GO:0005488	cell surface	GO:0009928,GO:0009986	Q99836		1
O00221	4794	<ul><li>K->R at 145: No effect</li><li>S->A at 157: No degradation</li><li>S->A at 161: No degradation</li></ul>									1
O00254	2151	<ul><li>T->P at 39: No proteolytic cleavage by thrombin</li><li>F->A at 40: Altered signal upon thrombin cleavage</li></ul>							P84122		1
O00267	6829	<ul><li>R->A at 681: Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-696 and A-698</li><li>R->K at 681: Increases promoter association and enhances transcriptional elongation; when associated with K-696 and K-698</li><li>R->A at 696: Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-681 and A-698</li><li>R->K at 696: Increases promoter association and enhances transcriptional elongation; when associated with K-681 and K-698</li><li>R->A at 698: Enhances transcriptional elongation. Enhances interactions with CDK9 and RNA polymerase II and enhances transcriptional elongation; when associated with A-681 and A-696</li><li>R->K at 698: Increases promoter association and enhances transcriptional elongation; when associated with K-681 and K-696</li><li>G->D at 1002: Defective in regulation of transcriptional elongation</li></ul>							<li>Q5EAB2</li><li>Q5ZKN1</li><li>P50750</li>		1
O00291	3092	<ul><li>K->E at 56: Abolishes 3-phosphoinositide-binding; when associated with GLU-58</li><li>K->E at 58: Abolishes 3-phosphoinositide-binding; when associated with GLU-56</li><li>F->G at 432: Abolishes HIP1-induced cell death</li><li>R->E at 1005: Reduces AR-induced nuclear translocation</li></ul>	cell death	GO:0008219	phosphoinositide-binding	GO:0035091			<li>O00291</li><li>P06775</li>		1
O00300	4982	<ul><li>Missing at 400-401: Abolishes dimerization</li><li>C->S at 400: Abolishes dimerization</li></ul>									1
O00327	406	<ul><li>S->A,E at 9: Enhanced PER1 reporter activity by CLOCK-ARNTL</li><li>S->F at 9: 2-2.5-fold increase in CLOCK-BMAL1 transcriptional activity in the absence of CRY1. No change in repression activity in the presence of CRY1</li><li>S->A,E at 10: Enhanced PER1 reporter activity by CLOCK-ARNTL</li><li>S->L at 10: 2-2.5-fold increase in CLOCK-ARNTL transcriptional activity in the absence of CRY1. No change in repression activity in the presence of CRY1</li><li>A->S,T at 611: Increased desensitization to CRY1, in the presence of CLOCK. Approximately 2-fold increase in CLOCK-ARNTL transcriptional activity in the absence of CRY1; when associated with E-407</li><li>G->E at 612: Increased desensitization to CRY1, in the presence of CLOCK. Approximately 2-fold increase in CLOCK-ARNTL transcriptional activity in the absence of CRY1</li></ul>							<li>Q96506</li><li>Q5R4T2</li><li>Q70AD6</li><li>Q9I8T7</li><li>O61734</li><li>O61735</li><li>Q00925</li><li>Q8QG61</li><li>Q5IZC5</li><li>P27069</li><li>Q8K3T3</li><li>O04005</li><li>Q43125</li><li>O00327</li><li>Q6YGZ5</li><li>Q6YGZ4</li><li>P06367</li><li>Q5RAK8</li><li>Q16526</li><li>O88529</li><li>P52572</li><li>Q6ZZY0</li><li>Q91YA9</li><li>O15516</li><li>O15534</li><li>Q8WP19</li><li>Q8QGQ6</li><li>P25625</li><li>P46295</li>		1
O00329	5293	<ul><li>R->P at 894: Abolishes lipid and protein kinase activities</li><li>S->A at 1039: Abolishes autophosphorylation, no effect on lipid kinase activity</li><li>S->D,E at 1039: Abolishes autophosphorylation, reduced lipid kinase activity</li></ul>	autophosphorylation	GO:0046777	lipid kinase activity	GO:0001727			<li>P00513</li><li>P25848</li>		1
O00330	8050	<ul><li>R->A at 183: Strongly decreased DLD binding</li><li>S->A at 185: Strongly decreased DLD binding</li><li>P->A at 186: Strongly decreased DLD binding</li><li>A->M at 187: Strongly decreased DLD binding</li><li>R->A at 189: Strongly decreased DLD binding</li><li>N->A at 190: Strongly decreased DLD binding</li><li>E->A at 193: Strongly decreased DLD binding</li><li>R->A at 208: Strongly decreased DLD binding</li><li>I->A at 210: Strongly decreased DLD binding</li><li>K->A at 213: Strongly decreased DLD binding</li><li>E->A at 214: Strongly decreased DLD binding</li></ul>			binding	GO:0005488			<li>Q60HG3</li><li>Q86WU2</li><li>Q7TNG8</li><li>Q5R4B1</li><li>P49819</li><li>P32891</li><li>P09622</li><li>Q8CIZ7</li><li>Q12627</li><li>P09623</li>		1
O00429	10059	<ul><li>K->A at 38: Impairs mitochondrial division and induces changes in peroxisome morphology</li><li>K->E at 38: Overexpression delays protein secretion</li><li>S->I at 39: Decreased localization to the perinuclear region</li><li>S->N at 39: Reduces peroxisomal abundance</li><li>V->F at 41: Temperature-sensitive. Impairs mitochondrial division</li><li>T->A at 59: Impairs mitochondrial division. Reduces peroxisomal abundance</li><li>G->D at 281: Temperature-sensitive. Impairs mitochondrial division</li></ul>	<li>protein secretion</li><li>mitochondrial division</li><li>localization</li>	<li>GO:0009306</li><li>GO:0000266</li><li>GO:0051179</li>			peroxisome	GO:0005777			1
O00443	5286	<ul><li>LLLDD->AAAAA at 103-107: Reduces clathrin binding</li><li>S->A at 254: No effect on phosphorylation in vitro</li><li>S->A,D,E at 259: Abolishes phosphorylation, no change in activity</li><li>S->A at 259: Protects from proteolysis</li><li>S->A at 262: No effect on phosphorylation in vitro</li><li>S->A at 266: No effect on phosphorylation in vitro</li><li>R->A at 1488: Reduces affinity for PtdIns(4,5)P2-containing membranes 7-fold</li><li>V->A at 1490: Reduces affinity for PtdIns(4,5)P2-containing membranes 7-fold</li><li>L->A at 1491: Reduces affinity for PtdIns(4,5)P2-containing membranes 5-fold</li><li>R->A at 1493: Reduces affinity for PtdIns(4,5)P2-containing membranes 23-fold</li><li>R->A at 1503: Abolishes interaction with PtdIns(4,5)P2-containing membranes</li></ul>	phosphorylation	GO:0016310	clathrin binding	GO:0030276	membranes	GO:0016020			1
O00482	2494	<ul><li>Y->A at 96: Slightly reduced DNA binding. Strongly reduced transactivation; when associated with A-168 and A-172</li><li>F->A at 168: Slightly reduced DNA binding. Strongly reduced transactivation; when associated with A-96 and A-172</li><li>GP->VA at 169-170: Reduced DNA binding. Loss of transactivation</li><li>Y->A at 172: Slightly reduced DNA binding. Strongly reduced transactivation; when associated with A-96 and A-168</li><li>F->W at 342: Reduced phospholipid binding. Strongly reduced transactivation; when associated with W-416</li><li>I->W at 416: Reduced phospholipid binding. Strongly reduced transactivation; when associated with W-342</li></ul>			<li>phospholipid binding</li><li>DNA binding</li>	<li>GO:0005543</li><li>GO:0003677</li>					1
O00506	10494	<ul><li>K->R at 49: Loss of kinase activity and autophosphorylation</li><li>D->A at 158: Loss of kinase activity</li></ul>	autophosphorylation	GO:0046777	kinase activity	GO:0016301					1
O00562	9600	<ul><li>T->A at 59: Prevents association with lipid droplets</li><li>T->E at 59: Causes association with lipid droplets</li><li>T->A at 287: Slightly reduced phosphorylation. Strongly reduced phosphorylation; when associated with A-794 or A-389. Loss of threonine phosphorylation; when associated with A-389; A-793 and A-1222</li><li>S->A at 300: No effect on phosphorylation</li><li>S->A at 326: No effect on phosphorylation</li><li>EFFDA->ALLAG at 349-353: Loss of interaction with VAPB</li><li>S->A at 382: Strongly reduced phosphorylation</li><li>T->A at 389: No detectable effect on phosphorylation; when associated with A-793 and A-1222. Strongly reduced phosphorylation; when associated with A-287. Loss of threonine phosphorylation; when associated with A-287; A-794 and A-1222</li><li>T->A at 794: No detectable effect on phosphorylation; when associated with A-389 and A-1222. Strongly reduced phosphorylation; when associated with A-287. Loss of threonine phosphorylation; when associated with A-287; A-389 and A-1222</li><li>S->A at 896: Reduced phosphorylation</li><li>T->A at 1223: No detectable effect on phosphorylation; when associated with A-389 and A-793. Loss of threonine phosphorylation; when associated with A-287; A-389 and A-794</li></ul>	phosphorylation	GO:0016310			lipid droplets	GO:0005811	<li>O95292</li><li>Q25691</li>		1
O00571	1654	<ul><li>K->E at 230: Abolishes ATPase activity and RNA-unwinding activity</li><li>S->L at 382: Abolishes ATPase activity and RNA-unwinding activity</li></ul>			ATPase activity	GO:0016887					1
O00623	5193	<ul><li>C->W at 304: Abolishes interaction with PEX19; when associated with Q-307</li><li>C->Q at 307: Abolishes interaction with PEX19; when associated with W-304</li></ul>							<li>P40855</li><li>Q60415</li><li>Q3SZD1</li><li>Q5R7U2</li><li>Q07418</li>		1
O00762	11065	<ul><li>C->S at 114: Inhibition of cyclin B degradation</li></ul>							<li>P04961</li><li>P22177</li><li>O16852</li><li>Q00268</li><li>Q00265</li><li>P24314</li><li>P61074</li><li>P17070</li><li>P17917</li><li>P18248</li><li>P31008</li><li>P17918</li><li>P53358</li><li>O01377</li><li>P12004</li>		1
O14497	8289	<ul><li>W->A at 1073: Partial loss of DNA-binding activity. Complete loss of activity; when associated with A-1096</li><li>Y->A at 1096: Partial loss of DNA-binding activity. Complete loss of activity; when associated with A-1073</li></ul>			DNA-binding	GO:0003677					1
O14512	30837	<ul><li>RDS->KDC at 425-427: Loss of IRS1 ubiquitination and degradation</li></ul>							<li>Q28224</li><li>P35568</li><li>P09715</li>		1
O14543	9021	<ul><li>L->A,F at 22: Little effect on EPO-induced STAT5 signaling suppression</li><li>L->D at 22: Complete loss of EPO-induced STAT5 signaling suppression. No suppression of JAK2 phosphorylation</li><li>F->A at 25: Complete loss of EPO-induced STAT5 signaling suppression. Abolishes binding to JH1</li><li>E->R at 30: Partial loss of EPO-induced STAT5 signaling suppression. No effect on LIF-induced signaling suppression. Abolishes binding to JH1. Inhibits JAK2 phosphorylation</li><li>Y->A at 31: Complete loss of EPO-induced STAT5 signaling suppression. No effect on LIF-induced STAT3 signaling. Abolishes binding to JH1</li><li>Y->F at 31: Little effect on EPO-induced signaling suppression</li><li>V->E at 34: Complete loss of EPO/LIF-induced signaling suppression</li><li>L->R at 41: Complete loss of EPO/LIF-induced signaling inhibition. Abolishes binding to JH1</li><li>G->A at 45: Little effect on EPO/LIF signaling</li><li>G->V at 53: No effect on binding to Y429/Y431 phosphorylated EPOR</li><li>L->A at 58: Impaired binding to Y429/Y431 phosphorylated EPOR</li><li>R->E at 71: Complete loss of EPO/LIF-induced signaling suppression. No inhibition of JAK2 phosphorylation</li><li>R->K at 71: No effect on EPO/LIF-induced signaling suppression. Partial suppression of JAK2 phosphorylation. No effect on binding to JH1. Loss of binding to IL12RB2</li><li>L->A at 93: Impaired binding to Y429/Y431 phosphorylated EPOR</li><li>R->E at 94: Greatly impaired binding to Y429/Y431 phosphorylated EPOR</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488			<li>Q27956</li><li>Q8MJS1</li><li>P17777</li><li>P61635</li><li>P07865</li><li>P42229</li><li>P49157</li><li>P09056</li><li>Q6H8T2</li><li>Q6H8T1</li><li>Q99665</li><li>O60674</li><li>Q28513</li><li>Q2KL21</li><li>Q9BEG2</li><li>Q9MYZ9</li><li>O62728</li><li>P49290</li><li>P33709</li><li>P42231</li><li>P15018</li><li>Q9GKA2</li><li>P19235</li><li>Q867B1</li><li>P48617</li><li>P33707</li><li>P33708</li><li>P11678</li><li>P80550</li><li>P01588</li><li>Q6H8S9</li><li>P40763</li>		1
O14613	10435	<ul><li>HTIH->ATIA at 39-42: No binding with CDC42; no induced pseudopodia formation</li></ul>			binding	GO:0005488			<li>Q90694</li><li>O94103</li><li>O14426</li><li>P60953</li><li>Q17031</li><li>P60952</li><li>Q9HF56</li><li>P19073</li>		1
O14618	9973	<ul><li>C->S at 22: Reduces copper binding by half; when associated with S-25. Negligible effect on zinc binding</li><li>C->S at 25: Reduces copper binding by half; when associated with S-22. Negligible effect on zinc binding</li><li>C->S at 244: Reduces copper binding by half; when associated with S-246. Negligible effect on zinc binding</li><li>C->S at 246: Reduces copper binding by half; when associated with S-244. Negligible effect on zinc binding</li></ul>			<li>copper binding</li><li>zinc binding</li>	<li>GO:0005507</li><li>GO:0008270</li>					1
O14649	3777	<ul><li>H->N at 98: Greatly reduces pH sensitivity</li></ul>									1
O14654	8471	<ul><li>Y->F at 700: No effect. Reduces interaction with CRK by 50%; when associated with F-717. Abolishes interaction with CRK; when associated with F-717; F-743 and F-779</li><li>Y->F at 717: No effect. Reduces interaction with CRK by 50%; when associated with F-700. Abolishes interaction with CRK; when associated with F-700; F-743 and F-779</li><li>Y->F at 743: No effect. Reduces interaction with CRK by 50%; when associated with F-779. Abolishes interaction with CRK; when associated with F-700; F-717 and F-779</li><li>Y->F at 779: No effect. Reduces interaction with CRK by 50%; when associated with F-743. Abolishes interaction with CRK; when associated with F-700; F-717 and F-743</li></ul>							<li>Q04929</li><li>Q01917</li><li>P54664</li><li>P53681</li><li>P46108</li>		1
O14713	9270	<ul><li>T->D at 38: Changes in cell spreading</li><li>L->A at 82: Decrease in binding to beta 1 integrin; when associated with T-144 no binding to beta 1 integrin</li><li>L->Q at 82: No change in binding to beta 1 integrin</li><li>L->Q at 86: No change in binding to beta 1 integrin; when associated with T-144 no binding to beta 1 integrin</li><li>L->A at 135: No binding to beta 1 integrin</li><li>I->A at 138: No binding to beta 1 integrin</li><li>I->A at 139: No binding to beta 1 integrin</li><li>Y->T at 144: No binding to beta 1 integrin</li></ul>			binding	GO:0005488					1
O14727	317	<ul><li>K->R at 160: No association with APAF-1. No binding to pro-caspase-9</li><li>M->L at 368: Activation of pro-caspase-9 independent of cytochrome c. Increased ability to induce apoptosis</li></ul>	apoptosis	GO:0006915	binding	GO:0005488			<li>P00073</li><li>P00074</li><li>P00075</li><li>P00076</li><li>P00070</li><li>P00071</li><li>P00072</li><li>Q6C9Q0</li><li>P00067</li><li>P00066</li><li>P00069</li><li>P00068</li><li>P68100</li><li>P00064</li><li>P00065</li><li>P00062</li><li>P00063</li><li>P00060</li><li>P00061</li><li>P67881</li><li>P67882</li><li>Q6WUX8</li><li>P15451</li><li>Q6QLW4</li><li>P19681</li><li>P00059</li><li>P00058</li><li>P00057</li><li>P68517</li><li>P00056</li><li>P68518</li><li>P68519</li><li>P00055</li><li>P62773</li><li>P62772</li><li>Q7YR71</li><li>Q4HVX7</li><li>P00008</li><li>P00007</li><li>P32556</li><li>P00004</li><li>P00003</li><li>Q640U4</li><li>P00002</li><li>Q753F4</li><li>P99999</li><li>P99998</li><li>Q52V08</li><li>Q52V09</li><li>P00079</li><li>P00078</li><li>P00077</li><li>O13393</li><li>P81459</li><li>P00030</li><li>Q5RFH4</li><li>P00032</li><li>P00031</li><li>Q52V10</li><li>O93863</li><li>P00027</li><li>P00028</li><li>P12831</li><li>P00029</li><li>P68096</li><li>P00022</li><li>P68097</li><li>P68098</li><li>P00024</li><li>P62896</li><li>P68099</li><li>P81280</li><li>P00025</li><li>P62895</li><li>P62894</li><li>Q6Q4H8</li><li>P18822</li><li>P00021</li><li>P00020</li><li>P00017</li><li>P38091</li><li>P00018</li><li>P00013</li><li>P00014</li><li>P00011</li><li>O07091</li><li>P00012</li><li>P53698</li><li>P00019</li><li>O22642</li><li>P25400</li><li>P22342</li><li>P00052</li><li>P00051</li><li>P00054</li><li>P00053</li><li>P00046</li><li>Q96VP3</li><li>P00047</li><li>P00048</li><li>P00049</li><li>Q41346</li><li>P19974</li><li>P21665</li><li>P56205</li><li>P00043</li><li>P00042</li><li>P00041</li><li>Q6IQM2</li><li>P00040</li><li>P00035</li><li>P00036</li><li>P00039</li><li>P00037</li><li>P29380</li><li>P00038</li><li>P59218</li>		1
O14744	10419	<ul><li>GR->AA at 367-368: Abolishes enzymatic activity</li></ul>									1
O14745	9368	<ul><li>F->R at 355: Loss of MSX binding</li><li>Missing at 358: Reduces MSX binding</li></ul>			binding	GO:0005488					1
O14746	7015	<ul><li>D->A at 712: Loss of telomerase activity</li><li>DD->AA at 868-869: Loss of telomerase activity</li><li>D->A at 868: Loss of telomerase activity</li><li>D->A at 869: Loss of telomerase activity</li></ul>			telomerase activity	GO:0003720					1
O14757	1111	<ul><li>K->R at 38: Abolishes kinase activity</li><li>D->A at 130: Abolishes kinase activity</li><li>S->A at 317: Abrogates interaction with RAD51; when associated with A-345. Reduces phosphorylation and impairs activation by hydroxyurea and ionizing radiation. Abrogates nuclear retention upon checkpoint activation</li><li>S->E at 317: Enhances interaction with RAD51; when associated with E-345</li><li>F->A at 344: Impairs nuclear export</li><li>S->A at 345: Abrogates interaction with RAD51; when associated with A-317. Reduces phosphorylation and impairs activation by hydroxyurea and ionizing radiation. Impairs interaction with YWHAZ which is required for nuclear retention after checkpoint activation</li><li>S->E at 345: Enhances interaction with RAD51; when associated with E-317</li><li>M->A at 353: Impairs nuclear export</li><li>S->A at 357: No effect on phosphorylation induced by hydroxyurea</li><li>S->A at 366: No effect on phosphorylation induced by hydroxyurea</li><li>S->A at 468: No effect on phosphorylation induced by hydroxyurea</li></ul>	<li>phosphorylation</li><li>nuclear export</li>	<li>GO:0016310</li><li>GO:0051168</li>	kinase activity	GO:0016301			<li>Q5ZKC9</li><li>P94102</li><li>Q2KJ94</li><li>Q8MKI8</li><li>P37383</li><li>P70099</li><li>Q40134</li><li>P63103</li><li>P29361</li><li>O77507</li><li>Q99133</li><li>Q5R651</li><li>P25454</li><li>Q06609</li><li>P63104</li>		1
O14773	1200	<ul><li>H->A at 236: No effect</li><li>D->A at 360: Inactive. Impaired processing</li><li>S->A at 475: Inactive. Impaired processing</li><li>D->A at 517: Inactive. Impaired processing</li></ul>									1
O14776	10915	<ul><li>YYY->AAA at 148-150: Reduces repression of transcription by 35%. Reduces repression of transcription by 63%; when associated with 446-AAA-448</li><li>YYY->AAA at 446-448: Loss of interaction with SF1. Reduces repression of transcription by 35%. Reduces repression of transcription by 63%; when associated with 148-AAA-150</li><li>FFY->AAA at 545-547: No effect</li></ul>	transcription	GO:0006350					<li>Q9GKL2</li><li>Q95L87</li><li>Q13285</li><li>Q12186</li><li>Q15637</li>		1
O14777	10403	<ul><li>E->K at 234: Abrogates binding to RB1</li></ul>			binding	GO:0005488			P06400		1
O14827	5924	<ul><li>S->A at 737: Loss of phosphorylation by CDK5</li></ul>	phosphorylation	GO:0016310					<li>Q02399</li><li>Q00535</li>		1
O14920	3551	<ul><li>K->A at 44: Loss of kinase activity and no effect on binding to NIK</li><li>S->A at 177: Decrease of activity</li><li>S->E at 177: Full activation</li><li>S->A at 181: Decrease of activity</li><li>S->E at 181: Full activation</li></ul>			<li>binding</li><li>kinase activity</li>	<li>GO:0005488</li><li>GO:0016301</li>			<li>O95819</li><li>Q99558</li>		1
O14940	4337										1
O14950	103910	<ul><li>TS->AA at 19-20: Shows a decrease in the number of actin filament bundles</li><li>TS->DD at 19-20: Shows a larger number of actin filament bundles</li></ul>							<li>Q92192</li><li>Q92193</li><li>P53499</li><li>P26183</li><li>P53498</li><li>O13419</li><li>Q9P4D1</li><li>P48465</li><li>P53455</li><li>Q39596</li><li>Q39758</li><li>P26182</li><li>P80709</li><li>Q9UVX4</li><li>O17320</li><li>P53689</li><li>P78711</li><li>P30161</li><li>P17128</li><li>P45521</li><li>P45520</li><li>P20904</li><li>P81085</li><li>Q6TCF2</li><li>Q99023</li><li>Q75D00</li><li>P51775</li><li>P10365</li><li>P60011</li><li>P60010</li><li>Q8SWN8</li><li>O16808</li><li>P02577</li><li>P10989</li><li>P68555</li><li>Q05214</li><li>Q8X119</li><li>O65316</li><li>O65315</li><li>O65314</li><li>P53491</li><li>P91754</li><li>P13363</li><li>P11426</li><li>O81221</li><li>Q11212</li><li>P50138</li><li>P53477</li><li>P53476</li><li>P60009</li><li>P53502</li><li>Q2U7A3</li><li>P53500</li><li>Q9UVZ8</li><li>P14235</li><li>O00937</li><li>Q9UVF3</li><li>Q24733</li><li>P90689</li><li>P24902</li><li>O74258</li>		1
O14964	9146	<ul><li>A->Q at 266: Strongly reduced ubiquitin-binding. Reduced degradation of ubiquitinated EGFR</li><li>A->Q at 268: Strongly reduced ubiquitin-binding. Reduced degradation of ubiquitinated EGFR</li></ul>			binding	GO:0005488			<li>P69326</li><li>P08565</li><li>P69322</li><li>P69323</li><li>P69324</li><li>P69325</li><li>P68196</li><li>O46543</li><li>P68197</li><li>P13387</li><li>Q05550</li><li>P68198</li><li>P68199</li><li>P19848</li><li>P42739</li><li>P68195</li><li>Q867C2</li><li>P62991</li><li>P62990</li><li>P61863</li><li>P61864</li><li>P61862</li><li>Q867C4</li><li>Q867C3</li><li>P23398</li><li>P68204</li><li>P84589</li><li>P55245</li><li>Q865C5</li><li>P42740</li><li>P68201</li><li>Q8MKD1</li><li>P14792</li><li>P63049</li><li>P0C072</li><li>P63051</li><li>P69308</li><li>P69309</li><li>P20685</li><li>P15174</li><li>P62976</li><li>P62977</li><li>P62974</li><li>P62975</li><li>P62972</li><li>P13117</li><li>P14624</li><li>P62973</li><li>P46574</li><li>P69310</li><li>P69313</li><li>P69314</li><li>P69311</li><li>P08618</li><li>P69312</li><li>P69317</li><li>P69318</li><li>P69315</li><li>P0C014</li><li>P69316</li><li>P59263</li><li>P69319</li><li>P49634</li><li>P49635</li><li>Q9Y848</li><li>P22589</li><li>P62988</li><li>P62989</li><li>P00533</li><li>P69321</li><li>P23324</li><li>P69320</li><li>P59669</li>		1
O14979	9987	<ul><li>G->A at 404: Reduces significantly its nuclear localization</li></ul>	localization	GO:0051179							1
O14980	7514	<ul><li>S->A at 191: Does not abolish Rex-mediated mRNA export</li><li>V->E at 284: Does not abolish Rex-mediated mRNA export</li><li>D->G at 334: Does not abolish Rex-mediated mRNA export</li><li>I->L at 337: Does not abolish Rex-mediated mRNA export</li><li>T->A at 346: Does not abolish Rex-mediated mRNA export</li><li>V->I at 402: Does not abolish Rex-mediated mRNA export</li><li>P->T at 411: Strongly abolishes interaction with Rex and RANBP3, abolishes Rex-mediated mRNA export. Does not abolish interaction with RANBP3; when associated with S-414. Abolishes Rex multimerization; when associated with S-414</li><li>M->V at 412: Does not abolish interaction with Rex and RANBP3, and Rex-mediated mRNA export</li><li>F->S at 414: Strongly abolishes interaction with Rex and RANBP3, abolishes Rex-mediated mRNA export. Does not abolish interaction with RANBP3; when associated with T-411. Abolishes Rex multimerization; when associated with T-411</li><li>EEVLVVENDQGEVVR at 428-447: Abolishes Ran binding activity in absence of cargo and abolishes partially Ran binding activity in presence of cargo</li><li>VLVVENDQGEVVREF at 430-446: Partially restores Ran binding activity in presence of cargo</li><li>VLVV->DEDE at 430-433: Abolishes Ran binding activity both in absence or presence of cargo</li><li>Y->A at 454: Does not abolish Ran binding activity and nuclear export complex formation</li><li>R->I at 474: Strongly abolishes interaction with Rex and RANBP3, abolishes Rex-mediated mRNA export</li><li>H->Q at 481: Strongly abolishes interaction with Rex and RANBP3, abolishes Rex-mediated mRNA export</li><li>E->A at 513: Abolishes Ran binding activity and nuclear export complex formation. Abolishes Ran binding activity and nuclear export complex formation; when associated with A-553 and A-554</li><li>L->A at 525: Enhances Ran binding activity and does not abolish nuclear export complex formation. Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-561. Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-568 and A-572</li><li>Q->A at 550: Enhances Ran binding activity and does not abolish nuclear export complex formation; when associated with A-553 and A-590</li><li>R->A at 553: Enhances Ran binding activity and does not abolish nuclear export complex formation; when associated with A-550 and A-590. Abolishes Ran binding activity and nuclear export complex formation; when associated with A-513 and A-554</li><li>F->A at 554: Partially abolishes Ran binding activity and does not abolish nuclear export complex formation. Abolishes Ran binding activity and nuclear export complex formation; when associated with A-561. Abolishes Ran binding activity and nuclear export complex formation; when associated with A-553 and A-513</li><li>F->A at 561: Abolishes Ran binding activity and nuclear export complex formation. Abolishes Ran binding activity and nuclear export complex formation; when associated with A-554. Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-525</li><li>K->A at 568: Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-525 and A-572</li><li>F->A at 572: Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-525 and A-568</li><li>M->A at 583: Enhances Ran binding activity; when associated with A-590</li><li>K->A at 590: Enhances Ran binding activity and does not abolish nuclear export complex formation. Enhances Ran binding activity and does not abolish nuclear export complex formation; when associated with A-583. Enhances Ran binding activity and does not abolish nuclear export complex formation; when associated with A-550 and A-553</li></ul>	nuclear export	GO:0051168	binding	GO:0005488			<li>Q5R4Y2</li><li>Q9H6Z4</li><li>Q4R4T9</li>		1
O15031	23654	<ul><li>RQKR->AQKA at 1161-1164: Abolishes cleavage by proprotein convertases</li></ul>									1
O15055	8864	<ul><li>S->D at 662: Restores CSNK1E-dependent phosphorylation of variant G-662</li></ul>	phosphorylation	GO:0016310					P49674		1
O15084	23243	<ul><li>SKTVS->AKTVA at 1040-1044: Marked decrease in phosphorylation. Increased PPP1C-binding. No effect on HNRPK-binding</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488			<li>Q3T0D0</li><li>O19049</li><li>P61978</li>		1
O15105	4092	<ul><li>K->A at 64: Loss of acetylation, and of SMURF1-dependent degradation; when associated with A-70</li><li>K->A at 70: Loss of acetylation, and of SMURF1-dependent degradation; when associated with A-64</li><li>Missing at 207-211: Diminishes interaction with SMURF2</li><li>Y->A at 211: Diminishes interaction with SMURF2 and reduces inhibition of TGF-beta signaling</li><li>Missing at 409-426: 90% reduction in TGF-beta receptor binding</li></ul>			TGF-beta receptor binding	GO:0005160			<li>Q9HCE7</li><li>Q9HAU4</li>		1
O15111	1147	<ul><li>T->A at 23: Loss of phosphorylation and decrease of kinase activity</li><li>K->A at 44: Loss of kinase activity</li><li>K->M at 44: Loss of autophosphorylation</li><li>S->A at 176: Loss of phosphorylation and of activity</li><li>S->E at 176: Full activation</li><li>T->A at 179: No change in phosphorylation</li><li>S->A at 180: No change in phosphorylation</li></ul>	<li>phosphorylation</li><li>autophosphorylation</li>	<li>GO:0016310</li><li>GO:0046777</li>	kinase activity	GO:0016301					1
O15118	4864	<ul><li>C->S at 63: Loss of function</li><li>C->S at 97: Loss of function</li></ul>									1
O15151	4194	<ul><li>C->G at 437: Fails to interact with MDM2</li></ul>							<li>Q60524</li><li>Q00987</li><li>P56950</li><li>Q7YRZ8</li><li>P56951</li>		1
O15162	5359	<ul><li>Y->F at 69: Decrease in phosphorylation</li><li>Y->F at 74: Decrease in phosphorylation</li><li>T->A at 161: No induction by PKC</li><li>D->A at 273: Reduces the Ca(2+)-dependent phospholipid scrambling</li><li>D->A at 275: Complete inactivation of the Ca(2+)-dependent phospholipid scrambling</li><li>F->A at 277: Reduces the Ca(2+)-dependent phospholipid scrambling</li><li>I->A at 279: Reduces the Ca(2+)-dependent phospholipid scrambling</li><li>F->A at 281: Complete inactivation of the Ca(2+)-dependent phospholipid scrambling</li><li>D->A at 284: Reduces the Ca(2+)-dependent phospholipid scrambling</li></ul>	<li>phospholipid scrambling</li><li>phosphorylation</li>	<li>GO:0017121</li><li>GO:0016310</li>					<li>P13678</li><li>P13677</li><li>P05130</li><li>P34722</li>		1
O15245	6580	<ul><li>G->A at 465: No changes in the MPP uptake</li></ul>							<li>Q6WEB5</li><li>P10522</li><li>P37301</li><li>P27573</li><li>P06907</li><li>P29677</li><li>P25189</li><li>P20938</li>		1
O15264	5603	<ul><li>T->A at 180: Loss of kinase activity</li><li>Y->A at 182: Loss of kinase activity</li></ul>			kinase activity	GO:0016301					1
O15297	8493	<ul><li>D->A at 314: Abrogates phosphatase activity</li></ul>							<li>Q5X1E5</li><li>Q7M7K5</li><li>Q7MAZ9</li><li>Q8XBL4</li><li>Q88A53</li><li>Q5P3T0</li><li>Q7MBF4</li><li>Q8Z3M9</li><li>Q5PC82</li><li>Q5ZRX9</li><li>Q821A6</li><li>Q87SK9</li><li>Q9JZ88</li><li>Q9CP21</li><li>Q82U82</li><li>Q9I5V3</li><li>Q5F8K9</li><li>Q63YC3</li><li>Q8Y395</li><li>Q6LV05</li><li>Q8ZLY4</li><li>Q6FA38</li><li>Q9PDL7</li><li>Q62EU1</li><li>Q9JUB2</li><li>Q5WT58</li><li>Q665U9</li><li>Q57JQ5</li><li>Q9KPC6</li><li>Q8P5D4</li><li>Q8CWL6</li><li>Q8PPG9</li><li>P06961</li><li>P45269</li><li>Q9L7A3</li><li>Q88QU2</li><li>Q6D160</li><li>Q8ZI64</li><li>Q60CQ4</li><li>Q87DS9</li><li>Q65Q41</li><li>Q5E2K7</li><li>Q8CXX6</li>		1
O15304	10572	<ul><li>Y->F at 34: Abolishes phosphorylation and apoptotic activity</li><li>Y->F at 53: No effect on phosphorylation or apoptotic activity</li></ul>	phosphorylation	GO:0016310							1
O15350	7161	<ul><li>Y->A at 487: Loss of interaction with WWOX</li><li>K->R at 627: Strongly diminishes sumoylation but does not affect transcriptional activity</li></ul>	sumoylation	GO:0016925					<li>Q5F389</li><li>Q5R9W5</li><li>Q9NZC7</li><li>Q9VLU5</li>		1
O15357	3636	<ul><li>R->G at 47: Abolishes interaction with p130Cas/BCAR1 and its ability to induce increased adhesion. Abolishes phosphorylation upon FCGR2A clustering</li><li>D->A at 607: Abolishes enzyme activity but not phosphorylation upon FCGR2A clustering</li><li>T->A at 958: Reduces PDGF-stimulated tyrosine phosphorylation and association with SHC1</li><li>YY->FF at 986-987: Inducer a strong reduction of phosphorylation upon re-plating on collagen I</li></ul>	phosphorylation	GO:0016310			collagen	GO:0005581	<li>P56945</li><li>P12318</li><li>Q8SPV8</li><li>P29353</li>		1
O15382	587	<ul><li>C->A at 342: Reduces activity about 6-fold</li><li>C->A at 345: Slight reduction of activity</li></ul>									1
O15392	332	<ul><li>T->A at 34: Loss of HBXIP binding</li><li>T->E at 34: Higher affinity for HBXIP binding</li><li>C->A at 84: Loss of cytoprotection</li></ul>			binding	GO:0005488			O43504		1
O15393	7113	<ul><li>R->Q at 255: Loss of cleavage</li><li>S->A at 441: Loss of activity</li></ul>									1
O15455	7098	<ul><li>C->A at 95: Reduced response to ds-RNA</li><li>C->A at 122: Reduced response to ds-RNA</li><li>N->G at 196: Reduced expression levels; when associated with R-247</li><li>N->R at 247: Reduced response to ds-RNA. Reduced expression levels; when associated with G-196</li><li>H->A at 539: No effect</li><li>H->E at 539: Loss of RNA binding. Constitutive activation of NF-kappa-B</li><li>N->A at 541: Loss of RNA binding. Abolishes activation of NF-kappa-B</li><li>Y->F at 759: Reduced activation of NF-kappa-B in response to ds-RNA. Reduced induction of IL-8 in response to ds-RNA</li></ul>			RNA binding	GO:0003723			<li>Q9XSX5</li><li>P26894</li><li>P36925</li><li>O62812</li><li>P79255</li><li>P08317</li><li>P67813</li><li>Q102R3</li><li>P67814</li><li>Q7YRB5</li><li>P19874</li><li>P49113</li><li>P46653</li><li>P10145</li><li>P41324</li>		1
O15488	8908	<ul><li>Y->F at 228: Loss of activity</li><li>Y->F at 230: No loss of activity</li></ul>									1
O15492	6004	<ul><li>Y->F at 168: 30% decrease in GAP activity</li><li>Y->F at 177: No effect on GAP activity</li></ul>							<li>Q92263</li><li>P20936</li><li>Q92211</li><li>P09851</li><li>Q5PEA9</li><li>P74873</li><li>P74851</li><li>P50904</li>		1
O15498	10652	<ul><li>F->E at 42: Increases palmitoylation. Targeted to Golgi membranes. Targeted to Golgi and cytosol; when associated with S-194. Targeted to cytosol; when associated with S-195</li><li>C->S at 194: Decreases palmitoylation by 55%. Prevents palmitoylation; when associated with S-195. Targeted to Golgi and cytosol; when associated with E-42</li><li>C->S at 195: Prevents farnesylation. Targeted to cytosol; when associated with E-42. Decreases palmitoylation by 13%. Prevents palmitoylation; when associated with S-194</li></ul>					<li>Golgi membranes</li><li>cytosol</li>	<li>GO:0000139</li><li>GO:0005829</li>			1
O15503	3638	<ul><li>K->R at 156: Loss of ubiquitination and degradation</li><li>K->R at 158: Loss of ubiquitination and degradation</li><li>D->A at 205: Loss of ability to suppress the cleavage of SREBP2 and to accelerate the degradation of HMGCR</li></ul>							<li>P16393</li><li>Q60429</li><li>Q5R6N3</li><li>P00347</li><li>Q1W675</li><li>Q12772</li><li>Q29512</li><li>P04035</li><li>P09610</li>		1
O15516	9575	<ul><li>E->K at 116: 3-fold increase in PER1 reporter activity by CLOCK-ARNTL. Some reduction of CRY1 inhibition of CLOCK-ARNTL transcriptional activity; when associated with K-367 and L-601</li><li>G->E at 332: 3-fold increase in PER1 reporter activity by CLOCK-ARNTL. Some reduction of CRY1 inhibition of CLOCK-ARNTL transcriptional activity; when associated with L-840</li><li>H->Y at 360: 3-fold increase in PER1 reporter activity by CLOCK-ARNTL. Some reduction of CRY1 inhibition of CLOCK-ARNTL transcriptional activity</li><li>E->K at 367: 3-fold increase in PER1 reporter activity by CLOCK-ARNTL. Some reduction of CRY1 inhibition CLOCK-ARNTL transcriptional activity; when associated with E-116 and L-601</li><li>V->L at 601: 3-fold increase in PER1 reporter activity by CLOCK-ARNTL. Some reduction of CRY1 inhibition of CLOCK-ARNTL transcriptional activity; when associated with K-116 and K-367</li><li>P->L at 840: 3-fold increase in PER1 reporter activity by CLOCK-ARNTL. Some reduction of CRY1 inhibition of CLOCK-ARNTL transcriptional activity; when associated with E-332</li></ul>							<li>Q96506</li><li>Q5R4T2</li><li>Q70AD6</li><li>Q9I8T7</li><li>O61735</li><li>Q00925</li><li>Q8QG61</li><li>Q5IZC5</li><li>P27069</li><li>Q8K3T3</li><li>O04005</li><li>Q43125</li><li>O00327</li><li>Q6YGZ5</li><li>Q6YGZ4</li><li>P06367</li><li>Q5RAK8</li><li>Q16526</li><li>O88529</li><li>P52572</li><li>Q6ZZY0</li><li>O15516</li><li>O15534</li><li>Q8WP19</li><li>Q8QGQ6</li><li>P25625</li><li>P46295</li>		1
O15519	8837	<ul><li>Y->F at 360: Decreases apoptosis-inducing activity. Reduces interaction with caspase-3 and proteolytic processing</li><li>D->N,A at 376: Abolishes proteolytic processing</li></ul>	apoptosis	GO:0006915							1
O15527	4968	<ul><li>K->Q at 249: Loss of activity</li><li>D->E,Q at 268: No effect on activity</li><li>D->N at 268: Decreases activity about 65-fold</li></ul>									1
O15529		<ul><li>W->R at 174: Restores responses to propionate</li></ul>									1
O15530	5170	<ul><li>Y->F at 9: Slight reduction in pervanadate-stimulated tyrosine phosphorylation</li><li>S->A at 25: No effect</li><li>S->A at 241: No activation</li><li>A->V at 277: 3-fold increase in kinase activity</li><li>Y->F at 373: Reduction in basal activity</li><li>Y->F at 376: Reduction in basal activity</li><li>S->A at 393: No effect</li><li>S->A at 396: No effect</li><li>S->A at 410: No effect</li><li>R->A at 474: No PDGF-dependent translocation to the membrane</li></ul>	phosphorylation	GO:0016310	kinase activity	GO:0016301	membrane	GO:0016020			1
O15550	7403	<ul><li>H->A at 1146: Abolishes histone demethylase activity</li></ul>							Q9UBB5		1
O15554	3783	<ul><li>T->S at 250: Loss of sensitivity to triarylmethanes</li><li>V->A at 275: Loss of sensitivity to triarylmethanes</li></ul>									1
O43148	8731	<ul><li>KKRK->AAAA at 80-83: Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 103-AAAAA-107 and I-127</li><li>KKRKR->AAAAA at 103-107: Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 80-AAAA-83 and I-127</li><li>R->I at 127: Does not abolish nuclear localization. Abolishes nuclear localization; when associated with 80-AAAA-83 and 103-AAAAA-107</li><li>D->A at 203: Loss of activity</li><li>R->A at 239: Loss of activity</li><li>Y->A at 289: Loss of activity</li><li>F->A at 291: Strongly impairs enzyme activity</li><li>F->A at 354: Loss of activity</li></ul>	localization	GO:0051179							1
O43150	8853	<ul><li>C->A at 436: Loss of Arf-GAP activity</li></ul>							<li>Q92263</li><li>P20936</li><li>P14112</li><li>Q92211</li><li>P09851</li><li>Q5PEA9</li><li>P74873</li><li>P74851</li><li>P50904</li>		1
O43157	5364	<ul><li>RRRR->AAAA at 1302-1305: Abolishes cleavage by proprotein convertases</li></ul>									1
O43252	9061	<ul><li>H->A at 425: Loss of activity</li><li>N->K at 426: Increased activity</li><li>GH->AA at 427-428: Loss of activity</li><li>G->A at 427: 30% decrease in activity</li><li>H->A at 428: Loss of activity</li></ul>									1
O43257	10467	<ul><li>T->A at 103: Impairs the p38 MAPK-mediated phosphorylation of ZNHIT1</li><li>S->A at 124: No change in the in vitro MAPK14/MAPK11-induced phosphorylation level of ZNHIT1</li></ul>	phosphorylation	GO:0016310					<li>Q24JY4</li><li>Q95NE7</li><li>O02812</li><li>Q15759</li><li>O43257</li><li>Q16539</li><li>O62618</li>		1
O43283	9175	<ul><li>K->A at 195: Kinase inactive. Fails to activate NF-kappa-B</li></ul>									1
O43294	7041	<ul><li>Y->F at 60: Prevents phosphorylation by FAK2 and FYN. Prevents interaction with CSK</li><li>FLQLF->ALQAA at 338-342: Loss of interaction with AR; when associated with 456-A--A-460</li><li>C->S at 369: Loss of AR coactivation; when associated with S-372</li><li>C->S at 372: Loss of AR coactivation; when associated with S-369</li><li>H->S at 428: Loss of AR coactivation; when associated with S-431</li><li>C->S at 431: Loss of AR coactivation; when associated with S-428</li><li>FLKLF->ALKAA at 456-460: Loss of interaction with AR; when associated with 338-A--A-342</li></ul>	phosphorylation	GO:0016310					<li>Q05876</li><li>P41239</li><li>Q0VBZ0</li><li>Q14289</li><li>P41240</li><li>P06241</li><li>P27446</li>		1
O43318	6885	<ul><li>K->W at 63: Loss of kinase activity</li></ul>			kinase activity	GO:0016301					1
O43353	8767	<ul><li>K->A at 47: Abolishes kinase activity</li><li>K->M at 47: Reduces FAS-mediated apoptosis</li><li>D->N at 146: Abolishes kinase activity</li></ul>	apoptosis	GO:0006915	kinase activity	GO:0016301			<li>O77736</li><li>Q9TSN4</li><li>P12276</li><li>P49327</li><li>Q9BDN4</li><li>P36189</li><li>P29251</li><li>P63103</li><li>P51867</li><li>Q9BDN0</li><li>P08757</li><li>P25445</li><li>Q9BDP2</li>		1
O43432	8672	<ul><li>R->D at 756: Reduces binding to EIF4A; when associated with D-759 and D-764</li><li>R->D at 759: Reduces binding to EIF4A; when associated with D-756 and D-764</li><li>K->D at 764: Reduces binding to EIF4A; when associated with D-756 and D-759</li><li>R->D at 814: Reduces binding to EIF4A; when associated with D-820</li><li>K->D at 820: Reduces binding to EIF4A; when associated with D-814</li><li>RK->DD at 834-835: Reduces binding to IRES</li></ul>			binding	GO:0005488			Q02748		1
O43447	10465	<ul><li>W->F at 133: Abolishes inhibition by cyclosporin A</li></ul>									1
O43462	51360	<ul><li>H->F at 171: Loss of activity</li><li>E->A,Q at 172: Loss of activity</li><li>E->D at 172: Partial loss of activity</li><li>H->F at 175: Loss of activity</li><li>D->N at 467: Loss of activity</li></ul>									1
O43463	6839	<ul><li>W->A at 64: Abolishes methyltransferase activity</li><li>Y->A at 67: Abolishes methyltransferase activity</li><li>H->R at 320: Strongly increases methylation of histone H3</li><li>H->L,K at 324: Abolishes methylation of histone H3</li><li>C->A at 326: Abolishes methylation of histone H3</li></ul>							<li>P61835</li><li>P61834</li><li>Q9P427</li><li>P61833</li><li>Q98RY4</li><li>P61832</li><li>P03588</li><li>P61831</li><li>P03589</li><li>P61830</li><li>P83864</li><li>P07041</li><li>P90543</li><li>P02299</li><li>P28726</li><li>P08437</li><li>Q757N1</li><li>P61836</li><li>P50564</li><li>Q00020</li><li>Q83270</li><li>P28931</li><li>P06011</li><li>Q06196</li><li>P08898</li><li>Q9HDN1</li><li>P20122</li><li>P17769</li><li>P23753</li><li>Q66121</li><li>Q7XYZ0</li><li>O40976</li><li>Q9U7D1</li><li>Q2UCQ0</li><li>Q5DWI3</li><li>P80553</li><li>P40285</li><li>P84239</li><li>P84238</li><li>P84237</li><li>P27752</li><li>P84236</li><li>P84235</li><li>Q83264</li><li>P22843</li>		1
O43464	27429	<ul><li>A->M at 134: Loss of interaction with XIAP. Loss of inhibition of XIAP activity</li><li>S->A at 306: Loss of protease activity</li></ul>							<li>P19028</li><li>Q9QBZ5</li><li>P24107</li><li>Q9QBZ1</li><li>Q79666</li><li>P15833</li><li>P03362</li><li>P18042</li><li>Q8AII1</li><li>P03363</li><li>P04024</li><li>P04023</li><li>P10978</li><li>O93215</li><li>P26810</li><li>Q1A249</li><li>P03356</li><li>P03355</li><li>O41798</li><li>P20892</li><li>Q9Y6I0</li><li>P10210</li><li>Q9QBY3</li><li>P03353</li><li>P16901</li><li>Q74120</li><li>Q09SZ9</li><li>P98170</li><li>Q89928</li><li>Q73368</li><li>P84454</li><li>Q9WC63</li><li>P20825</li><li>Q9IDV9</li><li>P0C211</li><li>P0C210</li><li>P51518</li><li>Q4U0X6</li><li>P12451</li><li>P07570</li><li>P28936</li><li>O89940</li><li>P24740</li><li>P26809</li><li>P26808</li><li>Q0R5R3</li><li>Q0R5R2</li><li>P18802</li><li>P10394</li><li>P19561</li><li>P16423</li><li>P63119</li><li>P19560</li><li>Q75002</li><li>P04589</li><li>P04587</li><li>P04588</li><li>Q9QSR3</li><li>O91080</li><li>P16046</li><li>P17757</li><li>P12497</li><li>P12499</li><li>P12498</li><li>P03311</li><li>P20875</li><li>P20876</li><li>P10273</li><li>Q9WC54</li><li>P10272</li><li>P10271</li><li>P10270</li><li>P19199</li><li>P05962</li><li>P18096</li><li>P10265</li><li>P04584</li><li>P11227</li><li>P04585</li><li>Q76634</li><li>Q8I7P9</li><li>Q9Q720</li><li>P14078</li><li>P31822</li><li>P11365</li><li>P35963</li><li>P14074</li><li>P05959</li><li>P63131</li><li>P04323</li><li>P10274</li><li>P21407</li><li>O89290</li><li>P35956</li><li>P05960</li><li>P05961</li><li>Q1A267</li><li>P63122</li><li>P63123</li><li>P63124</li><li>P63125</li><li>P63120</li><li>P63121</li><li>P03366</li><li>P03367</li><li>P03369</li><li>P63127</li><li>P63128</li><li>P63129</li><li>Q77373</li><li>P03370</li><li>P27502</li><li>P21414</li>		1
O43493	10618	<ul><li>Y->A at 430: Loss of relocalization to the trans-Golgi</li></ul>									1
O43504	10542	<ul><li>T->A at 12: No change</li><li>T->A at 36: No interaction with XABX14-154 (truncated form of HBX)</li></ul>									1
O43524	2309	<ul><li>T->A at 32: Abolishes YWHAZ-binding; when associated with A-253. Exclusively nuclear, induces transcription and promotes apoptosis; when associated with A-253 and A-315</li><li>S->A at 209: Impairs nuclear translocation upon oxidative stress</li><li>K->A at 242: Slightly decreases DNA affinity</li><li>K->A at 245: Decreases DNA affinity</li><li>S->A at 253: Abolishes YWHAZ-binding; when associated with A-32. Exclusively nuclear, induces transcription and promotes apoptosis; when associated with A-32 and A-315</li><li>S->A at 315: No effect on YWHAZ-binding. Promotes nuclear translocation. Exclusively nuclear, induces transcription and promotes apoptosis; when associated with A-32 and A-253</li></ul>	<li>apoptosis</li><li>transcription</li>	<li>GO:0006915</li><li>GO:0006350</li>	binding	GO:0005488			<li>P63103</li><li>P29361</li><li>Q5ZKC9</li><li>Q5R651</li><li>P63104</li>		1
O43525	3786	<ul><li>G->S at 318: >50% Reduction of wt heteromeric current; ratio of 1</li></ul>									1
O43526	3785	<ul><li>S->E at 52: 40% increase in potassium current amplitude. Ratio of 1</li><li>S->Q at 52: Decrease of PKA stimulation. Ratio of 1</li><li>G->S at 279: More than 50% reduction of wt heteromeric current. Ratio of 1</li></ul>			PKA	GO:0004691					1
O43529	9486	<ul><li>K->A at 128: Loss of function</li><li>K->R at 128: Induces a reduction in enzyme activity</li><li>R->A,K at 189: Loss of function</li><li>D->A at 190: Loss of function</li><li>D->E at 190: Induces a mild reduction in enzyme activity</li><li>P->A,G at 191: Loss of function</li><li>S->A,T at 197: Loss of function</li></ul>									1
O43541	4091	<ul><li>S->A at 435: Loss of phosphorylation</li><li>G->S at 471: Loss of interaction with SMAD1 and BMP-receptor</li><li>Missing at 478-496: Loss of interaction with SMAD1</li></ul>	phosphorylation	GO:0016310					<li>Q1JQA2</li><li>P35855</li><li>Q15797</li><li>Q9I962</li>		1
O43561	27040	<ul><li>C->A at 26: Reduces palmitoylation; abolishes localization to lipid rafts</li><li>C->A at 29: Reduces palmitoylation; impairs localization to lipid rafts</li><li>Y->F at 161: Abolishes interaction with PLCG1</li><li>Y->F at 200: Abolishes interaction with GRB2 and PIK3R1; when associated with F-220</li><li>Y->F at 220: Abolishes interaction with GRB2 and PIK3R1; when associated with F-200</li></ul>	localization	GO:0051179			lipid rafts	GO:0045121	<li>P27986</li><li>Q5R4J7</li><li>Q07883</li><li>P62993</li><li>P23727</li><li>P08487</li><li>P19174</li>		1
O43586	9051	<ul><li>W->A at 232: Abolishes binding to MEFV</li><li>Y->F at 345: Decreases binding to MEFV</li></ul>			binding	GO:0005488			O15553		1
O43592	11260	<ul><li>RKQLK->AAQLA at 405-409: Abolishes binding to tRNA. Does not abolish shuttling behavior</li><li>KVRSR->AVRSA at 539-543: Does not abolish binding to tRNA. Does not abolish shuttling behavior</li><li>LFSRF->AFSRA at 547-551: Does not abolish binding to tRNA. Does not abolish shuttling behavior</li><li>FSRFV->ASRFA at 548-552: Does not abolish binding to tRNA. Does not abolish shuttling behavior</li><li>RFVKSLNK->AFVAS at 550-557: Abolishes binding to tRNA. Does not abolish shuttling behavior</li></ul>	behavior	GO:0007610	<li>binding</li><li>tRNA</li>	<li>GO:0005488</li><li>GO:0030533</li>					1
O43617	27095	<ul><li>C->S at 68: Loss of palmitoylation</li></ul>									1
O43639	8440	<ul><li>W->K at 148: Abolishes interaction with DOCK1</li><li>W->K at 234: Abolishes interaction with DOCK1</li></ul>							Q14185		1
O43663	9055	<ul><li>T->A at 470: No effect. Reduces in vitro cyclin E-CDK2 phosphorylation and causes extensive bundling of microtubules to the mitotic spindle; when associated with A-481</li><li>T->A at 481: No effect. Reduces in vitro cyclin E-CDK2 phosphorylation and causes extensive bundling of microtubules to the mitotic spindle; when associated with A-470</li></ul>	phosphorylation	GO:0016310			<li>microtubules</li><li>spindle</li>	<li>GO:0005874</li><li>GO:0005819</li>	<li>P04961</li><li>P22177</li><li>O16852</li><li>Q00268</li><li>Q00265</li><li>P24314</li><li>P61074</li><li>P24941</li><li>O55076</li><li>P17070</li><li>P48963</li><li>Q5E9Y0</li><li>P43450</li><li>P17917</li><li>P18248</li><li>P31008</li><li>P17918</li><li>P53358</li><li>O01377</li><li>P12004</li>		1
O43719	27336	<ul><li>Y->D at 136: Loss of interaction with U snRNPs</li></ul>					snRNPs	GO:0030532			1
O43808	10478	<ul><li>LMF->KKK at 283-285: Impairs interaction with PEX19</li><li>EK->LL at 289-290: Impairs interaction with PEX19</li><li>KR->EE at 302-303: No effect on interaction with PEX19</li></ul>							<li>P40855</li><li>Q60415</li><li>Q3SZD1</li><li>Q5R7U2</li><li>Q07418</li>		1
O43809	11051	<ul><li>K->R at 23: Abolishes acetylation</li><li>K->R at 29: No effect on acetylation</li></ul>									1
O43918	326	<ul><li>C->P at 302: Reduces transcription activation</li><li>C->P at 437: Reduces transcription activation</li></ul>	transcription	GO:0006350							1
O60216	5885	<ul><li>R->A at 172: Abolishes first cleavage by ESPL1</li><li>D->A at 279: Abolishes cleavage by caspase-3</li><li>R->A at 450: Abolishes second cleavage by ESPL1</li></ul>							Q14674		1
O60229	8997	<ul><li>K->A at 2712: Loss of autophosphorylation</li></ul>	autophosphorylation	GO:0046777							1
O60239	9467	<ul><li>L->A at 347: Loss of phosphorylation and binding by phospho-JNK; when associated with A-349</li><li>L->A at 349: Loss of phosphorylation and binding by phospho-JNK; when associated with A-347</li><li>L->A at 434: No change of phosphorylation or binding by phospho-JNK; when associated with A-436</li><li>L->A at 436: No change of phosphorylation or binding by phospho-JNK; when associated with A-434</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488			<li>Q966Y3</li><li>P92208</li>		1
O60260	5071	<ul><li>C->S at 332: Impairs folding of IBR domain</li><li>C->A at 337: Impairs the ability to ubiquitinate SNCAIP</li><li>C->S at 365: Impairs protein folding</li><li>C->R at 418: Fails to ubiquitinate SYT11. Does not loose ability to bind SYT11</li><li>C->A at 421: Impairs the ability to ubiquitinate SNCAIP</li><li>C->A at 431: Impairs the ability to ubiquitinate SNCAIP</li></ul>	protein folding	GO:0006457					<li>Q9Y6H5</li><li>Q9BT88</li>		1
O60264	8467	<ul><li>K->R at 211: Loss of ATP hydrolysis and no association of the SMARCA5/cohesin/NuRD complex with chromatin</li></ul>	ATP hydrolysis	GO:0006200			chromatin	GO:0000785	<li>Q06851</li><li>O60264</li>		1
O60285	9891	<ul><li>T->A at 211: Prevents phosphorylation and activation by STK11 complex</li><li>S->A at 600: No phosphorylation</li></ul>	phosphorylation	GO:0016310					<li>Q15831</li><li>Q0GGW5</li>		1
O60337	10299	<ul><li>C->A at 9: Abolishes auto-ubiquitination</li></ul>									1
O60341	23028	<ul><li>N->A at 535: Strongly reduces demethylase activity</li><li>H->A at 564: Strongly reduces demethylase activity</li><li>K->A at 661: Abolishes histone demethylase activity</li><li>Y->A at 761: Strongly reduces demethylase activity</li></ul>							Q9UBB5		1
O60346	23239	<ul><li>Missing at 1715-1717: Loss of function in vivo, but does not abolishes intrinsic phosphatase activity</li></ul>							<li>Q5X1E5</li><li>Q7M7K5</li><li>Q7MAZ9</li><li>Q8XBL4</li><li>Q88A53</li><li>Q5P3T0</li><li>Q7MBF4</li><li>Q8Z3M9</li><li>Q5PC82</li><li>Q5ZRX9</li><li>Q821A6</li><li>Q87SK9</li><li>Q9JZ88</li><li>Q9CP21</li><li>Q82U82</li><li>Q9I5V3</li><li>Q5F8K9</li><li>Q63YC3</li><li>Q8Y395</li><li>Q6LV05</li><li>Q8ZLY4</li><li>Q6FA38</li><li>Q9PDL7</li><li>Q62EU1</li><li>Q9JUB2</li><li>Q5WT58</li><li>Q665U9</li><li>Q57JQ5</li><li>Q9KPC6</li><li>Q8P5D4</li><li>Q8CWL6</li><li>Q8PPG9</li><li>P06961</li><li>P45269</li><li>Q9L7A3</li><li>Q88QU2</li><li>Q6D160</li><li>Q8ZI64</li><li>Q60CQ4</li><li>Q87DS9</li><li>Q65Q41</li><li>Q5E2K7</li><li>Q8CXX6</li>		1
O60504	10174	<ul><li>W->F at 649: Loss of SOS-binding ability</li><li>Y->V at 667: Loss of SOS-binding ability</li></ul>			binding	GO:0005488					1
O60516	8637	<ul><li>Y->A at 40: Loss of interaction with EIF4E</li><li>L->A at 45: Loss of interaction with EIF4E</li></ul>							<li>Q9P974</li><li>P63074</li><li>Q9P975</li><li>Q9N0T5</li><li>P29338</li><li>P48598</li><li>Q75AV8</li><li>P06730</li><li>P48597</li><li>O77210</li><li>P07260</li><li>Q5UQG4</li><li>Q9PW28</li><li>P63073</li>		1
O60563	904	<ul><li>C->Y at 261: Loss of HIV-1 Tat transactivation</li></ul>									1
O60566	701	<ul><li>D->E at 579: Abolishes the cleavage by caspase-3</li><li>D->E at 610: Abolishes the cleavage by caspase-3</li><li>K->A at 795: Does not abolish the capacity to inhibit APC/CDC20</li><li>K->R at 795: Inhibits kinase activity</li></ul>			kinase activity	GO:0016301			<li>P25054</li><li>Q12834</li><li>P26309</li>		1
O60573	9470	<ul><li>W->A at 63: Unable to bind capped mRNA</li><li>W->A at 95: Ability to bind capped mRNA reduced to 40% of wild-type</li><li>WED->FAA at 124-126: Unable to bind capped mRNA</li><li>W->A at 124: Ability to bind capped mRNA reduced to less than 10% of wild-type</li><li>W->F at 124: Ability to bind capped mRNA reduced to 13% of wild-type</li><li>E->A at 125: Ability to bind capped mRNA reduced to less than 10% of wild-type</li><li>D->A at 126: Slight reduction in ability to bind capped mRNA</li><li>W->A at 135: Unable to bind capped mRNA</li><li>W->A at 148: Unable to bind capped mRNA</li><li>W->A at 183: Ability to bind capped mRNA reduced to less than 10% of wild-type</li><li>W->F at 183: Unable to bind capped mRNA</li></ul>									1
O60583	905	<ul><li>N->C at 260: Activation of HIV-1 Tat function</li></ul>									1
O60603	7097	<ul><li>N->S at 114: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain</li><li>N->D at 199: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain</li><li>T->A at 416: Prevents addition of N-glycans. Reduces secretion of the N-terminal ectodomain</li><li>N->D at 442: Prevents addition of N-glycans. Prevents secretion of the N-terminal ectodomain</li><li>P->F at 681: Abolishes the interaction with MYD88. No effect on oligomerization or on the structure of the TIR domain</li></ul>	secretion	GO:0046903					Q99836		1
O60671	5810	<ul><li>SLLKPSTK->AAAAA at 226-233: Abolishes association of the 9-1-1 complex with RAD17</li></ul>							<li>Q9MBA3</li><li>P48581</li><li>Q758W7</li><li>Q5R652</li><li>Q9XT62</li><li>O75943</li>		1
O60759	9595	<ul><li>K->E at 82: No membrane-association. No change in the binding to CYTH1; when associated with A-90 and A-92</li><li>F->A at 90: No membrane-association. No change in the binding to CYTH1; when associated with E-82 and A-92</li><li>I->A at 92: No membrane-association. No change in the binding to CYTH1; when associated with E-82 and A-90</li></ul>			binding	GO:0005488	membrane	GO:0016020			1
O60763	8615	<ul><li>S->A at 942: Loss of phosphorylation</li></ul>	phosphorylation	GO:0016310							1
O60828	10084	<ul><li>W->A at 52: Enhances activity. Reduces activity; when associated with A-75. Markedly reduced activity; when associated with A-64; A-65 and A-66. Abolishes activity; when associated with A-64; A-65; A-66 and A-75</li><li>Y->A at 64: No effect on activity; when associated with A-65 and A-66. Markedly reduced activity; when associated with A-52; A-65 and A-66. Abolishes activity; when associated with A-52; A-65; A-66 and A-75</li><li>Y->A at 65: No effect on activity; when associated with A-64 and A-66. Markedly reduced activity; when associated with A-52; A-64 and A-66. Abolishes activity; when associated with A-52; A-64; A-66 and A-75</li><li>W->A at 66: No effect on activity; when associated with A-64 and A-65. Markedly reduced activity; when associated with A-52; A-64 and A-65. Abolishes activity; when associated with A-52; A-64; A-65 and A-75</li><li>W->A at 75: No effect on activity. Reduces activity; when associated with A-52. Abolishes activity; when associated with A-52; A-64; A-65 and A-66</li><li>P->G at 78: No effect on activity</li></ul>									1
O60841	9669	<ul><li>V->G at 640: Loss of activity in vivo. Retains full activity in vitro</li><li>H->E at 706: Loss of activity; both in vivo and in vitro</li><li>H->Q at 706: Loss of activity in vivo. Partial activity in vitro</li><li>D->N at 759: Loss of activity; both in vivo and in vitro</li></ul>									1
O60869	8721	<ul><li>T->D at 40: Loss of interaction with CALM; when associated with D-58; D-91 and D-111</li><li>T->D at 58: Loss of interaction with CALM; when associated with D-40; D-91 and D-111</li><li>T->D at 65: No effect on CALM-binding. No effect; when associated with D-74</li><li>T->D at 74: No effect on CALM-binding. No effect; when associated with D-65</li><li>S->A at 87: No effect on CALM-binding</li><li>S->D at 87: Loss of interaction with CALM and higher affinity for TBP. Same effect; when associated with D-65 and D-74</li><li>T->A at 91: No effect on CALM-binding</li><li>T->D at 91: Partial loss of interaction with CALM. Complete loss of interaction; when associated with D-40; D-58 and D-111</li><li>S->D at 111: Loss of interaction with CALM; when associated with D-40; D-58 and D-91</li></ul>			binding	GO:0005488			<li>Q12731</li><li>O29874</li><li>P58178</li><li>P58177</li><li>Q57930</li><li>Q8TX38</li><li>Q8ZVR0</li><li>O27664</li><li>P53360</li><li>Q9P9I9</li><li>P13393</li><li>O43133</li><li>Q9V024</li><li>O23894</li><li>Q92117</li><li>P62144</li><li>Q92146</li><li>P26354</li><li>P26355</li><li>Q5RAD2</li><li>Q971V3</li><li>Q9YAT1</li><li>P93348</li><li>Q42808</li><li>P62001</li><li>P62000</li><li>P62149</li><li>Q27850</li><li>O13270</li><li>P46272</li><li>O17488</li><li>P48511</li><li>Q9YGV8</li><li>Q978J5</li><li>P62157</li><li>O58737</li><li>P26357</li><li>Q56253</li><li>O74045</li><li>P62158</li><li>Q13492</li><li>P62160</li><li>Q9HLM8</li><li>Q52366</li><li>P32085</li><li>P32086</li><li>P20226</li><li>Q6M0L3</li><li>P52653</li><li>Q9UWN7</li><li>P17871</li><li>Q7M6Y3</li><li>Q6L1R1</li><li>P91809</li><li>P53361</li><li>Q55031</li>		1
O60870	22944	<ul><li>K->E at 302: Significant reduction of RNA-binding activity</li><li>K->E at 391: Significant reduction of RNA-binding activity</li></ul>			RNA-binding	GO:0003723					1
O60880	4068	<ul><li>R->Q at 32: Strongly reduced affinity for SLAMF1</li></ul>							<li>Q95MM9</li><li>Q13291</li>		1
O60934	4683	<ul><li>R->A at 28: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation</li><li>H->A at 45: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation</li><li>GG->EE at 136-137: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation</li><li>Y->A at 176: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation</li><li>S->A at 343: Abrogates ATM-dependent phosphorylation</li><li>S->A at 397: Abrogates ATM-dependent phosphorylation. No loss of interaction with KPNA2</li><li>KR->AA at 465-466: Blocks the association with KPNA2, and reduces nuclear foci formation in response to ionizing radiation</li><li>Q->K at 583: No loss of interaction with KPNA2</li><li>S->A at 615: Abrogates ATM-dependent phosphorylation</li><li>EE->AA at 736-737: Decreases ATM binding</li><li>DD->AA at 741-742: Decreases ATM binding</li><li>RY->AA at 745-746: Decreases ATM binding</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488			<li>Q13315</li><li>Q6PQD5</li><li>P52292</li><li>Q9M3G7</li>		1
O60942	8732	<ul><li>K->A at 294: Loss of GTase activity</li><li>R->A at 299: Loss of GTase activity</li><li>E->A at 345: Loss of GTase activity</li><li>K->A at 458: Loss of GTase activity</li><li>K->A at 460: Loss of GTase activity</li></ul>							<li>Q80DX6</li><li>P25950</li><li>P32094</li><li>Q6FQ31</li><li>Q17607</li><li>Q5UQX1</li><li>O57209</li><li>Q9J584</li><li>P78587</li><li>Q9JFA8</li><li>Q01159</li><li>Q6BT58</li><li>P33057</li><li>Q8V2R8</li><li>Q6C783</li><li>Q6CWR0</li><li>P20979</li><li>O55236</li><li>P40997</li><li>Q775U0</li><li>Q755D0</li><li>Q7SB53</li><li>Q8QMV9</li><li>O60942</li><li>P04298</li>		1
O75030	4286	<ul><li>K->R at 289: Loss of sumoylation; when associated with R-423</li><li>S->A,P at 405: Loss of phosphorylation and function</li><li>K->R at 423: Loss of sumoylation; when associated with R-289</li></ul>	<li>phosphorylation</li><li>sumoylation</li>	<li>GO:0016310</li><li>GO:0016925</li>							1
O75077	8745	<ul><li>E->A at 566: Significantly lower of adhesion-promoting activity</li></ul>									1
O75081	863	<ul><li>V->P,A at 494: Loss of interaction with PRKAR2A</li></ul>							<li>P13861</li><li>P05207</li><li>P00515</li>		1
O75150	9810	<ul><li>L->S at 109: Abolishes interaction with RB1</li><li>C->M at 111: Abolishes interaction with RB1</li><li>E->Q at 113: Abolishes interaction with RB1</li></ul>							P06400		1
O75164	9682	<ul><li>G->A at 133: Abolishes histone demethylase activity; when associated with A-138</li><li>G->A at 138: Abolishes histone demethylase activity; when associated with A-138</li><li>G->A at 165: Abolishes histone demethylase activity; when associated with A-165</li><li>G->A at 170: Abolishes histone demethylase activity; when associated with A-165</li><li>H->A at 188: Abolishes histone demethylase activity</li><li>ST->AI at 288-289: Displays histone demethylase activity for both dimethylated and H3-K9Me3</li><li>ST->TV,NV,GG at 288-289: Abolishes histone demethylase activity</li><li>D->A at 945: Impairs binding to H3-K4Me3</li><li>D->R at 945: Abolishes binding to H3-K4Me3</li><li>W->H at 967: Abolishes binding to H3-K4Me3</li><li>Y->A at 973: Abolishes binding to H3-K4Me3</li></ul>			binding	GO:0005488			Q9UBB5		1
O75192	8800	<ul><li>N->D at 9: No effect on peroxisomal location</li><li>KLK->SLS at 243-245: No effect on peroxisomal location</li></ul>									1
O75223	79017	<ul><li>G->A at 23: Marked decrease in catalytic efficiency</li><li>E->A,Q at 98: Abolishes activity without altering structure</li><li>Y->F at 105: Marked decrease in catalytic efficiency and specific activity</li><li>Y->F at 125: Little or no change in reaction kinetics</li></ul>									1
O75319	8446	<ul><li>C->S at 152: Loss of activity. No effect in RNA-binding</li></ul>			RNA-binding	GO:0003723					1
O75340	10016	<ul><li>E->A at 47: Loss of interaction with SEC31A and loss of localization to the endoplasmic reticulum; when associated with A-114</li><li>E->A at 114: Loss of interaction with SEC31A and loss if localization to the endoplasmic reticulum; when associated with A-47</li></ul>	localization	GO:0051179			endoplasmic reticulum	GO:0005783			1
O75351	9525	<ul><li>A->D at 15: Reduces HIV-1 release 2-fold</li><li>A->D at 15: Reducews HIV-1 release 10-fold; when associated with D-66</li><li>L->D at 66: Reduces HIV-1 release 3-fold</li><li>L->D at 66: Reducews HIV-1 release 10-fold; when associated with D-15</li><li>WL->AA at 208-209: Strongly impairs HIV-1 release</li><li>G->A at 210: Impairs HIV-1 release</li><li>E->Q at 235: Defective in vacuolar protein sorting</li><li>Missing at 390-396: Abolishes interaction with VTA1</li></ul>							Q06263		1
O75355	956	<ul><li>R->G at 67: Increase of activity</li><li>R->A at 143: Loss of activity</li><li>R->K at 143: Increase of activity</li><li>R->N at 146: No effect</li><li>R->P at 146: Increase of ATPase activity, decrease of ADPase activity</li><li>R->T at 146: Increase of activity</li><li>E->D at 182: Complete loss of activity</li><li>E->Q at 182: Complete loss of activity</li><li>W->A at 187: Complete loss of activity</li><li>N->A at 191: Loss of ATPase activity, increase of ADPase activity</li><li>D->E at 219: Increase of activity</li><li>S->A at 224: Complete loss of activity</li><li>Q->A at 226: Loss of activity</li><li>W->A at 459: Increase of activity, especially the ATP hydrolysis</li></ul>	ATP hydrolysis	GO:0006200	ATPase activity	GO:0016887			<li>P40009</li><li>P80595</li><li>P50635</li>		1
O75365	100131062	<ul><li>C->A at 49: No effect on enzymatic activity</li><li>D->A at 71: No effect on enzymatic activity</li><li>D->A at 72: Abolishes enzymatic activity</li><li>C->A,S at 104: 95% loss of enzymatic activity</li><li>C->S at 104: Reduces migration-promoting activity</li><li>A->S at 111: Enhances catalytic activity</li></ul>			catalytic activity	GO:0003824					1
O75398	10522	<ul><li>Y->Q at 215: Reduces transcription activation</li><li>R->A at 226: Reduces transcription activation</li><li>R->A at 246: Reduces transcription activation</li><li>K->A at 250: Abolishes DNA-binding</li><li>W->Q at 252: Abolishes DNA-binding</li><li>K->A at 253: Abolishes DNA-binding</li><li>R->T at 302: Abolishes nuclear localization</li><li>K->T at 304: Abolishes nuclear localization</li></ul>	<li>localization</li><li>transcription</li>	<li>GO:0051179</li><li>GO:0006350</li>	DNA-binding	GO:0003677					1
O75436	9559	<ul><li>IM->DD at 235-236: Abolishes interaction with VPS35 and endosomal subcellular location</li></ul>							<li>P34110</li><li>Q96QK1</li><li>Q2HJG5</li>		1
O75449	11104	<ul><li>K->A at 255: Abolishes ATP dependent microtubule severing activity and localization to spindle poles</li><li>D->N at 308: Abolishes ATP dependent microtubule severing activity and localization to spindle poles; when associated with N-309</li><li>E->N at 309: Abolishes ATP dependent microtubule severing activity and localization to spindle poles; when associated with N-308</li></ul>	localization	GO:0051179			<li>spindle poles</li><li>microtubule</li>	<li>GO:0000922</li><li>GO:0005874</li>			1
O75460	2081	<ul><li>C->S at 109: No effect on dimerization</li><li>C->S at 148: No effect on dimerization. Weakens dimer; when associated with S-148</li><li>C->S at 332: No effect on dimerization. Weakens dimer; when associated with S-332</li><li>K->A at 599: Loss of autophosphorylation and of endoribonuclease activity. Inhibition of growth arrest</li></ul>	autophosphorylation	GO:0046777					<li>O75460</li><li>Q9EQY0</li><li>Q9Z2E3</li><li>Q76MJ5</li><li>P32361</li><li>Q09499</li>		1
O75461	1876	<ul><li>L->E at 68: Reduction in repressor activity, little effect on S-phase entry</li></ul>	S-phase	GO:0051320							1
O75475	11168	<ul><li>I->A at 365: Loss of interaction with human HIV-1 integrase</li><li>D->A,N at 366: Loss of interaction with human HIV-1 integrase</li><li>F->A at 406: Loss of interaction with human HIV-1 integrase</li><li>V->A at 408: Reduced interaction with human HIV-1 integrase</li></ul>									1
O75506	3281	<ul><li>V->K at 16: Loss of interaction with HSF1; in association with K-19</li><li>L->K at 19: Loss of interaction with HSF1; in association with K-16</li><li>I->K at 45: Loss of interaction with HSF1; in association with K-48</li><li>L->K at 48: Loss of interaction with HSF1; in association with K-45</li></ul>							<li>Q08DJ8</li><li>P41151</li><li>P38529</li><li>P10961</li><li>Q00613</li>		1
O75525	10656	<ul><li>Missing at 212-251: Complete loss of SIAH1-mediated degradation</li><li>Missing at 327-346: Complete loss of nuclear sublocalization</li></ul>							Q8IUQ4		1
O75530	8726	<ul><li>I->N at 193: Impairs interaction with EZH2</li><li>L->P at 196: Impairs interaction with EZH2</li><li>ST->AA at 300-301: Impairs interaction with the matrix protein MA of HIV-1</li><li>HRNY->AAAA at 305-308: Impairs interaction with the matrix protein MA of HIV-1</li></ul>							<li>P04876</li><li>P06166</li><li>P13844</li><li>P19718</li><li>P30026</li><li>P22046</li><li>P29990</li><li>P29991</li><li>P04888</li><li>Q88428</li><li>P09732</li><li>P25223</li><li>P25224</li><li>P03419</li><li>P25058</li><li>P41358</li><li>Q15910</li><li>P18356</li><li>P03344</li><li>P06503</li><li>P06502</li><li>P32886</li><li>Q9YRV3</li><li>P52637</li><li>P03426</li><li>P12446</li><li>P31035</li><li>P19692</li><li>P07564</li><li>P26034</li><li>Q89277</li><li>O12705</li><li>P06942</li><li>P36355</li><li>P36356</li><li>P06943</li><li>P16629</li><li>Q9YNA8</li><li>P27019</li><li>Q074N0</li><li>P16628</li><li>P18611</li><li>P12823</li><li>P24615</li><li>Q6DV88</li><li>P11206</li><li>Q01427</li><li>P25182</li><li>P06935</li><li>P27020</li><li>P63117</li><li>P27912</li><li>P27913</li><li>P27910</li><li>P17763</li><li>P27915</li><li>O57299</li><li>P08325</li><li>P06446</li><li>P62690</li><li>P07873</li><li>P03519</li><li>Q9UKH8</li><li>P33515</li><li>P35976</li><li>P03314</li><li>P63145</li><li>P29165</li><li>Q88266</li><li>P27287</li><li>P31620</li><li>Q66112</li><li>P17748</li><li>P13616</li><li>P05769</li><li>O18559</li><li>P19110</li><li>Q04538</li><li>P27395</li><li>P24266</li><li>P63130</li><li>Q91B74</li><li>Q9IK90</li><li>Q01299</li><li>P33478</li><li>O89341</li><li>P07720</li><li>P33482</li><li>Q7LDI9</li><li>P08671</li><li>P27663</li><li>Q96PI4</li><li>Q6J3P1</li><li>P09866</li><li>Q1X880</li><li>P14340</li><li>Q84131</li><li>Q1X881</li><li>P14403</li><li>P87889</li><li>P06157</li><li>P87577</li><li>P29983</li><li>P29984</li><li>Q9HDB9</li><li>P63126</li><li>P16287</li><li>P22338</li><li>P63128</li><li>Q98803</li><li>P29837</li><li>P29838</li><li>P35947</li><li>P62684</li><li>P62685</li><li>P62683</li><li>Q9NRZ4</li><li>P15200</li><li>Q9JAF2</li><li>P62689</li><li>P14336</li><li>P14335</li>		1
O75531	8815	<ul><li>S->A at 4: Complete loss of phosphorylation</li><li>S->E at 4: Complete loss of phosphorylation and mislocalization of EMD in nucleus</li><li>K->A at 6: Complete loss of LEMD3/MAN1 and histone H1/H3 binding</li><li>K->E at 6: Complete loss of dsDNA and LEMD3/MAN1 binding</li><li>R->A at 8: Enhances histone H1/H3 binding</li><li>R->E at 8: Complete loss of LEMD3/MAN1 binding</li><li>D->A at 9: Reduces binding to dsDNA, LEMD3/MAN1 and histone H1/H3</li><li>P->A at 14: No effect on LEMD3/MAN1 and enhances histone H1/H3 binding</li><li>K->A at 18: No effect on histone H1/H3 binding</li><li>G->E at 25: Complete loss of dsDNA, EMD, histone H1/H3 and LEMD3/MAN1 binding</li><li>G->Q at 25: Complete loss of EMD binding and reduces dsDNA binding</li><li>I->A at 26: Reduces histone H1/H3 and LEMD3/MAN1 binding. Fails to promote HIV-1 genome integration</li><li>I->K at 26: Fails to promote HIV-1 genome integration</li><li>G->E at 27: Fails to bind dsDNA</li><li>G->Q at 27: Reduces binding to dsDNA</li><li>V->A at 29: No effect on histone H1/H3 binding</li><li>K->E at 32: No effect on histone H1/H3 binding</li><li>K->E at 33: No effect on histone H1/H3 binding</li><li>R->A at 37: No effect on histone H1/H3 binding</li><li>R->E at 37: Reduces LEMD3/MAN1 binding</li><li>K->A at 41: No effect on histone H1/H3 and LEMD3/MAN1 binding</li><li>K->E at 41: Reduces histone H1/H3 binding</li><li>L->E at 46: Complete loss of dsDNA, histone H1/H3 and LEMD3/MAN1 binding</li><li>G->E at 47: Complete loss of EMD, histone H1/h3 and LEMD3/MAN1 binding</li><li>L->A at 50: Reduces LEMD3/MAN1 binding. No effect on Histone H1/H3 binding</li><li>L->K at 50: Fails to promote HIV-1 genome integration</li><li>V->E at 51: Complete loss of EMD, and histone H1/H3 binding. Reduces dsDNA and LEMD3/MAN1 binding</li><li>K->A at 53: No effect on LEMD3/MAN1 binding. Enhances histone H1/H3 binding</li><li>K->E at 53: Complete loss of EMD binding. Reduces LEMD3/MAN1 binding. Enhances histone H1/H3 binding</li><li>K->A at 54: Reduces LEMD3/MAN1 binding. No effect on histone H1/H3 binding</li><li>K->E at 54: Reduces binding to dsDNA</li><li>R->E at 60: No effect on histone H1/H3 binding</li><li>W->A at 62: Complete loss of LEMD3/MAN1 binding. Enhances histone H1/H3 binding</li><li>K->E at 64: Enhances histone H1/H3 binding</li><li>R->E at 75: Reduces binding to dsDNA. No effect on histone H1/H3 binding</li><li>C->A at 80: No effect on histone H1/H3 and LEMD3/MAN1 binding</li><li>R->E at 82: No effect on histone H1/H3 binding</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488	nucleus	GO:0005634	<li>P06350</li><li>Q9HFU4</li><li>P12305</li><li>P08283</li><li>P23444</li><li>P09426</li><li>P02255</li><li>Q9UV33</li><li>Q9P8F8</li><li>Q8J0U2</li><li>P09987</li><li>P15868</li><li>P21895</li><li>Q9M5W4</li><li>P10156</li><li>P50402</li><li>P84408</li><li>P17268</li><li>Q75C22</li><li>P37218</li><li>P54671</li><li>P27806</li><li>P35060</li><li>P02254</li><li>Q9Y2U8</li><li>P53551</li><li>Q6FJX6</li><li>P40267</li>		1
O75533	23451	<ul><li>T->A at 223: No effect on interaction with PPP1R8</li><li>T->A at 227: No effect on interaction with PPP1R8</li><li>T->A at 235: No effect on interaction with PPP1R8</li><li>T->A at 244: Slight inhibition of interaction with PPP1R8</li><li>T->A at 248: Slight inhibition of interaction with PPP1R8</li><li>T->A at 257: No effect on interaction with PPP1R8</li><li>T->A at 261: Slight inhibition of interaction with PPP1R8</li><li>T->A at 267: No effect on interaction with PPP1R8</li><li>T->A at 273: No effect on interaction with PPP1R8</li><li>T->A at 278: No effect on interaction with PPP1R8</li><li>T->A at 296: No effect on interaction with PPP1R8</li><li>T->A at 303: No effect on interaction with PPP1R8</li><li>T->A at 313: No effect on interaction with PPP1R8</li></ul>							<li>Q12972</li><li>Q28147</li>		1
O75582	9252	<ul><li>D->A at 195: Loss of kinase activity</li><li>S->A at 212: Inactives the N-terminal kinase domain</li><li>S->A at 360: Decreases kinase activity by 60% in response to PMA and UV-C</li><li>S->A at 376: Loss of kinase activity, and decreases the phosphorylation of S-360 and T-581</li><li>D->A at 565: Loss of kinase activity</li><li>T->A at 581: Loss of kinase activity, and blocks phosphorylation of S-212; S-376 and S-381 in response to PMA and UV-C</li></ul>	phosphorylation	GO:0016310	kinase activity	GO:0016301					1
O75593	8928	<ul><li>H->R at 83: Loss of activity</li></ul>									1
O75628	28954	<ul><li>T->N at 94: No endothelial cell sprouting</li></ul>									1
O75648	55687	<ul><li>D->A at 16: Loss of activity</li></ul>									1
O75689	11033	<ul><li>C->A at 21: Loss of GTPase-activating activity</li><li>C->A at 24: Loss of GTPase-activating activity</li><li>R->C at 149: 40-45% reduction in PtdInsP2 3-kinase dependent membrane localization. Almost complete loss of PtdInsP2 3-kinase dependent membrane localization; when associated with C-273</li><li>R->C at 273: 70% reduction in PtdInsP2 3-kinase dependent membrane localization. Almost complete loss of PtdInsP2 3-kinase dependent membrane localization; when associated with C-149</li></ul>	localization	GO:0051179			membrane	GO:0016020			1
O75695	6102	<ul><li>G->A at 2: Loss of membrane association</li><li>C->S at 3: Targeting to internal membranes. Loss of targeting to the plasma membrane</li></ul>					<li>plasma membrane</li><li>membrane</li>	<li>GO:0005886</li><li>GO:0016020</li>			1
O75716	8576	<ul><li>G->A at 2: Loss of myristoylation</li><li>C->S at 6: Loss of palmitoylation</li><li>C->S at 8: Loss of palmitoylation</li></ul>									1
O75807	23645	<ul><li>KVRF->AAAA at 555-558: Reduces interaction with SMARCB1</li><li>VRF->ARA at 556-558: Impairs PP1 activation</li><li>R->K at 612: Reduces PP1-binding; when associated with K-614</li><li>R->K at 614: Reduces PP1-binding; when associated with K-612</li><li>R->D at 618: Reduces PP1-binding</li></ul>			binding	GO:0005488			<li>P80074</li><li>P48488</li><li>Q63447</li><li>Q12824</li><li>Q61041</li><li>P50391</li><li>P30366</li><li>P48487</li><li>P22198</li><li>O42467</li><li>Q5ZK40</li><li>Q5BIN2</li>		1
O75843	8906	<ul><li>L->G at 369: Greatly diminishes interaction with ubiquitin; when associated with G-372</li><li>A->G at 372: Greatly diminishes interaction with ubiquitin; when associated with G-369</li><li>A->G at 372: Greatly diminishes interaction with ubiquitin; when associated with G-376</li><li>S->G at 376: Greatly diminishes interaction with ubiquitin; when associated with G-372</li></ul>							<li>P69326</li><li>P08565</li><li>P69322</li><li>P69323</li><li>P69324</li><li>P69325</li><li>P68196</li><li>O46543</li><li>P68197</li><li>Q05550</li><li>P68198</li><li>P68199</li><li>P19848</li><li>P42739</li><li>P68195</li><li>Q867C2</li><li>P62991</li><li>P62990</li><li>P61863</li><li>P61864</li><li>P61862</li><li>Q867C4</li><li>Q867C3</li><li>P23398</li><li>P68204</li><li>P84589</li><li>Q865C5</li><li>P42740</li><li>P68201</li><li>Q8MKD1</li><li>P14792</li><li>P63049</li><li>P0C072</li><li>P63051</li><li>P69308</li><li>P69309</li><li>P20685</li><li>P15174</li><li>P62976</li><li>P62977</li><li>P62974</li><li>P62975</li><li>P62972</li><li>P13117</li><li>P14624</li><li>P62973</li><li>P46574</li><li>P69310</li><li>P69313</li><li>P69314</li><li>P69311</li><li>P08618</li><li>P69312</li><li>P69317</li><li>P69318</li><li>P69315</li><li>P0C014</li><li>P69316</li><li>P59263</li><li>P69319</li><li>P49634</li><li>P49635</li><li>Q9Y848</li><li>P22589</li><li>P62988</li><li>P62989</li><li>P69321</li><li>P23324</li><li>P69320</li><li>P59669</li>		1
O75884	10741	<ul><li>L->Q at 63: Loss of retinoblastoma protein binding</li></ul>			protein binding	GO:0005515					1
O75888	8741	<ul><li>RKRR->AKRA at 101-104: Abolishes proteolytic processing</li></ul>									1
O75900	8510	<ul><li>R->G at 78: Abolishes processing of soluble form</li></ul>									1
O75923	8291	<ul><li>V->D at 67: Reduces calcium-sensitive phospholipid binding and interaction with AHNAK and AHNAK2</li></ul>			phospholipid binding	GO:0005543			Q09666		1
O75925	8554	<ul><li>C->A,S at 351: Loss of UBE2I-binding; almost complete loss of promotion of TP53 sumoylation; no loss of SUMO1- and TP53-binding</li></ul>	sumoylation	GO:0016925	binding	GO:0005488			<li>Q2EF74</li><li>Q9TUB2</li><li>Q5R6J4</li><li>Q2EF73</li><li>P56423</li><li>P55857</li><li>P56424</li><li>O12946</li><li>P25035</li><li>Q5E9D1</li><li>O36006</li><li>Q64662</li><li>O57538</li><li>P63279</li><li>P10360</li><li>P61260</li><li>Q9MZD5</li><li>Q9W679</li><li>Q9W678</li><li>P13481</li><li>Q9TTA1</li><li>Q95330</li><li>O93379</li><li>P41685</li><li>Q8SPZ3</li><li>Q92143</li><li>P79820</li><li>P63165</li><li>P04637</li><li>Q29537</li><li>Q29480</li><li>O09185</li><li>P63283</li><li>O09181</li><li>Q00366</li><li>P79892</li><li>P51664</li><li>Q9WUR6</li><li>P67939</li><li>P67938</li>		1
O75928	9063	<ul><li>C->S,A at 362: Loss of MDM2 and TP53 sumoylation and of autosumoylation; no loss of JUN- and TP53-binding</li><li>V->A at 467: Reduces affinity for SUMO1</li><li>V->A at 469: Abolishes binding to SUMO1</li><li>I->A at 470: Abolishes binding to SUMO1</li><li>L->A at 472: Abolishes binding to SUMO1</li><li>T->A at 473: Reduces affinity for SUMO1</li></ul>	sumoylation	GO:0016925	binding	GO:0005488			<li>Q2EF74</li><li>Q9TUB2</li><li>Q5R6J4</li><li>P56423</li><li>P55857</li><li>P56424</li><li>O12946</li><li>P05411</li><li>P25035</li><li>Q5E9D1</li><li>Q00987</li><li>O36006</li><li>Q64662</li><li>P56950</li><li>O57538</li><li>Q7YRZ8</li><li>P10360</li><li>P56951</li><li>P61260</li><li>Q9MZD5</li><li>O77627</li><li>Q9W679</li><li>Q9W678</li><li>P13481</li><li>Q9TTA1</li><li>P18870</li><li>Q95330</li><li>P12981</li><li>O93379</li><li>P41685</li><li>Q8SPZ3</li><li>Q92143</li><li>P79820</li><li>P63165</li><li>P54864</li><li>Q29537</li><li>P04637</li><li>Q60524</li><li>Q29480</li><li>P05412</li><li>P56432</li><li>O09185</li><li>Q00366</li><li>P79892</li><li>P51664</li><li>Q9WUR6</li><li>P67939</li><li>P67938</li>		1
O75943	5884	<ul><li>K->E at 143: Impairs phosphorylation on S-656. Abolishes interaction with the RAD1-RAD9-HUS1 complex; does not affect interaction with RFC3</li><li>K->G at 143: Impairs phosphorylation. Impairs interaction with DNA and the RAD1-RAD9-HUS1 complex; does not affect interaction with RFC3</li><li>S->A at 191: No effect on phosphorylation by ATR</li><li>S->A at 646: Reduces by 50% phosphorylation by ATR, and abolishes interaction with RAD1. Abolishes phosphorylation by ATR and checkpoint activation without affecting interaction with RFC3, RFC4, ATM or ATR; when associated with A-656</li><li>S->D at 646: Abolishes interaction with RAD1; when associated with D-656</li><li>S->A at 656: Reduces by 50% phosphorylation by ATR, and abolishes interaction with RAD1. Abolishes phosphorylation by ATR and checkpoint activation without affecting interaction with RFC3, RFC4, ATM or ATR; when associated with A-646</li><li>S->D at 656: Abolishes interaction with RAD1; when associated with D-646</li></ul>	phosphorylation	GO:0016310					<li>P14737</li><li>P38629</li><li>Q6PQD5</li><li>P55043</li><li>P55042</li><li>O74111</li><li>Q5R7X9</li><li>P35249</li><li>Q9M3G7</li><li>P40339</li><li>P20848</li><li>Q13315</li><li>Q13535</li><li>P06777</li><li>Q2TBV1</li><li>O60921</li><li>Q9H6X2</li><li>Q9FKS4</li><li>O60671</li><li>P40938</li><li>Q9LKI5</li>		1
O75952	26256	<ul><li>T->A at 146: Does not affect phosphorylation</li><li>T->A at 151: Decreases phosphorylation. Abolishes phosphorylation; when associated with A-155</li><li>S->A at 154: Does not affect phosphorylation. Does not affect phosphorylation; when associated with A-159</li><li>S->A at 155: Decreases phosphorylation and interaction with GSK3B. Abolishes phosphorylation and decreases interaction with GSK3B; when associated with A-151</li><li>T->A at 159: Does not affect phosphorylation. Does not affect phosphorylation; when associated with A-154</li></ul>	phosphorylation	GO:0016310					<li>Q5YJC2</li><li>P49841</li>		1
O75962	7204	<ul><li>E->A at 1240: 50% decrease in nucleotide exchange activity</li><li>T->A at 1244: 40% decrease in nucleotide exchange activity</li><li>N->A at 1330: No change in nucleotide exchange activity</li><li>V->A at 1367: 90% decrease in nucleotide exchange activity</li><li>Q->A at 1368: 80% decrease in nucleotide exchange activity</li><li>R->A at 1369: 80% decrease in nucleotide exchange activity</li><li>T->A at 1371: 80% decrease in nucleotide exchange activity</li><li>K->A at 1372: Loss of nucleotide exchange activity</li><li>L->A at 1375: 40% decrease in nucleotide exchange activity</li><li>K->A at 1378: No change in nucleotide exchange activity</li><li>E->A at 1379: 30% decrease in nucleotide exchange activity</li></ul>									1
O75969	10566	<ul><li>L->P at 131: Abolishes interaction with ROPN1</li></ul>									1
O75970	8777	<ul><li>GLGF->PSES at 147-150: Loss of interaction with CAMK2A</li></ul>							<li>Q5RCC4</li><li>Q9UQM7</li>		1
O75971	10302	<ul><li>L->A at 8: Reduced SNAPC4 binding in both the presence or absence of SNAPC1</li><li>L->A at 18: Minimal effect on SNAPC4 binding in the absence of SNAPC1. Reduced SNAPC4 binding in the presence of SNAPC1</li></ul>			binding	GO:0005488			<li>Q4R6W9</li><li>Q16533</li><li>Q5SXM2</li>		1
O76064	9025	<ul><li>R->A at 42: Abolishes interaction with ATM-phosphorylated MDC1</li><li>C->S at 403: Marked reduction of E2-dependent ubiquitination of histone H2A. Loss of UBE2E2- and UBE2N-binding. Loss of nuclear localization</li></ul>	localization	GO:0051179	<li>binding</li><li>E2</li>	<li>GO:0005488</li><li>GO:0004840</li>			<li>Q6PQD5</li><li>Q6WV67</li><li>Q6WV66</li><li>Q6WV69</li><li>Q8X132</li><li>O13413</li><li>Q9M531</li><li>P27325</li><li>O74268</li><li>P02264</li><li>Q6C4I6</li><li>P21896</li><li>Q767L8</li><li>Q8SSG3</li><li>Q6PV61</li><li>Q8I0T3</li><li>Q7YR40</li><li>P02269</li><li>P02268</li><li>P35061</li><li>Q14676</li><li>P59890</li><li>Q96LR5</li><li>Q9HGX4</li><li>P35066</li><li>Q2U5A8</li><li>P02270</li><li>Q4R4I1</li><li>P13912</li><li>P40280</li><li>Q5R7J6</li><li>Q6WV88</li><li>Q9M3G7</li><li>P55897</li><li>P40279</li><li>Q13315</li><li>Q6CK59</li><li>P84056</li><li>P84055</li><li>P84057</li><li>P84052</li><li>P50567</li><li>P84051</li><li>P84054</li><li>P84053</li><li>P82897</li><li>P19178</li><li>P19177</li><li>Q4HTT1</li><li>P61088</li><li>Q5KMT5</li><li>Q5G578</li><li>Q5TM68</li><li>Q4WWC6</li><li>Q875B8</li><li>P08844</li><li>P40282</li><li>P09588</li><li>P13630</li><li>Q4PEF9</li>		1
O76082	6584	<ul><li>M->R at 352: Loss of both carnitine and organic cation transport functionalities</li></ul>	organic cation transport	GO:0015695							1
O94759	7226	<ul><li>M->I at 1397: Only slight effect on activity</li></ul>									1
O94766	26229	<ul><li>C->A at 33: Loss of dimer formation and reduced activity</li><li>C->A at 301: Enzyme inactivation and loss of glycosylation</li></ul>									1
O94768	9262	<ul><li>K->A at 62: Loss of activity and of apoptotic function</li></ul>									1
O94782	7398	<ul><li>C->S at 90: Loss of catalytic activity including autolysis</li><li>GG->AA at 670-671: Loss of autolysis-mediated degradation upon UV irradiation. No effect on catalytic activity</li></ul>			catalytic activity	GO:0003824					1
O94810	8786	<ul><li>S->A at 245: Diminishes interaction with Gbeta5</li><li>W->F at 274: Diminishes interaction with Gbeta5</li></ul>							<li>O14775</li><li>Q6PNB6</li><li>P62881</li><li>Q5RDY7</li><li>Q80ZD0</li><li>P62882</li>		1
O94830	23259	<ul><li>S->A at 351: Abolishes phospholipase activity</li></ul>			phospholipase activity	GO:0004620					1
O94905	11160	<ul><li>N->Q at 106: Loss of glycosylation</li></ul>									1
O94985	22883	<ul><li>NP->AA at 913-914: Abolishes interaction with APBA2</li><li>Y->A at 918: No effect on APBA2-binding</li></ul>			binding	GO:0005488			<li>Q99767</li><li>Q5RD33</li>		1
O94992	10614	<ul><li>KHRR->ILAA at 152-155: Abolishes interaction with 7SK snRNA</li><li>RRR->AAA at 154-156: Abolishes interaction with 7SK snRNA</li><li>Y->D at 203: Abolishes interaction with P-TEFb; when associated with D-205</li><li>T->D at 205: Abolishes interaction with P-TEFb. Same effect; when associated with D-203</li><li>F->A,D,K at 208: Partial loss of function</li><li>Y->A,E at 271: Loss of function</li><li>L->A at 287: Loss of oligomerization; when associated with A-294; A-332 and A-339. Loss of function and interaction with P-TEFb; when associated with A-294</li><li>L->A at 294: Loss of oligomerization; when associated with A-287; A-332 and A-339. Loss of function and interaction with P-TEFb; when associated with A-287</li><li>L->A at 332: Loss of oligomerization; when associated with A-287; A-294 and A-339</li><li>L->A at 339: Loss of oligomerization; when associated with A-287; A-294 and A-332</li></ul>									1
O95071	51366	<ul><li>C->A at 2768: Loss of ubiquitin binding</li></ul>			binding	GO:0005488			<li>P69326</li><li>P08565</li><li>P69322</li><li>P69323</li><li>P69324</li><li>P69325</li><li>P68196</li><li>O46543</li><li>P68197</li><li>Q05550</li><li>P68198</li><li>P68199</li><li>P19848</li><li>P42739</li><li>P68195</li><li>Q867C2</li><li>P62991</li><li>P62990</li><li>P61863</li><li>P61864</li><li>P61862</li><li>Q867C4</li><li>Q867C3</li><li>P23398</li><li>P68204</li><li>P84589</li><li>Q865C5</li><li>P42740</li><li>P68201</li><li>Q8MKD1</li><li>P14792</li><li>P63049</li><li>P0C072</li><li>P63051</li><li>P69308</li><li>P69309</li><li>P20685</li><li>P15174</li><li>P62976</li><li>P62977</li><li>P62974</li><li>P62975</li><li>P62972</li><li>P13117</li><li>P14624</li><li>P62973</li><li>P46574</li><li>P69310</li><li>P69313</li><li>P69314</li><li>P69311</li><li>P08618</li><li>P69312</li><li>P69317</li><li>P69318</li><li>P69315</li><li>P0C014</li><li>P69316</li><li>P59263</li><li>P69319</li><li>P49634</li><li>P49635</li><li>Q9Y848</li><li>P22589</li><li>P62988</li><li>P62989</li><li>P69321</li><li>P23324</li><li>P69320</li><li>P59669</li>		1
O95140	9927	<ul><li>K->A,T at 109: Does not affect its ability to cluster mitochondria; when overexpressed</li><li>S->N at 110: Does not affect its ability to cluster mitochondria; when overexpressed</li><li>R->L at 259: Does not affect its ability to cluster mitochondria; when overexpressed</li><li>GGV->AAL at 622-624: Does not affect the targeting to mitochondrial outer membrane</li><li>GGV->RRE at 622-624: Abolishes the targeting to mitochondrial outer membrane</li><li>KER->TGV at 657-659: Does not affect the targeting to mitochondrial outer membrane</li></ul>					mitochondrial outer membrane	GO:0005741			1
O95149	10073	<ul><li>R->A at 27: Abolishes interaction with KPNB1 and m3G-cap U1 snRNP import receptor activity</li><li>W->A at 107: Reduces binding to m3G-cap structure, interaction with XPO1 and snRNP import receptor activity</li><li>FRFYW->A at 203-207: Reduces binding to m3G-cap structure</li><li>W->A at 276: Reduces binding to m3G-cap structure, interaction with XPO1 and snRNP import receptor activity</li></ul>			<li>binding</li><li>receptor activity</li>	<li>GO:0005488</li><li>GO:0004872</li>	snRNP	GO:0030532	<li>Q14974</li><li>O14980</li><li>P30822</li>		1
O95155	10277	<ul><li>D->A at 109: Abolishes cleavage by caspase-3 and caspase-7</li><li>D->A at 121: Abolishes cleavage by caspase-6. No effect on cleavage by granzyme B</li><li>D->A at 123: Abolishes cleavage by caspase-6 and granzyme B</li></ul>							P18291		1
O95159	7542	<ul><li>C->A at 27: Impairs the interaction with OLGA2/GM130 and cis-Golgi assembly</li><li>C->A at 53: Impairs the interaction with OLGA2/GM130 and cis-Golgi assembly</li></ul>							Q62225		1
O95237	9227	<ul><li>C->A,S at 161: Loss of activity</li><li>C->A at 168: Loss of activity</li><li>C->S at 168: Does not affect activity</li><li>C->A at 182: Does not affect activity</li><li>C->A at 208: Does not affect activity</li></ul>									1
O95251	11143	<ul><li>C->A at 371: No interaction with MCM2 and ORC1L</li></ul>							<li>Q58DC8</li><li>P33993</li><li>Q9JI69</li><li>Q13415</li><li>P49736</li><li>P29469</li>		1
O95267	10125	<ul><li>R->E at 271: Loss of function; prevents Ras activation</li><li>Y->F at 549: Loss of localization to the endoplasmic reticulum and the Golgi apparatus</li></ul>	localization	GO:0051179			<li>Golgi apparatus</li><li>endoplasmic reticulum</li>	<li>GO:0005794</li><li>GO:0005783</li>	<li>P03967</li><li>Q07152</li><li>P22126</li>		1
O95271	8658	<ul><li>H->A at 1184: Loss of activity; when associated with A-1291</li><li>E->A at 1291: Loss of activity; when associated with A-1184</li></ul>									1
O95278	7957	<ul><li>K->A at 87: Partial loss of phosphatase activity. Abolishes glycogen binding</li><li>D->A at 235: Loss of phosphatase activity. Does not affect glycogen binding</li><li>C->S at 266: Complete loss of phosphatase activity. Does not affect glycogen binding. Does not affect self-interaction. Increases the interaction with PPP1R5</li></ul>			binding	GO:0005488			<li>Q5X1E5</li><li>Q7M7K5</li><li>Q7MAZ9</li><li>Q8XBL4</li><li>Q88A53</li><li>Q5P3T0</li><li>Q7MBF4</li><li>Q8Z3M9</li><li>Q5PC82</li><li>Q5ZRX9</li><li>Q821A6</li><li>Q87SK9</li><li>Q9JZ88</li><li>Q9CP21</li><li>Q82U82</li><li>Q9I5V3</li><li>Q5F8K9</li><li>Q63YC3</li><li>Q8Y395</li><li>Q6LV05</li><li>Q8ZLY4</li><li>Q6FA38</li><li>Q9PDL7</li><li>Q62EU1</li><li>Q9JUB2</li><li>Q5WT58</li><li>Q665U9</li><li>Q57JQ5</li><li>Q9KPC6</li><li>Q8P5D4</li><li>Q8CWL6</li><li>Q8PPG9</li><li>P06961</li><li>P45269</li><li>Q9L7A3</li><li>Q88QU2</li><li>Q6D160</li><li>Q8ZI64</li><li>Q60CQ4</li><li>Q87DS9</li><li>Q65Q41</li><li>Q5E2K7</li><li>Q8CXX6</li>		1
O95297	9019	<ul><li>Y->F at 241: Significantly decreases phosphorylation. Complete loss of phosphorylation; when associated with F-263</li><li>Y->F at 263: Significantly decreases phosphorylation. Complete loss of phosphorylation; when associated with F-241</li></ul>	phosphorylation	GO:0016310							1
O95373	10527	<ul><li>K->A,D at 61: Lowered affinity for RanGTP-binding</li></ul>			binding	GO:0005488					1
O95391	10569	<ul><li>R->N at 116: Abolishes nuclear localization</li><li>K->N at 117: Abolishes nuclear localization</li><li>C->S at 120: Induces a cytoplasmic localization; when associated with S-123; G-128 and S-133</li><li>C->S at 123: Induces a cytoplasmic localization; when associated with S-120; G-128 and S-133</li><li>AM->VP at 125-126: Does not affect nuclear localization</li><li>H->G at 128: Induces a cytoplasmic localization; when associated with S-120; S-123 and S-133</li><li>K->N at 129: Abolishes nuclear localization</li><li>C->S at 133: Induces a cytoplasmic localization; when associated with S-120; S-123 and G-128</li><li>R->N at 136: Abolishes nuclear localization</li><li>K->N at 166: Abolishes nuclear localization</li></ul>	localization	GO:0051179							1
O95394	5238	<ul><li>S->A at 64: Loss of activity</li><li>H->A at 65: Loss of activity</li><li>D->A,E at 278: Loss of activity</li><li>R->A,K at 281: Loss of activity</li></ul>									1
O95398	10411	<ul><li>L->W at 315: Abolishes activation of RAP1A</li><li>R->K at 321: Reduces activation of RAP1A</li><li>F->A,T at 342: Diminishes GEF activity dependence on cAMP concentration</li></ul>							<li>Q9NR83</li><li>Q6Q9I2</li><li>P62833</li><li>P62834</li>		1
O95405	9372	<ul><li>Y->A at 782: Diminishes complex formation with SMAD2</li><li>Y->E at 782: Diminishes complex formation with SMAD2</li><li>C->A at 783: Diminishes complex formation with SMAD2</li><li>C->E at 783: Diminishes complex formation with SMAD2</li><li>P->A at 788: Diminishes complex formation with SMAD2</li><li>P->E at 788: Diminishes complex formation with SMAD2</li><li>V->A at 805: Diminishes complex formation with SMAD2</li><li>V->E at 805: Diminishes complex formation with SMAD2</li></ul>							<li>Q15796</li><li>Q1W668</li>		1
O95429	9530	<ul><li>E->A at 414: Reduces interaction with HSP70</li><li>D->A at 424: Abolishes interaction with HSP70</li><li>RK->AA at 438-439: Reduces interaction with HSP70</li><li>Q->A at 446: Abolishes interaction with HSP70</li></ul>							<li>P27541</li><li>Q8RB68</li><li>Q73GL7</li><li>P27542</li><li>Q6AMQ3</li><li>Q8DF66</li><li>Q71ZJ7</li><li>P56836</li><li>Q7NAU6</li><li>Q3IUI0</li><li>Q8RH05</li><li>Q6B8V2</li><li>Q92260</li><li>P19993</li><li>Q892R0</li><li>P69377</li><li>Q01100</li><li>Q3Z601</li><li>Q47HK2</li><li>Q9ZAD3</li><li>Q8YE76</li><li>Q39JC8</li><li>Q9HHB9</li><li>P69376</li><li>Q5QXL1</li><li>Q5YNI0</li><li>Q818E9</li><li>P14834</li><li>O83246</li><li>Q49Y22</li><li>P30722</li><li>P16394</li><li>P30721</li><li>P75344</li><li>Q8ZIM7</li><li>Q9ZFC6</li><li>Q74IT6</li><li>P99110</li><li>Q9WYK6</li><li>Q9L7Z1</li><li>Q634M7</li><li>P96133</li><li>Q8D2Q5</li><li>P48205</li><li>P26791</li><li>Q9RY23</li><li>Q9K0N4</li><li>P09189</li><li>Q9HRY2</li><li>Q8KEP3</li><li>P48209</li><li>Q5PAB8</li><li>Q8NLY6</li><li>P20442</li><li>Q48E62</li><li>P80462</li><li>Q4A8U5</li><li>Q6F6N3</li><li>Q87RX3</li><li>P28608</li><li>Q07437</li><li>Q87BS8</li><li>Q9HV43</li><li>Q7MN85</li><li>Q74H59</li><li>O96772</li><li>Q89YW6</li><li>O69268</li><li>Q93R27</li><li>Q7VIE3</li><li>P41753</li><li>Q8CP17</li><li>Q7VVY2</li><li>Q7W519</li><li>Q3JP10</li><li>O06942</li><li>Q4JXX6</li><li>O85282</li><li>P91902</li><li>Q6G1F9</li><li>Q6F149</li><li>P50019</li><li>P40918</li><li>Q5WV15</li><li>O87777</li><li>Q92BN8</li><li>Q493S7</li><li>Q91233</li><li>O93866</li><li>P47547</li><li>Q8Z9R1</li><li>Q8K624</li><li>Q65U55</li><li>P11503</li><li>P0A5C0</li><li>P83709</li><li>Q5H186</li><li>Q01233</li><li>P94317</li><li>Q5FFM4</li><li>Q5UQ49</li><li>Q6D0B7</li><li>P0A6Y9</li><li>P0A6Y8</li><li>Q49539</li><li>Q5M6D1</li><li>Q8EHT7</li><li>Q45551</li><li>Q8PAK9</li><li>O86103</li><li>P50023</li><li>Q67S54</li><li>Q661A3</li><li>Q5X3M7</li><li>Q5NPS6</li><li>Q5M1T8</li><li>Q05981</li><li>O68191</li><li>Q8GH79</li><li>P95334</li><li>P0A3J2</li><li>P0A3J3</li><li>Q4QJW4</li><li>P0A3J0</li><li>P0A3J1</li><li>P0A3J4</li><li>P12795</li><li>Q7N8Y4</li><li>P08108</li><li>Q48RR3</li><li>Q7NXI3</li><li>Q9WWG9</li><li>Q9UXR0</li><li>P57870</li><li>Q6L0S7</li><li>P80692</li><li>Q6MB26</li><li>P95829</li><li>P59565</li><li>P0A6Z0</li><li>O06430</li><li>Q52701</li><li>Q4L6T0</li><li>P08106</li><li>P29215</li><li>Q64X01</li><li>O87384</li><li>Q3KIA0</li><li>P0A5B9</li><li>P02827</li><li>P41797</li><li>P87047</li><li>Q6G554</li><li>P05646</li><li>Q9L7P1</li><li>Q54215</li><li>Q8G6W1</li><li>Q47TI0</li><li>O33522</li><li>Q05647</li><li>P27894</li><li>Q05746</li><li>Q6MT06</li><li>O33528</li><li>P64410</li><li>Q9ZMW4</li><li>P08418</li><li>Q6GGC0</li><li>P0C0C6</li><li>Q84BU4</li><li>Q5HAY1</li><li>P37899</li><li>Q4KIH1</li><li>Q3APD2</li><li>O52064</li><li>Q9JVQ9</li><li>Q8FXX2</li><li>P05456</li><li>P26823</li><li>Q57TP3</li><li>P27094</li><li>P61443</li><li>Q72IK5</li><li>Q68XI2</li><li>Q24789</li><li>Q5HFI0</li><li>Q56235</li><li>Q4UJK7</li><li>Q97BG8</li><li>Q5HNW6</li><li>Q4AAR4</li><li>Q2SSB0</li><li>P61442</li><li>Q37106</li><li>Q4FNP9</li><li>Q3YRR6</li><li>Q5FSL5</li><li>Q5NFG7</li><li>Q6NCY4</li><li>O32464</li><li>Q6AC76</li><li>P29133</li><li>Q02028</li><li>Q9PB05</li><li>P68837</li><li>Q9ZDX9</li><li>Q66ET0</li><li>Q730M1</li><li>Q72DW8</li><li>Q32KA5</li><li>Q3K3T2</li><li>P26413</li><li>P43736</li><li>Q62HD5</li><li>P48720</li><li>Q3IYM7</li><li>Q93GF1</li><li>Q05945</li><li>Q46XI7</li><li>Q57AD7</li><li>Q9ZIV1</li><li>Q9KWS7</li><li>Q3BVB8</li><li>Q5HV33</li><li>Q9PQF2</li><li>Q3J7D8</li><li>Q9XCB1</li><li>P25840</li><li>Q9TLT1</li><li>Q81LS2</li><li>P0C0C5</li><li>Q9KD72</li><li>Q00488</li><li>Q8TQR2</li><li>P94695</li><li>Q05558</li><li>Q5PDJ5</li><li>Q326K7</li><li>O05714</li><li>Q7MA35</li><li>Q9ZEJ0</li><li>Q9LCQ5</li><li>Q5F6W5</li><li>O32482</li><li>O52960</li><li>Q8XW40</li><li>Q88VM0</li><li>Q824B2</li><li>Q6NEY9</li><li>Q4FPS9</li><li>Q85FW4</li><li>Q7NDH1</li><li>P49463</li><li>Q65H54</li><li>O05700</li><li>P81875</li><li>Q5LG30</li><li>Q5LWJ6</li><li>Q87WP0</li><li>Q5WHG1</li><li>Q3ZYV1</li><li>Q88DU2</li><li>O69298</li><li>Q92J36</li><li>Q6YPM1</li><li>Q5ZTY3</li><li>Q98QY7</li><li>Q4A658</li><li>Q8EUH7</li><li>P78983</li><li>Q8KML6</li><li>P17804</li><li>Q8CWT3</li><li>Q3Z6P1</li><li>Q56073</li><li>Q5GSE1</li><li>O27351</li><li>Q3SIN4</li><li>Q4UT11</li><li>Q3IC08</li><li>P71331</li><li>Q7VQL4</li><li>Q3AF08</li><li>P55994</li><li>Q95YL7</li><li>O87712</li><li>Q91291</li><li>P11144</li><li>P11143</li><li>Q7UM31</li><li>Q5P1H5</li><li>P11145</li><li>Q73Q16</li><li>Q8FM78</li><li>Q98DD1</li><li>O67118</li><li>Q3KLV7</li><li>Q6HDK7</li><li>Q835R7</li><li>Q46I76</li><li>P17821</li><li>Q00043</li><li>P45554</li><li>P17820</li><li>P81341</li><li>Q4ZNP7</li><li>P64407</li><li>O34241</li><li>Q313S2</li><li>Q8PMB0</li><li>P64409</li><li>P64408</li><li>Q465Y6</li><li>Q9S5A4</li><li>Q7WGI4</li><li>Q38W93</li><li>Q6KIH7</li><li>Q5XAD6</li><li>Q8K9Y8</li><li>Q3SW76</li><li>P42374</li><li>Q8EPW4</li><li>Q83MH5</li><li>Q6MNF8</li><li>P42373</li><li>Q6G8Y7</li><li>Q607A5</li><li>Q3A8C2</li><li>Q5KWZ7</li>		1
O95445	55937	<ul><li>N->Q at 135: Loss of glycosylation</li><li>N->Q at 148: No loss of glycosylation</li></ul>									1
O95453	5073	<ul><li>D->A at 28: Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs</li><li>D->C at 28: Loss of function in the presence of Mg(2+) but not in the presence of Mn(2+), Zn(2+), Co(2+) or Cd(2+)</li><li>E->A at 30: Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs</li><li>E->C at 30: Loss of function in the presence of Mg(2+), Mn(2+), Zn(2+), Co(2+) or Cd(2+)</li><li>F->A at 31: Reduced affinity for poly(A). Loss of activity</li><li>I->A at 34: Reduced affinity for poly(A). Strongly reduced activity</li><li>I->A at 113: Loss of dimerization. Loss of activity</li><li>F->A at 115: Reduced affinity for poly(A). Little effect on activity</li><li>F->A at 123: Loss of dimerization. Loss of activity</li><li>D->A at 292: Loss of function but does not abolish ability to bind RNA</li><li>D->C at 292: Loss of function in the presence of Mg(2+) but not in the presence of Mn(2+), Zn(2+), Co(2+) or Cd(2+)</li><li>K->A at 326: Reduced affinity for poly(A). Little effect on activity</li><li>H->A at 377: Loss of activity</li><li>D->A at 382: Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs</li><li>D->C at 382: Loss of function in the presence of Mg(2+) but not in the presence of Mn(2+), Zn(2+), Co(2+) or Cd(2+)</li></ul>									1
O95461	9215	<ul><li>DTD->NNN at 242-244: Loss of function, but does not abolish subcellular location</li><li>DQD->NNN at 334-336: Loss of function, but does not abolish subcellular location</li><li>DID->NNN at 563-565: Loss of function and abolishes subcellular location</li></ul>									1
O95470	8879	<ul><li>C->G at 218: Loss of activity</li><li>C->S at 317: Almost no activity</li><li>K->L at 353: Loss of activity</li></ul>									1
O95476	23399	<ul><li>D->N,E at 67: Abolishes phosphatase activity</li></ul>							<li>Q5X1E5</li><li>Q7M7K5</li><li>Q7MAZ9</li><li>Q8XBL4</li><li>Q88A53</li><li>Q5P3T0</li><li>Q7MBF4</li><li>Q8Z3M9</li><li>Q5PC82</li><li>Q5ZRX9</li><li>Q821A6</li><li>Q87SK9</li><li>Q9JZ88</li><li>Q9CP21</li><li>Q82U82</li><li>Q9I5V3</li><li>Q5F8K9</li><li>Q63YC3</li><li>Q8Y395</li><li>Q6LV05</li><li>Q8ZLY4</li><li>Q6FA38</li><li>Q9PDL7</li><li>Q62EU1</li><li>Q9JUB2</li><li>Q5WT58</li><li>Q665U9</li><li>Q57JQ5</li><li>Q9KPC6</li><li>Q8P5D4</li><li>Q8CWL6</li><li>Q8PPG9</li><li>P06961</li><li>P45269</li><li>Q9L7A3</li><li>Q88QU2</li><li>Q6D160</li><li>Q8ZI64</li><li>Q60CQ4</li><li>Q87DS9</li><li>Q65Q41</li><li>Q5E2K7</li><li>Q8CXX6</li>		1
O95613	5116	<ul><li>FR->AA at 3196-3197: Decrease in calmodulin binding</li><li>V->A at 3203: Decrease in calmodulin binding</li><li>RL->AA at 3208-3209: Decrease in calmodulin binding</li></ul>			binding	GO:0005488			<li>Q40302</li><li>Q8STF0</li><li>P04353</li><li>P41040</li><li>P04352</li><li>Q9GRJ1</li><li>P61860</li><li>P02594</li><li>P02595</li><li>P61861</li><li>P48976</li><li>O82018</li><li>P93171</li><li>P62184</li><li>P62144</li><li>P62145</li><li>Q5RAD2</li><li>P07463</li><li>P24044</li><li>P11121</li><li>P62149</li><li>P06787</li><li>O02367</li><li>Q6IT78</li><li>P05935</li><li>P05933</li><li>O16305</li><li>Q6PI52</li><li>P05934</li><li>Q6YNX6</li><li>Q7Y052</li><li>Q95NR9</li><li>P11118</li><li>P62157</li><li>P62156</li><li>P21251</li><li>P62155</li><li>Q5EHV7</li><li>P62154</li><li>P62152</li><li>P62151</li><li>Q7T3T2</li><li>P69097</li><li>P69098</li><li>P60206</li><li>Q9U6D3</li><li>Q9HFY6</li><li>P60205</li><li>P62158</li><li>P60204</li><li>O96102</li><li>P62201</li><li>P18061</li><li>P11120</li><li>Q8X187</li><li>P93087</li><li>O60041</li><li>Q05055</li><li>P62204</li><li>P62160</li><li>P62203</li><li>P62202</li><li>P61859</li><li>P17928</li><li>P15094</li><li>Q95NI4</li><li>Q9UWF0</li><li>P62162</li><li>P02598</li><li>P62161</li><li>P02599</li><li>Q71UH6</li><li>Q71UH5</li><li>O97341</li><li>P04464</li><li>P27165</li><li>Q39752</li><li>P84339</li><li>P27166</li><li>P23286</li><li>O94739</li><li>P27161</li><li>P41041</li><li>Q6R520</li>		1
O95628	4850	<ul><li>L->A,E at 16: Abolishes interaction with E2 ubiquitin ligases</li><li>C->A at 17: Abolishes interaction with E2 ubiquitin ligases</li><li>M->A at 18: Strongly reduces interaction with E2 ubiquitin ligases</li><li>C->R at 33: Abolishes interaction with E2 ubiquitin ligases</li><li>W->A at 42: Strongly reduces interaction with E2 ubiquitin ligases</li><li>R->A,E at 44: Strongly reduces interaction with E2 ubiquitin ligases</li><li>I->A,W at 45: Strongly reduces interaction with E2 ubiquitin ligases</li><li>E->A at 49: Strongly reduces interaction with E2 ubiquitin ligases</li><li>P->A at 54: Strongly reduces interaction with E2 ubiquitin ligases</li><li>R->A,E at 57: Strongly reduces interaction with E2 ubiquitin ligases</li></ul>			E2	GO:0004840			<li>P69326</li><li>P08565</li><li>P69322</li><li>P69323</li><li>P69324</li><li>P69325</li><li>P68196</li><li>O46543</li><li>P68197</li><li>Q05550</li><li>P68198</li><li>P68199</li><li>P19848</li><li>P42739</li><li>P68195</li><li>Q867C2</li><li>P62991</li><li>P62990</li><li>P61863</li><li>P61864</li><li>P61862</li><li>Q867C4</li><li>Q867C3</li><li>P23398</li><li>P68204</li><li>P84589</li><li>Q865C5</li><li>P42740</li><li>P68201</li><li>Q8MKD1</li><li>P14792</li><li>P63049</li><li>P0C072</li><li>P63051</li><li>P69308</li><li>P69309</li><li>P20685</li><li>P15174</li><li>P62976</li><li>P62977</li><li>P62974</li><li>P62975</li><li>P62972</li><li>P13117</li><li>P14624</li><li>P62973</li><li>P46574</li><li>P69310</li><li>P69313</li><li>P69314</li><li>P69311</li><li>P08618</li><li>P69312</li><li>P69317</li><li>P69318</li><li>P69315</li><li>P0C014</li><li>P69316</li><li>P59263</li><li>P69319</li><li>P49634</li><li>P49635</li><li>Q9Y848</li><li>P22589</li><li>P62988</li><li>P62989</li><li>P69321</li><li>P23324</li><li>P69320</li><li>P59669</li>		1
O95630	10617	<ul><li>D->A at 348: Promotes accumulation of ubiquitin on endosomes, ablates enzymatic activity toward polyubiquitin substrate and allows ubiquitinated STAM stabilization</li></ul>					endosomes	GO:0005768	<li>P69326</li><li>P08565</li><li>P69322</li><li>P69323</li><li>P69324</li><li>P69325</li><li>P68196</li><li>O46543</li><li>P68197</li><li>Q05550</li><li>P68198</li><li>P68199</li><li>P19848</li><li>P42739</li><li>P68195</li><li>Q867C2</li><li>P62991</li><li>P62990</li><li>P61863</li><li>P61864</li><li>P61862</li><li>Q867C4</li><li>Q867C3</li><li>P23398</li><li>P68204</li><li>P84589</li><li>Q865C5</li><li>P42740</li><li>P68201</li><li>Q8MKD1</li><li>P14792</li><li>P63049</li><li>P0C072</li><li>P63051</li><li>P69308</li><li>P69309</li><li>P20685</li><li>P15174</li><li>P62976</li><li>P62977</li><li>P62974</li><li>P62975</li><li>P62972</li><li>P13117</li><li>P14624</li><li>P62973</li><li>P46574</li><li>P69310</li><li>P69313</li><li>P69314</li><li>P69311</li><li>P08618</li><li>P69312</li><li>P69317</li><li>P69318</li><li>P69315</li><li>P0C014</li><li>Q92783</li><li>P69316</li><li>P59263</li><li>P69319</li><li>P49634</li><li>P49635</li><li>Q9Y848</li><li>P22589</li><li>P62988</li><li>P62989</li><li>P69321</li><li>P23324</li><li>P69320</li><li>P59669</li>		1
O95644	4772	<ul><li>S->A at 169: No effect on subcellular localization</li><li>S->A at 172: Partial nuclear translocation</li><li>S->A at 187: No effect on subcellular localization</li></ul>	localization	GO:0051179							1
O95684	11116	<ul><li>V->F at 74: Abolishes homodimerization and leads to aggregation</li></ul>									1
O95747	9943	<ul><li>K->A at 46: Loss of autophosphorylation and kinase activity</li><li>K->M at 46: Loss of RELT, RELL1 and RELL2 phosphorylation. Retention of some autophosphorylation activity may be due to complex formation with other endogenous kinases in the assay</li></ul>	<li>phosphorylation</li><li>autophosphorylation</li>	<li>GO:0016310</li><li>GO:0046777</li>	kinase activity	GO:0016301			<li>Q969Z4</li><li>Q9N092</li>		1
O95786	23586	<ul><li>T->I at 55: No IRF3 signaling activity; no effect on dsRNA binding</li><li>K->A at 270: No IRF3 signaling activity</li></ul>			binding	GO:0005488			<li>Q4JF28</li><li>Q764M6</li><li>Q90643</li><li>Q14653</li>		1
O95832	9076	<ul><li>I->M at 32: 90% loss of HCV infection susceptibility in cell culture</li><li>E->K at 48: No effect on HCV infection susceptibility in cell culture</li></ul>									1
O95835	9113	<ul><li>K->A at 734: Loss of kinase activity, autophosphorylation, increased ploidy, prolonged duration of mitosis and lack of p53 expression</li></ul>	<li>mitosis</li><li>autophosphorylation</li>	<li>GO:0007067</li><li>GO:0046777</li>	kinase activity	GO:0016301			<li>Q9W679</li><li>Q9TUB2</li><li>Q9W678</li><li>Q9TTA1</li><li>P02340</li><li>O93379</li><li>P19559</li><li>P56423</li><li>P19558</li><li>P56424</li><li>Q8SPZ3</li><li>O12946</li><li>Q92143</li><li>P79820</li><li>Q29537</li><li>P04637</li><li>Q42578</li><li>O09185</li><li>P79892</li><li>O57538</li><li>P61260</li><li>P10361</li>		1
O95866	80739	<ul><li>Y->F at 211: Loss of tyrosine phosphorylation and loss of interaction with PTPN6 and PTPN11</li><li>Y->F at 237: Reduced level of tyrosine phosphorylation and interaction with PTPN6 and PTPN11</li></ul>	phosphorylation	GO:0016310					<li>P29350</li><li>Q90687</li><li>Q06124</li>		1
O95881	51060	<ul><li>C->S at 66: Loss of oxidase activity</li><li>C->S at 69: Loss of oxidase activity</li></ul>									1
O95931	23492	<ul><li>K->A at 31: Loss of cellular lifespan extension</li><li>W->A at 32: Loss of cellular lifespan extension</li></ul>									1
O95983	53615	<ul><li>H->K at 30: No effect. Confers strong binding to methylated CpG (in vitro); when associated with Y-30</li><li>F->A at 34: Augments DNA binding activity, irrespective of DNA methylation</li><li>F->Y at 34: Confers weak binding to methylated CpG (in vitro). Confers strong binding to methylated CpG (in vitro); when associated with K-30</li></ul>	DNA methylation	GO:0006306	<li>binding</li><li>DNA binding</li>	<li>GO:0005488</li><li>GO:0003677</li>					1
O95989	11165	<ul><li>G->A,V at 50: Loss of function</li><li>G->A at 51: Loss of function</li><li>G->A,V at 52: Loss of function</li><li>E->Q at 66: Loss of function</li><li>E->Q at 70: Loss of function</li><li>G->A at 72: Loss of function</li><li>G->A at 75: Loss of function</li><li>G->A at 78: No effect</li><li>G->V at 78: Loss of function</li><li>G->A at 82: Loss of function</li><li>F->Y at 84: Induces a strong decrease in Ap6A and [PP]-InsP4 hydrolysis, while it only weakly affects PP-InsP5 hydrolysis</li><li>H->L at 91: Induces a strong decrease in Ap6A and [PP]-InsP4 hydrolysis, while it only weakly affects PP-InsP5 hydrolysis</li></ul>									1
O95997	9232	<ul><li>R->A at 61: Abolishes ubiquitination and subsequent degradation; when associated with A-64</li><li>L->A at 64: Abolishes ubiquitination and subsequent degradation; when associated with A-61</li><li>P->A at 163: Strongly reduces transforming capability; when associated with L-170; A-172 and L-173</li><li>S->A at 165: Abolishes phosphorylation</li><li>PSPP->LSAL at 170-173: Strongly reduces transforming capability; when associated with A-163</li></ul>	phosphorylation	GO:0016310							1
O95999	8915	<ul><li>L->A at 28: Abolishes cell death-inducing capability</li><li>L->A at 41: Abolishes cell death-inducing capability</li><li>L->Q at 41: Abolishes NF-kappa-B activation and homo/hetero-dimerization</li><li>I->A at 46: Abolishes cell death-inducing capability</li><li>L->A at 47: Abolishes cell death-inducing capability</li><li>E->A at 53: Abolishes cell death-inducing capability</li><li>I->A at 55: Abolishes cell death-inducing capability</li><li>G->R at 78: Abolishes NF-kappa-B activation</li><li>R->G at 228: Abolishes MALT1-mediated cleavage</li><li>S->A at 231: Promotes NF-kappa-B activation</li></ul>	cell death	GO:0008219					Q9UDY8		1
O96017	11200	<ul><li>T->A at 68: Loss of activation and phosphorylation</li><li>D->A at 347: Loss of kinase activity</li><li>D->N at 368: Loss of autophosphorylation activity</li></ul>	<li>phosphorylation</li><li>autophosphorylation</li>	<li>GO:0016310</li><li>GO:0046777</li>	kinase activity	GO:0016301					1
O96020	9134	<ul><li>T->A at 392: Increase of steady state level</li></ul>									1
O97980	57824	<ul><li>E->A at 9: Decreased CTL recognition</li><li>E->A at 10: Decreased CTL recognition</li><li>K->A at 11: Complete loss of CTL recognition</li><li>R->A at 12: Complete loss of CTL recognition</li><li>G->A at 13: Complete loss of CTL recognition</li><li>S->A at 14: Complete loss of CTL recognition</li><li>L->A at 15: Complete loss of CTL recognition</li><li>H->A at 16: Complete loss of CTL recognition</li><li>H->R at 16: CTL recognition</li><li>V->A at 17: Decreased CTL recognition</li><li>W->A at 18: Complete loss of CTL recognition</li></ul>							P41416		1
P00367	2746	<ul><li>S->A at 501: Reduces activity and inhibition by GTP</li><li>H->A at 507: Strongly reduces inhibition by GTP</li><li>R->A at 516: Abolishes activation by ADP</li></ul>							P02783		1
P00441	6647	<ul><li>C->S at 7: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-58; S-112 and S-147</li><li>FG->EE at 51-52: Abolishes dimerization; when associated with Q-134</li><li>C->S at 58: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-112 and S-147</li><li>H->A at 81: Loss of zinc binding and enhanced tendency to form aggregates; when associated with A-84</li><li>H->S at 81: Destabilization of dimer and loss of zinc binding; when associated with S-84</li><li>D->A at 84: Loss of zinc binding and enhanced tendency to form aggregates; when associated with A-81</li><li>D->S at 84: Destabilization of dimer and loss of zinc binding; when associated with S-81</li><li>C->S at 112: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-58 and S-147</li><li>E->Q at 134: Abolishes dimerization; when associated with E-50 and E-51</li><li>C->S at 147: Enhances formation of fibrillar aggregates in the absence of bound zinc; when associated with S-7; S-58 and S-112</li></ul>			zinc binding	GO:0008270					1
P00533	1956	<ul><li>Y->F at 1016: 50% decrease in interaction with PIK3C2B. 65% decrease in interaction with PIK3C2B; when associated with F-1197. Abolishes interaction with PIK3C2B; when associated with F-1197 and F-1092</li><li>Y->F at 1092: No change in interaction with PIK3C2B. Abolishes interaction with PIK3C2B; when associated with F-1197 and F-1016</li><li>Y->F at 1110: No change in interaction with PIK3C2B</li><li>Y->F at 1172: No change in interaction with PIK3C2B</li><li>Y->F at 1197: No change in interaction with PIK3C2B. 65% decrease in interaction with PIK3C2B; when associated with F-1016. Abolishes interaction with PIK3C2B; when associated with F-1092 and F-1016</li></ul>							O00750		1
P00749	5328	<ul><li>S->E at 158: Abolishes phosphorylation, proadhesive function and ability to induce chemotactic response; when associated with E-323</li><li>S->E at 323: Abolishes phosphorylation, proadhesive function and ability to induce chemotactic response; when associated with E-158</li></ul>	phosphorylation	GO:0016310							1
P00973	4938	<ul><li>D->A at 75: Loss of activity; when associated with A-77</li><li>D->A at 77: Loss of activity; when associated with A-75</li><li>C->A at 331: Loss of activity; when associated with A-332 and A-333</li><li>F->A at 332: Loss of activity; when associated with A-331 and A-333</li><li>K->A at 333: Loss of activity; when associated with A-331 and A-332</li></ul>									1
P01008	462	<ul><li>A->K at 414: Reduces interaction with thrombin by 99%</li><li>A->Q at 414: Reduces interaction with thrombin by 80%</li></ul>							P84122		1
P01009	5265	<ul><li>M->V at 382: Oxidation-resistant inhibitor of therapeutic importance</li></ul>									1
P01024	718	<ul><li>IL->RR at 1108-1109: Impaired binding of C3d to CR2; when associated with A-1163</li><li>N->A at 1163: Impaired binding of C3d to CR2; when associated with 1108-R-R-1109</li><li>N->R at 1163: Impaired binding of C3d to CR2</li></ul>			binding	GO:0005488			P20023		1
P01034	1471	<ul><li>A->S at 25: Shows a dual distribution to the Golgi apparatus and to the mitochondria</li></ul>					Golgi apparatus	GO:0005794			1
P01100	2353	<ul><li>K->R at 128: No change in sumoylation</li><li>K->R at 192: No change in sumoylation</li><li>T->D at 232: Decreased sumoylation levels</li><li>K->R at 265: Abolishes sumoylation. No change in nuclear location nor on protein stability. Increased AP1 transactivation activity when heterodimerized with cJUN</li><li>T->D at 325: No change in sumoylation levels</li><li>T->D at 331: No change in sumoylation levels</li><li>S->A at 362: Loss of protein stability. Reduced MOS/MAPK-mediated transforming ability; when associated with A-374</li><li>S->D at 362: Increased protein stability. Increased MOS/MAPK-mediated transforming ability and no change in sumoylation levels; when associated with D-374</li><li>S->A at 374: No change in sumoylation levels. Loss of protein stability. Reduced MOS/MAPK-mediated transforming ability; when associated with A-362</li><li>S->D at 374: Increased protein stability. Increased MOS/MAPK-mediated transforming ability and no change in sumoylation levels; when associated with D-362</li></ul>	sumoylation	GO:0016925					<li>P50118</li><li>Q00859</li><li>Q8AX01</li><li>Q9C5X8</li><li>Q8AX00</li><li>Q8IU29</li><li>Q9VRA2</li><li>Q9N0E7</li><li>P27638</li><li>Q655R6</li><li>P10741</li><li>Q14CH1</li><li>Q96EN8</li><li>Q9ZTS2</li><li>Q21657</li><li>Q2UH11</li><li>P00540</li><li>Q29GM0</li><li>O77627</li><li>P17325</li><li>Q4WPE6</li><li>O42781</li><li>P10650</li><li>Q8AX02</li><li>Q41276</li><li>Q8QHF0</li><li>P05412</li><li>P56432</li><li>P87347</li><li>Q90XV7</li><li>P35631</li><li>P05627</li><li>Q90XV6</li><li>Q8LGM7</li><li>Q90XV9</li><li>Q9UV64</li><li>Q90XV8</li>		1
P01111	4893	<ul><li>R->A at 164: Loss of GTP-binding activity</li></ul>			GTP-binding	GO:0005525					1
P01112	3265	<ul><li>S->N at 17: Dominant negative. Prevents PLCE1 EGF-induced recruitment to plasma membrane</li><li>N->G at 26: Loss of interaction with PLCE1; when associated with V-12</li><li>V->A at 29: No effect on interaction with PLCE1; when associated with V-12</li><li>Y->F at 32: Loss of interaction and recruitment to plasma membrane of PLCE1; when associated with V-12</li><li>P->G at 34: No effect on interaction with PLCE1; when associated with V-12</li><li>T->S at 35: Loss of interaction with PLCE1; when associated with V-12</li><li>E->G at 37: No effect on interaction with PLCE1; when associated with V-12</li><li>D->N at 38: No effect on interaction with PLCE1; when associated with V-12</li><li>S->C at 39: No effect on interaction with PLCE1; when associated with V-12</li><li>A->T at 59: Loss of GTPase activity and creation of an autophosphorylation site</li><li>Q->I at 61: Moderately increased transformation of cultured cell lines</li><li>Q->V at 61: Strongly increased transformation of cultured cell lines</li><li>A->T at 83: GTP-binding activity reduced by factor of 30</li><li>C->S at 118: Abolishes S-nitrosylation. No stimulation of guanine nucleotide exchange</li><li>D->N at 119: Loss of GTP-binding activity</li><li>T->I at 144: GTP-binding activity reduced by factor of 25</li><li>RQ->AV at 164-165: Loss of GTP-binding activity</li><li>C->S at 181: Exclusively localized in Golgi. Non-specifically localized on all endomembranes; when associated with S-184</li><li>C->S at 184: Mainly localized in Golgi. Non-specifically localized on all endomembranes; when associated with S-181</li></ul>	autophosphorylation	GO:0046777	<li>GTPase activity</li><li>GTP-binding</li>	<li>GO:0003924</li><li>GO:0005525</li>	plasma membrane	GO:0005886	<li>Q9P212</li><li>Q9BEA0</li><li>P26224</li><li>P01132</li><li>P01133</li><li>Q95ND4</li><li>Q00968</li><li>P07522</li>		1
P01116	3845	<ul><li>R->A at 164: Loss of GTP-binding activity</li></ul>			GTP-binding	GO:0005525					1
P01236	5617	<ul><li>G->D,F,L,N,R,V, at 157: Inhibits signaling via PRLR; mutant PRL acts as PRLR antagonist</li></ul>							<li>Q8HXS1</li><li>Q3Y4G6</li><li>Q7ZZV3</li><li>P14676</li><li>O62781</li><li>P12420</li><li>P35395</li><li>P21993</li><li>P10765</li><li>P06879</li><li>Q28235</li><li>Q28318</li><li>P33090</li><li>P87495</li><li>Q28172</li><li>P33091</li><li>P55151</li><li>P33096</li><li>Q28632</li><li>Q9YGV6</li><li>P34181</li><li>P33089</li><li>O46561</li><li>P14787</li><li>P37884</li><li>Q6JTA8</li><li>P01237</li><li>P29234</li><li>P01236</li><li>P29235</li><li>P01239</li><li>P48249</li><li>P01238</li><li>Q90374</li><li>Q6UC74</li><li>P46403</li><li>Q04594</li><li>Q91094</li><li>Q91513</li><li>P22393</li><li>O93337</li><li>P43299</li><li>P01240</li><li>P48096</li><li>P51904</li><li>P17572</li><li>P43001</li><li>Q9QZL1</li><li>P16471</li><li>O62819</li><li>P40424</li><li>P09585</li>		1
P01350	2520	<ul><li>A->D at 86: Small increase in ratio of gastrin-17 versus gastrin-34 production. No change in ratio of gastrin-17 versus gastrin-34 production; when associated with F-87</li><li>Y->F at 87: Small decrease in ratio of gastrin-17 versus gastrin-34 production. No change in ratio of gastrin-17 versus gastrin-34 production; when associated with D-86</li></ul>							<li>P01351</li><li>P01352</li><li>P01350</li><li>O02686</li><li>P04563</li><li>P04564</li><li>P55885</li><li>P01354</li><li>P01353</li><li>P48757</li>		1
P01375	7124	<ul><li>L->S at 105: Low activity</li><li>R->W at 108: Biologically inactive</li><li>L->F at 112: Biologically inactive</li><li>A->V at 160: Biologically inactive</li><li>S->F at 162: Biologically inactive</li><li>V->A,D at 167: Biologically inactive</li><li>E->K at 222: Biologically inactive</li></ul>									1
P01730	920	<ul><li>M->T at 432: No effect</li><li>S->A at 433: No effect</li><li>LL->AA at 438-439: Loss of Nef-induced CD4 down-modulation</li><li>S->L at 440: No effect</li><li>Missing at 457-458: Abolished interaction with SPG21 and induced T-cell activation</li></ul>	T-cell activation	GO:0042110					<li>Q9QBZ7</li><li>P20886</li><li>Q9QBZ3</li><li>O91087</li><li>P03406</li><li>P03404</li><li>P24103</li><li>Q75009</li><li>Q89842</li><li>Q77378</li><li>Q1A242</li><li>P03407</li><li>P20885</li><li>Q4R5H6</li><li>O70903</li><li>Q79671</li><li>Q9QPN3</li><li>P17664</li><li>O12165</li><li>Q29037</li><li>Q9QBY1</li><li>P04601</li><li>P04600</li><li>Q9IDV1</li><li>P05863</li><li>P15829</li><li>P17753</li><li>Q9QBY9</li><li>P04604</li><li>P04603</li><li>P04602</li><li>Q76639</li><li>P18092</li><li>P33705</li><li>Q74127</li><li>P05857</li><li>P12481</li><li>P20868</li><li>Q9Q713</li><li>P05856</li><li>P12482</li><li>P05859</li><li>Q1A260</li><li>P05858</li><li>P04324</li><li>O41804</li><li>P01730</li><li>P05855</li><li>P12447</li><li>P05854</li><li>P12480</li><li>P20867</li><li>P27970</li><li>Q5RES2</li><li>Q9NZD8</li><li>Q89868</li><li>P11262</li><li>O89293</li><li>P19546</li><li>P19545</li><li>P35959</li><li>P12479</li><li>P05860</li><li>P12478</li><li>P05861</li><li>Q9WC61</li><li>P05862</li><li>P31818</li><li>P19501</li><li>Q9XS78</li><li>Q08338</li><li>P46630</li><li>Q08336</li><li>Q08339</li><li>P05542</li><li>Q02840</li><li>P24741</li><li>P18038</li><li>P22378</li><li>Q70627</li><li>P18801</li><li>O89945</li><li>Q9QSQ6</li><li>P79185</li><li>P27979</li><li>P19032</li><li>Q08340</li><li>P16004</li><li>P79184</li><li>P16003</li><li>Q9WC70</li><li>Q8MJJ1</li>		1
P01732	925	<ul><li>G->R at 111: Prevents CD8 expression</li></ul>									1
P02545	4000	<ul><li>C->S at 661: Loss of interaction with NARF</li></ul>							Q8WVD3		1
P02786	7037	<ul><li>FSNL->YTRF at 9-12: Only 80% as active as wild-type receptor</li><li>YTRFSLARQVDGDNS at 20-34: No influence on endocytic uptake of the receptor</li><li>YTRF->PPGY at 20-23: Only 16% as active as wild-type receptor</li><li>Y->C at 20: Only 35% as active as wild-type receptor</li><li>Y->G at 20: Only 20% as active as wild-type receptor</li><li>T->F at 21: Only 88% as active as wild-type receptor</li><li>T->TA at 21: Only 14% as active as wild-type receptor</li><li>T->TAA at 21: Only 19% as active as wild-type receptor</li><li>F->Y at 23: Only 48% as active as wild-type receptor</li><li>GDNS->YTRF at 31-34: 2-fold increase of the endocytic uptake of the receptor</li><li>NADN->YTRF at 47-50: 1.27-fold increase of the endocytic uptake of the receptor</li><li>L->A at 619: 20-fold reduced affinity for transferrin receptor. No binding to HFE</li><li>V->A at 622: No significant effect on binding to transferrin nor HFE</li><li>R->A at 623: No significant effect on binding to transferrin nor HFE</li><li>R->A at 629: >5-fold reduced affinity for transferrin. >10-fold reduced affinity for HFE</li><li>Q->A at 640: No effect on binding to transferrin. >10-fold reduced affinity for HFE</li><li>W->A at 641: No significant effect on binding to transferrin nor HFE</li><li>Y->A at 643: 20-fold reduced affinity for transferrin. No binding to HFE</li><li>S->A at 644: No significant effect on binding to transferrin nor HFE</li><li>R->A,H at 646: No binding to transferrin</li><li>R->K at 646: 5% binding to transferrin</li><li>G->A at 647: Large effect on affinity for transferrin. 4-fold reduced affinity for HFE</li><li>D->A at 648: 16% binding to transferrin</li><li>D->E at 648: 57% binding to transferrin</li><li>F->Q at 650: >5-fold reduced affinity for transferrin. >10-fold reduced affinity for HFE</li></ul>			binding	GO:0005488			<li>P02787</li><li>Q9GL41</li><li>Q9GL42</li><li>Q9GL43</li><li>P12346</li><li>P60018</li><li>P27425</li><li>P09571</li><li>Q921I1</li><li>Q29443</li><li>Q9GKZ0</li><li>Q30201</li><li>P19134</li>		1
P02788	4057	<ul><li>K->A at 92: Almost no protease activity</li><li>P->V at 270: No effect</li><li>S->A at 278: No protease activity</li></ul>							<li>P19028</li><li>Q9QBZ5</li><li>P24107</li><li>Q9QBZ1</li><li>Q79666</li><li>P15833</li><li>P03362</li><li>P18042</li><li>Q8AII1</li><li>P03363</li><li>P04024</li><li>P04023</li><li>P10978</li><li>O93215</li><li>P26810</li><li>Q1A249</li><li>P03356</li><li>P03355</li><li>O41798</li><li>P20892</li><li>Q9Y6I0</li><li>P10210</li><li>Q9QBY3</li><li>P03353</li><li>P16901</li><li>Q74120</li><li>Q09SZ9</li><li>Q89928</li><li>Q73368</li><li>P84454</li><li>Q9WC63</li><li>P20825</li><li>Q9IDV9</li><li>P0C211</li><li>P0C210</li><li>P51518</li><li>Q4U0X6</li><li>P12451</li><li>P07570</li><li>P28936</li><li>O89940</li><li>P24740</li><li>P26809</li><li>P26808</li><li>Q0R5R3</li><li>Q0R5R2</li><li>P18802</li><li>P10394</li><li>P19561</li><li>P16423</li><li>P63119</li><li>P19560</li><li>Q75002</li><li>P04589</li><li>P04587</li><li>P04588</li><li>Q9QSR3</li><li>O91080</li><li>P16046</li><li>P17757</li><li>P12497</li><li>P12499</li><li>P12498</li><li>P03311</li><li>P20875</li><li>P20876</li><li>P10273</li><li>Q9WC54</li><li>P10272</li><li>P10271</li><li>P10270</li><li>P19199</li><li>P05962</li><li>P18096</li><li>P10265</li><li>P04584</li><li>P11227</li><li>P04585</li><li>Q76634</li><li>Q8I7P9</li><li>Q9Q720</li><li>P14078</li><li>P31822</li><li>P11365</li><li>P35963</li><li>P14074</li><li>P05959</li><li>P63131</li><li>P04323</li><li>P10274</li><li>P21407</li><li>O89290</li><li>P35956</li><li>P05960</li><li>P05961</li><li>Q1A267</li><li>P63122</li><li>P63123</li><li>P63124</li><li>P63125</li><li>P63120</li><li>P63121</li><li>P03366</li><li>P03367</li><li>P03369</li><li>P63127</li><li>P63128</li><li>P63129</li><li>Q77373</li><li>P03370</li><li>P27502</li><li>P21414</li>		1
P03372	2099	<ul><li>S->A at 104: Loss of cyclin A-dependent induction of transcriptional activation</li><li>S->A at 106: Loss of cyclin A-dependent induction of transcriptional activation</li><li>S->A at 118: Decrease in phosphorylation</li><li>C->A at 447: Loss of hormone binding capacity and temperature-sensitive loss in DNA-binding</li></ul>	phosphorylation	GO:0016310	<li>hormone binding</li><li>DNA-binding</li>	<li>GO:0042562</li><li>GO:0003677</li>			<li>P30274</li><li>P51943</li><li>P20248</li><li>Q92161</li><li>P43449</li><li>P37881</li>		1
P03950	283	<ul><li>D->H,S,A at 140: 15- to 18-fold increase in RNase activity</li><li>Q->G at 141: Over 18-fold increase in RNase activity</li><li>IF->AA at 143-144: 3- to 5-fold increase in RNase activity</li></ul>									1
P04004	7448	<ul><li>T->A at 69: Abolishes phosphorylation by CK2 and inhibits adhesion and spreading; when associated with A-76</li><li>T->E at 69: Abolishes phosphorylation by CK2 and enhances adhesion and spreading; when associated with E-76</li><li>T->A at 76: Abolishes phosphorylation by CK2 and inhibits adhesion and spreading; when associated with A-69</li><li>T->E at 76: Abolishes phosphorylation by CK2 and enhances adhesion and spreading; when associated with E-69</li></ul>	phosphorylation	GO:0016310					<li>Q65ZV5</li><li>P43893</li><li>O51759</li>		1
P04062	2629	<ul><li>C->S at 43: Loss of activity</li><li>C->S at 57: Loss of activity</li><li>C->S at 62: Loss of activity</li><li>E->G at 379: Decreases activity 1000-fold</li></ul>									1
P04114	338	<ul><li>D->N at 483: Impairs protein secretion</li><li>D->Q at 483: Does not affect protein secretion</li><li>R->A at 490: Impairs protein secretion</li><li>R->K at 490: Does not affect protein secretion</li></ul>	protein secretion	GO:0009306							1
P04150	2908	<ul><li>M->T at 1: Abolishes expression of A-type isoforms</li><li>M->T at 27: Abolishes expression of B-type isoforms</li><li>F->D at 191: Reduces transactivation by the ADA complex</li><li>I->D at 193: Reduces transactivation by the ADA complex</li><li>L->A at 194: Strongly reduces transactivation by the ADA complex; when associated with V-224 and F-225</li><li>L->E at 197: Reduces transactivation by the ADA complex</li><li>W->A at 213: Strongly reduces transactivation by the ADA complex</li><li>L->V at 224: Strongly reduces transactivation by the ADA complex; when associated with A-194 and F-225</li><li>L->F at 225: Strongly reduces transactivation by the ADA complex; when associated with A-194 and V-224</li><li>F->L at 235: Strongly reduces transactivation by the ADA complex; when associated with V-236</li><li>L->V at 236: Strongly reduces transactivation by the ADA complex; when associated with L-235</li><li>K->R at 277: Strongly reduces sumoylation. Almost complete loss of sumoylation; when associated with R-293</li><li>K->R at 293: Strongly reduces sumoylation. Almost complete loss of sumoylation; when associated with R-277</li><li>R->A at 585: Reduces activation mediated by ligand binding domain; when associated with A-590</li><li>D->A at 590: Reduces activation mediated by ligand binding domain; when associated with A-585</li><li>F->S at 602: Increases solubility. No effect on transactivation by dexamethasone</li><li>P->A at 625: Decreases transactivation by dexamethasone by 95%</li><li>I->A at 628: Decreases dimerization and transactivation by dexamethasone; when associated with S-602</li><li>K->R at 703: Slightly reduces sumoylation</li></ul>	sumoylation	GO:0016925	binding	GO:0005488			<li>Q5ZKP6</li><li>P56658</li><li>P00813</li>		1
P04155	7031	<ul><li>C->S at 82: Abolishes inhibition of gastric cancer cell growth</li></ul>									1
P04179	6648	<ul><li>Y->F at 58: Loss of nitration. Enhanced dityrosine formation on peroxynitrite treatment</li></ul>									1
P04424	435	<ul><li>K->N at 51: 2-fold reduction in activity</li><li>H->Q at 89: 10-fold reduction in activity</li></ul>									1
P04629	4914	<ul><li>Y->F at 496: No phosphorylation of SHC1</li><li>K->N at 544: Inactive</li><li>Y->F at 791: No phosphorylation of PLC-gamma-1. Lack of NGF-promoted increase of the peripherin protein</li></ul>	phosphorylation	GO:0016310					<li>P21807</li><li>P17810</li><li>P10686</li><li>P08487</li><li>P21617</li><li>P19174</li><li>Q90W38</li><li>P15499</li><li>P48676</li><li>Q6YBR5</li><li>P41219</li><li>O42281</li><li>P52204</li><li>P17438</li><li>P15331</li><li>P23942</li><li>P35906</li><li>Q62077</li><li>P34129</li><li>O42583</li><li>P29353</li>		1
P04637	7157	<ul><li>S->A at 46: Abolishes phosphorylation by HIPK2 and acetylation of K-382 by CREBBP</li><li>Missing at 46: Alters interaction with WWOX</li><li>T->A at 55: Blocks phosphorylation by TAF1</li><li>C->Y at 135: Decreased E6-mediated binding to E6-AP</li><li>P->D at 359: Abolishes binding to USP7</li><li>G->E at 361: Abolishes binding to USP7</li><li>S->A at 362: Abolishes binding to USP7</li><li>K->R at 370: Induces a decrease in methylation by SMYD2</li><li>K->R at 372: Induces a decrease in protein stabilization</li><li>K->A at 382: Abolishes acetylation by CREBBP</li><li>F->A at 385: Reduced SUMO1 conjugation</li><li>K->A at 386: Abolishes SUMO1 conjugation, in vitro and in vivo</li><li>T->A at 387: No effect SUMO1 conjugation</li><li>E->A at 388: Abolishes SUMO1 conjugation</li></ul>	<li>conjugation</li><li>phosphorylation</li><li>protein stabilization</li>	<li>GO:0000746</li><li>GO:0016310</li><li>GO:0050821</li>	binding	GO:0005488			<li>Q2EF74</li><li>Q5R6J4</li><li>Q9H2X6</li><li>P21675</li><li>Q99142</li><li>P55857</li><li>Q92793</li><li>Q9NZC7</li><li>P63165</li><li>P38724</li><li>Q93009</li><li>Q5F389</li><li>P46677</li><li>Q5E9D1</li><li>Q5R9W5</li><li>Q9NRG4</li><li>Q9VLU5</li><li>Q9MZD5</li>		1
P04746	279	<ul><li>R->A,Q at 210: Abolishes chloride binding; strongly reduces activity</li><li>D->A,N at 212: Abolishes activity</li><li>E->A,Q at 248: Reduces activity</li><li>N->S at 313: Reduces affinity for chloride; reduces activity</li><li>D->A,N at 315: Strongly reduces activity</li><li>R->A at 352: Abolishes chloride binding; has only slight effect on activity</li></ul>			binding	GO:0005488					1
P04908	3012	<ul><li>S->A at 2: Blocks the inhibition of transcription by RPS6KA5/MSK1</li></ul>	transcription	GO:0006350					<li>P32048</li><li>Q5R4K3</li><li>Q5F3L1</li><li>O75582</li>		1
P05067	351	<ul><li>KRGR->NQGG at 99-102: Reduced heparin-binding</li><li>H->N at 137: Binds copper. Forms dimer</li><li>M->T at 141: Binds copper. Forms dimer</li><li>C->S at 144: Binds copper. No dimer formation. No copper reducing activity</li><li>HLH->ALA at 147-149: 50% decrease in copper reducing activity</li><li>H->A at 147: Some decrease in copper reducing activity</li><li>H->N at 147: Binds copper. Forms dimer</li><li>H->Y at 147: Greatly reduced copper-mediated low-density lipoprotein oxidation</li><li>H->K at 151: Greatly reduced copper-mediated low-density lipoprotein oxidation</li><li>H->N at 151: Binds copper. Forms dimer</li><li>S->A at 198: Greatly reduced casein kinase phosphorylation</li><li>S->A at 206: Reduced casein kinase phosphorylation</li><li>R->A at 499: Reduced affinity for heparin; when associated with A-503</li><li>K->A at 503: Reduced affinity for heparin; when associated with A-499</li><li>S->A at 656: Abolishes chondroitin sulfate binding in L-APP733 isoform</li><li>R->G at 676: 60-70% zinc-induced beta-APP (28) peptide aggregation</li><li>Y->F at 681: 60-70% zinc-induced beta-APP (28) peptide aggregation</li><li>H->R at 684: Only 23% zinc-induced beta-APP (28) peptide aggregation</li><li>G->V at 704: Reduced protein oxidation. No hippocampal neuron toxicity</li><li>M->L at 706: Reduced lipid peroxidation inhibition</li><li>M->V at 706: No free radical production. No hippocampal neuron toxicity</li><li>V->C,S at 717: Unchanged beta-APP42/total APP-beta ratio</li><li>V->F,G,I at 717: Increased beta-APP42/beta-APP40 ratio</li><li>V->K at 717: Decreased beta-APP42/total APP-beta ratio</li><li>V->M at 717: Increased beta-APP42/beta-APP40 ratio. No change in apoptosis after caspase cleavage</li><li>Y->A at 728: No effect on APBA1 nor APBB1 binding. Greatly reduces the binding to APPBP2. APP internalization unchanged. No change in beta-APP42 secretion</li><li>D->A at 739: No cleavage by caspases during apoptosis</li><li>D->N at 739: No effect on FADD-induced apoptosis</li><li>T->A at 743: Greatly reduces the binding to SHC1 and APBB family members; no effect on NGF-stimulated neurite extension</li><li>T->E at 743: Reduced NGF-stimulated neurite extension. No effect on APP maturation</li><li>G->A at 756: APP internalization unchanged. No change in beta-APP42 secretion</li><li>Y->A at 757: Little APP internalization. Reduced beta-APP42 secretion</li><li>Y->G at 757: Loss of binding to MAPK8IP1, APBA1, APBB1, APPBP2 and SHC1</li><li>N->A at 759: No binding to APBA1, no effect on APBB1 binding. Little APP internalization. Reduced beta-APP42 secretion</li><li>P->A at 760: Little APP internalization. Reduced beta-APP42 secretion</li><li>Y->A at 762: Loss of binding to APBA1 and APBB1. APP internalization unchanged. No change in beta-APP42 secretion</li></ul>	<li>phosphorylation</li><li>lipoprotein oxidation</li><li>apoptosis</li><li>secretion</li>	<li>GO:0016310</li><li>GO:0042161</li><li>GO:0006915</li><li>GO:0046903</li>	<li>binding</li><li>heparin-binding</li>	<li>GO:0005488</li><li>GO:0008201</li>			<li>Q60495</li><li>P0A3Z4</li><li>Q28280</li><li>O73683</li><li>P0A3Z2</li><li>P0A3Z3</li><li>P21617</li><li>P0A3Z1</li><li>Q28757</li><li>P29216</li><li>Q02410</li><li>Q92624</li><li>Q13158</li><li>P12023</li><li>Q11207</li><li>P53601</li><li>Q29149</li><li>P29353</li><li>P75313</li><li>P79307</li><li>P08592</li><li>O00213</li><li>Q90W38</li><li>P05067</li><li>P46310</li><li>Q28748</li><li>Q6YBR5</li><li>Q28053</li><li>Q5IS80</li><li>P47566</li><li>O93279</li><li>Q95241</li><li>Q9UQF2</li><li>P34129</li>		1
P05111	3623	<ul><li>RR->AA at 56-57: Loss of cleavage; when associated with 60-AA-61</li><li>RR->AA at 60-61: Loss of cleavage; when associated with 55-AA-56</li><li>RR->EA at 231-232: Loss of cleavage</li><li>N->Q at 268: Loss of glycosylation</li><li>N->Q at 302: Loss of glycosylation</li></ul>									1
P05231	3569	<ul><li>A->V at 173: Almost no loss of activity</li><li>W->R at 185: No loss of activity</li><li>S->P at 204: 87% loss of activity</li><li>R->K,E,Q,T,A,P at 210: Loss of activity</li><li>M->T,N,S,R at 212: Loss of activity</li></ul>									1
P05546	3053	<ul><li>R->L at 122: Normal thrombin inhibition and glycosaminoglycan affinity</li><li>R->Q at 122: Greatly reduced thrombin inhibition. Normal glycosaminoglycan affinity</li><li>R->W at 122: Greatly reduced thrombin inhibition. Normal glycosaminoglycan affinity</li><li>K->M at 204: Reduced heparin- and no dermatan sulfate-activated inhibition</li><li>K->N at 204: Reduced heparin- and no dermatan sulfate-activated inhibition</li><li>K->T at 204: Reduced heparin- and no dermatan sulfate-activated inhibition</li></ul>							P84122		1
P05549	7020	<ul><li>S->A at 239: No phosphorylation</li></ul>	phosphorylation	GO:0016310							1
P05556	3688	<ul><li>G->Q at 778: Loss of beta-1A interaction with FLNA and FLNB</li><li>A->P at 786: Loss of beta-1A interaction with FLNA and FLNB</li></ul>							<li>P21333</li><li>Q9MZD2</li><li>O75369</li>		1
P05783	3875	<ul><li>S->A at 2: No effect on phosphorylation; when associated with A-7 and A-10</li><li>S->A at 7: No effect on phosphorylation; when associated with A-2 and A-10</li><li>S->A at 10: No effect on phosphorylation; when associated with A-2 and A-7</li><li>S->A at 15: No effect on phosphorylation; when associated with A-18 and A-23. Abolishes phosphorylation; when associated with A-18; A-34; A-47; A-49; A-51 and A-53</li><li>S->A at 18: No effect on phosphorylation; when associated with A-15 and A-23. Abolishes phosphorylation; when associated with A-15; A-34; A-47; A-49; A-51 and A-53</li><li>S->A at 23: No effect on phosphorylation; when associated with A-15 and A-18</li><li>S->A at 30: No effect on phosphorylation; when associated with A-31 and A-34, or with A-31; A-44 and A-51. Abolishes glycosylation but does not affect binding to YWHAE and YWHAZ; when associated with A-31 and A-49</li><li>S->A at 31: No effect on phosphorylation; when associated with A-30 and A-34, or with A-30; A-44 and A-51. Abolishes glycosylation but does not affect binding to YWHAE and YWHAZ; when associated with A-30 and A-49</li><li>S->A at 34: No effect on phosphorylation; when associated with A-30 and A-31. Abolishes phosphorylation; when associated with A-15; A-18; A-47; A-49; A-51 and A-53. Abolishes binding to YWHAE and YWHAZ; and when associated with A-53</li><li>S->D,E at 34: Abolishes binding to YWHAE and YWHAZ</li><li>S->A at 42: No effect on phosphorylation; when associated with A-44</li><li>S->A at 44: No effect on phosphorylation; when associated with A-42, or with A-30; A-31 and A-51</li><li>S->A at 47: No effect on phosphorylation; when associated with A-49. Abolishes phosphorylation; when associated with A-49; A-51 and A-53, or with A-15; A-18; A-34; A-49; A-51 and A-53</li><li>S->A at 49: No effect on phosphorylation; when associated with A-47. Abolishes phosphorylation; when associated with A-47; A-51 and A-53, or with A-15; A-18; A-34; A-47; A-51 and A-53. Abolishes glycosylation but does not affect binding to YWHAE and YWHAZ; when associated with A-30 and A-31</li><li>S->A at 51: No effect on phosphorylation; when associated with A-30; A-31 and A-47. Abolishes phosphorylation; when associated with A-47; A-49 and A-53, or with A-15; A-18; A-34; A-47; A-49 and A-53</li><li>S->A at 53: Abolishes phosphorylation; when associated with A-47; A-49 and A-51, or with A-15; A-18; A-34; A-47; A-49 and A-51. Abolishes binding to YWHAE and YWHAZ; when associated with A-34. No effect on caspase cleavage during apoptosis</li><li>R->C,H at 90: In transgenic mice, induces marked disruption of liver and pancreas keratin filament network. Increases phosphorylation and glycosylation</li><li>D->E at 238: Prevents cleavage by caspase-6 during apoptosis. Induces aggregates of keratin filaments in an altered organization</li></ul>	<li>phosphorylation</li><li>apoptosis</li>	<li>GO:0016310</li><li>GO:0006915</li>	binding	GO:0005488	keratin filament	GO:0045095	<li>P63103</li><li>P29361</li><li>Q5ZKC9</li><li>P62258</li><li>Q5R651</li><li>Q5ZMT0</li><li>P62262</li><li>P63104</li><li>P62261</li>		1
P05787	3856	<ul><li>L->P at 72: Increases phosphorylation</li><li>S->A at 74: Generates normal-appearing filaments, that remain stable after okadaic acid treatment</li><li>S->D at 74: Generates normal-appearing filaments, that are destabilized by okadaic acid</li></ul>	phosphorylation	GO:0016310							1
P06132	7389	<ul><li>D->E at 86: 5-10% of wild-type activity</li><li>D->G at 86: Very low activity. Binds substrate with similar geometry as wild-type</li><li>D->N at 86: No activity. Unable to bind substrate</li><li>Y->F at 164: 25-30% of wild-type activity</li></ul>									1
P06213	3643	<ul><li>L->A at 991: Reduces interaction with IRS1 but has no effect on interaction with SHC1</li><li>Y->A at 992: Reduces interaction with IRS1 but has no effect on interaction with SHC1</li><li>NP->AA at 996-997: Abolishes interaction with IRS1. Severely disrupts, but does not abolish interaction with SHC1</li><li>N->A at 996: Abolishes interaction with IRS1 and significantly reduces interaction with SHC1. Has no effect on interaction with PIK3R1</li><li>P->A at 997: Abolishes interaction with IRS1 and significantly reduces interaction with SHC1. Has no effect on interaction with PIK3R1</li><li>E->A at 998: Does not affect interaction with IRS1, SHC1 or PIK3R1</li><li>Y->E at 999: Abolishes interaction with IRS1 and SHC1</li><li>Y->F at 999: Has no effect on insulin-stimulated autophosphorylation, but inhibits the biological activity of the receptor. Abolishes interaction with IRS1 and almost completely prevents interaction with SHC1. Has no effect on interaction with PIK3R1</li><li>L->A,R at 1000: Severely reduces interaction with SHC1. Has no effect on interaction with IRS1</li><li>A->D at 1002: Reduces interaction with IRS1 but has no effect on interaction with SHC1</li><li>K->A at 1057: Abolishes the kinase activity and abolishes interaction with IRS1, SHC1 and PIK3R1</li><li>K->M,R at 1057: Abolishes the kinase activity</li></ul>	autophosphorylation	GO:0046777	kinase activity	GO:0016301			<li>P67974</li><li>P67973</li><li>P23727</li><li>P67971</li><li>Q28224</li><li>P69048</li><li>P01330</li><li>P0C236</li><li>P69047</li><li>P07453</li><li>P35568</li><li>P42633</li><li>P01324</li><li>P27986</li><li>P68243</li><li>P01320</li><li>P68992</li><li>P81423</li><li>P01328</li><li>P29353</li><li>P09715</li><li>Q9TQY7</li><li>P01340</li><li>P68990</li><li>P67969</li><li>P68991</li><li>P67968</li><li>P68245</li><li>P81881</li><li>P69046</li><li>P01336</li><li>P68988</li><li>P68987</li><li>P01316</li><li>P01334</li><li>P13190</li><li>P01331</li><li>P01314</li><li>P01319</li><li>P09477</li><li>P29335</li><li>P09476</li><li>P12703</li><li>P18109</li><li>P12704</li><li>P68989</li><li>P12708</li>		1
P06239	3932	<ul><li>S->E at 59: Allows interaction with SQSTM1</li><li>R->K at 154: No effect on interaction with SQSTM1</li></ul>							<li>Q5RBA5</li><li>Q13501</li>		1
P06307	885	<ul><li>Y->F at 97: Reduces the quantity of secreted CCK8 by 50%</li></ul>							<li>P80345</li><li>P23362</li><li>Q9PU29</li><li>P09240</li><li>P06307</li><li>P80344</li><li>P41520</li><li>O93464</li><li>O57312</li><li>P01356</li><li>Q9PU41</li><li>P01355</li>		1
P06729	914	<ul><li>K->R at 67: Loss of LFA-3 binding</li><li>Q->K at 70: Loss of LFA-3 binding</li><li>Y->D at 110: Loss of LFA-3 and CD59 binding</li><li>D->H at 111: Loss of LFA-3 and CD59 binding</li></ul>			binding	GO:0005488			<li>O77541</li><li>P13987</li><li>Q5R510</li><li>P47777</li><li>O62680</li><li>Q28785</li><li>Q28216</li><li>Q8SQ46</li><li>P46657</li><li>P58020</li><li>P51447</li>		1
P06730	1977	<ul><li>S->A,D at 53: No effect on phosphorylation level nor incorporation into eIF4F complex</li><li>W->L at 102: Decrease in binding; when associated with A-105</li><li>E->A at 103: No effect</li><li>D->A at 104: No effect</li><li>E->A at 105: Decrease in binding; when associated with A-105</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488					1
P06731	1048	<ul><li>F->I at 63: No effect on dimerization. Reduced affinity for E.coli Dr adhesins</li><li>F->R at 63: Abolishes dimerization. Reduced affinity for E.coli Dr adhesins</li><li>S->N at 66: Abolishes dimerization</li><li>Y->A at 68: Abolishes dimerization</li><li>Y->F at 68: No effect on dimerization</li><li>K->A at 69: Abolishes dimerization</li><li>V->A at 73: Abolishes dimerization</li><li>D->A at 74: No effect on dimerization</li><li>D->L,R at 74: Abolishes dimerization</li><li>Q->L,R at 78: Abolishes dimerization. Reduced affinity for E.coli Dr adhesins</li><li>I->A at 125: Abolishes dimerization. Reduced affinity for E.coli Dr adhesins</li><li>L->A,C at 129: No effect on dimerization. Reduced affinity for E.coli Dr adhesins</li><li>L->S at 129: Abolishes dimerization. Reduced affinity for E.coli Dr adhesins</li><li>E->A at 133: Abolishes dimerization</li></ul>							<li>P31522</li><li>Q9CB42</li><li>Q56982</li><li>P42188</li><li>P0A5P7</li><li>P0A5P6</li>		1
P06733	2023	<ul><li>M->I at 94: MBP1 protein production. No MBP1 protein production; when associated with I-97</li><li>M->I at 97: MBP1 protein production. No MBP1 protein production; when associated with I-94</li><li>L->A at 384: Loss of transcriptional repression and cell growth inhibition; when associated with A-388</li><li>L->A at 388: Loss of transcriptional repression and cell growth inhibition; when associated with A-384</li></ul>							<li>Q66S41</li><li>Q66S50</li><li>Q66S60</li><li>Q66S61</li><li>Q66S62</li><li>Q66S63</li><li>Q66S54</li><li>Q66S65</li><li>Q66S64</li><li>Q66S37</li><li>P11226</li><li>Q66S45</li><li>Q66S58</li><li>P39678</li><li>P39679</li><li>P55034</li><li>P22032</li>		1
P06746	5423	<ul><li>K->Q,R at 35: Reduces DNA lyase activity slightly</li><li>Y->Q at 39: Abolishes DNA polymerase and DNA lyase activity</li><li>K->Q,R at 68: Reduces DNA lyase activity slightly</li><li>K->Q,R at 72: Abolishes DNA lyase activity. No effect on DNA polymerase activity</li><li>K->R at 84: No effect</li></ul>			lyase activity	GO:0016829			<li>Q9YUS3</li><li>O59610</li><li>Q9YUS2</li><li>P56689</li><li>P06538</li><li>Q69025</li><li>Q9HH84</li><li>P04495</li><li>P43139</li><li>Q56366</li><li>P77933</li><li>P03261</li><li>P19894</li><li>P52025</li><li>P03158</li><li>Q6S6P1</li><li>Q85428</li><li>P09252</li><li>O64235</li><li>P03198</li><li>P52367</li><li>P28859</li><li>P74918</li><li>P52342</li><li>O72539</li><li>P20311</li><li>O70736</li><li>P28857</li><li>P28858</li><li>P20509</li><li>Q9HH05</li><li>Q88469</li><li>P61875</li><li>P61876</li><li>O72540</li><li>Q05254</li><li>Q64751</li><li>P06950</li><li>P06856</li><li>P05664</li><li>Q83948</li><li>P05468</li><li>P08546</li><li>O71121</li><li>Q37882</li><li>P19822</li><li>P10479</li><li>Q58295</li><li>P87553</li><li>P30321</li><li>P30320</li><li>P10582</li><li>P21402</li><li>Q51334</li><li>O33845</li><li>P42489</li><li>P18131</li><li>O27276</li><li>P09804</li><li>P24907</li><li>P41712</li><li>Q84173</li><li>P48311</li><li>P33793</li><li>O57191</li><li>P04415</li><li>P03680</li><li>P00581</li><li>Q5UQR0</li><li>Q90162</li><li>P87503</li><li>Q37989</li><li>P04292</li><li>P30318</li><li>P04293</li><li>P30317</li><li>Q65946</li><li>Q38087</li><li>P07917</li><li>O29753</li><li>P07918</li><li>P30319</li><li>P06225</li><li>P27172</li><li>P30314</li><li>P09854</li>		1
P07225	5627	<ul><li>R->A,E at 515: Markedly reduced secretion of the mutant</li><li>R->K at 515: No change in secretion of the mutant</li></ul>	secretion	GO:0046903							1
P07320	1421	<ul><li>PN->TK at 24-25: Wild-type solubility</li><li>P->S at 24: Lowered solubility, but more soluble than T-23</li><li>P->TP at 24: Wild-type solubility</li><li>P->V at 24: Slightly lowered solubility</li></ul>									1
P07355	302	<ul><li>Y->A at 24: Abolishes heat stress-induced cell surface localization</li></ul>	localization	GO:0051179			cell surface	GO:0009928,GO:0009986			1
P07359	2811	<ul><li>G->A at 249: No change</li><li>G->K,D at 249: Decreased binding to vWF</li><li>G->S,V at 249: Increased binding to vWF</li></ul>			binding	GO:0005488			<li>P80012</li><li>Q28833</li><li>P04275</li><li>Q8CIZ8</li><li>Q28295</li>		1
P07477	5644	<ul><li>Y->F at 154: Lack of sulfation</li></ul>									1
P07550	154	<ul><li>D->N at 79: Affects binding of catecholamines, and produces an uncoupling between the receptor and stimulatory G proteins</li><li>C->G at 341: Uncoupled receptor</li><li>SS->AA at 345-346: Delayed agonist-promoted desensitization</li></ul>			binding	GO:0005488					1
P07602	5660	<ul><li>I->C at 240: Strongly decreases stimulation of cerebroside sulfate hydrolysis</li></ul>									1
P07910	3183	<ul><li>K->R at 197: No effect on sumoylation</li><li>K->R at 250: Loss of sumoylation</li></ul>	sumoylation	GO:0016925							1
P07998	6035	<ul><li>NG->RS at 116-117: No effect on inhibition by RNase inhibitor 1</li></ul>							P13489		1
P08069	3480	<ul><li>Y->F at 980: Reduces tyrosine phosphorylation. Abolishes interaction with IRS1 and SHC1. Does not abolish interaction with PIK3R1</li><li>K->A at 1033: Kinase inactive. Abolishes tyrosine phosphorylation and abolishes interaction with IRS1, SHC1 and PIK3R1</li></ul>	phosphorylation	GO:0016310					<li>P27986</li><li>P23727</li><li>Q28224</li><li>P35568</li><li>P29353</li><li>P09715</li>		1
P08195	6520	<ul><li>C->S at 109: Abolishes dimerization, leucine uptake and interaction with beta-1 integrins</li><li>C->S at 330: No effect on dimerization, leucine uptake or interaction with beta-1 integrins</li></ul>									1
P08235	4306	<ul><li>S->N at 767: Loss of transcription transactivation</li><li>S->Q at 767: Strong decrease of transcription transactivation</li><li>N->A,D,H,Q,S,T at 770: Abolishes aldosterone binding and transcription transactivation</li><li>Q->A at 776: Reduces aldosterone binding and transcription transactivation</li><li>K->E at 782: Decreased coactivator binding</li><li>K->E at 785: Loss of coactivator binding</li><li>E->R at 796: Decreased coactivator binding</li><li>C->S at 808: Increases aldosterone-binding</li><li>S->M at 810: Alters receptor specificity</li><li>R->A at 817: Reduces aldosterone binding and transcription transactivation</li><li>C->S at 849: Strongly decreases affinity for aldosterone and transcription transactivation</li><li>C->S at 942: Abolishes steroid binding and transcription transactivation</li><li>T->A at 945: Decreases aldosterone-binding and cortisol-binding</li><li>L->A at 952: Reduces transcription transactivation</li><li>K->A at 953: Slightly reduces aldosterone binding and abolishes transcription transactivation</li><li>V->A at 954: Reduces aldosterone binding and abolishes transcription transactivation</li><li>F->A at 956: Abolishes aldosterone binding and transcription transactivation</li><li>P->A at 957: Slightly reduces aldosterone binding and transcription transactivation</li></ul>	transcription	GO:0006350	<li>binding</li><li>steroid binding</li>	<li>GO:0005488</li><li>GO:0005496</li>					1
P08243	440	<ul><li>C->A at 2: Loss of the glutamine-dependent asparagine synthetase activity, while the ammonia-dependent activity remained unaffected</li></ul>							<li>Q5R6W9</li><li>P49094</li><li>Q61024</li><li>P49091</li><li>P49088</li><li>P49078</li><li>O24338</li><li>Q5ZJU3</li><li>P78753</li><li>P08243</li><li>O24661</li><li>Q5UQE1</li><li>P19891</li><li>P19251</li><li>Q43011</li><li>P17714</li><li>P19252</li>		1
P08514	3674	<ul><li>PP->AA at 1029-1030: Imparts constitutive activity (ligand-binding) to alpha-IIb/beta-3</li></ul>			binding	GO:0005488					1
P08575	5788	<ul><li>C->S at 851: Loss of activity. Abolishes interaction with SKAP1</li></ul>									1
P08588	153	<ul><li>E->A,D at 474: Loss of interaction with GOPC</li><li>E->K at 474: Loss of interaction with GOPC; when associated with A-477</li><li>S->A at 475: Loss of interaction with GOPC</li><li>S->T at 475: Partial loss of interaction with GOPC</li><li>K->A at 476: Partial loss of interaction with GOPC</li><li>V->A,F,L,I,M at 477: Loss of interaction with GOPC</li></ul>							<li>Q9HD26</li><li>Q5RD32</li>		1
P08686	1589	<ul><li>S->C,M,T at 268: No loss of function</li><li>V->I at 281: Normal KM but 50% reduced Vmax</li><li>V->T at 281: Normal KM but 10% reduced Vmax</li><li>C->M,S,T at 428: Loss of activity and loss of P450 absorption</li></ul>									1
P08727	3880	<ul><li>S->A at 10: No effect on phosphorylation; no functional effect</li><li>S->A at 35: Abolishes phosphorylation; induces perinuclear collapse or short cytoplasmic filaments</li></ul>	phosphorylation	GO:0016310							1
P08887	3570	<ul><li>C->S at 121: Complete loss of ligand-binding</li><li>F->A at 122: No change of ligand-binding and IL6 signaling</li><li>C->A at 132: Complete loss of ligand-binding</li><li>W->L at 134: Complete loss of ligand-binding</li><li>P->G at 140: No change of ligand-binding and IL6 signaling</li><li>F->L at 153: No change of ligand-binding and IL6 signaling</li><li>C->L at 165: Complete loss of ligand-binding</li><li>F->L at 174: No change of ligand-binding and IL6 signaling</li><li>C->A at 176: Complete loss of ligand-binding</li><li>D->T at 184: 30% decrease of ligand-binding and IL6 signaling</li><li>V->G at 190: 80% decrease of ligand-binding and no IL6 signaling</li><li>C->D at 193: Complete loss of ligand-binding</li><li>C->A at 211: No change of ligand-binding and IL6 signaling</li><li>D->V at 217: Complete loss of ligand-binding</li><li>R->S at 232: 30% decrease of ligand-binding and IL6 signaling</li><li>W->Q at 233: 30% decrease of ligand-binding and increase of IL6 signaling</li><li>E->A at 254: 50% decrease of ligand-binding and IL6 signaling</li><li>C->D at 277: 30% increase of ligand-binding and 100% increase in IL6 signaling</li><li>V->N at 278: 50% Decrease of ligand-binding and 50% increase in IL6 signaling</li><li>I->D at 279: Complete loss of ligand-binding</li><li>H->I at 280: No change of ligand-binding and no IL6 signaling</li><li>D->G at 281: 70% decrease of ligand-binding and no IL6 signaling</li><li>G->D at 285: 80% decrease of ligand-binding and no IL6 signaling</li><li>Q->K at 291: Complete loss of ligand-binding</li><li>R->G at 293: Complete loss of ligand-binding</li></ul>			binding	GO:0005488			<li>P46650</li><li>O35736</li><li>P26892</li><li>Q6V919</li><li>P26893</li><li>P29455</li><li>Q25BC2</li><li>Q9XT80</li><li>Q28319</li><li>Q2MH06</li><li>Q865X6</li><li>Q865W7</li><li>Q28747</li><li>P41683</li><li>P05231</li><li>P51494</li><li>Q9MZR1</li><li>P41693</li><li>P41323</li><li>Q28819</li><li>P79341</li><li>Q95181</li><li>Q5I6E3</li><li>Q8MKH0</li>		1
P08913	150	<ul><li>D->N at 79: No change in binding affinity. eliminates guanine nucleotide-sensitive agonist binding</li><li>D->N at 113: No binding to yohimbine. Increase in adenylate cyclase activity</li><li>D->N at 130: Lower affinity for agonists. Eliminates guanine nucleotide-sensitive agonist binding</li><li>S->A at 200: Lower affinity for agonists. No change in guanine nucleotide-sensitive agonist binding</li><li>S->A at 204: Lower affinity for agonists. Reduced guanine nucleotide-sensitive agonist binding</li><li>F->N at 412: 350-fold reduced affinity for alpha-2 antagonist yohimbine, 3000-fold increase for beta-antagonist alprenolol</li></ul>			binding	GO:0005488			<li>P30528</li><li>P23466</li><li>P00936</li><li>Q59685</li><li>Q9WXC3</li><li>P0A1A7</li><li>P0A1A8</li><li>Q05766</li><li>P40134</li><li>P40135</li><li>P40130</li><li>P14605</li><li>Q59119</li><li>P43524</li><li>P27580</li><li>P08678</li><li>P40127</li><li>Q8XAP1</li><li>Q8FBP0</li><li>P0A4Y1</li><li>P0A4Y0</li><li>Q01513</li><li>P59739</li><li>P49606</li><li>Q01631</li>		1
P09012	6626	<ul><li>T->V at 11: Abolishes RNA binding</li><li>Y->F at 13: Substantially reduces RNA binding</li><li>N->V at 15: Abolishes RNA binding</li><li>N->V at 16: Substantially reduces RNA binding</li><li>R->Q at 52: Abolishes RNA binding</li></ul>			RNA binding	GO:0003723					1
P09086	5452	<ul><li>VIR->FNP at 340-342: Suppresses DNA-binding ability</li></ul>			DNA-binding	GO:0003677					1
P09467	2203	<ul><li>D->A at 119: Reduced activity</li><li>D->A at 122: Reduced activity</li></ul>									1
P09486	6678	<ul><li>R->A,L,K at 166: Strongly reduced collagen binding</li><li>N->A,Q at 173: Strongly reduced collagen binding</li><li>L->A at 259: Loss of collagen binding</li><li>M->A at 262: Strongly reduced collagen binding</li><li>E->A at 263: Loss of collagen binding</li></ul>			collagen binding	GO:0005518					1
P09488	2944	<ul><li>H->S at 108: Changes the properties of the enzyme toward some substrates</li></ul>									1
P09603	1435	<ul><li>Missing at 489-554: Produces biologically active protein which is secreted</li></ul>									1
P09651	3178	<ul><li>G->A at 326: No nuclear import nor export</li><li>P->A at 327: No nuclear import nor export</li><li>GG->LL at 334-335: Normal nuclear import and export</li></ul>	nuclear import	GO:0051170							1
P09693	917	<ul><li>L->A at 153: Abolishes lysosomal targeting</li><li>L->I at 153: Diminished but persistent lysosomal targeting</li><li>L->A at 154: Diminished but persistent lysosomal targeting</li><li>L->I at 154: No effect</li><li>Y->A at 160: Abolishes lysosomal targeting</li><li>L->A at 163: Abolishes lysosomal targeting</li></ul>									1
P09874	142	<ul><li>L->P at 797: 1.5% of wild-type activity</li><li>N->S at 868: 4% of wild-type activity</li><li>M->V at 890: <0.5% of wild-type activity</li><li>K->I at 893: Abolishes enzymatic activity</li><li>F->S at 897: 10% of wild-type activity</li><li>D->N at 899: 0.6% of wild-type activity</li><li>C->R at 908: <0.5% of wild-type activity</li><li>L->F at 926: 1.5% of wild-type activity</li><li>Y->H at 986: 14% of wild-type activity and increased branching 15-fold</li><li>E->K at 988: 1.25% of wild-type activity; only monomers are added</li><li>L->P at 1003: 1.5% of wild-type activity</li></ul>									1
P09917	240	<ul><li>D->N at 359: No loss of activity</li><li>H->S,N at 363: Still some substantial activity</li><li>H->S,N,A at 368: No activity</li><li>H->S,N at 373: No activity</li><li>E->Q at 377: No activity</li><li>H->A at 391: No activity</li><li>H->S,N at 391: Still some substantial activity</li><li>H->A at 400: No activity</li><li>H->S,N at 400: Still some substantial activity</li><li>H->N,A at 433: Almost no loss of activity</li><li>S->A at 524: Prevents phosphorylation by PKA</li><li>H->N,A at 551: No activity</li></ul>	phosphorylation	GO:0016310	PKA	GO:0004691					1
P09936	7345	<ul><li>Q->R at 73: No effect on enzymatic parameters</li><li>C->S at 90: Abolishes enzymatic activity</li><li>H->Q,N at 97: 2-fold increase in affinity for ubiquitin ethyl ester, slight reduction in enzymatic activity</li><li>H->D at 161: 10000-fold decrease in enzymatic activity; no change in affinity for ubiquitin ethyl ester</li><li>H->K,Q,N,Y at 161: Abolishes enzymatic activity</li><li>D->N at 176: 6-fold decrease in affinity for ubiquitin ethyl ester; 97.5% decrease in enzymatic activity</li></ul>							<li>P69326</li><li>P08565</li><li>P69322</li><li>P69323</li><li>P69324</li><li>P69325</li><li>P68196</li><li>O46543</li><li>P68197</li><li>Q05550</li><li>P68198</li><li>P68199</li><li>P19848</li><li>P42739</li><li>P68195</li><li>Q867C2</li><li>P62991</li><li>P62990</li><li>P61863</li><li>P61864</li><li>P61862</li><li>Q867C4</li><li>Q867C3</li><li>P23398</li><li>P68204</li><li>P84589</li><li>Q865C5</li><li>P42740</li><li>P68201</li><li>Q8MKD1</li><li>P14792</li><li>P63049</li><li>P0C072</li><li>P63051</li><li>P69308</li><li>P69309</li><li>P20685</li><li>P15174</li><li>P62976</li><li>P62977</li><li>P62974</li><li>P62975</li><li>P62972</li><li>P13117</li><li>P14624</li><li>P62973</li><li>P46574</li><li>P69310</li><li>P69313</li><li>P69314</li><li>P69311</li><li>P08618</li><li>P69312</li><li>P69317</li><li>P69318</li><li>P69315</li><li>P0C014</li><li>P69316</li><li>P59263</li><li>P69319</li><li>P49634</li><li>P49635</li><li>Q9Y848</li><li>P22589</li><li>P62988</li><li>P62989</li><li>P69321</li><li>P23324</li><li>P69320</li><li>P59669</li>		1
P09960	4048	<ul><li>Q->A at 137: No loss of activity</li><li>Q->L at 137: Aminopeptidase activity strongly impaired, but keeps LTA4 activity</li><li>Q->N at 137: Aminopeptidase activity almost absent, but keeps LTA4 activity</li><li>G->A at 269: No loss of activity</li><li>G->A at 270: No loss of activity</li><li>M->L at 271: No loss of activity</li><li>E->A,D at 272: Complete loss of activity</li><li>E->Q at 272: Loss of LTA4 activity, and aminopeptidase activity strongly impaired</li><li>N->A at 273: No loss of activity</li><li>H->Y at 296: Complete loss of activity</li><li>E->A at 297: Loss of both activities</li><li>E->K at 297: Loss of both activities</li><li>E->Q at 297: Loss of aminopeptidase activity, but keeps LTA4 activity</li><li>H->L at 300: Complete loss of activity</li><li>E->A at 319: Complete loss of activity</li></ul>							<li>P09960</li><li>P80561</li><li>P80474</li>		1
P0C0S8	8329	<ul><li>S->A at 2: Blocks the inhibition of transcription by RPS6KA5/MSK1</li></ul>	transcription	GO:0006350					<li>P32048</li><li>Q5R4K3</li><li>Q5F3L1</li><li>O75582</li>		1
P0C869	8681	<ul><li>S->A at 335: Abolishes enzyme activity</li><li>H->A at 417: No effect</li><li>D->A at 615: Abolishes enzyme activity</li><li>R->A at 632: Abolishes enzyme activity</li></ul>									1
P10114	5911	<ul><li>G->V at 12: 2-fold decrease in GDP dissociation rate constant and GTPase activity</li><li>S->N at 17: Severely impairs GTP-binding</li><li>T->A at 35: Decreases affinity for GTP and 3-fold reduction of GTPase activity</li><li>T->I at 145: Imperfect binding of guanyl nucleotides</li></ul>			<li>binding</li><li>GTPase activity</li><li>GTP-binding</li>	<li>GO:0005488</li><li>GO:0003924</li><li>GO:0005525</li>					1
P10147	6348	<ul><li>R->A at 40: Slightly reduces heparin binding</li><li>D->A at 49: Reduces self-association; in BB-10010</li><li>R->A at 68: Strongly reduces heparin binding</li><li>R->A at 70: Reduces heparin binding</li><li>E->A at 89: Reduces self-association</li></ul>			heparin binding	GO:0008201					1
P10253	2548	<ul><li>W->R at 516: Loss of activity</li><li>D->G,N,E at 518: Loss of activity</li></ul>									1
P10265		<ul><li>D->M at 26: Loss of activity</li></ul>									1
P10275	367	<ul><li>Y->F at 223: Decrease of CSK-induced phosphorylation</li><li>Y->F at 267: Decrease of CSK-induced phosphorylation</li><li>Y->F at 307: Decrease of CSK-induced phosphorylation</li><li>Y->F at 346: Decrease of CSK-induced phosphorylation</li><li>Y->F at 357: Decrease of CSK-induced phosphorylation</li><li>Y->F at 362: Decrease of CSK-induced phosphorylation</li><li>Y->F at 363: Decrease of CSK-induced phosphorylation</li><li>Y->F at 393: Decrease of CSK-induced phosphorylation</li><li>Y->F at 534: Greatest decrease of CSK-induced phosphorylation and inhibition of transcriptional activity induced by EGF</li><li>Y->F at 551: Decrease in CSK-induced phosphorylation</li><li>L->A at 701: Alters receptor specificity, so that transcription is activated by the antiandrogen cyproterone acetate</li><li>K->A at 720: Loss of transcription activation in the presence of androgen and of interaction with NCOA2</li><li>W->L at 741: Strongly decreased transcription activation in the presence of androgen</li><li>E->A,Q at 897: Reduced transcription activation in the presence of androgen</li><li>E->K,R at 897: Loss of transcription activation in the presence of androgen</li><li>Y->F at 915: Decrease in CSK-induced phosphorylation</li></ul>	<li>phosphorylation</li><li>transcription</li>	<li>GO:0016310</li><li>GO:0006350</li>					<li>Q9BEA0</li><li>P26224</li><li>P41239</li><li>P01132</li><li>Q0VBZ0</li><li>Q15596</li><li>P41240</li><li>P01133</li><li>Q95ND4</li><li>Q00968</li><li>P07522</li>		1
P10415	596	<ul><li>D->A at 34: Abolishes cleavage by caspase-3</li><li>D->A at 64: No effect on cleavage by caspase-3</li><li>G->A at 145: No heterodimerization with BAX and loss of anti-apoptotic activity</li><li>W->A at 188: No heterodimerization with BAX and loss of anti-apoptotic activity</li></ul>							<li>Q07815</li><li>Q07812</li><li>Q07814</li><li>O02703</li><li>P55269</li>		1
P10586	5792	<ul><li>C->S at 1548: Loss of activity</li></ul>									1
P10619	5476	<ul><li>S->A at 178: Inactivates the enzyme</li><li>H->Q at 457: Inactivates the enzyme</li></ul>									1
P10636	4137	<ul><li>S->E at 515: No association with plasma membrane</li><li>S->E at 516: No association with plasma membrane</li><li>S->E at 519: No association with plasma membrane</li><li>S->A at 531: No decrease in microtubule-binding and nucleation activity after in vitro phosphorylation of mutant protein</li><li>T->A at 548: 50% Decrease in microtubule-binding after in vitro phosphorylation of mutant protein</li><li>T->E at 548: No association with plasma membrane</li><li>S->A at 552: 70% decrease in microtubule-binding after in vitro phosphorylation of mutant protein</li><li>S->E at 552: No association with plasma membrane</li><li>S->A at 579: 8% decrease in microtubule-binding after in vitro phosphorylation of mutant protein</li><li>S->E at 713: No association with plasma membrane</li><li>S->E at 721: No association with plasma membrane</li><li>S->E at 726: No association with plasma membrane</li><li>S->E at 730: No association with plasma membrane</li><li>S->E at 739: No association with plasma membrane</li></ul>	phosphorylation	GO:0016310	microtubule-binding	GO:0008017	plasma membrane	GO:0005886			1
P10646	7035	<ul><li>K->I at 64: Abolishes inhibition of VII(a)/TF</li><li>R->L at 135: Abolishes inhibition of X(a)</li><li>R->L at 227: Abolishes inhibition of VII(a)/TF</li></ul>									1
P10721	3815	<ul><li>I->A at 571: Reduction in APS binding. Abolishes APS binding; when associated with A-939</li><li>K->M at 623: Stronger interaction with MPDZ</li><li>L->A at 939: Reduction in APS binding. Abolishes APS binding; when associated with A-571</li></ul>			binding	GO:0005488			<li>P33619</li><li>Q6DT45</li><li>P22325</li><li>P04802</li><li>O14492</li><li>P07288</li><li>P55228</li><li>O75970</li><li>Q12650</li>		1
P10911	4168	<ul><li>LLLKELL->IIIRDI at 640-646: Transformation capability reduced; no stimulation of GDP dissociation</li></ul>									1
P10912	2690	<ul><li>E->A at 260: No change in shedding activity</li><li>E->A at 261: No change in shedding activity</li><li>D->A at 262: No change in shedding activity</li></ul>									1
P11086	5409	<ul><li>Y->F at 35: Strongly increases KM for substrate and S-adenosyl-L-methionine</li><li>E->A,Q at 185: Strongly reduced enzyme activity. Increases affinity for S-adenosyl-L-methionine</li><li>E->D at 185: Strongly reduced enzyme activity. Decreases affinity for substrate and S-adenosyl-L-methionine 3-fold</li><li>E->A at 219: Reduced enzyme activity. Decreases affinity for substrate 6-fold. Decreases affinity for S-adenosyl-L-methionine 2-fold</li><li>D->A,N at 267: Strongly reduced enzyme activity. Decreases affinity for substrate 200-fold. Decreases affinity for S-adenosyl-L-methionine 3-fold</li></ul>									1
P11161	1959	<ul><li>DHLY->AAAA at 162-165: Inhibits association with HCFC1</li></ul>							<li>P51611</li><li>P51610</li>		1
P11171	2035	<ul><li>T->A at 60: Loss of CDC2-mediated phosphorylation. Abolishes targeting onto the mitotic spindle; when associated with A-712</li><li>S->A at 712: Loss of CDC2-mediated phosphorylation. Abolishes targeting onto the mitotic spindle; when associated with A-60</li></ul>	phosphorylation	GO:0016310			spindle	GO:0005819	<li>Q9W739</li><li>Q9DGA2</li><li>Q9DGA5</li><li>P19026</li><li>Q5RCH1</li><li>Q9DG98</li><li>P06493</li><li>P48734</li><li>P43290</li><li>P23111</li><li>P13863</li><li>Q04770</li><li>P52389</li><li>P15436</li><li>P24100</li><li>P51958</li><li>Q41639</li><li>P54119</li><li>P93101</li><li>Q9DGD3</li>		1
P11172	7372	<ul><li>D->N at 312: Loss of OMPdecase activity</li></ul>							<li>P77888</li><li>Q2YXG4</li><li>Q482F9</li><li>Q5J2D0</li><li>Q4UNV9</li><li>P14017</li><li>O58462</li><li>P41769</li><li>O94127</li><li>Q3AZD9</li><li>Q8YE79</li><li>P13649</li><li>Q5WFJ5</li><li>P78748</li><li>Q66AI1</li><li>Q9UZ35</li><li>P09556</li><li>P07922</li><li>Q4VWW3</li><li>Q9C150</li><li>Q8K7V3</li><li>Q834E3</li><li>Q6GHN1</li><li>Q9ZHA7</li><li>Q96WP7</li><li>Q42942</li><li>Q2J838</li><li>Q9EYV3</li><li>Q9HFN9</li><li>Q06375</li><li>Q9LCT0</li><li>Q5PB36</li><li>Q71HN5</li><li>Q6LZM2</li><li>P57358</li><li>Q6F9Z3</li><li>Q9RSC5</li><li>Q12595</li><li>P46535</li><li>Q57700</li><li>Q2RNS7</li><li>Q5QZ42</li><li>P50924</li><li>Q5F9J2</li><li>Q6A911</li><li>P31754</li><li>Q8XL62</li><li>Q2SCG0</li><li>Q6D5T3</li><li>Q8PV88</li><li>Q9C131</li><li>Q5L0U0</li><li>Q7VLR5</li><li>Q3YSH4</li><li>Q97FS5</li><li>P07817</li><li>P24220</li><li>Q9KXR8</li><li>Q2NHA5</li><li>Q2LQ82</li><li>Q9ABW5</li><li>Q2J316</li><li>Q57NV3</li><li>Q9C1J2</li><li>Q8J269</li><li>Q9KQT7</li><li>O93864</li><li>Q8P1C0</li><li>Q9UX10</li><li>Q5E3Z6</li><li>Q74J28</li><li>O08323</li><li>Q2FHN4</li><li>Q2JTW6</li><li>Q636E3</li><li>Q8NQ40</li><li>Q97CS3</li><li>P10652</li><li>Q3Z131</li><li>Q2W019</li><li>Q8D8J6</li><li>Q87N49</li><li>Q38X21</li><li>Q46GE2</li><li>Q72DM8</li><li>Q71YI4</li><li>Q884R0</li><li>Q9P8X9</li><li>Q46JD8</li><li>P56155</li><li>Q9A077</li><li>Q732I6</li><li>Q9WYG7</li><li>Q9CMM1</li><li>Q5FJB3</li><li>Q2GG43</li><li>O29333</li><li>Q6IUR4</li><li>Q977X5</li><li>P33283</li><li>Q3IY00</li><li>Q8U1U1</li><li>Q8ER36</li><li>O26232</li><li>Q2JPF1</li><li>P79075</li><li>Q5GRJ9</li><li>Q3MEN8</li><li>Q819S6</li><li>Q2P8Z6</li><li>Q8K9Q1</li><li>Q2KDF0</li><li>Q3BMA4</li><li>P65596</li><li>P65595</li><li>Q6HET1</li><li>Q9ZN53</li><li>Q9HF68</li><li>Q6GA09</li><li>Q9Y9D9</li><li>Q5R514</li><li>Q3J8N5</li><li>Q7MAE8</li><li>Q31ZX5</li><li>P43230</li><li>Q9Y720</li><li>P25971</li><li>Q92AH6</li><li>Q9Y726</li><li>Q83E06</li><li>Q01378</li><li>P05035</li><li>Q8FXW9</li><li>Q7V0D8</li><li>Q31GC7</li><li>Q3AHU2</li><li>Q8DZQ2</li><li>Q48U10</li><li>P07691</li><li>Q9CFW9</li><li>Q5XCK8</li><li>Q7U8P3</li><li>Q7N4C1</li><li>Q65SI1</li><li>Q9HFX0</li><li>Q5JDB0</li><li>Q5M4I0</li><li>Q9CCR1</li><li>Q12724</li><li>Q1E9A1</li><li>Q7V5Y2</li><li>P48844</li><li>Q42586</li><li>Q757S1</li><li>Q609Y2</li><li>Q21IS8</li><li>Q31K20</li><li>Q3SRG9</li><li>Q39VY5</li><li>Q2NT36</li><li>P78724</li><li>Q5HGM8</li><li>Q4QJV1</li><li>Q5ZVL5</li><li>P96076</li><li>Q01637</li><li>Q4FRL9</li><li>Q4ZVD9</li><li>Q6NCY0</li><li>O42771</li><li>Q5HW86</li><li>Q9JV18</li><li>Q49WY5</li><li>Q2YQU9</li><li>Q8P3D7</li><li>Q8YSY4</li><li>P08244</li><li>Q5N1T9</li><li>Q57AD4</li><li>P58883</li><li>Q8PER4</li><li>Q25566</li><li>Q65JU4</li><li>Q47R19</li><li>Q89AL6</li><li>Q9P9M3</li><li>Q12709</li><li>Q4L5Q6</li><li>Q9HFV8</li><li>Q7Z8L4</li><li>Q3K8H1</li><li>Q9K9W2</li><li>P15188</li><li>Q3SK77</li><li>Q88LW2</li><li>Q8FHU2</li><li>O13416</li><li>Q4KFV3</li><li>Q74D58</li><li>Q8DTV1</li><li>Q1QA56</li><li>Q6BY69</li><li>Q7MLX2</li><li>P09463</li><li>Q32GQ2</li><li>P11172</li><li>O13410</li><li>Q8FT43</li><li>Q82TD8</li><li>P0A5M6</li><li>Q8EUY3</li><li>P0A5M7</li><li>Q81WF5</li><li>Q87FA3</li><li>P03962</li><li>Q5WWS3</li><li>Q2RK39</li><li>P43812</li><li>Q8E5F0</li><li>Q9PHB0</li><li>O67520</li><li>Q2IGK0</li><li>Q5LZW9</li><li>Q319F9</li><li>Q5FNS8</li><li>Q5X5E0</li><li>Q83RM1</li><li>Q8D2J1</li><li>Q8EXA4</li><li>P32431</li><li>P32430</li><li>Q7VAP8</li><li>Q8DLT3</li><li>Q28K56</li><li>Q7UIA4</li><li>Q3IGA7</li><li>Q8CPJ3</li><li>Q21CH8</li><li>Q3K145</li><li>Q3A6R4</li><li>Q2Y7B1</li><li>P58643</li><li>P58644</li><li>P58641</li><li>P58642</li><li>Q2G8S2</li><li>Q8RG83</li><li>Q44843</li><li>P13439</li><li>Q9K005</li><li>P49434</li><li>Q8DQL6</li><li>Q59654</li><li>Q30XT2</li><li>Q48KP5</li><li>Q8J0E6</li><li>Q3AC06</li><li>Q9UVZ5</li><li>Q98DD5</li><li>Q7NTL2</li><li>P58638</li><li>P58639</li><li>Q5PD06</li><li>P21593</li><li>P21594</li><li>Q8TS37</li><li>Q92SN8</li><li>Q7NK22</li><li>Q8EEI4</li><li>O74110</li><li>Q970X0</li><li>Q5HPY7</li><li>Q30QK7</li><li>Q12604</li><li>P73761</li><li>Q6LPE7</li><li>P14964</li><li>P14965</li><li>Q5H6B9</li><li>Q9PIC1</li><li>Q5LND3</li><li>P58640</li><li>P99145</li>		1
P11233	5898	<ul><li>K->E at 47: Strongly reduces interaction with EXOC8</li><li>K->I at 47: No effect on interaction with EXOC8</li><li>A->W at 48: Strongly reduces interaction with EXOC8</li><li>S->W at 50: Strongly reduces interaction with EXOC8</li><li>R->A at 52: Strongly reduces interaction with EXOC8</li><li>R->W at 52: No effect on interaction with EXOC8</li><li>N->A at 81: No effect on interaction with EXOC8</li><li>N->R at 81: Strongly reduces interaction with EXOC8</li></ul>							<li>Q8IYI6</li><li>Q5ZJ43</li>		1
P11274	613	<ul><li>Missing at 1269-1271: Abolishes interaction with PDZK1</li><li>V->A at 1271: Reduces interaction with PDZK1</li></ul>							<li>Q5T2W1</li><li>Q3T0X8</li><li>Q865P3</li><li>Q5RCF7</li>		1
P11310	34	<ul><li>L->M at 86: Strongly reduced rate of electron transfer to ETF</li><li>L->W at 98: Strongly reduced rate of electron transfer to ETF</li><li>L->Y at 100: Strongly reduced rate of electron transfer to ETF</li><li>I->M at 108: Strongly reduced rate of electron transfer to ETF</li><li>W->A at 191: Loss of electron transfer to ETF</li><li>W->F at 191: Reduces rate of electron transfer to ETF about six-fold</li><li>E->A at 237: Strongly reduced rate of electron transfer to ETF</li><li>E->A at 384: Reduces rate of electron transfer to ETF three-fold</li><li>E->Q at 384: Reduces rate of electron transfer to ETF two-fold</li></ul>	electron transfer	GO:0006118					P48301		1
P11362	2260	<ul><li>Y->F at 766: Fails to interact with PLC-gamma and SHB</li></ul>							Q15464		1
P11387	7150	<ul><li>K->R at 103: Localizes in both nucleoplasm and nucleoli; when associated with R-117 or R-153. Almost complete loss of sumoylation, concentrates in nucleoli and no clearing from nucleoli on CPT treatment; when associated with R-117 and R-153</li><li>K->R at 117: 5-fold decrease in sumoylation. Localizes in both nucleoplasm and nucleoli; when associated with or without R-103 or R-153. Almost complete loss of sumoylation, concentrates in nucleoli and no clearing from nucleoli on CPT treatment; when associated with R-103 and R-153</li><li>K->R at 153: Localizes in both nucleoplasm and nucleoli; when associated with R-103 or R-117. Almost complete loss of sumoylation, concentrates in nucleoli and no clearing from nucleoli on CPT treatment; when associated with R-103 and R-117</li><li>Y->F at 723: No change in CPT-induced clearing from nuclei</li></ul>	sumoylation	GO:0016925			nucleoplasm	GO:0005654	<li>Q56148</li><li>P56872</li>		1
P11388	7153	<ul><li>S->A at 1469: Abolishes binding to the antibody MPM2</li></ul>			binding	GO:0005488					1
P11473	7421	<ul><li>PF->AA at 61-62: Promotes heterodimerization with RXRA; when associated with A-75</li><li>H->A at 75: Promotes heterodimerization with RXRA; when associated with A-61 and A-62</li></ul>							P19793		1
P11474	2101	<ul><li>K->R at 14: Some loss of sumoylation. Complete loss of sumoylation; when associated with R-403</li><li>S->A at 19: 50% loss of phosphorylation but represses transactivation activity in the absence of coactivator. Almost complete loss of phosphorylation and 2-fold loss of repression of transactivation activity in response to coactivator; when associated with A-22</li><li>S->D at 19: Represses transactivation activity in response to coactivator as for wild type; when associated with D-22</li><li>S->A at 22: 15% loss of phosphorylation but little transactivating activity. Almost complete loss of phosphorylation and 2-fold loss of repression of transactivation activity in the presence of coactivator; when associated with A-19</li><li>S->D at 22: Represses transactivation activity in response to coactivator as for wild type; when associated with D-19</li><li>S->A at 118: Binds DNA as a monomer or as a dimer as for wild type. No effect on interaction with PPARGC1A</li><li>T->A at 124: Binds DNA predominantly as a monomer. Loss of interaction with PPARGC1A</li><li>MSVLQ->VSVLE at 258-262: Almost complete loss of interaction to L2 or to L3 of PPARGC1A</li><li>S->H at 259: Little effect on binding L2 of PPARGC1A. Greatly reduced binding to L3 of PPARGC1A</li><li>R->A at 315: Almost complete loss of interaction to L2 or to L3 of PPARGC1A</li><li>D->A at 338: Almost complete loss of interaction to L2 or to L3 of PPARGC1A</li><li>H->A at 341: Little effect on binding L3 of PPARGC1A</li><li>E->A at 343: No effect on binding L3 of PPARGC1A</li><li>K->R at 403: Decrease in sumoylation. No effect on transcriptional activity. Complete loss of sumoylation; when associated with R-14</li><li>L->A at 413: Loss of coactivation activity; when associated with A-418. Loss of increased response to coactivator; when associated with A-19 and A-418</li><li>L->A at 418: Loss of coactivation activity; when associated with A-413. Loss of increased response to coactivator activity; when associated with A-19 and A-413</li><li>Missing at 421-423: Greatly reduced interaction with L3 motif of PPARGC1A. Less effect on binding to L2 motif of PPARGC1A</li><li>D->A at 423: Little effect on binding L3 of PPARGC1A</li></ul>	<li>phosphorylation</li><li>sumoylation</li>	<li>GO:0016310</li><li>GO:0016925</li>	binding	GO:0005488			<li>Q9UBK2</li><li>Q865B7</li><li>Q865B6</li>		1
P11498	5091	<ul><li>F->A,E at 1077: Loss of tetramerization and enzyme activity, resulting in an inactive homodimer</li></ul>									1
P11586	4522	<ul><li>S->A at 49: No effect on dehydrogenase and cyclohydrolase activity. Strong increase of Km for NADP</li><li>S->Q at 49: Reduces dehydrogenase by 75% and cyclohydrolase activity by 99%. No effect on Km for NADP and for 5,10-methenyltetrahydrofolate</li><li>Y->A,S at 52: Reduces dehydrogenase activity by 99%. Reduces cyclohydrolase activity by 70%. No effect on Km for NADP and for 5,10-methenyltetrahydrofolate</li><li>Y->F at 52: Slightly reduces dehydrogenase and cyclohydrolase activity. Increase of Km for NADP and for 5,10-methenyltetrahydrofolate</li><li>K->A,I,S,T at 56: Decreases dehydrogenase activity over 90%. Loss of cyclohydrolase activity</li><li>K->E,M,Q at 56: Moderate decrease of dehydrogenase activity. Loss of cyclohydrolase activity. Strong increase of Km for NADP. Decrease of Km for 5,10-methenyltetrahydrofolate</li><li>K->R at 56: Reduces dehydrogenase and cyclohydrolase activity by 99%. No effect on Km for NADP and for 5,10-methenyltetrahydrofolate</li><li>C->Q at 147: Reduces dehydrogenase activity by 50% and cyclohydrolase activity by 87%</li></ul>			cyclohydrolase activity	GO:0019238					1
P11597	1071	<ul><li>T->Y at 155: Reduces triglyceride transfer and cholesteryl ester transfer 5-fold</li><li>V->W at 215: Reduces triglyceride transfer 10-fold. No effect on cholesteryl ester transfer</li><li>R->S at 218: Reduces triglyceride transfer 10-fold. Slight reduction of cholesteryl ester transfer</li><li>S->A at 247: Reduces triglyceride transfer 5-fold. Slight reduction of cholesteryl ester transfer</li><li>F->R at 282: Not secreted</li><li>F->R at 287: Not secreted</li><li>F->D at 309: Not secreted</li><li>L->Q at 313: Reduces cholesteryl ester transfer by 60%</li><li>Y->S at 392: Not secreted</li><li>L->W at 399: Not secreted</li><li>V->R at 433: Reduces activity by 60%</li></ul>									1
P11766	128	<ul><li>R->A,D at 115: Loss of FDH activity and loss of activation by fatty acids</li></ul>							<li>P79896</li><li>P11766</li><li>Q570B4</li><li>Q03134</li><li>P32771</li><li>O19053</li><li>P19854</li><li>P25437</li><li>P12711</li><li>P80467</li><li>Q9S7E4</li><li>P93629</li><li>P73138</li><li>P81600</li><li>P81601</li><li>Q07103</li><li>P33677</li><li>P72324</li><li>Q07511</li><li>P80360</li><li>Q96533</li><li>Q06099</li><li>P44557</li><li>O74685</li><li>P46415</li><li>P33160</li><li>O74540</li><li>P47734</li><li>P80572</li><li>P39450</li><li>Q17335</li><li>P46154</li><li>Q9ZRI8</li><li>P81431</li><li>P28474</li><li>P78870</li><li>P93436</li>		1
P11801	5681	<ul><li>D->A at 218: Loss of autophosphorylation</li></ul>	autophosphorylation	GO:0046777							1
P11912	973	<ul><li>S->A at 197: Increased phosphorylation of Y-188; when associated with A-203 and V-209</li><li>S->A at 203: Increased phosphorylation of Y-188; when associated with A-197 and V-209</li><li>T->V at 209: Increased phosphorylation of Y-188; when associated with A-197 and A-203</li></ul>	phosphorylation	GO:0016310							1
P11926	4953	<ul><li>C->A at 360: 25% decrease of in vitro nitrosylation level</li></ul>									1
P11940	26986	<ul><li>R->A at 455: Greatly reduces methylation by CARM1 (in vitro); when associated with A-460</li><li>R->A at 460: Greatly reduces methylation by CARM1 (in vitro); when associated with A-455</li></ul>							Q86X55		1
P12004	5111	<ul><li>K->R at 164: Abolishes ubiquitination. No effect on interaction with SHPRH</li></ul>									1
P12104	2169	<ul><li>L->G at 39: Reduced stability</li><li>E->G at 64: Localized reduction in stability</li><li>L->A at 65: Reduced stability</li><li>L->G at 65: Reduced stability</li><li>V->G at 67: Localized reduction in stability</li><li>L->G at 90: Reduced stability</li><li>V->G at 123: Reduced stability</li></ul>									1
P12277	1152	<ul><li>C->S,Y at 283: Complete loss of activity</li><li>R->H,L,Q at 292: Complete loss of activity</li><li>R->K at 292: 42% of wild-type activity</li><li>D->E at 340: No change in activity</li></ul>									1
P12314	2209	<ul><li>N->D at 306: Decreases cell membrane expression by 50% in absence of FCER1G</li><li>N->G at 306: Increases cell membrane expression in absence of FCER1G</li></ul>					cell membrane	GO:0005886	<li>Q8SPW1</li><li>P30273</li><li>Q07249</li><li>Q9XSZ6</li><li>Q9BDR7</li>		1
P12821	1636	<ul><li>S->A at 1299: Abolishes phosphorylation and decreases membrane retention</li></ul>	phosphorylation	GO:0016310			membrane	GO:0016020			1
P12830	999	<ul><li>GGG->AAA at 759-761: Binds to CTNNB1 but abolishes formation of the PSEN1/CTNNB1 complex; when associated with CTNNB1 D-431. Abolishes binding PSEN1. Abolishes gamma-secretase cleavage</li></ul>			binding	GO:0005488			<li>Q9XT97</li><li>P49768</li><li>Q5R780</li><li>Q6RH31</li><li>P79802</li><li>P35222</li><li>Q4JIM4</li><li>Q8HXW5</li>		1
P13010	7520	<ul><li>EE->AA at 720-721: Abolishes interaction with PRKDC and its recruitment to sites of DNA damage</li><li>DD->AA at 726-727: Abolishes interaction with PRKDC and its recruitment to sites of DNA damage</li></ul>							<li>Q8QGX4</li><li>Q8WN22</li><li>P78527</li>		1
P13051	7374	<ul><li>D->E,N at 154: Loss of activity</li><li>Y->A,C,S at 156: Thymine-DNA glycosylase activity</li><li>N->D at 213: Cytosine-DNA glycosylase activity</li></ul>			DNA glycosylase	GO:0019104			P29588		1
P13498	1535	<ul><li>P->Q at 157: Loss of interaction with NOXO1</li></ul>							Q8NFA2		1
P13500	6347	<ul><li>Missing at 24-91: 83% reduction in activity</li><li>Missing at 24-85: 90% reduction in activity</li><li>Missing at 24: Loss of activity</li><li>Missing at 25-31: Loss of signaling</li><li>D->A at 26: Reduction in activity</li><li>I->A at 28: Slight reduction in activity</li><li>N->A at 29: 50% reduction in activity</li><li>P->A at 31: Loss of dimerization; slight reduction of activity</li><li>V->A at 32: Slight reduction in activity</li><li>V->E at 32: Slight reduction in affinity</li><li>T->A at 33: Slight reduction in activity</li><li>T->E at 33: Slight reduction in affinity</li><li>Y->A at 36: Loss of activity</li><li>R->F at 47: 95% reduction in activity; strong reduction of receptor binding</li><li>S->Q at 50: 40% reduction in activity</li><li>Y->D at 51: Loss of activity</li><li>R->L at 53: Loss of activity</li><li>K->A at 79: No effect on heparin binding</li><li>K->A at 81: Strongly reduces heparin binding</li><li>H->A at 89: Strongly reduces heparin binding</li><li>D->L at 91: 90% reduction in activity</li><li>Missing at 95-99: No effect on heparin binding</li></ul>			<li>receptor binding</li><li>heparin binding</li>	<li>GO:0005102</li><li>GO:0008201</li>					1
P13612	3676	<ul><li>K->Q at 590: Abolishes almost completely cleavage</li><li>R->L at 591: Abolishes completely cleavage</li><li>S->A at 1021: Abolishes phosphorylation</li><li>S->D at 1021: Reduces PXN binding</li><li>Y->A at 1024: Disrupts PXN binding</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488			<li>P49024</li><li>Q5R7I1</li><li>P49023</li>		1
P13674	5033	<ul><li>Y->A at 210: Strongly reduced affinity for peptide substrate</li><li>Y->A at 213: Strongly reduced affinity for peptide substrate</li><li>Y->A at 247: Strongly reduced affinity for peptide substrate</li></ul>									1
P13725	5008	<ul><li>C->S at 74: Inactive</li><li>C->S at 192: Inactive</li><li>F->G at 201: Inactive</li><li>F->G at 209: Inactive</li></ul>									1
P13866	6523	<ul><li>N->Q at 248: Loss of N-glycosylation</li></ul>									1
P13987	966	<ul><li>Y->R at 29: No loss of function</li><li>N->R,Q at 33: No loss of function</li><li>D->R at 37: No loss of function</li><li>F->R at 48: Some loss of function. Some lysis</li><li>D->R at 49: Loss of function. Lysis</li><li>L->E at 58: No loss of function</li><li>K->E at 63: No loss of function</li><li>W->E at 65: Complete loss of function. Lysis</li><li>K->D at 66: No loss of function</li><li>K->Q at 66: Loss of glycation mediated inactivation</li><li>F->K at 67: No loss of function</li><li>H->Q at 69: Loss of glycation mediated inactivation</li><li>F->E at 72: Almost complete loss of function. Lysis</li><li>R->E at 78: Loss of function. Lysis</li><li>L->D at 79: No loss of function</li><li>E->R at 81: Almost complete loss of function. Lysis</li><li>N->K at 82: No loss of function</li><li>Y->R at 87: No loss of function</li></ul>									1
P14061	3292	<ul><li>L->V at 150: Alters substrate specificity</li></ul>									1
P14091	1510	<ul><li>C->A at 60: Abolishes homodimerization</li></ul>									1
P14210	3082	<ul><li>R->Q at 494: Loss of activity due to absence of proteolytic cleavage</li></ul>									1
P14384	1368	<ul><li>E->A at 277: 5-fold decrease in substrate affinity. 22-fold decrease in specific affinity. 104-fold decrease in catalytic efficiency. Greatly reduced heat stability</li><li>E->Q at 277: 2-fold decrease in substrate affinity. Small increase in specific affinity. Reduced heat stability by 50%</li><li>E->Q at 281: Abolishes enzyme activity</li><li>S->A,T at 423: Expressed on cell membrane. Released from membrane by PI-PLC</li><li>S->P at 423: Little expression on cell membrane. Perinuclear localization. Not released from membrane by PI-PLC</li></ul>	localization	GO:0051179			<li>membrane</li><li>cell membrane</li>	<li>GO:0016020</li><li>GO:0005886</li>	<li>P08954</li><li>P14262</li><li>P45723</li><li>P34024</li>		1
P14550	10327	<ul><li>Y->F at 50: Complete loss of enzymatic activity</li><li>Y->H at 50: Complete loss of enzymatic activity</li><li>K->M at 80: Complete loss of enzymatic activity</li><li>H->Q at 113: Strong decrease in enzymatic activity</li><li>I->A at 299: No change in enzymatic activity</li><li>I->C at 299: No change in enzymatic activity</li><li>V->C at 300: No change in enzymatic activity</li></ul>									1
P14672	6517	<ul><li>LL->AA at 489-490: Changes subcellular location mainly to the plasma membrane</li></ul>					plasma membrane	GO:0005886			1
P14784	3560	<ul><li>Y->F at 418: Partial loss of interaction with SHB; when associated with F-536</li><li>Y->F at 536: Partial loss of interaction with SHB; when associated with F-418</li></ul>							Q15464		1
P15121	231	<ul><li>D->N at 44: Reduced enzymatic activity</li><li>Y->F at 49: Complete loss of enzymatic activity</li><li>K->M at 78: Reduced enzymatic activity</li><li>H->N at 111: Reduced enzymatic activity</li></ul>									1
P15144	290	<ul><li>DYVEKQAS->QSVEE at 288-295: No change in receptor activity and HCoV-229E infection</li><li>DYVEKQAS->QSVNE at 288-295: No change in receptor activity and HCoV-229E infection</li><li>DYVEKQAS->QSVNE at 288-295: Complete loss of receptor activity and blocks HCoV-229E infection. No loss of enzymatic activity</li><li>EKQ->NKT at 291-293: Complete loss of receptor activity and blocks HCoV-229E infection. No loss of enzymatic activity</li><li>E->N at 291: No change of receptor activity and HCoV-229E infection</li><li>Q->T at 293: No change of receptor activity and HCoV-229E infection</li><li>N->E at 818: Very low receptor activity and HCoV-229E infection</li></ul>			receptor activity	GO:0004872					1
P15151	5817	<ul><li>KCSR->ACSA at 369-372: Partial loss of DYNLT1 binding</li></ul>			binding	GO:0005488			<li>P63171</li><li>P63172</li>		1
P15153	5880	<ul><li>C->W at 189: Abolishes in vitro prenylation</li></ul>									1
P15289	410	<ul><li>C->A at 69: Abolishes enzyme activity</li><li>C->S at 69: Strongly decreases enzyme activity</li></ul>									1
P15291	2683	<ul><li>Y->G at 282: Reduction In N-acetylglucosamine binding</li><li>Y->F at 285: No change in enzymatic activity</li><li>Y->G at 307: Reduction In N-acetylglucosamine and UDP-galactose binding</li><li>W->G at 308: Reduction In N-acetylglucosamine binding</li><li>W->G at 310: Reduction In N-acetylglucosamine binding</li></ul>			<li>galactose binding</li><li>binding</li>	<li>GO:0005534</li><li>GO:0005488</li>					1
P15313	525	<ul><li>L->G at 513: Loss of interactions with SLC9A3R1 and SCL4A7</li></ul>							<li>Q28619</li><li>O14745</li>		1
P15374	7347	<ul><li>C->S at 95: Abolishes enzymatic activity</li></ul>									1
P15382	3753	<ul><li>K->H at 69: Lowers current 2-fold and leads to faster deactivation of KCNQ1/KCNE1 channel</li></ul>							<li>Q9MYS6</li><li>P51787</li><li>Q5R8Q2</li><li>O97531</li><li>Q60409</li><li>Q28705</li><li>O73925</li><li>Q9XSP1</li><li>Q9TUH9</li><li>P15382</li><li>O70344</li><li>Q9TTJ7</li>		1
P15428	3248	<ul><li>Y->A at 151: Loss of activity</li></ul>									1
P15498	7409	<ul><li>C->R at 529: Abolishes transforming activity</li></ul>									1
P15516	3347	<ul><li>R->I at 31: No effect on candidacidal activity of histatin-3 1/24</li><li>K->T,E at 32: 3-fold reduction in candidacidal activity of histatin-3 1/24</li><li>K->N at 36: No effect on candidacidal activity of histatin-3 1/24</li><li>H->P at 38: No effect on candidacidal activity of histatin-3 1/24</li><li>H->L,R at 40: No effect on candidacidal activity of histatin-3 1/24</li><li>R->G at 41: 10-fold reduction in candidacidal activity of histatin-3 1/24; when associated with E-32: in dbSNP rsrs58376281</li></ul>							P15516	rs58376281	1
P15529	4179	<ul><li>N->Q at 83: No effect on cytoprotective function. No effect on Neisseria binding. No effect on Measles virus binding</li><li>N->Q at 114: Strongly decreases cytoprotective function. Decreases Neisseria binding. Abolishes Measles virus binding</li><li>N->Q at 273: Strongly decreases cytoprotective function. Abolishes Neisseria binding. No effect on Measles virus binding</li></ul>			binding	GO:0005488					1
P15531	4830	<ul><li>F->W at 60: No loss of activity or substrate binding</li><li>P->S at 96: Increased motility of carcinoma cells</li><li>H->F at 118: Loss of serine/threonine kinase activity. Some loss of motility of carcinoma cells</li><li>H->G at 118: Loss of activity</li><li>S->A at 120: Limited increase in motility of carcinoma cells</li></ul>			<li>kinase activity</li><li>binding</li>	<li>GO:0016301</li><li>GO:0005488</li>					1
P15813	912	<ul><li>Y->A at 331: Strongly reduced internalization</li><li>V->A at 334: Strongly reduced internalization</li></ul>									1
P15923	6929	<ul><li>RR->GG at 550-551: No DNA-binding</li><li>R->K at 551: No DNA-binding</li><li>RVR->GVG at 561-563: No DNA-binding</li><li>R->K at 561: No DNA-binding</li><li>R->K at 563: No DNA-binding</li><li>K->A at 588: No DNA-binding and no dimerization</li><li>IL->DE at 591-592: No DNA-binding and no dimerization</li><li>A->D at 595: No change in DNA-binding or dimerization</li></ul>			DNA-binding	GO:0003677					1
P15927	6118	<ul><li>S->A at 29: Reduces phosphorylation by CDC2</li></ul>	phosphorylation	GO:0016310					<li>Q9W739</li><li>Q9DGA2</li><li>Q9DGA5</li><li>P19026</li><li>Q5RCH1</li><li>Q9DG98</li><li>P06493</li><li>P48734</li><li>P43290</li><li>P23111</li><li>P13863</li><li>Q04770</li><li>P52389</li><li>P15436</li><li>P24100</li><li>P51958</li><li>Q41639</li><li>P54119</li><li>P93101</li><li>Q9DGD3</li>		1
P15941	4582	<ul><li>S->A,D,E,F,G,H, at 1098: Completely abrogates cleavage</li><li>S->C,T at 1098: Almost complete cleavage</li><li>D->A at 1116: Greatly reduced formation of isoform 5/isoform 7 complex</li><li>D->E at 1116: No effect on formation of isoform 5/isoform 7 complex</li><li>C->A at 1184: S-palmitoylation reduced by 50%. Complete loss of palymitoylation, no effect on endocytosis, recycling inhibited and AP1S1 binding reduced by 30%; when associated with C-1186. Accumulates in intracellular comparments; when associated with C-1186 and N-1203</li><li>C->A at 1186: S-palmitoylation reduced by 50%. Complete loss of palymitoylation, no effect on endocytosis, recycling inhibited, and AP1S1 binding reduced by 30%; when associated with C-1184. Accumulates in intracellular comparments; when associated with C-1184 and N-1203</li><li>RRK->AAA at 1187-1189: No nuclear targeting of HRG-stimulated MUC1 C-terminal nor JUP/gamma-catenin. No effect on interaction with JUP/gamma-catenin</li><li>RRK->QQQ at 1187-1189: No effect on palmitoylation</li><li>Y->F at 1191: No effect on EGFR-mediated phosphorylation</li><li>Y->N at 1191: No effect on endocytosis</li><li>Y->E at 1203: No effect on nuclear colocalization of MUC1CT and CTNNB1. No effect on in vitro PDFGR-induced cell invasiveness</li><li>Y->F at 1203: No effect on EGFR-mediated phosphorylation. No nuclear localization of MUC1CT. Reduced in vitro PDGFR-induced cell invasiveness</li><li>Y->N at 1203: Reduced endocytosis by 30%. Greatly reduced binding to AP1S2 and GRB2. Binding AP1S1 reduced by 25%. Reduced endocytosis by 77%; when associated with N-1243. Accumulates in intracellular compartments; when associated with C-1184 and C-1186</li><li>Y->F at 1209: Some reduction in EGFR-mediated phosphorylation</li><li>Y->F at 1218: No effect on EGFR-mediated phosphorylation. No nuclear colocalization of MUC1CT and CTNNB1</li><li>S->A at 1223: No change in PRKCD- nor GSK3B-mediated phosphorylation</li><li>T->A at 1224: Loss of PRKCD-mediated phosphorylation. Decreased PRKCD binding. No increased binding to CTNNB1 in the prescence of autophosphorylated PRKCD. Increases formation of E-cadherin/beta-catenin complex</li><li>S->A at 1227: No change in PRKCD-mediated phosphorylation. Loss of GSK3B-mediated phosphorylation. CTNNB1</li><li>Y->F at 1229: Greatly reduced EGFR- and Src-mediated phosphorylation. No nuclear localization of MUC1CT. Reduced in vitro PDGFR-mediated phosphorylation. Decreased Src-binding</li><li>Y->N at 1229: No effect on endocytosis</li><li>Y->N at 1243: Reduces binding to AP1S2 by 33%. Greatly reduced binding to GRB2. Reduced endocytosis by 50%. Reduced endocytosis by 77%; when associated with N-1203</li></ul>	<li>phosphorylation</li><li>localization</li><li>endocytosis</li>	<li>GO:0016310</li><li>GO:0051179</li><li>GO:0006897</li>	binding	GO:0005488	intracellular	GO:0005622	<li>P04196</li><li>Q02297</li><li>Q8SPJ1</li><li>Q5YJC2</li><li>Q28640</li><li>P13387</li><li>Q9WUD9</li><li>P35223</li><li>P35222</li><li>P35224</li><li>Q29435</li><li>P62993</li><li>Q07883</li><li>Q5PU49</li><li>P33433</li><li>Q02248</li><li>P49841</li><li>P55245</li><li>P43322</li><li>P14923</li><li>P15941</li><li>Q05655</li><li>Q60528</li><li>Q9WU82</li><li>P05480</li><li>Q5R4J7</li><li>P56377</li><li>P08640</li><li>P00533</li><li>P26233</li><li>P61966</li>		1
P15976	2623	<ul><li>K->R at 137: Abolishes sumoylation</li><li>S->A at 142: Loss of sumoylation</li><li>S->D at 142: Increased sumoylation in vitro</li><li>C->R at 204: Increase of dissociation rate from bound DNA</li></ul>	sumoylation	GO:0016925							1
P16050	246	<ul><li>M->V at 418: Catalyzes 15- and 12-lipoxygenation</li></ul>									1
P16083	4835	<ul><li>N->H at 162: Loss of activity toward CB1954, no effect toward menadione</li></ul>									1
P16104	3014	<ul><li>Q->N at 141: Reduced phosphorylation of S-140 in response to DNA damage</li></ul>	phosphorylation	GO:0016310							1
P16157	286	<ul><li>T->P at 1824: Abolishes interaction with OBSCN (in isoform Mu17)</li><li>K->E at 1826: Abolishes interaction with OBSCN (in isoform Mu17)</li><li>R->G at 1829: Abolishes interaction with OBSCN (in isoform Mu17)</li><li>K->E at 1830: Abolishes interaction with OBSCN (in isoform Mu17)</li></ul>							Q5VST9		1
P16442	28	<ul><li>M->T,V at 214: Alters substrate specificity so that both UDP-N-acetyl-D-galactosamine and UDP-galactose are utilized</li><li>P->S at 234: Alters substrate specificity of group B transferase</li><li>E->A at 303: Decreases specific activity of group B transferase almost to zero</li></ul>									1
P16444	1800	<ul><li>E->D,C at 141: Complete loss of activity</li><li>E->Q at 141: Partial loss of activity</li></ul>									1
P16455	4255	<ul><li>Y->A at 114: Decreases activity towards methylated DNA over 1000-fold. Slightly reduced reactivity with O6-benzylguanine</li><li>Y->E at 114: Loss of DNA repair activity. Slightly reduced reactivity with O6-benzylguanine</li><li>R->A,D at 128: Decreases activity towards methylated DNA over 1000-fold. No effect on reactivity with O6-benzylguanine</li><li>R->G at 128: Loss of DNA repair activity</li><li>R->K,L at 128: Slightly reduced DNA repair activity</li><li>P->K at 138: Decreased reactivity with O6-benzylguanine</li><li>P->A at 140: Decreased reactivity with O6-benzylguanine</li><li>C->A at 145: Loss of DNA repair activity</li><li>G->A at 156: Decreased reactivity with O6-benzylguanine</li><li>Y->A at 158: Reduced DNA repair activity. Decreased reactivity with O6-benzylguanine</li><li>Y->F at 158: Slightly reduced DNA repair activity</li></ul>	DNA repair	GO:0006281							1
P16930	2184	<ul><li>Q->R at 279: Lower activity</li></ul>									1
P17081	23433	<ul><li>T->N at 23: Loss of interaction with GOPC</li><li>D->A at 44: Loss of interaction with GOPC</li><li>Q->L at 67: Constitutively active. Interacts with PARD6 proteins and GOPC</li></ul>							<li>Q9HD26</li><li>Q5RD32</li>		1
P17213	671	<ul><li>S->C at 49: No impairment of secretion and increased propensity for dimer formation</li><li>C->A at 163: No impairment of secretion and/or biological actvity. Loss of dimer formation</li><li>C->S at 166: Poorly secreted. Loss of LPS-binding and biological activity</li><li>C->A at 206: Not secreted</li></ul>	secretion	GO:0046903	LPS-binding	GO:0001530					1
P17707	262	<ul><li>F->A at 7: No effect</li><li>E->Q at 8: Loss of activity. Normal putrescine-stimulated processing</li><li>E->Q at 11: Loss of activity. Loss of putrescine-stimulated processing</li><li>E->Q at 15: Little effect</li><li>C->A at 49: Little effect</li><li>E->Q at 61: Little effect</li><li>E->Q at 67: Little effect</li><li>K->A at 80: Greatly reduced catalytic activity. No putrescine-stimulated processing</li><li>C->A at 82: Loss of activity. Greatly reduced putrescine-stimulated processing</li><li>F->A at 223: No effect</li><li>C->A at 226: Little effect</li><li>S->A at 229: Loss of processing</li><li>S->C at 229: Greatly reduced processing</li><li>S->T at 229: Greatly reduced catalytic activity but little effect on processing</li><li>H->A at 243: Greatly reduced catalytic activity and processing</li><li>H->E at 243: Greatly reduced catalytic activity and processing</li><li>H->F at 243: Loss of processing</li><li>H->Y at 243: Loss of processing</li><li>E->Q at 247: Little effect</li><li>E->Q at 249: Little effect</li></ul>			catalytic activity	GO:0003824					1
P17948	2321	<ul><li>Y->F at 914: No loss of phosphorylation</li><li>Y->F at 1213: Loss of phosphorylation</li><li>Y->F at 1242: Loss of phosphorylation</li><li>Y->F at 1327: Loss of phosphorylation</li><li>Y->F at 1333: Loss of phosphorylation</li></ul>	phosphorylation	GO:0016310							1
P17980	5702	<ul><li>K->H at 233: Loss of function</li><li>D->A at 289: Loss of function</li></ul>									1
P18031	5770	<ul><li>S->A,D at 50: No phosphorylation</li></ul>	phosphorylation	GO:0016310							1
P18074	2068	<ul><li>K->R at 48: Decreased transcriptional activity of the reconstituted TFIIH complex</li></ul>									1
P18440	9	<ul><li>R->A,M,Q,K at 64: Reduced enzymatic activity</li></ul>									1
P18615	7936	<ul><li>RNCAF->EQMAT at 295-299: Abolishes interaction with RNA but not the interaction with other proteins of the NELF complex</li></ul>							Q6X4W1		1
P18850	22926	<ul><li>N->F at 391: Loss of proteolytic cleavage; when associated with L-394</li><li>P->L at 394: Loss of proteolytic cleavage; when associated with F-391</li><li>RR->AA at 415-416: Reduces proteolytic cleavage</li><li>L->V at 419: Reduces proteolytic cleavage</li></ul>									1
P19235	2057	<ul><li>T->A at 114: Little effect on EPO binding</li><li>S->A at 115: Little effect on EPO binding</li><li>S->A at 116: 10-fold reduction in EPO binding</li><li>F->A,L at 117: Greatly reduced EPO binding</li><li>F->W at 117: 60-fold reduction in EPO binding</li><li>F->Y at 117: 8-fold reduction in EPO binding</li><li>V->A at 118: 16-fold reduction in EPO binding</li><li>L->A at 120: Some reduction in EPO binding</li><li>E->A at 121: Little effect on EPO binding</li><li>R->A at 165: Little effect on EPO binding</li><li>M->A at 174: Little effect on EPO binding</li><li>S->A at 176: 16-fold reduction in EPO binding</li><li>H->A at 177: Little effect on EPO binding</li><li>R->A at 179: Little effect on EPO binding</li><li>Y->F at 454: Some loss of SOCS3 binding</li><li>Y->F at 456: Inhibition of STAT1/STAT3 activity. No effect on STAT5 activity. Some loss of SOCS3 binding</li><li>Y->F at 468: No effect on STAT1/STAT3 nor STAT5 activity</li></ul>			binding	GO:0005488			<li>P42224</li><li>P07865</li><li>P61635</li><li>P42229</li><li>P49157</li><li>Q6H8T2</li><li>Q6H8T1</li><li>Q90X67</li><li>Q28513</li><li>Q764M5</li><li>P49290</li><li>P33709</li><li>P42231</li><li>Q9BEG9</li><li>Q9GKA2</li><li>Q68AM8</li><li>Q867B1</li><li>P48617</li><li>P33707</li><li>P33708</li><li>P11678</li><li>P80550</li><li>P01588</li><li>Q6H8S9</li><li>O14543</li><li>P40763</li>		1
P19419	2002	<ul><li>K->R at 230: 9-fold increase in transcriptional activator activity; when associated with R-249. Reduction in sumoylation</li><li>K->R at 249: 9-fold increase in transcriptional activator activity; when associated with R-230. Reduction in sumoylation</li><li>K->R at 254: Reduction in sumoylation</li><li>S->A at 324: No effect on ternary complex formation</li><li>T->A at 336: No effect on ternary complex formation</li><li>T->A at 353: No effect on ternary complex formation</li><li>T->A at 363: No effect on ternary complex formation</li><li>T->A at 368: No effect on ternary complex formation</li><li>S->A at 383: 17% reduction in ternary complex formation</li><li>S->A at 389: 34% reduction in ternary complex formation</li><li>T->A at 417: No effect on ternary complex formation</li><li>S->A at 422: Slight reduction in ternary complex formation</li></ul>	sumoylation	GO:0016925	transcriptional activator activity	GO:0016563					1
P19440	2678	<ul><li>K->N at 100: No effect on activity</li><li>E->Q at 102: No effect on activity</li><li>R->K at 107: Reduces enzyme activity by 99%</li><li>R->Q,H at 107: Abolishes enzyme activity</li><li>E->Q at 108: Reduces enzyme activity by 98%</li><li>R->Q at 112: No effect on activity</li><li>R->Q at 139: No effect on activity</li><li>R->Q at 147: No effect on activity</li><li>R->Q at 150: No effect on activity</li><li>H->A at 383: Reduces enzyme activity by 66%</li><li>S->A at 385: No effect on activity</li><li>S->A at 413: No effect on activity</li><li>D->A at 422: Reduces enzyme activity by 90%</li><li>D->A at 423: Abolishes enzyme activity. Increases KM by over 1000-fold</li><li>S->A at 425: No effect on activity</li><li>S->A at 451: Reduces enzyme activity by 99%. Abolishes activity; when associated with A-452</li><li>S->A at 452: Reduces enzyme activity by 99%. Abolishes activity; when associated with A-451</li><li>C->A at 454: No effect on activity</li><li>H->A at 505: Reduces enzyme activity by 90%</li></ul>									1
P19447	2071	<ul><li>K->R at 346: No transcriptional activity of the reconstituted TFIIH complex</li></ul>									1
P19525	5610	<ul><li>SK->AA at 59-60: In FL-PKR-2AI; moderate loss of activity but no effect on dsRNA binding</li><li>K->A at 60: Impairs dsRNA binding but not dimerization or activity</li><li>A->E at 67: Significant loss of activity; loss of dsRNA binding and dimerization</li><li>S->A at 83: No effect on enzymatic activity; when associated with A-88; A-89 and A-90</li><li>T->A at 88: No effect on enzymatic activity; when associated with A-83; A-89 and A-90</li><li>T->A at 89: No effect on enzymatic activity; when associated with A-83; A-88 and A-90</li><li>T->A at 90: No effect on enzymatic activity; when associated with A-83; A-88 and A-89</li><li>TK->AA at 149-150: In FL-PKR-2AII; no effect on activity</li><li>S->A at 242: Moderate loss of activity; when associated with A-255 and A-258</li><li>Missing at 244-296: Loss of activity</li><li>T->A at 255: Moderate loss of activity; when associated with A-242 and A-255</li><li>T->A at 258: Moderate loss of activity</li><li>K->R at 296: Loss of activity</li><li>T->A at 446: Significant loss of activity and impairs autophosphorylation of T-451</li><li>T->A at 451: Loss of activity</li></ul>	autophosphorylation	GO:0046777	binding	GO:0005488			<li>P19525</li><li>Q03963</li>		1
P19634	6548	<ul><li>F->C at 155: Almost complete loss of activity</li><li>L->C at 156: Almost complete loss of activity</li><li>Q->C at 157: Reduces activity</li><li>S->C at 158: Almost complete loss of activity</li><li>D->C at 159: Almost complete loss of activity</li><li>V->C at 160: Reduces activity</li><li>F->C at 161: Reduces activity</li><li>F->C at 162: Almost complete loss of activity</li><li>L->C at 163: Reduces activity</li><li>F->C at 164: Almost complete loss of activity</li><li>L->C at 165: Reduces activity</li><li>L->C at 166: Reduces activity</li><li>P->A at 167: Reduces activity</li><li>P->C,G at 167: Almost complete loss of activity. Reduces membrane localization</li><li>P->A,C at 168: Almost complete loss of activity</li><li>P->G at 168: Reduces activity</li><li>I->C at 169: Reduces activity</li><li>I->C at 170: Reduces activity</li><li>L->C at 171: Reduces activity</li><li>D->C at 172: Almost complete loss of activity</li><li>A->C at 173: Reduces activity</li><li>G->C at 174: Reduces activity</li><li>Y->C at 175: Almost complete loss of activity</li><li>F->C at 176: Almost complete loss of activity</li><li>L->C at 177: Reduces activity</li><li>P->A at 178: No effect</li><li>R->C at 180: Reduces activity</li><li>Q->C at 181: Reduces activity</li><li>I->D,K at 534: Strongly reduced interaction with CHP2</li><li>I->K at 537: Strongly reduced interaction with CHP2</li></ul>	localization	GO:0051179			membrane	GO:0016020	O43745		1
P19835	1056	<ul><li>H->Q at 455: Abolishes lipase activity. Decreases Vmax for esterase activity by 2.5-fold</li></ul>							<li>Q7M4U7</li><li>P16397</li><li>P18773</li>		1
P19838	4790	<ul><li>C->S at 61: Suppresses S-nitrosylation-induced inhibition of DNA-binding activity</li><li>S->A at 903: Prevents p105 proteolysis in response to TNF-alpha</li><li>S->A at 907: Prevents p105 proteolysis in response to TNF-alpha</li><li>S->A at 921: Decrease in stimuli-induced phosphorylation. Loss of phosphorylation; when associated with A-923 and A-932</li><li>S->A at 923: Decrease in stimuli-induced phosphorylation. Loss of phosphorylation; when associated with A-921 and A-932</li><li>S->A at 932: Decrease in stimuli-induced phosphorylation. Loss of phosphorylation; when associated with A-921 and A-923</li></ul>	phosphorylation	GO:0016310	DNA-binding	GO:0003677			<li>Q8WNR1</li><li>P13296</li><li>Q8HZD9</li><li>Q8JFG3</li><li>P59684</li><li>P36939</li><li>P01375</li><li>O77764</li><li>Q8MKG8</li><li>Q2MH05</li><li>P04924</li><li>P33620</li><li>P79337</li><li>P23563</li><li>O35734</li><li>Q06599</li><li>Q9BEA1</li><li>P19101</li><li>P48094</li><li>Q75N23</li><li>Q9Y7R3</li><li>P52590</li><li>Q1G1A2</li><li>P16599</li><li>P59695</li><li>P59694</li><li>P59693</li><li>Q539C2</li><li>P06804</li><li>P51435</li><li>Q14511</li><li>P29553</li><li>P41895</li><li>Q19LH4</li><li>P55290</li><li>O49160</li><li>O77510</li><li>P23383</li><li>P51742</li><li>P51743</li><li>Q1WM27</li><li>O35177</li><li>P79374</li>		1
P20138	945	<ul><li>Y->A at 340: Abolishes binding to PTPN6 and PTPN11. Increases binding of red blood cells</li><li>Y->A,F at 358: Reduces binding to PTPN6</li></ul>			binding	GO:0005488			<li>P29350</li><li>Q90687</li><li>Q06124</li>		1
P20160	566	<ul><li>C->S at 52: Loss of antibiotic activity</li><li>C->S at 68: Loss of antibiotic activity</li></ul>									1
P20309	1131	<ul><li>E->A at 276: Loss of basolateral sorting</li><li>E->D at 276: Loss of basolateral sorting. No effect on basolateral sorting; when associated with L-280 and L-281</li><li>F->A at 280: Loss of basolateral sorting</li><li>F->L at 280: No effect on basolateral sorting</li><li>V->A at 281: Loss of basolateral sorting</li><li>V->L at 281: No effect on basolateral sorting</li></ul>									1
P20472	5816	<ul><li>D->A at 52: Inactivation</li><li>E->V at 63: Inactivation</li><li>D->A at 91: Inactivation</li><li>E->V at 102: Inactivation</li></ul>									1
P20671	3013	<ul><li>S->A at 2: Blocks the inhibition of transcription by RPS6KA5/MSK1</li></ul>	transcription	GO:0006350					<li>P32048</li><li>Q5R4K3</li><li>Q5F3L1</li><li>O75582</li>		1
P21397	4128	<ul><li>C->S at 165: No loss of activity</li><li>C->S at 266: No loss of activity</li><li>C->S at 306: No loss of activity</li><li>C->S at 321: No loss of activity</li><li>C->S at 323: No loss of activity</li><li>C->S at 374: Complete loss of activity</li><li>C->S at 398: No loss of activity</li><li>C->S at 406: Complete loss of activity</li></ul>									1
P21453	1901	<ul><li>R->A at 120: Drastically reduced affinity for sphingosine 1-phosphate</li><li>E->A at 121: Drastically reduced affinity for sphingosine 1-phosphate</li><li>E->Q at 121: Slight activation of the receptor at maximal ligand concentration</li><li>T->A at 236: Acts as a dominant negative GPCR and inhibits S1P-induced Rac activation, chemotaxis, and angiogenesis</li><li>R->A,V at 292: Drastically reduced affinity for sphingosine 1-phosphate</li></ul>	<li>chemotaxis</li><li>angiogenesis</li>	<li>GO:0006935</li><li>GO:0001525</li>	GPCR	GO:0004930			<li>Q9Z2A8</li><li>P31750</li><li>Q14703</li>		1
P21549	189	<ul><li>K->R at 209: Affects pyridoxal phosphate binding</li></ul>			pyridoxal phosphate binding	GO:0030170					1
P21580	7128	<ul><li>C->S at 103: Loss of deubiquitinating activity</li></ul>									1
P21673	6303	<ul><li>Y->F at 140: Reduces activity by 95%</li></ul>									1
P21675	6872	<ul><li>S->A at 137: No decrease in kinase activity</li><li>D->A at 145: Reduces kinase activity; when associated with A-147; A-149; A-150; A-152 and A-154</li><li>D->A at 147: Reduces kinase activity; when associated with A-145; A-149; A-150; A-152 and A-154</li><li>E->A at 149: Reduces kinase activity; when associated with A-145; A-147; A-150; A-152 and A-154</li><li>D->A at 150: Reduces kinase activity; when associated with A-145; A-147; A-149; A-152 and A-154</li><li>D->A at 152: Reduces kinase activity; when associated with A-145; A-147; A-149; A-150 and A-154</li><li>K->A at 154: Reduces kinase activity; when associated with A-145; A-147; A-149; A-150 and A-152</li><li>C->A at 305: Reduces kinase activity; when associated with A-307; A-308; A-309 and A-310</li><li>S->A at 307: Reduces kinase activity; when associated with A-305; A-308; A-309 and A-310</li><li>D->A at 308: Reduces kinase activity; when associated with A-305; A-307; A-309 and A-310</li><li>D->A at 309: Reduces kinase activity; when associated with A-305; A-307; A-308 and A-310</li><li>E->A at 310: Reduces kinase activity; when associated with A-305; A-307; A-308 and A-309</li></ul>			kinase activity	GO:0016301					1
P21731	6915	<ul><li>L->R at 291: Suppresses antagonist binding</li><li>R->Q at 295: Reduces antagonist binding</li><li>W->L at 299: Reduces antagonist binding</li><li>W->R at 299: Reduces antagonist binding</li></ul>			binding	GO:0005488					1
P21918	1816	<ul><li>N->Q at 7: Impairs subcellular location</li></ul>									1
P21926	928	<ul><li>C->A at 9: Loss of palmitoylation; when associated with A-78; A-79; A-87; A-218 and A-219</li><li>C->A at 78: Loss of palmitoylation; when associated with A-9; A-79; A-87; A-218 and A-219</li><li>C->A at 79: Loss of palmitoylation; when associated with A-9; A-78; A-87; A-218 and A-219</li><li>C->A at 87: Loss of palmitoylation; when associated with A-9; A-78; A-79; A-218 and A-219</li><li>C->A at 218: Loss of palmitoylation; when associated with A-9; A-78; A-79; A-87 and A-219</li><li>C->A at 219: Loss of palmitoylation; when associated with A-9; A-78; A-79; A-87 and A-218</li></ul>									1
P22064	4052										1
P22234	10606	<ul><li>H->Y at 303: Loss of AIR carboxylase activity</li><li>S->A at 332: Loss of AIR carboxylase activity</li><li>G->A at 334: Loss of AIR carboxylase activity</li><li>S->A at 400: No change of AIR carboxylase activity</li></ul>							<li>O74197</li><li>O28997</li><li>Q01930</li><li>Q49WI9</li><li>O06456</li><li>O06457</li><li>Q5HQA5</li><li>Q58033</li><li>Q5KGS6</li><li>P21264</li><li>P55195</li><li>Q8FYW3</li><li>P50504</li><li>Q9KVT7</li><li>Q54975</li><li>Q9KVT8</li><li>O58058</li><li>P43850</li><li>P38024</li><li>O66608</li><li>Q44678</li><li>Q44679</li><li>P74724</li><li>P65898</li><li>P65899</li><li>Q55498</li><li>O67239</li><li>Q4L574</li><li>Q7A695</li><li>P43849</li><li>P96880</li><li>Q9UY68</li><li>Q9DCL9</li><li>P22348</li><li>Q10457</li><li>P0AG18</li><li>P0AG19</li><li>Q5HH19</li><li>Q87KE0</li><li>Q87KE1</li><li>P72157</li><li>P72158</li><li>Q6GAE8</li><li>P41654</li><li>Q6GI19</li><li>Q7MGL1</li><li>Q7MGL2</li><li>P12045</li><li>Q9I7S8</li><li>Q5E1R4</li><li>Q5E1R3</li><li>Q8DDD7</li><li>Q8DDD8</li><li>Q8CPP2</li><li>P0C017</li><li>Q92210</li><li>P52558</li><li>Q9WYS7</li><li>P12044</li><li>Q99V32</li><li>P52559</li><li>P22234</li><li>P51583</li><li>P46701</li><li>P46702</li><li>P15567</li><li>Q8NX94</li><li>P09029</li><li>Q5RB59</li>		1
P22303	43	<ul><li>D->N at 206: Misfolding, absence of secretion</li><li>S->A at 234: Loss of activity</li><li>E->A at 365: Loss of activity</li><li>D->N at 435: Misfolding, absence of secretion</li><li>H->A at 478: Loss of activity</li><li>C->A at 611: Impairment of interchain disulfide bridge formation</li></ul>	secretion	GO:0046903							1
P22307	6342	<ul><li>N->D at 528: Strongly reduces sterol carrier and phosphatidylcholine transfer activity; when associated with D-530</li><li>N->I at 528: Strongly reduces sterol carrier and phosphatidylcholine transfer activity</li><li>G->D at 530: Strongly reduces sterol carrier and phosphatidylcholine transfer activity; when associated with D-528</li></ul>									1
P22681	867	<ul><li>S->D at 80: Abolishes interaction with ZAP70</li><li>P->A at 82: Abolishes interaction with ZAP70</li><li>D->Q at 229: Abolishes interaction with ZAP70</li><li>E->S at 240: Abolishes interaction with ZAP70</li><li>R->K at 294: Abolishes interaction with ZAP70</li><li>G->E at 306: Abolishes interaction with ZAP70, but does not affect interaction with SLA</li><li>Y->F at 371: Strongly reduces tyrosine phosphorylation by INSR; when associated with F-700 and F-774</li><li>Y->F at 700: Strongly reduces tyrosine phosphorylation by INSR; when associated with F-371 and F-774</li><li>Y->F at 731: No effect on tyrosine phosphorylation by INSR</li><li>Y->F at 774: Strongly reduces tyrosine phosphorylation by INSR; when associated with F-371 and F-700</li></ul>	phosphorylation	GO:0016310					<li>Q13239</li><li>Q9HD40</li><li>P43403</li><li>Q28516</li><li>P06213</li>		1
P22748	762	<ul><li>S->F at 284: Loss of C-terminal domain removal and inactivation</li></ul>									1
P22830	2235	<ul><li>C->S at 196: Loss of activity</li><li>C->S at 360: No loss of activity</li><li>C->S at 395: No loss of activity</li><li>C->D,H at 403: Loss of activity</li><li>C->D,H,S at 406: Loss of activity</li><li>C->H,S at 411: Loss of activity</li><li>F->L at 417: Decreased activity</li><li>F->Y,W at 417: Greatly reduced activity</li></ul>									1
P22888	3973	<ul><li>C->G at 643: Loss of palmitoylation</li><li>C->G at 644: Loss of palmitoylation</li></ul>									1
P23141	1066	<ul><li>N->A at 79: Abolishes glycosylation</li><li>S->A at 221: Loss of activity</li><li>E->A at 354: Loss of activity</li><li>H->A at 468: Loss of activity</li><li>Missing at 564-567: Does not result in secretion</li></ul>	secretion	GO:0046903							1
P23219	5742	<ul><li>S->N at 529: Abolishes cyclooxygenase activity</li></ul>									1
P23276	3792	<ul><li>C->S at 72: Loss of Kell-XK complex</li><li>C->S at 319: No loss of Kell-XK complex</li></ul>									1
P23368	4200	<ul><li>R->S at 67: Abolishes activation by fumarate</li><li>R->T at 91: Abolishes activation by fumarate</li></ul>									1
P23468	5789	<ul><li>R->A at 1178: 2.5-fold reduction in cleavage. 10-fold reduction in cleavage; when associated with A-1181</li><li>R->A at 1181: No reduction in cleavage. 10-fold reduction in cleavage; when associated with A-1178</li></ul>									1
P23560	627	<ul><li>R->A at 54: Abolishes processing by S1P</li></ul>							<li>Q9Z2A8</li><li>Q14703</li>		1
P24394	3566	<ul><li>Y->A at 38: 700-fold reduction in IL4 binding</li><li>Y->F at 38: 25-fold reduction in IL4 binding</li><li>M->A at 39: No effect on IL4 binding</li><li>S->A at 40: No effect on IL4 binding</li><li>L->A at 64: 100-fold reduction in IL4 binding</li><li>F->A at 66: 45-fold reduction in IL4 binding</li><li>L->A at 67: No effect on IL4 binding</li><li>L->A at 68: No effect on IL4 binding</li><li>D->A at 91: Little effect on IL4 binding</li><li>D->A at 92: 50-fold reduction in IL4 binding</li><li>V->A at 93: Little effect on IL4 binding</li><li>V->A at 94: 35-fold reduction in IL4 binding</li><li>S->A at 95: No effect on IL4 binding</li><li>D->A,N at 97: >150-fold reduction in IL4 binding</li><li>N->A at 98: No effect on IL4 binding</li><li>Y->A at 99: 10-fold reduction in IL4 binding</li><li>K->A at 116: Little effect on IL4 binding</li><li>P->A at 117: Little effect on IL4 binding</li><li>S->A at 118: No effect on IL4 binding</li><li>E->A at 119: No effect on IL4 binding</li><li>D->A at 150: Little effect on IL4 binding</li><li>N->A at 151: Little effect on IL4 binding</li><li>Y->A at 152: 40-fold reduction in IL4 binding</li><li>Y->F at 152: No effect on IL4 binding</li><li>L->A at 153: Little effect on IL4 binding</li><li>Y->A at 154: Little effect on IL4 binding</li><li>Y->A at 208: 500-fold reduction in IL4 binding</li><li>Y->F at 208: 200-fold reduction in IL4 binding</li><li>Y->F at 497: Abolishes IRS1 tyrosine phosphorylation. No cell proliferation</li><li>Y->F at 575: Loss of CD23 gene induction; when associated with F-603 and F-631</li><li>Y->F at 603: Loss of CD23 gene induction; when associated with F-575 and F-631</li><li>Y->F at 631: Loss of CD23 gene induction; when associated with F-575 and F-603</li><li>Y->F at 713: Increased IL4-induced cell proliferation and STAT6 activation</li></ul>	<li>phosphorylation</li><li>cell proliferation</li>	<li>GO:0016310</li><li>GO:0008283</li>	binding	GO:0005488			<li>Q9XS58</li><li>Q9MZR8</li><li>Q28224</li><li>P42202</li><li>Q2PE74</li><li>O77762</li><li>P79339</li><li>Q865X5</li><li>P35568</li><li>P42226</li><li>Q7YS71</li><li>Q865Y0</li><li>Q04745</li><li>P79155</li><li>P46652</li><li>P09715</li><li>Q3S4V6</li><li>P47966</li><li>P55030</li><li>Q60440</li><li>P51492</li><li>P05112</li><li>Q8HYB1</li><li>P30367</li><li>P30368</li><li>P51744</li><li>Q58M18</li>		1
P24530	1910	<ul><li>C->S at 402: Abolishes palmitoylation; when associated with S-403 and S-405</li><li>C->S at 403: Abolishes palmitoylation; when associated with S-402 and S-405</li><li>C->S at 405: Abolishes palmitoylation; when associated with S-402 and S-403</li></ul>									1
P24588	9495	<ul><li>L->P at 392: Prevents or diminishes RII binding</li><li>A->P at 396: Prevents or diminishes RII binding</li><li>V->P at 400: Prevents or diminishes RII binding</li><li>Q->P at 405: Prevents or diminishes RII binding</li><li>I->P at 408: Prevents or diminishes RII binding</li></ul>			binding	GO:0005488					1
P24666	52	<ul><li>C->S at 13: Inactive</li><li>Y->F at 132: Reduced phosphorylation and activity</li><li>Y->F at 133: Reduced phosphorylation. No effect on activity</li></ul>	phosphorylation	GO:0016310							1
P24941	1017	<ul><li>T->A at 14: 2-fold increase in activity</li><li>Y->F at 15: 2-fold increase in activity</li><li>T->A at 160: Abolishes activity</li></ul>									1
P25205	4172	<ul><li>S->A at 535: 50% reduction in phosphorylation by ATM or ATR</li></ul>	phosphorylation	GO:0016310					<li>Q13315</li><li>Q6PQD5</li><li>Q13535</li><li>Q9H6X2</li><li>Q9FKS4</li><li>Q9M3G7</li><li>P20848</li>		1
P25440	6046	<ul><li>Q->A at 78: Loss of homodimerization</li><li>MQ->AA at 142-143: Loss of homodimerization</li><li>Y->K at 153: Loss of homodimerization</li><li>I->A at 154: Partial loss of homodimerization; when associated with A-182</li><li>E->A at 170: Loss of homodimerization</li><li>L->E at 174: Loss of homodimerization</li><li>V->E at 177: Loss of homodimerization</li><li>Q->A at 182: Partial loss of homodimerization; when associated with A-154</li></ul>									1
P25963	4792	<ul><li>K->R at 21: Little change in Tax-stimulated transactivation. No sumoylation. Greatly reduced Tax- or cytokine-stimulated transactivation and decrease in ubiquitination and degradation; when associated with R-22</li><li>K->R at 22: Little change in Tax-stimulated transactivation. No sumoylation. Greatly reduced Tax- or cytokine-stimulated transactivation and decrease in ubiquitination and degradation; when associated with R-21</li><li>D->A at 31: Loss of phosphorylation; when associated with A-35</li><li>S->A at 32: Loss of phosphorylation and degradation; when associated with A-36</li><li>S->T at 32: Decrease in phosphorylation and degradation; when associated with T-36</li><li>D->A at 35: Loss in phosphorylation; when associated with A-31</li><li>D->G at 35: No change neither in phosphorylation, nor on degradation</li><li>S->A at 36: Loss of phosphorylation and degradation; when associated with A-32</li><li>S->T at 36: Decrease in phosphorylation and degradation; when associated with T-32</li><li>K->R at 38: No change in Tax-stimulated transactivation. No change in Tax-stimulated transactivation; when associated with R-47</li><li>Y->F at 42: No phosphorylation</li><li>MVKELQEI->AAKEA at 45-52: No nuclear export</li><li>K->R at 47: Little change in Tax-stimulated transactivation. No change in Tax-stimulated transactivation; when associated with R-38</li><li>LHLAVI->AHAAVA at 115-120: Greatly reduced nuclear localization. Great reduction in its ability to inhibit DNA binding of RELA</li><li>S->A at 234: No inducible ubiquitination nor protein degradation</li><li>S->A at 262: No inducible ubiquitination nor protein degradation</li><li>T->A at 263: No inducible ubiquitination nor protein degradation</li></ul>	<li>protein degradation</li><li>phosphorylation</li><li>sumoylation</li><li>nuclear export</li><li>localization</li>	<li>GO:0030163</li><li>GO:0016310</li><li>GO:0016925</li><li>GO:0051168</li><li>GO:0051179</li>	DNA binding	GO:0003677			<li>Q04206</li><li>P98152</li>		1
P26010	3695	<ul><li>D->A at 159: Loss of integrin alpha-E/beta-7 binding to E-cadherin and of integrin alpha-4/beta-7 binding to MADCAM1</li></ul>			binding	GO:0005488			Q13477		1
P26358	1786	<ul><li>R->A at 163: Abolishes interaction with PCNA</li><li>Q->A at 164: Abolishes interaction with PCNA</li><li>T->A at 166: Abolishes interaction with PCNA</li><li>I->A at 167: Abolishes interaction with PCNA</li><li>S->A at 169: No loss of interaction with PCNA</li><li>H->V at 170: Abolishes interaction with PCNA</li><li>F->V at 171: Abolishes interaction with PCNA</li><li>A->S at 172: No loss of interaction with PCNA</li><li>K->A at 173: No loss of interaction with PCNA</li></ul>							<li>O16852</li><li>Q9HJQ0</li><li>Q6B6N4</li><li>Q8PX25</li><li>P61074</li><li>O29912</li><li>Q9DDF1</li><li>Q43124</li><li>Q57697</li><li>P18248</li><li>O02115</li><li>P53358</li><li>O01377</li><li>Q6LWJ8</li><li>Q9MAY3</li><li>Q00268</li><li>Q00265</li><li>Q8TUF7</li><li>Q9DEA3</li><li>P17070</li><li>O58398</li><li>Q9M7Q7</li><li>O10308</li><li>P31008</li><li>P17917</li><li>P61258</li><li>P17918</li><li>P11038</li><li>P15873</li><li>Q7T6Y0</li><li>Q03392</li><li>P22177</li><li>P04961</li><li>Q979S2</li><li>P57761</li><li>O73947</li><li>Q9W644</li><li>Q9UWR9</li><li>Q9PTP1</li><li>Q74MV1</li><li>Q8TWK3</li><li>O82134</li><li>Q9HN45</li><li>Q6KZF1</li><li>O82797</li><li>P12004</li><li>P24314</li><li>Q9UYX8</li><li>Q9P9H8</li><li>Q43266</li><li>O27367</li>		1
P26368	11338	<ul><li>W->A at 92: Decreases affinity for UAF1 by 3 orders of magnitude</li><li>P->G at 96: Decreases affinity for UAF1 by 2 orders of magnitude</li><li>P->G at 104: Decreases affinity for UAF1 by 2 orders of magnitude</li><li>EE->RR at 387-388: Reduces interaction with SF1</li><li>DDEE->AAAA at 391-394: Reduces interaction with SF1</li><li>DDEE->RRKK at 391-394: Reduces interaction with SF1</li><li>EE->AA at 396-397: No effect</li><li>EE->GA at 396-397: Reduces interaction with SF1</li><li>EE->KK at 396-397: Reduces interaction with SF1</li><li>F->A at 454: Reduces interaction with SF1</li></ul>							<li>Q9GKL2</li><li>Q95L87</li><li>Q13285</li><li>Q12186</li><li>Q15637</li>		1
P26440	3712	<ul><li>E->D at 283: Residual activity</li><li>E->G,Q at 283: Loss of activity</li></ul>									1
P27105	2040	<ul><li>T->A at 182: No effect on oligomerization</li><li>W->A at 185: Complete loss of oligomerization</li><li>Y->A at 252: Complete loss of oligomerization</li><li>K->A at 263: Reduced oligomerization and lipid raft association</li><li>N->A at 264: Reduced oligomerization and lipid raft association</li><li>S->A at 265: Oligomerization reduced to 18%. Reduced lipid raft association</li><li>T->A at 266: Complete loss of oligomerization. Reduced lipid raft association</li><li>I->A at 267: Complete loss of oligomerization and lipid raft association</li><li>V->A at 268: Complete loss of oligomerization and lipid raft association</li><li>F->A at 269: Complete loss of oligomerization and lipid raft association</li><li>P->A at 270: Complete loss of oligomerization. No effect on lipid raft association</li><li>L->A at 271: Complete loss of oligomerization. Reduced lipid raft association</li><li>P->A at 272: Oligomerization reduced to 18%. Reduced lipid raft association</li><li>I->A at 273: Complete loss of oligomerization. Reduced lipid raft association</li><li>D->A at 274: Reduced oligomerization and lipid raft association</li><li>M->A at 275: Reduced oligomerization and lipid raft association</li><li>L->A at 276: Reduced oligomerization and lipid raft association</li></ul>					lipid raft	GO:0045121			1
P27169	5444	<ul><li>HQ->AA at 20-21: The signal peptide is cleaved; not associated with HDL</li><li>C->A,S at 284: No loss of activity</li></ul>									1
P27338	4129	<ul><li>C->S at 5: No loss of activity</li><li>C->S at 156: Complete loss of activity</li><li>T->A at 158: Dramatic loss of activity</li><li>C->S at 172: No loss of activity</li><li>C->S at 192: No loss of activity</li><li>I->F at 199: Alters specificity towards synthetic inhibitors</li><li>C->S at 297: No loss of activity</li><li>C->S at 312: No loss of activity</li><li>C->S at 365: Complete loss of activity</li><li>H->R at 382: Significant loss of activity</li><li>K->M at 386: No loss of activity</li><li>C->A at 389: Complete loss of activity</li><li>C->S at 389: No loss of activity</li><li>S->A at 394: No loss of activity</li><li>C->S at 397: Complete loss of activity</li></ul>									1
P27695	328	<ul><li>N->A at 212: Abolishes the AP endonuclease activity</li><li>N->Q,D at 212: Decreases the AP endonuclease activity</li></ul>							Q10002		1
P27816	4134	<ul><li>S->E at 696: No change in microtubule binding; no change in microtubule polymerization activity</li><li>S->E at 787: No change in microtubule binding; reduced microtubule polymerization activity</li></ul>	microtubule polymerization	GO:0046785	microtubule binding	GO:0008017					1
P28065	5698	<ul><li>G->A at 20: Impairs correct processing at the consensus site</li><li>T->A at 21: Impairs correct processing at the consensus site</li><li>K->A at 53: Impairs correct processing at the consensus site</li></ul>									1
P28068	3109	<ul><li>Y->A at 248: Abolishes targeting to endosomes and results in relocalization to the cell membrane</li><li>L->A at 251: Abolishes targeting to endosomes and results in relocalization to the cell membrane</li></ul>					<li>cell membrane</li><li>endosomes</li>	<li>GO:0005886</li><li>GO:0005768</li>			1
P28223	3356	<ul><li>G->V at 463: Loss of interaction with INADL</li><li>N->S at 465: No effect on interaction with INADL. Acquires the binding properties of HTR2C; when associated with S-470</li><li>C->S at 470: No effect on interaction with INADL. Acquires the binding properties of HTR2C; when associated with S-465</li><li>V->A at 471: Loss of interaction with INADL, CASK, APBA1, DLG1 and DLG4</li></ul>			binding	GO:0005488			<li>P78352</li><li>Q02410</li><li>P07498</li><li>Q15334</li><li>Q60F97</li><li>Q8NI35</li><li>O14936</li><li>Q5IS66</li><li>P28335</li><li>Q12959</li>		1
P28288	5825	<ul><li>G->R at 478: Decreased ATP-binding affinity</li><li>S->I at 572: Decreased ATPase activity</li></ul>			<li>ATPase activity</li><li>ATP-binding</li>	<li>GO:0016887</li><li>GO:0005524</li>					1
P28335	3358	<ul><li>S->A at 456: Loss of interaction with MPDZ</li><li>S->T at 456: No effect on interaction with MPDZ</li><li>S->A at 457: No effect on interaction with MPDZ</li><li>V->A at 458: Loss of interaction with MPDZ</li></ul>							O75970		1
P28370	6594	<ul><li>K->R at 214: No effect on neurite outgrowth</li></ul>									1
P28749	5933	<ul><li>S->A at 640: Strongly reduces phosphorylation by CDK2 and CDK4</li><li>S->R at 643: No effect on S-640 phosphorylation, but strongly increases S-640 phosphorylation; when associated to 657-A--A-660</li><li>S->A at 650: No effect on phosphorylation by CDK2</li><li>KRRL->AAAA at 657-660: Reduces S-640 phosphorylation by CDK2 and CDK4</li></ul>	phosphorylation	GO:0016310					<li>P48963</li><li>Q5E9Y0</li><li>P43450</li><li>P79432</li><li>P11802</li><li>P24941</li><li>O55076</li>		1
P28845	3290	<ul><li>KK->RR at 5-6: Predominantly inverted topology. No effect on activity</li><li>KK->SS at 5-6: Inverted topology. Reduced Vmax</li><li>K->R at 5: Predominantly inverted topology. No effect on activity</li><li>K->S at 5: Inverted topology. No effect on activity</li><li>K->R at 6: No effect on topology. Increased Km for corticosterone</li><li>K->S at 6: No effect on topology or activity</li><li>YYYY->AAAA at 18-21: No effect on topology. Reduced Vmax</li><li>YYYY->FFFF at 18-21: No effect on topology or activity</li><li>YYY->AYA at 19-21: No effect on topology. Reduced Vmax</li><li>EE->KK at 25-26: Inverted topology. Reduced Vmax</li><li>EE->KQ at 25-26: No effect on topology. Reduced Vmax</li><li>EE->QQ at 25-26: Reduced Vmax</li><li>E->K,Q at 25: No effect on activity</li><li>E->K at 26: No effect on activity</li><li>KK->SS at 35-36: Complete loss of activity</li></ul>									1
P28907	952	<ul><li>C->K at 119: Loss of cADPr hydrolase activity</li><li>C->R,E,A at 119: Loss of cADPr hydrolase and ADP-ribosyl cyclase activity</li><li>C->A at 160: Loss of cADPr hydrolase and ADP-ribosyl cyclase activity</li><li>C->A at 173: Loss of cADPr hydrolase and ADP-ribosyl cyclase activity</li><li>C->D,K,A at 201: Loss of cADPr hydrolase and ADP-ribosyl cyclase activity</li><li>C->E at 201: Loss of cADPr hydrolase activity</li></ul>			hydrolase activity	GO:0016787			<li>Q9P4P9</li><li>Q9SZ30</li><li>P02783</li><li>O94303</li><li>P33734</li>		1
P29016	910	<ul><li>YQ->AA at 329-330: Strongly reduced internalization and trafficking to endosomes</li></ul>					endosomes	GO:0005768			1
P29218	3612	<ul><li>K->Q at 36: 50-fold reduction in activity</li></ul>									1
P29373	1382	<ul><li>K->A at 21: Loss of ligand-induced nuclear import; when associated with A-30 and A-31</li><li>R->A at 30: Loss of ligand-induced nuclear import; when associated with A-21 and A-31</li><li>K->A at 31: Loss of ligand-induced nuclear import; when associated with A-21 and A-30</li></ul>	nuclear import	GO:0051170							1
P29466	834	<ul><li>C->A,S at 285: Loss of activity</li></ul>									1
P29508	6317	<ul><li>A->R at 341: Loss of inhibitory activity</li><li>F->A at 352: Loss of inhibitory activity</li><li>SS->PP at 354-355: Loss of inhibitory activity</li></ul>									1
P29590	5371	<ul><li>K->R at 65: Loss of one sumoylation. No effect on nuclear body formation. Loss of 2 sumoylations; when associated with R-490 with or without R-133 or R-150. No effect on nuclear body formation; when associated with R-490. No sumoylation nor nuclear body formation; when associated with R-160 and R-490</li><li>K->R at 68: No effect on sumoylation levels</li><li>K->R at 133: Loss of 2 sumoylations; when associated with R-65 and R-490</li><li>K->R at 150: Loss of 2 sumoylations; when associated with R-65 and R-490</li><li>K->R at 160: Loss of 2 sumoylations; when asociated with or without R-65. No sumoylation nor nuclear body formation; when associated with or without R-65 and R-490</li><li>K->R at 490: Loss of 2 sumoylations; when associated with R-65 with or without R-133. No effect on nuclear body formation; when associated with R-65. No sumoylation nor nuclear body formation; when associated with R-65 and R-160</li></ul>	sumoylation	GO:0016925							1
P29728	4939	<ul><li>D->A at 408: Loss of activity; when associated with A-410</li><li>D->A at 410: Loss of activity; when associated with A-408</li><li>D->A at 481: Loss of activity</li><li>C->A at 668: Loss of activity; when associated with A-669 and A-670</li><li>F->A at 669: Loss of activity; when associated with A-668 and A-670</li><li>K->A at 670: Loss of activity; when associated with A-668 and A-669</li></ul>									1
P30041	9588	<ul><li>S->A at 32: Loss of AIPLA2 activity, but no effect on NSGPX activity</li><li>C->S at 47: Loss of NSGPX activity, but no effect on AIPLA2 activity</li></ul>									1
P30044	25824	<ul><li>C->S at 100: Complete loss of activity</li><li>C->S at 125: No change in activity</li><li>C->S at 204: Complete loss of activity</li></ul>									1
P30101	2923	<ul><li>C->A at 57: No loss of activity. No loss of activity; when associated with A-406</li><li>C->S at 57: Activity changed to serine protease</li><li>C->S at 60: Activity changed to serine protease; when associated with S-409</li><li>C->A at 406: No loss of activity. No loss of activity; when associated with A-57</li><li>C->S at 406: Activity changed to serine protease</li><li>C->S at 409: Activity changed to serine protease; when associated with S-60</li></ul>							P83290		1
P30291	7465	<ul><li>K->R at 328: Abolishes activity</li></ul>									1
P30304	993	<ul><li>S->A at 76: Abolishes ubiquitination and impairs CHEK1-dependent degradation following checkpoint activation</li><li>S->A at 79: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination</li><li>D->A at 81: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination</li><li>S->A at 82: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination</li><li>S->A at 124: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-178; A-279 and A-293</li><li>S->A at 178: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-279 and A-293. Abrogates 14-3-3 protein binding</li><li>S->A at 279: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-293</li><li>S->A at 293: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-279</li><li>C->S at 431: Abolishes phosphatase activity</li><li>T->A at 507: Abrogates 14-3-3 protein binding; increases binding to cyclin B1</li><li>K->L at 514: Abrogates binding to CCNB1; when associated with L-520</li><li>R->L at 520: Abrogates binding to CCNB1; when associated with L-514</li></ul>			binding	GO:0005488			<li>Q5X1E5</li><li>O16852</li><li>Q7MBF4</li><li>Q88A53</li><li>Q5PC82</li><li>P61074</li><li>Q821A6</li><li>Q87SK9</li><li>Q9JZ88</li><li>Q5F8K9</li><li>Q9I5V3</li><li>Q63YC3</li><li>Q8Y395</li><li>Q6LV05</li><li>P18248</li><li>P53358</li><li>O01377</li><li>Q9PDL7</li><li>Q9UKB1</li><li>O14757</li><li>Q5WT58</li><li>Q00268</li><li>Q57JQ5</li><li>Q00265</li><li>Q8P5D4</li><li>P06961</li><li>P45269</li><li>P14635</li><li>P17070</li><li>Q88QU2</li><li>Q60CQ4</li><li>Q8ZI64</li><li>P31008</li><li>P17917</li><li>P17918</li><li>Q5E2K7</li><li>Q8CXX6</li><li>P22177</li><li>P04961</li><li>Q7M7K5</li><li>Q7MAZ9</li><li>Q8XBL4</li><li>Q9DG97</li><li>Q5P3T0</li><li>Q9Y297</li><li>Q8Z3M9</li><li>Q5ZRX9</li><li>Q60FY0</li><li>Q9CP21</li><li>Q82U82</li><li>Q6FA38</li><li>Q8ZLY4</li><li>Q9IBG1</li><li>P12004</li><li>Q62EU1</li><li>O96436</li><li>Q9JUB2</li><li>Q08301</li><li>Q9DGA4</li><li>Q665U9</li><li>Q8AYC9</li><li>Q9DGA0</li><li>Q9KPC6</li><li>P24314</li><li>Q8CWL6</li><li>Q8PPG9</li><li>Q9L7A3</li><li>Q6D160</li><li>Q87DS9</li><li>Q65Q41</li><li>P37882</li>		1
P30307	995	<ul><li>E->K at 352: Partial loss of HIV-1 Vpr binding</li><li>K->E at 359: No effect on HIV-1 Vpr binding</li></ul>			binding	GO:0005488					1
P30419	4836	<ul><li>G->D,K at 492: Reduced activity</li></ul>									1
P30518	554	<ul><li>C->S at 341: Reduced palmitoylation, reduced cell surface localization but coupling to G protein unaffected</li><li>C->S at 342: Reduced palmitoylation, reduced cell surface localization but coupling to G protein unaffected</li></ul>	localization	GO:0051179			cell surface	GO:0009928,GO:0009986			1
P30530	558	<ul><li>E->R at 56: Slightly reduced affinity for GAS6</li><li>E->R at 59: Reduced affinity for GAS6</li><li>T->R at 77: Reduced affinity for GAS6</li></ul>							Q14393		1
P30533	4043	<ul><li>H->A at 283: Strongly reduced interaction with LRP1; when associated with A-291; A-293; A-302; A-307 and A-341</li><li>H->A at 291: Strongly reduced interaction with LRP1; when associated with A-283; A-293; A-302; A-307 and A-341</li><li>H->A at 293: Strongly reduced interaction with LRP1; when associated with A-283; A-291; A-302; A-307 and A-341</li><li>H->A at 302: Strongly reduced interaction with LRP1; when associated with A-283; A-291; A-293; A-307 and A-341</li><li>H->A at 307: Strongly reduced interaction with LRP1; when associated with A-283; A-291; A-293; A-302 and A-341</li><li>H->A at 341: Strongly reduced interaction with LRP1; when associated with A-283; A-291; A-293; A-302 and A-307</li></ul>							<li>Q07954</li><li>P98157</li>		1
P31350	6241	<ul><li>S->A at 20: Enhances inhibitory effect on Wnt signaling</li><li>S->E at 20: Prevents inhibitory effect on Wnt signaling</li></ul>									1
P31689	3301	<ul><li>C->S at 394: Loss of farnesylation</li></ul>									1
P31749	207	<ul><li>T->D at 308: 5-fold activation and 18-fold activation; when associated with D-473</li><li>S->D at 473: 7-fold activation and 25-fold activation; when associated with D-308</li><li>Y->F at 474: 55% inhibition of activation</li></ul>									1
P31751	208	<ul><li>T->E at 309: Constitutively active; when associated with D-474</li><li>S->D at 474: Constitutively active; when associated with E-309</li></ul>									1
P33032	4161	<ul><li>Q->K at 235: 10% increase of binding to alpha-MSH</li><li>R->C at 272: 690% increase of binding to alpha-MSH</li></ul>			binding	GO:0005488			<li>P68000</li><li>P68001</li><li>Q9YGK2</li><li>Q9YGK4</li><li>P10000</li><li>P22923</li><li>P01189</li><li>P01197</li><li>P01196</li><li>P87352</li><li>P01194</li><li>P01193</li><li>P01192</li><li>P01191</li><li>P01190</li><li>P19402</li><li>P61281</li><li>P41589</li><li>P01201</li><li>Q91082</li><li>P61280</li><li>P06298</li><li>P06297</li><li>P11280</li><li>Q9YGK5</li><li>P06299</li><li>P11885</li><li>P21252</li>		1
P33527	4363	<ul><li>Q->A at 580: No effect</li><li>T->A at 581: No effect</li><li>S->A at 585: No effect</li><li>N->A at 597: Increases resistance to vincristine and decreases resistance to VP-16</li><li>S->A at 604: Increases estradiol glucuronide transport</li><li>S->A at 605: Decreases resistance to vincristine, VP-16 and doxorubicin</li><li>D->A at 792: Only partially affects protein maturation; impairs leukotriene C4 transport</li><li>D->L at 792: Impairs protein maturation and leukotriene C4 transport</li><li>D->L at 793: No effect on protein maturation and leukotriene C4 transport</li><li>R->D at 1046: Slightly impairs leukotriene C4 and estradiol glucuronide transport</li><li>D->R at 1084: Impairs leukotriene C4 and estradiol glucuronide transport</li><li>E->A,L,N,Q at 1089: Decreases resistance to anthracyclines</li><li>E->D at 1089: No effect</li><li>E->K at 1089: Abolishes resistance to anthracyclines</li><li>R->E at 1131: Slightly impairs leukotriene C4 and estradiol glucuronide transport</li><li>W->A,F,Y at 1246: Impairs estradiol glucuronide transport</li><li>W->C at 1246: Impairs estradiol glucuronide transport; loss of resistance to alkaloid vincristine, cationic anthracyclines, epipodophyllotoxin VP-16, but not potassium antimony tartrate; partial loss of resistance to sodium arsenite</li><li>K->L at 1333: Impairs leukotriene C4 transport</li><li>DE->LL at 1454-1455: Impairs leukotriene C4 transport</li></ul>	<li>transport</li><li>glucuronide transport</li>	<li>GO:0006810</li><li>GO:0015779</li>							1
P34913	2053	<ul><li>D->A at 9: Loss of phosphatase activity</li></ul>							<li>Q5X1E5</li><li>Q7M7K5</li><li>Q7MAZ9</li><li>Q8XBL4</li><li>Q88A53</li><li>Q5P3T0</li><li>Q7MBF4</li><li>Q8Z3M9</li><li>Q5PC82</li><li>Q5ZRX9</li><li>Q821A6</li><li>Q87SK9</li><li>Q9JZ88</li><li>Q9CP21</li><li>Q82U82</li><li>Q9I5V3</li><li>Q5F8K9</li><li>Q63YC3</li><li>Q8Y395</li><li>Q6LV05</li><li>Q8ZLY4</li><li>Q6FA38</li><li>Q9PDL7</li><li>Q62EU1</li><li>Q9JUB2</li><li>Q5WT58</li><li>Q665U9</li><li>Q57JQ5</li><li>Q9KPC6</li><li>Q8P5D4</li><li>Q8CWL6</li><li>Q8PPG9</li><li>P06961</li><li>P45269</li><li>Q9L7A3</li><li>Q88QU2</li><li>Q6D160</li><li>Q8ZI64</li><li>Q60CQ4</li><li>Q87DS9</li><li>Q65Q41</li><li>Q5E2K7</li><li>Q8CXX6</li>		1
P35125	9098	<ul><li>T->R at 150: Does not restore GAP activity in yeast complementation assay</li><li>R->Q at 187: Does not restore GAP activity in yeast complementation assay</li></ul>							<li>Q92263</li><li>P20936</li><li>Q92211</li><li>P09851</li><li>Q5PEA9</li><li>P74873</li><li>P74851</li><li>P50904</li>		1
P35222	1499	<ul><li>S->F at 29: No effect</li><li>F->A at 253: Abolishes or strongly reduces AXIN2 binding</li><li>H->A at 260: Abolishes or strongly reduces AXIN1 and AXIN2 binding. Strongly reduces phosphorylation and degradation; when associated with A-386 and A-383</li><li>K->A at 292: Abolishes or strongly reduces AXIN1 and AXIN2 binding</li><li>K->E at 312: Abolishes TCF7L2 binding</li><li>K->A at 345: Abolishes APC binding</li><li>W->A at 383: Abolishes APC binding. Strongly reduces phosphorylation and degradation; when associated with A-260 and A-386</li><li>R->A at 386: Strongly reduces APC binding. Strongly reduces phosphorylation and degradation; when associated with A-260 and A-383</li><li>N->A at 426: Abolishes TCF7L2 and LEF1 binding</li><li>K->A at 435: Strongly reduces or abolishes LEF1 binding</li><li>K->E at 435: Abolishes TCF7L2 binding</li><li>R->A at 469: Abolishes TCF7L2 binding, and strongly reduces or abolishes LEF1 binding</li><li>H->A at 470: Abolishes TCF7L2 binding, and strongly reduces or abolishes LEF1 binding</li><li>K->A at 508: Abolishes TCF7L2 and LEF1 binding</li><li>Y->E at 654: Enhances TBP binding and transactivation of target genes</li><li>Y->F at 654: Abolishes increase of TBP binding after phosphorylation by CSK</li><li>F->A at 660: Abolishes CTNNBIP1 binding; when associated with A-661</li><li>R->A at 661: Abolishes CTNNBIP1 binding; when associated with A-660</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488			<li>Q12731</li><li>O29874</li><li>P58178</li><li>P58177</li><li>O15169</li><li>Q57930</li><li>P41240</li><li>Q8TX38</li><li>Q8ZVR0</li><li>P53360</li><li>O27664</li><li>Q9P9I9</li><li>P13393</li><li>O43133</li><li>P25054</li><li>Q9UJU2</li><li>Q9V024</li><li>O23894</li><li>Q9NQB0</li><li>Q92117</li><li>Q92146</li><li>P26354</li><li>P26355</li><li>Q971V3</li><li>Q9YAT1</li><li>P93348</li><li>Q42808</li><li>Q9Y2T1</li><li>P62001</li><li>P62000</li><li>Q9NSA3</li><li>Q27850</li><li>O13270</li><li>Q0VBZ0</li><li>P46272</li><li>O17488</li><li>P48511</li><li>Q9YGV8</li><li>Q978J5</li><li>O58737</li><li>P26357</li><li>Q56253</li><li>O74045</li><li>Q9HLM8</li><li>Q52366</li><li>P41239</li><li>P32085</li><li>P32086</li><li>P20226</li><li>Q6M0L3</li><li>P52653</li><li>Q9UWN7</li><li>P17871</li><li>Q6L1R1</li><li>P91809</li><li>P53361</li><li>Q55031</li>		1
P35236	5778	<ul><li>S->A at 44: Prevents dissociation of bound MAP kinase and enhances their dephosphorylation</li><li>S->D at 44: Reduces binding of MAP kinase</li><li>T->A at 66: Prevents dissociation of bound MAP kinase and enhances their dephosphorylation; when associated with A-93</li><li>S->A at 93: Prevents dissociation of bound MAP kinase and enhances their dephosphorylation; when associated with A-66</li><li>Y->A at 125: Strongly reduced catalytic activity</li><li>D->A at 257: Loss of catalytic activity</li><li>C->S at 291: Loss of catalytic activity</li><li>Q->A at 335: Reduced catalytic activity</li></ul>	dephosphorylation	GO:0016311	<li>binding</li><li>catalytic activity</li>	<li>GO:0005488</li><li>GO:0003824</li>					1
P35240	4771	<ul><li>L->P at 64: Abolishes binding to AGAP2</li></ul>			binding	GO:0005488			Q99490		1
P35269	2962	<ul><li>S->A at 385: Eliminates putative kinase activity; when associated with A-389</li><li>T->A at 389: Eliminates putative kinase activity; when associated with A-385</li></ul>			kinase activity	GO:0016301					1
P35270	6697	<ul><li>S->A at 213: Abolishes phosphorylation by CaMK2. No effect on kinetic parameters</li></ul>	phosphorylation	GO:0016310							1
P35520	875	<ul><li>C->A at 272: Reduced heme content and cystathionine beta-synthase activity</li><li>C->S at 275: Reduced heme content and cystathionine beta-synthase activity</li></ul>							<li>Q9N0V7</li><li>P35520</li><li>Q58H57</li><li>Q91WT9</li><li>P32582</li><li>P46794</li><li>P32232</li><li>Q9YBL2</li>		1
P35527	3857	<ul><li>R->QHA at 163: Leads to aggregate formation</li></ul>									1
P35548	4488	<ul><li>T->A at 147: Does not bind DNA but still suppresses OCFRE activation</li></ul>									1
P35557	2645	<ul><li>E->K at 177: Small change in activity</li><li>E->A at 256: Inactive enzyme</li><li>K->A at 414: Small change in activity</li></ul>									1
P35568	3667	<ul><li>S->A at 794: Loss of phosphorylation by SNF1LK2</li></ul>	phosphorylation	GO:0016310					<li>Q9H0K1</li><li>Q9IA88</li><li>Q5REX1</li>		1
P35575	2538	<ul><li>H->A at 9: Partial loss of catalytic activity</li><li>H->A at 52: Partial loss of catalytic activity</li><li>K->N at 76: Loss of catalytic activity</li><li>H->A at 119: Loss of catalytic activity</li><li>R->Q at 170: Loss of catalytic activity</li><li>H->A at 176: Loss of catalytic activity</li><li>H->A at 179: Loss of catalytic activity</li><li>H->T at 197: Partial loss of catalytic activity</li><li>H->A at 252: Partial loss of catalytic activity</li><li>H->A at 307: Partial loss of catalytic activity</li><li>H->A at 353: Partial loss of catalytic activity</li></ul>			catalytic activity	GO:0003824					1
P35611	118	<ul><li>T->D at 445: Abolishes phosphorylation by ROCK1; when associated with D-480</li><li>T->D at 480: Abolishes phosphorylation by ROCK1; when associated with D-445</li></ul>	phosphorylation	GO:0016310					<li>Q8MIT6</li><li>Q13464</li><li>P61584</li><li>O77819</li>		1
P35712	55553	<ul><li>K->R at 404: Partial loss of sumoylation. Complete loss of sumoylation; when associated with R-417</li><li>K->R at 417: Partial loss of sumoylation. Complete loss of sumoylation; when associated with R-404</li></ul>	sumoylation	GO:0016925							1
P35869	196	<ul><li>V->A at 381: Increases specific ligand binding</li><li>V->D at 381: Abolishes specific ligand binding</li><li>V->L,G at 381: No effect on specific ligand binding</li></ul>			binding	GO:0005488					1
P35900	54474	<ul><li>S->A at 13: Promotes keratin filament disassembly</li><li>S->A at 14: No effect on keratin filament organization</li><li>R->H at 80: Leads to collapsed filaments</li></ul>					keratin filament	GO:0045095			1
P36404	402	<ul><li>Q->L at 70: Cell cycle arrest, reduced ability to form microtubules, and centrosome fragmentation</li></ul>	Cell cycle arrest	GO:0007050			<li>centrosome</li><li>microtubules</li>	<li>GO:0005813</li><li>GO:0005874</li>			1
P36406	373	<ul><li>T->N at 418: Maintains GTPase activity. Increases interaction with PSCD1</li><li>K->I at 458: Suppresses GTPase activity. Decreases interaction with PSCD1</li></ul>			GTPase activity	GO:0003924			<li>Q76MZ1</li><li>Q15438</li>		1
P36873	5501	<ul><li>C->A,S,L at 273: Abolishes interaction with microcystin toxin</li></ul>									1
P36897	7046	<ul><li>TT->VV at 185-186: Loss of phosphorylation on threonine residues. Loss of threonine phosphorylation, reduced phosphorylation on serine residues and loss of response to TGF-beta; when associated with A-187; A-189 and A-191</li><li>S->A at 187: Loss of threonine phosphorylation, reduced phosphorylation on serine residues and loss of response to TGF-beta; when associated with 185-VV-186; A-189 and A-191</li><li>S->A at 189: Loss of threonine phosphorylation, reduced phosphorylation on serine residues and loss of response to TGF-beta; when associated with 185-VV-186; A-187 and A-191</li><li>S->A at 191: Loss of threonine phosphorylation, reduced phosphorylation on serine residues and loss of response to TGF-beta; when associated with 185-VV-186; A-187 and A-189</li><li>T->D at 200: Loss of response to TGF-beta</li><li>T->V at 200: Loss of phosphorylation. Loss of response to TGF-beta</li><li>T->D at 204: Constitutive activation</li><li>T->V at 204: Reduced phosphorylation. Reduced response to TGF-beta</li></ul>	phosphorylation	GO:0016310							1
P36956	6720	<ul><li>S->A at 455: No effect on proteolytic processing</li><li>D->A at 456: No effect on proteolytic processing</li><li>S->A at 457: No effect on proteolytic processing</li><li>D->A at 460: No effect on proteolytic processing</li><li>D->A at 466: No effect on proteolytic processing</li><li>G->A at 481: No effect on proteolytic processing</li><li>M->A at 482: No effect on proteolytic processing</li><li>L->A at 483: No effect on proteolytic processing</li><li>DRSR->AS at 484-487: Strong reduction of proteolytic processing in response to low sterol</li><li>D->A at 484: Loss of proteolytic processing in response to low sterol</li><li>R->A at 485: No effect on proteolytic processing</li><li>R->A at 527: Loss of proteolytic processing in response to low sterol</li></ul>									1
P37173	7048	<ul><li>K->R at 277: Abolishes kinase activity, TGF-beta signaling and interaction with DAXX</li></ul>			kinase activity	GO:0016301			<li>O18805</li><li>Q5TJE1</li><li>Q9UER7</li>		1
P37840	6622	<ul><li>Y->F at 39: No effect on osmotic stress-induced phosphorylation</li><li>Y->F at 125: Abolishes osmotic stress-induced phosphorylation</li><li>Y->F at 133: No effect on osmotic stress-induced phosphorylation</li><li>Y->F at 136: No effect on osmotic stress-induced phosphorylation</li></ul>	phosphorylation	GO:0016310							1
P38398	672	<ul><li>R->G at 71: No effect on interaction with BAP1</li><li>S->A at 1143: Reduces in vitro phosphorylation by ATR</li><li>S->A at 1239: No effect on in vitro phosphorylation by ATR</li><li>S->A at 1280: Reduces in vitro phosphorylation by ATR</li><li>S->A at 1298: No effect on in vitro phosphorylation by ATR</li><li>S->A at 1330: No effect on in vitro phosphorylation by ATR</li><li>S->A at 1387: Loss of IR-induced S-phase checkpoint. Reduces in vitro phosphorylation by ATR</li><li>T->A at 1394: Reduces in vitro phosphorylation by ATR</li><li>S->A at 1423: Inhibition of the IR-induced G2 arrest. Reduces phosphorylation by ATR</li><li>S->A at 1457: Reduces in vitro phosphorylation by ATR</li><li>S->A at 1466: No effect on in vitro phosphorylation by ATR</li><li>S->A at 1524: No change in IR S-phase delay; when associated with A-1387. No effect on in vitro phosphorylation by ATR</li><li>T->A at 1720: No effect on in vitro phosphorylation by ATR: in dbSNP rsrs56195342</li><li>S->A at 1755: No effect on in vitro phosphorylation by ATR</li></ul>	<li>phosphorylation</li><li>S-phase</li>	<li>GO:0016310</li><li>GO:0051320</li>					<li>Q13535</li><li>Q00947</li><li>Q9H6X2</li><li>Q9FKS4</li><li>Q96QZ7</li><li>P23196</li><li>P20848</li><li>Q99496</li><li>Q92560</li>	rs56195342	1
P38484	3460	<ul><li>T->A,Q at 168: Does not affect function</li></ul>									1
P38567	6677	<ul><li>D->N at 146: Reduces activity by 80%</li><li>E->Q at 148: Loss of activity</li><li>R->G at 211: Reduces activity by over 90%</li><li>E->Q at 284: Loss of activity</li><li>R->T at 287: Loss of activity</li></ul>									1
P38570	3682	<ul><li>D->A at 208: Loss of E-cadherin binding</li><li>F->A at 316: Loss of E-cadherin binding</li></ul>			cadherin binding	GO:0045296					1
P38936	1026	<ul><li>T->A at 145: Reduces phosphorylation by Akt; no change in interaction with PCNA, CDK2 or CDK4; no change in subcellular location</li><li>T->D at 145: No interaction with PCNA; 59% inhibition of CDK2 binding; modest inhibition of CDK4 binding; no change in subcellular location</li><li>S->A at 146: No change in interaction with PCNA</li><li>S->D at 146: Reduces interaction with PCNA</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488			<li>O16852</li><li>Q9HJQ0</li><li>Q6B6N4</li><li>Q8PX25</li><li>P61074</li><li>Q8INB9</li><li>O29912</li><li>Q9DDF1</li><li>Q43124</li><li>Q57697</li><li>P18248</li><li>O02115</li><li>P53358</li><li>O01377</li><li>Q6LWJ8</li><li>Q9MAY3</li><li>Q00268</li><li>Q00265</li><li>Q8TUF7</li><li>Q9DEA3</li><li>P17070</li><li>Q5E9Y0</li><li>O58398</li><li>Q9M7Q7</li><li>O10308</li><li>P31008</li><li>P17917</li><li>P17918</li><li>P11038</li><li>P61258</li><li>P15873</li><li>Q7T6Y0</li><li>Q03392</li><li>P22177</li><li>P04961</li><li>Q979S2</li><li>P57761</li><li>O73947</li><li>Q9W644</li><li>Q9UWR9</li><li>O55076</li><li>Q9PTP1</li><li>Q74MV1</li><li>Q8TWK3</li><li>O82134</li><li>Q9HN45</li><li>P31750</li><li>Q6KZF1</li><li>O82797</li><li>P12004</li><li>P24314</li><li>Q9UYX8</li><li>P24941</li><li>Q9P9H8</li><li>Q43266</li><li>O27367</li><li>P48963</li><li>P43450</li><li>P79432</li><li>P11802</li>		1
P39748	2237	<ul><li>R->A at 29: No significant effect on exonuclease activity or Flap endonuclease activity</li><li>D->A at 34: Loss of Flap endonuclease activity but substrate binding activity is retained</li><li>R->A at 47: Significantly reduced exonuclease activity and reduced substrate binding. The positions of the cleavage sites are also shifted</li><li>R->A at 70: Loss of exonuclease activity and reduced endonuclease activity. Reduced substrate binding</li><li>R->A at 73: No significant effect on exonuclease activity or Flap endonuclease activity</li><li>K->A at 80: No significant effect on exonuclease activity or Flap endonuclease activity</li><li>D->A at 86: Loss of Flap endonuclease activity but substrate binding activity is retained</li><li>R->A at 103: No effect on Flap endonuclease activity or substrate binding</li><li>E->A at 158: Loss of Flap endonuclease activity and substrate binding</li><li>D->A at 179: No effect on Flap endonuclease activity or substrate binding</li><li>D->A at 181: Loss of Flap endonuclease activity but substrate binding activity is retained</li><li>G->A at 231: Loss of Flap endonuclease activity and substrate binding</li><li>D->A at 233: Loss of Flap endonuclease activity and substrate binding</li></ul>			binding	GO:0005488			<li>P04323</li><li>P20825</li><li>P10399</li><li>P10978</li><li>P00641</li><li>P20321</li><li>Q00962</li><li>P38446</li><li>P15629</li><li>P00638</li><li>P13717</li><li>P05400</li><li>P03554</li><li>Q03269</li><li>P03556</li><li>P03555</li><li>Q03277</li><li>P10394</li><li>Q03278</li><li>Q03275</li><li>Q05118</li><li>Q03276</li><li>P11283</li><li>P16423</li><li>Q03273</li><li>Q03274</li><li>Q03271</li><li>Q03272</li><li>P09523</li><li>P11369</li><li>Q8I7P9</li><li>Q03270</li><li>P03697</li><li>P11367</li><li>Q02964</li><li>P10400</li><li>P20314</li><li>Q03279</li><li>P10401</li>		1
P40189	3572	<ul><li>S->A at 782: Increases cell surface expression</li></ul>					cell surface	GO:0009928,GO:0009986			1
P40198	1084	<ul><li>Y->F at 230: Loss of phosphorylation and 30% reduction in bacterial uptake. More than 60% reduction in bacterial uptake and loss of RAC1 stimulation; when associated with F-241</li><li>Y->F at 241: Loss of phosphorylation and 30% reduction in bacterial uptake. More than 60% reduction in bacterial uptake and loss of RAC1 stimulation; when associated with F-230</li></ul>	phosphorylation	GO:0016310					<li>Q9SSX0</li><li>Q38912</li><li>O04369</li><li>P13362</li><li>P80236</li><li>P62999</li><li>P63000</li><li>P62998</li>		1
P40337	7428	<ul><li>Y->N at 98: No interaction with HIF1A. No HIF1A degradation</li></ul>							<li>Q98SW2</li><li>Q0PGG7</li><li>Q309Z6</li><li>Q9YIB9</li><li>Q16665</li><li>Q9XTA5</li>		1
P40855	5824	<ul><li>Missing at 296-299: Abolishes binding to PEX10, PEX11B, PEX12 and PEX13. Does not affect binding to PEX3 and PEX16</li><li>C->A at 296: Slightly inhibits PEX19 function on peroxisome biogenesis</li><li>C->S at 296: Abolishes farnesylation. Abolishes PEX19 function on peroxisome biogenesis. Does not affect binding to ABCD1, ABCD2 and ABCD3</li></ul>			binding	GO:0005488	peroxisome	GO:0005777	<li>Q04370</li><li>P80667</li><li>Q3SZD1</li><li>P56589</li><li>Q00940</li><li>O94227</li><li>Q01497</li><li>Q9UBJ2</li><li>Q92262</li><li>Q9SYU4</li><li>Q5RFI0</li><li>Q92265</li><li>Q05568</li><li>Q60HE1</li><li>Q874C0</li><li>Q60415</li><li>P28795</li><li>Q92266</li><li>Q92968</li><li>P78980</li><li>Q00317</li><li>O96011</li><li>O00623</li><li>Q759H4</li><li>P40855</li><li>Q01961</li><li>P28288</li><li>Q9Y5Y5</li><li>Q5R7U2</li><li>Q07418</li><li>P33897</li><li>O60683</li><li>Q8HXW8</li><li>Q6BK00</li><li>Q9ET67</li><li>Q9JJK3</li>		1
P41181	359	<ul><li>S->A at 148: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis</li><li>S->D at 148: Retained in the endoplasmic reticulum</li><li>S->A at 229: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis</li><li>S->D at 229: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis</li><li>S->A at 231: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis</li><li>S->D at 231: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis</li><li>T->A at 244: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis</li><li>T->E at 244: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis</li><li>S->A at 256: Retained in vesicles</li><li>S->D at 256: Expressed in the apical membrane</li></ul>	endocytosis	GO:0006897			<li>membrane</li><li>ER</li>	<li>GO:0016020</li><li>GO:0005783</li>			1
P41182	604	<ul><li>S->A at 333: Decrease in phosphorylation by MAPK1</li><li>S->A at 343: Decrease in phosphorylation by MAPK1</li></ul>	phosphorylation	GO:0016310					<li>P46196</li><li>P28482</li><li>Q5Z9J0</li>		1
P41212	2120	<ul><li>S->A at 22: No effect</li><li>S->A at 213: No effect</li><li>S->A at 238: No effect</li><li>S->A at 257: No phosphorylation by MAPK14</li></ul>	phosphorylation	GO:0016310					<li>Q95NE7</li><li>O02812</li><li>Q16539</li>		1
P41229	8242	<ul><li>H->A at 514: Abolishes enzymatic activity</li></ul>									1
P41240	1445	<ul><li>Y->F at 184: Abolishes phosphorylation</li><li>Y->F at 304: Decreases activity by two-thirds and alters conformation</li></ul>	phosphorylation	GO:0016310							1
P41743	5584	<ul><li>K->A at 20: No effect on interaction with SQSTM1</li><li>D->A at 63: Loss of interaction with PARD6A and with SQSTM1</li><li>E->A at 76: Slight decrease of interaction with PARD6A. Loss of interaction with PARD6A; when associated with A-82</li><li>R->A at 82: Slight decrease of interaction with PARD6A. Loss of interaction with PARD6A; when associated with A-76</li><li>Y->F at 256: No effect on the Src-mediated phosphorylation state. No effect on Src-induced enzyme activity. Little effect on TRAF6-mediated activation of NF-kappa-B. Decreased binding to KPNB1/importin-beta</li><li>Y->F at 271: No effect on the Src-mediated phosphorylation state. No effect on Src-induced enzyme activity. No effect on TRAF6-mediated activation of NF-kappa-B</li><li>Y->F at 325: No effect on the Src-mediated phosphorylation state. Significant reduction of Src-induced enzyme activity. Greatly reduced TRAF6-mediated activation of NF-kappa-B. Reduces NGF-dependent cell survival</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488			<li>P05480</li><li>Q5RBA5</li><li>Q14974</li><li>Q9NPB6</li><li>P21617</li><li>Q90W38</li><li>Q13501</li><li>Q9WUD9</li><li>Q6YBR5</li><li>P34129</li><li>Q9Y4K3</li>		1
P42126	1632	<ul><li>E->A at 178: Loss of activity</li></ul>									1
P42224	6772	<ul><li>K->R at 110: Sumoylated</li><li>Y->F at 701: No effect on basal sumoylation. Enhances sumoylation in the presence of MAPK stimulation</li><li>K->R at 703: Abolishes sumoylation by SUMO1. Increased IFN-gamma-mediated transactivation</li><li>S->A at 727: Decreased transcriptional activation. No effect on basal sumoylation. No enhancement of sumoylation on MAPK stimulation. No PKCdelta-induced apoptosis</li><li>S->D at 727: No change in enhancement of MAPK-induced sumoylation. Basal interaction with PIAS1. Interaction with PIAS1 increased on MAPK stimulation</li><li>S->E at 727: No change in enhancement of MAPK-induced sumoylation</li></ul>	<li>sumoylation</li><li>apoptosis</li>	<li>GO:0016925</li><li>GO:0006915</li>					<li>O35735</li><li>Q2EF74</li><li>Q25BC0</li><li>P07353</li><li>Q9TTB0</li><li>O77763</li><li>P27638</li><li>Q2PE75</li><li>Q866Y6</li><li>Q5E9D1</li><li>P79154</li><li>Q9TV67</li><li>Q865Y4</li><li>Q4ZH68</li><li>P17803</li><li>O42781</li><li>P30123</li><li>P42160</li><li>P42161</li><li>P42162</li><li>Q9QXX2</li><li>Q62574</li><li>Q7TSP4</li><li>Q9YGB9</li><li>P49708</li><li>O73915</li><li>O75925</li><li>P28333</li><li>P63309</li><li>Q5R6J4</li><li>Q00859</li><li>O57608</li><li>P55857</li><li>P46402</li><li>O57603</li><li>P28341</li><li>Q9MZD5</li><li>P01579</li><li>Q865W6</li><li>P63310</li><li>P63311</li><li>Q8MKF5</li><li>O35497</li><li>O57571</li><li>P63165</li><li>Q647G2</li><li>Q865X1</li><li>P17773</li><li>Q1WM28</li><li>P10829</li><li>P01581</li><li>P01580</li><li>Q8SPW9</li><li>Q5CCK0</li><li>Q5I6S9</li>		1
P42226	6778	<ul><li>L->A at 802: Abolishes the interaction with NCOA1; when associated with A-805</li><li>L->A at 805: Abolishes the interaction with NCOA1; when associated with A-802</li></ul>							Q15788		1
P42330	8644	<ul><li>K->E at 75: No effect on 17beta-HSD activity</li></ul>									1
P42566	2060	<ul><li>V->E at 154: Loss of interaction with STON2 NPF motifs</li><li>W->A at 169: Loss of interaction with STON2 NPF motifs</li></ul>							<li>P41334</li><li>P41321</li><li>Q8MP00</li><li>Q8WXE9</li><li>P41967</li>		1
P42575	835	<ul><li>C->S at 320: Loss of function</li><li>A->T at 369: Loss of function</li></ul>									1
P43119	5739	<ul><li>C->S at 308: Reduced palmitoylation, coupling to G protein unaffected. Abolished palmitoylation and coupling to G protein; when associated with S-311</li><li>C->S at 309: No effect on palmitoylation level</li><li>C->S at 311: Reduced palmitoylation, coupling to G protein unaffected. Abolished palmitoylation and coupling to G protein; when associated with S-308</li><li>C->S at 383: Abolishes isoprenylation</li></ul>									1
P43155	1384	<ul><li>Y->A at 452: Increases the KM for carnitine 100-fold</li><li>Y->F at 452: Increases the KM for carnitine 320-fold and reduces enzyme activity 10000-fold</li><li>T->A at 465: Increases the KM for carnitine almost 70-fold and reduces enzyme activity 450-fold</li><li>R->Q at 518: Increases the KM for carnitine 230-fold and reduces enzyme activity almost 100-fold</li><li>F->A at 566: Increases the KM for carnitine 18-fold and reduces enzyme activity 100-fold</li><li>F->Y at 566: No effect</li></ul>									1
P43246	4436	<ul><li>G->A at 674: Mainly causes defects in mismatch binding or release efficiency</li><li>K->R at 675: No effect on mismatch binding, complete loss of DNA repair function when associated with MSH6 mutant R-1140</li></ul>	DNA repair	GO:0006281	binding	GO:0005488			<li>P52701</li><li>Q03834</li>		1
P43250	2870	<ul><li>C->S at 561: Abolishes palmitoylation; when associated with S-562 and S-565</li><li>C->S at 562: Abolishes palmitoylation; when associated with S-561 and S-565</li><li>C->S at 565: Abolishes palmitoylation; when associated with S-561 and S-562</li></ul>									1
P43355	4100	<ul><li>D->A at 163: Abolishes HLA-A1 binding</li><li>Y->A at 169: Abolishes HLA-A1 binding</li></ul>			binding	GO:0005488					1
P43356	266740	<ul><li>V->D at 170: Improves ability to bind to HLA-A1</li></ul>									1
P43357	4102	<ul><li>D->A at 170: Abolishes HLA-A1 binding</li><li>Y->A at 176: Abolishes HLA-A1 binding</li></ul>			binding	GO:0005488					1
P43403	7535	<ul><li>Y->F at 315: No inhibition of activation</li><li>Y->F at 319: Inhibition of activation</li></ul>									1
P45381	443	<ul><li>R->K at 71: Reduces activity by 99%</li><li>Y->F at 164: Reduces activity by 99%</li><li>R->K at 168: Reduces activity by 99%</li><li>E->A at 178: Reduces activity by 99%</li><li>E->D at 285: 5-fold decrease in activity</li><li>Y->F at 288: Reduces activity by 99%</li></ul>									1
P45983	5599	<ul><li>T->A at 183: Phosphorylation blocked</li><li>Y->F at 185: Phosphorylation blocked</li></ul>	Phosphorylation	GO:0016310							1
P46060	5905	<ul><li>K->R at 524: No association with mitotic spindles during mitosis</li></ul>	mitosis	GO:0007067			spindles	GO:0005819			1
P46063	5965	<ul><li>K->A at 119: Abrogates helicase activity</li></ul>							<li>Q8V736</li><li>O67037</li><li>Q9UZ86</li><li>Q68772</li><li>O51934</li><li>P74759</li><li>P37987</li><li>P22657</li><li>Q04575</li><li>Q971T7</li><li>P27328</li><li>P28726</li><li>Q07630</li><li>P27327</li><li>Q9WJB2</li><li>Q3I5J6</li><li>Q66914</li><li>P16342</li><li>Q89273</li><li>P36286</li><li>Q66198</li><li>P22168</li><li>P19751</li><li>Q8V6W7</li><li>P28897</li><li>Q96725</li><li>P19811</li><li>Q91A29</li><li>O29238</li><li>P09395</li><li>P15402</li><li>Q86117</li><li>P09498</li><li>Q86119</li><li>Q58907</li><li>Q83017</li><li>Q97ZF5</li><li>Q8R979</li><li>Q6F598</li><li>Q08582</li><li>Q91AV2</li><li>P17779</li><li>O58530</li><li>O67226</li><li>Q07518</li><li>P95479</li><li>P54634</li><li>Q8ZXT5</li><li>Q9IW06</li><li>Q04544</li><li>Q975P6</li><li>Q8V439</li><li>P17965</li><li>Q91QT2</li><li>Q04561</li><li>Q97ZZ8</li><li>P27411</li><li>P27410</li><li>P27920</li><li>P22591</li><li>Q9PYA3</li><li>P20951</li><li>P15095</li><li>Q9YN02</li><li>P27407</li><li>Q06502</li><li>P18458</li><li>Q05002</li><li>Q9YCB6</li><li>P59641</li><li>Q69014</li><li>Q8B912</li><li>P27409</li><li>Q9YC75</li>		1
P46098	3359	<ul><li>W->S at 178: Abolished ligand binding to the heteromeric receptor</li><li>R->Q at 432: Little effect on conductance. Massive increase of conductance; when associated with D-436 and A-440</li><li>R->D at 436: Increased conductance. Massive increase of conductance; when associated with Q-432 and A-440</li><li>R->A at 440: Increased conductance. Massive increase of conductance; when associated with Q-432 and D-436</li></ul>			binding	GO:0005488					1
P46108	1398	<ul><li>D->K at 150: Abolishes interaction with DOCK1</li></ul>							Q14185		1
P46379	7917	<ul><li>D->A at 1001: Abolishes cleavage by caspase-3</li></ul>									1
P46527	1027	<ul><li>S->A at 10: Loss of phosphorylation by UHMK1. No translocation to the cytoplasm. Greater cell cycle arrest</li><li>S->D at 10: Exported to the cytoplasm. Inhibits cell cycle arrest</li><li>S->E at 10: Increased stability in vivo and in vitro</li><li>Y->F at 74: No change in binding CDK4. Translocates to nucleus</li><li>Y->F at 88: Abolishes LYN-mediated phosphorylation. Reduced CDK2 phosphorylation on T-187. Greater cell cycle arrest into S-phase. No effect on binding CDK2 complexes. Reduction of CDK4 binding. No nuclear translocation. Completely abolishes CDK4 binding; when associated with F-89</li><li>Y->F at 89: No effect on binding CDK2 complexes. Reduction of CDK4 binding. No nuclear translocation. Completely abolishes CDK4 binding; when associated with F-88</li><li>T->A at 157: Greatly reduced PKB/AKT1-mediated phosphorylation. Nuclear location. Inhibits cyclin E/CDK2 cell cycle progression. No effect on binding AKT1. Completely abolishes PKB/AKT1-mediated phosphorylation and no cytoplasmic translocation; when associated with A-198</li><li>S->A at 161: No change in PKB/AKT1-mediated phosphorylation</li><li>T->A at 162: No change in PKB/AKT1-mediated phosphorylation</li><li>T->A,D at 187: No change in PKB/AKT1- nor UHMK1-mediated phosphorylation</li><li>T->A,D at 198: Abolishes PKB/AKT1-mediated phosphorylation. 46% cytoplasmic location. Greatly reduced binding to YWHAQ. Equally reduced binding; when associated with A-10 and A-187. No nuclear import; when associated with A-157. Completely abolishes PKB/AKT1-mediated phosphorylation and no cytoplasmic translocation; when associated with A-157</li></ul>	<li>phosphorylation</li><li>cell cycle</li><li>nuclear import</li><li>S-phase</li><li>cell cycle arrest</li>	<li>GO:0016310</li><li>GO:0007049</li><li>GO:0051170</li><li>GO:0051320</li><li>GO:0007050</li>	binding	GO:0005488	<li>cytoplasm</li><li>nucleus</li>	<li>GO:0005737</li><li>GO:0005634</li>	<li>P22177</li><li>P04961</li><li>O16852</li><li>Q5ZMD1</li><li>P61074</li><li>Q5RFJ2</li><li>Q8INB9</li><li>Q38998</li><li>O55076</li><li>P27348</li><li>P31750</li><li>Q6Q6X0</li><li>P18248</li><li>P53358</li><li>P47196</li><li>O01377</li><li>Q01314</li><li>P12004</li><li>Q8VYX2</li><li>P07948</li><li>Q3SZI4</li><li>Q00268</li><li>Q00265</li><li>Q8TAS1</li><li>P24314</li><li>P24941</li><li>P17070</li><li>P48963</li><li>Q5E9Y0</li><li>P43450</li><li>O97790</li><li>P79432</li><li>P11802</li><li>P31008</li><li>P17917</li><li>P17918</li><li>P31749</li>		1
P46734	5606	<ul><li>S->A at 218: Inactivation</li><li>S->E at 218: Constitutive activation</li><li>T->A at 222: Inactivation</li><li>T->E at 222: Constitutive activation</li></ul>									1
P46940	8826	<ul><li>S->A at 1441: Abolishes neurite outgrowth promoting activity; when associated with A-1443</li><li>S->E at 1441: Strongly enhances neurite outgrowth promoting activity; when associated with A-1443</li><li>S->A at 1443: Abolishes neurite outgrowth promoting activity; when associated with A-1441</li><li>S->D at 1443: Strongly enhances neurite outgrowth promoting activity; when associated with A-1441</li></ul>									1
P47712	5321	<ul><li>C->A at 139: No effect on phospholipase activity; when associated with A-141 and A-151</li><li>C->A at 141: No effect on phospholipase activity; when associated with A-139 and A-151</li><li>C->A at 151: No effect on phospholipase activity; when associated with A-139 and A-141</li><li>S->A at 195: 5-fold reduced phospholipase and lysophosphatase activities. 100-fold reduced phospholipase and lysophosphatase activities; when associated with A-577</li><li>S->A at 215: No effect on phospholipase or lysophosphatase activity</li><li>C->A at 220: No effect on phospholipase activity</li><li>S->A,C,T at 228: Abolishes both phospholipase and lysophosphatase activities</li><li>C->A at 324: No effect on phospholipase activity; when associated with A-331</li><li>C->A at 331: No effect on phospholipase activity; when associated with A-324</li><li>S->A at 505: Decreases agonist-stimulated release of arachidonic acid</li><li>S->A at 577: 7-fold reduced phospholipase and lysophosphatase activities. 100-fold reduced phospholipase and lysophosphatase activities; when associated with A-195</li><li>C->A at 620: No effect on phospholipase activity; when associated with A-634</li><li>C->A at 634: No effect on phospholipase activity; when associated with A-620</li><li>C->A at 726: No effect on phospholipase activity</li></ul>			phospholipase activity	GO:0004620					1
P48023	356	<ul><li>P->D,F,R at 206: Lowers binding to TNFRSF6 and reduces cytotoxity more than 100-fold</li><li>Y->F,R at 218: Lowers binding to TNFRSF6 and abolishes cytotoxity</li><li>F->L at 275: Abolishes binding to TNRFSF6 and cytotoxicity</li></ul>			binding	GO:0005488			<li>O77736</li><li>Q9TSN4</li><li>P51867</li><li>Q9BDN0</li><li>P25445</li><li>Q9BDP2</li><li>Q9BDN4</li>		1
P48357	3953	<ul><li>Y->F at 986: Greatly reduced PTPN11 binding; no PTPN11 phosphorylation; no effect on STAT3 phosphorylation</li><li>YY->FF at 1078-1079: No effect on PTPN11 nor STAT3 phosphorylation</li><li>Y->F at 1141: No effect on PTPN11 phosphorylation; no STAT3 phosphorylation</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488			<li>Q90687</li><li>Q06124</li><li>P61635</li><li>P40763</li>		1
P48552	8204	<ul><li>PIDL->AAAA at 440-443: Abolishes interaction with CTBP1</li><li>PID->AIA at 440-442: Abolishes interaction with CTBP1 and attenuates nuclear hormone receptor-dependent transcription repression</li><li>DL->AA at 442-443: Reduces, but does not completely abolish, interaction with CTBP. Reduces transcriptional repression</li><li>DL->AS at 442-443: Disrupts interaction with CTBP1, and CTBP2 to a lesser extent. Disrupts transcriptional repression; when associated with 567-AS-568</li><li>K->Q at 446: Disrupts interaction with CTBP1. Decreases lysine acetylation. Disrupts nuclear hormone receptor-dependent transcription repression</li><li>K->R at 446: Does not disrupt nuclear hormone receptor-dependent transcription repression</li><li>NL->AA at 567-568: Disrupts transcriptional repression</li><li>NL->AS at 567-568: Disrupts interaction with CTBP1 and CTBP2. Disrupts transcriptional repression; when associated with 442-AS-443</li><li>SMDLT->PIAAS at 599-603: Does not further disrupt transcriptional repression; when associated with 442-AA-443 and 567-AA-568</li><li>DL->AA at 948-949: Abolishes CTBP binding but retains transcriptional repressor activity</li></ul>	transcription	GO:0006350	<li>transcriptional repressor activity</li><li>binding</li>	<li>GO:0016564</li><li>GO:0005488</li>			<li>P56545</li><li>Q13363</li><li>Q61990</li>		1
P48595	5273	<ul><li>KKRK->AAAA at 74-77: Abolishes nuclear localization</li></ul>	localization	GO:0051179							1
P49336	1024	<ul><li>D->A at 173: Abrogates kinase activity and TFIIH-dependent transcriptional repression</li></ul>			kinase activity	GO:0016301					1
P49354	2339	<ul><li>K->N at 164: Reduced activity</li><li>N->K at 199: Reduced catalytic efficiency</li></ul>									1
P49356	2342	<ul><li>D->N at 200: Reduced catalytic efficiency</li><li>G->V at 249: Reduced catalytic efficiency</li><li>G->S at 349: Reduced catalytic efficiency</li></ul>									1
P49366	1725	<ul><li>N->A at 106: Strongly reduced NAD and spermidine binding. Reduced activity</li><li>S->A at 109: Strongly reduced spermidine binding. Reduced activity</li><li>E->A at 137: Strongly reduced NAD binding. Strongly reduced formation of covalent intermediate</li><li>D->A at 238: Strongly reduced NAD binding. Strongly reduced formation of covalent intermediate</li><li>D->A at 243: Reduces spermidine binding by 98%. Strongly reduced formation of covalent intermediate</li><li>K->A at 287: Reduces covalent intermediate formation and deoxyhypusine synthesis by 99.5%. Retains low spermidine cleavage activity</li><li>H->A at 288: Reduces spermidine binding by 98%. Strongly reduced NAD binding. Strongly reduced formation of covalent intermediate</li><li>Y->A at 305: Strongly reduced NAD binding. No effect on enzyme activity</li><li>D->A at 313: Strongly reduced NAD binding</li><li>D->A at 316: Reduces spermidine binding by 98%. Loss of covalent intermediate formation and deoxyhypusine synthesis</li><li>S->A at 317: Strongly reduced NAD binding. No effect on enzyme activity</li><li>E->A at 323: Reduces spermidine binding by 98%. Strongly reduced formation of covalent intermediate</li><li>W->A at 327: Reduces spermidine binding by 98%. Loss of covalent intermediate formation and deoxyhypusine synthesis</li><li>K->A,R at 329: Loss of covalent intermediate formation and deoxyhypusine synthesis</li><li>D->A at 342: Strongly reduced NAD binding. Strongly reduced activity</li></ul>			<li>reduced NAD binding</li><li>spermidine binding</li>	<li>GO:0051287</li><li>GO:0019809</li>					1
P49427	997	<ul><li>C->S at 93: Loss of function</li><li>L->S at 97: Loss of function</li><li>S->A at 231: Abolishes phosphorylation by CK2</li></ul>	phosphorylation	GO:0016310					<li>Q65ZV5</li><li>P43893</li><li>O51759</li>		1
P49450	1058	<ul><li>S->A at 7: Induces a delay at the terminal stage of cytokinesis and chromosome misalignment during mitosis due to a defect in kinetochore attachment to microtubules</li></ul>	<li>cytokinesis</li><li>mitosis</li>	<li>GO:0000910</li><li>GO:0007067</li>			<li>chromosome</li><li>microtubules</li><li>kinetochore</li>	<li>GO:0005694</li><li>GO:0005874</li><li>GO:0000776</li>			1
P49662	837	<ul><li>C->S at 258: Loss of activity</li></ul>									1
P49683	2834	<ul><li>Missing at 365-370: Abolishes binding to GRIP1 and PICK1</li><li>T->A at 365: No effect on binding to GRIP1</li><li>V->A at 366: No effect on binding to GRIP1</li><li>S->A at 367: Abolishes binding to GRIP1</li><li>V->A at 368: Abolishes binding to GRIP1</li><li>V->A at 369: No effect on binding to GRIP1</li><li>I->A at 370: Abolishes binding to GRIP1</li></ul>			binding	GO:0005488			<li>Q9Y3R0</li><li>Q9NRD5</li><li>Q96DT0</li>		1
P49716	1052	<ul><li>K->A at 120: Loss of sumoylation</li></ul>	sumoylation	GO:0016925							1
P49736	4171	<ul><li>S->A at 108: Reduces phosphorylation by ATR</li></ul>	phosphorylation	GO:0016310					<li>Q13535</li><li>Q9H6X2</li><li>Q9FKS4</li><li>P20848</li>		1
P49758	9628	<ul><li>D->A at 297: Loss of interaction with Gbeta5</li><li>W->F at 309: Diminishes interaction with Gbeta5</li></ul>							<li>O14775</li><li>Q6PNB6</li><li>P62881</li><li>Q5RDY7</li><li>Q80ZD0</li><li>P62882</li>		1
P49767	7424	<ul><li>R->S at 227: No proteolytic processing and lower effect on VEGFR-2 and VEGFR-3</li></ul>							<li>P35968</li><li>Q8AXB3</li><li>P52583</li><li>Q91ZT1</li><li>P79701</li><li>P35917</li><li>P35916</li><li>O08775</li><li>P35918</li><li>Q5MD89</li>		1
P49768	5663	<ul><li>Missing at 66-72: No effect on interaction with GFAP</li><li>KY->AA at 76-77: No effect on interaction with GFAP</li><li>VI->EE at 82-83: Loss of interaction with GFAP</li><li>V->K,E at 82: Loss of interaction with GFAP</li><li>ML->EE at 84-85: Loss of interaction with GFAP</li><li>Y->F at 256: Alters gamma-secretase cleavage specificity. Increased production of amyloid beta(42). No effect on enzymatic activity</li><li>D->A at 257: Loss of endoproteolytic cleavage; reduces production of amyloid beta in APP processing and of NICD in NOTCH1 processing</li><li>D->E at 257: Abolishes gamma-secretase activity. Reduces production of amyloid beta in APP processing. Accumulation of full-length PS1. Loss of binding of transition state analog gamma-secretase inhibitor</li><li>L->A,E,P,Q,R,W at 286: Increases production of amyloid beta in APP processing</li><li>L->E,R at 286: Reduces production of NICD in NOTCH1 processing</li><li>M->D at 292: Loss of endoproteolytic cleavage</li><li>S->A at 310: Abolishes PKA-mediated phosphorylation; no effect on caspase-mediated cleavage</li><li>D->N at 345: Abolishes caspase cleavage</li><li>S->A at 346: Abolishes PKC-mediated phosphorylation; no effect on PKA-mediated phosphorylation</li><li>S->E at 346: Inhibits caspase-mediated cleavage. Modulates progression of apoptosis</li><li>D->N at 373: No effect on caspase cleavage</li><li>D->A at 385: Loss of endoproteolytic cleavage. Reduces production of amyloid beta in APP processing. Disassembly of the N-cadherin/PS1 complex at the cell surface. Impairs CDH2 processing</li><li>D->E at 385: Abolishes gamma-secretase activity. Reduces production of amyloid beta in APP processing. Accumulation of full-length PS1. Loss of binding of transition state analog gamma-secretase inhibitor</li><li>D->N at 385: No effect on caspase cleavage</li><li>Y->F at 389: Alters gamma-secretase cleavage specificity. Increased production of amyloid beta(42). No effect on enzymatic activity</li><li>P->A at 433: No effect on endoproteolytic cleavage. No effect on APP nor NOTCH1 processing. Slightly increased Abeta42/Abeta40 ratio</li><li>P->D,F,L,N,V at 433: No endoproteolytic cleavage; no APP nor NOTCH1 processing. No detectable Abetano detectable Abeta</li><li>P->G at 433: Very little endoproteolysis. Little APP processing. No NOTCH1 processing. Very low levels Abeta40 and no detectable Abeta42</li><li>A->C at 434: Some loss of endoproteolytic cleavage. Some loss of APP and NOTCH1 processing. Six-fold increase in Abeta42/Abeta40 ratio</li><li>A->D,I,L,V at 434: No endoproteolytic cleavage. No APP nor NOTCH1 processing. No detectable Abeta</li><li>A->G at 434: No effect on endoproteolytic cleavage. No effect on APP nor NOTCH1 processing. Reduced Abeta42/Abeta40 ratio</li><li>L->A at 435: No effect on endoproteolytic cleavage. No effect on APP processing. Impaired NOTCH1 processing. Greatly reduced Abeta42/Abeta40 ratio</li><li>L->F at 435: No endoproteolytic cleavage. No APP nor NOTCH1 processing. No detectable Abeta</li><li>L->G at 435: Greatly reduced endoproteolytic cleavage. Very little APP and NOTCH1 processing. Very low levels of Abeta40 and no detectable Abeta42</li><li>L->I at 435: No effect on endoproteolytic cleavage. No effect on APP nor NOTCH1 processing</li><li>L->V at 435: No effect on endoproteolytic cleavage. No effect on APP processing. Impaired NOTCH1 processing. Some increase in Abeta42/Abeta40 ratio</li></ul>	<li>phosphorylation</li><li>apoptosis</li>	<li>GO:0016310</li><li>GO:0006915</li>	<li>binding</li><li>PKA</li>	<li>GO:0005488</li><li>GO:0004691</li>	cell surface	GO:0009928,GO:0009986	<li>Q60495</li><li>P0A3Z4</li><li>P0A3Z2</li><li>O73683</li><li>Q28280</li><li>P0A3Z3</li><li>P19022</li><li>P49768</li><li>P0A3Z1</li><li>Q28757</li><li>P29216</li><li>P46531</li><li>P34722</li><li>P12023</li><li>Q11207</li><li>P47819</li><li>P53601</li><li>Q29149</li><li>Q5R9X1</li><li>Q9W6T7</li><li>P75313</li><li>P08592</li><li>P79307</li><li>P05067</li><li>Q28748</li><li>P79802</li><li>Q28053</li><li>Q5IS80</li><li>P10288</li><li>P13678</li><li>P47566</li><li>P13677</li><li>P05130</li><li>O93279</li><li>P03995</li><li>P19534</li><li>P14136</li><li>Q28115</li><li>Q95241</li><li>O55075</li><li>Q8HXW5</li>		1
P49789	2272	<ul><li>H->N at 35: 50% decrease in catalytic activity. No loss in substrate binding</li><li>H->N at 94: 75% decrease in catalytic activity. No loss in substrate binding</li><li>H->G at 96: Total loss of catalytic activity. Rescuable with free imidazole</li><li>H->N at 96: Total loss of catalytic activity. No loss in substrate binding</li><li>H->N at 98: 99% decrease in catalytic activity. No loss in substrate binding</li><li>Y->F at 114: Loss of phosphorylation by SRC</li><li>Y->F at 145: No affect on phosphorylation by SRC</li></ul>	phosphorylation	GO:0016310	<li>binding</li><li>catalytic activity</li>	<li>GO:0005488</li><li>GO:0003824</li>			<li>P00523</li><li>P12931</li>		1
P49792	5903	<ul><li>V->K at 2632: Abolishes interaction with sumoylated RANGAP1</li><li>I->K at 2634: Abolishes interaction with sumoylated RANGAP1</li><li>V->K at 2635: Abolishes interaction with sumoylated RANGAP1</li><li>P->A at 2640: No effect on SUMO E3 ligase activity</li><li>K->A at 2645: No effect on SUMO E3 ligase activity</li><li>L->A at 2651: Abolishes binding to UBE2I and SUMO E3 ligase activity</li><li>K->A at 2652: No effect on SUMO E3 ligase activity</li><li>L->A at 2653: Abolishes binding to UBE2I and SUMO E3 ligase activity</li><li>P->A at 2654: Impairs SUMO E3 ligase activity</li><li>P->A at 2655: No effect on SUMO E3 ligase activity</li><li>T->A at 2656: Impairs SUMO E3 ligase activity</li><li>F->A at 2657: Abolishes binding to UBE2I and SUMO E3 ligase activity</li><li>F->A at 2658: Abolishes binding to UBE2I and SUMO E3 ligase activity</li><li>C->S,A at 2659: Impairs SUMO E3 ligase activity</li><li>D->A at 2676: Impairs SUMO E3 ligase activity</li><li>F->A at 2677: Impairs SUMO E3 ligase activity</li><li>Y->A at 2689: Impairs SUMO E3 ligase activity</li></ul>			<li>binding</li><li>ligase activity</li>	<li>GO:0005488</li><li>GO:0016874</li>			<li>Q2EF73</li><li>P63283</li><li>O09181</li><li>P46060</li><li>P63279</li>		1
P49795	10287	<ul><li>S->A at 151: Diminishes gap activity towards G(i)-alpha3 and autophagy in colon cancer cells</li></ul>	autophagy	GO:0006914					<li>P08754</li><li>Q9DC51</li><li>P08753</li><li>P38403</li><li>P27045</li><li>Q60397</li>		1
P49802	6000	<ul><li>W->F at 306: Diminishes interaction with Gbeta5</li></ul>							<li>O14775</li><li>Q6PNB6</li><li>P62881</li><li>Q5RDY7</li><li>Q80ZD0</li><li>P62882</li>		1
P49810	5664	<ul><li>D->A at 263: Reduces production of amyloid beta in APP processing</li><li>D->A at 366: Reduces production of amyloid beta in APP processing and of NICD in NOTCH1 processing</li></ul>							<li>Q60495</li><li>P0A3Z4</li><li>Q28280</li><li>O73683</li><li>P0A3Z2</li><li>P75313</li><li>P79307</li><li>P08592</li><li>P0A3Z3</li><li>P0A3Z1</li><li>Q28757</li><li>P05067</li><li>Q28748</li><li>P29216</li><li>Q28053</li><li>Q5IS80</li><li>P46531</li><li>P47566</li><li>O93279</li><li>Q11207</li><li>P12023</li><li>Q95241</li><li>P53601</li><li>Q29149</li>		1
P49841	2932	<ul><li>S->A at 9: Loss of phosphorylation; insensitive to inhibitory phosphorylation</li></ul>	phosphorylation	GO:0016310							1
P49842	8859	<ul><li>K->P at 300: Partial loss of activity</li><li>K->P at 315: Partial loss of activity</li><li>K->P at 317: Complete loss of activity</li></ul>									1
P49888	6783	<ul><li>S->A at 137: Decreased gradually the catalytic activity</li><li>S->C at 137: Decreased gradually the catalytic activity</li><li>V->E at 269: Does not prevent the formation of homodimer</li></ul>			catalytic activity	GO:0003824					1
P49903	22929	<ul><li>G->C at 268: No change in ATP-binding</li><li>G->R at 270: No change in ATP-binding</li><li>G->A,D,V at 273: Loss of ATP-binding</li><li>H->N at 274: Reduced ATP-binding</li><li>H->Y at 274: Increased ATP-binding</li></ul>			ATP-binding	GO:0005524					1
P50225	6817	<ul><li>C->S at 70: Increased sensitivity of enzyme activity to heat inactivation</li></ul>									1
P50402	2010	<ul><li>S->A at 49: Abolishes phosphorylation. No effect on targeting to nuclear envelope nor on interaction with LMNA</li><li>S->E at 49: Mimics phosphorylation. No effect on targeting to nuclear envelope nor on interaction with LMNA</li></ul>	phosphorylation	GO:0016310			nuclear envelope	GO:0005635	<li>P02545</li><li>Q3ZD69</li><li>P13648</li>		1
P50542	5830	<ul><li>W->A at 118: Strongly reduced interaction with PEX14</li><li>F->A at 122: Strongly reduced interaction with PEX14</li></ul>							<li>Q9HG09</li><li>P78723</li><li>P53112</li><li>O75381</li>		1
P50548	2077	<ul><li>T->A at 526: Loss of a phosphorylation site</li></ul>	phosphorylation	GO:0016310							1
P50552	7408	<ul><li>F->A at 370: Lower stability of tetramerization domain</li><li>F->I,K at 370: No change in stability of tetramerization domain</li></ul>									1
P50613	1022	<ul><li>K->A at 41: Total loss of activity</li><li>S->A at 164: No mitotic repression of transcriptional activity of the reconstituted TFIIH complex</li><li>T->A at 170: Total loss of activity. Total loss of transcriptional activity of the reconstituted TFIIH complex</li></ul>									1
P50750	1025	<ul><li>D->N at 167: Abrogates kinase activity</li><li>T->A at 186: Abrogates autophosphorylation; no effect on kinase activity</li></ul>	autophosphorylation	GO:0046777	kinase activity	GO:0016301					1
P51149	7879	<ul><li>L->A at 8: Abolishes interaction with RAB7 and reduces its localization to late endosomal/lysosomal compartments</li><li>K->A at 10: Abolishes interaction with RAB7 and localization to late endosomal/lysosomal compartments</li><li>T->N at 22: Abolishes localization on late endosomes, lysosomes and phagosomes and reduces phagosomal fusions. Abolishes association of RILP with the phagosomes</li><li>Q->L at 67: Does not abolish localization on late endosomes, lysosomes and phagosomes and does not reduce phagosomal fusions</li><li>V->A at 180: Abolishes interaction with RAB7 and localization to late endosomal/lysosomal compartments</li><li>L->A at 182: Does not abolish interaction with RAB7 and localization to late endosomal/lysosomal compartments. Does not abolish interaction with RAB7 and localization to late endosomal/lysosomal compartments; when associated with A-183</li><li>Y->A at 183: Does not abolish interaction with RAB7 and localization to late endosomal/lysosomal compartments. Does not abolish interaction with RAB7 and localization to late endosomal/lysosomal compartments; when associated with A-182</li></ul>	localization	GO:0051179			<li>phagosomes</li><li>late endosomes</li><li>lysosomes</li>	<li>GO:0045335</li><li>GO:0005770</li><li>GO:0005764</li>	<li>Q3T0F5</li><li>Q96NA2</li><li>Q96MT3</li><li>O04157</li><li>P18067</li><li>O97572</li><li>Q9XER8</li><li>P51149</li><li>Q5R9Y4</li>		1
P51572	10134	<ul><li>D->A at 164: Abolishes cleavage by caspases, inhibits apoptotic membrane blebbing and release of cytochrome c from mitochondria; when associated with A-238</li><li>D->A at 238: Abolishes cleavage by caspases, inhibits apoptotic membrane blebbing and release of cytochrome c from mitochondria; when associated with A-164</li></ul>					membrane	GO:0016020	<li>P00073</li><li>P00074</li><li>P00075</li><li>P00076</li><li>P00070</li><li>P00071</li><li>P00072</li><li>Q6C9Q0</li><li>P00067</li><li>P00066</li><li>P00069</li><li>P00068</li><li>P68100</li><li>P00064</li><li>P00065</li><li>P00062</li><li>P00063</li><li>P00060</li><li>P00061</li><li>P67881</li><li>P67882</li><li>Q6WUX8</li><li>P15451</li><li>Q6QLW4</li><li>P19681</li><li>P00059</li><li>P00058</li><li>P00057</li><li>P68517</li><li>P00056</li><li>P68518</li><li>P68519</li><li>P00055</li><li>P62773</li><li>P62772</li><li>Q7YR71</li><li>Q4HVX7</li><li>P00008</li><li>P00007</li><li>P32556</li><li>P00004</li><li>P00003</li><li>Q640U4</li><li>P00002</li><li>Q753F4</li><li>P99999</li><li>P99998</li><li>Q52V08</li><li>Q52V09</li><li>P00079</li><li>P00078</li><li>P00077</li><li>O13393</li><li>P81459</li><li>P00030</li><li>Q5RFH4</li><li>P00032</li><li>P00031</li><li>Q52V10</li><li>O93863</li><li>P00027</li><li>P00028</li><li>P12831</li><li>P00029</li><li>P68096</li><li>P00022</li><li>P68097</li><li>P68098</li><li>P00024</li><li>P62896</li><li>P68099</li><li>P81280</li><li>P00025</li><li>P62895</li><li>P62894</li><li>Q6Q4H8</li><li>P18822</li><li>P00021</li><li>P00020</li><li>P00017</li><li>P38091</li><li>P00018</li><li>P00013</li><li>P00014</li><li>P00011</li><li>O07091</li><li>P00012</li><li>P53698</li><li>P00019</li><li>O22642</li><li>P25400</li><li>P22342</li><li>P00052</li><li>P00051</li><li>P00054</li><li>P00053</li><li>P00046</li><li>Q96VP3</li><li>P00047</li><li>P00048</li><li>P00049</li><li>Q41346</li><li>P19974</li><li>P21665</li><li>P56205</li><li>P00043</li><li>P00042</li><li>P00041</li><li>Q6IQM2</li><li>P00040</li><li>P00035</li><li>P00036</li><li>P00039</li><li>P00037</li><li>P29380</li><li>P00038</li><li>P59218</li>		1
P51582	5030	<ul><li>S->A at 243: No effect</li><li>Missing at 333-365: Abolishes agonist-induced phosphorylation. Prevents agonist-induced desensitization and loss of cell surface receptors</li><li>SSLALVSLPEDSSCR at 333-359: Greatly reduces agonist-induced desensitization and loss of cell surface receptors</li><li>S->A at 333: Greatly reduces agonist-induced desensitization and loss of cell surface receptors; when associated with A-334 and A-339</li><li>S->A at 334: Greatly reduces agonist-induced desensitization and loss of cell surface receptors; when associated with A-333 and A-339</li><li>S->A at 339: Greatly reduces agonist-induced desensitization and loss of cell surface receptors; when associated with A-333 and A-334</li><li>Missing at 344-365: No effect on agonist-induced phosphorylation, no functional effect</li><li>Missing at 356-365: No functional effect</li></ul>	phosphorylation	GO:0016310			cell surface	GO:0009928,GO:0009986			1
P51610	3054	<ul><li>P->S at 30: Severely reduces VP16-induced complex (VIC) formation, but retains association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells</li><li>P->S at 79: Severely reduces VIC formation, but retains association with VP16. Severely reduces association with CREB3. Unable to rescue proliferation in temperature-sensitive arrested cells</li><li>C->D at 82: Moderately reduces VIC formation and association with VP16 and CREB3. Unable to rescue proliferation in temperature-sensitive arrested cells</li><li>K->D at 105: Minor reduction in VIC formation and association with VP16 and CREB3. Able to rescue proliferation in temperature-sensitive arrested cells</li><li>P->S at 134: Eliminates VIC formation and association with VP16. Weak association with POU2F1. Unable to associate with CREBZF. Unable to rescue proliferation in temperature-sensitive arrested cells</li><li>R->D at 137: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells</li><li>P->S at 197: Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells</li><li>R->D at 200: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells</li><li>R->D at 228: Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells</li><li>P->S at 252: Minor reduction in VIC formation, but retains association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells</li><li>R->D at 255: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells</li><li>EWK->AAA at 289-291: Minor reduction in VIC formation and association with VP16. Weak association with POU2F1. Severely reduces association with CREB3. Able to rescue proliferation in temperature-sensitive arrested cells</li><li>P->S at 319: Eliminates VIC formation and association with VP16. Unable to rescue proliferation in temperature-sensitive arrested cells</li><li>R->D at 322: Eliminates VIC formation. Unable to rescue proliferation in temperature-sensitive arrested cells</li><li>S->A at 338: Moderately reduces association with VP16 and CREB3. Able to rescue proliferation in temperature-sensitive arrested cells</li><li>RK->AA at 344-345: Eliminates VIC formation, but only minor reduction in association with VP16. Unable to associate with POU2F1, but only minor reduction in association with CREB3. Able to rescue proliferation in temperature-sensitive arrested cells</li><li>PCETH->AAAAA at 1017-1021: Reduces and disrupts cleavage at HCF repeat</li><li>V->A at 1072: No effect on cleavage at HCF repeat</li><li>R->A at 1073: No effect on cleavage at HCF repeat</li><li>V->A at 1074: No effect on cleavage at HCF repeat</li><li>C->A at 1075: No effect on cleavage at HCF repeat</li><li>S->A at 1076: No effect on cleavage at HCF repeat</li><li>N->A at 1077: No effect on cleavage at HCF repeat</li><li>P->A at 1078: Inactivates cleavage at HCF repeat</li><li>PCETH->AAAAA at 1079-1083: Reduces and disrupts cleavage at HCF repeat</li><li>P->A at 1079: Inactivates cleavage at HCF repeat</li><li>C->A at 1080: Inactivates cleavage at HCF repeat</li><li>E->A at 1081: Inactivates cleavage at HCF repeat</li><li>E->D at 1081: Inactivates cleavage at HCF repeat</li><li>T->A at 1082: Inactivates cleavage at HCF repeat</li><li>T->F at 1082: Reduces cleavage at HCF repeat</li><li>T->S at 1082: Reduces cleavage at HCF repeat</li><li>H->A at 1083: Reduces cleavage at HCF repeat</li><li>E->A at 1084: No effect on cleavage at HCF repeat</li><li>T->A at 1085: Inactivates cleavage at HCF repeat</li><li>G->A at 1086: No effect on cleavage at HCF repeat</li><li>T->A at 1087: Inactivates cleavage at HCF repeat</li><li>T->A at 1088: Inactivates cleavage at HCF repeat</li><li>N->A at 1089: Reduces cleavage at HCF repeat</li><li>T->A at 1090: Inactivates cleavage at HCF repeat</li><li>T->A at 1092: Inactivates cleavage at HCF repeat</li><li>T->A at 1093: Inactivates cleavage at HCF repeat</li><li>T->A at 1095: Reduces cleavage at HCF repeat</li><li>S->A at 1096: No effect on cleavage at HCF repeat</li><li>N->A at 1097: No effect on cleavage at HCF repeat</li></ul>							<li>Q43358</li><li>Q29076</li><li>P14859</li><li>P22389</li><li>P51611</li><li>P51610</li><li>P68335</li><li>Q8SQ19</li><li>Q28466</li><li>P68336</li><li>P23943</li><li>O43889</li><li>Q9NFL5</li><li>P15143</li><li>Q61191</li>		1
P51617	3654	<ul><li>K->S at 239: Loss of kinase activity</li></ul>			kinase activity	GO:0016301					1
P51681	1234	<ul><li>Y->D at 3: No sulfation and greatly decreased binding CCL4 and CCL5; when associated with D-10; D-14 and D-15. Restored most CCL4 binding; when associated with D-10 and D-15</li><li>Y->F at 3: No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-10; F-14 and F-15</li><li>S->A at 6: No change in glycosylation status and greatly decreased CCL4 binding. Loss of molecular mass of about 2 kDa as compared to wild type. Dramatically reduced binding of CCL4; when associated with A-7; A-16; A-17. Similar molecular mass loss. Dramatically reduced binding of CCL4; when associated with A-7 only</li><li>S->A at 7: No change in glycosylation status and binds CCL4 as efficiently as wild type. Loss of molecular mass of about 2 kDa as compared to wild type. Dramatically reduced binding of CCL4; when associated with A-6; A-16; A-17. Similar molecular mass loss. Dramatically reduced binding of CCL4; when associated with A-6 only</li><li>Y->F at 10: No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-3; F-14 and F-15. Small loss of sulfation; when associated with F-14 and F-15</li><li>Y->D at 14: No sulfation and greatly decreased binding CCL4 and CCL5; when associated with D-3; D-10 and D-14. No restoration of CCL4 binding; when associated with D-10 and D-15</li><li>Y->F at 14: No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-3; F-10; and F-15. Small loss of sulfation; when associated with F-10 and F-15</li><li>Y->D at 15: No sulfation and greatly decreased binding CCL4 and CCL5; when associated with D-3; D-10 and D-14. Restored most CCL4 binding; when associated with D-3 and D-10</li><li>Y->F at 15: No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-3; F-10 and F-14. Small loss of sulfation; when associated with F-10 and F-14</li><li>T->A at 16: Similar decrease in molecular mass when treated with O-glycosidase as for wild type; when associated with A-17</li><li>S->A at 17: Similar decrease in molecular mass when treated with O-glycosidase as for wild type; when associated with A-16</li><li>C->A at 321: Small reduction in palmitoylation. Cell surface expression reduced by 50%. Greatly reduced palmitoylation. Cell surface expression greatly reduced; when associated with A-323 or A-324. No palmitoylation. Cell surface expression greatly reduced. HIV entry reduced by 50%; when associated with A-323 and A-324</li><li>C->A at 323: Small reduction in palmitoylation. Cell surface expression reduced by 50%. Greatly reduced palmitoylation. Cell surface expression greatly reduced; when associated with A-321 or A-324. No palmitoylation. Cell surface expression greatly reduced. HIV entry reduced by 50%; when associated with A-321 and A-324</li><li>C->A at 324: Small reduction in palmitoylation. Cell surface expression reduced by 50%. Greatly reduced palmitoylation. Cell surface expression greatly reduced; when associated with A-321 or A-323. No palmitoylation. Cell surface expression greatly reduced. HIV entry reduced by 50%; when associated with A-321 and A-323</li><li>S->A at 336: APO-RANTES-stimulated phosphorylation reduced by 15%; APO-RANTES-stimulated phosphorylation reduced by 30-50%; when associated with A-337 or A-342 or A-349; APO-RANTES-stimulated phosphorylation reduced by 80%; when associated with A-337 and A-342 or A-349; No APO-RANTES-stimulated phosphorylation; when associated with A-337; A-342 and A349</li><li>S->A at 337: APO-RANTES-stimulated phosphorylation reduced by 18%; APO-RANTES-stimulated phosphorylation reduced by 30-50% on APO-RANTES stimulation; when associated with A-336 or A-342 or A-349; APO-RANTES-stimulated phosphorylation reduced by 80%; when associated with A-336 and A-342 or A-349; No APO-RANTES-stimulated phosphorylation; when associated with A-336; A-342 and A349</li><li>S->A at 342: APO-RANTES-stimulated phosphorylation reduced by 42%. Phosphorylation reduced by 50% on APO-RANTES stimulation; when associated with A-336 or A-337 or A-349; APO-RANTES-stimulated phosphorylation reduced by 80% when associated with A-336 and A-337 or A-349; No APO-RANTES-stimulated phosphorylation; when associated with A-336; A-337 and A349</li><li>S->A at 349: APO-RANTES-stimulated phosphorylation reduced by 43%; APO-RANTES-stimulated phosphorylation reduced by 30-50%; when associated with A-336 or A-337 or A-342; APO-RANTES-stimulated phosphorylation reduced by 80%; when associated with A-336 and A-337 or A-342; No APO-RANTES-stimulated phosphorylation stimulation; when associated with A-336; A-337 and A347</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488	Cell surface	GO:0009928,GO:0009986	<li>Q90826</li><li>P13501</li><li>Q8N6M6</li><li>Q8BXQ6</li><li>P13236</li><li>Q8MKD0</li><li>O97919</li><li>Q91ZL1</li><li>P97272</li><li>P50231</li><li>P50230</li><li>Q29288</li><li>Q8SQ40</li><li>P69527</li><li>P14097</li><li>Q8HYQ1</li><li>Q8HYS0</li><li>P30882</li><li>P46632</li>		1
P51787	3784	<ul><li>G->M at 589: No effect</li><li>A->W at 590: Reduced cell surface expression and strongly reduced potassium current</li><li>N->G at 593: Reduced cell surface expression and moderately reduced potassium current</li></ul>					cell surface	GO:0009928,GO:0009986			1
P51790	1182	<ul><li>G->E at 280: Changes channel selectivity from I(-)>Cl(-) to Cl(-)>I(-)</li></ul>									1
P51795	1184	<ul><li>Y->A at 672: Abolishes interaction with NEDD4 and NEDD4L</li></ul>							<li>Q5RBF2</li><li>Q96PU5</li><li>P46934</li>		1
P51811	7504	<ul><li>C->S at 347: Loss of Kell-XK complex</li></ul>									1
P51843	190	<ul><li>ML->AA at 16-17: Strongly reduces homodimodimerization and interaction with NR0B2</li><li>ML->AA at 83-84: Strongly reduces homodimodimerization and interaction with NR0B2</li><li>LL->AA at 149-150: Strongly reduces homodimodimerization and interaction with NR0B2</li><li>MM->AA at 461-462: Strongly reduces homodimodimerization and interaction with NR0B2</li></ul>							Q15466		1
P51857	6718	<ul><li>Y->A at 58: Loss of activity</li><li>E->A at 120: Loss of activity</li></ul>									1
P51946	902	<ul><li>S->A at 5: No effect on the transcriptional activity of the reconstituted TFIIH complex</li><li>S->A at 304: No effect on the transcriptional activity of the reconstituted TFIIH complex</li></ul>									1
P51955	4751	<ul><li>K->R at 37: Loss of kinase activity and of ability to activate NEK11</li><li>D->A at 141: Loss of autophosphorylation</li><li>T->A at 170: No effect on kinase activity</li><li>T->E at 170: Kinase activity increased by two fold</li><li>S->A at 171: No effect on kinase activity</li><li>S->D at 171: Kinase activity increased by two fold</li><li>T->A at 175: Kinase activity decreased by two fold</li><li>T->E at 175: Kinase activity increased by two fold</li><li>T->A at 179: Loss of kinase activity</li><li>T->E at 179: Loss of kinase activity</li><li>S->A at 241: Loss of kinase activity</li><li>S->D at 241: Loss of kinase activity</li></ul>	autophosphorylation	GO:0046777	kinase activity	GO:0016301			<li>Q8NG66</li><li>Q8WNU8</li>		1
P52564	5608	<ul><li>S->A at 207: Inactivation</li><li>S->E at 207: Constitutive activation according to PubMed</li><li>T->A at 211: Inactivation</li><li>T->E at 211: Constitutive activation according to PubMed</li></ul>									1
P52630	6773	<ul><li>R->A at 374: Prevents the nuclear import; when associated with A-375</li><li>K->A at 375: Prevents the nuclear import; when associated with A-374</li><li>R->A at 409: Prevents the nuclear import; when associated with A-415</li><li>K->A at 415: Prevents the nuclear import; when associated with A-409</li></ul>	nuclear import	GO:0051170							1
P52655	2957	<ul><li>V->A at 270: Slightly affects cleavage and yields elevated levels of the precursor</li><li>Q->A at 272: Abolishes cleavage</li><li>V->A at 273: Abolishes cleavage</li><li>D->A at 274: Abolishes cleavage</li><li>G->A at 275: Abolishes cleavage</li><li>T->A at 276: Does not affect cleavage</li><li>G->A at 277: Does not affect cleavage</li><li>D->A at 278: Significant reduction of cleavage</li><li>S->A at 280: Slightly affects cleavage, yields elevated levels of the precursor. Eliminates phosphorylation; when associated with A-281; A-316 and A-321</li><li>S->A at 281: Eliminates phosphorylation; when associated with A-280; A-316 and A-321</li><li>E->A at 282: Slightly affects cleavage and yields elevated levels of the precursor</li><li>S->A at 316: Strongly reduces phosphorylation; when associated with A-321. Eliminates phosphorylation; when associated with A-280; A-281 and A-321</li><li>S->A at 321: Strongly reduces phosphorylation; when associated with A-316. Eliminates phosphorylation; when associated with A-280; A-281 and A-316</li></ul>	phosphorylation	GO:0016310							1
P52701	2956	<ul><li>K->R at 1140: No effect on mismatch binding, complete loss of DNA repair function when associated with MSH2 mutant R-675</li></ul>	DNA repair	GO:0006281	binding	GO:0005488			<li>Q5XXB5</li><li>P25847</li><li>O24617</li><li>P43246</li><li>Q3MHE4</li>		1
P52732	3832	<ul><li>T->A at 926: No mitotic phosphorylation. No binding to spindle apparatus</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488	spindle	GO:0005819			1
P52788	6611	<ul><li>D->A,N at 201: 100,000-fold decrease in catalytic efficiency</li><li>D->N at 276: 200,000-fold decrease in catalytic efficiency</li><li>E->Q at 353: 800-fold decrease in catalytic efficiency</li></ul>									1
P52799	1948	<ul><li>LW->YM at 121-122: Complete loss of Nipah protein G binding</li></ul>			binding	GO:0005488			<li>P62555</li><li>P62554</li>		1
P52848	3340	<ul><li>K->A at 614: Loss of sulfotransferase activity</li></ul>			sulfotransferase activity	GO:0008146					1
P53350	5347	<ul><li>K->M at 82: Abolishes activity</li><li>S->A at 137: No change in activity</li><li>S->D at 137: Increases activity. Results in a block in G1/S</li><li>D->N at 194: Abolishes activity</li><li>D->R at 194: Abolishes activity</li><li>E->D at 206: No change in activity</li><li>E->V at 206: Decreases activity</li><li>T->D at 210: Increases activity</li><li>T->E at 210: Slightly increases activity</li><li>T->V at 210: Abolishes activity</li></ul>									1
P53355	1612	<ul><li>K->A at 42: Loss of activity, apoptotic function and of autophosphorylation</li><li>S->A at 308: Elevated Ca(2+)-calmodulin binding and Ca(2+)-calmodulin-independent kinase activity. Increases apoptotic activity</li><li>S->D at 308: Reduced Ca(2+)-calmodulin binding and Ca(2+)-calmodulin-independent kinase activity. Decreases apoptotic activity</li><li>S->A at 313: Minimal effect on activity</li></ul>	autophosphorylation	GO:0046777	<li>kinase activity</li><li>binding</li>	<li>GO:0016301</li><li>GO:0005488</li>			<li>Q40302</li><li>Q8STF0</li><li>P04353</li><li>P41040</li><li>P04352</li><li>Q9GRJ1</li><li>P61860</li><li>P02594</li><li>P02595</li><li>P61861</li><li>P48976</li><li>O82018</li><li>P93171</li><li>P62184</li><li>P62144</li><li>P62145</li><li>Q5RAD2</li><li>P07463</li><li>P24044</li><li>P11121</li><li>P62149</li><li>P06787</li><li>O02367</li><li>Q6IT78</li><li>P05935</li><li>P05933</li><li>O16305</li><li>Q6PI52</li><li>P05934</li><li>Q6YNX6</li><li>Q7Y052</li><li>Q95NR9</li><li>P11118</li><li>P62157</li><li>P62156</li><li>P21251</li><li>P62155</li><li>Q5EHV7</li><li>P62154</li><li>P62152</li><li>P62151</li><li>Q7T3T2</li><li>P69097</li><li>P69098</li><li>P60206</li><li>Q9U6D3</li><li>Q9HFY6</li><li>P60205</li><li>P62158</li><li>P60204</li><li>O96102</li><li>P62201</li><li>P18061</li><li>P11120</li><li>Q8X187</li><li>P93087</li><li>O60041</li><li>Q05055</li><li>P62204</li><li>P62160</li><li>P62203</li><li>P62202</li><li>P61859</li><li>P17928</li><li>P15094</li><li>Q95NI4</li><li>Q9UWF0</li><li>P62162</li><li>P02598</li><li>P62161</li><li>P02599</li><li>Q71UH6</li><li>Q71UH5</li><li>O97341</li><li>P04464</li><li>P27165</li><li>Q39752</li><li>P84339</li><li>P27166</li><li>P23286</li><li>O94739</li><li>P27161</li><li>P41041</li><li>Q6R520</li>		1
P53667	3984	<ul><li>C->S at 84: Enhances actin aggregation</li><li>GL->EA at 177-178: Enhances actin aggregation</li><li>D->N at 460: Abrogates kinase activity</li><li>Missing at 496-506: Reduces actin aggregation</li><li>RKK->GAA at 503-505: Abolishes kinase activity</li><li>T->A at 508: Abolishes activation by ROCK1</li><li>T->EE at 508: Enhances kinase activity</li><li>T->V,E at 508: Reduces kinase activity</li></ul>			kinase activity	GO:0016301			<li>Q92192</li><li>Q92193</li><li>P53499</li><li>P26183</li><li>P53498</li><li>O13419</li><li>Q9P4D1</li><li>P48465</li><li>P53455</li><li>Q39596</li><li>Q39758</li><li>P26182</li><li>P80709</li><li>Q9UVX4</li><li>O17320</li><li>P53689</li><li>P78711</li><li>P30161</li><li>P17128</li><li>P45521</li><li>P45520</li><li>P20904</li><li>P81085</li><li>Q6TCF2</li><li>Q99023</li><li>Q75D00</li><li>P51775</li><li>P10365</li><li>P60011</li><li>Q8MIT6</li><li>P60010</li><li>Q8SWN8</li><li>O16808</li><li>Q13464</li><li>P02577</li><li>O77819</li><li>P10989</li><li>P68555</li><li>Q05214</li><li>Q8X119</li><li>O65316</li><li>O65315</li><li>O65314</li><li>P61584</li><li>P53491</li><li>P91754</li><li>P13363</li><li>P11426</li><li>O81221</li><li>Q11212</li><li>P50138</li><li>P53477</li><li>P53476</li><li>P60009</li><li>P53502</li><li>Q2U7A3</li><li>P53500</li><li>Q9UVZ8</li><li>P14235</li><li>O00937</li><li>Q9UVF3</li><li>Q24733</li><li>P90689</li><li>P24902</li><li>O74258</li>		1
P53671	3985	<ul><li>T->E at 505: Increases kinase activity</li><li>T->V at 505: Abolishes cofilin phosphorylation and enhancement of stress fiber formation</li></ul>	phosphorylation	GO:0016310	kinase activity	GO:0016301	stress fiber	GO:0001725	<li>P78929</li><li>Q4I963</li><li>Q6CQ22</li><li>Q759P0</li><li>Q96VU9</li><li>Q6C0Y0</li><li>Q03048</li><li>Q5KJM6</li><li>Q4P6E9</li><li>Q9HF97</li><li>Q6FV81</li><li>P54706</li><li>Q6BWX4</li>		1
P53778	6300	<ul><li>D->A at 179: Emulation of the active state</li><li>Y->F at 185: Loss of activity</li><li>F->S at 330: No effect</li></ul>									1
P53999	10923	<ul><li>K->G at 68: Reduced ssDNA binding</li><li>R->G at 75: Reduced ssDNA binding</li><li>FKGK->AGG at 77-80: Loss of ssDNA binding</li><li>R->G at 86: Loss of ssDNA binding</li><li>K->G at 101: Loss of ssDNA binding</li></ul>			binding	GO:0005488					1
P54198	7290	<ul><li>Missing at 449-458: Impairs binding to ASF1A</li><li>RRR->AKK at 458-460: Abrogates binding to ASF1A</li><li>RRR->KKK at 458-460: Impairs binding to ASF1A</li><li>RR->AK at 458-459: Impairs binding to ASF1A</li><li>R->A at 458: Impairs binding to ASF1A</li><li>R->K at 458: Impairs binding to ASF1A; when associated with K-460</li><li>Missing at 459-468: Abrogates binding to ASF1A</li><li>R->A at 459: Abrogates binding to ASF1A</li><li>R->A at 460: Abrogates binding to ASF1A</li><li>R->K at 460: Impairs binding to ASF1A; when associated with K-458</li><li>I->D at 461: Abrogates binding to ASF1A</li><li>L->D at 464: Impairs binding to ASF1A</li><li>I->D at 466: Impairs binding to ASF1A</li><li>T->A at 555: Impairs phosphorylation by CDK2</li><li>KRKL->AAAA at 628-631: Impairs binding to CCNA1 and phosphorylation by CDK2</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488			<li>P48963</li><li>Q5E9Y0</li><li>P43450</li><li>P78396</li><li>P24941</li><li>Q92161</li><li>O55076</li>		1
P54252	4287	<ul><li>C->A at 14: Loss of ubiquitinated protein retention</li><li>S->A at 236: Inhibits substrate trapping</li><li>S->A at 256: Inhibits substrate trapping</li><li>S->A at 347: No effect on ubiquitination</li></ul>	protein retention	GO:0045185							1
P54274	7013	<ul><li>A->D at 74: Abolishes dimerization and telomere binding; when associated with P-75</li><li>A->P at 75: Abolishes dimerization and telomere binding; when associated with D-74</li><li>W->P at 77: Abolishes telomere binding</li><li>F->P at 81: Abolishes telomere binding</li><li>F->P at 90: Diminishes telomere binding</li><li>S->A at 219: Loss of phosphorylation; induction of mitotic entry and apoptosis and increased radiation hypersensitivity of ataxia-telangiectasia cells</li><li>S->D,E at 219: Fails to induce apoptosis and decreases radiation hypersensitivity of ataxia-telangiectasia cells (phospho-mimicking mutants)</li></ul>	<li>phosphorylation</li><li>apoptosis</li>	<li>GO:0016310</li><li>GO:0006915</li>	binding	GO:0005488					1
P54762	2047	<ul><li>Y->F at 928: Disrupts binding with the GRB10 SH2 domain, providing evidence for phosphorylation</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488			<li>Q13322</li><li>P55241</li>		1
P55072	7415	<ul><li>K->A at 524: Impairs catalytic activity of RNF19A toward SOD1 mutant</li></ul>			catalytic activity	GO:0003824			<li>Q9SQL5</li><li>P00445</li><li>P00443</li><li>P00442</li><li>Q8HXQ1</li><li>P00441</li><li>Q8HXQ0</li><li>Q8HXQ3</li><li>Q8HXQ2</li><li>Q8HXQ4</li><li>Q8HXP9</li><li>Q5FB29</li><li>Q711T9</li><li>P33431</li><li>Q751L8</li><li>P80566</li><li>Q96VL0</li><li>Q6CPE2</li><li>P09670</li><li>Q8HXP8</li><li>Q8J0N3</li><li>Q8J0N2</li><li>Q6T3B0</li><li>P60052</li><li>Q52RN5</li><li>Q9C0N4</li><li>O46412</li><li>Q6FWL5</li><li>O42724</li><li>Q7M1R5</li><li>Q8WNN6</li><li>P09212</li><li>P04178</li><li>P93258</li><li>O94178</li><li>Q42684</li><li>Q6C662</li><li>O59924</li>		1
P55157	4547	<ul><li>R->K at 540: No change of activity</li><li>C->S at 878: Loss of activity</li></ul>									1
P55210	840	<ul><li>C->A at 186: No apoptotic activity</li></ul>									1
P55212	839	<ul><li>S->A at 257: Suppression of caspase-6 activation</li></ul>									1
P55265	103	<ul><li>K->R at 418: Abolishes sumoylation</li></ul>	sumoylation	GO:0016925							1
P55316	2290	<ul><li>VP->AA at 388-389: Abolishes interaction with JARID1B</li><li>VP->AA at 394-395: Abolishes interaction with JARID1B</li><li>P->A at 404: Abolishes interaction with JARID1B</li></ul>									1
P55769	4809	<ul><li>G->K at 38: Abolishes completely RNA-binding</li><li>A->F at 57: Abolishes completely RNA-binding</li><li>Y->A at 80: Abolishes 50% of RNA-binding</li><li>Missing at 96-128: Abolishes completely RNA-binding</li></ul>			RNA-binding	GO:0003723					1
P55771	5083	<ul><li>VP->AA at 173-174: Abolishes interaction with JARID1B</li><li>VP->AA at 179-180: Abolishes interaction with JARID1B</li><li>P->A at 189: Abolishes interaction with JARID1B</li></ul>									1
P55854	6612	<ul><li>K->R at 11: Abolishes the formation of poly(SUMO) chains</li></ul>									1
P56279	8115	<ul><li>D->G at 16: Greatly reduced binding to AKT1, AKT2 and AKT3. Abolishes nuclear transport of AKT1</li><li>K->M at 30: Slightly reduced binding to AKT2</li><li>PLT->AAA at 36-38: Unable to homodimerize but has no effect on interaction with AKT1, AKT2 or AKT3</li><li>Q->R at 46: Slightly increased binding to AKT2</li><li>I->V at 74: Greatly reduced binding to AKT2. Abolishes nuclear transport of AKT1</li><li>M->V at 106: Slightly increased binding to AKT2</li></ul>	nuclear transport	GO:0051169	binding	GO:0005488			<li>Q9Y243</li><li>P31751</li><li>Q9Y896</li><li>Q38998</li><li>Q01314</li><li>Q38898</li><li>Q8VYX2</li><li>P31749</li>		1
P56524	9759	<ul><li>S->A at 246: Reduces phosphorylation and its subsequent nuclear export</li><li>S->A at 467: Reduces phosphorylation and its subsequent nuclear export</li><li>K->R at 559: Abolishes sumoylation and reduces the histone deacetylase activity</li><li>S->A at 632: Reduces phosphorylation and its subsequent nuclear export</li><li>H->L at 803: Abolishes histone deacetylase activity</li><li>V->A at 1056: Reduces CaMK-dependent nuclear export</li><li>L->A at 1062: Reduces CaMK-dependent nuclear export</li></ul>	<li>phosphorylation</li><li>sumoylation</li><li>nuclear export</li>	<li>GO:0016310</li><li>GO:0016925</li><li>GO:0051168</li>					O22446		1
P56589	8504	<ul><li>L->P at 125: Abolishes binding to PEX19 without affecting targeting to peroxisomes; when associated with D-134</li><li>N->D at 134: Abolishes binding to PEX19 without affecting targeting to peroxisomes; when associated with P-125</li></ul>			binding	GO:0005488	peroxisomes	GO:0005777	<li>P40855</li><li>Q60415</li><li>Q3SZD1</li><li>Q5R7U2</li><li>Q07418</li>		1
P57059	150094	<ul><li>T->A at 182: Prevents phosphorylation and activation by STK11 complex</li></ul>	phosphorylation	GO:0016310					<li>Q15831</li><li>Q0GGW5</li>		1
P57075	53347	<ul><li>W->A at 317: Loss of interaction with CBL</li></ul>							<li>P18949</li><li>P43623</li><li>P22681</li><li>P53780</li><li>P44527</li><li>P53101</li><li>Q52811</li><li>Q07703</li><li>P0A4K2</li><li>P23256</li><li>P0A4K3</li><li>P06721</li>		1
P58753	114609	<ul><li>P->H at 125: Abolishes NF-kappa-B activation</li></ul>									1
P60484	5728	<ul><li>D->A at 92: 700-fold reduction in phosphatase activity towards PtdIns(3,4,5)P3. Loss of protein phosphatase activity. Unable to inhibit focal adhesion formation</li><li>H->A at 93: 75% reduction in phosphatase activity towards PtdIns(3,4,5)P3. Modest reduction in phosphatase activity towards PtsIns(3,4)P2</li><li>C->A at 124: Loss of protein phosphatase activity. Unable to inhibit focal adhesion formation</li><li>K->M at 125: Reduced phosphatase activity towards PtdIns(3,4,5)P3, PtsIns(3,4)P2 and PtdIns(3)P</li><li>K->M at 128: 85% reduction in phosphatase activity towards PtdIns(3,4,5)P3</li><li>K->R at 128: Does not reduce phosphatase activity towards PtdIns(3,4,5)P3</li><li>R->M at 130: Does not affect the ability to inhibit AKT/PKB activation</li><li>T->A,D at 167: 60% reduction in phosphatase activity towards PtdIns(3,4,5)P3</li><li>Q->A,E at 171: 75% reduction in phosphatase activity towards PtdIns(3,4,5)P3</li><li>KMLKKDK->AAGAAD at 263-269: Reduces the growth suppression activity and cells show anchorage-independent growth. Reduces binding to phospholipid membranes in vitro. Phosphatase activity towards PtdIns(3,4,5)P3 is not affected</li><li>KANKDKANR->AAGA at 327-335: Reduces the growth suppression activity and cells show anchorage-independent growth. Reduces binding to phospholipid membranes in vitro; phosphatase activity towards PtdIns(3,4,5)P3 is not affected</li><li>T->A at 401: Loss of DLG1-binding. No effect on MAGI2- and MAST2-binding</li><li>K->A at 402: No effect on MAGI2-, MAST2- and DLG1-binding</li><li>K->W at 402: Loss of DLG1-, MAGI2-, MAGI3- and MAST2-binding. Decrease of protein stability</li><li>V->A at 403: Loss of DLG1-, MAGI2-, MAGI3-, MAST1-, MAST2- and MAST3-binding</li></ul>	focal adhesion formation	GO:0048041	binding	GO:0005488	membranes	GO:0016020	<li>Q5X1E5</li><li>O60307</li><li>Q7MBF4</li><li>Q88A53</li><li>Q5PC82</li><li>Q9Y2H9</li><li>Q821A6</li><li>Q8INB9</li><li>Q87SK9</li><li>Q9JZ88</li><li>Q5F8K9</li><li>Q9I5V3</li><li>Q63YC3</li><li>Q8Y395</li><li>Q6LV05</li><li>Q9PDL7</li><li>Q5WT58</li><li>Q57JQ5</li><li>Q8P5D4</li><li>P06961</li><li>P45269</li><li>Q6P0Q8</li><li>Q88QU2</li><li>Q60CQ4</li><li>Q8ZI64</li><li>Q5E2K7</li><li>Q8CXX6</li><li>Q12959</li><li>Q7M7K5</li><li>Q7MAZ9</li><li>Q8XBL4</li><li>Q5P3T0</li><li>Q8Z3M9</li><li>Q5ZRX9</li><li>Q9CP21</li><li>Q82U82</li><li>P31750</li><li>Q6FA38</li><li>Q8ZLY4</li><li>P47196</li><li>Q86UL8</li><li>Q01314</li><li>Q62EU1</li><li>Q9JUB2</li><li>Q665U9</li><li>Q9KPC6</li><li>Q8CWL6</li><li>Q8PPG9</li><li>Q7Z460</li><li>Q9L7A3</li><li>Q6D160</li><li>Q87DS9</li><li>Q65Q41</li><li>P31749</li>		1
P60510	5531	<ul><li>E->K at 39: Diminishes interaction with PPP4R4</li><li>E->K at 64: Abolishes interaction with PPP4R4</li><li>N->D at 76: Diminishes interaction with PPP4R4</li><li>R->E at 107: Diminishes interaction with PPP4R4</li><li>E->K at 277: Abolishes interaction with PPP4R4; no effect on interaction with PPP4R1 and PPP4R2</li></ul>							Q8TF05		1
P60953	998	<ul><li>G->V at 12: Constitutively active. Interacts with PARD6 proteins</li><li>T->N at 17: Constitutively inactive. Does not interact with PARD6 proteins</li><li>Q->L at 61: Constitutively active. Interacts with PARD6 proteins</li></ul>									1
P61020	5869	<ul><li>S->N at 34: Constitutively inactivated. Strongly reduces interaction with RIN2</li><li>Q->L at 79: Constitutively active</li></ul>							Q8WYP3		1
P61073	7852	<ul><li>Y->F at 7: Sulfate incorporation greatly reduced; when associated with F-12 and F-21. Moderate reduction in sulfate incorporation; when associated with F-12 and A-18. No sulfate incorporation and binding PDF1alpha greatly reduced; when associated with F-12; A-18 and F-21</li><li>T->A at 8: No effect on sulfate incorporation; when associated with A-9 and A-13</li><li>S->A at 9: No effect on sulfate incorporation; when associated with A-8 and A-13</li><li>N->A at 11: Reduced molecular weight. Enhanced coreceptor activity on R5 HIV-1 isolate Envs. Slight further enhancement of coreceptor activity; when associated with A-13</li><li>Y->F at 12: Sulfate incorporation greatly reduced; when associated with F-7 and F-21. Moderate reduction in sulfate incorporation; when associated with F-7 and A-18. No sulfate incorporation and binding PDF1alpha greatly reduced; when associated with F-7; A-18 and F-21</li><li>T->A at 13: Enhanced coreceptor activity on R5 HIV-1 isolate Envs. No effect on sulfate incorporation; when associated with A-8 and A-9</li><li>S->A at 18: Sulfate incorporation greatly reduced; when associated with F-21. Moderate reduction in sulfate incorporation; when associated with F-7 and F-12. No sulfate incorporation and binding PDF1alpha greatly reduced; when associated with F-7; F-12; and F-21</li><li>Y->F at 21: Sulfate incorporation greatly reduced; when associated with F-7 and F-12. Sulfate incorporation greatly reduced; when associated with A-18. No sulfate incorporation and binding PDF1alpha greatly reduced; when associated with F-7; F-12 and A-18</li><li>N->A at 176: Enhanced coreceptor activity on R5 HIV-1 isolate Envs; when associated with A-11</li></ul>			<li>binding</li><li>coreceptor activity</li>	<li>GO:0005488</li><li>GO:0015026</li>			<li>P24105</li><li>Q9QBZ8</li><li>P15831</li><li>P33498</li><li>Q9QBZ4</li><li>P23422</li><li>P11268</li><li>P18040</li><li>P05877</li><li>P05878</li><li>P05879</li><li>P23423</li><li>P11267</li><li>P08360</li><li>P05880</li><li>P16082</li><li>Q1A243</li><li>P25057</li><li>P05882</li><li>P05881</li><li>P05884</li><li>P05883</li><li>Q9QBZ0</li><li>Q79670</li><li>P22427</li><li>P22428</li><li>P31872</li><li>P22429</li><li>P51520</li><li>Q9QBY2</li><li>P23064</li><li>P19503</li><li>P17281</li><li>Q02076</li><li>Q89607</li><li>Q74126</li><li>P04027</li><li>P16090</li><li>P21436</li><li>Q09SZ7</li><li>Q9WC69</li><li>Q04995</li><li>P27757</li><li>P23073</li><li>P12449</li><li>P19549</li><li>P0C212</li><li>P51515</li><li>Q73372</li><li>P21445</li><li>P51519</li><li>P21444</li><li>P19550</li><li>P21443</li><li>P19551</li><li>P07575</li><li>P19556</li><li>P19557</li><li>P20829</li><li>Q9WC60</li><li>P31819</li><li>P26804</li><li>O12164</li><li>P40932</li><li>P26803</li><li>Q9TTC0</li><li>P05885</li><li>P05886</li><li>P16899</li><li>P22380</li><li>Q04993</li><li>P11306</li><li>P08359</li><li>P08810</li><li>P20888</li><li>P32541</li><li>Q02837</li><li>Q75008</li><li>Q77377</li><li>O91086</li><li>P31789</li><li>P03399</li><li>O70902</li><li>P10259</li><li>O56861</li><li>P17755</li><li>P18799</li><li>P04502</li><li>P31794</li><li>P31796</li><li>P11370</li><li>P31791</li><li>P31626</li><li>P31627</li><li>P31793</li><li>P06445</li><li>P04577</li><li>P15073</li><li>P04578</li><li>Q9IDV2</li><li>P32536</li><li>P04579</li><li>P03388</li><li>P03389</li><li>P20871</li><li>P31621</li><li>P20872</li><li>P04580</li><li>P03396</li><li>P10269</li><li>P03395</li><li>P04582</li><li>P03398</li><li>P18094</li><li>P04581</li><li>P03397</li><li>Q76638</li><li>P03392</li><li>P06752</li><li>P04583</li><li>P03391</li><li>Q03804</li><li>P03394</li><li>P03393</li><li>P06751</li><li>Q0R5Q9</li><li>P35961</li><li>P03390</li><li>P14075</li><li>Q05312</li><li>Q9Q714</li><li>P25506</li><li>P25507</li><li>P14351</li><li>Q1A261</li><li>P27399</li><li>P03379</li><li>P11261</li><li>P03377</li><li>P03378</li><li>P25504</li><li>P25505</li><li>P03383</li><li>Q03816</li><li>Q03817</li><li>P03381</li><li>P03380</li><li>P04624</li><li>P03387</li><li>P03386</li><li>O89292</li><li>P03385</li><li>P03384</li><li>P35954</li><li>P04283</li><li>Q85646</li><li>O41803</li><li>P12492</li><li>Q02282</li><li>P12490</li><li>P12491</li><li>Q70626</li><li>P22430</li><li>Q9QSQ7</li><li>P10403</li><li>P27977</li><li>P03374</li><li>P21415</li><li>P19030</li><li>P03375</li><li>P21412</li><li>P12489</li><li>P12488</li><li>P12487</li>		1
P61081	9040	<ul><li>M->A at 1: No effect on thioester intermediate formation</li><li>L->A at 4: Impairs thioester intermediate formation</li><li>F->A at 5: Strongly impairs thioester intermediate formation</li><li>S->A at 6: Slightly impairs thioester intermediate formation</li><li>L->A at 7: Strongly impairs thioester intermediate formation</li><li>Q->A at 9: Impairs thioester intermediate formation</li><li>Q->A at 10: No effect on thioester intermediate formation</li><li>K->A at 11: No effect on thioester intermediate formation</li><li>K->A at 12: Impairs thioester intermediate formation</li><li>L->A at 32: Strongly impairs thioester intermediate formation</li><li>Q->A at 35: Strongly impairs thioester intermediate formation</li><li>K->A at 36: Strongly impairs thioester intermediate formation</li><li>I->A at 38: Strongly impairs thioester intermediate formation</li><li>N->A at 39: No effect on thioester intermediate formation</li><li>L->A at 41: Strongly impairs thioester intermediate formation</li><li>F->A at 51: Strongly impairs thioester intermediate formation</li><li>D->A at 55: Strongly impairs thioester intermediate formation</li><li>L->A at 57: Strongly impairs thioester intermediate formation</li><li>C->S at 111: Forms a stable complex with NEDD8, which prevents subsequent NEDD8 conjugation to cullins</li></ul>	conjugation	GO:0000746					<li>Q15843</li><li>Q9SHE7</li><li>P0C031</li><li>Q4PLJ0</li><li>P0C030</li><li>P61282</li><li>P0C032</li>		1
P61088	7334	<ul><li>C->A at 87: Impairs interaction with SHPRH</li><li>K->R at 92: No ISGylation</li><li>K->R at 94: No effect on ISGylation</li></ul>									1
P61244	4149	<ul><li>K->Q at 66: Kept nuclear localization. Loss of nuclear localization; when associated with Q-153 and Q-154</li><li>K->R at 66: Loss of acetylation, kept nuclear localization; when associated with R-153 and R-154</li><li>K->Q at 153: Loss of nuclear localization; when associated with Q-66 and Q-154. Kept nuclear localization; when associated with Q-154</li><li>K->R at 153: Loss of acetylation, kept nuclear localization; when associated with R-66 and R-154</li><li>K->Q at 154: Loss of nuclear localization; when associated with Q-66 and Q-153. Kept nuclear localization; when associated with Q-153</li><li>K->R at 154: Loss of acetylation, kept nuclear localization; when associated with R-66 and R-153</li></ul>	localization	GO:0051179							1
P61326	4116	<ul><li>KF->EA at 16-17: Impaired nonsense-mediated decay activity</li><li>KN->DA at 41-42: Complete loss of nonsense-mediated decay activity</li><li>DSE->RSR at 66-68: Slightly reduced nonsense-mediated decay activity</li><li>ED->RK at 72-73: Fully active</li><li>RQE->EQR at 85-87: Fully active</li><li>KCLVF->ECLVA at 130-134: Complete loss of nonsense-mediated decay activity</li><li>L->R at 136: Complete loss of nonsense-mediated decay activity</li></ul>									1
P61586	387	<ul><li>G->V at 14: Causes constitutive activation</li><li>Q->L at 63: Causes constitutive activation</li><li>L->M at 193: Converts geranyl-geranylation to farnesylation; does not prevent the cleavage by yopT</li></ul>							<li>P27475</li><li>O68703</li><li>Q93RN4</li>		1
P61956	6613	<ul><li>K->R at 11: Abolishes the formation of poly(SUMO) chains</li></ul>									1
P61960	51569	<ul><li>G->A at 83: Confers resistance to cleavage</li></ul>									1
P62166	23413	<ul><li>E->T at 81: Reduces calcium binding; when associated with A-117 or A-165. Abolishes calcium binding; when associated with A-117 and A-165</li><li>T->A at 117: Reduces calcium binding; when associated with T-81. Abolishes calcium binding; when associated with T-81 and A-165</li><li>T->A at 165: Reduces calcium binding; when associated with A-117. Abolishes calcium binding; when associated with T-81 and A-117</li></ul>			binding	GO:0005488					1
P62328	7114	<ul><li>K->P at 12: Very weak actin binding; no inhibition of actin polymerization</li><li>S->A at 16: Binds actin 2.5-fold less than wild-type; little change in inhibition of actin polymerization</li><li>S->AS at 16: Very weak actin binding; no inhibition of actin polymerization</li><li>L->A,P at 18: Very weak actin binding; no inhibition of actin polymerization</li></ul>			binding	GO:0005488			<li>Q92192</li><li>Q92193</li><li>P53499</li><li>P26183</li><li>P53498</li><li>P14883</li><li>O13419</li><li>Q9P4D1</li><li>P48465</li><li>P53455</li><li>Q4YU79</li><li>P53456</li><li>Q39596</li><li>Q39758</li><li>P26182</li><li>P80709</li><li>Q03341</li><li>Q9UVX4</li><li>O17320</li><li>P53689</li><li>P78711</li><li>P30161</li><li>P17128</li><li>P27132</li><li>P45521</li><li>P45520</li><li>P20904</li><li>P81085</li><li>Q6TCF2</li><li>Q99023</li><li>Q75D00</li><li>P32392</li><li>P51775</li><li>P10365</li><li>P10984</li><li>P60011</li><li>P60010</li><li>P26197</li><li>Q8SWN8</li><li>O16808</li><li>P30163</li><li>P02577</li><li>Q9Y896</li><li>P30165</li><li>Q7RPB4</li><li>P10989</li><li>P68555</li><li>Q05214</li><li>Q8X119</li><li>O65316</li><li>O65315</li><li>O65314</li><li>P53491</li><li>P53492</li><li>P61157</li><li>P91754</li><li>P42023</li><li>P23344</li><li>P13363</li><li>P11426</li><li>O81221</li><li>Q11212</li><li>P53471</li><li>P50138</li><li>Q9Y707</li><li>P17298</li><li>P53477</li><li>P53476</li><li>P60009</li><li>P53502</li><li>Q2U7A3</li><li>P53500</li><li>Q9UVZ8</li><li>P14235</li><li>O00937</li><li>Q9UVF3</li><li>Q8ILW9</li><li>P92176</li><li>Q24733</li><li>P90689</li><li>P24902</li><li>Q96292</li><li>O74258</li><li>P22132</li><li>O18500</li>		1
P62330	382	<ul><li>G->A at 2: Fails to associate with membranes</li></ul>					membranes	GO:0016020			1
P62487	5436	<ul><li>H->E at 14: Strongly reduces RNA-binding</li><li>E->K at 33: Strongly reduces RNA-binding</li><li>K->E at 41: Strongly reduces RNA-binding</li><li>T->A at 90: Reduces RNA-binding</li><li>N->A at 93: Reduces RNA-binding</li><li>K->E at 94: Reduces RNA-binding</li><li>F->E at 107: Reduces RNA-binding</li><li>S->A at 109: Strongly reduces RNA-binding</li><li>H->E at 111: Strongly reduces RNA-binding</li><li>R->E at 151: Strongly reduces RNA-binding</li><li>D->E at 153: Strongly reduces RNA-binding</li><li>F->A at 158: Strongly reduces RNA-binding</li></ul>			RNA-binding	GO:0003723					1
P62745	388	<ul><li>G->V at 14: No effect on internalization of EGF receptor but decreases trafficking of receptor to the lysosome with associated accumulation in late endosomes</li><li>F->G at 39: Abolishes binding to PKN1 and trafficking of EGF receptor</li><li>C->S at 189: No effect on prenylation. Reduced palmitoylation. Abolishes palmitoylation; when associated with S-192</li><li>C->S at 192: Reduced geranylgeranylation but no effect on farnesylation. Reduced palmitoylation. Abolishes palmitoylation; when associated with S-189</li><li>C->S at 193: Abolishes methylation, palmitoylation and prenylation</li><li>K->L at 194: No effect on palmitoylation or prenylation</li></ul>			binding	GO:0005488	<li>late endosomes</li><li>lysosome</li>	<li>GO:0005770</li><li>GO:0005764</li>	<li>Q9BEA0</li><li>P26224</li><li>P01132</li><li>Q16512</li><li>P01133</li><li>Q95ND4</li><li>Q00968</li><li>P07522</li>		1
P62826	5901	<ul><li>G->V at 19: Blocks DNA replication; when associated with L-69</li><li>Q->L at 69: Blocks DNA replication; when associated with V-19</li></ul>	DNA replication	GO:0006260							1
P62877	9978	<ul><li>C->A at 53: Strong reduction in ligase activity; when associated with A-56</li><li>C->A at 56: Strong reduction in ligase activity; when associated with A-53</li><li>C->A at 75: Strong reduction in ligase activity; when associated with A-77</li><li>H->A at 77: Strong reduction in ligase activity; when associated with A-75</li></ul>			ligase activity	GO:0016874					1
P62917	6132	<ul><li>H->A,G at 209: No incorporation into translating E.coli polysomes; ribosomes assembled normally. Significantly reduced translational activity</li></ul>					<li>ribosomes</li><li>polysomes</li>	<li>GO:0005840</li><li>GO:0005844</li>			1
P62937	5478	<ul><li>W->A at 121: 200-fold decrease of sensitivity to CsA</li><li>W->F at 121: 75-fold decrease of sensitivity to CsA</li></ul>									1
P62993	2885	<ul><li>P->L at 49: Ineffective in DNA synthesis. Abolishes interaction with SHB; when associated with L-206</li><li>G->R at 203: Ineffective in DNA synthesis</li><li>P->L at 206: Abolishes interaction with SHB; when associated with L-49</li></ul>							Q15464		1
P63000	5879	<ul><li>G->V at 12: Constitutively active. Interacts with PARD6 proteins</li><li>T->N at 17: Constitutively inactivated. Abolishes interaction with PARD6 proteins</li><li>F->A at 37: Strongly reduced interaction with PLCB2</li><li>W->A at 56: Strongly reduced interaction with PLCB2</li><li>Q->L at 61: Constitutively active. Interacts with PARD6 proteins</li><li>L->A at 67: Strongly reduced interaction with PLCB2</li><li>L->A at 70: Strongly reduced interaction with PLCB2</li></ul>							Q00722		1
P63010	163	<ul><li>R->E at 879: Strongly reduces interaction with EPN1. Reduces interaction with SNAP91 and clathrin. No effect on EPS15 binding</li><li>Y->V at 888: Strongly reduces interaction with SNAP91, EPN1 and clathrin. No effect on EPS15 binding</li><li>K->Q at 917: Strongly reduces interaction with SNAP91 and clathrin. Reduces interaction with EPN1. No effect on EPS15 binding</li></ul>			binding	GO:0005488			<li>O60641</li><li>P13506</li><li>P42566</li><li>Q9Y6I3</li>		1
P63092	2778	<ul><li>Q->A at 170: Increases GDP release but does not affect receptor-mediated activation</li><li>R->A at 258: Increases GDP release and impairs receptor-mediated activation; markedly elevated intrinsic GTPase rate which will lead to more rapid inactivation</li></ul>									1
P63104	7534	<ul><li>K->E at 49: Loss of interaction with NOXA1</li></ul>									1
P63165	7341	<ul><li>F->A at 36: Abolishes binding to PIAS2</li></ul>			binding	GO:0005488			O75928		1
P63279	7329	<ul><li>RK->AA at 13-14: Impairs binding to SUMO1 and catalytic activity</li><li>RK->AA at 17-18: Impairs binding to SUMO1 and catalytic activity</li><li>F->A at 22: Impairs binding to RANBP2</li><li>V->A at 25: Impairs binding to RANBP2</li><li>V->A at 27: Impairs binding to RANBP2</li><li>E->A at 42: Slightly impairs binding to RANBP2</li><li>K->A at 48: Slightly impairs binding to RANBP2</li><li>E->A at 54: Slightly impairs binding to RANBP2</li><li>L->A at 57: Impairs binding to RANBP2</li><li>K->A at 59: Impairs binding to RANBP2</li><li>R->A at 61: Slightly impairs binding to RANBP2</li><li>N->Q at 85: Impairs catalytic activity</li><li>Y->A at 87: Impairs catalytic activity</li><li>C->S at 93: Loss of enhancement of sumoylation by RWDD3. No effect on RWDD3 protein levels</li><li>DK->AA at 100-101: Impairs catalytic activity</li><li>D->A at 127: Impairs catalytic activity</li><li>D->S at 127: No effect on catalytic activity</li></ul>	sumoylation	GO:0016925	<li>binding</li><li>catalytic activity</li>	<li>GO:0005488</li><li>GO:0003824</li>			<li>Q2EF74</li><li>Q5R6J4</li><li>Q9Y3V2</li><li>Q5E9D1</li><li>P49792</li><li>P55857</li><li>P40517</li><li>P48820</li><li>P63165</li><li>Q9MZD5</li>		1
P67775	5515	<ul><li>L->A at 309: Loss of binding to PP2A B-alpha regulatory subunit</li></ul>			binding	GO:0005488			<li>Q06009</li><li>P23696</li><li>Q9ZSE4</li>		1
P67809	4904	<ul><li>S->A at 102: Loss of phosphorylation by PKB/AKT1. Inhibits translocation to the nucleus and tumor cell growth</li></ul>	phosphorylation	GO:0016310			nucleus	GO:0005634	<li>P31750</li><li>Q8INB9</li><li>Q38998</li><li>P47196</li><li>Q01314</li><li>Q8VYX2</li><li>P31749</li>		1
P78310	1525	<ul><li>VII->AID at 70-72: Abolishes binding to adenovirus type 5</li><li>CC->AA at 259-260: Loss of palmitoylation and altered localization</li><li>Y->A at 318: Affects basolateral localization in airway epithelial cells</li><li>LSRM->AAAA at 345-348: Affects basolateral localization in airway epithelial cells</li></ul>	localization	GO:0051179	binding	GO:0005488					1
P78347	2969	<ul><li>Y->F at 248: Abloishes BTK-mediated transcriptional activation. Abolishes BTK-mediated phosphorylation and impairs BTK-mediated transcriptional activation; when associated with F-398 and F-503</li><li>Y->F at 398: Abolishes BTK-mediated transcriptional activation. Abolishes BTK-mediated phosphorylation and impairs BTK-mediated transcriptional activation; when associated with F-248 and F-503</li><li>Y->F at 460: No change on BTK-mediated transcriptional activation</li><li>Y->F at 503: Impairs BTK-mediated transcriptional activation. Abolishes BTK-mediated phosphorylation and impairs BTK-mediated transcriptional activation; when associated with F-248 and F-398</li></ul>	phosphorylation	GO:0016310					<li>Q06187</li><li>Q8JH64</li>		1
P78348	41	<ul><li>S->A at 478: No effect on phosphorylation</li><li>S->A at 479: Loss of phosphorylation</li></ul>	phosphorylation	GO:0016310							1
P78363	24	<ul><li>G->D at 966: Abolishes basal and retinal-stimulated ATP hydrolysis</li><li>K->M at 969: Abolishes basal and retinal-stimulated ATP hydrolysis</li><li>G->D at 1975: Inhibition of retinal-stimulated ATP hydrolysis</li><li>K->M at 1978: Inhibition of retinal-stimulated ATP hydrolysis</li></ul>	ATP hydrolysis	GO:0006200							1
P78380	4973	<ul><li>KKAK->EEAE at 22-25: Impairs sorting into the cell surface but retains ability to bind oxLDL. Abolishes sorting into the cell surface; when associated with K-69</li><li>E->K at 70: Abolishes sorting into the cell surface; when associated with 22-E--E-25</li><li>C->S at 140: Abolishes homodimerization</li><li>C->S at 144: Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-155; S-172; S-243; S-256 and S-264</li><li>W->A at 150: Abolishes binding to acetylated LDL (AcLDL), probably due to inappropriate homodimerization</li><li>C->S at 155: Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-144; S-172; S-243; S-256 and S-264</li><li>C->S at 172: Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-144; S-155; S-243; S-256 and S-264</li><li>N->Q at 183: Does not affect glycosylation state</li><li>Q->L at 193: Impairs binding to acetylated LDL (AcLDL); when associated with 198-AA-199</li><li>SS->AA at 198-199: Impairs binding to acetylated LDL (AcLDL); when associated with L-193</li><li>R->N at 208: Does not affect subcellular location but displays a strongly reduced affinity for acetylated LDL (AcLDL)</li><li>RN->LL at 209-210: Abolishes binding to acetylated LDL (AcLDL)</li><li>R->N at 209: Does not affect binding to acetylated LDL (AcLDL)</li><li>H->A at 226: No effect</li><li>H->Q at 226: Abolishes binding to acetylated LDL (AcLDL); when associated with N-229 and N-231</li><li>R->N at 229: Does not affect subcellular location but displays a reduced affinity for acetylated LDL (AcLDL). Abolishes binding to acetylated LDL (AcLDL); when associated with Q-226 and N-231</li><li>R->N at 231: Abolishes binding to acetylated LDL (AcLDL). Abolishes binding to AcLDL; when associated with Q-226 and N-229</li><li>SQ->AL at 235-236: Impairs binding to acetylated LDL (AcLDL); when associated with A-240</li><li>S->A at 240: Impairs binding to acetylated LDL (AcLDL); when associated with 235-AL-236</li><li>C->S at 243: Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-144; S-155; S-172; S-256 and S-264</li><li>R->N at 248: Does not affect subcellular location but displays a reduced affinity for acetylated LDL (AcLDL)</li><li>C->S at 256: Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-144; S-155; S-172; S-243 and S-264</li><li>C->S at 264: Abolishes sorting into the cell surface and binding to acetylated LDL (AcLDL) while increasing N-glycosylation; when associated with S-144; S-155; S-172; S-243 and S-256</li><li>Missing at 267-273: Impairs protein folding and transport</li></ul>	<li>protein folding</li><li>transport</li>	<li>GO:0006457</li><li>GO:0006810</li>	binding	GO:0005488	cell surface	GO:0009928,GO:0009986			1
P78527	5591	<ul><li>L->P at 1510: Loss of interaction with C1D</li><li>EL->PD at 1516-1517: Loss of interaction with C1D</li></ul>									1
P78545	1999	<ul><li>RGRP->AAAA at 247-250: No effect on transcriptional repression on KRT4 promoter</li><li>W->A at 315: Partially abrogates repressive effect on the KRT4 promoter; when associated with A-319</li><li>K->A at 319: Partially abrogates repressive effect on the KRT4 promoter; when associated with A-315</li><li>RYYY->AAAA at 334-337: Partially abrogates repressive effect on the KRT4 promoter</li></ul>							P19013		1
P78549	4913	<ul><li>K->Q at 220: Inactivates enzyme</li><li>K->R at 220: 85-fold reduction in activity</li></ul>									1
P80192	4293	<ul><li>K->A at 171: Loss of kinase activity and threonine phosphorylation</li><li>T->A at 304: Reduces threonine phosphorylation. Impairs JNK activation</li><li>T->A at 305: Little effect on threonine phosphorylation. Mildly impairs JNK activation</li><li>S->A at 308: Impairs JNK activation</li><li>T->A at 312: Loss of threonine phosphorylation. Strongly impairs JNK activation</li></ul>	phosphorylation	GO:0016310	kinase activity	GO:0016301			<li>Q966Y3</li><li>P92208</li>		1
P80365	3291	<ul><li>E->K,Q at 115: Abolishes cofactor specificity</li></ul>									1
P83876	10907	<ul><li>C->A at 38: Viable when expressed in S.pombe</li></ul>									1
P83916	10951	<ul><li>I->E at 161: Abolishes homodimer formation and binding to EMSY</li></ul>			binding	GO:0005488			Q7Z589		1
P84022	4088	<ul><li>SSVS->AAVA at 422-425: Does not abolish protein nuclear export</li><li>SSVS->RRVR at 422-425: Diminishes cargo protein export</li></ul>	nuclear export	GO:0051168							1
P98082	1601	<ul><li>SYF->AAA at 684-686: Greatly reduced binding to MYO6</li></ul>			binding	GO:0005488			Q9UM54		1
P98088	4586	<ul><li>W->A at 2122: No binding to mannose-specific lectin. Loss of secretion from the endoplasmic reticulum</li><li>D->A,E at 4302: Abolishes cleavage</li></ul>	secretion	GO:0046903	binding	GO:0005488	endoplasmic reticulum	GO:0005783	P82953		1
P98170	331	<ul><li>Y->G at 75: Loss of interaction with MAP3K7IP1; when associated with G-75</li><li>V->A at 80: Strongly reduced interaction with MAP3K7IP1. Reduced activation of MAP3K7/TAK1. Reduced activation of NF-kappa-B</li><li>V->D at 80: Loss of interaction with MAP3K7IP1. Reduced activation of MAP3K7/TAK1. Strongly reduced activation of NF-kappa-B</li><li>V->E at 86: Loss of dimerization. Reduces activation of NF-kappa-B</li><li>S->A at 87: No effect on dimerization</li><li>S->D,E at 87: Abolishes dimerization. Interferes with ubiquitination</li><li>L->G at 98: Loss of interaction with MAP3K7IP1; when associated with G-75</li><li>L->A at 141: Reduced inhibition of caspase-3</li><li>V->A at 147: Reduced inhibition of caspase-3</li><li>D->A at 148: Abolishes inhibition of caspase-3. Reduced interaction with PRSS25; when associated with S-214</li><li>I->A at 149: Reduced inhibition of caspase-3</li><li>D->A at 151: Reduced inhibition of caspase-3</li><li>L->A at 167: Reduced inhibition of caspase-3</li><li>D->A at 196: Reduced inhibition of caspase-3. May affect protein folding and stability</li><li>D->S at 214: Reduced interaction with PRSS25. Reduced interaction with PRSS25; when associated with A-148</li><li>N->D at 259: Reduced interaction with PRSS25; when associated with S-314</li><li>W->R at 310: Reduced interaction with PRSS25; when associated with S-314</li><li>E->S at 314: Decreased interaction with SMAC and with PRSS25. Decreases interaction with PRSS25; when associated with D-259 or A-310</li><li>C->A,S at 450: Inhibits degradation of active caspase-3</li><li>H->A at 467: Loss of E3 ubiquitin-protein ligase activity</li></ul>	protein folding	GO:0006457					<li>O43464</li><li>O43318</li><li>Q8RSY1</li><li>P49116</li><li>P43565</li><li>Q9NR28</li><li>Q15750</li><li>Q2QCI9</li>		1
P98177	4303	<ul><li>T->A at 32: Abolishes phosphorylation. Protein is located mainly in cytoplasm and shows increased transcriptional activity</li><li>S->A at 197: Abolishes phosphorylation. Protein is located mainly in cytoplasm and shows increased transcriptional activity</li><li>S->A at 262: Abolishes phosphorylation. No effect on cellular location or transcriptional activity</li></ul>	phosphorylation	GO:0016310			cytoplasm	GO:0005737			1
P98187	11283	<ul><li>G->E at 328: No effect on U-44069 and U-51605 hydroxylation. 20</li></ul>									1
Q00403	2959	<ul><li>EWRTFS->AWRTFA at 51-56: Partial loss of HIV-1 Vpr binding</li><li>W->A at 52: Partial loss of HIV-1 Vpr binding</li><li>RT->AA at 53-54: Partial loss of HIV-1 Vpr binding</li><li>F->A at 55: Partial loss of HIV-1 Vpr binding</li></ul>			binding	GO:0005488					1
Q00587	11135	<ul><li>DMISHPLGDFRH->A at 36-47: No binding with CDC42</li></ul>			binding	GO:0005488			<li>Q90694</li><li>O94103</li><li>O14426</li><li>P60953</li><li>Q17031</li><li>P60952</li><li>Q9HF56</li><li>P19073</li>		1
Q00604	4693	<ul><li>C->A at 95: Impairs oligomerization</li></ul>									1
Q00613	3297	<ul><li>K->R at 91: No effect on sumoylation</li><li>T->A at 120: No effect on binding HSE nor on transcriptional activity</li><li>S->A at 121: Increased binding HSE and transcriptional activity. Greatly reduced binding to HSP90AA1. No effect on MAPKAPK2 binding</li><li>S->D at 121: Some inhibition of binding HSE and transcriptional activity. No change in binding HSP90AA1. Inhibits MAPKAPK2 binding</li><li>S->A at 123: No effect on binding HSE nor on transcriptional activity</li><li>T->A at 124: No effect on binding HSE nor on transcriptional activity</li><li>K->R at 126: No effect on sumoylation</li><li>T->A at 142: Reduced promoter activity by about 90%. Almost no transcriptional activity when coexpressed with CK2</li><li>K->R at 150: No effect on sumoylation</li><li>K->R at 162: No effect on sumoylation</li><li>S->A at 230: No phosphorylation. Impaired transcriptional activity. No change in inducible DNA-binding activity</li><li>S->D at 230: Mimics phosphorylation. No effect on transcriptional activity</li><li>S->A at 275: Reduced increase in heat-induced transcriptional activity</li><li>R->A at 296: No effect on repression of transcriptional activity at control temperature</li><li>V->A at 297: Slight effect on repression of transcriptional activity at control temperature</li><li>K->A at 298: Derepression of transcriptional activity at control temperature by 18.5%</li><li>K->R at 298: Abolishes sumoylation. No effect on phosphorylation of S-303 nor of S-307. No effect on binding to HSE nor on transactivation of HSP70</li><li>E->A at 299: No effect on repression of transcriptional activity at control temperature</li><li>E->A at 300: Derepression of transcriptional activity at control temperature by 11%</li><li>S->A at 303: No phosphorylation nor sumoylation. No change in subcellular location to nuclear stress granules. Slight decrease in transcriptional activity on heat treatment. 2.5-fold increase in transcriptional activity on heat treatment; when associated with A-303</li><li>S->D at 303: Mimics phosphorylation. No effect on in vitro sumoylation. Greatly increased transcriptional activity on heat induction. 5-fold derepression of transcriptional activity at control temperature; when associated with A-307</li><li>S->A at 307: No phosphorylation. 5-fold derepression of transcriptional activity at control temperature; when associated with A-303. 1.5% increase in transcriptional activity on heat-treatment. 2.5-fold increase in transcriptional activity on heat treatment; when associated with A-303</li><li>R->A at 309: No effect on repression of transcriptional activity at control temperature</li><li>E->A at 311: No effect on repression of transcriptional activity at control temperature</li><li>S->A at 326: Significant increase in transcriptional activity. No effect on DNA binding nor on nuclear translocation</li><li>S->A at 363: No effect on sumoylation</li><li>K->R at 381: No effect on sumoylation</li><li>T->A at 527: No change in binding HSE nor on transcriptional activity. Decreased binding HSE; when associated with A-529</li><li>S->A at 529: No change in binding HSE nor on transcriptional activity. Decreased binding HSE; when associated with A-527</li></ul>	<li>phosphorylation</li><li>sumoylation</li>	<li>GO:0016310</li><li>GO:0016925</li>	<li>binding</li><li>DNA-binding</li>	<li>GO:0005488</li><li>GO:0003677</li>			<li>P27541</li><li>Q8RB68</li><li>Q73GL7</li><li>P27542</li><li>Q6AMQ3</li><li>Q8DF66</li><li>Q71ZJ7</li><li>P56836</li><li>Q7NAU6</li><li>Q3IUI0</li><li>Q8RH05</li><li>Q6B8V2</li><li>Q92260</li><li>P19993</li><li>Q892R0</li><li>P69377</li><li>Q01100</li><li>Q3Z601</li><li>Q47HK2</li><li>Q9ZAD3</li><li>Q8YE76</li><li>Q39JC8</li><li>Q9HHB9</li><li>P69376</li><li>Q5QXL1</li><li>Q5YNI0</li><li>Q818E9</li><li>P14834</li><li>O83246</li><li>Q49Y22</li><li>P30722</li><li>P16394</li><li>P30721</li><li>P75344</li><li>Q8ZIM7</li><li>Q9ZFC6</li><li>Q74IT6</li><li>P99110</li><li>Q9WYK6</li><li>Q9L7Z1</li><li>Q634M7</li><li>P96133</li><li>Q8D2Q5</li><li>P48205</li><li>P26791</li><li>Q9RY23</li><li>Q9K0N4</li><li>P09189</li><li>Q9HRY2</li><li>Q8KEP3</li><li>P48209</li><li>Q5PAB8</li><li>P46633</li><li>Q8NLY6</li><li>P20442</li><li>Q48E62</li><li>P80462</li><li>Q4A8U5</li><li>Q6F6N3</li><li>Q87RX3</li><li>P28608</li><li>Q07437</li><li>Q87BS8</li><li>Q9HV43</li><li>Q7MN85</li><li>Q74H59</li><li>O96772</li><li>Q89YW6</li><li>O69268</li><li>Q93R27</li><li>Q7VIE3</li><li>P41753</li><li>Q8CP17</li><li>Q7VVY2</li><li>Q7W519</li><li>Q3JP10</li><li>O06942</li><li>Q4JXX6</li><li>O85282</li><li>P91902</li><li>Q6G1F9</li><li>Q6F149</li><li>P50019</li><li>P40918</li><li>Q5WV15</li><li>O87777</li><li>Q92BN8</li><li>Q493S7</li><li>Q91233</li><li>O93866</li><li>P47547</li><li>Q8Z9R1</li><li>Q8K624</li><li>P43893</li><li>Q65U55</li><li>P11503</li><li>Q5H186</li><li>P0A5C0</li><li>P83709</li><li>P11501</li><li>Q01233</li><li>P94317</li><li>Q5FFM4</li><li>Q5UQ49</li><li>Q6D0B7</li><li>P0A6Y9</li><li>P0A6Y8</li><li>Q5M6D1</li><li>Q49539</li><li>Q8EHT7</li><li>Q45551</li><li>Q8PAK9</li><li>O86103</li><li>P50023</li><li>Q67S54</li><li>Q661A3</li><li>Q5X3M7</li><li>Q5NPS6</li><li>Q5M1T8</li><li>Q05981</li><li>O68191</li><li>Q8GH79</li><li>P95334</li><li>P0A3J2</li><li>P0A3J3</li><li>Q4QJW4</li><li>P0A3J0</li><li>P0A3J1</li><li>P0A3J4</li><li>P12795</li><li>Q7N8Y4</li><li>P07900</li><li>P08108</li><li>Q48RR3</li><li>Q7NXI3</li><li>Q9WWG9</li><li>Q9UXR0</li><li>P57870</li><li>Q6L0S7</li><li>P30946</li><li>P80692</li><li>Q6MB26</li><li>P95829</li><li>P59565</li><li>P0A6Z0</li><li>O06430</li><li>Q52701</li><li>Q9GKX7</li><li>Q4L6T0</li><li>P08106</li><li>P29215</li><li>Q64X01</li><li>O87384</li><li>Q3KIA0</li><li>P0A5B9</li><li>P02827</li><li>P41797</li><li>O02705</li><li>P87047</li><li>Q6G554</li><li>P05646</li><li>Q9L7P1</li><li>Q54215</li><li>Q8G6W1</li><li>Q47TI0</li><li>O33522</li><li>Q05647</li><li>P27894</li><li>Q05746</li><li>Q6MT06</li><li>O33528</li><li>P64410</li><li>Q9ZMW4</li><li>P08418</li><li>Q6GGC0</li><li>P0C0C6</li><li>Q84BU4</li><li>Q5HAY1</li><li>P37899</li><li>P49136</li><li>P49137</li><li>Q4KIH1</li><li>Q3APD2</li><li>O52064</li><li>P49139</li><li>Q9JVQ9</li><li>Q8FXX2</li><li>P05456</li><li>P26823</li><li>Q57TP3</li><li>P27094</li><li>P61443</li><li>Q72IK5</li><li>Q68XI2</li><li>Q5HFI0</li><li>Q24789</li><li>Q56235</li><li>Q4UJK7</li><li>Q97BG8</li><li>Q5HNW6</li><li>Q4AAR4</li><li>Q2SSB0</li><li>P61442</li><li>Q37106</li><li>Q4FNP9</li><li>Q3YRR6</li><li>Q5FSL5</li><li>Q5NFG7</li><li>Q6NCY4</li><li>O32464</li><li>Q6AC76</li><li>P29133</li><li>Q02028</li><li>Q9PB05</li><li>P68837</li><li>Q9ZDX9</li><li>Q66ET0</li><li>Q730M1</li><li>Q72DW8</li><li>Q32KA5</li><li>Q3K3T2</li><li>P26413</li><li>P43736</li><li>Q62HD5</li><li>P48720</li><li>Q3IYM7</li><li>Q93GF1</li><li>Q05945</li><li>Q46XI7</li><li>Q57AD7</li><li>Q9ZIV1</li><li>Q9KWS7</li><li>Q5HV33</li><li>Q3BVB8</li><li>Q9PQF2</li><li>Q3J7D8</li><li>Q9XCB1</li><li>P25840</li><li>Q9TLT1</li><li>Q81LS2</li><li>P0C0C5</li><li>Q9KD72</li><li>Q65ZV5</li><li>Q00488</li><li>Q8TQR2</li><li>P94695</li><li>Q05558</li><li>O51759</li><li>Q5PDJ5</li><li>Q326K7</li><li>O05714</li><li>Q7MA35</li><li>Q9ZEJ0</li><li>Q9LCQ5</li><li>Q5F6W5</li><li>O52960</li><li>O32482</li><li>Q8XW40</li><li>Q88VM0</li><li>Q824B2</li><li>Q6NEY9</li><li>Q4FPS9</li><li>Q85FW4</li><li>Q7NDH1</li><li>P49463</li><li>Q65H54</li><li>Q5LWJ6</li><li>Q5LG30</li><li>O05700</li><li>P81875</li><li>Q87WP0</li><li>Q5WHG1</li><li>Q3ZYV1</li><li>Q88DU2</li><li>O69298</li><li>Q92J36</li><li>Q6YPM1</li><li>Q5ZTY3</li><li>Q98QY7</li><li>Q4A658</li><li>Q8EUH7</li><li>P78983</li><li>Q8KML6</li><li>P17804</li><li>Q8CWT3</li><li>Q3Z6P1</li><li>Q56073</li><li>Q5GSE1</li><li>O27351</li><li>Q3SIN4</li><li>Q4UT11</li><li>Q3IC08</li><li>P71331</li><li>Q7VQL4</li><li>Q3AF08</li><li>P55994</li><li>Q95YL7</li><li>O87712</li><li>Q91291</li><li>P11144</li><li>P11143</li><li>Q7UM31</li><li>Q5P1H5</li><li>P11145</li><li>Q73Q16</li><li>Q8FM78</li><li>Q98DD1</li><li>O67118</li><li>Q3KLV7</li><li>Q6HDK7</li><li>Q835R7</li><li>Q46I76</li><li>P17821</li><li>Q00043</li><li>P45554</li><li>P17820</li><li>P81341</li><li>Q4ZNP7</li><li>O34241</li><li>P64407</li><li>Q313S2</li><li>Q8PMB0</li><li>P64409</li><li>P64408</li><li>Q465Y6</li><li>Q9S5A4</li><li>Q76LV2</li><li>Q7WGI4</li><li>Q38W93</li><li>Q6KIH7</li><li>Q5XAD6</li><li>Q8K9Y8</li><li>Q3SW76</li><li>P42374</li><li>Q8EPW4</li><li>Q83MH5</li><li>Q6MNF8</li><li>P42373</li><li>Q6G8Y7</li><li>Q607A5</li><li>Q3A8C2</li><li>Q5KWZ7</li>		1
Q00653	4791	<ul><li>YLL->AAA at 247-249: Two-fold reduction in heterodimerization with RelA</li><li>P->A at 399: No change in cleavage rate or products</li><li>G->A at 404: No change in cleavage rate or products</li><li>A->P at 405: No change in cleavage rate or products</li><li>Q->N at 406: No change in cleavage rate or products</li><li>S->G at 713: Loss of phosphorylation; when associated with A-715 and A-717</li><li>S->A at 715: Loss of phosphorylation; when associated with G-713 and A-717</li><li>S->A at 717: Loss of phosphorylation; when associated with G-713 and A-715</li><li>S->A at 866: Decrease in MAP3K14-induced phosphorylation; no inducible processing occurs; when associated with A-869</li><li>S->A at 870: Decrease in MAP3K14-induced phosphorylation; no inducible processing occurs; when associated with A-865</li></ul>	phosphorylation	GO:0016310					<li>P52560</li><li>O87331</li><li>Q99558</li><li>Q931Q4</li><li>Q99TL8</li><li>Q54089</li><li>Q8CS97</li><li>P0A0E9</li><li>P0AG22</li><li>P44644</li><li>P0AG23</li><li>P0AG20</li><li>Q6G8T5</li><li>P0AG21</li><li>P66015</li><li>O54408</li><li>P66014</li><li>P0A0F0</li><li>Q5HNR8</li><li>O52177</li><li>O85709</li><li>Q49640</li><li>P55133</li><li>Q6GG70</li>		1
Q00722	5330	<ul><li>Q->A at 52: Strongly reduces interaction with RAC1</li></ul>							<li>Q9SSX0</li><li>Q38912</li><li>O04369</li><li>P13362</li><li>P80236</li><li>P62999</li><li>P63000</li><li>P62998</li>		1
Q00987	4193	<ul><li>C->S at 305: No loss of ubiquitin ligase E3 activity</li><li>C->T at 374: No loss of ubiquitin ligase E3 activity</li><li>C->L at 438: No loss of ubiquitin ligase E3 activity</li><li>C->G at 441: Fails to interact with MDM4</li><li>C->A at 449: Loss of ubiquitin ligase E3 activity</li><li>C->S at 449: No substantial decrease of ubiquitin ligase E3 activity</li><li>H->A at 452: Loss of ubiquitin ligase E3 activity</li><li>T->A at 455: Significant decrease of ubiquitin ligase E3 activity</li><li>H->S at 457: Loss of ubiquitin ligase E3 activity</li><li>C->S at 461: Loss of ubiquitin ligase E3 activity</li><li>C->A at 464: Loss of ubiquitin ligase E3 activity, enhances protein stability</li><li>C->G at 475: Loss of ubiquitin ligase E3 activity</li><li>C->R at 478: Fails to interact with MDM4</li><li>C->S at 478: Loss of ubiquitin ligase E3 activity</li></ul>							<li>P69326</li><li>P08565</li><li>P69322</li><li>P69323</li><li>P69324</li><li>P69325</li><li>P68196</li><li>O46543</li><li>P68197</li><li>Q05550</li><li>P68198</li><li>P68199</li><li>P19848</li><li>P42739</li><li>P68195</li><li>Q867C2</li><li>P62991</li><li>P62990</li><li>P61863</li><li>P61864</li><li>P61862</li><li>Q867C4</li><li>Q867C3</li><li>P23398</li><li>P68204</li><li>P84589</li><li>Q865C5</li><li>P42740</li><li>P68201</li><li>Q8MKD1</li><li>P14792</li><li>P63049</li><li>P0C072</li><li>P63051</li><li>O15151</li><li>P69308</li><li>P69309</li><li>P20685</li><li>P15174</li><li>P62976</li><li>P62977</li><li>P62974</li><li>P62975</li><li>P62972</li><li>P13117</li><li>P14624</li><li>P62973</li><li>P46574</li><li>P69310</li><li>P69313</li><li>P69314</li><li>P69311</li><li>P08618</li><li>P69312</li><li>P69317</li><li>P69318</li><li>P69315</li><li>P0C014</li><li>P69316</li><li>P59263</li><li>P69319</li><li>P49634</li><li>P49635</li><li>Q9Y848</li><li>P22589</li><li>P62988</li><li>P62989</li><li>P69321</li><li>P23324</li><li>P69320</li><li>P59669</li>		1
Q01081	7307	<ul><li>W->A at 134: Decreases affinity for UAF2 by 3 orders of magnitude</li></ul>									1
Q01094	1869	<ul><li>Y->C at 411: No retinoblastoma protein binding</li></ul>			protein binding	GO:0005515					1
Q01167	3607	<ul><li>K->A at 258: Decreases DNA-binding to 40%</li><li>K->A at 300: Decreases DNA-binding to 20%</li><li>S->A at 305: Decreases DNA-binding to 70%</li><li>R->A at 307: Abolishes DNA-binding</li><li>K->A at 328: Decreases DNA-binding to 25%</li></ul>			DNA-binding	GO:0003677					1
Q01196	861	<ul><li>R->A at 80: Strongly reduces DNA-binding</li><li>K->A at 83: Strongly reduces DNA-binding</li><li>T->A at 84: No effect on DNA binding</li><li>A->T at 107: Loss of heterodimerization</li><li>G->R at 108: Loss of heterodimerization</li><li>R->A at 135: Strongly reduces DNA-binding</li><li>R->A at 139: Strongly reduces DNA-binding</li><li>R->A at 142: Strongly reduces DNA-binding</li><li>Missing at 145-453: No DNA-binding</li><li>K->A at 167: Reduces DNA-binding</li><li>T->A at 169: Strongly reduces DNA-binding</li><li>D->A at 171: Strongly reduces DNA-binding</li><li>R->A at 174: Strongly reduces DNA-binding</li><li>R->A at 177: Strongly reduces DNA-binding</li></ul>			DNA-binding	GO:0003677					1
Q01581	3157	<ul><li>C->A,S at 129: Loss of activity</li></ul>									1
Q01892	6689	<ul><li>S->A at 144: Reduces interaction with IRF4 and transcriptional activation</li><li>K->G at 242: Abrogates DNA-binding</li></ul>			DNA-binding	GO:0003677			Q15306		1
Q01954	646	<ul><li>S->A at 537: No effect on phosphorylation. Abolishes phosphorylation and induces nuclear restriction; when associated to A-541</li><li>S->D at 537: Reduces phosphorylation and induces partial relocation into the cytoplasm</li><li>S->D at 540: No effect on phosphorylation, no effect on subcellular location</li><li>S->A at 541: Strongly reduces phosphorylation. Abolishes phosphorylation and induces nuclear restriction; when associated to A-537</li><li>S->D at 541: Strongly reduces phosphorylation and induces partial relocation into the cytoplasm</li></ul>	phosphorylation	GO:0016310			cytoplasm	GO:0005737			1
Q02156	5581	<ul><li>K->W at 437: Abolishes activity and S-729 phosphorylation</li><li>T->A at 566: Abolishes phosphorylation by PDK1, and S-729 phosphorylation</li><li>T->E at 566: No effect on S-729 phosphorylation</li><li>T->E at 710: No effect on activity; no effect on S-729 phosphorylation</li><li>S->A at 729: Enhances T-566 dephosphorylation</li></ul>	<li>phosphorylation</li><li>dephosphorylation</li>	<li>GO:0016310</li><li>GO:0016311</li>					<li>Q15118</li><li>O15530</li><li>Q9W0V1</li>		1
Q02410	320	<ul><li>F->V at 608: Diminishes interaction with APP</li></ul>							<li>Q60495</li><li>P0A3Z4</li><li>Q28280</li><li>O73683</li><li>P0A3Z2</li><li>P75313</li><li>P79307</li><li>P08592</li><li>P0A3Z3</li><li>P0A3Z1</li><li>Q28757</li><li>P05067</li><li>Q28748</li><li>P29216</li><li>Q28053</li><li>Q5IS80</li><li>P47566</li><li>O93279</li><li>Q11207</li><li>P12023</li><li>Q95241</li><li>P53601</li><li>Q29149</li>		1
Q02750	5604	<ul><li>K->R at 97: Inactivation</li><li>S->A at 150: No loss of activity</li><li>S->A at 212: No loss of activity</li><li>S->A at 218: Inactivation</li><li>S->A at 222: Inactivation</li></ul>									1
Q02809	5351	<ul><li>C->A at 369: Loss of activity</li></ul>									1
Q02928	1579	<ul><li>G->S at 130: Loss of activity</li><li>E->A at 321: Loss of covalent heme binding</li></ul>			heme binding	GO:0020037					1
Q03393	5805	<ul><li>S->A at 19: Decrease in activity; abolishes phosphorylation by PKG</li></ul>	phosphorylation	GO:0016310	PKG	GO:0004692					1
Q03721	3749	<ul><li>S->A at 8: Decreased inhibition of channel closure by PKC. Inhibition of channel closure is nearly abolished; when associated with A-9</li><li>S->D at 8: Decreased rate of channel inactivation. Loss of channel inactivation; when associated with D-9; D-15 and D-21</li><li>S->A at 9: Strong decrease of inhibition of channel closure by PKC. Inhibition of channel closure is nearly abolished; when associated with A-8</li><li>S->D at 9: Decreased rate of channel inactivation. Loss of channel inactivation; when associated with D-8; D-15 and D-21</li><li>S->A at 15: Decreased inhibition of channel closure by PKC</li><li>S->D at 15: Slightly decreased rate of channel inactivation. Loss of channel inactivation; when associated with D-8; D-9 and D-21</li><li>S->A at 21: Decreased inhibition of channel closure by PKC</li><li>S->D at 21: Slightly decreased rate of channel inactivation. Loss of channel inactivation; when associated with D-8; D-9 and D-15</li></ul>							<li>P13678</li><li>P13677</li><li>P05130</li><li>P34722</li>		1
Q03933	3298	<ul><li>R->G at 109: Fails to translocate to nucleus</li><li>RKR->ASS at 196-198: Fails to translocate to nucleus</li></ul>					nucleus	GO:0005634			1
Q04206	5970	<ul><li>T->A at 254: Abolishes interaction with PIN1</li><li>S->C at 276: Loss of phosphorylation</li></ul>	phosphorylation	GO:0016310					<li>Q9SL42</li><li>Q94G00</li><li>Q5BIN5</li><li>Q4R383</li><li>Q13526</li><li>Q9C6B8</li><li>Q5SMQ9</li><li>P22696</li>		1
Q04609	2346	<ul><li>N->A at 51: Loss of glycosylation. Reduces enzyme activity</li><li>N->A at 76: Loss of glycosylation. Reduces enzyme activity</li><li>N->A at 121: Loss of glycosylation. Severely reduced enzyme activity</li><li>N->A at 140: Loss of glycosylation. Severely reduced enzyme activity</li><li>N->A at 153: Loss of glycosylation. Severely reduced enzyme activity</li><li>N->A at 195: Loss of glycosylation. Severely reduced enzyme activity</li><li>N->A at 336: Loss of glycosylation. Reduces enzyme activity</li><li>H->A,G,Q at 377: Complete loss of activity</li><li>D->E,N at 379: Complete loss of activity</li><li>D->E,L at 387: Complete loss of activity</li><li>D->N at 387: No effect on enzyme activity</li><li>P->A at 388: No effect on enzyme activity</li><li>E->D at 424: Reduces enzyme activity</li><li>E->Q at 424: Reduces enzyme activity</li><li>E->Q,D at 425: Complete loss of activity</li><li>D->N,L at 453: Complete loss of activity</li><li>D->Q at 453: Reduces enzyme activity</li><li>S->A at 454: Reduces enzyme activity</li><li>N->A at 459: Loss of glycosylation. Reduces enzyme activity</li><li>N->A at 476: Loss of glycosylation. Reduces enzyme activity</li><li>N->A at 638: Loss of glycosylation. Abolishes enzyme activity</li><li>T->A at 640: Abolishes enzyme activity</li></ul>									1
Q04637	1981	<ul><li>KRERK->AAAAA at 174-178: Loss of PABPC1 binding; when associated with 184-AAAA-187</li><li>I->A at 180: Loss of PABPC1 binding</li><li>I->A at 182: Loss of PABPC1 binding</li><li>DPNQ->AAAA at 184-187: Loss of PABPC1 binding; when associated with 174-AAAAA-178</li><li>I->A at 192: Loss of PABPC1 binding</li><li>I->A at 196: Loss of PABPC1 binding</li><li>Y->A,F at 612: Abolishes binding to EIF4E</li><li>LL->AA at 617-618: Abolishes binding to EIF4E</li><li>G->A,V,W,R,E at 682: Reduced cleavage by protease 2A from human rhinovirus 2</li><li>L->A at 769: Abolishes binding to EIF4A; when associated with A-772 and A-777</li><li>L->A at 772: Abolishes binding to EIF4A; when associated with A-769 and A-777</li><li>F->A at 777: Abolishes binding to EIF4A; when associated with A-769 and A-772</li><li>LL->AA at 843-844: Abolishes binding to EIF4A; when associated with A-852 and K-853</li><li>FE->AK at 852-853: Abolishes binding to EIF4A; when associated with A-843 and A-844</li><li>L->A at 897: Abolishes binding to EIF4A; when associated with A-903 and A-906</li><li>I->A at 903: Abolishes binding to EIF4A; when associated with A-897 and A-906</li><li>L->A at 906: Abolishes binding to EIF4A; when associated with A-897 and A-903</li><li>R->A at 975: Abolishes binding to EIF4A; when associated with A-978</li><li>F->A at 978: Abolishes binding to EIF4A; when associated with A-975</li><li>L->A at 986: Slightly reduced binding to EIF4A; when associated with A-991</li><li>W->A at 991: Slightly reduced binding to EIF4A; when associated with A-986</li></ul>			binding	GO:0005488			<li>P19028</li><li>Q9QBZ5</li><li>P24107</li><li>Q9QBZ1</li><li>Q79666</li><li>P15833</li><li>P03362</li><li>P18042</li><li>Q8AII1</li><li>P04024</li><li>P03363</li><li>P04023</li><li>O93215</li><li>P10978</li><li>P26810</li><li>Q1A249</li><li>P03356</li><li>P03355</li><li>O41798</li><li>P20892</li><li>Q9Y6I0</li><li>P10210</li><li>Q9PW28</li><li>Q9QBY3</li><li>P03353</li><li>P16901</li><li>P11940</li><li>Q74120</li><li>Q09SZ9</li><li>Q89928</li><li>Q73368</li><li>P84454</li><li>P63074</li><li>Q9WC63</li><li>P20825</li><li>Q9IDV9</li><li>P0C211</li><li>P0C210</li><li>P51518</li><li>Q4U0X6</li><li>Q02748</li><li>P12451</li><li>P07570</li><li>P28936</li><li>O89940</li><li>P24740</li><li>P26809</li><li>P26808</li><li>Q0R5R3</li><li>Q0R5R2</li><li>P18802</li><li>P10394</li><li>P19561</li><li>P16423</li><li>P63119</li><li>P63073</li><li>P19560</li><li>Q75002</li><li>Q9N0T5</li><li>P29338</li><li>P04589</li><li>P04587</li><li>P48598</li><li>P04588</li><li>Q9QSR3</li><li>O91080</li><li>P16046</li><li>P17757</li><li>P12497</li><li>P12499</li><li>P12498</li><li>P03311</li><li>P61286</li><li>P20875</li><li>P20876</li><li>P10273</li><li>Q9WC54</li><li>P10272</li><li>P10271</li><li>P10270</li><li>P19199</li><li>P05962</li><li>P18096</li><li>P10265</li><li>P04584</li><li>P11227</li><li>P04585</li><li>Q76634</li><li>Q8I7P9</li><li>Q9Q720</li><li>P14078</li><li>P31822</li><li>P11365</li><li>Q5UQG4</li><li>P35963</li><li>P14074</li><li>P05959</li><li>P63131</li><li>P04323</li><li>P10274</li><li>P21407</li><li>O89290</li><li>P35956</li><li>P05960</li><li>P05961</li><li>Q1A267</li><li>P07260</li><li>P63122</li><li>P63123</li><li>P63124</li><li>Q9P974</li><li>P63125</li><li>Q9P975</li><li>P63120</li><li>P63121</li><li>P03366</li><li>P03367</li><li>P03369</li><li>Q75AV8</li><li>P63127</li><li>P63128</li><li>P63129</li><li>Q77373</li><li>P03370</li><li>P06730</li><li>P27502</li><li>P48597</li><li>P21414</li><li>O77210</li>		1
Q04656	538	<ul><li>LL->AA at 1487-1488: Loss of relocalization to the trans-Golgi</li></ul>									1
Q04695	3872	<ul><li>R->A at 103: Down-regulates both proliferation of psoriatic T-cells and IFN-gamma production; suppresses keratinocyte growth when part of the altered peptide epitope S1</li><li>E->A at 106: Down-regulates proliferation of psoriatic T-cells and IFN-gamma production when part of the altered peptide epitope S1</li><li>N->A at 109: No significant effect on T-cell proliferation or IFN-gamma production when part of the altered peptide epitope S1</li><li>N->A at 154: No significant effect on T-cell proliferation but reduces IFN-gamma production when part of the altered peptide epitope S2</li><li>I->A at 155: No significant effect on T-cell proliferation but reduces IFN-gamma production when part of the altered peptide epitope S2</li><li>L->A at 157: Down-regulates proliferation of psoriatic T-cells and IFN-gamma production when part of the altered peptide epitope S2</li><li>D->A at 160: No significant effect on T-cell proliferation but reduces IFN-gamma production when part of the altered peptide epitope S4</li><li>N->A at 333: No significant effect on T-cell proliferation but reduces IFN-gamma production when part of the altered peptide epitope S4</li><li>R->A at 334: No significant effect on T-cell proliferation but can induce IFN-gamma production when part of the altered peptide epitope S2</li><li>C->A at 336: No significant effect on T-cell proliferation but reduces IFN-gamma production when part of the altered peptide epitope S2</li><li>L->A at 339: Down-regulates both proliferation of psoriatic T-cells and IFN-gamma production; suppresses keratinocyte growth when part of the altered peptide epitope S4</li></ul>	T-cell proliferation	GO:0042098					<li>O35735</li><li>P63309</li><li>Q25BC0</li><li>P07353</li><li>Q9TTB0</li><li>O57608</li><li>O77763</li><li>P46402</li><li>O57603</li><li>Q2PE75</li><li>Q866Y6</li><li>P79154</li><li>P28341</li><li>Q9TV67</li><li>P01579</li><li>Q865Y4</li><li>Q4ZH68</li><li>P17803</li><li>P30123</li><li>P42160</li><li>P42161</li><li>P42162</li><li>Q865W6</li><li>P63310</li><li>Q8MKF5</li><li>P63311</li><li>O35497</li><li>Q9QXX2</li><li>Q62574</li><li>O57571</li><li>Q7TSP4</li><li>Q9YGB9</li><li>Q647G2</li><li>Q865X1</li><li>P49708</li><li>P17773</li><li>O73915</li><li>Q1WM28</li><li>P01581</li><li>Q8SPW9</li><li>P01580</li><li>Q5CCK0</li><li>Q5I6S9</li><li>P28333</li>		1
Q04724	7088	<ul><li>V->S at 486: Abolishes HESX1 binding</li><li>Y->H at 532: Abolishes HESX1 binding</li><li>L->S at 702: Abolishes HESX1 binding</li><li>S->P at 715: Abolishes HESX1 binding</li></ul>			binding	GO:0005488			<li>Q9UBX0</li><li>O97670</li>		1
Q04759	5588	<ul><li>T->A at 219: Loss of transactivation of the IL2 promoter and translocation to the plasma membrane. No effect on kinase activity</li><li>K->A at 409: Loss of kinase activity</li><li>T->A at 538: Loss of kinase activity</li><li>S->A at 676: Reduction in kinase activity</li><li>S->A at 695: Reduction in kinase activity</li></ul>			kinase activity	GO:0016301	plasma membrane	GO:0005886	<li>Q9XT83</li><li>P26891</li><li>P05016</li><li>Q25BC3</li><li>P68290</li><li>O62641</li><li>P68291</li><li>Q9XS38</li><li>P36835</li><li>Q29615</li><li>Q2PE78</li><li>Q865X2</li><li>Q865Y1</li><li>Q7JFM4</li><li>Q7JFM3</li><li>Q07885</li><li>Q7JFM5</li><li>Q4U313</li><li>O77620</li><li>Q08081</li><li>Q7JFM2</li><li>Q9XT84</li><li>O97513</li><li>P37997</li><li>Q29416</li><li>Q95KP3</li><li>P60568</li><li>P60569</li><li>Q5MBA8</li><li>Q5PXD0</li><li>P46649</li><li>Q1WM29</li><li>Q2PE47</li><li>P19114</li><li>Q8MKH2</li><li>P51747</li>		1
Q04828	1645	<ul><li>E->D at 127: 30-fold decrease in k(cat)/K(m) value for progesterone reduction; no effect on the K(m) value</li><li>H->I at 222: Marked decrease in k(cat)/K(m) value for progesterone; 24-fold decrease for progesterone reduction; 18-fold decrease for 20alpha-OHProg oxidation. 95-fold decrease in K(m) value for NADPH</li><li>H->S at 222: Marked decrease in k(cat)/K(m) value for progesterone; 10-fold decrease for progesterone reduction; 3-fold decrease for 20alpha-OHProg oxidation. 10-fold decrease in K(m) value for NADPH</li><li>R->L at 304: 70-fold decrease in progesterone reduction. No effect on DHT reduction</li><li>Y->F at 305: No effect on progesterone reduction</li><li>T->V at 307: No effect on progesterone reduction</li><li>D->V at 309: No effect on progesterone reduction</li></ul>									1
Q05066	100130809	<ul><li>SSS->AAA at 31-33: Abolishes its phosphorylation by PKA. Does not enhance its DNA-binding activity. Abolishes stimulation of transcription repression</li><li>R->G at 62: Strongly reduces nuclear localization. Strongly reduces nuclear localization; when associated with W-133. Reduces interaction with KPNB1. Abolishes DNA-binding</li><li>M->I at 64: Abolishes nuclear localization</li><li>R->N at 75: Strongly reduces nuclear localization. Abolishes DNA-binding. Does not reduce interaction with KPNB1 and CAML</li><li>R->P at 76: Reduces nuclear localization. Reduces DNA-binding. Does not reduce interaction with KPNB1 and CAML</li><li>K->R at 115: Does not abolish acetylation activity</li><li>K->R at 123: Does not abolish acetylation</li><li>K->R at 128: Does not abolish acetylation</li><li>R->W at 133: Reduces nuclear localization. Strongly reduces nuclear localization; when associated with G-62. Reduces interaction with KPNB1. Does not reduce interaction with CAML. Does not abolish DNA-binding</li><li>K->R at 134: Does not abolish acetylation</li><li>K->R at 136: Abolishes acetylation. Does not abolish interaction with EP300. Does not abolish DNA-binding. Enhances cytoplasmic localization. Abolishes interaction with KPNB1</li></ul>	<li>phosphorylation</li><li>localization</li><li>transcription</li>	<li>GO:0016310</li><li>GO:0051179</li><li>GO:0006350</li>	<li>DNA-binding</li><li>PKA</li>	<li>GO:0003677</li><li>GO:0004691</li>			<li>Q14974</li><li>Q09472</li><li>P49070</li><li>P49069</li>		1
Q05397	5747	<ul><li>V->G at 928: Loss of interaction with TGFB1I1</li><li>L->S at 1034: Loss of interaction with TGFB1I1</li></ul>									1
Q05513	5590	<ul><li>K->A at 19: No effect on interaction with SQSTM1 and PARD6B</li><li>D->A at 62: Loss of interaction with SQSTM1 and PARD6B</li><li>D->A at 66: Loss of interaction with SQSTM1 and PARD6B</li></ul>							<li>Q5RBA5</li><li>Q13501</li><li>Q9BYG5</li>		1
Q05823	6041	<ul><li>K->N at 240: Reduced 2-5A binding activity; almost complete loss of 2-5A binding activity; when associated with N-274</li><li>K->N at 274: Reduced 2-5A binding activity; almost complete loss of 2-5A binding activity; when associated with N-240</li><li>K->R at 392: Complete loss of enzymatic activity and enzyme dimerization. No change in binding to 2-5A and RNA</li><li>H->A at 583: No change in enzymatic activity</li><li>P->A at 584: No change in enzymatic activity</li><li>W->A at 632: No change in enzymatic activity</li><li>D->A at 661: Complete loss of enzymatic activity</li><li>R->A at 667: Complete loss of enzymatic activity. No change in 2-5A binding and enzyme dimerization</li><li>H->A at 672: Complete loss of enzymatic activity. No change in 2-5A binding activity and enzyme dimerization</li></ul>			binding	GO:0005488					1
Q06124	5781	<ul><li>C->S at 463: Abolishes phosphatase activity</li></ul>							<li>Q5X1E5</li><li>Q7M7K5</li><li>Q7MAZ9</li><li>Q8XBL4</li><li>Q88A53</li><li>Q5P3T0</li><li>Q7MBF4</li><li>Q8Z3M9</li><li>Q5PC82</li><li>Q5ZRX9</li><li>Q821A6</li><li>Q87SK9</li><li>Q9JZ88</li><li>Q9CP21</li><li>Q82U82</li><li>Q9I5V3</li><li>Q5F8K9</li><li>Q63YC3</li><li>Q8Y395</li><li>Q6LV05</li><li>Q8ZLY4</li><li>Q6FA38</li><li>Q9PDL7</li><li>Q62EU1</li><li>Q9JUB2</li><li>Q5WT58</li><li>Q665U9</li><li>Q57JQ5</li><li>Q9KPC6</li><li>Q8P5D4</li><li>Q8CWL6</li><li>Q8PPG9</li><li>P06961</li><li>P45269</li><li>Q9L7A3</li><li>Q88QU2</li><li>Q6D160</li><li>Q8ZI64</li><li>Q60CQ4</li><li>Q87DS9</li><li>Q65Q41</li><li>Q5E2K7</li><li>Q8CXX6</li>		1
Q06187	695	<ul><li>E->K at 41: No effect on phosphorylation of GTF2I</li><li>P->A at 189: No effect on phosphorylation of GTF2I</li><li>Y->F at 223: Loss of phosphorylation of GTF2I</li><li>WW->LL at 251-252: Large decrease in binding by SH3BP5</li><li>W->L at 251: No effect on phosphorylation of GTF2I</li><li>R->K at 307: Loss of phosphorylation of GTF2I</li><li>Y->F at 551: Loss of phosphorylation of GTF2I</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488			<li>P78347</li><li>O60239</li>		1
Q06413	4208	<ul><li>K->R at 116: Reduced acetylation. Further reduction in acetylation; when associated with R-119. Complete loss of acetylation, 15% less transactivation activity and slightly reduced DNA binding; when associated with R-119; R-234; R-239; R-252; R-262</li><li>K->R at 119: Reduced acetylation. Further reduction in acetylation; when associated with R-119. Complete loss of acetylation, 15% less transactivation activity and slightly reduced DNA binding; when associated with R-116; R-234; R-239; R-252; R-262</li><li>K->R at 234: Reduced acetylation. Complete loss of acetylation, 15% less transactivation activity and slightly reduced DNA binding; when associated with R-116; R-119; R-239; R-252; R-264</li><li>K->R at 239: Reduced acetylation. Complete loss of acetylation, 15% less transactivation activity and slightly reduced DNA binding; when associated with R-116; R-119; R-234; R-252; R-264</li><li>K->R at 252: Reduced acetylation. Complete loss of acetylation, 15% less transactivation activity and slightly reduced DNA binding; when associated with R-116; R-119; R-234; R-239; R-264</li><li>K->R at 264: Reduced acetylation. Complete loss of acetylation, 15% less transactivation activity and slightly reduced DNA binding; when associated with R-116; R-119; R-234; R-239; R-252</li><li>S->A at 271: No effect on transcriptional activation</li><li>E->Q at 272: Reduced transcriptional activation. Completely abolishes transcriptional activation; when associated with Asn-273 and Asn-275</li><li>D->N at 273: Reduced transcriptional activation. Completely abolishes transcriptional activation; when associated with Gln-272 and Asn-275</li><li>D->N at 275: Reduced transcriptional activation. Completely abolishes transcriptional activation; when associated with Gln-272 and Asn-273</li><li>T->A at 293: Abolishes MAPK14-mediated phosphorylation. No effect on MAPK7-mediated phosphorylation.; when associated with A-300</li><li>T->A at 300: Abolishes MAPK14-mediated phosphorylation. No effect on MAPK7-mediated phosphorylation; when associated with A-293</li><li>S->A at 387: No change in transactivational avtivation for isoforms with or without the beta domain</li><li>K->R at 391: Abolishes sumoylation</li><li>S->A,C at 396: Abolishes sumoylation. Enhanced transcriptional activity</li><li>S->A at 396: No change in transactivational avtivation for isoforms with or without the beta domain</li><li>S->E at 396: No effect on sumoylation. No effect on transcriptional activity</li><li>S->A at 419: No effect on MAPK14-mediated phosphorylation. Abolishes MAPK7-mediated phosphorylation and reduces transactivation activity</li><li>D->A at 432: Abolishes cleavage by caspase 7</li></ul>	<li>phosphorylation</li><li>sumoylation</li>	<li>GO:0016310</li><li>GO:0016925</li>	DNA binding	GO:0003677			<li>P54420</li><li>Q95NE7</li><li>O02812</li><li>O25424</li><li>Q13164</li><li>Q16539</li><li>Q9ZLB9</li><li>P06608</li>		1
Q06418	7301	<ul><li>I->R at 99: Abolishes dimerization</li></ul>									1
Q06455	862	<ul><li>K->A,D at 125: Loss of interaction with TCF12</li><li>L->A at 126: Loss of interaction with TCF12</li><li>R->D at 128: Loss of interaction with TCF12</li><li>F->A at 129: Loss of interaction with TCF12</li><li>F->K at 129: Abolishes interaction with corepressor</li><li>F->A at 136: Abolishes interaction with corepressor</li><li>Q->A at 170: Abolishes interaction with corepressor</li><li>T->Q at 173: Abolishes interaction with corepressor</li><li>F->A at 175: Abolishes interaction with corepressor</li><li>L->A at 177: Abolishes interaction with corepressor</li><li>R->A,D at 178: Loss of interaction with TCF12</li><li>F->A at 184: Loss of interaction with TCF12</li><li>H->A at 547: Causes unfolding of the MYND-type zinc finger domain</li></ul>							<li>Q60420</li><li>Q99081</li><li>P30985</li><li>Q28772</li>		1
Q06547	2553	<ul><li>QQ->AA at 262-263: Minor reduction in transcriptional activation; when associated with A-295 or A-305 and A-306</li><li>VV->AA at 264-265: Minor effect upon interaction with HCFC1 and transcriptional activation. Loss of activity; when associated with A-297; A-298 and A-299, or with A-307 and A-310</li><li>QQ->AA at 270-271: Minor reduction in transcriptional activation. Moderate reduction in activity; when associated with A-305 and A-306</li><li>ITI->ATA at 273-275: Strongly reduces interaction with HCFC1 and transcriptional activation. Loss of activity; when associated with A-297; A-298 and A-299, or with A-307 and A-310</li><li>Q->A at 295: No effect on transcriptional activation. Minor reduction in activity; when associated with A-270 and A-271</li><li>IIV->AAA at 297-299: Strongly reduces interaction with HCFC1 and transcriptional activation. Loss of activity; when associated with A-264 and A-265, or A-273 and A-275</li><li>QQ->AA at 305-306: Minor reduction in transcriptional activation. Moderate reduction in activity; when associated with A-270 and A-271</li><li>VLTV->ALTA at 307-310: Moderately reduces interaction with HCFC1 and transcriptional activation. Loss of activity; when associated with A-273 and A-275</li></ul>							<li>Q5I4B8</li><li>P51611</li><li>P51610</li>		1
Q06609	5888	<ul><li>T->A at 309: Confers hypersensitivity to hydroxyurea</li></ul>									1
Q06787	2332	<ul><li>TF->AA at 125-126: Alters the structural integrity of the N-terminus and leads to aggregation</li><li>S->A at 500: Loss of phosphorylation</li><li>R->K at 544: Reduces arginine methylation by 80%</li><li>R->K at 546: Slightly reduced methylation</li></ul>	phosphorylation	GO:0016310							1
Q06830	5052	<ul><li>T->A at 90: Abolishes phosphorylation by CDC2; 30% reduction in enzymatic activity</li><li>T->D at 90: 87% reduction in enzymatic activity</li></ul>	phosphorylation	GO:0016310					<li>Q9W739</li><li>Q9DGA2</li><li>Q9DGA5</li><li>P19026</li><li>Q5RCH1</li><li>Q9DG98</li><li>P06493</li><li>P48734</li><li>P43290</li><li>P23111</li><li>P13863</li><li>Q04770</li><li>P52389</li><li>P15436</li><li>P24100</li><li>P51958</li><li>Q41639</li><li>P54119</li><li>P93101</li><li>Q9DGD3</li>		1
Q07812	581	<ul><li>S->D,E,H,K at 184: Constitutive cytoplasmic location</li><li>S->V at 184: Constitutive mitochondrial location</li></ul>									1
Q07817	598	<ul><li>D->A at 61: No cleavage by caspase-1 nor by caspase-3</li><li>FRD->VRA at 131-133: No heterodimerization with BAX</li><li>VNW->AIL at 135-137: Loss of anti-apoptotic activity</li><li>GRI->ELN at 138-140: Loss of anti-apoptotic activity</li><li>G->A at 138: No heterodimerization with BAX</li><li>G->E at 148: No heterodimerization with BAX</li><li>D->A at 156: No effect on caspase-1 cleavage</li><li>D->A at 176: No effect on caspase-1 cleavage</li><li>WD->GA at 188-189: Reduces anti-apoptotic activity by about half</li><li>D->A at 189: No effect on caspase-1 cleavage</li></ul>							<li>Q07815</li><li>Q07812</li><li>Q07814</li><li>O02703</li><li>P55269</li>		1
Q07820	4170	<ul><li>K->R at 5: Reduced ubiquitination</li><li>K->R at 40: Reduced ubiquitination</li><li>D->A at 127: Abolishes formation of 28 and 17 kDa cleavage products by CASP3. Abolishes cleavage by caspase-3; when associated with A-157</li><li>K->R at 136: Reduced ubiquitination</li><li>D->A at 157: Abolishes formation of 23 and 21 kDa cleavage products by CASP3. Abolishes cleavage by caspase-3; when associated with A-127</li><li>S->A at 162: No effect</li><li>T->A at 163: Abolishes phosphorylation by MAPK. No effect on phosphorylation induced by okadaic acid or taxol</li><li>K->R at 194: Reduced ubiquitination</li><li>K->R at 197: Reduced ubiquitination</li><li>K->R at 208: No effect on ubiquitination</li><li>K->R at 234: No effect on ubiquitination</li></ul>	phosphorylation	GO:0016310					<li>Q8MJU1</li><li>Q8MKI5</li><li>Q5IS99</li><li>Q2PFV2</li><li>O42781</li><li>Q00859</li><li>Q95ND5</li><li>Q5IS54</li><li>P27638</li><li>Q60431</li><li>Q8MJC3</li><li>P42574</li><li>Q08DY9</li>		1
Q07954	4035	<ul><li>T->A at 4460: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4517; A-4520 and A-4523</li><li>NPTY->APTA at 4470-4473: No effect on tyrosine phosphorylation</li><li>N->A at 4470: No effect on interaction with GULP1</li><li>T->A at 4472: No detectable effect on phosphorylation</li><li>NPVY->APVA at 4504-4507: Loss of tyrosine phosphorylation. Abolishes interaction with SHC1 and GULP1</li><li>N->A at 4504: Loss of interaction with GULP1</li><li>S->A at 4517: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4520 and A-4523</li><li>S->A at 4520: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4517 and A-4523</li><li>S->A at 4523: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4517 and A-4520</li></ul>	phosphorylation	GO:0016310					P29353		1
Q07955	6426	<ul><li>FV->SR at 58-59: In FV1; loss of ability to activate splicing. Slight reduction in splice site switching activity and no effect on RNA-binding</li><li>FV->SR at 162-163: In FV2; loss of ability to activate splicing. Great reduction in splice site switching activity and RNA-binding</li><li>F->A at 162: In AV; loss of ability to activate splicing. Great reduction in splice site switching activity and no effect on RNA-binding</li><li>F->D at 162: Reduced nucleocytoplasmic shuttling; when associated with D-190</li><li>F->D at 180: Reduced nucleocytoplasmic shuttling; when associated with D-162</li><li>Missing at 182-248: In MR-B; strongly inhibits splicing</li><li>Missing at 182-199: In MR-E; loss of ability to activate splicing</li><li>Missing at 192-248: In MR-A; loss of ability to activate splicing</li><li>Missing at 192-199: In MR-D; loss of ability to activate splicing</li><li>Missing at 199-224: In RS-A; loss of ability to activate splicing but retains splice site switching</li><li>Missing at 215-248: In RS-C; loss of ability to activate splicing but retains splice site switching</li><li>Missing at 226-248: In RS-B; retains both splice activation and splice site switching activity</li></ul>			RNA-binding	GO:0003723					1
Q08211	1660	<ul><li>W->A at 332: Abrogates transcriptional activation by the MTAD domain</li><li>W->A at 339: Abrogates transcriptional activation and RNA polymerase II binding by the MTAD domain</li><li>W->A at 342: Abrogates transcriptional activation by the MTAD domain</li><li>K->R at 417: Abrogates transcriptional activation</li><li>Missing at 1163: Abolishes nuclear localization</li><li>R->L at 1166: Abolishes nuclear localization</li><li>Missing at 1166: Abolishes nuclear localization</li></ul>	localization	GO:0051179	binding	GO:0005488					1
Q08357	6575	<ul><li>D->N at 28: Impairs phosphate transport; no effect on retroviral receptor function</li><li>E->D,K at 55: Abolishes sodium-dependent phosphate transport; no effect on retroviral receptor function</li><li>E->Q at 55: Abolishes phosphate but not sodium uptake; when associated with Q-91 and Q-575</li><li>N->V at 81: Abolishes N-glycosylation</li><li>E->Q at 91: Abolishes phosphate but not sodium uptake; when associated with Q-55 and Q-575</li><li>D->N at 506: Impairs phosphate transport; no effect on retroviral receptor function</li><li>E->D,K at 575: Abolishes sodium-dependent phosphate transport; no effect on retroviral receptor function</li><li>E->Q at 575: Abolishes phosphate but not sodium uptake; when associated with Q-55 and Q-91</li></ul>	phosphate transport	GO:0006817							1
Q08378	2802	<ul><li>D->A at 59: Abolishes cleavage by caspase-2</li><li>L->A at 121: Loss of interaction with GOPC; when associated with A-128 and A-135</li><li>L->A at 128: Loss of interaction with GOPC; when associated with A-121 and A-135</li><li>L->A at 135: Loss of interaction with GOPC; when associated with A-121 and A-128</li><li>D->A at 139: Abolishes cleavage by caspase-3</li><li>D->A at 311: Abolishes cleavage by caspase-7</li></ul>							<li>Q9HD26</li><li>Q5RD32</li>		1
Q08499	5144	<ul><li>D->R at 527: Abolishes homodimerization</li><li>R->D at 563: Abolishes homodimerization</li></ul>									1
Q08945	6749	<ul><li>D->A at 450: Abolishes cleavage by caspase</li><li>S->A at 510: Unable to bind DNA; when associated with A-657 and A-688</li><li>S->A at 657: Unable to bind DNA; when associated with A-510 and A-688. Still able to bind DNA; when associated with A-688</li><li>S->A at 688: Unable to bind DNA; when associated with A-510 and A-657. Still able to bind DNA; when associated with A-657</li></ul>									1
Q08ET2	100049587	<ul><li>R->A at 362: Loss of interaction with TYROBP</li></ul>							<li>Q95J79</li><li>Q9TU45</li><li>Q8WNQ8</li><li>O43914</li>		1
Q08J23	54888	<ul><li>S->A at 139: Induces a constitutive association with NPM1</li><li>S->E at 139: Mimicks constitutive phosphorylation and abolishes methyltransferase activity</li></ul>	phosphorylation	GO:0016310					<li>Q00020</li><li>P03588</li><li>Q83270</li><li>P03589</li><li>P28931</li><li>P06011</li><li>P06748</li><li>P16039</li><li>P17769</li><li>P20122</li><li>Q66121</li><li>O40976</li><li>P28726</li><li>P27752</li><li>Q3T160</li><li>Q83264</li>		1
Q09013	1760	<ul><li>K->A at 110: Loss of kinase activity</li></ul>			kinase activity	GO:0016301					1
Q09470	3736	<ul><li>CC->AA at 35-36: No effect on palmitoylation, no effect on current kinetics</li><li>C->A at 243: Strongly decreases palmitoylation and alters current kinetics</li></ul>									1
Q09472	2033	<ul><li>R->K at 2056: No effect on interaction with NCOA2</li><li>R->K at 2088: Abolishes interaction with NCOA2</li><li>R->K at 2142: Strongly reduces interaction with NCOA2</li></ul>							Q15596		1
Q09MP3	729475	<ul><li>L->A at 1134: Strongly decreases interaction with RAD51; when associated with 1143-AA-1144</li><li>LH->AA at 1143-1144: Strongly decreases interaction with RAD51; when associated with A-1134</li></ul>							<li>Q40134</li><li>P94102</li><li>Q2KJ94</li><li>Q8MKI8</li><li>Q99133</li><li>O77507</li><li>P37383</li><li>P70099</li><li>P25454</li><li>Q06609</li>		1
Q0JRZ9	115548	<ul><li>F->E at 10: Binds preferentially to larger liposomes</li></ul>									1
Q0VD86	388324	<ul><li>S->A at 23: Loss of phosphorylation site</li><li>T->A at 182: Reduced phosphorylation. Phosphorylation is almost abolished; when asssociated with A-191</li><li>S->A at 191: Strongly reduced phosphorylation. Phosphorylation is almost abolished; when asssociated with A-182</li><li>S->A at 194: Reduced phosphorylation</li></ul>	phosphorylation	GO:0016310							1
Q0WX57	728369	<ul><li>C->S at 89: Abolishes enzymatic activity. Loss of the pro-apoptotic function</li></ul>									1
Q12772	6721	<ul><li>DRSR->AAAA at 478-481: Loss of cleavage by S2P</li><li>DRSR->AS at 478-481: Loss of cleavage by S2P</li><li>D->A at 478: No effect on proteolytic processing in response to low sterol</li><li>RSR->AAA at 479-481: Loss of cleavage by S2P</li><li>R->A at 479: No effect on cleavage by S2P</li><li>R->A at 481: No effect on cleavage by S2P</li><li>LC->FF at 484-485: No effect on cleavage by S2P</li><li>L->A at 484: No effect on cleavage by S2P</li><li>C->A at 485: No effect on cleavage by S2P</li><li>LC->NP at 490-491: Restores cleavage by S2P; when associated with F-495 and L-496. No effect on site of cleavage by S2P</li><li>NP->FL at 495-496: Loss of cleavage by S2P</li><li>N->F at 495: Reduced cleavage by S2P</li><li>P->L at 496: Reduced cleavage by S2P</li><li>R->A at 519: Loss of proteolytic processing in response to low sterol</li><li>R->K at 519: No effect on proteolytic processing in response to low sterol</li></ul>							<li>O43462</li><li>O54862</li>		1
Q12778	2308	<ul><li>T->A at 24: Nuclear targeting and enhanced transactivation; when associated with A-319</li><li>K->A at 245: Disrupts DNA binding; when associated with A-248</li><li>K->A at 248: Disrupts DNA binding; when associated with A-245</li><li>RRR->SAS at 251-253: Disrupts DNA binding</li><li>S->A at 256: Nuclear targeting. Abolishes the ability of IGF1 to suppress transactivation. Prevents T-24 and S-319 phosphorylation. Enhances transactivation; when associated with A-24 and A-319</li><li>S->D at 256: Reduces DNA binding, promotes nuclear exclusion and partially promotes T-24 and S-319 phosphorylation. Reduces DNA binding, does not promote nuclear exclusion but reduces transactivation; when associated with A-24 and A-319</li><li>S->A at 319: Nuclear targeting and enhanced transactivation; when associated with A-24</li><li>S->A at 329: Nuclear targeting and enhanced transactivation</li></ul>	phosphorylation	GO:0016310	DNA binding	GO:0003677			<li>P17647</li><li>Q6IVA5</li><li>P05019</li><li>Q6GUL6</li><li>Q28933</li><li>Q68LC0</li><li>P16545</li><li>P51457</li><li>P07455</li><li>P51458</li><li>P51462</li><li>P01343</li><li>P10763</li><li>Q6JLX1</li><li>Q95222</li><li>P33712</li><li>P18254</li>		1
Q12791	3778	<ul><li>L->R,H at 269: No effect in the coupling between calcium and channel opening</li><li>R->E at 272: Induces reduction in the coupling between calcium and channel opening</li><li>R->N at 275: Induces reduction in the coupling between calcium and channel opening</li><li>R->Q at 278: Induces reduction in the coupling between calcium and channel opening</li><li>Q->R at 281: No effect in the coupling between calcium and channel opening</li><li>E->K at 284: No effect in the coupling between calcium and channel opening</li><li>GYG->AAA at 354-356: Loss of function</li><li>C->S at 680: Loss of heme-induced channel inhibition</li><li>H->R at 681: Loss of heme-induced channel inhibition</li></ul>									1
Q12796	10957	<ul><li>P->A at 287: Abolishes the interaction with the nuclear receptors; when associated with A-290</li><li>P->A at 290: Abolishes the interaction with the nuclear receptors; when associated with A-287</li></ul>									1
Q12800	7024	<ul><li>V->E at 211: Does not affect DNA-binding activity</li><li>I->R at 213: Does not affect DNA-binding activity</li><li>Q->L at 234: Significant reduction of DNA-binding activity</li><li>K->E at 236: Significant reduction of DNA-binding activity</li></ul>			DNA-binding	GO:0003677					1
Q12802	11214	<ul><li>A->P at 1251: Loss of PKA anchoring; when associated with P-1260</li><li>I->P at 1260: Loss of PKA anchoring; when associated with P-1251</li><li>A->P at 1265: Abolishes RII-binding</li><li>Y->F at 2153: Loss of interaction with RHOA</li></ul>			<li>binding</li><li>PKA</li>	<li>GO:0005488</li><li>GO:0004691</li>			<li>P61586</li><li>P24406</li><li>P61585</li>		1
Q12809	3757	<ul><li>F->A at 29: Slows down deactivation</li><li>Y->A at 43: Slows down deactivation</li><li>S->A at 283: Abolishes phosphorylation; when associated with A-890; A-895 and A-1137</li><li>N->Q at 598: No effect on cell surface expression, but changes inactivation kinetics; when associated with A-631</li><li>N->Q at 629: Abolishes cell surface expression; has no effect on N-glycosylation</li><li>S->A at 631: No effect on cell surface expression, but changes inactivation kinetics; when associated with Q-598</li><li>S->A at 890: Abolishes phosphorylation; when associated with A-283; A-895 and A-1137</li><li>T->A at 895: Abolishes phosphorylation; when associated with A-283; A-890 and A-1137</li><li>S->A at 1137: Abolishes phosphorylation; when associated with A-283; A-890 and A-895</li></ul>	phosphorylation	GO:0016310			cell surface	GO:0009928,GO:0009986			1
Q12830	2186	<ul><li>Y->T at 2869: Abolishes binding to histone H3-K4Me3</li><li>Y->T at 2876: Strongly reduces binding to histone H3-K4Me3</li><li>Y->S at 2882: Abolishes binding to histone H3-K4Me3</li><li>G->E,L at 2884: Strongly reduces binding to histone H3-K4Me3</li><li>D->N,A at 2886: Abolishes binding to histone H3-K4Me3</li><li>Q->K at 2889: Strongly reduces binding to histone H3-K4Me3</li><li>W->E,F at 2891: Abolishes binding to histone H3-K4Me3</li></ul>			binding	GO:0005488			<li>P61835</li><li>P61834</li><li>Q9P427</li><li>P61833</li><li>Q98RY4</li><li>P61832</li><li>P61831</li><li>P61830</li><li>P83864</li><li>P07041</li><li>P90543</li><li>P02299</li><li>P08437</li><li>Q757N1</li><li>P50564</li><li>P61836</li><li>Q06196</li><li>P08898</li><li>Q9HDN1</li><li>P23753</li><li>Q7XYZ0</li><li>Q9U7D1</li><li>Q2UCQ0</li><li>Q5DWI3</li><li>P80553</li><li>P40285</li><li>P84239</li><li>P84238</li><li>P84237</li><li>P84236</li><li>P22843</li><li>P84235</li>		1
Q12840	3798	<ul><li>R->S at 280: Strongly reduces microtubule affinity; slightly reduces gliding velocity</li></ul>					microtubule	GO:0005874			1
Q12888	7158	<ul><li>SQS->AQA at 176-178: Loss of phosphorylation site</li><li>R->A at 1396: No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1398; A-1400; A-1401 and A-1403</li><li>R->K at 1396: No detectable effect on methylation by PRMT1 (in vitro)</li><li>R->A at 1398: No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1396; A-1400; A-1401 and A-1403</li><li>R->K at 1398: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1400. Strongly reduced methylation; when associated with K-1401</li><li>R->A at 1400: No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1396; A-1398; A-1401 and A-1403</li><li>R->K at 1400: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1398. Strongly reduced methylation; when associated with K-1401</li><li>R->A at 1401: No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1396; A-1398; A-1400 and A-1403</li><li>R->K at 1401: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1398. Strongly reduced methylation; when associated with K-1400</li><li>R->A at 1403: No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1396; A-1398; A-1400 and A-1401</li><li>R->K at 1403: No detectable effect on methylation by PRMT1 (in vitro)</li><li>W->A,H at 1495: Loss of interaction with histone H4 that has been dimethylated at 'Lys-20'</li><li>W->F at 1495: No effect on recruitment to double strand breaks</li><li>W->V at 1495: Reduces recruitment to double strand breaks</li><li>Y->A at 1500: Reduces affinity for histone H4 that has been dimethylated at 'Lys-20'</li><li>Y->A at 1502: Reduces affinity for histone H4 that has been dimethylated at 'Lys-20'</li><li>Y->L,Q at 1502: Abolishes recruitment to double strand breaks</li><li>D->A at 1521: Loss of interaction with histone H4 that has been dimethylated at 'Lys-20'. Abolishes recruitment to double strand breaks</li><li>D->R at 1521: Abolishes recruitment to double strand breaks</li><li>Y->A at 1523: Increases affinity for histone H4 that has been dimethylated at 'Lys-20'. No effect on recruitment to double strand breaks</li><li>Y->S at 1523: Decreases affinity for histone H4 that has been dimethylated at 'Lys-20'</li></ul>	phosphorylation	GO:0016310					<li>Q76FE7</li><li>P82888</li><li>Q6LAF1</li><li>P91882</li><li>Q6LAF3</li><li>Q27443</li><li>Q8MTV8</li><li>P23630</li><li>Q76FD9</li><li>Q99873</li><li>P51728</li><li>P08436</li><li>Q03709</li><li>P35059</li><li>P35057</li><li>P91890</li><li>Q6WZ83</li><li>P83865</li><li>P84048</li><li>P84049</li><li>P84044</li><li>Q7K8C0</li><li>Q7KQD1</li><li>P84045</li><li>P62779</li><li>P84046</li><li>P62778</li><li>P84047</li><li>P84040</li><li>P62777</li><li>P84041</li><li>P62776</li><li>Q8I0Y4</li><li>P84042</li><li>P84043</li><li>P84050</li><li>Q43083</li><li>P15176</li><li>Q6WV90</li><li>P62782</li><li>P62781</li><li>P62784</li><li>Q8NIG3</li><li>P62783</li><li>P62780</li><li>Q9HDF5</li><li>P62789</li><li>Q7LKT3</li><li>P62788</li><li>Q27765</li><li>Q6WV73</li><li>P62787</li><li>Q6WV74</li><li>P59259</li><li>Q7M3Z5</li><li>P91849</li><li>Q6ZXX3</li><li>P13345</li><li>P13344</li><li>P09322</li><li>Q76H85</li><li>P62796</li><li>P62797</li><li>P62798</li><li>P62799</li><li>P62790</li><li>P62791</li><li>P62792</li><li>P62793</li><li>P62794</li><li>P62795</li><li>Q6WV72</li><li>P05821</li><li>P80739</li><li>P80738</li><li>Q9T1X2</li><li>Q9U7D0</li><li>P27996</li><li>P90516</li><li>Q8T7J8</li><li>P62803</li><li>P62802</li><li>P62801</li><li>P62800</li><li>Q76MU7</li><li>P02309</li><li>Q8J1L3</li><li>P10099</li><li>Q6V9I2</li><li>P62806</li><li>P50566</li><li>P62804</li><li>P62805</li><li>P04915</li><li>Q76FF5</li><li>Q8SQP4</li><li>P04914</li><li>Q76FF1</li><li>Q6PMI5</li><li>P62887</li><li>P40287</li><li>Q71V09</li>		1
Q12908	6555	<ul><li>N->D at 10: Abolishes glycosylation</li><li>N->D at 328: No effect on glycosylation</li></ul>									1
Q12959	1739	<ul><li>INI->ANA at 38-40: Loss of membrane association and DLG2-binding</li></ul>			binding	GO:0005488	membrane	GO:0016020	<li>Q15700</li><li>Q14168</li>		1
Q12962	6881	<ul><li>K->Q at 189: Abolishes methylation</li></ul>									1
Q12972	5511	<ul><li>SRVH->AAAA at 68-71: Abolishes interaction with CDC5L, SF3B1 and MELK, and localization in nuclear speckles. No effect on repressor activity</li><li>KRKRK->AAAAA at 193-197: No effect on interaction with EED</li><li>KRK->AAA at 195-197: Abolishes nuclear import; when associated with A-234--237-A</li><li>S->A,D at 199: No change in subcellular location, no effect on interaction with EED or repressor activity; when associated with A-204 or D-204</li><li>V->A at 201: Reduces PP-1 binding, but no effect on subcellular location or repressor activity; when associated with A-203</li><li>F->A at 203: Reduces PP-1 binding, but no effect on subcellular location or repressor activity; when associated with A-201</li><li>S->A,D at 204: No change in subcellular location, no effect on interaction with EED or repressor activity; when associated with A-199 or D-199</li><li>KKKR->AAAA at 234-237: Abolishes nuclear import; when associated with A-195-197-A</li><li>Y->D at 264: Abolishes in vitro phosphorylation of isoform gamma by Lyn</li><li>Y->D at 335: Decreases the ability of isoform Gamma to bind and inhibit PP-1</li><li>T->D at 346: No effect on the ability of isoform Gamma to inhibit PP-1</li><li>S->D at 348: No effect on the ability of isoform Gamma to inhibit PP-1</li></ul>	<li>phosphorylation</li><li>nuclear import</li><li>localization</li>	<li>GO:0016310</li><li>GO:0051170</li><li>GO:0051179</li>	binding	GO:0005488	nuclear speckles	GO:0016607	<li>Q14680</li><li>Q99459</li><li>Q2KJC1</li><li>O75533</li>		1
Q12974	8073	<ul><li>Missing at 164-167: Locates in the nucleus and cytosol. No interaction with RABGGTB</li><li>C->S at 165: No effect on interaction with RABGGTB</li></ul>					<li>nucleus</li><li>cytosol</li>	<li>GO:0005634</li><li>GO:0005829</li>	<li>P53611</li><li>Q5E9B3</li>		1
Q12981	662	<ul><li>L->A at 114: Loss of proapoptotic effect. No effect on interaction with RINT1</li></ul>							Q6NUQ1		1
Q12986	4799	<ul><li>F->A at 20: Reduces PABPC1 and PABC4 binding</li></ul>			binding	GO:0005488			<li>P11940</li><li>P61286</li>		1
Q13029	7799	<ul><li>C->Y at 106: Reduced histone methyltransferase activity</li><li>A->V at 159: Reduced histone methyltransferase activity</li><li>I->V at 188: Loss of histone methyltransferase activity</li></ul>							<li>Q00020</li><li>P03588</li><li>P03589</li><li>Q83270</li><li>P28931</li><li>P06011</li><li>P17769</li><li>P20122</li><li>Q66121</li><li>O40976</li><li>P28726</li><li>P27752</li><li>Q83264</li>		1
Q13043	6789	<ul><li>K->R at 59: Loss of activity</li><li>T->A at 175: No effect on activity</li><li>T->A at 177: No effect on activity</li><li>T->A at 183: Loss of activity</li><li>D->N at 326: Resistant to proteolytic cleavage by caspase during apoptosis; when associated with N-349</li><li>D->N at 349: Resistant to proteolytic cleavage by caspase during apoptosis; when associated with N-326</li><li>L->P at 444: Loss of homodimerization, activation, and autophosphorylation</li></ul>	<li>autophosphorylation</li><li>apoptosis</li>	<li>GO:0046777</li><li>GO:0006915</li>							1
Q13045	2314	<ul><li>E->K at 586: No change in ESR1 binding but reduced binding to ACTL6A and reduced coactivator function</li><li>G->S at 603: No change in binding to ACTL6A or in coactivator function</li></ul>			binding	GO:0005488			<li>Q9TV98</li><li>Q9QZJ5</li><li>P49884</li><li>Q91424</li><li>Q91250</li><li>Q29040</li><li>O96019</li><li>P38111</li><li>Q9YHT3</li><li>P50242</li><li>P50241</li><li>P03372</li><li>P16058</li><li>Q9YH33</li><li>Q9PVZ9</li><li>P50240</li><li>Q4R333</li><li>P06212</li><li>P57753</li><li>Q53AD2</li><li>P49885</li><li>P49886</li><li>Q9YHZ7</li><li>O42132</li>		1
Q13085	31	<ul><li>S->A at 78: No effect on interaction with BRCA1</li><li>S->A at 344: No effect on interaction with BRCA1</li><li>S->A at 432: No effect on interaction with BRCA1</li><li>S->A at 1201: No effect on interaction with BRCA1</li><li>S->A at 1263: Abolishes interaction with BRCA1</li><li>S->A at 1585: No effect on interaction with BRCA1</li><li>S->A at 1952: No effect on interaction with BRCA1</li><li>S->A at 2211: No effect on interaction with BRCA1</li></ul>							<li>Q864U1</li><li>P38398</li><li>Q95153</li><li>Q6J6J0</li><li>Q6J6I8</li><li>Q9GKK8</li><li>Q6J6I9</li>		1
Q13093	7941	<ul><li>S->A at 108: Activity is higher than wild-type</li><li>S->A at 273: Loss of activity</li><li>D->A at 286: Almost no activity</li><li>D->N at 286: Diminishes activity</li><li>D->A at 296: Loss of activity</li><li>D->N at 296: Loss of activity</li><li>D->A at 304: No change in activity</li><li>D->A at 338: Activity is higher than wild-type</li><li>H->A at 351: Loss of activity</li></ul>									1
Q13107	7375	<ul><li>C->A at 311: Loss of activity</li></ul>									1
Q13137	10241	<ul><li>C->A at 400: Loss of interaction with MYO6</li><li>C->A at 425: No effect on interaction with MYO6</li></ul>							Q9UM54		1
Q13148	23435	<ul><li>Missing at 106-175: Completely abolishes RNA binding</li><li>LIVLGL->DIDLGD at 106-111: Completely abolishes RNA binding</li><li>Missing at 106-111: Completely abolishes RNA binding</li><li>FGF->LGL at 147-149: Highly reduces binding to RNA and DNA</li><li>Missing at 193-257: Alters but does not abolish RNA binding</li></ul>			<li>binding</li><li>RNA binding</li>	<li>GO:0005488</li><li>GO:0003723</li>					1
Q13153	5058	<ul><li>H->L at 83: Decreases activity; when associated with L-86</li><li>H->L at 86: Decreases activity; when associated with L-83</li><li>L->F at 107: Constitutively active</li><li>T->A at 423: Decreases CDC42-stimulated activity and autophosphorylation</li></ul>	autophosphorylation	GO:0046777					<li>Q90694</li><li>O94103</li><li>O14426</li><li>P60953</li><li>Q17031</li><li>P60952</li><li>Q9HF56</li><li>P19073</li>		1
Q13158	8772	<ul><li>V->N at 121: No interaction with Fas receptor</li></ul>							<li>P25446</li><li>Q63199</li>		1
Q13163	5607	<ul><li>K->M at 195: Inactivation</li><li>S->A at 311: Inactivation</li><li>T->A at 315: Inactivation</li></ul>									1
Q13164	5598	<ul><li>TEY->AEF at 219-221: Loss activation by MAP2K5</li></ul>							Q13163		1
Q13177	5062	<ul><li>D->N at 212: Inhibits caspase-mediated cleavage</li><li>G->A at 213: Abolishes myristoylation of PAK-2p34 and membrane location</li><li>IVSIG->REGRS at 239-243: Abolishes nuclear export</li><li>KKK->MHE at 246-248: Greatly inhibits nuclear localization</li><li>K->R at 278: Abolishes kinase activity and autophosphorylation</li><li>T->A at 402: Abolishes kinase activity and greatly inhibits autophosphorylation of PAK-2p27 and PAK-2p34</li></ul>	<li>autophosphorylation</li><li>nuclear export</li><li>localization</li>	<li>GO:0046777</li><li>GO:0051168</li><li>GO:0051179</li>	kinase activity	GO:0016301	membrane	GO:0016020			1
Q13188	6788	<ul><li>K->R at 56: Loss of activity</li></ul>									1
Q13191	868	<ul><li>G->E at 298: Inhibits interaction with SYK. No effect on E3 activity</li><li>C->A at 373: Abolishes E3 activity but does not affect binding to substrates</li><li>Y->F at 665: Slightly inhibits interaction with CRKL. Abolishes interaction with CRKL; when associated to F-709</li><li>Y->F at 709: Inhibits interaction with CRKL. Abolishes interaction with CRKL; when associated to F-665</li><li>R->A at 904: No effect on interaction with CD2AP. Reduced interaction with SH3KBP1. Strongly reduced interaction with SH3KBP1; when associated with A-911</li><li>K->A at 907: No effect on interaction with SH3KBP1. Reduced interaction with CD2AP. Strongly reduced interaction with CD2AP; when associated with A-911</li><li>R->A at 911: Reduced interaction with CD2AP and with SH3KBP1. Strongly reduced interaction with CD2AP; when associated with A-907. Strongly reduced interaction with SH3KBP1; when associated with A-904</li><li>A->E at 937: Loss of ubiquitin binding. Reduced levels of tyrosine phosphorylation</li><li>M->A at 940: Loss of ubiquitin binding. Reduced levels of tyrosine phosphorylation</li><li>GY->AQ at 943-944: Abolishes interaction with ubiquitinated proteins</li><li>F->A at 946: Loss of ubiquitin binding. Reduced levels of tyrosine phosphorylation</li><li>I->E at 966: Interferes with dimerization. Reduced E3 ubiquitin-protein ligase activity. Reduced levels of tyrosine phosphorylation</li><li>L->A at 967: No effect on interaction with ubiquitinated proteins</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488			<li>P69326</li><li>P08565</li><li>P69322</li><li>P69323</li><li>P69324</li><li>P69325</li><li>P68196</li><li>O46543</li><li>P68197</li><li>Q05550</li><li>P68198</li><li>P68199</li><li>P19848</li><li>P42739</li><li>P68195</li><li>Q867C2</li><li>P62991</li><li>P62990</li><li>P61863</li><li>Q96B97</li><li>P61864</li><li>P61862</li><li>Q867C4</li><li>Q867C3</li><li>P23398</li><li>P68204</li><li>P84589</li><li>Q865C5</li><li>P42740</li><li>P68201</li><li>Q8MKD1</li><li>P14792</li><li>P63049</li><li>P0C072</li><li>P63051</li><li>Q8RSY1</li><li>P69308</li><li>P69309</li><li>P20685</li><li>Q9Y5K6</li><li>Q2QCI9</li><li>P15174</li><li>Q00655</li><li>P46109</li><li>P62976</li><li>P62977</li><li>P62974</li><li>P62975</li><li>P62972</li><li>P43405</li><li>P13117</li><li>P14624</li><li>P62973</li><li>P46574</li><li>P69310</li><li>P69313</li><li>P69314</li><li>P69311</li><li>P69312</li><li>P08618</li><li>P69317</li><li>P69318</li><li>P69315</li><li>P0C014</li><li>P69316</li><li>P59263</li><li>P69319</li><li>P49634</li><li>P49635</li><li>Q9Y848</li><li>P22589</li><li>P62988</li><li>P62989</li><li>P69321</li><li>P23324</li><li>P69320</li><li>P59669</li>		1
Q13239	6503	<ul><li>R->K at 111: Strongly reduces interaction with ZAP70, CD3Z, SYK and LAT</li><li>L->S at 218: Abolishes interaction with CBL. Does not affect dimerization; when associated with S-224 and S-229</li><li>L->S at 224: Abolishes interaction with CBL. Does not affect dimerization; when associated with S-218 and S-229</li><li>L->S at 229: Abolishes interaction with CBL. Does not affect dimerization; when associated with S-218 and S-224</li><li>LSL->QSQ at 237-239: Abolishes interaction with CBL. Slightly affects dimerization</li></ul>							<li>P20963</li><li>P29329</li><li>P43623</li><li>P22681</li><li>P53780</li><li>P44527</li><li>Q9TUF8</li><li>Q9XSJ9</li><li>P53101</li><li>Q52811</li><li>Q07703</li><li>O43561</li><li>P23256</li><li>P41929</li><li>P06721</li><li>Q00655</li><li>P43403</li><li>P18949</li><li>P43405</li><li>P0A4K2</li><li>P0A4K3</li>		1
Q13261	3601	<ul><li>Y->F at 227: Abrogates association with SYK and phosphorylation upon IL-15 stimulation</li></ul>	phosphorylation	GO:0016310					<li>O97687</li><li>P40933</li><li>Q4U0U2</li><li>P40221</li><li>P97604</li><li>Q4GZL1</li><li>Q00655</li><li>Q9XSJ6</li><li>Q3Y5G8</li><li>P43405</li><li>P48092</li><li>Q95253</li><li>Q28028</li><li>P48346</li>		1
Q13283	10146	<ul><li>S->A at 149: Cytoplasmic; no effect on stress granule assembly</li><li>S->E at 149: Cytoplasmic and nuclear; no assembly of stress granules; no homo-oligomerization</li><li>S->A at 232: Cytoplasmic. Partially nuclear; when associated with E-149</li><li>S->E at 232: Cytoplasmic. Partially nuclear; when associated with E-149</li></ul>									1
Q13285	2516	<ul><li>K->R at 119: Loss of sumoylation; when associated with R-194</li><li>K->R at 194: Loss of sumoylation</li><li>A->F at 269: Strongly reduced transactivation</li><li>G->E at 341: Reduced transactivation. Strongly reduced transactivation; when associated with F-344</li><li>L->F at 344: Reduced transactivation. Strongly reduced transactivation; when associated with E-341</li><li>A->F at 433: Strongly reduced transactivation</li><li>Y->F at 436: Loss of transactivation; when associated with A-440</li><li>K->A at 440: Loss of transactivation; when associated with F-436</li></ul>	sumoylation	GO:0016925							1
Q13315	472	<ul><li>D->A at 2870: Loss of kinase activity</li><li>N->K at 2875: Loss of kinase activity</li></ul>			kinase activity	GO:0016301					1
Q13352	23421	<ul><li>L->A at 9: Decreased interaction with nuclear receptors</li><li>S->A at 28: Loss of repressor function</li><li>Missing at 63-66: Abolishes localization to nucleus</li><li>KRK->AAA at 63-65: Abolishes localization to nucleus</li><li>L->R at 89: Abolishes dimerization, but not interactions with nuclear receptors; when associated with R-96</li><li>L->R at 96: Abolishes dimerization, but not interactions with nuclear receptors; when associated with R-89</li><li>LKAIL->AKAAA at 172-176: Abolishes interaction with nuclear receptors</li></ul>	localization	GO:0051179			nucleus	GO:0005634			1
Q13363	1487	<ul><li>C->A at 134: Strongly reduces E1A binding; when associated with A-138; A-141 and A-150</li><li>N->A at 138: Strongly reduces E1A binding; when associated with A-134; A-141 and A-150</li><li>RR->AA at 141-142: Strongly reduces E1A binding; when associated with A-163 and A-171</li><li>R->A at 141: Strongly reduces E1A binding; when associated with A-134; A-138 and A-150</li><li>L->A at 150: Strongly reduces E1A binding; when associated with A-134; A-138 and A-141</li><li>R->A at 163: Strongly reduces E1A binding; when associated with A-141; A-142 and A-171</li><li>R->A at 171: Strongly reduces E1A binding; when associated with A-141; A-142 and A-163</li><li>G->V at 181: Strongly reduces E1A binding; when associated with V-183 and A-204</li><li>G->V at 183: Strongly reduces E1A binding; when associated with V-181 and A-204</li><li>D->A at 204: Strongly reduces E1A binding; when associated with V-181 and V-183</li><li>R->A at 266: Strongly reduces E1A binding; when associated with A-290; A-295 and A-315</li><li>D->A at 290: Strongly reduces E1A binding; when associated with A-266; A-295 and A-315</li><li>E->A at 295: Strongly reduces E1A binding; when associated with A-266; A-290 and A-315</li><li>H->A at 315: Strongly reduces E1A binding; when associated with A-266; A-290 and A-295</li><li>S->A at 422: Abolishes phosphorylation by HIPK2 and prevents UV-induced clearance</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488			Q9H2X6		1
Q13418	3611	<ul><li>H->D at 99: Alters interaction with LIMS1</li><li>E->K at 359: Inactivation of ILK</li></ul>							<li>Q3SWY2</li><li>P57044</li><li>Q5R5V4</li><li>P48059</li><li>Q13418</li>		1
Q13426	7518	<ul><li>K->R at 140: No change in sumoylation</li><li>K->R at 210: Abolishes sumoylation. No nuclear location. 5-fold decrease in recombination efficiency</li></ul>	sumoylation	GO:0016925							1
Q13439	2803	<ul><li>Y->A at 2177: Abolishes Golgi localization</li><li>Y->F at 2177: No effect</li><li>V->A at 2181: Abolishes Golgi localization</li><li>F->A at 2183: Abolishes Golgi localization</li><li>M->A at 2186: Abolishes Golgi localization</li><li>T->A at 2193: Abolishes Golgi localization</li><li>M->A at 2194: Abolishes Golgi localization</li><li>V->A at 2197: Abolishes Golgi localization</li><li>I->A at 2198: Abolishes Golgi localization</li><li>L->A at 2202: Abolishes Golgi localization</li><li>F->A at 2204: Abolishes Golgi localization</li><li>I->A at 2212: Abolishes Golgi localization</li></ul>	localization	GO:0051179							1
Q13464	6093	<ul><li>D->A at 1113: Abolishes cleavage by caspase-3</li></ul>									1
Q13501	8878	<ul><li>K->A at 7: Loss of interactions with PRKCZ, PRCKI and NBR1. Loss of dimerization; when associated with A-69</li><li>Y->F at 9: No effect on interaction with LCK</li><li>K->A at 13: No effect on interaction with PRKCI</li><li>RR->AA at 21-22: Loss of interaction with PRKCI. Alters dimerization</li><li>Y->A at 67: No effect on interaction with PRKCZ</li><li>D->A at 69: No effect on interactions with PRKCZ, PRKCI and NBR1. Loss of dimerization; when associated with A-7</li><li>D->A at 71: No effect on interaction with PRKCI</li><li>D->A at 73: No effect on interactions with PRKCZ and PRKCI</li><li>D->A at 80: No effect on interaction with PRKCI</li><li>E->A at 82: No effect on interaction with PRKCI</li><li>L->V at 398: No effect on polyubiquitin-binding</li><li>F->V at 406: Loss of polyubiquitin-binding</li><li>L->V at 413: No effect on polyubiquitin-binding</li><li>L->V at 417: Loss of polyubiquitin-binding</li><li>I->V at 431: Partial loss of polyubiquitin-binding</li></ul>			binding	GO:0005488			<li>Q5RC94</li><li>Q5R4K9</li><li>P41743</li><li>Q5PXS1</li><li>P42683</li><li>P06239</li><li>Q14596</li><li>Q95KR7</li><li>O19111</li><li>Q05513</li>		1
Q13522	5502	<ul><li>T->A at 35: No activity</li><li>T->D at 35: 1000-fold reduction in activity, inhibits equally PP1 and PP2A</li></ul>							<li>P80074</li><li>P48488</li><li>Q63447</li><li>Q06009</li><li>Q61041</li><li>P50391</li><li>P30366</li><li>P23696</li><li>Q9ZSE4</li><li>P48487</li><li>P22198</li>		1
Q13526	5300	<ul><li>Y->A at 23: Reduced affinity for MPHOSPH1</li></ul>									1
Q13535	545	<ul><li>K->R at 2327: Abolishes kinase activity</li><li>D->A at 2475: Abolishes kinase activity; increases sensitivity to IR and impairs translocation to nuclear foci upon DNA damage</li><li>D->E at 2494: Abolishes kinase activity; reduces cell viability, augments sensitivity to IR and UV</li></ul>			kinase activity	GO:0016301					1
Q13546	8737	<ul><li>K->A at 45: Abolishes kinase activity</li><li>D->K at 324: Abolishes cleavage by caspase-8</li></ul>			kinase activity	GO:0016301					1
Q13547	3065	<ul><li>Missing at 391-482: Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes</li><li>S->A at 421: Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes</li><li>S->D,E at 421: Slightly decreases deacetylase activity</li><li>S->A at 423: Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes</li><li>S->D,E at 423: Decreases deacetylase activity</li><li>E->A at 424: Slightly decreases deacetylase activity, no effect on interaction with NuRD and SIN3 complexes</li><li>E->A at 425: No effect on deacetylase activity, no effect on interaction with NuRD and SIN3 complexes</li><li>E->A at 426: Decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes</li></ul>			deacetylase activity	GO:0019213			P22579		1
Q13564	8883	<ul><li>D->A at 331: Impairs the formation of the NEDD8-UBA3 thioester</li></ul>							<li>P31252</li><li>Q15843</li><li>Q5R4A0</li><li>Q9SHE7</li><li>P0C031</li><li>Q4PLJ0</li><li>P0C030</li><li>P61282</li><li>Q8TBC4</li><li>Q99344</li><li>P0C032</li>		1
Q13569	6996	<ul><li>R->A at 281: Restores the DNA-binding ability of the sumoylated form</li><li>E->Q at 310: Restores the DNA-binding ability of the sumoylated form</li><li>F->A at 315: Restores the DNA-binding ability of the sumoylated form</li></ul>			DNA-binding	GO:0003677					1
Q13572	3705	<ul><li>K->A at 18: Loss of kinase activity</li><li>H->A at 58: No effect</li><li>K->A at 59: Loss of kinase activity</li><li>R->A at 106: Loss of kinase activity</li><li>K->A at 157: Loss of kinase activity</li><li>H->Q at 162: Loss of kinase activity</li><li>G->A,P at 163: Loss of kinase activity</li><li>G->A at 163: No effect</li><li>H->A,Q at 167: Loss of kinase activity</li><li>Q->A at 188: No effect</li><li>H->A at 193: Loss of kinase activity</li><li>K->A at 199: Loss of kinase activity</li><li>R->A at 212: Loss of kinase activity</li><li>S->A at 214: Loss of kinase activity</li><li>L->A at 215: No effect</li><li>D->A at 281: Loss of kinase activity</li><li>D->A at 295: Loss of kinase activity</li><li>N->A,L at 297: Loss of kinase activity</li><li>N->D at 297: Induces a strong reduction in kinase activity</li><li>G->A at 301: Loss of kinase activity</li></ul>			kinase activity	GO:0016301					1
Q13574	8525	<ul><li>TA->NS at 1115-1116: Loss of interaction with SNTG1</li></ul>							Q9NSN8		1
Q13586	6786	<ul><li>D->A,N at 76: Increases Ca(2+) influx even when Ca(2+) stores are not depleted</li><li>D->N at 78: Increases Ca(2+) influx even when Ca(2+) stores are not depleted</li><li>E->A,Q at 87: Increases Ca(2+) influx through activation of CRAC channels, even when Ca(2+) stores are not depleted</li></ul>									1
Q13614	8898	<ul><li>C->S at 417: Loss of activity</li><li>D->A at 419: No effect</li><li>D->A at 422: Loss of activity</li><li>L->Y at 607: Reduces homodimerization and interaction with SBF1</li></ul>							O95248		1
Q13615	8897	<ul><li>C->S at 413: Loss of activity</li></ul>									1
Q13617	8453	<ul><li>K->R at 621: No effect on conjugation with NEDD8</li><li>K->R at 689: Loss of conjugation with NEDD8</li><li>K->R at 719: No effect on conjugation with NEDD8</li></ul>	conjugation	GO:0000746					<li>Q15843</li><li>Q9SHE7</li><li>P0C031</li><li>Q4PLJ0</li><li>P0C030</li><li>P61282</li><li>P0C032</li>		1
Q13619	8451	<ul><li>LYQAV->AAAAA at 86-90: Largely reduces interaction with DDB1; abolishes interaction with DDB2</li><li>WQDH->AADA at 139-142: Largely reduces interaction with DDB1; abolishes interaction with DDB2</li></ul>							<li>Q16531</li><li>Q6QNU4</li><li>Q92466</li><li>Q6E7D1</li><li>P33194</li>		1
Q13625	7159	<ul><li>W->K at 1098: Loss of interaction with APC2</li></ul>							<li>Q9UJX6</li><li>Q8BZQ7</li><li>Q12440</li><li>P02655</li><li>P34514</li>		1
Q13636	11031	<ul><li>Q->L at 64: No change in GTPase activity</li></ul>			GTPase activity	GO:0003924					1
Q13637	10981	<ul><li>T->N at 39: Decreased GTP-binding activity</li><li>Q->L at 85: No change in GTPase activity</li><li>A->F at 185: Abolishes binding to protein kinase A type II regulatory subunit</li><li>L->P at 188: Abolishes binding to protein kinase A type II regulatory subunit</li></ul>			<li>binding</li><li>GTPase activity</li><li>GTP-binding</li>	<li>GO:0005488</li><li>GO:0003924</li><li>GO:0005525</li>			<li>Q9RI12</li><li>Q05608</li>		1
Q13671	9610	<ul><li>S->A at 351: Abolishes phosphorylation by PKD and the interaction with 14-3-3 proteins</li></ul>	phosphorylation	GO:0016310					<li>Q15139</li><li>O96436</li>		1
Q13772	8031	<ul><li>LL->AA at 95-96: Decreased interaction with PPAR and RXR</li></ul>			RXR	GO:0004886			Q07869		1
Q13794	5366	<ul><li>L->A at 29: Reduced interaction with BAX</li><li>L->E at 29: Loss of interaction with MCL1 and of increased MCL1 degradation; when associated with E-32 and E-32</li><li>F->E at 32: Loss of interaction with MCL1 and of increased MCL1 degradation; when associated with E-29 and E-36</li><li>F->I at 32: Alters specificity of protein interaction and enhances pro-apoptotic activity; when associated with E-35</li><li>K->E at 35: Alters specificity of protein interaction and enhances pro-apoptotic activity; when associated with I-32</li><li>L->E at 36: Loss of interaction with MCL1 and of increased MCL1 degradation; when associated with E-29 and E-32</li></ul>							<li>Q07815</li><li>Q8HYS5</li><li>Q07812</li><li>Q07814</li><li>Q07820</li><li>O02703</li><li>P55269</li><li>Q7YRZ9</li>		1
Q13825	549	<ul><li>K->N at 105: Abolishes RNA-binding; when associated with E-109 and Q-113</li><li>K->E at 109: Abolishes RNA-binding; when associated with N-105 and Q-113</li><li>K->Q at 113: Abolishes RNA-binding; when associated with N-105 and E-109</li></ul>			RNA-binding	GO:0003723					1
Q13838	7919	<ul><li>C->A at 198: No effect on ATPase activity</li></ul>			ATPase activity	GO:0016887					1
Q13882	5753	<ul><li>W->A at 44: Strong decrease in STAP2 phosphorylation</li><li>Y->A at 66: Decrease in STAP2 phosphorylation</li><li>R->L at 105: Decrease in STAP2 phosphorylation</li><li>K->M at 219: Abolishes kinase activity and cell transformation, and no more phosphorylation of STAP2</li><li>Y->F at 447: Decrease in transforming potential and increase in the kinase activity level</li></ul>	phosphorylation	GO:0016310	kinase activity	GO:0016301			Q9UGK3		1
Q13888	2966	<ul><li>C->A at 291: Reconstituted TFIIH complex lacks p62 and has no transcriptional activity</li><li>C->A at 308: Reconstituted TFIIH complex lacks p62 and has no transcriptional activity</li><li>C->A at 345: No effect on the transcriptional activity of the reconstituted TFIIH complex</li><li>C->A at 360: No effect on the transcriptional activity of the reconstituted TFIIH complex</li><li>C->A at 363: No effect on the transcriptional activity of the reconstituted TFIIH complex</li><li>H->A at 376: No effect on the transcriptional activity of the reconstituted TFIIH complex</li><li>H->A at 380: No effect on the transcriptional activity of the reconstituted TFIIH complex</li><li>C->A at 382: No effect on the transcriptional activity of the reconstituted TFIIH complex</li></ul>							<li>Q9JGK8</li><li>Q8JJX0</li><li>Q8QZ72</li><li>O90371</li><li>P09592</li><li>P03315</li><li>P89946</li><li>P03316</li><li>Q9FKA4</li><li>Q8QL52</li><li>P13890</li><li>Q5WQY5</li><li>Q306W7</li><li>P19109</li><li>P49847</li><li>P13897</li><li>Q5Y388</li><li>P27285</li><li>P36331</li><li>P36332</li><li>P27284</li><li>P08491</li><li>P36330</li><li>Q306W5</li><li>P36329</li><li>Q5XXP3</li><li>Q80S27</li><li>Q8JUX5</li><li>P08768</li><li>Q86925</li><li>O90369</li><li>P22056</li><li>P05674</li><li>Q4QXJ7</li>		1
Q13936	775	<ul><li>E->K at 363: Loss of selectivity for divalent over monovalent cations</li><li>G->F at 954: Affects voltage-dependent inhibition by dihydropyridines; when associated with I-958</li><li>Y->I at 958: Affects voltage-dependent inhibition by dihydropyridines; when associated with F-954</li><li>E->K at 1135: Loss of selectivity for divalent over monovalent cations</li><li>E->K at 1464: Loss of selectivity for divalent over monovalent cations</li></ul>									1
Q13948	1523	<ul><li>Y->L at 624: Retained in the endoplasmic reticulum</li><li>H->L at 629: No effect on subcellular location</li></ul>					endoplasmic reticulum	GO:0005783			1
Q14012	8536	<ul><li>K->A at 49: Loss of activity</li><li>T->A at 177: Loss of activation by CaMKK1</li><li>T->D at 177: Partial activation in absence of CAMKK1</li></ul>							<li>Q8VBY2</li><li>P97756</li><li>Q8N5S9</li>		1
Q14019	23406	<ul><li>K->A at 75: Abolishes actin-binding activity</li><li>K->A at 130: No effect on 5LO-binding activity</li><li>K->A at 131: Abolishes 5LO-binding activity</li><li>K->E at 131: Abolishes 5LO-binding activity</li><li>K->R at 131: No effect on 5LO-binding activity</li></ul>			binding	GO:0005488			<li>Q92192</li><li>Q92193</li><li>P53499</li><li>P26183</li><li>P53498</li><li>O13419</li><li>Q9P4D1</li><li>P48465</li><li>P53455</li><li>Q39596</li><li>Q39758</li><li>P26182</li><li>P80709</li><li>Q9UVX4</li><li>O17320</li><li>P53689</li><li>P78711</li><li>P30161</li><li>P17128</li><li>P12527</li><li>P45521</li><li>P45520</li><li>P20904</li><li>P81085</li><li>Q6TCF2</li><li>Q99023</li><li>Q75D00</li><li>P51775</li><li>P10365</li><li>P60011</li><li>P60010</li><li>Q8SWN8</li><li>O16808</li><li>P02577</li><li>P10989</li><li>P68555</li><li>Q05214</li><li>Q8X119</li><li>O65316</li><li>O65315</li><li>O65314</li><li>P53491</li><li>P91754</li><li>P13363</li><li>P09917</li><li>P11426</li><li>O81221</li><li>Q11212</li><li>P50138</li><li>P53477</li><li>P53476</li><li>P51399</li><li>P60009</li><li>P53502</li><li>Q2U7A3</li><li>P53500</li><li>Q9UVZ8</li><li>P48999</li><li>P14235</li><li>O00937</li><li>Q9UVF3</li><li>Q24733</li><li>P90689</li><li>P24902</li><li>O74258</li>		1
Q14028	1258	<ul><li>L->E at 226: Loss of calcium/calmodukin modulation</li></ul>									1
Q14032	570	<ul><li>C->A at 235: Abolishes activity</li><li>C->S at 235: Lowers N-acyltransferase activity; enhanced thioesterase activity presumably dependent on the formation of a bile acid-enzyme covalent intermediate via a thioester bond</li><li>D->A at 328: Abolishes activity</li><li>H->A at 362: Abolishes activity</li><li>C->A at 372: Retains activity</li><li>Q->K at 417: Translocation to peroxisomes</li></ul>					peroxisomes	GO:0005777	<li>P05521</li><li>Q9S3Z2</li><li>P19197</li><li>P21309</li><li>P23148</li><li>Q06878</li><li>Q7N576</li><li>P41302</li><li>Q9AJA7</li>		1
Q14108	950	<ul><li>L->A,G,D,V at 475: Prevents the targeting of the protein to lysosomes</li><li>L->I at 475: Some loss in the efficiency of targeting of the protein to lysosomes</li><li>I->A,V at 476: Does not prevent the targeting of the protein to lysosomes completely</li><li>I->D,E,G at 476: Prevents the targeting of the protein to lysosomes</li><li>I->L at 476: Normal targeting of the protein to lysosomes</li><li>R->A,E,G,K,Q at 477: Normal targeting of the protein to lysosomes</li><li>T->G,I,S,V at 478: Normal targeting of the protein to lysosomes</li></ul>					lysosomes	GO:0005764			1
Q14145	9817	<ul><li>IEG->AAA at 125-127: Increases ubiquitination and proteolytic degradation</li><li>C->S at 151: Constitutive repression of NFE2L2-dependent gene expression. Promotes increased degradation of NFE2L2. Resistance of ubiquitination of PGAM5 to inhibition by oxidative stress and sulforaphane</li><li>YQI->AAA at 162-164: Increases ubiquitination and proteolytic degradation</li><li>C->S at 273: Abolishes repression of NFE2L2-dependent gene expression. Slows down degradation of NFE2L2</li><li>C->S at 288: Abolishes repression of NFE2L2-dependent gene expression. Slows down degradation of NFE2L2</li><li>L->A at 308: Loss of export from nucleus; when associated with A-310</li><li>L->A at 310: Loss of export from nucleus; when associated with A-308</li><li>Y->A at 334: Loss of interaction with NFE2L2. Strongly reduces repression of NFE2L2-dependent gene expression. Loss of interaction with PGAM5</li><li>R->A at 380: Loss of interaction with NFE2L2. Abolishes repression of NFE2L2-dependent gene expression</li><li>N->A at 382: Loss of interaction with NFE2L2. Strongly reduces repression of NFE2L2-dependent gene expression</li><li>R->A at 415: Loss of interaction with NFE2L2. Abolishes repression of NFE2L2-dependent gene expression. Loss of interaction with PGAM5</li><li>H->A at 436: Loss of interaction with NFE2L2. Abolishes repression of NFE2L2-dependent gene expression</li><li>F->A at 478: Abolishes repression of NFE2L2-dependent gene expression</li><li>R->A at 483: Loss of interaction with NFE2L2. Abolishes repression of NFE2L2-dependent gene expression. Loss of interaction with PGAM5</li><li>Y->A at 525: Loss of interaction with NFE2L2. Strongly reduces repression of NFE2L2-dependent gene expression</li><li>Y->A at 572: Loss of interaction with NFE2L2. Strongly reduces repression of NFE2L2-dependent gene expression. Loss of interaction with PGAM5</li></ul>	export from nucleus	GO:0051168					Q16236		1
Q14164	9641	<ul><li>K->A at 38: Loss of kinase activity</li><li>E->A at 168: Slight decrease of kinase activity</li><li>S->A at 172: Loss of autophosphorylation and of kinase activity</li><li>S->E at 172: Decrease in kinase activity</li></ul>	autophosphorylation	GO:0046777	kinase activity	GO:0016301					1
Q14185	1793	<ul><li>YI->AA at 1401-1402: Abolishes Rac GEF activity</li><li>ISP->AAA at 1487-1489: Abolishes Rac GEF activity</li></ul>							<li>Q9NR83</li><li>P31750</li>		1
Q14190	6493	<ul><li>R->A,G at 367: Reduced nuclear translocation</li><li>K->A at 368: No effect on nuclear translocation</li><li>L->A at 369: No effect on nuclear translocation</li><li>V->A at 370: No effect on nuclear translocation</li><li>K->A at 371: No effect on nuclear translocation</li><li>P->A at 372: No effect on nuclear translocation</li><li>K->A,G at 373: Reduced nuclear translocation</li><li>T->A at 375: No effect on nuclear translocation</li><li>K->A at 376: No effect on nuclear translocation</li><li>M->A at 377: No effect on nuclear translocation</li><li>K->G at 378: No effect on nuclear translocation</li><li>T->A at 379: No effect on nuclear translocation</li><li>K->A at 380: No effect on nuclear translocation</li><li>L->A at 381: No effect on nuclear translocation</li><li>R->A at 382: No effect on nuclear translocation</li><li>T->A at 383: No effect on nuclear translocation</li><li>P->A at 385: Reduced nuclear translocation</li><li>Y->A at 386: Reduced nuclear translocation</li></ul>									1
Q14207	4863	<ul><li>V->A at 7: Impairs activation of histone gene transcription; when associated with A-10; A-11; A-15 and A-18</li><li>L->A at 10: Impairs activation of histone gene transcription; when associated with A-7; A-11; A-15 and A-18</li><li>V->A at 11: Impairs activation of histone gene transcription; when associated with A-7; A-10; A-15 and A-18</li><li>L->A at 15: Impairs activation of histone gene transcription; when associated with A-7; A-10; A-11 and A-18</li><li>E->A at 18: Impairs activation of histone gene transcription; when associated with A-7; A-10; A-11 and A-15</li><li>F->A at 27: Impairs activation of histone gene transcription; when associated with A-30</li><li>E->A at 30: Impairs activation of histone gene transcription; when associated with A-27</li><li>LFD->AAA at 331-333: Impairs activation of histone gene transcription. Impairs interaction with BZW1, RUVBL1, RUVBL2 and TRRAP</li><li>S->A at 775: Impairs activation of histone gene transcription; when associated with A-779; A-1100; A-1270 and A-1350</li><li>S->A at 779: Impairs activation of histone gene transcription; when associated with A-775; A-1100; A-1270 and A-1350</li><li>S->A at 1100: Impairs activation of histone gene transcription; when associated with A-775; A-779; A-1270 and A-1350</li><li>T->A at 1270: Impairs activation of histone gene transcription; when associated with A-775; A-779; A-1100 and A-1350</li><li>T->A at 1350: Impairs activation of histone gene transcription; when associated with A-775; A-779; A-1100 and A-1270</li></ul>	transcription	GO:0006350					<li>Q5ZLT7</li><li>Q12464</li><li>Q03940</li><li>Q7L1Q6</li><li>Q2TBU9</li><li>Q5R7L4</li><li>Q9Y230</li><li>Q9Y265</li><li>Q9Y4A5</li>		1
Q14242	6404	<ul><li>T->A at 44: No effect on L-selectin binding nor neutrophil rolling</li><li>YEYLDYD->FEFLDF at 46-52: No sulfation. Almost complete loss of P-selectin binding. No effect on E-selectin binding</li><li>YEYLDY->FEFLDF at 46-51: No sulfation. Almost complete loss of P-selectin binding. No effect on E-selectin binding</li><li>Y->F at 46: Binding L-selectin reduced by 20%, neutrophil recruitment reduced by 30%, and lymphocyte rolling reduced by 32%; when associated with F-48. Binding L-selectin reduced by 86%, neutrophil recruitment reduced by 75%, and lymphocyte rolling reduced by 69%; when associated with F-51. Binding L-selectin reduced by 89%, and neutrophil recruitment reduced by 90%; when associated with F-48 and F-51. Binding of L-selectin reduced by 91%; when associated with F-48; F-51 and A-57</li><li>Y->F at 48: Binding L-selectin reduced by 20%, neutrophil recruitment reduced by 30%, and lymphocyte rolling reduced by 32%; when associated with F-46. Binding L-lectin reduced by 31%, neutrophil recruitment reduced by 52%, and lymphocyte rolling reduced by 52%; when associated with F-51. Binding L-selectin reduced by 89%, and neutrophil recruitment reduced by 90%; when associated with F-46 and F-51. Binding of L-selectin reduced by 91%; when associated with F-46; F-51 and A-57</li><li>Y->F at 51: Binding L-selectin reduced by 86%, neutrophil recruitment reduced by 75% and, lymphocyte rolling reduced by 69%; when associated with F-46. Binding L-selectin reduced by 31%, neutrophil recruitment reduced by 52%, and lymphocyte rolling reduced by 52%; when associated with F-48; Binding L-selectin reduced by 89%, and neutrophil recruitment reduced by 90%; when associated with F-46 and F-48. Binding of L-selectin reduced by 91%; when associated with F-46; F-48 and A-57</li><li>T->A at 57: No E- nor P-selctin binding, and very little neutrophil rolling. Binding of L-selectin reduced by 91%; when associated with F-46; F-48 and F-51</li><li>C->A,S at 320: No dimer formation. No effect on P-selectin binding</li></ul>			binding	GO:0005488			<li>Q41114</li><li>P16349</li><li>P02871</li><li>P07386</li><li>P42088</li><li>P02873</li><li>P02874</li><li>P02875</li><li>P84987</li><li>P16352</li><li>P16108</li><li>P16351</li><li>P33888</li><li>P83511</li><li>P83410</li><li>P38662</li>		1
Q14289	2185	<ul><li>P->A at 859: Loss of interaction with nephrocystin</li></ul>									1
Q14315	2318	<ul><li>M->D at 2669: Abolishes dimerization</li></ul>									1
Q14344	10672	<ul><li>C->S at 14: Fails to localize to plasma membranes and failed to activate Rho-dependent serum response factor-mediated transcription and actin stress fiber formation</li><li>C->S at 18: Fails to localize to plasma membranes and failed to activate Rho-dependent serum response factor-mediated transcription and actin stress fiber formation</li><li>T->A at 203: Abolishes phosphorylation by PKA; disrupts heterotrimer stability</li></ul>	<li>phosphorylation</li><li>transcription</li>	<li>GO:0016310</li><li>GO:0006350</li>	PKA	GO:0004691	<li>stress fiber</li><li>plasma membranes</li>	<li>GO:0001725</li><li>GO:0005886</li>	<li>P26183</li><li>Q9P4D1</li><li>P48465</li><li>P53455</li><li>Q06447</li><li>Q39596</li><li>P26182</li><li>Q39758</li><li>P80709</li><li>Q9UVX4</li><li>O17320</li><li>P78711</li><li>P17128</li><li>P45521</li><li>P45520</li><li>Q99023</li><li>Q9JM73</li><li>P35359</li><li>P17593</li><li>P10989</li><li>P17594</li><li>P91754</li><li>P11426</li><li>O81221</li><li>P53477</li><li>P53476</li><li>P56466</li><li>P60009</li><li>P53502</li><li>P53500</li><li>P11831</li><li>O00937</li><li>P14235</li><li>Q9UVF3</li><li>O51891</li><li>O74258</li><li>O67031</li><li>Q92192</li><li>P53499</li><li>Q92193</li><li>P53498</li><li>P51489</li><li>O13419</li><li>P0AG30</li><li>P0AG31</li><li>P0AG32</li><li>P0AG33</li><li>P53689</li><li>P30161</li><li>P20904</li><li>P81085</li><li>Q6TCF2</li><li>Q75D00</li><li>P51775</li><li>P10365</li><li>P60011</li><li>P44619</li><li>P60010</li><li>O16808</li><li>Q8SWN8</li><li>P52156</li><li>P02577</li><li>P52155</li><li>P52158</li><li>P52157</li><li>P57652</li><li>P52152</li><li>P68555</li><li>P52154</li><li>O83281</li><li>P52153</li><li>P15409</li><li>Q05214</li><li>Q8X119</li><li>O65316</li><li>O65315</li><li>O65314</li><li>P03304</li><li>P53491</li><li>P20350</li><li>P13363</li><li>Q11212</li><li>P50138</li><li>P23790</li><li>Q89A22</li><li>P45835</li><li>Q90718</li><li>Q2U7A3</li><li>Q03222</li><li>Q9UVZ8</li><li>P38527</li><li>P33561</li><li>Q24733</li><li>P90689</li><li>P24902</li><li>P66028</li><li>P66029</li><li>Q9ZLS9</li><li>P0A296</li><li>P0A295</li><li>P29403</li><li>Q9ZD24</li>		1
Q14376	2582	<ul><li>S->A at 132: Loss of activity</li><li>Y->F at 157: Loss of activity</li><li>C->Y at 307: No effect on activity towards UDP-galactose. Loss of activity towards UDP-N-acetylgalactosamine</li></ul>									1
Q14393	2621	<ul><li>R->E at 353: Strongly reduced affinity for AXL. Abolishes phosphorylation of AXL</li><li>K->E at 355: Strongly reduced affinity for AXL. Abolishes phosphorylation of AXL</li><li>F->A at 530: Decreases activation of AXL</li><li>L->A at 663: Reduces affinity for AXL 15-fold and decreases activation of AXL</li><li>Y->A at 703: Reduces affinity for AXL 3-fold</li></ul>	phosphorylation	GO:0016310					P30530		1
Q14444	4076	<ul><li>R->A at 612: Major reduction in MYC and CCND2 RNA-binding; when associated with A-633 and A-690</li><li>R->A at 633: Major reduction in MYC and CCND2 RNA-binding; when associated with A-612 and A-690</li><li>R->A at 690: Major reduction in MYC and CCND2 RNA-binding; when associated with A-612 and A-633</li></ul>			RNA-binding	GO:0003723			<li>P01110</li><li>P30279</li><li>Q9MZT9</li><li>Q9MZT7</li><li>Q9MZT8</li><li>P10395</li><li>Q9MZT6</li><li>Q28566</li><li>P68272</li><li>P68271</li><li>P12523</li><li>P22555</li><li>P01109</li><li>P01106</li><li>P49032</li><li>P49033</li><li>Q28350</li><li>Q2HJ27</li><li>Q9MZU0</li><li>Q17103</li><li>P06646</li><li>Q29031</li><li>P49706</li><li>P0C0N8</li><li>P49709</li><li>P23583</li><li>P06295</li><li>P21438</li><li>P0C0N9</li>		1
Q14493	7884	<ul><li>Missing at 230-270: Decrease in 3' end processing efficiency</li></ul>									1
Q14512	9982	<ul><li>C->A at 214: Strongly reduces interaction with FGF2</li></ul>							<li>P20003</li><li>P09038</li><li>P48798</li><li>P48800</li><li>P48799</li><li>P03969</li><li>Q60487</li>		1
Q14524	6331	<ul><li>Q->K at 1476: Induces accelerated recovery from channel fast inactivation</li><li>P->A at 1974: Strongly reduces interaction with NEDD4, NEDD4L or WWP2</li><li>P->A at 1975: Strongly reduces interaction with NEDD4, NEDD4L or WWP2</li><li>S->A at 1976: Strongly reduces interaction with NEDD4, NEDD4L or WWP2</li><li>Y->A at 1977: Strongly reduces interaction with NEDD4, NEDD4L or WWP2</li><li>D->A at 1978: No effect on interaction with NEDD4, NEDD4L or WWP2</li><li>S->A at 1979: No effect on interaction with NEDD4, NEDD4L or WWP2</li><li>V->A at 1980: No effect on interaction with NEDD4, NEDD4L or WWP2</li><li>V->D,R at 1980: Strongly reduces interaction with NEDD4L</li></ul>							<li>O00308</li><li>Q5RBF2</li><li>Q96PU5</li><li>P46934</li>		1
Q14526	3090	<ul><li>K->R at 333: Abolishes sumoylation; impairs transcriptional repression activity</li><li>E->A at 335: Impairs transcriptional repression activity</li><li>P->A at 336: Impairs K-333 acetylation; no effect on sumoylation</li></ul>	sumoylation	GO:0016925							1
Q14562	1659	<ul><li>K->E at 594: In GET; inhibition of pre-mRNA splicing and nuclear export of unspliced RNA</li><li>S->L at 717: In LAT; inhibition of pre-mRNA splicing and nuclear export of unspliced RNA</li></ul>	nuclear export	GO:0051168					<li>O43561</li><li>P41929</li>		1
Q14565	11144	<ul><li>E->A,Q at 258: Decreases octamer stability</li></ul>									1
Q14596	4077	<ul><li>K->A at 12: No effect on interaction with SQSTM1</li><li>D->R at 50: Loss of interaction with SQSTM1</li></ul>							<li>Q5RBA5</li><li>Q13501</li>		1
Q14644	22821	<ul><li>K->Q at 599: No binding to IP4 and loss of plasma membrane localization</li><li>K->Q at 600: No binding to IP4 and loss of plasma membrane localization</li><li>R->Q at 601: No binding to IP4 and loss of plasma membrane localization</li></ul>	localization	GO:0051179	binding	GO:0005488	plasma membrane	GO:0005886			1
Q14653	3661	<ul><li>KR->NG at 77-78: Abolishes nuclear localization</li><li>RK->LQ at 86-87: No effect on subcellular localization</li><li>IL->MM at 139-140: Abolishes nuclear export</li><li>SS->AA at 385-386: Complete loss of viral infection induced phosphorylation</li><li>S->A,D,E at 385: Complete loss of viral infection induced phosphorylation</li><li>S->A,D,E at 386: Complete loss of viral infection induced phosphorylation</li><li>SNSHPLSLTS->ANA at 396-405: Complete loss of viral infection induced phosphorylation</li><li>SNSHPLSLTS->DND at 396-405: Acts as a constitutively activated IRF3</li><li>SNS->ANA at 396-398: Complete loss of viral infection induced phosphorylation</li><li>SLTS->ALAA at 402-405: Complete loss of viral infection induced phosphorylation</li></ul>	<li>phosphorylation</li><li>nuclear export</li><li>localization</li>	<li>GO:0016310</li><li>GO:0051168</li><li>GO:0051179</li>					<li>Q4JF28</li><li>Q764M6</li><li>Q90643</li><li>Q14653</li>		1
Q14671	9698	<ul><li>NY->SN at 1043-1044: Changes the specificity for RNA; when associated with E-1047</li><li>Q->E at 1047: Changes the specificity for RNA; when associated with 1043-SN-1044</li></ul>									1
Q14674	9700	<ul><li>S->A at 1126: Abolishes phosphorylation at this site, as well as the negative regulation due to phosphorylation</li><li>EIMR->RIME at 1483-1486: Abolishes autocleavage; when associated with R-1178; E-1181; R-1207 and E-1210. Does not affect the protease function</li><li>R->A at 1486: Abolishes autocleavage; when associated with A-1181 and A-1210</li><li>EILR->RILE at 1503-1506: Does not affect autocleavage. Does not affect the protease function</li><li>R->A at 1506: Abolishes autocleavage; when associated with A-1161 and A-1210</li><li>ELLR->RLLE at 1532-1535: Strongly reduces autocleavage at this site, but enhances autocleavage at site 1. Does not affect the protease function</li><li>R->A at 1535: Abolishes autocleavage; when associated with A-1161 and A-1281</li><li>C->A at 2029: Abolishes protease activity</li></ul>	phosphorylation	GO:0016310					<li>P19028</li><li>Q9QBZ5</li><li>P24107</li><li>Q9QBZ1</li><li>Q79666</li><li>P15833</li><li>P03362</li><li>P18042</li><li>Q8AII1</li><li>P03363</li><li>P04024</li><li>P04023</li><li>P10978</li><li>O93215</li><li>P26810</li><li>Q1A249</li><li>P03356</li><li>P03355</li><li>O41798</li><li>P20892</li><li>Q9Y6I0</li><li>P10210</li><li>Q9QBY3</li><li>P03353</li><li>P16901</li><li>Q74120</li><li>Q09SZ9</li><li>Q89928</li><li>Q73368</li><li>P84454</li><li>Q9WC63</li><li>P20825</li><li>Q9IDV9</li><li>P0C211</li><li>P0C210</li><li>P51518</li><li>Q4U0X6</li><li>P12451</li><li>P07570</li><li>P28936</li><li>O89940</li><li>P24740</li><li>P26809</li><li>P26808</li><li>Q0R5R3</li><li>Q0R5R2</li><li>P18802</li><li>P10394</li><li>P19561</li><li>P16423</li><li>P63119</li><li>P19560</li><li>Q75002</li><li>P04589</li><li>P04587</li><li>P04588</li><li>Q9QSR3</li><li>O91080</li><li>P16046</li><li>P17757</li><li>P12497</li><li>P12499</li><li>P12498</li><li>P03311</li><li>P20875</li><li>P20876</li><li>P10273</li><li>Q9WC54</li><li>P10272</li><li>P10271</li><li>P10270</li><li>P19199</li><li>P05962</li><li>P18096</li><li>P10265</li><li>P04584</li><li>P11227</li><li>P04585</li><li>Q76634</li><li>Q8I7P9</li><li>Q9Q720</li><li>P14078</li><li>P31822</li><li>P11365</li><li>P35963</li><li>P14074</li><li>P05959</li><li>P63131</li><li>P04323</li><li>P10274</li><li>P21407</li><li>O89290</li><li>P35956</li><li>P05960</li><li>P05961</li><li>Q1A267</li><li>P63122</li><li>P63123</li><li>P63124</li><li>P63125</li><li>P63120</li><li>P63121</li><li>P03366</li><li>P03367</li><li>P03369</li><li>P63127</li><li>P63128</li><li>P63129</li><li>Q77373</li><li>P03370</li><li>P27502</li><li>P21414</li>		1
Q14676	9656	<ul><li>R->A at 58: Abrogates binding to the MRE11 complex and to CHEK2</li><li>S->A at 72: Abrogates binding to CHEK2</li><li>N->A at 96: Abrogates binding to CHEK2; when associated with A-97 and A-98</li><li>G->A at 97: Abrogates binding to CHEK2; when associated with A-96 and A-98</li><li>T->A at 98: Abrogates binding to CHEK2; when associated with A-96 and A-97</li></ul>			binding	GO:0005488			<li>Q9IAM7</li><li>P49959</li><li>Q9UVN9</li><li>P32829</li><li>O96017</li><li>Q9XGM2</li>		1
Q14677	9685	<ul><li>R->L at 29: Reduces lipid binding. Abolishes lipid binding; when associated with G-34</li><li>D->G at 34: Abolishes lipid binding; when associated with L-29</li><li>D->R at 349: Decreases AP-1 and AP-2 binding</li><li>D->R at 371: Slightly decreases AP-1 binding</li><li>D->R at 422: Strongly decreases clathrin binding</li><li>LFDL->AFAA at 423-426: Strongly reduces clathrin binding</li></ul>			<li>clathrin binding</li><li>binding</li><li>lipid binding</li>	<li>GO:0030276</li><li>GO:0005488</li><li>GO:0008289</li>			<li>P05549</li><li>P34056</li><li>Q9N0N3</li><li>P58197</li><li>P21525</li>		1
Q14680	9833	<ul><li>D->A at 150: Abolishes enzymatic activity</li><li>T->A at 345: No effect on interaction with PPP1R8</li><li>T->A at 387: No effect on interaction with PPP1R8</li><li>T->A at 409: No effect on interaction with PPP1R8</li><li>T->A at 415: No effect on interaction with PPP1R8</li><li>T->A at 428: No effect on interaction with PPP1R8</li><li>T->A at 446: Inhibits interaction with PPP1R8</li><li>T->A at 460: Inhibits interaction with PPP1R8</li><li>T->A at 466: Inhibits interaction with PPP1R8</li><li>T->A at 478: Strongly inhibits interaction with PPP1R8. Enhances enzymatic activity</li><li>T->A at 518: No effect on interaction with PPP1R8</li></ul>							<li>Q12972</li><li>Q28147</li>		1
Q14683	8243	<ul><li>S->A at 957: Reduces phosphorylation and the S-phase checkpoint activation. Abolishes S-phase activation; when associated with A-966</li><li>S->A at 966: Reduces phosphorylation and the S-phase checkpoint activation. Increases sensitivity to DNA methylation. Abolishes S-phase activation; when associated with A-957</li></ul>	<li>DNA methylation</li><li>phosphorylation</li><li>S-phase</li>	<li>GO:0006306</li><li>GO:0016310</li><li>GO:0051320</li>							1
Q14686	23054	<ul><li>TSPLLVNLLQSD->E at 883-894: Reduced binding to THRB, RXRA, ESR2 and ESR1</li><li>TSPLLVNLLQSD->N at 883-894: Reduced binding to THRB, RXRA, ESR2 and ESR1</li><li>TSPLLVNLLQSD->V at 883-894: Reduced binding to THRB, RXRA, ESR2 and ESR1</li><li>TS->SY at 883-884: Strong increase in binding to THRB, RXRA and ESR2, but dramatic decrease in binding to ESR1</li><li>SPLLVNLLQSD->NP at 884-894: Reduced binding to THRB, RXRA, ESR2 and ESR1</li></ul>			binding	GO:0005488			<li>Q91279</li><li>Q9XSW2</li><li>Q91250</li><li>Q29040</li><li>P38111</li><li>Q9YHT3</li><li>P50242</li><li>P50241</li><li>P50240</li><li>Q9PVE2</li><li>P06212</li><li>Q95171</li><li>Q53AD2</li><li>P49885</li><li>P49886</li><li>O13012</li><li>Q28571</li><li>Q9W6M2</li><li>P68306</li><li>P68305</li><li>O42132</li><li>Q9TV98</li><li>Q9QZJ5</li><li>P49884</li><li>P19793</li><li>Q9IAK1</li><li>P10828</li><li>Q9PTU5</li><li>Q91424</li><li>O93511</li><li>P16058</li><li>P03372</li><li>Q92731</li><li>Q9YH33</li><li>Q9PVZ9</li><li>Q9YH32</li><li>P37243</li><li>P57753</li><li>P57781</li><li>Q02965</li><li>P57782</li><li>Q9TU15</li><li>Q9XSB5</li><li>Q9YHZ7</li><li>Q9TTE5</li>		1
Q14694	9100	<ul><li>C->A at 424: Abolishes de-ubiquitinating activity</li></ul>									1
Q14697	23193	<ul><li>D->N at 542: Loss of activity</li></ul>									1
Q14699	23180	<ul><li>G->A at 2: Loss of association with membranes. Same effect; when associated with S-3</li><li>C->S at 3: Partially affects association with membranes. Loss of association with membranes; when associated with A-2</li></ul>					membranes	GO:0016020			1
Q14767	4053	<ul><li>DL->EIFP at 1449-1450: Gain-of-function. Forms a complex with TGFB1</li></ul>							<li>P54831</li><li>P09533</li><li>P18341</li><li>P50414</li><li>O19011</li><li>P09531</li><li>P07200</li><li>Q9Z1Y6</li><li>Q9PTQ2</li><li>O93449</li><li>P01137</li><li>Q38HS2</li>		1
Q14790	841	<ul><li>D->A at 73: Abolishes binding to FLASH. Induces NF-kappa-B activation</li></ul>			binding	GO:0005488			Q9UKL3		1
Q14814	4209	<ul><li>S->A at 180: Abolishes MAPK7- and EGF-mediated transcriptional activation</li><li>T->A at 286: Same transcriptional activity as for isoforms with beta domain</li><li>E->Q at 287: Abolishes transcriptional activity; when associated with N-288 and N-291</li><li>D->A at 288: Abolishes cleavage by caspase 7</li><li>D->N at 288: Abolishes transcriptional activity; when associated with Q-287 and N-291</li><li>H->A at 289: Same transcriptional activity as for isoforms with beta domain</li><li>D->N at 291: Abolishes transcriptional activity; when associated with Q-287 and N-288</li><li>S->A at 437: No effect on MAPK7- or EGF-mediated transcriptional activity</li><li>I->A at 438: Abolishes K-439 sumoylation</li><li>K->R at 439: Abolishes sumoylation and acetylation</li><li>S->A at 444: Abolishes K-439 sumoylation. Reduced neurotoxin-induced apoptosis of neuronal cells. More resistant to degradation</li><li>S->E at 444: No effect on K-439 sumoylation</li></ul>	<li>sumoylation</li><li>apoptosis</li>	<li>GO:0016925</li><li>GO:0006915</li>					<li>Q9BEA0</li><li>P26224</li><li>P01132</li><li>P01133</li><li>Q95ND4</li><li>Q13164</li><li>P83108</li><li>Q00968</li><li>P07522</li>		1
Q14974	3837	<ul><li>I->A at 178: Largely reduced binding to FxFG repeats and reduced nuclear import</li><li>I->F,D at 178: Loss of binding to FxFG repeats and reduced nuclear import</li></ul>	nuclear import	GO:0051170	binding	GO:0005488					1
Q149N8	257218	<ul><li>C->A at 1432: Abolishes E3 activity</li></ul>									1
Q15004	9768	<ul><li>I->A at 65: Loss of binding to PCNA</li><li>F->A at 68: Loss of binding to PCNA</li></ul>			binding	GO:0005488			<li>O16852</li><li>Q9HJQ0</li><li>Q6B6N4</li><li>Q8PX25</li><li>P61074</li><li>O29912</li><li>Q9DDF1</li><li>Q43124</li><li>Q57697</li><li>P18248</li><li>O02115</li><li>P53358</li><li>O01377</li><li>Q6LWJ8</li><li>Q9MAY3</li><li>Q00268</li><li>Q00265</li><li>Q8TUF7</li><li>Q9DEA3</li><li>P17070</li><li>O58398</li><li>Q9M7Q7</li><li>O10308</li><li>P31008</li><li>P17917</li><li>P61258</li><li>P17918</li><li>P11038</li><li>P15873</li><li>Q7T6Y0</li><li>Q03392</li><li>P22177</li><li>P04961</li><li>Q979S2</li><li>P57761</li><li>O73947</li><li>Q9W644</li><li>Q9UWR9</li><li>Q9PTP1</li><li>Q74MV1</li><li>Q8TWK3</li><li>O82134</li><li>Q9HN45</li><li>Q6KZF1</li><li>O82797</li><li>P12004</li><li>P24314</li><li>Q9UYX8</li><li>Q9P9H8</li><li>Q43266</li><li>O27367</li>		1
Q15014	9643	<ul><li>Missing at 132-136: Abrogates both transcriptional activation and repression by MORF4L2</li><li>L->A at 263: Abrogates both transcriptional activation and repression by MORF4L2</li></ul>							<li>Q5R905</li><li>Q15014</li><li>Q4R578</li>		1
Q15021	9918	<ul><li>RRTTRR->AATTAA at 1343-1348: Abolishes localization to the nucleus, while it only reduces chromosome binding</li><li>KKK->AAA at 1358-1360: Abolishes localization to the nucleus, while it only reduces chromosome binding</li></ul>	localization	GO:0051179	binding	GO:0005488	<li>chromosome</li><li>nucleus</li>	<li>GO:0005694</li><li>GO:0005634</li>			1
Q15027	9744	<ul><li>K->N at 274: Loss of binding to PIP2 and PIP3. Loss of association with endosomal tubules when coexpressed with PIP5K1C</li><li>R->Q at 448: Loss of GAP acitivity. No effect on GULP1 binding or association with endosomal tubules when coexpressed with PIP5K1C</li><li>S->A at 554: Loss of phosphorylation by PKB, interaction with ITGB1 and ITGB1-dependent cell migration</li><li>S->A at 724: Loss of phosphorylation at Ser-554, interaction with ITGB1 and ITGB1-dependent cell migration</li></ul>	<li>phosphorylation</li><li>cell migration</li>	<li>GO:0016310</li><li>GO:0016477</li>	binding	GO:0005488			<li>Q8INB9</li><li>P93004</li><li>P18168</li><li>Q92263</li><li>P53044</li><li>P31750</li><li>Q9GLP0</li><li>Q5PEA9</li><li>P74873</li><li>P47196</li><li>Q01314</li><li>P53712</li><li>P53713</li><li>P74851</li><li>P50904</li><li>P20936</li><li>P05556</li><li>P07228</li><li>Q92211</li><li>P52960</li><li>P09851</li><li>Q02574</li><li>P52488</li><li>Q5RCA9</li><li>O60331</li><li>P31749</li>		1
Q15036	9784	<ul><li>K->A at 62: No association with endosomes</li></ul>					endosomes	GO:0005768			1
Q15042	22930	<ul><li>R->A at 619: No effect</li><li>R->A at 700: No effect</li><li>R->A at 728: Loss of function</li><li>R->A at 753: No effect</li></ul>									1
Q15047	9869	<ul><li>CDC->LDP at 729-731: Abolishes methyltransferase activity</li><li>H->K at 1224: Abolishes methyltransferase activity</li><li>C->A at 1226: Abolishes methyltransferase activity</li><li>C->Y at 1279: Abolishes methyltransferase activity</li></ul>							<li>Q00020</li><li>P03588</li><li>P03589</li><li>Q83270</li><li>P28931</li><li>P06011</li><li>P17769</li><li>P20122</li><li>Q66121</li><li>O40976</li><li>P28726</li><li>P27752</li><li>Q83264</li>		1
Q15057	23527	<ul><li>R->Q at 442: Loss of GAP acitivity</li></ul>							<li>Q92263</li><li>P20936</li><li>Q92211</li><li>P09851</li><li>Q5PEA9</li><li>P74873</li><li>P74851</li><li>P50904</li>		1
Q15072	7705	<ul><li>K->R at 157: Induces a decrease in sumoylation. Induces a strong decrease but does not abolishes sumoylation; when associated with R-169</li><li>K->R at 169: Induces a decrease in sumoylation. Induces a strong decrease but does not abolishes sumoylation; when associated with R-157</li></ul>	sumoylation	GO:0016925							1
Q15075	8411	<ul><li>E->A at 39: Strongly reduces interaction with RAB5C</li><li>F->A at 41: Strongly reduces interaction with RAB5C</li><li>I->A at 42: Strongly reduces interaction with RAB5C</li><li>P->A at 44: Strongly reduces interaction with RAB5C</li><li>M->A at 47: Strongly reduces interaction with RAB5C</li><li>Y->A at 60: Strongly reduces interaction with RAB5C</li><li>W->A at 1349: Reduces phosphatidylinositol 3-phosphate binding and endosomal location</li><li>D->V at 1352: Reduces phosphatidylinositol 3-phosphate binding and endosomal location</li><li>N->D at 1357: Reduces phosphatidylinositol 3-phosphate binding and endosomal location</li><li>C->S at 1358: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location</li><li>F->A at 1365: Strongly reduces phosphatidylinositol 3-phosphate binding and endosomal location</li><li>VT->EE,GG at 1367-1368: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location</li><li>R->A at 1370: Abolishes endosomal location</li><li>R->A at 1371: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location</li><li>H->A at 1372: Abolishes endosomal location</li><li>H->A at 1373: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location</li><li>C->A at 1374: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location</li><li>R->G at 1375: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location</li><li>C->A at 1377: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location</li><li>G->A at 1378: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location</li><li>C->A at 1385: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location</li><li>R->G at 1400: Strongly reduces phosphatidylinositol 3-phosphate binding and abolishes endosomal location</li><li>C->S at 1405: Abolishes phosphatidylinositol 3-phosphate binding and endosomal location</li></ul>			phosphate binding	GO:0042301			<li>Q58DS9</li><li>P51147</li><li>P51148</li>		1
Q15078	8851	<ul><li>G->A at 2: Absent from the cell periphery</li></ul>									1
Q15080	4689	<ul><li>T->A at 154: Reduces phosphorylation</li><li>T->A at 211: No effect on phosphorylation</li><li>T->A at 251: No effect on phosphorylation</li><li>T->A at 274: No effect on phosphorylation</li><li>S->A at 315: Reduces phosphorylation</li><li>T->A at 327: No effect on phosphorylation</li></ul>	phosphorylation	GO:0016310							1
Q15125	10682	<ul><li>W->A at 68: Reduces catalytic activity to less than 35% of wild-type</li><li>I->A at 75: Reduces catalytic activity to less than 35% of wild-type</li><li>H->A at 76: Reduces catalytic activity to less than 10% of wild-type</li><li>E->A at 80: Reduces catalytic activity to less than 10% of wild-type</li><li>Y->W at 111: Reduces catalytic activity to less than 2% of wild-type</li><li>M->A at 121: Reduces catalytic activity to less than 35% of wild-type</li><li>M->V at 121: No effect on catalytic activity</li><li>E->A at 122: Reduces catalytic activity to less than 10% of wild-type</li><li>T->A at 125: Reduces catalytic activity to less than 10% of wild-type</li><li>Y->A at 188: Reduces catalytic activity to less than 35% of wild-type</li><li>F->A at 189: Reduces catalytic activity to less than 35% of wild-type</li><li>F->L at 189: No effect on catalytic activity</li><li>N->A at 193: Reduces catalytic activity to less than 10% of wild-type</li><li>W->A at 196: Reduces catalytic activity to less than 10% of wild-type</li></ul>			catalytic activity	GO:0003824					1
Q15139	5587	<ul><li>Y->E at 432: Decreased phosphorylation level when coexpressed with SRC in HeLa cells. Unchanged phosphorylation level when coexpressed with ABL</li><li>Y->F at 432: Decreased phosphorylation level when coexpressed with SRC in HeLa cells. Unchanged phosphorylation level when coexpressed with ABL. Unaltered kinase activity. Decreased kinase activity; when associated with F-463 and F-502</li><li>Y->E at 463: Constitutive activation and constitutive phosphorylation of S-738 and S-742</li><li>Y->F at 463: Decreased phosphorylation level when coexpressed with either SRC or ABL in HeLa cells. Decreased kinase activity</li><li>Y->E at 502: Loss of activation</li><li>Y->F at 502: Decreased phosphorylation level when coexpressed with SRC in HeLa cells. Unchanged phosphorylation level when coexpressed with ABL. Unaltered kinase activity. Decreased kinase activity; when associated with F-432 and F-502</li></ul>	phosphorylation	GO:0016310	kinase activity	GO:0016301			<li>P11681</li><li>P00521</li><li>Q00022</li><li>P00523</li><li>P12931</li><li>P10447</li><li>P00519</li>		1
Q15170	9338	<ul><li>SS->AA at 31-32: Slight decrease of transcriptional repression</li><li>SS->AA at 36-37: Loss of transcriptional repression</li><li>SS->AA at 41-42: No effect on transcriptional repression</li><li>SS->AA at 47-48: Slight decrease of transcriptional repression</li></ul>									1
Q15208	11329	<ul><li>T->A at 74: Decreases autophosphorylation and kinase activity. Reduced binding of S100B</li><li>K->A at 118: Loss of autophosphorylation and kinase activity</li><li>S->A at 281: Loss of autophosphorylation and kinase activity</li><li>T->A at 444: Decreases autophosphorylation and kinase activity</li></ul>	autophosphorylation	GO:0046777	<li>binding</li><li>kinase activity</li>	<li>GO:0005488</li><li>GO:0016301</li>			<li>P02638</li><li>Q6YNR6</li><li>P04271</li>		1
Q15287	10921	<ul><li>S->A at 53: Abolishes phosphorylation by CSNK2A1 and partially reduces splicing stimulation. Does not abolish interaction with CSNK2A1 and subcellular localization</li><li>S->E at 53: Partially reduces splicing stimulation. Does not abolish interaction with CSNK2A1 and subcellular localization</li><li>Y->A at 205: Abolishes exon-skipping</li><li>Y->A at 207: Abolishes exon-skipping</li></ul>	<li>phosphorylation</li><li>localization</li>	<li>GO:0016310</li><li>GO:0051179</li>					<li>P33674</li><li>P21868</li><li>P68399</li><li>P68400</li>		1
Q15303	2066	<ul><li>Y->A at 1035: No effect on interaction with WWOX. Abolishes interaction with WWOX; when associated with A-1301</li><li>Y->A at 1301: No effect on interaction with WWOX. Abolishes interaction with WWOX; when associated with A-1035</li></ul>							<li>Q5F389</li><li>Q5R9W5</li><li>Q9NZC7</li><li>Q9VLU5</li>		1
Q15386	9690	<ul><li>C->A at 1051: Loss of activity</li></ul>									1
Q15435	5510	<ul><li>D->V at 148: Completely abolishes the interaction with protein phosphatase 1</li><li>F->A at 170: Severely impaired the binding of protein phosphatase 1</li><li>E->A at 192: Completely abolishes the interaction with protein phosphatase 1</li><li>F->A at 214: Completely abolishes the interaction with protein phosphatase 1</li><li>D->A at 280: Severely impairs the binding of protein phosphatase 1</li><li>E->A at 300: Completely abolishes the interaction with protein phosphatase 1</li><li>W->A at 302: Completely abolishes the interaction with protein phosphatase 1</li><li>Y->A at 327: Completely abolishes the interaction with protein phosphatase 1</li></ul>			binding	GO:0005488			<li>Q5X1E5</li><li>Q7M7K5</li><li>Q7MAZ9</li><li>Q8XBL4</li><li>Q88A53</li><li>Q5P3T0</li><li>Q7MBF4</li><li>Q8Z3M9</li><li>Q5PC82</li><li>Q5ZRX9</li><li>Q821A6</li><li>Q87SK9</li><li>Q9JZ88</li><li>Q9CP21</li><li>Q82U82</li><li>Q9I5V3</li><li>Q5F8K9</li><li>Q63YC3</li><li>Q8Y395</li><li>Q6LV05</li><li>Q8ZLY4</li><li>Q6FA38</li><li>Q9PDL7</li><li>Q62EU1</li><li>Q9JUB2</li><li>Q5WT58</li><li>Q665U9</li><li>Q57JQ5</li><li>Q9KPC6</li><li>Q8P5D4</li><li>Q8CWL6</li><li>Q8PPG9</li><li>P06961</li><li>P45269</li><li>Q9L7A3</li><li>Q88QU2</li><li>Q6D160</li><li>Q8ZI64</li><li>Q60CQ4</li><li>Q87DS9</li><li>Q65Q41</li><li>Q5E2K7</li><li>Q8CXX6</li>		1
Q15464	6461	<ul><li>R->K at 435: Loss of interaction with CD3Z. Alters LAT, PLCG1, VAV1 and LCP2 phosphorylation, MAP kinase signaling, Rac1 and JNK activation, intracellular calcium increase, activation of the nuclear factor for activation of T-cells and subsequent interleukin-2 expression which normally occur upon T-cells stimulation</li></ul>	phosphorylation	GO:0016310			intracellular	GO:0005622	<li>P25782</li><li>P20963</li><li>P29329</li><li>P08487</li><li>P63001</li><li>Q9TUF8</li><li>P19174</li><li>Q9XSJ9</li><li>P40792</li><li>O43561</li><li>P41929</li><li>Q13094</li><li>Q966Y3</li><li>P15498</li><li>P92208</li><li>Q6RUV5</li>		1
Q15465	6469	<ul><li>C->S at 24: Abolishes palmitoylation</li></ul>									1
Q15545	6879	<ul><li>K->R at 5: Abolishes methylation in vitro</li></ul>									1
Q15596	10499	<ul><li>LL->AA at 644-645: By itself, does not affect nuclear receptor binding or transcriptional coactivation. Abrogates ligand-induced nuclear receptor binding and transactivation; when associated with 693-A-A-694 and 748-A-A-749</li><li>LL->AA at 693-694: By itself, does not affect nuclear receptor binding or transcriptional coactivation. Abrogates ligand-induced nuclear receptor binding and transactivation; when associated with 644-A-A-665 and 748-A-A-749</li><li>LL->AA at 748-749: By itself, does not affect nuclear receptor binding or transcriptional coactivation. Abrogates ligand-induced nuclear receptor binding and transactivation; when associated with 644-A-A-665 and 693-A-A-694</li><li>LLDQL->AADQA at 1079-1083: Reduces transcriptional coactivation and disrupts interaction with CREBBP/CBP</li><li>DQ->AA at 1081-1082: Has little effect on transcriptional coactivation</li></ul>			receptor binding	GO:0005102			<li>O42720</li><li>P0AEN0</li><li>P0AEM9</li><li>Q9NWQ8</li><li>Q39962</li><li>Q92793</li><li>P00303</li><li>Q61990</li>		1
Q15637	7536	<ul><li>KKR->EED at 15-17: Abolishes interaction with U2AF2</li><li>KRK->EDE at 16-18: Abolishes interaction with U2AF2</li><li>S->A at 20: Strongly decreases interaction with U2AF2 and spliceosome assembly</li><li>S->T at 20: Decreases interaction with U2AF2</li><li>R->A at 21: Decreases interaction with U2AF2 and spliceosome assembly</li><li>R->K at 21: No effect</li><li>W->A at 22: Abolishes interaction with U2AF2</li><li>W->F at 22: No effect</li><li>N->A at 151: Decreases RNA-binding</li><li>R->A at 160: Strongly reduces RNA-binding</li><li>K->A at 184: Abolishes RNA-binding</li><li>L->A at 244: Decreases RNA-binding</li><li>L->A at 247: Decreases RNA-binding</li><li>L->A at 254: Slightly decreases RNA-binding</li><li>R->A at 255: Slightly decreases RNA-binding</li></ul>	spliceosome assembly	GO:0000245	RNA-binding	GO:0003723			P26368		1
Q15642	9322	<ul><li>I->S at 454: Abrogates interaction with CDC42</li><li>L->S at 468: Impairs interaction with CDC42</li></ul>							<li>Q90694</li><li>O94103</li><li>O14426</li><li>P60953</li><li>Q17031</li><li>P60952</li><li>Q9HF56</li><li>P19073</li>		1
Q15648	5469	<ul><li>SQNPILTSLLQITG- at 599-612: Enhances interaction with ESR1</li><li>QNPILTSLLQITG-> at 600-612: Enhances interaction with ESR1</li><li>L->A at 604: Impairs interaction with ESR2; when associated with A-607; A-645 and A-648</li><li>LL->AA at 607-608: Impairs interaction with ESR1, PPARG, RXRA and THRB. Impairs interaction with THRA; when associated with 648-A-A-649</li><li>L->A at 607: Impairs interaction with ESR2; when associated with A-604; A-645 and A-648</li><li>TKNHPMLMNLLKDNP at 639-653: Enhances interaction with ESR1</li><li>L->A at 645: Impairs interaction with ESR2; when associated with A-604; A-607 and A-648</li><li>LL->AA at 648-649: Impairs interaction with ESR1, PPARG, THRB and VDR. Impairs interaction with THRA; when associated with 607-A-A-608</li><li>L->A at 648: Impairs interaction with ESR2; when associated with A-604; A-607 and A-645</li><li>T->A at 1032: Enhances protein stability; when associated with A-1457</li><li>T->A at 1457: Enhances protein stability; when associated with A-1032</li></ul>							<li>Q91279</li><li>O13124</li><li>Q9W6I9</li><li>Q9YHT3</li><li>P50242</li><li>P50241</li><li>O42450</li><li>O19052</li><li>P50240</li><li>Q95MH5</li><li>P06212</li><li>O18924</li><li>Q53AD2</li><li>P49885</li><li>O13012</li><li>P49886</li><li>Q9W6M2</li><li>O42295</li><li>Q9QZJ5</li><li>P57797</li><li>Q9PTU5</li><li>Q90382</li><li>O93511</li><li>P16058</li><li>Q92731</li><li>Q02777</li><li>Q9PVZ9</li><li>Q28037</li><li>Q9W6N4</li><li>Q4U3Q4</li><li>P57753</li><li>P49701</li><li>Q02965</li><li>Q9XSB5</li><li>Q9YHZ7</li><li>Q9TTE5</li><li>O18971</li><li>Q9XSW2</li><li>Q91250</li><li>Q29040</li><li>P38111</li><li>O57606</li><li>O97716</li><li>O62807</li><li>Q28570</li><li>P04625</li><li>O42392</li><li>Q9PVE2</li><li>Q95171</li><li>Q28571</li><li>P37231</li><li>P68306</li><li>O42132</li><li>P68305</li><li>Q9TV98</li><li>P49884</li><li>Q9IAK1</li><li>P19793</li><li>P10828</li><li>P10827</li><li>Q91424</li><li>P11473</li><li>P48281</li><li>P03372</li><li>P13053</li><li>Q9YH33</li><li>Q9YH32</li><li>P37243</li><li>P57781</li><li>P57782</li><li>Q9TU15</li><li>Q9PUA8</li>		1
Q15653	4793	<ul><li>S->A at 19: No degradation; when associated with A-23</li><li>S->A at 23: No degradation; when associated with A-19</li></ul>									1
Q15691	22919	<ul><li>KK->EE at 59-60: No effect</li><li>K->E at 89: Loss of binding to microtubules</li></ul>			binding	GO:0005488	microtubules	GO:0005874			1
Q15722	1241	<ul><li>T->P,A at 308: No effect on affinity for leukotriene B4, induces resistance to desensitization by GRK6, but minor effect on phosphorylation by GRK6</li><li>S->A at 310: No effect on affinity for leukotriene B4 or on desensitization by GRK6</li></ul>	phosphorylation	GO:0016310					P43250		1
Q15750	10454	<ul><li>D->A at 213: Loss of interaction with XIAP</li><li>F->A at 216: Loss of interaction with XIAP</li></ul>							P98170		1
Q15759	5600	<ul><li>T->A at 180: Inactivation</li><li>Y->F at 182: Inactivation</li></ul>									1
Q15768	1949	<ul><li>LW->YM at 124-125: Complete loss of Nipah protein G binding</li></ul>			binding	GO:0005488			<li>P62555</li><li>P62554</li>		1
Q15788	8648	<ul><li>LL->AA at 636-637: Slightly affects interactions with steroid receptors. Abolishes interactions with steroid receptors; when associated with A-693; A-694; A-752 and A-753</li><li>LL->AA at 693-694: Slightly affects interactions with steroid receptors. Abolishes interactions with steroid receptors; when associated with A-636; A-637; A-752 and A-753</li><li>K->R at 732: Abolishes sumoylation; when associated with R-774</li><li>LL->AA at 752-753: Slightly affects interactions with steroid receptors. Abolishes interactions with steroid receptors; when associated with A-636; A-637; A-693 and A-694</li><li>K->R at 774: Abolishes sumoylation; when associated with R-732</li><li>K->R at 800: Does not affect sumoylation of the protein</li><li>K->R at 846: Does not affect sumoylation of the protein</li><li>K->R at 1378: Does not affect sumoylation of the protein</li></ul>	sumoylation	GO:0016925							1
Q15796	4087	<ul><li>K->R at 19: Loss of acetylation</li><li>K->R at 20: No effect on acetylation</li><li>Missing at 221-225: Loss of binding to SMURF2</li><li>N->S at 381: Loss of binding to SARA</li></ul>			binding	GO:0005488			<li>O95405</li><li>Q9NR31</li><li>Q9HAU4</li>		1
Q15797	4086	<ul><li>G->S at 419: Loss of phosphorylation</li></ul>	phosphorylation	GO:0016310							1
Q15811	6453	<ul><li>M->L at 1369: Decreases specificity for CDC42; when associated with I-1376</li><li>L->I at 1376: Decreases specificity for CDC42; when associated with L-1369</li></ul>							<li>Q90694</li><li>O94103</li><li>O14426</li><li>P60953</li><li>Q17031</li><li>P60952</li><li>Q9HF56</li><li>P19073</li>		1
Q15831	6794	<ul><li>D->Y at 176: Loss of kinase activity</li><li>D->A at 194: Loss of kinase activity</li></ul>			kinase activity	GO:0016301					1
Q15843	4738	<ul><li>A->R at 72: Prevents adenylation by UBE1C</li></ul>							<li>Q5R4A0</li><li>Q8TBC4</li>		1
Q15848	9370	<ul><li>K->R at 33: No effect on formation of HMW multimers</li><li>C->S at 36: Impaired formation of MMW and HMW multimers</li><li>K->R at 65: Impaired formation of HMW multimers; when associated with R-68</li><li>K->R at 68: Impaired formation of HMW multimers; when associated with R-65</li><li>K->R at 77: Impaired formation of HMW multimers; when associated with R-101</li><li>K->R at 101: Impaired formation of HMW multimers; when associated with R-77</li></ul>									1
Q15910	2146	<ul><li>S->A at 21: Enhances methyltransferase activity towards 'Lys-27' of histone H3 and abrogates phosphorylation by PKB/AKT1</li><li>S->D at 21: Reduces methyltransferase activity towards 'Lys-27' of histone H3 and abrogates phosphorylation by PKB/AKT1</li><li>C->Y at 588: Strongly impairs methyltransferase activity towards 'Lys-27' of histone H3</li><li>H->A at 689: Abrogates methyltransferase activity</li></ul>	phosphorylation	GO:0016310					<li>P61835</li><li>P13345</li><li>P61834</li><li>P13344</li><li>P61833</li><li>Q98RY4</li><li>P61832</li><li>P03588</li><li>P61831</li><li>P03589</li><li>P61830</li><li>Q8INB9</li><li>Q38998</li><li>P07041</li><li>P02299</li><li>P28726</li><li>Q757N1</li><li>P61836</li><li>P23630</li><li>P05821</li><li>Q00020</li><li>P51728</li><li>Q03709</li><li>Q66121</li><li>Q7XYZ0</li><li>Q9T1X2</li><li>Q9U7D1</li><li>Q5DWI3</li><li>Q9P427</li><li>P83864</li><li>P90543</li><li>P10099</li><li>P08437</li><li>P31750</li><li>P15176</li><li>P47196</li><li>Q01314</li><li>Q8VYX2</li><li>P50564</li><li>Q83270</li><li>P28931</li><li>P06011</li><li>Q06196</li><li>P08898</li><li>Q9HDN1</li><li>P17769</li><li>P20122</li><li>P23753</li><li>O40976</li><li>Q2UCQ0</li><li>P80553</li><li>P40285</li><li>P84239</li><li>P84238</li><li>P27752</li><li>P84237</li><li>P31749</li><li>P84236</li><li>Q83264</li><li>P22843</li><li>P84235</li>		1
Q15942	7791	<ul><li>F->A at 71: Reduced interaction with ENAH and VASP</li><li>F->A at 93: Reduced interaction with ENAH and VASP</li><li>F->A at 104: Greatly reduced interaction with ENAH and VASP; when associated with A-71 or with A-71 and A-93</li><li>F->A at 114: No targeting to focal adhesions and reduced actin-rich structures; when associated with A-71; A-93 and A-104</li></ul>					focal adhesions	GO:0005925	<li>Q92192</li><li>Q92193</li><li>P53499</li><li>P26183</li><li>P53498</li><li>O13419</li><li>Q9P4D1</li><li>P48465</li><li>P53455</li><li>Q39596</li><li>Q39758</li><li>P26182</li><li>P80709</li><li>Q9UVX4</li><li>O17320</li><li>P53689</li><li>P78711</li><li>P30161</li><li>P17128</li><li>P45521</li><li>P20904</li><li>P45520</li><li>P81085</li><li>Q6TCF2</li><li>Q99023</li><li>Q75D00</li><li>P51775</li><li>P10365</li><li>P60011</li><li>P60010</li><li>Q8SWN8</li><li>O16808</li><li>P02577</li><li>P10989</li><li>P68555</li><li>Q05214</li><li>Q8X119</li><li>O65316</li><li>O65315</li><li>O65314</li><li>P53491</li><li>P91754</li><li>P13363</li><li>P11426</li><li>O81221</li><li>Q11212</li><li>P50138</li><li>P53477</li><li>P53476</li><li>P70460</li><li>P60009</li><li>P53502</li><li>Q2U7A3</li><li>Q2TA49</li><li>P53500</li><li>Q9UVZ8</li><li>P14235</li><li>O00937</li><li>Q9UVF3</li><li>Q24733</li><li>P90689</li><li>P24902</li><li>P50551</li><li>P50552</li><li>O74258</li><li>Q8N8S7</li>		1
Q16206	10495	<ul><li>M->A at 396: No effect on activity but response to capsaicin is lost</li><li>C->A at 505: No effect on activity</li><li>C->A at 510: Loss of activity</li><li>H->A at 546: Loss of activity</li><li>C->A at 558: Period length of activity extended to 42 minutes</li><li>H->A at 562: Loss of activity</li><li>C->A at 569: Loss of activity</li><li>C->A at 575: Period length of activity extended to 36 minutes</li><li>G->V at 592: Loss of activity</li><li>C->A at 602: Period length of activity extended to 36 minutes</li></ul>									1
Q16236	4780	<ul><li>T->A at 80: Loss of interaction with KEAP1</li></ul>							Q14145		1
Q16394	2131	<ul><li>Q->A,P at 27: No effect on heparan-sulfate biosynthesis</li><li>Missing at 27: No effect on heparan-sulfate biosynthesis</li><li>D->E at 164: Abolishes heparan-sulfate biosynthesis</li><li>Missing at 164: Abolishes heparan-sulfate biosynthesis</li><li>N->A at 316: No effect on heparan-sulfate biosynthesis</li><li>Missing at 316: No effect on heparan-sulfate biosynthesis</li><li>A->H at 486: No effect on heparan-sulfate biosynthesis</li><li>Missing at 486: No effect on heparan-sulfate biosynthesis</li><li>P->H at 496: No effect on heparan-sulfate biosynthesis</li><li>Missing at 496: No effect on heparan-sulfate biosynthesis</li></ul>	biosynthesis	GO:0009058							1
Q16512	5585	<ul><li>K->R at 644: Substantial reduction of autophosphorylation</li></ul>	autophosphorylation	GO:0046777							1
Q16531	1642	<ul><li>YLDN->ALAA at 316-319: Impairs interaction with DDA1</li><li>E->A at 537: Slightly impairs interaction with CUL4A</li><li>W->A at 561: Strongly impairs interaction with CUL4A</li><li>EAE->AAA at 840-842: Impairs interaction with AMBRA1, DTL, DET1, VPRBP, WDR22, WDR23 and WDR42A</li><li>MALY->AAAA at 910-913: Impairs interaction with AMBRA1, DTL and WDR22</li><li>W->A at 953: Impairs interaction with AMBRA1, ERCC8, WDR22 and WDR23</li></ul>							<li>P41596</li><li>Q96JK2</li><li>Q5BIM8</li><li>Q8TEB1</li><li>Q9ZNU6</li><li>Q13619</li><li>Q13216</li><li>Q5E9I8</li><li>P48732</li><li>Q7L5Y6</li>		1
Q16539	1432	<ul><li>A->V at 34: Lowered kinase activity</li><li>K->R at 53: Loss of kinase activity</li><li>Y->H at 69: Lowered kinase activity</li><li>D->A at 168: Loss of kinase activity</li><li>T->A at 175: Loss of kinase activity</li><li>D->A at 176: Emulation of the active state. Increase in activity; when associated with S-327 or L-327</li><li>D->A at 177: Loss of kinase activity</li><li>T->E at 180: Loss of kinase activity</li><li>Y->F at 182: Loss of kinase activity</li><li>A->T at 320: Lowered kinase activity</li><li>F->L at 327: Emulation of the active state. Increase in activity; when associated with A-176</li><li>F->S at 327: Emulation of the active state. Increase in activity; when associated with A-176</li><li>W->R at 337: Loss of kinase activity</li></ul>			kinase activity	GO:0016301					1
Q16555	1808	<ul><li>D->N at 71: Inhibits axon outgrowth formation in hippocampal neurons and decreases binding to CYFIP1</li><li>S->A at 507: No effect</li><li>T->A at 509: Greatly diminishes binding to 3F4 antibody</li><li>T->A at 512: No effect</li><li>T->A at 514: No effect</li><li>S->A at 517: No effect</li><li>S->A at 518: Greatly diminishes binding to 3F4 antibody</li><li>T->A at 521: No effect</li><li>S->A at 522: Greatly diminishes binding to 3F4 antibody</li></ul>			binding	GO:0005488	axon	GO:0030424			1
Q16566	814	<ul><li>S->A at 12: Loss of activity</li><li>S->A at 13: Loss of activity</li><li>FN->DD at 320-321: Loss of interaction with PPP2CA/PPP2CB</li></ul>							<li>P67774</li><li>P62714</li><li>P67777</li><li>P67776</li><li>P67775</li><li>P48463</li><li>P11611</li><li>P11493</li>		1
Q16584	4296	<ul><li>K->A at 144: Greatly reduced autophosphorylation activity</li><li>K->R at 144: Loss of kinase activity. Prevents activation of SAPK and MAPK14</li><li>E->A at 164: Greatly reduced autophosphorylation activity</li><li>T->A at 277: Severely reduced autophosphorylation activity. Prevents phosphorylation of SAPK and MAPK14</li><li>T->E at 277: No effect on SAPK activation</li><li>T->A at 278: No effect on autophosphorylation activity or activation of SAPK and MAPK14</li><li>S->A at 281: Reduced autophosphorylation activity. Reduced activation of SAPK and MAPK14</li><li>S->E at 281: No effect on SAPK activation</li></ul>	<li>phosphorylation</li><li>autophosphorylation</li>	<li>GO:0016310</li><li>GO:0046777</li>	<li>kinase activity</li><li>SAPK</li>	<li>GO:0016301</li><li>GO:0016909</li>			<li>Q95NE7</li><li>O02812</li><li>Q16539</li>		1
Q16595	2395	<ul><li>R->G at 53: Abolished cleavage of frataxin(81-210); when associated with G-54</li><li>R->G at 54: Abolished cleavage of frataxin(81-210) and allows the accumulation of frataxin(56-210); when associated with G-53</li><li>R->G at 79: Abolished cleavage of frataxin(81-210) and allows the accumulation of frataxin(56-210); when associated with G-80</li><li>K->G at 80: Abolished cleavage of frataxin(81-210); when associated with G-79</li></ul>									1
Q16611	578	<ul><li>H->A at 164: Strongly reduced zinc binding and homodimerization</li></ul>			zinc binding	GO:0008270					1
Q16630	11052	<ul><li>G->V at 86: Abolishes interaction with NUDT21/CPSF5; when associated with V-87</li><li>N->V at 87: Abolishes interaction with NUDT21/CPSF5; when associated with V-86</li></ul>							<li>Q3ZCA2</li><li>O43809</li><li>Q8VY81</li><li>Q5RAI8</li>		1
Q16644	7867	<ul><li>K->M at 73: Higher affinity toward PCH2</li></ul>							P38126		1
Q16649	4783	<ul><li>K->A at 330: Interacts with DR1 and partially affects transcriptional repression; when associated with E-332</li><li>K->E at 330: Does not interact with DR1 and drastically affects transcriptional repression; when associated with E-332</li><li>K->A at 332: Interacts with DR1 and partially affects transcriptional repression; when associated with E-330</li><li>K->E at 332: Does not interact with DR1 and drastically affects transcriptional repression; when associated with E-330</li></ul>							<li>Q5ZMV3</li><li>P04229</li><li>Q01658</li><li>P49592</li>		1
Q16658	6624	<ul><li>S->A at 39: Loss of phosphorylation</li></ul>	phosphorylation	GO:0016310							1
Q16665	3091	<ul><li>K->R at 377: No change in HIF1A protein turnover rate but increased transcriptional activity; when associated with R-391; R-477 and R-532</li><li>K->R at 389: No change in sumoylation</li><li>K->R at 391: Abolishes 1 sumoylation. Abolishes 1 sumoylation; when associated with R-532. Abolishes 2 sumoylations; when associated with R-477. No change in HIF1A protein turnover rate but increased transcriptional activity; when associated with R-377; R-477 and R-532</li><li>K->R at 392: No change in sumoylation</li><li>P->A at 394: No change in VHLE3-dependent ubiquitination</li><li>L->A at 397: Abolishes VHLE3-dependent ubiquitination; when associated with A-400</li><li>L->A at 400: Abolishes VHLE3-dependent ubiquitination; when associated with A-397</li><li>P->A at 402: Abolishes in VHLE3-dependent ubiquitination, abolishes oxygen-dependent regulation of VP16, partially reduced VHLE target site ubiquitination and no interaction with VHL. No VHLE target site ubiquitination; when associated with G-564</li><li>K->R at 442: No change in sumoylation</li><li>K->R at 460: No change in sumoylation nor in ARD1-mediated acetylation</li><li>K->R at 477: Abolishes 1 sumoylation. Abolishes 2 sumoylations; when asociated with R-391. No change in HIF1A protein turnover rate but increased transcriptional activity; when associated with R-377; R-391 and R-532</li><li>K->R at 532: Reduced ubiquitination. No change in sumoylation nor on interaction with ARD1A. No change in HIF1A protein turnover rate but increased transcriptional activity; when associated with R-377; R-391 and R-477. Complete loss of ubiquitination, but no change in VHL binding; when associated with K-538 and K-547</li><li>K->R at 538: No change in sumoylation, but reduced ubiquitination. Complete loss of ubiquitination, but no change in VHL binding; when associated with K-532 and K-547</li><li>K->R at 547: No change in sumoylation, but reduced ubiquitination. Complete loss of ubiquitination, but no change in VHL binding; when associated with K-532 and K-538</li><li>S->G at 551: Constitutive expression under nonhypoxic conditions by decreasing ubiquitination</li><li>T->A at 552: Constitutive expression under nonhypoxic conditions by decreasing ubiquitination</li><li>P->G at 564: No change in VHL-dependent ubiquitination. Partially reduced VHLE target site ubiquitination. No VHLE target site ubiquitination; when associated with A-402</li><li>K->T at 719: Dramatic reduction of accumulation in the nucleus in response to hypoxia</li><li>C->A at 800: Blocks increase in transcriptional activation caused by nitrosylation</li><li>C->S at 800: Abolishes hypoxia-inducible transcriptional activation of ctaD</li><li>N->A at 803: Recruits CREBBP. No enhancement of CREBBP by Clioquinol in the presence of FIH1. No change in nuclear location nor on repression of transcriptional activity in the presence of histone deacetylase inhibitor</li></ul>	<li>response to hypoxia</li><li>sumoylation</li>	<li>GO:0001666</li><li>GO:0016925</li>	binding	GO:0005488	nucleus	GO:0005634	<li>Q98SW2</li><li>Q79VD7</li><li>P24010</li><li>P41227</li><li>P36406</li><li>P50676</li><li>Q92793</li><li>Q05885</li><li>Q9XTA5</li><li>Q2KI14</li><li>P63852</li><li>Q73VC3</li><li>Q08855</li><li>P63853</li><li>Q6NFM3</li><li>Q9YIB9</li><li>P98005</li><li>O22446</li><li>Q5Q9Z2</li><li>P31833</li><li>P33517</li><li>Q338A9</li><li>Q04440</li><li>Q06473</li><li>Q8FMT1</li><li>P98059</li><li>P43066</li><li>Q309Z6</li><li>P16262</li><li>P07347</li><li>Q9NWT6</li><li>P40337</li><li>Q16665</li><li>Q92I67</li><li>P68335</li><li>Q0PGG7</li><li>Q12972</li><li>O54069</li><li>Q9CBQ5</li><li>O48707</li><li>Q00502</li><li>P68336</li>		1
Q16769	25797	<ul><li>R->W at 54: Lowers activity by approximately 30%: in dbSNP rsrs2255991</li><li>K->A at 144: Lowers activity by approximately 40%</li><li>F->A at 146: Lowers activity by approximately 30%</li><li>E->D,Q at 201: Abolishes activity</li><li>W->L at 207: Greatly lowers activity</li><li>D->A at 248: Abolishes activity</li><li>Q->L at 304: Lowers activity by approximately 35%</li><li>D->L at 305: Abolishes activity</li><li>F->A at 325: Greatly lowers activity</li><li>W->A at 329: Abolishes activity</li></ul>								rs2255991	1
Q16777	8338	<ul><li>S->A at 2: Blocks the inhibition of transcription by RPS6KA5/MSK1</li></ul>	transcription	GO:0006350					<li>P32048</li><li>Q5R4K3</li><li>Q5F3L1</li><li>O75582</li>		1
Q16851	7360	<ul><li>C->S at 123: No significant loss of activity</li><li>W->S at 218: No significant loss of activity</li><li>H->R at 266: No significant loss of activity</li><li>W->S at 333: Loss of activity; possibly due to folding defect</li><li>R->H at 389: No significant loss of activity</li><li>R->H at 391: Loss of activity; possibly due to folding defect</li><li>R->H at 422: No significant loss of activity</li><li>R->H at 445: No significant loss of activity</li></ul>									1
Q16878	1036	<ul><li>R->Q at 60: Reduces enzyme activity by 70%. Reduces iron and zinc incorporation by 50%</li><li>C->S at 93: Reduces enzyme activity and iron incorporation by 50%. Zinc incorporation increased by 20%</li><li>Y->F at 157: Almost total loss of enzyme activity and iron incorporation. Reduces zinc incorporation by 20%</li><li>C->S at 164: Reduces enzyme activity by 20%. Little effect on iron incorporation. No effect on zinc incorporation</li></ul>									1
Q2HXU8	387837	<ul><li>Y->F at 7: Abolishes tyrosine phosphorylation. Abolishes interaction with PTPN6 and PTPN11. Abolishes protection against natural killer cell-mediated cytotoxicity</li></ul>	<li>phosphorylation</li><li>natural killer cell-mediated cytotoxicity</li>	<li>GO:0016310</li><li>GO:0042267</li>					<li>P29350</li><li>Q90687</li><li>Q06124</li>		1
Q2M1K9	23090	<ul><li>N->A at 420: Abolishes the ability to bind promoter of BMP target genes; when associated A-426; A-452; A-458; A-491; A-497; A-528; A-534; A-574 and A-581</li><li>E->A at 426: Abolishes the ability to bind promoter of BMP target genes; when associated A-420; A-452; A-458; A-491; A-497; A-528; A-534; A-574 and A-581</li><li>T->A at 452: Abolishes the ability to bind promoter of BMP target genes; when associated A-420; A-426; A-458; A-491; A-497; A-528; A-534; A-574 and A-581</li><li>E->A at 458: Abolishes the ability to bind promoter of BMP target genes; when associated A-420; A-426; A-452; A-491; A-497; A-528; A-534; A-574 and A-581</li><li>D->A at 491: Abolishes the ability to bind promoter of BMP target genes; when associated A-420; A-426; A-452; A-458; A-497; A-528; A-534; A-574 and A-581</li><li>E->A at 497: Abolishes the ability to bind promoter of BMP target genes; when associated A-420; A-426; A-452; A-458; A-491; A-528; A-534; A-574 and A-581</li><li>T->A at 528: Abolishes the ability to bind promoter of BMP target genes; when associated A-420; A-426; A-452; A-458; A-491; A-497; A-534; A-574 and A-581</li><li>E->A at 534: Abolishes the ability to bind promoter of BMP target genes; when associated A-420; A-426; A-452; A-458; A-491; A-497; A-528; A-574 and A-581</li><li>F->A at 574: Abolishes the ability to bind promoter of BMP target genes; when associated A-420; A-426; A-452; A-458; A-491; A-497; A-528; A-534 and A-581</li><li>T->A at 581: Abolishes the ability to bind promoter of BMP target genes; when associated A-420; A-426; A-452; A-458; A-491; A-497; A-528; A-534 and A-574</li></ul>							P35855		1
Q2NKX8	54821	<ul><li>GKT->AAA at 127-129: Abolishes chromatin association</li><li>T->A at 1063: Induces a descrease in phosphorylation</li></ul>	phosphorylation	GO:0016310			chromatin	GO:0000785			1
Q38SD2	79705	<ul><li>K->A at 674: Loss of GTP/GDP-binding</li><li>K->G at 769: No effect on GTP-binding but reduction in subsequent stimulation of kinase activity</li><li>F->C at 1045: No effect on GTP-binding but loss of subsequent stimulation of kinase activity</li><li>K->W at 1293: Loss of autophosphorylation</li><li>I->T at 1435: No effect on GTP-binding but reduction in subsequent stimulation of kinase activity</li></ul>	autophosphorylation	GO:0046777	<li>kinase activity</li><li>GTP-binding</li><li>GDP-binding</li>	<li>GO:0016301</li><li>GO:0005525</li><li>GO:0019003</li>					1
Q3KR16	55200	<ul><li>N->A at 351: Loss of exchange activity</li></ul>									1
Q3V6T2	55704	<ul><li>S->A at 1417: Disrupts actin organization, cell migration and lamellipodia formation</li></ul>	cell migration	GO:0016477					<li>Q92192</li><li>Q92193</li><li>P53499</li><li>P26183</li><li>P53498</li><li>O13419</li><li>Q9P4D1</li><li>P48465</li><li>P53455</li><li>Q39596</li><li>Q39758</li><li>P26182</li><li>P80709</li><li>Q9UVX4</li><li>O17320</li><li>P53689</li><li>P78711</li><li>P30161</li><li>P17128</li><li>P45521</li><li>P45520</li><li>P20904</li><li>P81085</li><li>Q6TCF2</li><li>Q99023</li><li>Q75D00</li><li>P51775</li><li>P10365</li><li>P60011</li><li>P60010</li><li>Q8SWN8</li><li>O16808</li><li>P02577</li><li>P10989</li><li>P68555</li><li>Q05214</li><li>Q8X119</li><li>O65316</li><li>O65315</li><li>O65314</li><li>P53491</li><li>P91754</li><li>P13363</li><li>P11426</li><li>O81221</li><li>Q11212</li><li>P50138</li><li>P53477</li><li>P53476</li><li>P60009</li><li>P53502</li><li>Q2U7A3</li><li>P53500</li><li>Q9UVZ8</li><li>P14235</li><li>O00937</li><li>Q9UVF3</li><li>Q24733</li><li>P90689</li><li>P24902</li><li>O74258</li>		1
Q49MI3	375298	<ul><li>G->D at 260: Loss of nuclear localization; in isoform 2</li></ul>	localization	GO:0051179							1
Q4G0J3	51574	<ul><li>Y->D at 128: Loss of 7SK RNA-binding and marked decrease in 7SK RNP complex formation</li></ul>			RNA-binding	GO:0003723					1
Q4G163	286151	<ul><li>DS->AA at 75-76: Impairs ubiquitination and degradation in response to calcium</li><li>DS->AA at 333-334: Impairs ubiquitination and degradation in response to calcium</li></ul>									1
Q4J6C6	9581	<ul><li>H->A at 690: Loss of activity</li><li>H->A at 696: No effect</li></ul>									1
Q4U2R8	9356	<ul><li>L->A at 30: Complete loss of PAH transport activity</li><li>T->A at 36: Complete loss of PAH transport activity</li><li>N->Q at 39: Complete loss of PAH transport activity</li><li>Y->A at 230: Loss of membrane protein expression and little uptake of cidofovir</li><li>K->A at 431: Decrease in the level of membrane protein expression and 70 % loss of PAH uptake</li><li>F->A at 438: Decrease in the level of membrane protein expression, 70 % loss of PAH uptake, increased affinity for cidofovir, lower Vmax for PAH, and lower Km and Vmax for cidofovir</li></ul>	transport	GO:0006810					<li>Q04565</li><li>P17276</li><li>P16629</li><li>P24266</li><li>P30967</li><li>P90925</li><li>Q9A7V7</li><li>Q9KLB8</li><li>P43334</li><li>P00439</li><li>P04176</li><li>Q8XU39</li><li>P28991</li><li>Q98D72</li><li>P16331</li><li>Q07252</li>		1
Q504Q3	9924	<ul><li>D->A at 1087: Loss of exonuclease activity</li></ul>							<li>P20321</li><li>P00638</li><li>P03697</li>		1
Q53ET0	200186	<ul><li>S->A at 70: No effect on cAMP- and calcium-regulated phosphorylation</li><li>S->A at 171: Loss of cAMP- and calcium-regulated phosphorylation. Greatly reduced interaction with 14-3-3 proteins</li><li>S->A at 368: Reduced cAMP- and calcium-regulated phosphorylation</li><li>S->A at 393: No effect on cAMP- and calcium-regulated phosphorylation</li></ul>	phosphorylation	GO:0016310					O96436		1
Q53EZ4	55165	<ul><li>W->A at 184: Abolishes interaction with PDCD6IP</li><li>Y->A at 187: Abolishes interaction with PDCD6IP</li><li>D->A at 188: Diminishes interaction with PDCD6IP</li><li>R->A at 191: Abolishes interaction with PDCD6IP</li><li>E->A at 192: Abolishes interaction with PDCD6IP</li><li>S->A at 396: No effect on phosphorylation in mitotic cells</li><li>S->A at 425: Partial loss of phosphorylation in mitotic cells. Complete loss of phosphorylation in mitotic cells; when associated with A-428. Remains associated with the centrosome throughout mitosis; when associated with A-428. Arrests mitotic cells at the midbody stage; when associated with A-428 and A-436</li><li>S->A at 428: Partial loss of phosphorylation in mitotic cells. Complete loss of phosphorylation in mitotic cells; when associated with A-425. Remains associated with the centrosome throughout mitosis; when associated with A-425. Arrests mitotic cells at the midbody stage; when associated with A-425 and A-436</li><li>S->A at 436: No effect on phosphorylation in mitotic cells. Arrests mitotic cells at the midbody stage; when associated with A-425 and A-428</li></ul>	<li>phosphorylation</li><li>mitosis</li>	<li>GO:0016310</li><li>GO:0007067</li>			<li>centrosome</li><li>midbody</li>	<li>GO:0005813</li><li>GO:0030496</li>	Q8WUM4		1
Q53GL0	51177	<ul><li>K->C at 42: No effect on subcellular localization. No effect on subcellular localization; when associated with C-44. Disruption of membrane localization, loss of phospholipid binding and impaired interaction with CK2; when associated with W-123. Disruption of membrane localization, loss of phospholipid binding and impaired interaction with CK2; when associated with C-44 and W-123</li><li>R->C at 44: No effect on subcellular localization. No effect on subcellular localization; when associated with C-42. Disruption of membrane localization, loss of phospholipid binding and impaired interaction with CK2; when associated with W-123. Disruption of membrane localization, loss of phospholipid binding and impaired interaction with CK2; when associated with C-42 and W-123</li><li>W->A at 123: Disruption of membrane localization and impaired interaction with CK2. Loss of phospholipid binding; when associated with C-42. Loss of phospholipid binding; when associated with C-44. Disruption of membrane localization, loss of phospholipid binding and impaired interaction with CK2; when associated with C-42 and C-44</li><li>R->A at 133: No effect on binding to capping proteins and loss of phospholipid binding; when associated with A-135 and A-137</li><li>R->E at 133: No effect on binding to capping proteins; when associated with E-135</li><li>K->A at 135: No effect on binding to capping proteins; when associated with A-133 and A-137</li><li>K->E at 135: No effect on binding to capping proteins; when associated with E-133</li><li>R->A at 137: No effect on binding to capping proteins; when associated with A-133 and A-135</li><li>R->A at 155: No change in cell morphology and actin cytoskeleton. Great loss of binding to capping proteins; when associated with A-157. Great loss of binding to capping proteins; when associated with A-157 and A-159</li><li>R->E at 155: No change in cell morphology and actin cytoskeleton. Great loss of binding to capping proteins and no change in cell morphology and actin cytoskeleton; when associated with E-157</li><li>R->A at 157: No change in cell morphology and actin cytoskeleton. Great loss of binding to capping proteins; when associated with A-155. Great loss of binding to capping proteins; when associated with A-155 and A-159</li><li>R->E at 157: No change in cell morphology and actin cytoskeleton. Great loss of binding to capping proteins and no change in cell morphology and actin cytoskeleton; when associated with E-155</li><li>K->A at 159: Great loss of binding to capping proteins; when associated with A-155 and A-157</li></ul>	localization	GO:0051179	<li>phospholipid binding</li><li>binding</li>	<li>GO:0005543</li><li>GO:0005488</li>	<li>membrane</li><li>cytoskeleton</li>	<li>GO:0016020</li><li>GO:0005856</li>	<li>Q92192</li><li>Q92193</li><li>P53499</li><li>P26183</li><li>P53498</li><li>O13419</li><li>Q9P4D1</li><li>P48465</li><li>P53455</li><li>Q39596</li><li>Q39758</li><li>P26182</li><li>P80709</li><li>Q9UVX4</li><li>P43893</li><li>O17320</li><li>P53689</li><li>P78711</li><li>P30161</li><li>P17128</li><li>P45521</li><li>P45520</li><li>P20904</li><li>P81085</li><li>Q6TCF2</li><li>Q99023</li><li>Q75D00</li><li>P51775</li><li>P10365</li><li>P60011</li><li>P60010</li><li>Q8SWN8</li><li>O16808</li><li>P02577</li><li>P10989</li><li>P68555</li><li>Q05214</li><li>Q8X119</li><li>O65316</li><li>O65315</li><li>O65314</li><li>P53491</li><li>P91754</li><li>P13363</li><li>P11426</li><li>O81221</li><li>Q11212</li><li>P50138</li><li>P53477</li><li>P53476</li><li>P60009</li><li>P53502</li><li>Q2U7A3</li><li>P53500</li><li>Q9UVZ8</li><li>P14235</li><li>O00937</li><li>Q9UVF3</li><li>Q24733</li><li>P90689</li><li>P24902</li><li>Q65ZV5</li><li>O51759</li><li>O74258</li>		1
Q53GQ0	51144	<ul><li>V->W at 196: No effect</li><li>F->A at 234: Allows the conversion of androstenedione to testosterone</li></ul>									1
Q53H47	6419	<ul><li>N->S at 210: Reduces activity in double strand break repair</li><li>D->S at 248: Reduces activity in double strand break repair</li><li>D->S at 490: Reduces activity in double strand break repair</li></ul>	double strand break repair	GO:0006302							1
Q53HL2	55143	<ul><li>S->A at 165: Results in reduction but not abolition of phosphorylation</li></ul>	phosphorylation	GO:0016310							1
Q53HV7	23583	<ul><li>N->A at 85: Markedly impaired the damage-excising activity for U/G, hoU/G, hmU/A and fU/A. No cytosine-excising activity for C/G, C/A, C/T and C/C</li><li>G->A,S at 87: Impaired the damage-excising activity for U/G, hoU/G, hmU/A and fU/A</li><li>G->F at 87: No damage-excising activity</li><li>F->A,G,S at 89: Did not impair the damage-excising activity for U/G, hoU/G, hmU/A and fU/A</li><li>G->A at 90: Lost the damage-excising activity for U/G and retained a weak but significant activity for hoU/G, hmU/A and fU/A</li><li>M->A at 91: Did not impair the damage-excising activity for U/G, hoU/G, hmU/A and fU/A</li><li>F->L at 98: Impaired the damage-excising activity for U/G, hoU/G, hmU/A and fU/A</li><li>N->D at 163: Impaired the damage-excising activity for U/G, hoU/G, hmU/A and fU/A. No cytosine-excising activity for C/G, C/A, C/T and C/C. hoC-excising activity for hoC/A, hoC/T and hoC/C</li><li>H->L,N at 239: Markedly impaired the damage-excising activity for U/G, hoU/G, hmU/A and fU/A</li></ul>									1
Q53RT3	151516	<ul><li>D->A,E at 212: Abolishes production of active form of enzyme</li></ul>									1
Q59H18	51086	<ul><li>K->R at 591: Loss of autophosphorylation activity</li></ul>	autophosphorylation	GO:0046777							1
Q5FVE4	81616	<ul><li>H->R at 511: Results in a shift of the pH optimum to a more acidic pH without affecting substrate specificity</li></ul>									1
Q5FWF5	114799	<ul><li>C->G at 622: No effect on association with chromosomes</li></ul>					chromosomes	GO:0005694			1
Q5H9F3	63035	<ul><li>DL->AS at 623-624: Strongly reduced repressor activity. Interferes with CTBP1 binding</li></ul>			binding	GO:0005488			Q13363		1
Q5JRX3	10531	<ul><li>E->Q at 107: Loss of function</li><li>C->S at 119: Still active under oxidizing conditions</li></ul>									1
Q5KSL6	139189	<ul><li>Y->F at 78: Induces a strong reduction in phosphorylation but is still sensitive to H(2)O(2)</li><li>Y->F at 1075: Does not affect phosphorylation</li></ul>	phosphorylation	GO:0016310							1
Q5MNZ9	55062	<ul><li>RR->AA at 226-227: Loss of binding to phosphoinositides, does not disrupt the MPR pathway</li></ul>			binding	GO:0005488			O00264		1
Q5SQ64	259215	<ul><li>Y->F at 281: No phosphorylation. No interaction with GRB2 and GRB7. No phosphorylation increase of p42/44 MAP kinase</li></ul>	phosphorylation	GO:0016310					<li>P46672</li><li>Q5R4J7</li><li>Q07883</li><li>P62993</li><li>Q9SB81</li><li>Q8NFH3</li><li>Q27272</li><li>Q1RMW5</li><li>Q14451</li>		1
Q5SW96	26119	<ul><li>F->A at 165: Abolishes LDLR cytoplasmic tail binding</li><li>F->V at 165: Abolishes LDLR cytoplasmic tail binding</li><li>LL->AA at 212-213: Abolishes clathrin binding</li><li>D->A at 214: Abolishes clathrin binding</li><li>E->A at 216: Abolishes clathrin binding</li><li>R->A at 266: Abolishes AP-2 complex binding</li></ul>			<li>clathrin binding</li><li>binding</li>	<li>GO:0030276</li><li>GO:0005488</li>			<li>P05549</li><li>P01130</li><li>P34056</li><li>Q9N0N3</li><li>P01131</li><li>Q28832</li><li>P58197</li><li>P35950</li><li>P20063</li>		1
Q5SXM2	6621	<ul><li>Q->A at 94: Abolishes SNAPC5 binding in the absence of SNAPC1. Minimal effect on SNAPC5 binding in the presence of SNAPC1</li><li>Q->L at 94: Abolishes SNAPC5 binding in the absence of SNAPC1. Minimal effect on SNAPC5 binding in the presence of SNAPC1</li><li>Q->L at 115: Abolishes SNAPC5 binding in the absence of SNAPC1. Minimal effect on SNAPC5 binding in the presence of SNAPC1</li><li>L->A at 1314: Abolishes SNAPC2-binding</li><li>L->A at 1355: Abolishes SNAPC2-binding</li><li>L->A at 1362: Abolishes SNAPC2-binding</li><li>L->A at 1364: Abolishes SNAPC2-binding</li><li>L->A at 1369: Decreased binding to SNAPC2</li></ul>			binding	GO:0005488			<li>Q4R6W9</li><li>Q16533</li><li>Q13487</li><li>O75971</li>		1
Q5T0N5	54874	<ul><li>MGD->IST at 441-443: Impairs interaction with CDC42 and reduces CDC42-induced actin assembly</li><li>W->K at 576: Impairs interaction with WASL and reduces CDC42-induced actin assembly</li></ul>							<li>Q92192</li><li>Q92193</li><li>P53499</li><li>P26183</li><li>P53498</li><li>O13419</li><li>Q9P4D1</li><li>P48465</li><li>P53455</li><li>Q39596</li><li>Q39758</li><li>P26182</li><li>P80709</li><li>Q9UVX4</li><li>O17320</li><li>P53689</li><li>P78711</li><li>Q17031</li><li>P30161</li><li>P17128</li><li>Q9HF56</li><li>P45521</li><li>P81085</li><li>P20904</li><li>P45520</li><li>Q6TCF2</li><li>Q99023</li><li>Q75D00</li><li>O00401</li><li>P51775</li><li>P10365</li><li>P60011</li><li>P60010</li><li>Q8SWN8</li><li>O16808</li><li>P02577</li><li>P10989</li><li>P68555</li><li>Q05214</li><li>Q8X119</li><li>O65316</li><li>O65315</li><li>O65314</li><li>P53491</li><li>P91754</li><li>P13363</li><li>P11426</li><li>P60953</li><li>P60952</li><li>O81221</li><li>Q11212</li><li>P50138</li><li>P53477</li><li>P53476</li><li>O94103</li><li>Q90694</li><li>P60009</li><li>P53502</li><li>Q2U7A3</li><li>P53500</li><li>Q9UVZ8</li><li>P14235</li><li>O00937</li><li>Q9UVF3</li><li>O14426</li><li>Q24733</li><li>P90689</li><li>P24902</li><li>O74258</li><li>Q95107</li><li>P19073</li>		1
Q5T230	8433	<ul><li>L->P at 296: Abolishes coactivation activity; when associated with P-303</li><li>L->P at 303: Abolishes coactivation activity; when associated with P-296</li></ul>									1
Q5T2T1	143098	<ul><li>L->S at 38: Abolishes interaction with DLG1</li><li>L->S at 95: Does not affect the interaction with DLG1</li></ul>							Q12959		1
Q5T5U3	57584	<ul><li>Y->A at 999: Altered interaction with ARF1 and loss of association to membranes</li><li>I->A at 1053: Altered interaction with ARF1 and loss of association to membranes</li><li>R->A at 1183: Loss of GTPase activity and loss of function</li></ul>			GTPase activity	GO:0003924	membranes	GO:0016020	<li>Q8L7G0</li><li>P84080</li><li>P36397</li><li>Q94650</li><li>P22274</li><li>P11076</li><li>P49076</li><li>P61210</li><li>O23778</li><li>O48649</li><li>Q96361</li><li>Q75A26</li><li>P61209</li><li>P51821</li><li>Q25761</li><li>P51822</li><li>P84077</li><li>Q4R5P2</li>		1
Q5T6X5	222545	<ul><li>S->A at 149: Loss of function</li><li>T->A at 172: Loss of function</li></ul>									1
Q5TA45	54973	<ul><li>E->Q at 203: Abolishes the ability of the Integrator complex to process U1 and U2 snRNA genes</li></ul>									1
Q5TCZ1	9644	<ul><li>R->A at 42: Loss of binding to (PtdIns(3)P) and (PtdIns(3,4)P2)</li><li>R->A at 93: Loss of binding to (PtdIns(3)P) and (PtdIns(3,4)P2)</li></ul>			binding	GO:0005488					1
Q5U5Q3	51320	<ul><li>G->D at 343: Prevents RNA binding</li></ul>			RNA binding	GO:0003723					1
Q5VT06	9857	<ul><li>LL->AA at 762-763: Abolishes recruitment of PPARA to specific nuclear foci. No effect on interaction with PPARA (in vitro)</li></ul>							<li>O35507</li><li>Q95N78</li><li>Q8HYL6</li><li>Q07869</li>		1
Q5VT25	8476	<ul><li>K->A at 106: Loss of kinase activity</li><li>S->L at 222: Increase in autophosphorylation but not kinase activity</li><li>S->A at 234: Loss of autophosphorylation and kinase activity</li><li>T->A at 240: Loss of autophosphorylation and kinase activity</li><li>T->A at 403: Loss of autophosphorylation and kinase activity</li><li>H->A at 1579: Loss of CDC42 binding; when associated with A-1582</li><li>H->A at 1582: Loss of CDC42 binding; when associated with A-1579</li></ul>	autophosphorylation	GO:0046777	<li>binding</li><li>kinase activity</li>	<li>GO:0005488</li><li>GO:0016301</li>			<li>Q90694</li><li>O94103</li><li>O14426</li><li>P60953</li><li>Q17031</li><li>P60952</li><li>Q9HF56</li><li>P19073</li>		1
Q5VTD9	8328	<ul><li>N->S at 290: Prevents DNA-binding</li></ul>			DNA-binding	GO:0003677					1
Q5VWG9	83860	<ul><li>W->R at 23: Loss of interaction with TAF10</li></ul>							<li>Q12962</li><li>Q12030</li>		1
Q5VWQ8	153090	<ul><li>KKK->AAA at 228-230: No effect on binding to MAP3K5</li><li>KKKK->AAAA at 281-284: Significantly reduced binding to MAP3K5</li><li>R->L at 413: No effect on binding to MAP3K5</li></ul>			binding	GO:0005488			Q99683		1
Q63HR2	23371	<ul><li>C->S at 231: Abolishes inhibition of AKT1 kinase activity</li></ul>							P31750		1
Q66K89	1877	<ul><li>C->S at 194: Increases DNA-binding; when associated with S-197</li><li>C->S at 197: Increases DNA-binding; when associated with S-194</li><li>H->A at 210: Alters DNA-binding</li><li>R->L at 237: Alters DNA-binding; when associated with N-238</li><li>H->N at 238: Alters DNA-binding; when associated with L-237</li><li>K->M at 249: Alters DNA-binding; when associated with S-250</li><li>C->S at 250: Alters DNA-binding; when associated with M-249</li></ul>			DNA-binding	GO:0003677					1
Q684P5	23108	<ul><li>S->A at 7: Abolishes phosphorylation by PKG/PRKG1</li><li>N->A at 357: Abolishes GAP activity</li></ul>	phosphorylation	GO:0016310	PKG	GO:0004692			<li>P20936</li><li>P21136</li><li>Q92211</li><li>P00516</li><li>Q13976</li><li>Q92263</li><li>P09851</li><li>Q5PEA9</li><li>O77676</li><li>P74873</li><li>P14619</li><li>P74851</li><li>P50904</li>		1
Q68CJ9	84699	<ul><li>R->A at 361: Decreases proteolytic cleaveage upon ER stress</li></ul>					ER	GO:0005783			1
Q68EM7	55114	<ul><li>R->A at 288: Loss of function; leading to defects in tight junction maintenance</li></ul>					tight junction	GO:0005923			1
Q69383		<ul><li>SEM->AAA at 4-6: No loss of function</li><li>RRR->AAA at 13-15: Total loss of function and dominant negative effect</li><li>R->A at 13: Total loss of function and dominant negative effect; when associated with A-14; A-16; A-18 and A-20</li><li>R->A at 14: Total loss of function and dominant negative effect; when associated with A-13; A-16; A-18 and A-20</li><li>R->A at 16: Total loss of function and dominant negative effect; when associated with A-13; A-14; A-18 and A-20</li><li>R->A at 18: Total loss of function and dominant negative effect; when associated with A-13; A-14; A-16 and A-20</li><li>NR->AA at 19-20: No loss of function</li><li>R->A at 20: Total loss of function and dominant negative effect; when associated with A-13; A-14; A-16 and A-18</li><li>MVT->AAA at 30-32: Total loss of function and dominant negative effect</li><li>MKL->AAA at 37-39: Total loss of function and dominant negative effect</li><li>TKK->AAA at 42-44: Total loss of function and dominant negative effect</li><li>PTW->AAA at 48-50: Total loss of function and dominant negative effect</li><li>LKK->AAA at 53-55: Total loss of function and dominant negative effect</li><li>L->A at 53: Exclusive nuclear localization; when associated with A-56 and A-59</li><li>L->A at 56: Exclusive nuclear localization; when associated with A-53 and A-59</li><li>LAT->AAA at 59-61: Partial loss of function</li><li>L->A at 59: Exclusive nuclear localization; when associated with A-53 and A-56</li><li>NTK->AAA at 66-68: Total loss of function and dominant negative effect</li><li>MLL->AAA at 76-78: Total loss of function and dominant negative effect</li><li>MIV->AAA at 82-84: Total loss of function and dominant negative effect</li><li>MVS->AAA at 86-88: Partial loss of function</li><li>NSS->AAA at 93-95: No loss of function</li></ul>	localization	GO:0051179							1
Q69YH5	157313	<ul><li>VTF->ATA at 394-396: Abolishes interaction with PPP1CC but not subcellular location</li></ul>							<li>P36873</li><li>P61287</li><li>Q8MJ46</li>		1
Q6DJT9	5324	<ul><li>RK->AA at 23-24: Inhibition of KPNA2 interaction when mutation occurs in the NLS; decreased nuclear import with localization in the nucleus but also in the cytoplasm; Complete inhibition of nuclear import When associated with a lack of zinc-finger domains</li><li>RK->AA at 31-32: No inhibition of KPNA2 interaction and no change in nuclear import</li><li>H->A at 92: Prevents formation of functional zinc-finger 3; induces drastic decrease of DNA affinity and complete modification of DNA binding specificity</li><li>H->A at 227: Prevents formation of functional zinc-finger 7 and inhibits DNA binding; No proliferation and transformation of cultured cells</li><li>K->R at 244: Abolishes single and double sumoylation; nuclear localization conserved. Increases transcriptional activity and inhibits repression domain activity; when associated with R-263 and R-353</li><li>K->R at 263: Decreases sumoylation; Abolishes double sumoylation only; Nuclear localization conserved. Increases transcriptional activity and inhibits repression domain activity; when associated with R-244 and R-353</li><li>T->A at 339: No effect on transcription activation capacity</li><li>S->A at 340: No effect on transcription activation capacity</li><li>K->R at 353: No effect on sumoylation. Increases transcriptional activity and inhibits repression domain activity; when associated with R-244 and R-263</li></ul>	<li>nuclear import</li><li>sumoylation</li><li>transcription</li><li>localization</li>	<li>GO:0051170</li><li>GO:0016925</li><li>GO:0006350</li><li>GO:0051179</li>	DNA binding	GO:0003677	<li>cytoplasm</li><li>nucleus</li>	<li>GO:0005737</li><li>GO:0005634</li>	P52292		1
Q6DN72	343413	<ul><li>Y->F at 356: No change of phosphorylation implicated in interaction with PTPN11</li><li>Y->F at 371: Loss of phosphorylation implicated in interaction with PTPN11</li></ul>	phosphorylation	GO:0016310					<li>Q90687</li><li>Q06124</li>		1
Q6FI13	723790	<ul><li>S->A at 2: Blocks the inhibition of transcription by RPS6KA5/MSK1</li></ul>	transcription	GO:0006350					<li>P32048</li><li>Q5R4K3</li><li>Q5F3L1</li><li>O75582</li>		1
Q6GQQ9	56957	<ul><li>C->A at 194: Increased ability to interact with polyubiquitin</li><li>C->S at 194: Loss of deubiquitinating activity</li></ul>									1
Q6GTX8	3903	<ul><li>Y->F at 251: Reduced tyrosine phosphorylation and loss of binding to PTPN6 and CSK as well as complete loss of inhibitory activity. Loss of phosphorylation and of inhibition of calcium mobilization; when associated with F-281</li><li>Y->F at 281: Reduced tyrosine phosphorylation and loss of binding to PTPN6. Partial inhibition of cytotoxic activity</li></ul>	<li>phosphorylation</li><li>calcium mobilization</li>	<li>GO:0016310</li><li>GO:0051209</li>	binding	GO:0005488			<li>P29350</li><li>P41239</li><li>Q0VBZ0</li><li>P41240</li>		1
Q6IA69	55191	<ul><li>C->S at 175: Eliminates glutamine-dependent NAD synthetase activity with the ammonia-dependent activity intact</li></ul>									1
Q6IQ20	222236	<ul><li>S->A at 152: Almost no change in activity: in dbSNP rsrs12540583</li><li>L->F at 207: Loss of activity: in dbSNP rsrs1861727</li><li>H->R at 380: Loss of activity: in dbSNP rsrs3181008</li><li>D->N at 389: Almost no change in activity: in dbSNP rsrs3181009</li></ul>								<li>rs3181008</li><li>rs3181009</li><li>rs12540583</li><li>rs1861727</li>	1
Q6NS38	121642	<ul><li>D->A at 173: Loss of activity</li><li>H->A at 236: Reduced activity</li></ul>									1
Q6NUP7	57718	<ul><li>R->W at 501: Abolishes interaction with PPP4C</li><li>V->A at 618: Diminishes interaction with PPP4C</li><li>V->D at 618: Abolishes interaction with PPP4C</li></ul>							<li>P60510</li><li>P11084</li>		1
Q6NYC1	23210	<ul><li>H->A at 187: Loss of catalytic activity; when associated with A-189 and A-273</li><li>D->A at 189: Loss of catalytic activity; when associated with A-187 and A-273</li><li>H->A at 273: Loss of catalytic activity; when associated with A-187 and A-189</li></ul>			catalytic activity	GO:0003824					1
Q6NYC8	170954	<ul><li>I->G at 540: Decrease binding to PP1. Complete inhibition of PP1 binding; when associated with G-542</li><li>F->G at 542: Decrease binding to PP1. Decrease binding to PP1. Complete inhibition of PP1 binding; when associated with G-540</li></ul>			binding	GO:0005488			<li>P80074</li><li>P48488</li><li>Q63447</li><li>Q61041</li><li>P50391</li><li>P30366</li><li>P48487</li><li>P22198</li>		1
Q6P5Z2	29941	<ul><li>K->E at 588: Abolishes autophosphorylation and catalytic activity</li><li>K->R at 588: Abolishes catalytic activity</li><li>T->A at 718: Abolishes phosphorylation</li></ul>	<li>phosphorylation</li><li>autophosphorylation</li>	<li>GO:0016310</li><li>GO:0046777</li>	catalytic activity	GO:0003824					1
Q6PHW0	389434	<ul><li>R->A at 101: Strongly reduces activity</li><li>R->H at 101: Reduces activity</li><li>F->A at 105: Activity as the wild type</li><li>F->Y at 105: Activity as the wild type</li><li>I->V at 116: Activity as the wild type</li></ul>									1
Q6PIZ9	50852	<ul><li>Y->F at 79: Abolishes interaction with PIK3R1</li></ul>							<li>P27986</li><li>P23727</li>		1
Q6PJP8	9937	<ul><li>D->N at 838: Impaired nuclear focus formation, reduced interaction with PIAS and increased sensitivity to cisplatin</li><li>H->A at 994: Impaired nuclear focus formation, reduced interaction with PIAS and increased sensitivity to cisplatin</li></ul>									1
Q6PL18	29028	<ul><li>K->T at 473: Reduces the ability to mediate estradiol-dependent induction of CCND1 and E2F1; when associated with Q-532</li><li>E->Q at 532: Reduces the ability to mediate estradiol-dependent induction of CCND1 and E2F1; when associated with T-473</li></ul>							<li>P55169</li><li>Q01094</li><li>P24385</li><li>Q5R6J5</li><li>Q2KI22</li><li>Q90977</li><li>Q64HP0</li><li>Q27368</li>		1
Q6QN14	391622	<ul><li>C->S at 89: Abolishes enzymatic activity</li></ul>									1
Q6R6M4	377630	<ul><li>C->S at 89: Abolishes both enzymatic activity and effects on cell proliferation</li></ul>	cell proliferation	GO:0008283							1
Q6RSH7	391104	<ul><li>NFRS->SYRG at 93-96: Preferentially binds to a hydroxylated ODD peptide</li></ul>							Q8TAX0		1
Q6S5L8	399694	<ul><li>R->Q at 315: Phosphorylation is markedly decreased. Completely reduces the phosphorylation and interaction with MUSK; when associated with K-549</li><li>YY->F at 374-375: Remains phosphorylated. Contains a residual phosphorylation; when associated with F-465. Retains the ability to bind MUSK. Reduced the phosphorylation in presence of MUSK; when associated with F-424 and F-465. Completely abolishes the phosphorylation in presence of MUSK; when associated with F-403; F-413; F-424 and F-465. Retains the ability to bind MUSK; when associated with F-465. Retains the ability to bind MUSK; when associated with F-424 and F-465. Retains the ability to bind MUSK; when associated with F-403; F-413; F-424 and F-465</li><li>Y->F at 403: Completely abolishes the phosphorylation in presence of MUSK; when associated with 374-F-F-375; F-413; F-424 and F-465</li><li>Y->F at 413: Completely abolishes the phosphorylation in presence of MUSK; when associated with 374-F-F-375; F-403; F-424 and F-465</li><li>Y->F at 424: Significantly decreased GRB2 interaction. Reduced the phosphorylation in presence of MUSK; when associated with 374-F-F-375 and F-465. Completely abolishes the phosphorylation in presence of MUSK; when associated with 374-F-F-375; F-403; F-413 and F-465</li><li>Y->F at 465: Remains phosphorylated. Contains a residual phosphorylation; when associated with 374-F-F-375. Reduced the phosphorylation in presence of MUSK; when associated with 374-F-F-375 and 424. Completely abolishes the phosphorylation in presence of MUSK; when associated with 374-F-F-375; F-403; F-413 and F-424. Retains the ability to bind MUSK. Retains the ability to bind MUSK; when associated with 374-F-F-375. Retains the ability to bind MUSK; when associated with 374-F-F-375 and F-424. Retains the ability to bind MUSK; when associated with 374-F-F-375; F-403; F-413 and F-424</li><li>R->K at 549: Completely reduces the phosphorylation and interaction with MUSK; when associated with Q-315</li></ul>	Phosphorylation	GO:0016310					<li>Q5R4J7</li><li>Q07883</li><li>P62993</li><li>Q8AXY6</li><li>O15146</li>		1
Q6UUV7	64784	<ul><li>Y->F at 282: Translocates to the cytoplasm. Represses basal TORC3 activity towards CREB</li></ul>					cytoplasm	GO:0005737	<li>P51984</li><li>P15337</li><li>P51985</li><li>P27925</li><li>Q01147</li><li>P16220</li>		1
Q6UWE0	90678	<ul><li>Missing at 649-664: Abolishes interaction with TSG101</li><li>C->A at 675: Abolishes ubiquitination of TSG101</li><li>H->A at 692: Abolishes ubiquitination of TSG101</li></ul>							Q99816		1
Q6UWP7	253558	<ul><li>D->C at 206: Abolishes LPIAT and LPGAT activities</li><li>D->R at 206: Does not increase enzyme activity</li><li>L->T at 207: Abolishes LPIAT activity. No effect on LPGAT activity</li></ul>									1
Q6UWV6	339221	<ul><li>S->F at 76: Loss of activity</li><li>C->N at 78: Strongly reduces activity</li><li>N->Q at 100: Strongly reduces N-glycosylation and enzyme activity; when associated with Q-121; Q-146; Q-168 and Q-267</li><li>N->Q at 121: Strongly reduces N-glycosylation and enzyme activity; when associated with Q-100; Q-146; Q-168 and Q-267</li><li>N->Q at 146: Strongly reduces N-glycosylation and enzyme activity; when associated with Q-100; Q-146; Q-168 and Q-267</li><li>N->Q at 168: Strongly reduces N-glycosylation and enzyme activity; when associated with Q-100; Q-121; Q-168 and Q-267</li><li>N->Q at 267: Strongly reduces N-glycosylation and enzyme activity; when associated with Q-100; Q-121; Q-146 and Q-168</li><li>H->A at 353: Loss of activity</li></ul>									1
Q6UX06	10562	<ul><li>C->A at 83: Abolishes secretion. No effect on multimer frmation</li><li>C->A at 85: Abolishes secretion. No effect on multimer frmation</li><li>C->A at 226: No effect on secretion. Affects multimer formation</li><li>C->A at 246: Abolishes secretion. No effect on multimer frmation</li><li>C->A at 437: Abolishes secretion. No effect on multimer frmation</li></ul>	secretion	GO:0046903							1
Q6UXB2	284340	<ul><li>C->S at 50: Inhibits migration of nonactivated dendritic cells and monocytes; when associated with S-52; S-75; S-77; S-103 and S-110</li><li>C->S at 52: Inhibits migration of nonactivated dendritic cells and monocytes; when associated with S-50; S-75; S-77; S-103 and S-110</li><li>C->S at 75: Inhibits migration of nonactivated dendritic cells and monocytes; when associated with S-50; S-52; S-77; S-103 and S-110</li><li>C->S at 77: Inhibits migration of nonactivated dendritic cells and monocytes; when associated with S-50; S-52; S-75; S-103 and S-110</li><li>C->S at 103: Inhibits migration of nonactivated dendritic cells and monocytes; when associated with S-50; S-52; S-75; S-77 and S-110</li><li>C->S at 110: Inhibits migration of nonactivated dendritic cells and monocytes; when associated with S-50; S-52; S-75; S-77 and S-103</li></ul>									1
Q6V1X1	54878	<ul><li>E->K at 275: 13-fold reduction in affinity for Ala-Pro-AFC; no effect on subcellular location</li><li>S->A at 755: Abolishes activity; no effect on subcellular location</li><li>D->A at 833: Abolishes activity; no effect on subcellular location</li><li>H->A at 865: Abolishes activity; no effect on subcellular location</li></ul>									1
Q6VMQ6	55729	<ul><li>D->A at 968: Abolishes the interaction with SUMO</li><li>L->A at 969: Abolishes the interaction with SUMO</li><li>L->R at 1224: Abolishes interaction with MBD1 and subsequent transcriptional repression</li></ul>							P56386		1
Q6WKZ4	80223	<ul><li>Y->F at 1254: Does not abolish the interaction with RAB11A, homooligomerization and subcellular location. Reduces the interaction with RAB4A</li><li>I->E at 1255: Abolishes the interaction with RAB11A and RAB4A, homooligomerization and subcellular location</li><li>D->N at 1256: Does not abolish the interaction with RAB11A, homooligomerization and subcellular location. Reduces the interaction with RAB4A</li></ul>							<li>Q40523</li><li>Q5R9M7</li><li>Q2TA29</li><li>P20338</li><li>P62490</li><li>Q40191</li><li>Q2TBH7</li><li>Q52NJ1</li><li>Q96283</li><li>P62491</li><li>P62493</li><li>Q5ZJN2</li>		1
Q6XPS3	93492	<ul><li>C->S at 320: Loss of activity</li></ul>									1
Q6XUX3	25778	<ul><li>K->Q at 681: No change</li></ul>									1
Q6XZB0	149998	<ul><li>S->A at 159: No activity</li></ul>									1
Q6Y288	145173	<ul><li>Missing at 495-498: Abolishes endoplasmic reticulum localization</li></ul>	localization	GO:0051179			endoplasmic reticulum	GO:0005783			1
Q6ZMC9	284266	<ul><li>R->A at 143: Abrogates glycan-binding</li><li>K->A at 274: Abrogates interaction with HCST and TYROBP</li></ul>			binding	GO:0005488			<li>Q95J79</li><li>Q9TU45</li><li>Q8WNQ8</li><li>O43914</li>		1
Q6ZN04	84206	<ul><li>G->D at 177: Prevents RNA binding</li></ul>			RNA binding	GO:0003723					1
Q712K3	54926	<ul><li>C->S at 93: Loss of function</li><li>L->S at 97: Loss of function</li><li>S->A at 233: Abolishes phosphorylation by CK2</li></ul>	phosphorylation	GO:0016310					<li>Q65ZV5</li><li>P43893</li><li>O51759</li>		1
Q71F23	79682	<ul><li>S->A at 77: Insensitive to PLK1-induced degradation</li><li>T->A at 78: Insensitive to PLK1-induced degradation</li><li>T->D at 78: Failed to enhance the PLK1-dependent degradation</li><li>T->E at 78: Failed to enhance the PLK1-dependent degradation</li></ul>							P53350		1
Q71SY5	81857	<ul><li>L->A at 646: Abrogates interaction with RARA</li><li>LL->AA at 649-650: Abrogates interaction with RARA</li></ul>							<li>Q9W5Z3</li><li>Q90966</li><li>P18514</li><li>P10276</li><li>Q5FBR4</li>		1
Q76I76	85464	<ul><li>C->S at 392: Abrogates phosphatase activity</li></ul>							<li>Q5X1E5</li><li>Q7M7K5</li><li>Q7MAZ9</li><li>Q8XBL4</li><li>Q88A53</li><li>Q5P3T0</li><li>Q7MBF4</li><li>Q8Z3M9</li><li>Q5PC82</li><li>Q5ZRX9</li><li>Q821A6</li><li>Q87SK9</li><li>Q9JZ88</li><li>Q9CP21</li><li>Q82U82</li><li>Q9I5V3</li><li>Q5F8K9</li><li>Q63YC3</li><li>Q8Y395</li><li>Q6LV05</li><li>Q8ZLY4</li><li>Q6FA38</li><li>Q9PDL7</li><li>Q62EU1</li><li>Q9JUB2</li><li>Q5WT58</li><li>Q665U9</li><li>Q57JQ5</li><li>Q9KPC6</li><li>Q8P5D4</li><li>Q8CWL6</li><li>Q8PPG9</li><li>P06961</li><li>P45269</li><li>Q9L7A3</li><li>Q88QU2</li><li>Q6D160</li><li>Q8ZI64</li><li>Q60CQ4</li><li>Q87DS9</li><li>Q65Q41</li><li>Q5E2K7</li><li>Q8CXX6</li>		1
Q76LX8	11093	<ul><li>R->K at 71: Abolishes pro-domain removal but no loss of proteolytic activity; when associated with D-73</li><li>R->D at 73: Abolishes pro-domain removal but no loss of proteolytic activity; when associated with K-71</li></ul>									1
Q76MJ5	10595	<ul><li>K->A at 548: Loss of autophosphorylation, of induction of apoptosis and of 28S rRNA cleavage, attenuation of repression of protein synthesis</li></ul>	<li>autophosphorylation</li><li>induction of apoptosis</li>	<li>GO:0046777</li><li>GO:0006917</li>							1
Q7KZI7	2011	<ul><li>T->A at 208: Prevents phosphorylation and activation by STK11 complex</li><li>T->A at 596: Loss of membrane dissociation and binding to YWHAZ</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488	membrane	GO:0016020	<li>P63103</li><li>P29361</li><li>Q15831</li><li>Q5ZKC9</li><li>Q0GGW5</li><li>Q5R651</li><li>P63104</li>		1
Q7L0Q8	58480	<ul><li>T->N at 63: Loss of GTP binding and localization to focal adhesions</li><li>T->S at 81: Loss of binding to PAK3; when associated with A-83 and C-86</li><li>F->A at 83: Loss of binding to PAK3; when associated with S-81 and C-86</li><li>F->C at 86: Loss of binding to PAK3; when associated with S-81 and A-83</li><li>Q->L at 107: Constitutively active. Results in increased rates of stress fiber dissolution and cell migration</li><li>C->S at 255: No effect on subcellular location</li><li>C->S at 256: Loss of subcellular location to plasma and intracellular membranes</li></ul>	<li>cell migration</li><li>localization</li>	<li>GO:0016477</li><li>GO:0051179</li>	<li>binding</li><li>GTP binding</li>	<li>GO:0005488</li><li>GO:0005525</li>	<li>intracellular</li><li>stress fiber</li><li>membranes</li><li>focal adhesions</li>	<li>GO:0005622</li><li>GO:0001725</li><li>GO:0016020</li><li>GO:0005925</li>	<li>P26364</li><li>Q7YQL3</li><li>O75914</li><li>Q7YQL4</li>		1
Q7L2H7	10480	<ul><li>L->P at 350: Reduces HSV binding and entry</li><li>L->P at 354: Reduces HSV binding and entry</li><li>L->P at 361: Reduces HSV binding and entry</li><li>V->P at 364: Reduces HSV binding and entry</li></ul>			binding	GO:0005488					1
Q7L622	55632	<ul><li>KK->AA at 30-31: Loss of nucleolar localization. No effect on nuclear localization</li><li>C->A at 84: Strong activity; when associated with A-258; A-261 and A-666. Strong activity; when associated with A-147 and A-666. No activity; when associated with A-147; A-258 and A-261</li><li>C->A at 147: Strong activity; when associated with A-84 and A-666. No activity; when associated with A-258; A-261 and A-666. No activity; when associated with A-84; A-258 and A-261</li><li>C->A at 258: Strong activity; when associated with A-84; A-261 and A-666. No activity; when associated with A-147; A-261 and A-666. No activity; when associated with A-84; A-147 and A-261</li><li>C->A at 261: Strong activity; when associated with A-84; A-258 and A-666. No activity; when associated with A-84; A-147 and A-258. No activity; when associated with A-147; A-258 and A-666</li><li>C->A at 666: No effect on subcellular location. Strong activity; when associated with A-84; A-258 and A261. Strong activity; when associated with A-84 and A-147. No activity; when associated with A-147; A-258 and A-261</li></ul>	localization	GO:0051179							1
Q7L7L0	92815	<ul><li>S->A at 2: Blocks the inhibition of transcription by RPS6KA5/MSK1</li></ul>	transcription	GO:0006350					<li>P32048</li><li>Q5R4K3</li><li>Q5F3L1</li><li>O75582</li>		1
Q7L804	22841	<ul><li>NPF->AAA at 406-408: Severe reduction of the interaction with REPS1 and AP2A1. No effects on its subcellular location. Modifies the endocytosis activity</li><li>YID->AAA at 480-482: Abolishes the interaction with REPS1 and AP2A1. Modifies its subcellular location and the endocytosis activity. Enhances homooligomerization</li></ul>	endocytosis	GO:0006897					<li>Q96D71</li><li>O95782</li>		1
Q7L8A9	22846	<ul><li>R->A at 29: Disappearance of 42 kDa processed form</li><li>R->A at 76: Disappearance of 36, 32 and 27 kDa processed forms</li></ul>									1
Q7RTN6	92335	<ul><li>T->A at 329: Loss of STK11-mediated phosphorylation</li><li>T->A at 419: Loss of STK11-mediated phosphorylation</li></ul>	phosphorylation	GO:0016310					<li>Q15831</li><li>Q0GGW5</li>		1
Q7RTT9	222962	<ul><li>D->A at 91: No significant change in cationic transport activity</li><li>D->A at 107: Loss of cationic transport activity</li><li>E->A at 128: No significant change in cationic transport activity</li><li>D->A at 154: Loss of cationic transport activity; increase in uridine uptake</li><li>D->A at 163: Loss of cationic transport activity</li><li>E->A at 206: Loss of cationic transport activity</li><li>E->D at 206: No loss of cationic transporter activity; no activity towards uridine</li><li>E->Q at 206: Loss of cationic transporter activity; increase in uridine uptake</li><li>E->R at 206: Loss of cationic transporter activity</li><li>T->A at 220: Reduced cationic transport activity</li><li>T->I at 220: Loss of cationic transporter activity</li><li>T->S at 220: Reduced cationic transport activity</li><li>E->A at 227: Functional with slight increased cationic transport activity</li><li>E->A at 242: Reduced cationic transport activity</li><li>W->A at 336: Loss of cationic transport activity</li><li>E->A at 375: Functional with slight increased cationic transport activity</li><li>E->Q at 375: No change in cationic activity and pH sensitivity</li></ul>	transport	GO:0006810	transporter activity	GO:0005215					1
Q7RTX0	83756	<ul><li>A->G at 537: Retains partial activity toward brazzein; however response to other sweeteners tested is suppressed</li><li>A->P at 537: Receptor unresponsive to all sweeteners tested</li><li>A->T,S,E,V at 537: Abolished the response to brazzein</li><li>F->A,H at 540: Reduces the response to brazzein and monellin</li><li>F->L at 540: Reduces the response to monellin</li><li>F->Y,P at 540: Reduces the response to brazzein; P-540 also enhances responses to the small molecule sweeteners</li></ul>							P56552		1
Q7Z2D5	9890	<ul><li>H->K at 252: Loss of activity</li></ul>									1
Q7Z2E3	54840	<ul><li>R->A at 43: Impairs interaction with XRCC1 and XRCC4</li><li>H->A at 274: Abolishes enzyme activity</li><li>C->A at 333: Abolishes DNA-binding and enzyme activity; when associated to A-336</li><li>C->A at 336: Abolishes DNA-binding and enzyme activity; when associated to A-333</li></ul>			DNA-binding	GO:0003677			<li>Q682V0</li><li>Q13426</li><li>O54935</li><li>P18887</li>		1
Q7Z3T8	9765	<ul><li>C->S at 753: Abolishes localization to endosomes and association with PI3P</li></ul>	localization	GO:0051179			endosomes	GO:0005768			1
Q7Z434	57506	<ul><li>T->A at 54: Impairs ability to induce IFN-beta</li><li>GWV->AAA at 67-69: Impairs ability to induce IFN-beta</li><li>Q->N at 145: No interaction with TRAF2</li><li>E->D at 155: No interaction with TRAF6; when associated with D-457</li><li>Q->A at 427: No cleavage by HHAV 3ABC</li><li>C->R at 435: No effect on cleavage by NS3/4A protease complex</li><li>C->R at 452: No effect on cleavage by NS3/4A protease complex</li><li>E->D at 457: No interaction with TRAF6; when associated with D-155</li><li>E->A at 463: No effect on cleavage by HHAV 3ABC</li><li>C->A,R at 508: No cleavage by HCV and hepatitis GB virus B NS3/4A protease complex</li></ul>							<li>P19028</li><li>Q9QBZ5</li><li>P24107</li><li>Q9QBZ1</li><li>Q79666</li><li>P15833</li><li>P03362</li><li>P18042</li><li>Q8AII1</li><li>P04024</li><li>P03363</li><li>P04023</li><li>O93215</li><li>P10978</li><li>P26810</li><li>Q1A249</li><li>P03356</li><li>P03355</li><li>O41798</li><li>P20892</li><li>Q9Y6I0</li><li>P10210</li><li>Q9QBY3</li><li>P03353</li><li>O77812</li><li>P16901</li><li>Q74120</li><li>Q09SZ9</li><li>Q89928</li><li>Q73368</li><li>P06591</li><li>P15775</li><li>P84454</li><li>Q9WC63</li><li>P15779</li><li>P20825</li><li>Q9IDV9</li><li>P0C211</li><li>P0C210</li><li>P51518</li><li>Q4U0X6</li><li>P12451</li><li>P07570</li><li>P28936</li><li>O89940</li><li>P24740</li><li>P26809</li><li>P26808</li><li>Q0R5R3</li><li>Q0R5R2</li><li>P18802</li><li>Q12933</li><li>P10394</li><li>P19561</li><li>P16423</li><li>P70499</li><li>P63119</li><li>P19560</li><li>Q75002</li><li>P04589</li><li>P04587</li><li>P04588</li><li>Q9QSR3</li><li>O91080</li><li>P16046</li><li>Q90056</li><li>P17757</li><li>P12497</li><li>P12499</li><li>P12498</li><li>P03311</li><li>P20875</li><li>P20876</li><li>Q6XZW6</li><li>P10273</li><li>Q9WC54</li><li>P10272</li><li>P10271</li><li>P10270</li><li>P19199</li><li>P05962</li><li>P18096</li><li>P10265</li><li>P04584</li><li>Q9N2J0</li><li>P11227</li><li>P04585</li><li>Q76634</li><li>Q8I7P9</li><li>Q9Q720</li><li>P14078</li><li>P31822</li><li>P11365</li><li>P05012</li><li>P35963</li><li>P14074</li><li>P05959</li><li>P63131</li><li>P04323</li><li>P10274</li><li>P21407</li><li>O89290</li><li>P35956</li><li>P05960</li><li>P05961</li><li>Q1A267</li><li>Q9Y4K3</li><li>P63122</li><li>O71152</li><li>P63123</li><li>P63124</li><li>P63125</li><li>P01575</li><li>P63120</li><li>P01574</li><li>P29076</li><li>P63121</li><li>P03366</li><li>P03367</li><li>P03369</li><li>P63127</li><li>P63128</li><li>P63129</li><li>Q77373</li><li>P03370</li><li>P27502</li><li>P21414</li><li>Q04854</li>		1
Q7Z4G1	170622	<ul><li>W->A at 24: Does not abolish homodimerization and interaction with COMMD1. Does not abolish repression of TNF-induced NFKB1 activation. Abolishes repression of TNF-induced NFKB1 activation; when associated with A-41</li><li>P->A at 41: Does not abolish homodimerization and interaction with COMMD1. Does not abolish repression of TNF-induced NFKB1 activation. Abolishes repression of TNF-induced NFKB1 activation; when associated with A-24</li></ul>							<li>Q8WNR1</li><li>P13296</li><li>Q8HZD9</li><li>Q8JFG3</li><li>P36939</li><li>P59684</li><li>P01375</li><li>O77764</li><li>Q2M2T5</li><li>Q8MKG8</li><li>Q2MH05</li><li>P04924</li><li>P33620</li><li>P23563</li><li>P79337</li><li>O35734</li><li>Q06599</li><li>Q9BEA1</li><li>P19101</li><li>P48094</li><li>Q75N23</li><li>Q8N668</li><li>Q6F3J0</li><li>Q1G1A2</li><li>P59695</li><li>P59694</li><li>P59693</li><li>Q539C2</li><li>Q04861</li><li>P51435</li><li>P19838</li><li>P29553</li><li>Q8WMD0</li><li>Q19LH4</li><li>O77510</li><li>P23383</li><li>P51742</li><li>P51743</li><li>Q1WM27</li><li>P79374</li>		1
Q7Z4W1	51181	<ul><li>N->L,D at 107: Loss of function. Probably due to defects in formation of the active site and binding of coenzyme</li></ul>			binding	GO:0005488					1
Q7Z569	8315	<ul><li>C->A at 264: Loss of E3 ubiquitin-protein ligase activity</li></ul>							<li>Q8RSY1</li><li>Q2QCI9</li>		1
Q7Z589	56946	<ul><li>VPL->APA at 100-102: Abolishes interaction with CBX1</li><li>L->A at 106: Abolishes interaction with ZMYND11</li></ul>							<li>P83916</li><li>Q15326</li>		1
Q7Z5G4	51125	<ul><li>C->A at 24: Slightly reduces palmitoylation</li><li>C->A at 69: Strongly reduces palmitoylation. Abolishes palmitoylation and Golgi localization; when associated with A-72</li><li>C->A at 72: Strongly reduces palmitoylation. Abolishes palmitoylation and Golgi localization; when associated with A-69</li><li>C->A at 81: Slightly reduces palmitoylation</li></ul>	localization	GO:0051179							1
Q7Z5Q5	353497	<ul><li>D->A at 623: No detectable activity</li></ul>									1
Q7Z614	124460	<ul><li>R->Q at 116: Decreased binding activity to all phospholipids</li></ul>			binding	GO:0005488					1
Q7Z6A9	151888	<ul><li>Y->F at 226: No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-257 and/or F-282</li><li>Y->F at 257: No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-226 and/or F-282</li><li>Y->F at 282: No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-226 and/or F-257</li></ul>	phosphorylation	GO:0016310					<li>P29350</li><li>Q90687</li><li>Q06124</li>		1
Q7Z6J0	57630	<ul><li>V->A at 14: Loss of Ubl activity</li><li>S->A at 304: Decreased level of phosphorylation and no change in the ability to induce apoptosis</li><li>S->D at 304: Decreased level of phosphorylation and Rac-binding ability and important loss of the ability to induce apoptosis</li><li>S->E at 304: Decreased Rac-binding ability</li></ul>	<li>phosphorylation</li><li>apoptosis</li>	<li>GO:0016310</li><li>GO:0006915</li>	binding	GO:0005488			P31750		1
Q7Z6Z7	10075	<ul><li>Y->S at 4268: Loss of activity</li><li>C->A,D at 4341: Loss of activity</li></ul>									1
Q7Z7A4	54899	<ul><li>R->Q at 54: No effect on subcellular location</li><li>Y->A at 56: Results in redistribution of protein from cytoplasm throughout entire cell</li><li>R->L at 92: Results in redistribution of protein from cytoplasm throughout entire cell</li></ul>					cytoplasm	GO:0005737			1
Q7Z7L7	10444	<ul><li>L->S at 9: Abolishes interaction with TCEB1</li></ul>							<li>Q15369</li><li>Q2KII4</li>		1
Q86SQ0	90102	<ul><li>KR->AA at 1162-1163: Loss of binding to PtdIns(3,4,5)P3</li></ul>			binding	GO:0005488					1
Q86T24	10009	<ul><li>C->R at 552: Abrogates both sequence-specific and methylation-dependent DNA-binding</li></ul>			DNA-binding	GO:0003677					1
Q86TG7	23089	<ul><li>D->A at 370: Inhibits proteolytic cleavage</li></ul>									1
Q86TM6	84447	<ul><li>C->S at 329: Abolishes E3 ligase activity</li></ul>			ligase activity	GO:0016874					1
Q86TP1	58497	<ul><li>D->A at 28: Partial loss of cAMP PDE activity. Partial loss of cAMP PDE activity; when associated with D-106. Partial loss of cAMP PDE activity; when associated with D-106 and D-179</li><li>D->A at 106: No change in cAMP PDE activity. Partial loss of cAMP PDE activity; when associated with D-28. Partial loss of cAMP PDE activity; when associated with D-28 and D-179</li><li>DHRP->AAAA at 126-129: Partial loss of cAMP PDE activity</li><li>D->A at 179: Partial loss of cAMP PDE activity. Partial loss of cAMP PDE activity; when associated with D-28 and D-106</li></ul>									1
Q86U42	8106	<ul><li>Missing at 213-220: Abolishes self-association, protein aggregation and cell death</li><li>Missing at 301-306: Abolishes self-association, protein aggregation and cell death</li></ul>	cell death	GO:0008219							1
Q86UA6	84268	<ul><li>K->R at 114: Abolishes sumoylation; when associated with N-103; R-121 and R-142</li><li>K->R at 121: Induces a strong decrease in sumoylation; when associated with N-103. Abolishes sumoylation; when associated with N-103; R-114 and R-142</li><li>K->R at 142: Abolishes sumoylation; when associated with N-103; R-114 and R-121</li></ul>	sumoylation	GO:0016925							1
Q86UD5	133308	<ul><li>DD->CC at 278-279: Loss of ion transport activity</li></ul>	ion transport	GO:0006811							1
Q86UE8	11011	<ul><li>D->A at 613: Loss of kinase activity</li></ul>			kinase activity	GO:0016301					1
Q86UN6	158798	<ul><li>L->P at 43: Abolishes RII-binding; when associated with P-47</li><li>V->P at 47: Abolishes RII-binding; when associated with P-43</li></ul>			binding	GO:0005488					1
Q86UQ8	58160	<ul><li>K->R at 43: Abolishes acetylation</li></ul>									1
Q86UR1	10811	<ul><li>P->A at 34: Partial loss of function</li><li>P->A at 37: Partial loss of function</li><li>D->A at 68: Loss of function and loss of interaction with RAC1</li><li>R->E at 103: Loss of function and loss of interaction with RAC1. Loss of localization to membranes</li><li>S->A at 172: Loss of phosphorylation. Loss of interaction with YHAWZ; when associated with A-461</li><li>S->E at 172: Constitutively interacts with YWHAZ; when associated with E-461</li><li>V->A at 205: Unable to activate NOX2</li><li>W->R at 436: Loss of interaction with NOXO1 and NCF1. Loss of localization to membranes. Partial loss of function</li><li>S->A at 461: Loss of phosphorylation. Loss of interaction with YHAWZ; when associated with A-172</li><li>S->E at 461: Constitutively interacts with YWHAZ; when associated with E-172</li></ul>	<li>phosphorylation</li><li>localization</li>	<li>GO:0016310</li><li>GO:0051179</li>			membranes	GO:0016020	<li>Q5ZKC9</li><li>O77774</li><li>Q8NFA2</li><li>Q9SSX0</li><li>P14598</li><li>P80236</li><li>P63000</li><li>P63103</li><li>P29361</li><li>P04839</li><li>Q5R651</li><li>O04369</li><li>Q38912</li><li>P13362</li><li>P62999</li><li>P62998</li><li>P63104</li>		1
Q86UR5	22999	<ul><li>RR->AA at 796-797: Abolishes interaction with SYT1 and CACNA1B</li><li>KK->AA at 1591-1592: Abolishes interaction with SYT1 and CACNA1B</li></ul>							<li>Q00975</li><li>Q60HC0</li><li>P41823</li><li>P21579</li><li>Q5R4J5</li><li>P47191</li><li>Q05152</li><li>O73706</li><li>P48018</li>		1
Q86US8	23293	<ul><li>D->A at 1353: Strongly reduced RNase activity</li></ul>									1
Q86VB7	9332	<ul><li>T->A at 1072: Impaired phosphorylation by PRKCA</li><li>S->A at 1084: Impaired phosphorylation by PRKCA</li><li>Y->A at 1096: Massive decrease of endocytotic activity</li></ul>	phosphorylation	GO:0016310					<li>P10102</li><li>P17252</li><li>P04409</li>		1
Q86VW2	115557	<ul><li>L->E at 301: Abolishes its exchange activity on RHOA</li><li>F->A at 471: Reduces exchange activity mediated by GNAQ activation; in truncated construct</li><li>L->A at 472: Reduces exchange activity mediated by GNAQ activation; in truncated construct</li><li>L->A at 475: Reduces exchange activity mediated by GNAQ activation; in truncated construct</li><li>P->A at 478: Reduces exchange activity mediated by GNAQ activation; in truncated construct</li><li>I->A at 479: Reduces exchange activity mediated by GNAQ activation; in truncated construct</li></ul>							<li>Q2PKF4</li><li>P61586</li><li>P24406</li><li>P61585</li><li>P50148</li><li>Q28294</li>		1
Q86W47	27345	<ul><li>T->A at 11: Suppresses the effect of okadaic acid and increases activation time constant; when associated with A-17 and A-210</li><li>T->D at 11: Suppresses its effect on KCNMA1 channel activation and on deactivation kinetics; when associated with E-17 and E-210</li><li>S->A at 17: Suppresses the effect of okadaic acid and increases activation time constant; when associated with A-11 and A-210</li><li>S->E at 17: Suppresses its effect on KCNMA1 channel activation and on deactivation kinetics; when associated with D-11 and E-210</li><li>N->A at 53: Loss of N-glycosylation and reduced protection against charybdotoxin; when associated with A-90</li><li>N->A at 90: Loss of N-glycosylation and reduced pr$otection against charybdotoxin; when associated with A-53</li><li>S->A at 210: Suppresses the effect of okadaic acid and increases activation time constant; when associated with A-11 and A-17</li><li>S->E at 210: Suppresses its effect on KCNMA1 channel activation and on deactivation kinetics; when associated with D-11 and E-17</li></ul>							<li>Q8AYS8</li><li>O18866</li><li>O18867</li><li>Q28204</li><li>P13487</li><li>Q28265</li><li>Q9BG98</li><li>Q12791</li>		1
Q86W56	8505	<ul><li>K->A at 12: Abolishes nuclear targeting; when associated with G-13</li><li>R->G at 13: Abolishes nuclear targeting; when associated with A-12</li><li>R->A at 36: No effect</li><li>R->G at 37: No effect</li></ul>									1
Q86WB0	51530	<ul><li>Y->F at 105: Does not strongly affect phosphorylation status; when associated with F-137</li><li>Y->F at 137: Does not strongly affect phosphorylation status; when associated with F-105</li><li>LP->FM at 170-171: Abolishes interaction with SKP1A</li><li>S->A at 354: Strongly reduces phosphorylation and induces the formation of a constitutive SCF(NIPA) E3 complex that degrades CCNB1 at G2/M phase and delays mitotic entry</li><li>RKAK->AAAA at 398-401: Induces a complete cytoplasmic redistribution</li><li>K->P at 399: Induces a partial cytoplasmic redistribution</li></ul>	<li>phosphorylation</li><li>M phase</li>	<li>GO:0016310</li><li>GO:0000279</li>					<li>P21583</li><li>Q9DG97</li><li>Q60FY0</li><li>P20826</li><li>P79169</li><li>Q95MD2</li><li>P63209</li><li>P63208</li><li>Q9IBG1</li><li>Q5R8V9</li><li>Q06220</li><li>Q08301</li><li>Q39255</li><li>P79368</li><li>P21581</li><li>Q9DGA4</li><li>Q9DGA0</li><li>Q86WB0</li><li>Q29030</li><li>Q95M19</li><li>Q90314</li><li>Q28132</li><li>P14635</li><li>Q95N18</li><li>Q09108</li><li>P37882</li>		1
Q86WV1	8631	<ul><li>Y->F at 219: Impairs interaction with PTPRC. No effect on interaction with FYN or GRB2</li><li>Y->F at 232: Abolishes interaction with PTPRC, translocation to cell membrane upon T-cell stimulation and activation of the MAP kinase pathway. No effect on interaction with FYN or GRB2</li><li>Y->F at 271: No effect on interaction with PTPRC and translocation to cell membrane upon T-cell stimulation. Abolishes interaction with FYN and GRB2 and activation of the MAP kinase pathway</li><li>Y->F at 295: Abolishes FYB-dependent activation of ITGAL clustering</li><li>Y->F at 298: Impairs interaction with FYB</li><li>W->R at 333: Abolishes homodimerization, interaction with FYB and activation of the MAP kinase pathway</li></ul>					cell membrane	GO:0005886	<li>Q5R4J7</li><li>Q07883</li><li>P62993</li><li>Q05876</li><li>P08575</li><li>P20701</li><li>P06241</li><li>P61625</li><li>O15117</li><li>P27446</li>		1
Q86WV6	340061	<ul><li>SLS->ALA at 324-326: Induces a decrease in phosphorylation by TBK1</li><li>S->A at 358: Induces a decrease in phosphorylation by TBK1 and ability to activate IRF-E</li></ul>	phosphorylation	GO:0016310					<li>Q9UHD2</li><li>Q969Q1</li>		1
Q86XP1	160851	<ul><li>W->G at 1151: Abolishes homo and heterooligomerization but not its catalytic activity</li></ul>			catalytic activity	GO:0003824					1
Q86XR7	353376	<ul><li>G->A at 2: Results in relocalization from membrane to cytosol; Loss of ability to transduce TLR4-signal</li><li>S->A at 6: Loss of phosphorylation. Significant reduction in the ability to activate IRF3 or NF-kappa-B</li><li>S->A at 10: No effect on phosphorylation and on the ability to activate IRF3 or NF-kappa-B</li><li>S->A at 14: No effect on phosphorylation and on the ability to activate IRF3 or NF-kappa-B</li><li>S->A at 16: Loss of phosphorylation. Abolishes ability to activate IRF3 or NF-kappa-B and to transduce TLR4 signal</li><li>S->E at 16: Significant decrease of localization in the membrane</li><li>P->H at 116: Loss of ability to dimerize. Significant loss of RANTES-inducing activity. Loss of ability to induce NF-kappa-B activation</li><li>C->H at 117: Loss of ability to dimerize. Loss of RANTES-inducing activity and ability to induce NF-kappa-B activation. Inhibition of TLR4-dependent activation of IRF3 and IRF7. Loss of interaction with TLR4</li></ul>	<li>phosphorylation</li><li>localization</li>	<li>GO:0016310</li><li>GO:0051179</li>			<li>membrane</li><li>cytosol</li>	<li>GO:0016020</li><li>GO:0005829</li>	<li>P58727</li><li>Q9GL65</li><li>Q9WV82</li><li>Q4JF28</li><li>O00206</li><li>Q9TSP2</li><li>Q92985</li><li>Q68Y56</li><li>Q9MYW3</li><li>Q14653</li><li>Q8SPE8</li><li>Q2V898</li><li>Q9TTN0</li><li>Q764M6</li><li>Q90643</li><li>Q8SPE9</li>		1
Q86Y13	9666	<ul><li>KKKTK->SGSTA at 662-666: Strongly decreases RNA-binding activity</li><li>C->S at 1187: Abolishes ubiquitin ligase activity</li></ul>			<li>ligase activity</li><li>RNA-binding</li>	<li>GO:0016874</li><li>GO:0003723</li>			<li>P69326</li><li>P08565</li><li>P69322</li><li>P69323</li><li>P69324</li><li>P69325</li><li>P68196</li><li>O46543</li><li>P68197</li><li>Q05550</li><li>P68198</li><li>P68199</li><li>P19848</li><li>P42739</li><li>P68195</li><li>Q867C2</li><li>P62991</li><li>P62990</li><li>P61863</li><li>P61864</li><li>P61862</li><li>Q867C4</li><li>Q867C3</li><li>P23398</li><li>P68204</li><li>P84589</li><li>Q865C5</li><li>P42740</li><li>P68201</li><li>Q8MKD1</li><li>P14792</li><li>P63049</li><li>P0C072</li><li>P63051</li><li>P69308</li><li>P69309</li><li>P20685</li><li>P15174</li><li>P62976</li><li>P62977</li><li>P62974</li><li>P62975</li><li>P62972</li><li>P13117</li><li>P14624</li><li>P62973</li><li>P46574</li><li>P69310</li><li>P69313</li><li>P69314</li><li>P69311</li><li>P08618</li><li>P69312</li><li>P69317</li><li>P69318</li><li>P69315</li><li>P0C014</li><li>P69316</li><li>P59263</li><li>P69319</li><li>P49634</li><li>P49635</li><li>Q9Y848</li><li>P22589</li><li>P62988</li><li>P62989</li><li>P69321</li><li>P23324</li><li>P69320</li><li>P59669</li>		1
Q86Y38	64131	<ul><li>C->A at 257: No effect</li><li>C->A at 276: Strongly reduced enzyme activity</li><li>C->A at 285: No effect</li><li>C->A at 301: No effect</li><li>D->G at 314: No effect</li><li>D->G at 316: No effect</li><li>C->A at 471: Strongly reduced enzyme activity</li><li>C->A at 542: No effect</li><li>C->A at 561: Strongly reduced enzyme activity</li><li>C->A at 563: No effect</li><li>C->A at 572: Strongly reduced enzyme activity</li><li>C->A at 574: Strongly reduced enzyme activity</li><li>C->A at 675: No effect</li><li>D->E at 745: No effect</li><li>D->G at 745: Abolishes enzyme activity but does not affect UDP-binding</li><li>W->D,N,G at 746: Strongly reduced enzyme activity but does not affect UDP-binding</li><li>D->G,E at 747: Reduced enzyme activity but does not affect UDP-binding</li><li>C->A at 920: No effect</li><li>C->A at 927: No effect</li><li>C->A at 933: No effect</li></ul>			binding	GO:0005488					1
Q86YJ5	92979	<ul><li>D->N at 231: Diminishes ability to promote MHC-I internalization</li></ul>									1
Q86YL7	10630	<ul><li>T->A at 52: Eliminates induction of platelet aggregation</li></ul>									1
Q86YN6	133522	<ul><li>LLAEL->AAAEA at 92-96: Reduces DNA transcriptional activity</li><li>LLQKLL->AAQKAA at 155-160: Reduces interaction and activation of ESR1. Loss of interaction and activation of ESR1; when associated with 343-AREAA-347</li><li>LRELL->AREAA at 343-347: Reduces interaction and activation of ESR1. Loss of interaction and activation of ESR1; when associated with 155-AAQKAA-160</li></ul>							<li>Q9TV98</li><li>Q9QZJ5</li><li>P49884</li><li>Q91424</li><li>Q91250</li><li>Q29040</li><li>P38111</li><li>Q9YHT3</li><li>P50242</li><li>P50241</li><li>P03372</li><li>P16058</li><li>Q9YH33</li><li>Q9PVZ9</li><li>P50240</li><li>P06212</li><li>P57753</li><li>Q53AD2</li><li>P49885</li><li>P49886</li><li>Q9YHZ7</li><li>O42132</li>		1
Q86YT9	120425	<ul><li>K->E at 54: Loss of localization to the plasma membrane</li></ul>	localization	GO:0051179			plasma membrane	GO:0005886			1
Q8IU60	167227	<ul><li>E->Q at 147: Loss of decapping activity; when associated with Q-148</li><li>E->Q at 148: Strongly reduced decapping activity</li></ul>									1
Q8IU85	57118	<ul><li>T->A at 180: Loss of ionomycin-induced activation</li></ul>									1
Q8IU99	255022	<ul><li>N->G at 72: Significant inhibition on the control of cytosolic Ca(2+) levels</li><li>N->A at 74: Has no effect on glycosylation</li><li>N->A at 140: Prevents glycosylation</li></ul>									1
Q8IUC4	85415	<ul><li>EN->AA at 58-59: Abolishes interaction with RhoA</li><li>R->A at 518: Does not induce actin disassembly but still interacts with RhoA; when associated with A-526 and A-527</li><li>LG->AA at 526-527: Does not induce actin disassembly but still interacts with RhoA; when associated with A-518</li></ul>							<li>Q92192</li><li>Q92193</li><li>P53499</li><li>P26183</li><li>P53498</li><li>O13419</li><li>Q9P4D1</li><li>P48465</li><li>P53455</li><li>Q39596</li><li>Q39758</li><li>P26182</li><li>P80709</li><li>Q9UVX4</li><li>O17320</li><li>P53689</li><li>P78711</li><li>P30161</li><li>P17128</li><li>P45521</li><li>P45520</li><li>P20904</li><li>P81085</li><li>Q6TCF2</li><li>Q99023</li><li>Q75D00</li><li>P51775</li><li>P10365</li><li>P60011</li><li>P60010</li><li>Q9C3Y4</li><li>Q8SWN8</li><li>O16808</li><li>P02577</li><li>P10989</li><li>P68555</li><li>Q05214</li><li>Q8X119</li><li>O65316</li><li>O65315</li><li>O65314</li><li>P53491</li><li>P91754</li><li>P13363</li><li>P11426</li><li>O81221</li><li>Q11212</li><li>P50138</li><li>P53477</li><li>P53476</li><li>P60009</li><li>P53502</li><li>Q2U7A3</li><li>P53500</li><li>Q9UVZ8</li><li>P14235</li><li>O00937</li><li>Q9UVF3</li><li>Q24733</li><li>P90689</li><li>P24902</li><li>O74258</li>		1
Q8IUC6	148022	<ul><li>E->A at 88: Reduces binding to TRAF6 and activation of NFKB signaling pathway; when associated with A-252 and A-303</li><li>E->A at 252: Reduces binding to TRAF6 and activation of NF-kappa-B signaling pathway; when associated with A-88 and A-303</li><li>E->A at 303: Reduces binding to TRAF6 and activation of NFKB signaling pathway; when associated with A-88 and A-252</li><li>P->H at 434: Abolishes binding to TLR3</li></ul>			binding	GO:0005488			<li>Q5TJ59</li><li>O15455</li><li>Q9Y4K3</li><li>Q0PV50</li>		1
Q8IUE6	317772	<ul><li>S->A at 2: Blocks the inhibition of transcription by RPS6KA5/MSK1</li></ul>	transcription	GO:0006350					<li>P32048</li><li>Q5R4K3</li><li>Q5F3L1</li><li>O75582</li>		1
Q8IUH2	200407	<ul><li>NN->QQ at 165-166: Abolishes N-glycosylation</li></ul>									1
Q8IUH5	23390	<ul><li>C->S at 467: Abolishes palmitoyltransferase activity</li></ul>			palmitoyltransferase activity	GO:0016409					1
Q8IUQ4	6477	<ul><li>E->R at 40: Loss of function</li><li>C->S at 41: Loss of function; when associated with S-44</li><li>C->S at 44: Loss of function</li><li>C->S at 55: Loss of function; when associated with Y-59</li><li>H->Y at 59: Loss of function</li><li>R->L at 66: Decreased activity; when associated with T-68</li><li>K->T at 68: Decreased activity; when associated with L-66</li><li>R->E at 76: Decreased activity</li><li>R->A at 124: In D; does not impair its ability to interact with CACYBP and degrade CTNNB1 and PML; when associated with A-214; A-215; A-231 and A-232</li><li>D->A at 142: In E; does not impair its ability to interact with CACYBP and degrade CTNNB1; when associated with A-151</li><li>Q->A at 151: In E; does not impair its ability to interact with CACYBP and degrade CTNNB1; when associated with A-142</li><li>H->Y at 152: Abolishes ability to degrade DCC</li><li>ED->AA at 161-162: In A; does not impair its ability to degrade PML while it abolishes its ability to interact with CACYBP and degrade CTNNB1; when associated with A-226 and A-237</li><li>H->Y at 202: No effect</li><li>L->R at 211: Abolishes ability to degrade DCC</li><li>TR->AA at 214-215: In mutant D; does not impair its ability to interact with CACYBP and degrade CTNNB1 and PML; when associated with A-124; A-231 and A-232</li><li>R->A at 224: In C; does not impair its ability to interact with CACYBP and degrade CTNNB1; when associated with A-233</li><li>E->A at 226: In A; does not impair its ability to degrade PML while it abolishes its ability to interact with CACYBP and degrade CTNNB1; when associated with A-161; A-162 and A-237</li><li>RR->AA at 231-232: In D; does not impair its ability to interact with CACYBP and degrade CTNNB1 and PML; when associated with A-124; A-214 and A-215</li><li>R->A at 233: In C; does not impair its ability to interact with CACYBP and degrade CTNNB1; when associated with A-233</li><li>E->A at 237: In A; does not impair its ability to degrade PML while it abolishes its ability to interact with CACYBP and degrade CTNNB1; when associated with A-161; A-162 and A-226</li><li>N->A at 253: In B; does not impair its ability to interact with CACYBP and degrade CTNNB1; when associated with A-265</li><li>Q->A at 265: In B; does not impair its ability to interact with CACYBP and degrade CTNNB1; when associated with A-253</li></ul>							<li>P43146</li><li>Q9HB71</li><li>Q5R6Z8</li><li>P35222</li><li>P29590</li>		1
Q8IV04	374403	<ul><li>R->A at 141: Loss of GAP activity</li></ul>							<li>Q92263</li><li>P20936</li><li>Q92211</li><li>P09851</li><li>Q5PEA9</li><li>P74873</li><li>P74851</li><li>P50904</li>		1
Q8IV77	1262	<ul><li>L->E at 292: Loss of inhibition produced by calcium/calmodulin binding</li></ul>			binding	GO:0005488			<li>Q40302</li><li>Q8STF0</li><li>P04353</li><li>P41040</li><li>P04352</li><li>Q9GRJ1</li><li>P61860</li><li>P02594</li><li>P02595</li><li>P61861</li><li>P48976</li><li>O82018</li><li>P93171</li><li>P62184</li><li>P62144</li><li>P62145</li><li>Q5RAD2</li><li>P07463</li><li>P24044</li><li>P11121</li><li>P62149</li><li>P06787</li><li>O02367</li><li>Q6IT78</li><li>P05935</li><li>P05933</li><li>O16305</li><li>Q6PI52</li><li>P05934</li><li>Q6YNX6</li><li>Q7Y052</li><li>Q95NR9</li><li>P11118</li><li>P62157</li><li>P62156</li><li>P21251</li><li>P62155</li><li>Q5EHV7</li><li>P62154</li><li>P62152</li><li>P62151</li><li>Q7T3T2</li><li>P69097</li><li>P69098</li><li>P60206</li><li>Q9U6D3</li><li>Q9HFY6</li><li>P60205</li><li>P62158</li><li>P60204</li><li>O96102</li><li>P62201</li><li>P18061</li><li>P11120</li><li>Q8X187</li><li>P93087</li><li>O60041</li><li>Q05055</li><li>P62204</li><li>P62160</li><li>P62203</li><li>P62202</li><li>P61859</li><li>P17928</li><li>P15094</li><li>Q95NI4</li><li>Q9UWF0</li><li>P62162</li><li>P02598</li><li>P62161</li><li>P02599</li><li>Q71UH6</li><li>Q71UH5</li><li>O97341</li><li>P04464</li><li>P27165</li><li>Q39752</li><li>P84339</li><li>P27166</li><li>P23286</li><li>O94739</li><li>P27161</li><li>P41041</li><li>Q6R520</li>		1
Q8IVG9		<ul><li>Missing at 1-3: Abolishes the neuroprotective activity</li><li>Missing at 1-2: No effect on the neuroprotective activity</li><li>C->A,D,E,F,G,I, at 8: Abolishes the neuroprotective activity</li><li>C->H at 8: Significantly reduces the neuroprotective activity</li><li>C->K,R at 8: No effect on the neuroprotective activity</li><li>S->A at 14: Abolishes the neuroprotective activity</li><li>S->G at 14: Potentiation of the neuroprotective activity</li><li>Missing at 19-24: Abolishes the neuroprotective activity</li><li>Missing at 20-24: No effect on the neuroprotective activity</li></ul>									1
Q8IVH8	8491	<ul><li>K->E at 48: Loss of kinase activity and ability to activate JNK family</li></ul>			kinase activity	GO:0016301			<li>Q966Y3</li><li>P92208</li>		1
Q8IVW6	10620	<ul><li>P->H at 240: Impairs binding to RB1</li><li>W->S at 271: Impairs binding to RB1</li></ul>			binding	GO:0005488			P06400		1
Q8IW41	8550	<ul><li>T->A at 182: No p38 beta-induced activation</li></ul>							<li>Q04929</li><li>Q63768</li><li>O75791</li><li>P80350</li><li>O97628</li><li>Q01552</li><li>O24473</li><li>P82869</li><li>Q9Y2S7</li><li>Q9LDA4</li><li>O95433</li><li>P46108</li><li>Q64010</li>		1
Q8IWA4	55669	<ul><li>K->T at 88: Induces a strong decrease in mitochondrial clustering</li><li>T->A at 109: Acts as a dominant negative mutant; induces fragmentation of mitochondria</li></ul>									1
Q8IWQ3	9024	<ul><li>T->A at 174: Prevents phosphorylation and activation by STK11 complex</li></ul>	phosphorylation	GO:0016310					<li>Q15831</li><li>Q0GGW5</li>		1
Q8IWU5	55959	<ul><li>CC->AA at 88-89: Loss of arylsulfatase activity</li></ul>							P51691		1
Q8IWU6	23213	<ul><li>CC->AA at 87-88: Loss of arylsulfatase activity and loss of ability to modulate apoptosis</li></ul>	apoptosis	GO:0006915					P51691		1
Q8IXI1	89941	<ul><li>A->V at 13: Causes constitutive activation inducing an aggregation of the mitochondrial network</li><li>T->N at 18: Induces an aggregation of the mitochondrial network</li></ul>									1
Q8IXI2	55288	<ul><li>P->V at 13: Causes constitutive activation inducing an aggregation of the mitochondrial network</li><li>T->N at 18: Causes constitutive inactivation</li><li>E->K at 208: Abolishes the formation of thread-like mitochondria</li><li>E->K at 328: Abolishes the formation of thread-like mitochondria</li><li>K->V at 427: No effect</li><li>S->N at 432: No effect</li></ul>									1
Q8IXJ6	22933	<ul><li>R->A at 97: No effect on deacetylase activity</li><li>Q->A at 167: Reduced deacetylase activity</li><li>N->A at 168: Abolishes acetylation of alpha-tubulin</li><li>D->A,N at 170: Reduced deacetylase activity</li><li>H->Y,A at 187: Loss of function. Abolishes acetylation of alpha-tubulin. No effect on phosphorylation</li></ul>	phosphorylation	GO:0016310	deacetylase activity	GO:0019213			<li>Q71G51</li><li>Q5I2J3</li><li>Q9C413</li><li>P10873</li>		1
Q8IXL7	253827	<ul><li>H->G at 134: 30-fold reduction in activity</li><li>N->F at 153: 7000-fold reduction in activity</li><li>N->Y at 153: 500-fold reduction in activity</li></ul>									1
Q8IY84	167359	<ul><li>T->A at 229: Loss of autophosphorylation and kinase activity</li><li>T->E at 229: Constitutively active</li></ul>	autophosphorylation	GO:0046777	kinase activity	GO:0016301					1
Q8IYB3	10250	<ul><li>K->A at 20: Strongly reduces DNA and RNA-binding</li><li>K->A at 22: Strongly reduces DNA and RNA-binding</li><li>K->A at 23: Strongly reduces DNA and RNA-binding</li></ul>			RNA-binding	GO:0003723					1
Q8IYB8	6832	<ul><li>G->V at 207: Abolishes dsDNA and dsRNA helicase activity</li><li>K->A,R at 213: Abolishes ATPase activity</li></ul>			ATPase activity	GO:0016887			<li>Q8V736</li><li>O67037</li><li>Q9UZ86</li><li>Q68772</li><li>O51934</li><li>P74759</li><li>P37987</li><li>P22657</li><li>Q04575</li><li>Q971T7</li><li>P27328</li><li>P28726</li><li>Q07630</li><li>P27327</li><li>Q9WJB2</li><li>Q3I5J6</li><li>Q66914</li><li>P16342</li><li>Q89273</li><li>P36286</li><li>Q66198</li><li>P22168</li><li>P19751</li><li>Q8V6W7</li><li>P28897</li><li>Q96725</li><li>P19811</li><li>Q91A29</li><li>O29238</li><li>P09395</li><li>P15402</li><li>Q86117</li><li>P09498</li><li>Q86119</li><li>Q58907</li><li>Q83017</li><li>Q97ZF5</li><li>Q8R979</li><li>Q6F598</li><li>Q08582</li><li>Q91AV2</li><li>P17779</li><li>O58530</li><li>O67226</li><li>Q07518</li><li>P95479</li><li>P54634</li><li>Q8ZXT5</li><li>Q9IW06</li><li>Q04544</li><li>Q975P6</li><li>Q8V439</li><li>P17965</li><li>Q91QT2</li><li>Q04561</li><li>Q97ZZ8</li><li>P27411</li><li>P27410</li><li>P27920</li><li>P22591</li><li>Q9PYA3</li><li>P20951</li><li>P15095</li><li>Q9YN02</li><li>P27407</li><li>Q06502</li><li>P18458</li><li>Q05002</li><li>Q9YCB6</li><li>P59641</li><li>Q69014</li><li>Q8B912</li><li>P27409</li><li>Q9YC75</li>		1
Q8IYD8	57697	<ul><li>G->A at 116: Reduces ATPase activity</li><li>K->R at 117: Abolishes ATPase activity</li></ul>			ATPase activity	GO:0016887					1
Q8IYM1	124404	<ul><li>G->N at 56: Abolishes binding to GTP and to SEPT11, and also abolishes the ability of SEPT12 to form filamentous structures</li></ul>			binding	GO:0005488			<li>Q3SZN0</li><li>Q9NVA2</li><li>Q5R8U3</li>		1
Q8IYU2	57531	<ul><li>C->S at 876: Loss of E3 ubiquitin ligase activity</li></ul>			ligase activity	GO:0016874			<li>P69326</li><li>P08565</li><li>P69322</li><li>P69323</li><li>P69324</li><li>P69325</li><li>P68196</li><li>O46543</li><li>P68197</li><li>Q05550</li><li>P68198</li><li>P68199</li><li>P19848</li><li>P42739</li><li>P68195</li><li>Q867C2</li><li>P62991</li><li>P62990</li><li>P61863</li><li>P61864</li><li>P61862</li><li>Q867C4</li><li>Q867C3</li><li>P23398</li><li>P68204</li><li>P84589</li><li>Q865C5</li><li>P42740</li><li>P68201</li><li>Q8MKD1</li><li>P14792</li><li>P63049</li><li>P0C072</li><li>P63051</li><li>P69308</li><li>P69309</li><li>P20685</li><li>P15174</li><li>P62976</li><li>P62977</li><li>P62974</li><li>P62975</li><li>P62972</li><li>P13117</li><li>P14624</li><li>P62973</li><li>P46574</li><li>P69310</li><li>P69313</li><li>P69314</li><li>P69311</li><li>P08618</li><li>P69312</li><li>P69317</li><li>P69318</li><li>P69315</li><li>P0C014</li><li>P69316</li><li>P59263</li><li>P69319</li><li>P49634</li><li>P49635</li><li>Q9Y848</li><li>P22589</li><li>P62988</li><li>P62989</li><li>P69321</li><li>P23324</li><li>P69320</li><li>P59669</li>		1
Q8IZ41	158158	<ul><li>S->N at 555: Impairs nucleotide binding and perinuclear localization</li><li>Q->L at 600: Favors GTP association</li></ul>	localization	GO:0051179	nucleotide binding	GO:0000166					1
Q8IZE3	57147	<ul><li>GSENS->M at 2-6: No Golgi targeting, accumulates in the cytoplasm</li></ul>					cytoplasm	GO:0005737			1
Q8IZJ1	219699	<ul><li>D->N at 412: Abolishes cleavage by caspase-3 and subsequent induction of apoptosis</li></ul>	induction of apoptosis	GO:0006917							1
Q8IZL9	23552	<ul><li>T->A at 161: Impairs CDK2 T-160 phosphorylation and activity</li></ul>	phosphorylation	GO:0016310					<li>P48963</li><li>Q5E9Y0</li><li>P43450</li><li>P24941</li><li>O55076</li>		1
Q8IZW8	84951	<ul><li>D->A at 506: No effect on cleavage by caspase-3</li><li>D->A at 570: Abolishes cleavage by caspase-3</li></ul>									1
Q8IZY5	414899	<ul><li>L->E at 5: Fails to induce apoptosis</li></ul>	apoptosis	GO:0006915							1
Q8N108	57708	<ul><li>W->A at 238: Loss of transcriptional repression and HDAC1 recruitment activity</li><li>FL->AA at 251-252: Loss of transcriptional repression and HDAC1 recruitment activity</li></ul>							<li>Q13547</li><li>Q94517</li><li>P56517</li><li>P56518</li>		1
Q8N264	83478	<ul><li>R->A at 175: Loss of function</li><li>R->K at 175: Does not abolish the effect on actin stress fibers but moderates its capability to induce membrane protrusions</li></ul>					<li>stress fibers</li><li>membrane</li>	<li>GO:0001725</li><li>GO:0016020</li>	<li>Q92192</li><li>Q92193</li><li>P53499</li><li>P26183</li><li>P53498</li><li>O13419</li><li>Q9P4D1</li><li>P48465</li><li>P53455</li><li>Q39596</li><li>Q39758</li><li>P26182</li><li>P80709</li><li>Q9UVX4</li><li>O17320</li><li>P53689</li><li>P78711</li><li>P30161</li><li>P17128</li><li>P45521</li><li>P45520</li><li>P20904</li><li>P81085</li><li>Q6TCF2</li><li>Q99023</li><li>Q75D00</li><li>P51775</li><li>P10365</li><li>P60011</li><li>P60010</li><li>Q8SWN8</li><li>O16808</li><li>P02577</li><li>P10989</li><li>P68555</li><li>Q05214</li><li>Q8X119</li><li>O65316</li><li>O65315</li><li>O65314</li><li>P53491</li><li>P91754</li><li>P13363</li><li>P11426</li><li>O81221</li><li>Q11212</li><li>P50138</li><li>P53477</li><li>P53476</li><li>P60009</li><li>P53502</li><li>Q2U7A3</li><li>P53500</li><li>Q9UVZ8</li><li>P14235</li><li>O00937</li><li>Q9UVF3</li><li>Q24733</li><li>P90689</li><li>P24902</li><li>O74258</li>		1
Q8N2W9	51588	<ul><li>LL->AA at 23-24: Loss of repression of AR- and STAT1-induced transcription; no effect on AR- and STAT1-binding</li><li>K->R at 35: Complete loss of sumoylation. No enhancement of TCF4 sumoylation. No effect on interaction with TCF4. Colocalizes with SUMO1 in nucleus but concentrated into nuclear granules</li><li>K->R at 128: Some loss of sumoylation</li><li>C->A at 342: Inhibits TCF4 sumoylation. Inhibits beta-catenin-mediated TCF7L2/TCF4 activity. No colocalization with TCF7L2/TCF4 in nuclear puntuate structures; when associated with A-347</li><li>C->A at 347: Inhibits TCF4 sumoylation. Inhibits beta-catenin-mediated TCF7L2/TCF4 activity. No colocalization with TCF7L2/TCF4 in nuclear puntuate structures; when associated with A-342. AR- and STAT1-binding</li></ul>	<li>sumoylation</li><li>transcription</li>	<li>GO:0016925</li><li>GO:0006350</li>	binding	GO:0005488	nucleus	GO:0005634	<li>P15881</li><li>Q2EF74</li><li>P42224</li><li>Q5R6J4</li><li>P55857</li><li>P35223</li><li>P35222</li><li>P63165</li><li>Q9WU82</li><li>P35224</li><li>Q90683</li><li>Q5E9D1</li><li>Q02248</li><li>P15884</li><li>Q764M5</li><li>P26233</li><li>Q9NQB0</li><li>Q9MZD5</li>		1
Q8N370	124935	<ul><li>S->A at 297: Abolishes sensitivity to N-ethymaleimide</li></ul>									1
Q8N3J5	152926	<ul><li>D->A at 298: Loss of activity</li></ul>									1
Q8N474	6422	<ul><li>N->Q at 173: Reduced molecular weight</li><li>N->Q at 263: No effect on molecular weight</li></ul>									1
Q8N4A0	8693	<ul><li>D->H at 459: Affects the glycopeptide specificity and abolishes ability to glycosylate Muc1, Muc2 and Muc5AC</li></ul>							<li>Q62635</li><li>Q02496</li>		1
Q8N4E7	94033	<ul><li>S->A at 204: Increases ferroxidase activity and iron binding</li></ul>			iron binding	GO:0005506			<li>Q61147</li><li>P13635</li><li>P00450</li><li>Q9XT27</li>		1
Q8N4Q1	131474	<ul><li>C->S at 53: Does not strongly affect import and stability of MIA40 in mitochondria; when associated with S-55</li><li>C->S at 55: Does not strongly affect import and stability of MIA40 in mitochondria; when associated with S-53</li><li>C->S at 64: Affects import and stability of MIA40 in mitochondria; when associated with S-74</li><li>C->S at 74: Affects import and stability of MIA40 in mitochondria; when associated with S-64</li><li>C->S at 87: Strongly affects import and stability of MIA40 in mitochondria; when associated with S-97</li><li>C->S at 97: Strongly affects import and stability of MIA40 in mitochondria; when associated with S-87</li></ul>							<li>P36046</li><li>Q2KHZ4</li><li>Q6BSK8</li><li>Q4IK03</li><li>Q757A5</li><li>Q6FW26</li><li>O94030</li><li>Q6CSA1</li><li>Q8N4Q1</li><li>Q5KGA4</li><li>Q4P8D2</li>		1
Q8N4X5	84632	<ul><li>Y->F at 4: Reduced interaction with SRC</li></ul>							<li>P00523</li><li>P12931</li>		1
Q8N556	60312	<ul><li>P->A at 71: Decreased tyrosine phosphorylation</li><li>P->A at 77: No effect on tyrosine phosphorylation</li><li>Y->F at 93: Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-94; F-125; F-451 and F-453</li><li>Y->F at 94: Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-93; F-125; F-451 and F-453</li><li>Y->F at 125: Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-93; F-94; F-451 and F-453</li><li>Y->F at 451: Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-93; F-94; F-125 and F-453</li><li>Y->F at 453: Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-93; F-94; F-125 and F-451</li></ul>	phosphorylation	GO:0016310					<li>P00523</li><li>P12931</li>		1
Q8N6P7	58985	<ul><li>K->A at 58: Strongly reduced response to IL22</li><li>Y->A,R at 60: Loss of response to IL22</li></ul>							Q9GZX6		1
Q8N807	204474	<ul><li>C->A at 135: Does not affect homodimerization; when associated with A-420</li><li>C->A at 420: Does not affect homodimerization; when associated with A-135</li></ul>									1
Q8NBJ7	25870	<ul><li>C->A at 156: Abolishes interaction with and inhibition of SUMF1. Can still form homodimers</li><li>C->A at 290: Abolishes interaction with and inhibition of SUMF1. Can still form homodimers</li></ul>							Q8NBK3		1
Q8NBK3	285362	<ul><li>S->A at 333: Loss of activity</li><li>S->T at 333: Reduces activity by 99%</li><li>C->S at 336: Loss of activity</li><li>H->A at 337: Reduces activity 5-fold</li><li>Y->F at 340: No effect</li><li>C->S at 341: Loss of activity</li></ul>									1
Q8NBP7	255738	<ul><li>C->A at 67: Does not affect multimerization or zymogen processing</li><li>H->A at 226: Remains in the endoplasmic reticulum and is not secreted</li><li>N->A at 533: 1.5 kDa decrease of the apparent molecular mass of pro-PCSK9 and PCSK9 and no effect on processing and secretion</li></ul>	secretion	GO:0046903			endoplasmic reticulum	GO:0005783	Q8NBP7		1
Q8NCD3	55355	<ul><li>S->A at 486: Loss of phosphorylation by AKT1 and binding to YWHAG</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488			<li>P68253</li><li>Q5RC20</li><li>P68252</li><li>Q38998</li><li>Q01314</li><li>P61981</li><li>Q8VYX2</li><li>P31749</li><li>Q5F3W6</li>		1
Q8NCE2	64419	<ul><li>C->S at 330: Drastically reduced enzymatic activity</li></ul>									1
Q8NCG7	221955	<ul><li>S->A at 443: Loss of activity</li><li>D->A at 495: Loss of activity</li></ul>									1
Q8ND25	84937	<ul><li>C->A at 184: Loss of E3 activity</li></ul>									1
Q8NEJ0	150290	<ul><li>D->A at 73: Abolishes most of in vitro phosphatase activity</li><li>L->V at 102: No effect on in vitro phosphatase activity</li><li>C->S at 104: Abolishes most of in vitro phosphatase activity</li><li>R->K at 110: Abolishes most of in vitro phosphatase activity</li><li>S->A at 111: Abolishes most of in vitro phosphatase activity</li></ul>							<li>Q5X1E5</li><li>Q7M7K5</li><li>Q7MAZ9</li><li>Q8XBL4</li><li>Q88A53</li><li>Q5P3T0</li><li>Q7MBF4</li><li>Q8Z3M9</li><li>Q5PC82</li><li>Q5ZRX9</li><li>Q821A6</li><li>Q87SK9</li><li>Q9JZ88</li><li>Q9CP21</li><li>Q82U82</li><li>Q9I5V3</li><li>Q5F8K9</li><li>Q63YC3</li><li>Q8Y395</li><li>Q6LV05</li><li>Q8ZLY4</li><li>Q6FA38</li><li>Q9PDL7</li><li>Q62EU1</li><li>Q9JUB2</li><li>Q5WT58</li><li>Q665U9</li><li>Q57JQ5</li><li>Q9KPC6</li><li>Q8P5D4</li><li>Q8CWL6</li><li>Q8PPG9</li><li>P06961</li><li>P45269</li><li>Q9L7A3</li><li>Q88QU2</li><li>Q6D160</li><li>Q8ZI64</li><li>Q60CQ4</li><li>Q87DS9</li><li>Q65Q41</li><li>Q5E2K7</li><li>Q8CXX6</li>		1
Q8NER1	7442	<ul><li>Y->A at 511: Loss of sensitivity to capsaicin</li><li>T->I at 550: Reduces sensitivity to capsaicin 40-fold</li></ul>									1
Q8NER5	130399	<ul><li>T->D at 194: Pro-apoptotic</li><li>K->R at 222: Loss of response to NODAL and SMAD2 phosphorylation</li></ul>	phosphorylation	GO:0016310					<li>Q15796</li><li>Q1W668</li><li>Q96S42</li>		1
Q8NET5	150372	<ul><li>Y->A,F at 220: Abolishes the ITAM-mediated-activating activity</li><li>Y->A,F at 231: Abolishes the ITAM-mediated-activating activity</li></ul>									1
Q8NF91	23345	<ul><li>Missing at 8758-8763: Abolishes the nuclear envelope targeting, induces a cytoplasmic localization</li></ul>	localization	GO:0051179			nuclear envelope	GO:0005635			1
Q8NFA2	124056	<ul><li>R->Q at 40: Loss of ability to activate NOX1 associated with loss of lipid-binding and plasma membrane localization</li><li>W->R at 202: Loss of ability to activate NOX3 and interact with CYBA. Induces interaction with NOXA1 in vitro</li><li>W->R at 274: Induces interaction with NOXA1 in vitro</li><li>P->A at 332: Loss of intramolecular interaction</li><li>R->A at 334: Loss of intramolecular interaction</li></ul>	localization	GO:0051179	lipid-binding	GO:0008289	plasma membrane	GO:0005886	<li>Q95MN4</li><li>P52650</li><li>Q9Y5S8</li><li>Q95L73</li><li>P13498</li><li>Q9N2H0</li><li>Q9HBY0</li><li>O46521</li>		1
Q8NFU5	253430	<ul><li>RK->QQ at 322-323: Interferes with nuclear localization</li><li>KK->QQ at 327-328: Interferes with nuclear localization</li></ul>	localization	GO:0051179							1
Q8NG08	92797	<ul><li>K->A at 481: No ATPase activity</li><li>E->Q at 591: No ATPase activity</li></ul>			ATPase activity	GO:0016887					1
Q8NG50	201299	<ul><li>RHK->AAA at 98-100: Reduces its nuclear and nucleolar accumulation. Increases its cytoplasmic accumulation</li><li>YYF->AAA at 120-122: Does not affect its subcellular distribution</li></ul>									1
Q8NG66	79858	<ul><li>K->R at 61: Loss of kinase activity</li></ul>			kinase activity	GO:0016301					1
Q8NHL6	10859	<ul><li>Y->F at 533: Impairs receptor phosphorylation and abolishes inhibition of serotonin release. No effect on PTPN6 binding; when associated with F-562</li><li>Y->F at 562: No effect on PTPN6 binding; when associated with F-533</li><li>Y->F at 614: No effect on PTPN6 binding. Abolishes PTPN6 binding; when associated with F-644</li><li>Y->F at 644: Reduces PTPN6 binding. Abolishes PTPN6 binding; when associated with F-614</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488			P29350		1
Q8NHW3	389692	<ul><li>S->A at 14: Abolishes transactivation activity; when associated with A-65</li><li>S->A at 49: Diminishes transcriptional activity and transforming activity and abolishes ubiquitination; when associated with A-53; A-57 and A-61</li><li>T->A at 53: Diminishes transcriptional activity and transforming activity and abolishes ubiquitination; when associates with A-49; A-57 and A-61</li><li>T->A at 57: Diminishes transcriptional activity and transforming activity and abolishes ubiquitination; when associates with A-49; A-53 and A-61</li><li>S->A at 61: Diminishes transcriptional activity and transforming activity and abolishes ubiquitination; when associated with A-49; A-53 and A-57</li><li>S->A at 65: Greatly reduces phosphorylation and reduces transcriptional activity; when associated with A-14</li></ul>	phosphorylation	GO:0016310							1
Q8NHY2	64326	<ul><li>RKR->AKA at 111-113: Abolishes localization to the nucleus</li><li>C->A at 136: Abolishes p53 ubiquitination and degradation but not that of JUN; when associated with A-139</li><li>C->A at 139: Abolishes p53 ubiquitination and degradation but not that of JUN; when associated with A-136</li></ul>	localization	GO:0051179			nucleus	GO:0005634	<li>Q9TUB2</li><li>P02340</li><li>P56423</li><li>P56424</li><li>O12946</li><li>P05411</li><li>Q42578</li><li>O57538</li><li>P61260</li><li>P10361</li><li>O77627</li><li>Q9W679</li><li>Q9W678</li><li>Q9TTA1</li><li>P18870</li><li>P12981</li><li>P19559</li><li>O93379</li><li>P19558</li><li>Q8SPZ3</li><li>P79820</li><li>Q92143</li><li>P54864</li><li>P04637</li><li>Q29537</li><li>P05412</li><li>P56432</li><li>O09185</li><li>P79892</li>		1
Q8NI08	135112	<ul><li>LNIHEDL->ANAHED at 511-517: No action on the E2-induced ESR1 binding</li><li>LI->AA at 522-523: Abolishes completely the E2-induced ESR1 binding</li></ul>			<li>binding</li><li>E2</li>	<li>GO:0005488</li><li>GO:0004840</li>			<li>Q9TV98</li><li>Q9QZJ5</li><li>P49884</li><li>Q91424</li><li>Q91250</li><li>Q29040</li><li>P38111</li><li>Q9YHT3</li><li>P50242</li><li>P50241</li><li>P03372</li><li>P16058</li><li>Q9YH33</li><li>Q9PVZ9</li><li>P50240</li><li>P06212</li><li>P57753</li><li>Q53AD2</li><li>P49885</li><li>P49886</li><li>Q9YHZ7</li><li>O42132</li>		1
Q8NI17	133396	<ul><li>Y->A at 639: No effect on STAT1 and STAT3 activation. Slight decrease; when associated with A-670 and A-708</li><li>Y->F at 639: Abrogates STAT5 activation. Mild effect on STAT1 activation. No effect on STAT3 activation</li><li>Y->A at 670: No effect on STAT1 and STAT3 activation. Slight decrease; when associated with A-639 and A-708</li><li>Y->F at 670: No effect on STAT3 and STAT5 activation. Mild effect on STAT1 activation</li><li>Y->A at 708: No effect on STAT1 and STAT3 activation. Slight decrease; when associated with A-639 and A-670</li><li>Y->F at 708: Abrogates STAT3 activation. Loss of interaction with STAT3. Mild effect on STAT1 activation. No effect on STAT5 activation</li></ul>							<li>P42224</li><li>P42231</li><li>P61635</li><li>Q764M5</li><li>P42229</li><li>P40763</li>		1
Q8NI35	10207	<ul><li>L->W at 19: Reduces L27 domain binding affinity to MPP5 L27 domain</li><li>F->W at 38: Reduces L27 domain binding affinity to MPP5 L27 domain</li></ul>			binding	GO:0005488			<li>Q5RDQ2</li><li>Q99546</li><li>Q8N3R9</li>		1
Q8TAI7	121268	<ul><li>N->A at 41: Partially impaired in RPS6K1 activation</li><li>F->A at 54: Partially deficient in guanine nucleotide binding</li><li>L->A at 56: Partially deficient in guanine nucleotide binding</li><li>D->K at 60: Significant decrease in NF-kappa B activation</li><li>Q->L at 64: Constitutively active</li></ul>			nucleotide binding	GO:0000166					1
Q8TAS1	127933	<ul><li>K->A at 54: Loss of kinase activity</li></ul>			kinase activity	GO:0016301					1
Q8TBC4	9039	<ul><li>F->G at 65: Reduces affinity for UBE2M</li><li>I->A at 148: No effect on NEDD8 adenylation</li><li>HI->AA at 160-161: Reduces affinity for UBE2M</li><li>D->A at 167: Abolishes NEDD8 adenylation</li><li>P->A at 192: Reduces affinity for UBE2M; when associated with A-195 and A-197</li><li>I->A at 195: Reduces affinity for UBE2M; when associated with A-192 and A-197</li><li>P->A at 197: Reduces affinity for UBE2M; when associated with A-192 and A-195</li><li>R->Q at 211: Abolishes specificity for NEDD8</li><li>L->A at 214: Reduces affinity for UBE2M; when associated with A-217</li><li>M->A at 217: Reduces affinity for UBE2M; when associated with A-214</li><li>LY->DD at 227-228: Strongly reduces NEDD8 adenylation</li><li>C->S at 237: Abolishes thioester intermediate formation</li><li>T->A at 238: No effect on NEDD8 adenylation; impairs thioester intermediate formation</li><li>I->A at 310: No effect on NEDD8 adenylation or thioester intermediate formation; impairs NEDD8 transfer to UBE2M</li><li>I->A at 331: Reduces affinity for UBE2M</li><li>YTYTFE->ATATA at 352-357: Abolishes NEDD8 adenylation</li><li>S->P at 368: Impairs NEDD8 transfer to UBE2M</li><li>Q->P at 369: No effect on NEDD8 transfer to UBE2M</li><li>L->P at 370: Impairs NEDD8 transfer to UBE2M</li><li>T->A at 412: Impairs NEDD8 transfer to UBE2M</li><li>L->A at 415: Impairs NEDD8 transfer to UBE2M</li><li>V->A at 418: Impairs NEDD8 transfer to UBE2M</li><li>I->A at 421: Impairs NEDD8 transfer to UBE2M</li><li>R->A at 424: No effect on NEDD8 transfer to UBE2M</li></ul>							<li>Q15843</li><li>Q9SHE7</li><li>P61081</li><li>P0C031</li><li>Q4PLJ0</li><li>P0C030</li><li>P61282</li><li>P0C032</li>		1
Q8TCJ0	26260	<ul><li>S->L at 244: Loss of SKP1 binding</li></ul>			binding	GO:0005488			<li>Q39255</li><li>P52286</li><li>P63208</li>		1
Q8TCT1	162466	<ul><li>D->N at 32: Abolishes phosphatase activity</li><li>D->N at 43: Strongly reduces reactivity toward PEA and PCho substrates. Abolishes phosphatase activity; when associated with N-123</li><li>D->N at 123: Strongly reduces reactivity toward PEA and PCho substrates. Abolishes phosphatase activity; when associated with N-43</li><li>D->S at 203: Abolishes phosphatase activity</li></ul>							<li>P0C1A8</li><li>P0C1A9</li><li>Q5X1E5</li><li>Q7M7K5</li><li>Q7MAZ9</li><li>Q8XBL4</li><li>Q88A53</li><li>Q5P3T0</li><li>Q7MBF4</li><li>Q8Z3M9</li><li>Q5PC82</li><li>Q5ZRX9</li><li>Q821A6</li><li>Q87SK9</li><li>Q9JZ88</li><li>Q9CP21</li><li>Q82U82</li><li>Q9I5V3</li><li>Q5F8K9</li><li>Q63YC3</li><li>Q8Y395</li><li>Q6LV05</li><li>Q8ZLY4</li><li>Q6FA38</li><li>Q9PDL7</li><li>Q62EU1</li><li>Q9JUB2</li><li>Q5WT58</li><li>Q665U9</li><li>Q57JQ5</li><li>Q9KPC6</li><li>Q8P5D4</li><li>Q8CWL6</li><li>Q8PPG9</li><li>P06961</li><li>P45269</li><li>Q9L7A3</li><li>Q88QU2</li><li>Q6D160</li><li>Q8ZI64</li><li>Q60CQ4</li><li>Q87DS9</li><li>Q65Q41</li><li>Q5E2K7</li><li>Q8CXX6</li>		1
Q8TCT7	56928	<ul><li>D->A at 421: Loss of catalytic activity toward ITM2B</li></ul>			catalytic activity	GO:0003824			<li>Q60HC1</li><li>Q9Y287</li><li>O42204</li><li>Q3T0P7</li><li>Q5R876</li>		1
Q8TCT8	84888	<ul><li>D->A at 412: Loss of catalytic activity toward ITM2B</li></ul>			catalytic activity	GO:0003824			<li>Q60HC1</li><li>Q9Y287</li><li>O42204</li><li>Q3T0P7</li><li>Q5R876</li>		1
Q8TCT9	81502	<ul><li>N->Q at 10: Abolishes N-glycosylation; when associated with Q-20</li><li>N->Q at 20: Abolishes N-glycosylation; when associated with Q-10</li><li>D->A at 265: No effect on inhibitor binding; abolishes catalytic activity</li></ul>			<li>binding</li><li>catalytic activity</li>	<li>GO:0005488</li><li>GO:0003824</li>					1
Q8TD08	225689	<ul><li>K->R at 42: Loss of autophosphorylation and activity</li><li>T->A at 175: Loss of autophosphorylation and activity</li><li>Y->A at 177: Loss of autophosphorylation and activity</li></ul>	autophosphorylation	GO:0046777							1
Q8TD19	91754	<ul><li>K->M at 81: Loss of activity and autophosphorylation</li><li>T->A at 210: Significant reduction of autophosphorylation</li><li>T->A at 214: No effect on autophosphorylation</li></ul>	autophosphorylation	GO:0046777							1
Q8TD43	54795	<ul><li>L->A,C at 275: Abolishes ability to restore sensitivity to Ca(2+) after desensitization</li><li>I->N at 278: No effect</li><li>D->N at 279: No effect</li><li>G->A at 324: No effect</li><li>G->A at 325: Abolishes ability to restore sensitivity to Ca(2+) after desensitization</li><li>R->A at 327: No effect</li><li>Q->E at 977: Alters the monovalent cation permeability sequence and results in a pore with moderate Ca(2+) permeability</li><li>EDMDVA->TIIDGP at 981-986: Induces a functional channel that combines the gating hallmarks of TRPM4 (activation by Ca(2+)) with TRPV6-like sensitivity to block by extracellular Ca(2+) and Mg(2+) as well as Ca(2+) permeation</li><li>E->A at 981: Results in a channel with normal permeability properties but with a reduced sensitivity to block by intracellular spermine</li><li>D->A at 982: Results in a functional channel that exhibits extremely fast desensitization, possibly indicating destabilization of the pore</li><li>D->A at 984: Results in a non-functional channel with a dominant negative phenotype</li><li>K->Q at 1059: Does not affect PIP2-binding</li><li>R->Q at 1072: Does not affect PIP2-binding</li><li>Missing at 1136-1141: Results in a channel with very rapid desensitization and highly reduced sensitivity to PIP2</li><li>S->A at 1145: Decreases the sensitivity to Ca(2+)</li><li>S->A at 1152: Decreases the sensitivity to Ca(2+)</li></ul>			binding	GO:0005488	<li>intracellular</li><li>pore</li><li>extracellular</li>	<li>GO:0005622</li><li>GO:0046930</li><li>GO:0005576</li>	<li>Q9H1D0</li><li>P52960</li><li>P52488</li><li>Q8TD43</li>		1
Q8TDC3	84446	<ul><li>K->A at 75: Loss of kinase activity</li><li>T->A at 205: Prevents phosphorylation and activation by STK11 complex</li></ul>	phosphorylation	GO:0016310	kinase activity	GO:0016301			<li>Q15831</li><li>Q0GGW5</li>		1
Q8TDF6	115727	<ul><li>F->S at 548: Loss of cell membrane targeting</li></ul>					cell membrane	GO:0005886			1
Q8TDG4	113510	<ul><li>K->M at 365: Abolishes ATPase and DNA helicase activity</li></ul>							<li>Q8V736</li><li>O67037</li><li>Q9UZ86</li><li>Q68772</li><li>O51934</li><li>P74759</li><li>P37987</li><li>P22657</li><li>Q04575</li><li>Q971T7</li><li>P27328</li><li>P28726</li><li>Q07630</li><li>P27327</li><li>Q9WJB2</li><li>Q3I5J6</li><li>Q66914</li><li>P16342</li><li>Q89273</li><li>P36286</li><li>Q66198</li><li>P22168</li><li>P19751</li><li>Q8V6W7</li><li>P28897</li><li>Q96725</li><li>P19811</li><li>Q91A29</li><li>O29238</li><li>P09395</li><li>P15402</li><li>Q86117</li><li>P09498</li><li>Q86119</li><li>Q58907</li><li>Q83017</li><li>Q97ZF5</li><li>Q8R979</li><li>Q6F598</li><li>Q08582</li><li>Q91AV2</li><li>P17779</li><li>O58530</li><li>O67226</li><li>Q07518</li><li>P95479</li><li>P54634</li><li>Q8ZXT5</li><li>Q9IW06</li><li>Q04544</li><li>Q975P6</li><li>Q8V439</li><li>P17965</li><li>Q91QT2</li><li>Q04561</li><li>Q97ZZ8</li><li>P27411</li><li>P27410</li><li>P27920</li><li>P22591</li><li>Q9PYA3</li><li>P20951</li><li>P15095</li><li>Q9YN02</li><li>P27407</li><li>Q06502</li><li>P18458</li><li>Q05002</li><li>Q9YCB6</li><li>P59641</li><li>Q69014</li><li>Q8B912</li><li>P27409</li><li>Q9YC75</li>		1
Q8TDQ1	146722	<ul><li>Y->F at 205: No interaction with PTPN6</li><li>Y->F at 249: Interaction with PTPN6</li><li>Y->F at 284: Interaction with PTPN6</li></ul>							P29350		1
Q8TDR2	140901	<ul><li>K->M at 98: No autophosphorylation</li></ul>	autophosphorylation	GO:0046777							1
Q8TEK3	84444	<ul><li>GSG->RCR at 163-165: Abolishes methyltransferase activity</li><li>N->A,D at 241: Loss of activity</li><li>Y->A at 312: Loss of activity</li><li>Y->F at 312: No effect</li></ul>							<li>Q00020</li><li>P03588</li><li>P03589</li><li>Q83270</li><li>P28931</li><li>P06011</li><li>P17769</li><li>P20122</li><li>Q66121</li><li>O40976</li><li>P28726</li><li>P27752</li><li>Q83264</li>		1
Q8TEW0	56288	<ul><li>Y->F at 1127: Delayed epithelial tight junction assembly</li></ul>					tight junction	GO:0005923			1
Q8TEY5	148327	<ul><li>R->G at 335: Abolishes cleavage by SP1</li></ul>							<li>P09179</li><li>P08047</li><li>Q9DF68</li>		1
Q8TF30	123720	<ul><li>W->A at 807: Decreases nucleation-promoting factor activity and Arp2/3 complex activation</li></ul>							<li>Q9R045</li><li>P61161</li><li>Q5M7U6</li><li>Q9UUJ1</li>		1
Q8WTP8	64782	<ul><li>D->A at 114: Abolishes exonuclease activity; when associated with A-116 and A-258</li><li>E->A at 116: Abolishes exonuclease activity; when associated with A-114 and A-258</li><li>D->A at 258: Abolishes exonuclease activity; when associated with A-114 and A-116</li></ul>							<li>P20321</li><li>P00638</li><li>P03697</li>		1
Q8WTS6	80854	<ul><li>E->A at 220: Increases near-attack conformations</li><li>E->A at 228: Increases near-attack conformations</li><li>Y->A at 245: Significantly reduces the monomethyltransferase activity but increases the dimethyltransferase activity</li><li>K->A at 294: Significantly reduces the catalytic activity</li><li>H->A,G at 297: Abolishes methyltransferase activity</li><li>K->A at 317: Induces a reduction in methyltransferase activity toward TAF10 but an increased methyltransferase activity for H3 and p53/TP53</li></ul>			catalytic activity	GO:0003824			<li>Q9TUB2</li><li>P03588</li><li>P03589</li><li>P28726</li><li>O36006</li><li>O57538</li><li>P10360</li><li>P10361</li><li>Q9W679</li><li>Q00020</li><li>Q9W678</li><li>Q9TTA1</li><li>Q95330</li><li>Q8SPZ3</li><li>P79820</li><li>Q92143</li><li>P04637</li><li>Q66121</li><li>Q00366</li><li>P51664</li><li>Q9WUR6</li><li>P67939</li><li>P67938</li><li>P02340</li><li>P56423</li><li>P56424</li><li>O12946</li><li>P25035</li><li>Q12962</li><li>Q42578</li><li>Q64662</li><li>Q12030</li><li>P61260</li><li>P13481</li><li>Q83270</li><li>P28931</li><li>P19559</li><li>O93379</li><li>P06011</li><li>P19558</li><li>P41685</li><li>P17769</li><li>P20122</li><li>Q29537</li><li>Q29480</li><li>O40976</li><li>O09185</li><li>P79892</li><li>P27752</li><li>Q83264</li>		1
Q8WUM9	6574	<ul><li>DTGDVSSKV->KQEA at 550-558: Loss of virus infectibility</li><li>D->K at 550: Drastic reduction of virus infectibility, but conserved virus binding ability</li><li>Missing at 550: Loss of virus infectibility</li></ul>			binding	GO:0005488					1
Q8WUP2	54751	<ul><li>KR->TG at 7-8: Localizes to cell-ECM adhesions; abolishes FLNA and FLNC interactions; failed to decorate actin filaments</li></ul>							<li>Q92192</li><li>Q92193</li><li>P53499</li><li>P26183</li><li>P53498</li><li>O13419</li><li>Q9P4D1</li><li>P48465</li><li>P53455</li><li>Q39596</li><li>Q39758</li><li>P26182</li><li>P80709</li><li>Q9UVX4</li><li>O17320</li><li>P53689</li><li>P78711</li><li>P30161</li><li>P17128</li><li>P45521</li><li>P45520</li><li>P20904</li><li>P81085</li><li>Q6TCF2</li><li>Q99023</li><li>Q75D00</li><li>P51775</li><li>P10365</li><li>P60011</li><li>P60010</li><li>Q8SWN8</li><li>O16808</li><li>P02577</li><li>P21333</li><li>P10989</li><li>P68555</li><li>Q05214</li><li>Q8X119</li><li>O65316</li><li>O65315</li><li>O65314</li><li>P53491</li><li>P91754</li><li>P13363</li><li>Q13201</li><li>P11426</li><li>O81221</li><li>Q11212</li><li>P50138</li><li>P53477</li><li>P53476</li><li>P60009</li><li>P53502</li><li>Q2U7A3</li><li>P53500</li><li>Q9UVZ8</li><li>P14235</li><li>O00937</li><li>Q9UVF3</li><li>Q24733</li><li>P90689</li><li>P24902</li><li>Q14315</li><li>O74258</li>		1
Q8WV28	29760	<ul><li>Y->F at 72: Significant phosphorylation reduction; when associated with F-84; F-96 and F-178</li><li>Y->F at 84: Significant phosphorylation reduction; when associated with F-72; F-96 and F-178</li><li>Y->F at 96: Significant phosphorylation reduction; when associated with F-72; F-84 and F-178</li><li>Y->F at 178: Significant phosphorylation reduction; when associated with F-72; F-84 and F-96</li></ul>	phosphorylation	GO:0016310							1
Q8WVM0	51106	<ul><li>G->A at 65: Abolishes methyltransferase activity, DNA-binding and SAM-binding. Does not abolish transcription activator function</li><li>N->A at 141: Does not affect SAM-binding, DNA-binding nor transcription activator function</li><li>K->A at 220: Abolishes methyltransferase activity. Does not affect SAM-binding, DNA-binding nor transcription activator function</li></ul>	transcription	GO:0006350	<li>binding</li><li>DNA-binding</li>	<li>GO:0005488</li><li>GO:0003677</li>			<li>Q00020</li><li>P03588</li><li>P03589</li><li>Q83270</li><li>P28931</li><li>P06011</li><li>P17769</li><li>P20122</li><li>Q66121</li><li>O40976</li><li>P28726</li><li>P27752</li><li>Q83264</li>		1
Q8WVQ1	124583	<ul><li>D->A at 112: Reduces activity by 99%</li><li>D->A at 114: Reduces activity by 99%</li><li>G->E at 152: Slightly reduced activity</li><li>E->Y at 160: Increases GDPase activity 2-fold and ADPase activity 5-fold</li><li>R->A at 163: Reduces activity by 98%</li><li>E->Q at 166: Reduces activity by 95%</li><li>S->A at 168: Reduces activity by over 99.9%</li><li>D->N at 169: Reduces activity by 96%</li><li>D->A at 181: Loss of activity</li><li>D->N at 182: Reduces activity by over 99.9%</li><li>D->A at 205: Slightly reduced activity</li><li>E->Q at 215: Reduces activity by 99%</li><li>E->M at 246: Increases activity 5-fold</li><li>R->A at 301: Reduces activity by 99%</li></ul>							<li>P40009</li><li>Q9HEM6</li><li>P80595</li><li>Q9UT35</li><li>Q8TGH6</li><li>Q8TGG8</li><li>P50635</li><li>P32621</li>		1
Q8WWA0	55600	<ul><li>C->S at 31: Forms mainly monomers; when associated with S-48</li><li>C->S at 48: Forms mainly dimers. Forms mainly monomers; when associated with S-31</li></ul>									1
Q8WWL7	85417	<ul><li>R->A at 60: In cycB3XA; prevents its destruction after completion of anaphase; when associated with A-63 and A-68</li><li>F->A at 63: In cycB3XA; prevents its destruction after completion of anaphase; when associated with A-60 and A-68</li><li>N->A at 68: In cycB3XA; prevents its destruction after completion of anaphase; when associated with A-60 and A-63</li></ul>	anaphase	GO:0051322							1
Q8WWN8	64411	<ul><li>RR->AA at 307-308: Loss of PtdIns(3,4,5)P3 binding</li></ul>			binding	GO:0005488					1
Q8WWY8	200879	<ul><li>S->A at 154: Loss of lipase activity</li></ul>							Q7M4U7		1
Q8WXD0	122042	<ul><li>D->Y at 647: Leads to constitutive increase of basal cAMP</li></ul>									1
Q8WXE1	84126	<ul><li>EE->AA at 769-770: Abolishes interaction with ATR and its recruitment to sites of DNA damage</li><li>DD->AA at 774-775: Abolishes interaction with ATR and its recruitment to sites of DNA damage</li></ul>							<li>Q13535</li><li>Q9H6X2</li><li>Q9FKS4</li><li>P20848</li>		1
Q8WXE9	85439	<ul><li>W->A at 738: Reduces interaction with SYT1</li><li>K->A at 740: Reduces interaction with SYT1</li></ul>							<li>Q60HC0</li><li>P41823</li><li>P21579</li><li>Q5R4J5</li><li>P47191</li><li>P48018</li>		1
Q8WXF1	55269	<ul><li>F->A at 119: Abolishes accumulation in paraspeckles, but not in perinucleolar caps; when associated with A-121; A-198 and A-200</li><li>F->A at 121: Abolishes accumulation in paraspeckles, but not in perinucleolar caps; when associated with A-119; A-198 and A-200</li><li>K->A at 198: Abolishes accumulation in paraspeckles, but not in perinucleolar caps; when associated with A-119; A-121 and A-200</li><li>F->A at 200: Abolishes accumulation in paraspeckles, but not in perinucleolar caps; when associated with A-119; A-121 and A-198</li></ul>					paraspeckles	GO:0042382			1
Q8WY64	29116	<ul><li>C->A at 387: Abolishes ubiquitin ligase activity</li></ul>			ligase activity	GO:0016874			<li>P69326</li><li>P08565</li><li>P69322</li><li>P69323</li><li>P69324</li><li>P69325</li><li>P68196</li><li>O46543</li><li>P68197</li><li>Q05550</li><li>P68198</li><li>P68199</li><li>P19848</li><li>P42739</li><li>P68195</li><li>Q867C2</li><li>P62991</li><li>P62990</li><li>P61863</li><li>P61864</li><li>P61862</li><li>Q867C4</li><li>Q867C3</li><li>P23398</li><li>P68204</li><li>P84589</li><li>Q865C5</li><li>P42740</li><li>P68201</li><li>Q8MKD1</li><li>P14792</li><li>P63049</li><li>P0C072</li><li>P63051</li><li>P69308</li><li>P69309</li><li>P20685</li><li>P15174</li><li>P62976</li><li>P62977</li><li>P62974</li><li>P62975</li><li>P62972</li><li>P13117</li><li>P14624</li><li>P62973</li><li>P46574</li><li>P69310</li><li>P69313</li><li>P69314</li><li>P69311</li><li>P08618</li><li>P69312</li><li>P69317</li><li>P69318</li><li>P69315</li><li>P0C014</li><li>P69316</li><li>P59263</li><li>P69319</li><li>P49634</li><li>P49635</li><li>Q9Y848</li><li>P22589</li><li>P62988</li><li>P62989</li><li>P69321</li><li>P23324</li><li>P69320</li><li>P59669</li>		1
Q8WYL5	54434	<ul><li>C->S at 393: Abrogates phosphatase activity</li><li>W->A at 458: Impairs stimulation of phosphatase activity by actin but does not affect basal activity</li><li>S->A at 937: Reduces binding to YWHAB, YWHAG, YWHAQ and YWHAZ. Abolishes binding to YWHAB, YWHAG, YWHAQ and YWHAZ and increases association with F-actin; when associated with A-978</li><li>S->A at 978: Reduces binding to YWHAB, YWHAG, YWHAQ and YWHAZ. Abolishes binding to YWHAB, YWHAG, YWHAQ and YWHAZ and increases association with F-actin; when associated with A-937</li></ul>			binding	GO:0005488			<li>P26183</li><li>Q88A53</li><li>Q7MBF4</li><li>Q5PC82</li><li>Q9P4D1</li><li>P48465</li><li>P53455</li><li>Q821A6</li><li>Q87SK9</li><li>Q39596</li><li>P26182</li><li>Q39758</li><li>P80709</li><li>Q9I5V3</li><li>Q5F8K9</li><li>Q9UVX4</li><li>O17320</li><li>P78711</li><li>P17128</li><li>P45521</li><li>P45520</li><li>Q99023</li><li>Q4R572</li><li>Q5WT58</li><li>Q8P5D4</li><li>P10989</li><li>P45269</li><li>P68253</li><li>P68251</li><li>P68252</li><li>P68250</li><li>Q8ZI64</li><li>Q60CQ4</li><li>P91754</li><li>Q7MAZ9</li><li>P11426</li><li>Q5P3T0</li><li>O81221</li><li>Q5ZRX9</li><li>P53477</li><li>P53476</li><li>P63103</li><li>Q9CP21</li><li>Q82U82</li><li>P27348</li><li>P60009</li><li>P53502</li><li>Q8ZLY4</li><li>Q6FA38</li><li>P53500</li><li>Q62EU1</li><li>P63104</li><li>O00937</li><li>P14235</li><li>Q9UVF3</li><li>Q5RC20</li><li>Q665U9</li><li>Q8PPG9</li><li>Q9L7A3</li><li>Q87DS9</li><li>O74258</li><li>Q92192</li><li>Q92193</li><li>P53499</li><li>Q5X1E5</li><li>P53498</li><li>O13419</li><li>P31946</li><li>Q9JZ88</li><li>Q63YC3</li><li>P53689</li><li>Q8Y395</li><li>P30161</li><li>Q6LV05</li><li>P20904</li><li>P81085</li><li>Q6TCF2</li><li>Q75D00</li><li>Q9PDL7</li><li>Q5F3W6</li><li>P51775</li><li>P10365</li><li>P60011</li><li>P60010</li><li>O16808</li><li>Q57JQ5</li><li>Q8SWN8</li><li>P02577</li><li>P68555</li><li>P06961</li><li>P29361</li><li>Q88QU2</li><li>Q05214</li><li>Q8X119</li><li>O65316</li><li>O65315</li><li>O65314</li><li>Q5ZLQ6</li><li>Q5E2K7</li><li>P53491</li><li>P13363</li><li>Q8CXX6</li><li>Q7M7K5</li><li>Q5ZMD1</li><li>Q8XBL4</li><li>Q8Z3M9</li><li>Q5RFJ2</li><li>Q11212</li><li>P50138</li><li>P61981</li><li>Q6Q6X0</li><li>Q2U7A3</li><li>Q9UVZ8</li><li>Q9JUB2</li><li>Q5ZKC9</li><li>Q3SZI4</li><li>Q9KPC6</li><li>Q8CWL6</li><li>Q24733</li><li>P90689</li><li>P24902</li><li>Q6D160</li><li>Q5R651</li><li>Q65Q41</li>		1
Q8WZ42	7273	<ul><li>K->A at 32207: Disrupts catalytic activity</li><li>Y->E at 32341: No phosphorylation on tyrosine</li></ul>	phosphorylation	GO:0016310	catalytic activity	GO:0003824					1
Q8WZ55	7809	<ul><li>Y->A at 98: Stimulation of CLCNKA and CLCNKB currents enhanced; intense localization in the plasma membrane with no intracellular localization observed</li></ul>	localization	GO:0051179			<li>intracellular</li><li>plasma membrane</li>	<li>GO:0005622</li><li>GO:0005886</li>	<li>P51803</li><li>P51800</li><li>P51801</li><li>P51804</li>		1
Q8WZ73	117584	<ul><li>H->A at 333: Loss of E3 ubiquitin protein ligase activity</li></ul>							<li>Q8RSY1</li><li>Q2QCI9</li>		1
Q92466	1643	<ul><li>L->A at 258: Impairs interaction with DDB1</li><li>S->A at 262: Impairs interaction with DDB1</li><li>D->A at 264: Impairs interaction with DDB1</li><li>I->A at 269: Impairs interaction with DDB1</li><li>W->A at 270: Impairs interaction with DDB1</li><li>L->A at 272: Impairs interaction with DDB1</li><li>R->A at 273: Impairs interaction with DDB1</li><li>L->P at 350: Impairs interaction with DDB1</li></ul>							<li>Q16531</li><li>Q6QNU4</li><li>Q6E7D1</li><li>P33194</li>		1
Q92502	9754	<ul><li>R->E at 608: No effect on cell morphology when overexpressed</li></ul>									1
Q92540	9887	<ul><li>K->E at 66: Abolishes interaction with RENT1; when associated with E-163</li><li>R->E at 163: Abolishes interaction with RENT1; when associated with E-66</li></ul>							<li>Q98TR3</li><li>Q92900</li>		1
Q92542	23385	<ul><li>DY->AA at 336-337: Increases production of amyloid beta (beta-APP40 and beta-APP42) in APP processing</li></ul>							<li>Q60495</li><li>P0A3Z4</li><li>P75313</li><li>P0A3Z2</li><li>O73683</li><li>Q28280</li><li>P0A3Z3</li><li>P08592</li><li>P79307</li><li>P0A3Z1</li><li>Q28757</li><li>P05067</li><li>P29216</li><li>Q28748</li><li>Q28053</li><li>Q5IS80</li><li>P47566</li><li>O93279</li><li>Q11207</li><li>P12023</li><li>P53601</li><li>Q95241</li><li>Q29149</li>		1
Q92560	8314	<ul><li>C->S at 91: Abolishes enzymatic activity</li><li>L->P at 691: Abolishes interaction with BRCA1</li></ul>							<li>Q864U1</li><li>P38398</li><li>Q95153</li><li>Q6J6J0</li><li>Q6J6I8</li><li>Q9GKK8</li><li>Q6J6I9</li>		1
Q92600	9125	<ul><li>R->E at 227: Loss of DNA binding</li></ul>			DNA binding	GO:0003677					1
Q92614	399687	<ul><li>RG->AA at 114-115: No effect on interaction with actin</li><li>VL->AA at 117-118: Abolishes interaction with actin</li></ul>							<li>Q92192</li><li>Q92193</li><li>P53499</li><li>P26183</li><li>P53498</li><li>O13419</li><li>Q9P4D1</li><li>P48465</li><li>P53455</li><li>Q39596</li><li>Q39758</li><li>P26182</li><li>P80709</li><li>Q9UVX4</li><li>O17320</li><li>P53689</li><li>P78711</li><li>P30161</li><li>P17128</li><li>P45521</li><li>P45520</li><li>P20904</li><li>P81085</li><li>Q6TCF2</li><li>Q99023</li><li>Q75D00</li><li>P51775</li><li>P10365</li><li>P60011</li><li>P60010</li><li>Q8SWN8</li><li>O16808</li><li>P02577</li><li>P10989</li><li>P68555</li><li>Q05214</li><li>Q8X119</li><li>O65316</li><li>O65315</li><li>O65314</li><li>P53491</li><li>P91754</li><li>P13363</li><li>P11426</li><li>O81221</li><li>Q11212</li><li>P50138</li><li>P53477</li><li>P53476</li><li>P60009</li><li>P53502</li><li>Q2U7A3</li><li>P53500</li><li>Q9UVZ8</li><li>P14235</li><li>O00937</li><li>Q9UVF3</li><li>Q24733</li><li>P90689</li><li>P24902</li><li>O74258</li>		1
Q92643	10026	<ul><li>C->A at 92: Partial loss of activity</li><li>C->S at 92: Decrease in activity</li><li>H->A at 164: Loss of activity</li><li>C->A at 206: Loss of activity</li><li>Missing at 311-395: Loss of activity</li></ul>									1
Q92698	8438	<ul><li>K->R at 189: Unable to rescue the MMS-sensitive phenotype of S cerevisiae rad54delta cells</li></ul>									1
Q92730	27289	<ul><li>T->N at 27: Impairs interaction with UBXD5</li><li>T->A at 45: Abolishes interaction with UBXD5</li></ul>									1
Q92738	9712	<ul><li>R->A at 106: Loss of GAP activity on RAB5A</li><li>D->A at 147: Loss of GAP activity on RAB5A</li><li>R->A at 150: Loss of GAP activity on RAB5A</li></ul>							<li>Q92263</li><li>P20936</li><li>P20339</li><li>Q92211</li><li>P09851</li><li>P18066</li><li>Q5PEA9</li><li>P74873</li><li>P61271</li><li>P74851</li><li>P50904</li>		1
Q92743	5654	<ul><li>S->A at 328: Loss of activity</li></ul>									1
Q92754	7022	<ul><li>Y->A at 59: Loss of interaction with WWOX; when associated with A-64</li><li>Y->A at 64: Loss of interaction with WWOX; when associated with A-59</li></ul>							<li>Q5F389</li><li>Q5R9W5</li><li>Q9NZC7</li><li>Q9VLU5</li>		1
Q92784	8110	<ul><li>W->E at 358: Abolishes binding to acetylated histones H3 and H4</li><li>C->R at 360: Abolishes binding to acetylated histones H3 and H4; when associated with R-363</li><li>C->R at 363: Abolishes binding to acetylated histones H3 and H4; when associated with R-360</li></ul>			binding	GO:0005488			<li>P61835</li><li>P61834</li><li>Q9P427</li><li>P61833</li><li>Q98RY4</li><li>P61832</li><li>P61831</li><li>P61830</li><li>P83864</li><li>P07041</li><li>P90543</li><li>P02299</li><li>P08437</li><li>Q757N1</li><li>P50564</li><li>P61836</li><li>Q06196</li><li>P08898</li><li>Q9HDN1</li><li>P23753</li><li>Q7XYZ0</li><li>Q9U7D1</li><li>Q2UCQ0</li><li>Q5DWI3</li><li>P80553</li><li>P40285</li><li>P84239</li><li>P84238</li><li>P84237</li><li>P84236</li><li>P22843</li><li>P84235</li>		1
Q92794	7994	<ul><li>C->G at 543: Abrogates HAT activity</li><li>G->E at 657: Abrogates HAT activity</li></ul>							<li>Q9EQQ9</li><li>Q8VIJ5</li><li>O60502</li><li>O60235</li>		1
Q92805	2800	<ul><li>Y->A at 697: Abolishes interaction with RAB6A and targeting to Golgi stack</li><li>W->A at 744: Reduces targeting to Golgi stack</li></ul>					Golgi stack	GO:0005795	<li>Q1KME6</li><li>Q5RAV6</li><li>P20340</li>		1
Q92831	8850	<ul><li>V->A at 752: Reduced acetyl-lysine binding</li><li>Y->A at 760: Reduced acetyl-lysine binding</li><li>Y->A at 802: Reduced acetyl-lysine binding</li><li>Y->A at 809: Complete loss of acetyl-lysine binding</li></ul>			binding	GO:0005488					1
Q92838	1896	<ul><li>R->C at 153: Abolishes proteolytic processing</li><li>K->N at 158: Abolishes proteolytic processing</li><li>R->A at 159: Abolishes proteolytic processing</li></ul>									1
Q92844	10010	<ul><li>Q->A at 182: Abolishes interaction with TRAF2 and TRAF3</li><li>T->A at 184: Abolishes interaction with TRAF2 and TRAF3</li><li>D->A at 185: Abolishes interaction with TRAF2; greatly diminishes interaction with TRAF3</li><li>D->A at 188: Diminishes interaction with TRAF2 and TRAF3</li><li>F->A at 194: Diminishes interaction with TRAF2 and TRAF3</li></ul>							<li>Q12933</li><li>Q13114</li>		1
Q92851	843	<ul><li>C->A at 401: Abolishes proteolytic activity</li></ul>									1
Q92878	10111	<ul><li>K->N at 42: Abolishes ability to degrade ATP</li><li>D->A at 1231: Abolishes ability to degrade ATP</li></ul>									1
Q92879	10658	<ul><li>F->L at 63: Does not reduce RNA-binding; when associated with D-331 and F-472. Abolishes ARE/EDEN-dependent deadenylation; when associated with D-331 and F-472</li><li>G->D at 331: Does not reduce RNA-binding; when associated with L-63 and F-472. Abolishes ARE/EDEN-dependent deadenylation; when associated with D-331 and F-472</li><li>L->F at 472: Does not reduce RNA-binding; when associated with L-63 and D-331. Abolishes ARE/EDEN-dependent deadenylation; when associated with D-331 and F-472</li></ul>			RNA-binding	GO:0003723					1
Q92887	1244	<ul><li>W->A,C at 1254: Fails to transport methotrexate, leukotriene C4 and estradiol glucuronide</li><li>W->F at 1254: Fails to transport methotrexate and leukotriene C4. Does not affect estradiol glucuronide transport</li><li>W->Y at 1254: Fails to transport methotrexate; reduces leukotriene C4 transport. Does not affect estradiol glucuronide transport</li></ul>	<li>glucuronide transport</li><li>transport</li>	<li>GO:0015779</li><li>GO:0006810</li>							1
Q92900	5976	<ul><li>R->C at 843: Abolishes NMD</li><li>S->A at 1089: Still phosphorylated but with less efficiency</li><li>S->A at 1107: Impairs phosphorylation</li><li>Q->N at 1108: Impairs phosphorylation</li></ul>	phosphorylation	GO:0016310							1
Q92932	5799	<ul><li>C->S at 945: Loss of activity</li></ul>									1
Q92947	2639	<ul><li>E->D at 414: Reduced catalytic activity</li></ul>			catalytic activity	GO:0003824					1
Q92963	6016	<ul><li>S->N at 35: Dominant negative. Loss of interaction with MLLT4, RLF and RALGDS</li><li>T->S at 53: Loss of interaction with MLLT4, RLF and RALGDS; when associated with L-79</li><li>E->G at 55: Loss of interaction with MLLT4, but not with RLF and RALGDS; when associated with L-79</li><li>Q->L at 79: Constitutively active. Dramatic reduction of the rate of GTP hydrolysis. Loss of interaction with MLLT4, RLF and RALGDS; when associated with S-53. Loss of interaction with MLLT4; when associated with G-55</li></ul>	GTP hydrolysis	GO:0006184					<li>P55196</li><li>Q5CZK3</li><li>O97937</li><li>Q13129</li><li>Q12967</li><li>Q6X7V3</li><li>P51461</li><li>P51460</li><li>O77801</li>		1
Q92974	9181	<ul><li>C->R at 53: Abolishes microtubule binding, increased activity in vitro</li><li>S->A at 143: Abolishes phosphorylation by PAK4, self aggregation in the cytoplasm. Increases activity; when associated with A-896</li><li>Y->A at 394: Reduces phosphorylation level, normal microtubule localization and activity</li><li>T->A at 679: Reduces phosphorylation level</li><li>S->A at 886: Normal activity</li><li>S->D at 886: Increases activity. Abolishes nucleotide exchange activity; when associated with D-960</li><li>S->A at 896: Abolishes phosphorylation by PAK4, self aggregation in the cytoplasm. Increases activity; when associated with A-143</li><li>S->A at 960: Normal activity</li><li>S->D at 960: Increases activity. Abolishes nucleotide exchange activity; when associated with D-886</li></ul>	<li>phosphorylation</li><li>localization</li>	<li>GO:0016310</li><li>GO:0051179</li>	microtubule binding	GO:0008017	<li>cytoplasm</li><li>microtubule</li>	<li>GO:0005737</li><li>GO:0005874</li>	O96013		1
Q92990	11146	<ul><li>P->A at 219: Loss of interaction with FKBP12 and FKBP59</li></ul>							<li>Q9TRY0</li><li>O04287</li><li>P48375</li><li>P30416</li><li>Q02790</li><li>Q8LGG0</li><li>P62942</li><li>Q9VL78</li><li>Q9QVC8</li><li>P27124</li><li>P62943</li>		1
Q92993	10524	<ul><li>S->A at 86: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-90. Reduced activity</li><li>S->A at 90: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-86. Reduced activity</li><li>L->A at 254: Does not affect phosphorylation; when associated with A-257</li><li>L->A at 257: Does not affect phosphorylation; when associated with A-254</li><li>G->A at 380: Loss of function. Does not affect phosphorylation</li></ul>	phosphorylation	GO:0016310							1
Q93009	7874	<ul><li>D->A at 164: Decreased binding to TP53 and MDM2</li><li>W->A at 165: Loss of binding to TP53 and MDM2</li><li>C->A at 223: Complete loss of activity</li><li>C->S at 223: No effect on TP53 binding but is defective in deubiquitinating p53</li><li>H->A at 456: Complete loss of activity</li><li>H->A at 464: Complete loss of activity</li></ul>			binding	GO:0005488			<li>Q9TUB2</li><li>P02340</li><li>P56423</li><li>P56424</li><li>O12946</li><li>P25035</li><li>Q42578</li><li>Q00987</li><li>O36006</li><li>Q64662</li><li>P56950</li><li>O57538</li><li>Q7YRZ8</li><li>P56951</li><li>P10360</li><li>P61260</li><li>P10361</li><li>Q9W679</li><li>Q9W678</li><li>P13481</li><li>Q9TTA1</li><li>Q95330</li><li>P19559</li><li>O93379</li><li>P19558</li><li>P41685</li><li>Q8SPZ3</li><li>P79820</li><li>Q92143</li><li>P04637</li><li>Q29537</li><li>Q60524</li><li>Q29480</li><li>O09185</li><li>Q00366</li><li>P79892</li><li>P51664</li><li>Q9WUR6</li><li>P67939</li><li>P67938</li>		1
Q93038	8718	<ul><li>L->A at 354: Suppresses homodimerization, TNFR1 interaction, and apoptosis induction</li><li>L->A at 356: Suppresses homodimerization, and TNFR1 interaction</li><li>D->A at 373: Suppresses homodimerization, and TNFR1 interaction</li></ul>	apoptosis	GO:0006915					<li>P19438</li><li>O19131</li><li>P50555</li>		1
Q93052	4026	<ul><li>T->A at 610: Abolishes binding to SCRIB</li><li>L->A at 612: Abolishes binding to SCRIB</li></ul>			binding	GO:0005488			Q14160		1
Q93077	8334	<ul><li>S->A at 2: Blocks the inhibition of transcription by RPS6KA5/MSK1</li></ul>	transcription	GO:0006350					<li>P32048</li><li>Q5R4K3</li><li>Q5F3L1</li><li>O75582</li>		1
Q93096	7803	<ul><li>T->F at 13: Reduces trimerization</li><li>D->A at 71: No effect on catalytic activity</li><li>D->A at 72: 80% loss of catalytic activity; delay in progression through G2/M</li><li>C->S at 104: Abolishes enzymatic activity</li><li>Q->A at 131: Reduces trimerization</li><li>C->S at 170: Redistributes to the nucleus in resting cells, but still locates to the mitotic spindle in dividing cells. Induces defects in cytokinesis</li><li>C->S at 171: No effect on subcellular location</li></ul>	cytokinesis	GO:0000910	catalytic activity	GO:0003824	<li>spindle</li><li>nucleus</li>	<li>GO:0005819</li><li>GO:0005634</li>			1
Q95460	3140	<ul><li>C->G at 283: No effect on cell surface expression</li></ul>					cell surface	GO:0009928,GO:0009986			1
Q969F2	85409	<ul><li>G->A at 2: Abrogates myristoylation and membrane association and impairs delivery of TGFA to the cell surface</li></ul>					<li>membrane</li><li>cell surface</li>	<li>GO:0016020</li><li>GO:0009928,GO:0009986</li>	<li>P98135</li><li>P98138</li><li>Q06922</li><li>P55244</li><li>P01135</li>		1
Q969H4	10256	<ul><li>W->A at 493: No interaction with Rho</li></ul>							<li>P51489</li><li>Q06447</li><li>P0AG30</li><li>P0AG31</li><li>P0AG32</li><li>P0AG33</li><li>Q89A22</li><li>P56466</li><li>P45835</li><li>Q03222</li><li>P38527</li><li>P35359</li><li>P44619</li><li>P33561</li><li>P52156</li><li>P52155</li><li>P52158</li><li>P52157</li><li>P57652</li><li>P17593</li><li>P52152</li><li>P52154</li><li>P17594</li><li>O83281</li><li>O51891</li><li>P52153</li><li>P66028</li><li>P15409</li><li>P66029</li><li>Q9ZLS9</li><li>P0A296</li><li>P0A295</li><li>P29403</li><li>Q9ZD24</li><li>P03304</li><li>O67031</li><li>P20350</li>		1
Q969K3	80196	<ul><li>H->A at 342: Loss of E3 ubiquitin protein ligase activity</li></ul>							<li>Q8RSY1</li><li>Q2QCI9</li>		1
Q969N2	51604	<ul><li>C->S at 182: Decrease in activity</li></ul>									1
Q969Q1	84676	<ul><li>C->A at 39: Loss of SUMO2-binding</li><li>H->A at 41: Loss of SUMO2-binding</li><li>C->A at 44: Loss of SUMO2-binding</li><li>C->A at 47: Loss of SUMO2-binding</li></ul>			binding	GO:0005488			<li>Q6LDZ8</li><li>P61958</li><li>P61956</li><li>P61955</li>		1
Q969S2	252969	<ul><li>K->R at 50: Loss of glycosylase and AP lyase activity</li><li>K->R at 154: No effect on glycosylase and AP lyase activity</li><li>C->S at 291: Loss of glycosylase and AP lyase activity</li><li>H->A at 295: Loss of glycosylase and AP lyase activity</li><li>R->Q at 310: Strongly reduces strand AP lyase activity</li><li>C->S at 315: Loss of glycosylase and AP lyase activity</li><li>C->S at 318: Loss of glycosylase and AP lyase activity</li></ul>							<li>O66612</li><li>Q972A8</li><li>Q9UZY0</li><li>Q8TXW8</li><li>Q6L1T6</li><li>O15527</li><li>Q9V3I8</li><li>Q58134</li><li>Q6M0G7</li><li>P53397</li><li>O58954</li><li>Q8R689</li><li>Q5UQ00</li><li>Q74MX2</li><li>Q8ZVK6</li><li>Q9X2E1</li><li>O27397</li><li>Q9YE60</li><li>Q5JI79</li><li>O70249</li><li>O29876</li><li>Q97CP1</li><li>Q9HM55</li><li>Q4J929</li><li>Q97ZK2</li><li>O08760</li><li>Q8U2D5</li>		1
Q969S8	83933	<ul><li>H->A at 135: Abolishes deacetylase activity. Does not affect interaction with HDAC3</li></ul>			deacetylase activity	GO:0019213			<li>P56520</li><li>O15379</li>		1
Q969T4	10477	<ul><li>C->S at 145: Loss of activity</li></ul>									1
Q969V5	79594	<ul><li>R->A at 260: Protein is targeted to the ER; when associated with A-261</li><li>K->A at 261: Protein is targeted to the ER; when associated with A-260</li><li>H->A at 319: Abolishes ligase activity. No effect on mitochondrial localization</li><li>C->A at 339: Abolishes ligase activity</li></ul>	localization	GO:0051179	ligase activity	GO:0016874	ER	GO:0005783			1
Q96AD5	57104	<ul><li>S->A at 47: Reduces rate of lipid hydrolysis; does not affect the localization around the rim of the adiposomes</li></ul>	localization	GO:0051179							1
Q96AQ6	57326	<ul><li>LASLL->AASAA at 615-619: Reduces interaction with ESR1</li></ul>							<li>Q9TV98</li><li>Q9QZJ5</li><li>P49884</li><li>Q91424</li><li>Q91250</li><li>Q29040</li><li>P38111</li><li>Q9YHT3</li><li>P50242</li><li>P50241</li><li>P03372</li><li>P16058</li><li>Q9YH33</li><li>Q9PVZ9</li><li>P50240</li><li>P06212</li><li>P57753</li><li>Q53AD2</li><li>P49885</li><li>P49886</li><li>Q9YHZ7</li><li>O42132</li>		1
Q96AV8	144455	<ul><li>LG->EE at 147-148: Loss of DNA-binding and E2F-dependent repression</li><li>R->A at 185: Loss of DNA-binding and inhibition of E2F1-dependent activation</li><li>R->A at 334: Loss of DNA-binding and inhibition of E2F1-dependent activation</li></ul>			DNA-binding	GO:0003677			<li>Q01094</li><li>Q90977</li><li>Q27368</li>		1
Q96B01	10635	<ul><li>R->A at 333: Strongly descreases interaction with RAD51; when associated with Q-336; A-345 and A-346</li><li>L->Q at 336: Strongly descreases interaction with RAD51; when associated with A-333; A-345 and A-346</li><li>LH->AA at 345-346: Strongly descreases interaction with RAD51; when associated with A-333; and Q-336</li></ul>							<li>Q40134</li><li>P94102</li><li>Q2KJ94</li><li>Q8MKI8</li><li>Q99133</li><li>O77507</li><li>P37383</li><li>P70099</li><li>P25454</li><li>Q06609</li>		1
Q96BA8	90993	<ul><li>P->L at 392: Abolishes proteolytic cleavage by PS2</li><li>R->A at 423: Abolishes proteolytic cleavage by PS1</li><li>L->V at 426: Abolishes proteolytic cleavage by PS1</li></ul>							<li>Q9W6T7</li><li>P04155</li><li>P79801</li><li>P49768</li><li>P84718</li><li>Q90ZE4</li><li>P49810</li><li>P79802</li><li>Q8HXW5</li>		1
Q96BD6	80176	<ul><li>Y->F at 31: Loss of phosphorylation</li><li>LPLP->AAAA at 260-263: Abolishes interaction with RNF7 and CUL5</li></ul>	phosphorylation	GO:0016310					<li>Q9UBF6</li><li>Q5RB36</li><li>Q29425</li><li>Q93034</li>		1
Q96BR1	23678	<ul><li>R->A at 90: Partially localized to the membrane</li><li>K->M at 191: Abolishes activity</li><li>S->D at 486: Increased activation</li></ul>					membrane	GO:0016020			1
Q96BY2	64112	<ul><li>Missing at 120-127: Abrogates interaction with BAX, resulting in a nonapoptotic protein</li><li>L->E at 120: Weakened interaction with BAX, resulting in a nonapoptotic protein</li><li>GHE->VLA at 125-127: Abrogates interaction with BAX, resulting in a nonapoptotic protein</li><li>KYKKLR->AYAALA at 161-166: No effect on RASSF1-binding</li><li>EEE->AAA at 178-180: No effect on RASSF1-binding; interacts with BAX in the absence of RASSF1</li><li>KRRR->AAAA at 202-205: Loss of RASSF1-binding; interacts with BAX in the absence of RASSF1</li></ul>			binding	GO:0005488			<li>Q9NS23</li><li>Q07815</li><li>Q07812</li><li>Q07814</li><li>O02703</li><li>P55269</li>		1
Q96C23	130589	<ul><li>H->A at 107: Reduces activity over 5-fold</li><li>H->A at 176: Loss of activity</li><li>E->A at 307: Loss of activity</li></ul>									1
Q96C86	28960	<ul><li>R->A at 58: Increases decapping activity to 125% of wild-type</li><li>I->A at 61: No effect</li><li>F->A at 63: No effect</li><li>I->A at 83: Strongly reduces decapping activity</li><li>E->A at 85: Reduces decapping activity</li><li>F->A at 108: Reduces decapping activity</li><li>N->A at 110: Loss of decapping activity</li><li>Y->A at 113: Loss of decapping activity</li><li>K->A at 128: No effect</li><li>K->D at 138: Increases decapping activity to 250% of wild-type</li><li>R->A at 145: Increases decapping activity to 180% of wild-type</li><li>Q->P at 146: Increases decapping activity to 140% of wild-type</li><li>W->A at 175: Loss of decapping activity</li><li>E->A at 185: Loss of decapping activity</li><li>P->A at 204: Reduces decapping activity</li><li>D->A at 205: Reduces decapping activity</li><li>L->A at 206: No effect</li><li>K->A at 207: Reduces decapping activity</li><li>K->R at 207: No effect</li><li>Y->A at 217: No effect</li><li>Y->F at 217: Reduces decapping activity</li><li>H->N at 268: Loss of decapping activity</li><li>S->A at 272: No effect</li><li>H->N at 277: Loss of decapping activity</li><li>H->N at 279: Loss of decapping activity</li><li>R->A,K at 294: No effect</li><li>R->A at 322: No effect</li></ul>									1
Q96CA5	79444	<ul><li>EE->AA at 87-88: No change in SMAC interaction and anti-apoptotic activity</li><li>D->A at 120: Abolishes inhibition of caspases, SMAC binding and anti-apoptotic activity</li><li>C->A at 124: Abolishes inhibition of caspases and anti-apoptotic activity</li><li>D->A at 138: Abolishes inhibition of caspases, SMAC binding and anti-apoptotic activity</li></ul>			binding	GO:0005488			Q9NR28		1
Q96CC6	64285	<ul><li>N->Q at 131: No effect</li><li>N->Q at 381: No effect</li><li>N->Q at 583: Loss of N-glycosylation</li></ul>									1
Q96CG3	92610	<ul><li>G->E at 50: Loss of trimerization and activation of NF-kappa-B and JNK pathways; when associated with A-66</li><li>S->A at 66: Loss of trimerization and activation of NF-kappa-B and JNK pathways; when associated with E-50</li><li>E->A at 178: Loss of binding to TRAF6 and activation of NF-kappa-B and JNK pathways</li></ul>			binding	GO:0005488			<li>Q966Y3</li><li>P92208</li><li>Q9Y4K3</li>		1
Q96D46	51068	<ul><li>K->A at 405: Reduces accumulation in the nucleus. Loss of nucleolar localization; when associated with A-406</li><li>K->A at 406: Reduces accumulation in the nucleus. Loss of nucleolar localization; when associated with A-405</li><li>L->A at 480: Reduces nuclear export</li><li>L->A at 484: Reduces nuclear export</li><li>L->A at 487: Reduces nuclear export</li></ul>	<li>nuclear export</li><li>localization</li>	<li>GO:0051168</li><li>GO:0051179</li>			nucleus	GO:0005634			1
Q96D96	84329	<ul><li>H->A at 140: Exhibits selectivity to protons but sensitivity to zinc ions is abolished; when associated with A-193</li><li>H->A at 193: Exhibits selectivity to protons but sensitivity to zinc ions is abolished; when associated with A-140</li><li>R->A at 205: Faster channel activation and deactivation kinetics</li><li>R->A at 208: Faster channel activation and deactivation kinetics</li><li>R->A at 211: Faster channel deactivation kinetics</li></ul>									1
Q96DC9	78990	<ul><li>C->S at 51: Loss of function in vitro</li></ul>									1
Q96DN0	121506	<ul><li>M->W at 168: Decreases somatostatin-14 binding</li><li>I->A,L,W at 196: Decreases somatostatin-14 binding</li><li>I->W at 196: Conserved PDIA3 binding in vivo and in vitro</li><li>E->K,A at 231: Greatly reduces PDIA3 binding in vivo and in vitro</li><li>W->A at 232: Greatly reduces PDIA3 binding in vivo and in vitro</li><li>D->G at 233: Greatly reduces PDIA3 binding in vivo and in vitro</li></ul>			binding	GO:0005488			<li>P38657</li><li>P30101</li><li>P60041</li><li>Q9W7F0</li><li>P60042</li><li>P19209</li><li>P33094</li><li>Q9PRZ6</li><li>P01171</li><li>P21779</li><li>Q9PRR0</li><li>P01169</li><li>Q9YGH5</li><li>P01168</li><li>P81246</li><li>P61279</li><li>P61278</li><li>O46688</li><li>P87384</li><li>P26917</li><li>P49670</li><li>P61299</li><li>P61298</li>		1
Q96DR7	26084	<ul><li>W->R at 826: Fails to localize at sites of membrane ruffling</li></ul>					membrane	GO:0016020			1
Q96DU3	114836	<ul><li>R->A at 108: Inhibits dimerization</li><li>Q->A at 110: Inhibits dimerization</li><li>S->A at 112: Inhibits dimerization</li></ul>									1
Q96DZ1	27248	<ul><li>G->S at 379: Abolishes binding to KREMEN2</li></ul>			binding	GO:0005488			Q8NCW0		1
Q96E14	116028	<ul><li>K->A at 24: Abolishes interaction with RMI1, TOP3A and BLM</li><li>W->A at 59: According to PubMed</li><li>K->A at 100: Does not affect interaction with RMI1, TOP3A and BLM</li><li>K->A at 121: According to PubMed</li><li>W->A at 135: Abolishes interaction with RMI1, TOP3A and BLM</li></ul>							<li>Q9H9A7</li><li>Q9I920</li><li>P54132</li><li>Q13472</li>		1
Q96EB6	23411	<ul><li>H->Y at 363: Loss of function</li></ul>									1
Q96EK6	64841	<ul><li>E->A at 156: Reduces affinity for glucosamine-6-phosphate 6-fold</li><li>E->D at 156: Slightly reduced catalytic activity</li></ul>			catalytic activity	GO:0003824					1
Q96EP1	55743	<ul><li>T->A at 39: Abolishes phosphorylation but not autoubiquitination; when associated with A-205</li><li>S->A at 205: Abolishes phosphorylation but not autoubiquitination; when associated with A-39</li><li>I->A at 306: Abolishes autoubiquitination in vitro. Does not affect phosphorylation</li><li>W->A at 332: Abolishes autoubiquitination in vitro</li></ul>	phosphorylation	GO:0016310							1
Q96EQ8	54941	<ul><li>G->A at 2: Abolishes ability to regulate T-cell activation but not E3 ligase activity in vitro</li><li>C->A at 37: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-41</li><li>C->A at 40: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-38</li><li>H->A at 54: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-58</li><li>C->A at 57: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-55</li><li>C->A at 72: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-76</li><li>C->A at 75: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-73</li></ul>	T-cell activation	GO:0042110	ligase activity	GO:0016874					1
Q96EY1	9093	<ul><li>H->Q at 121: Loss of modulation of apoptosis</li></ul>	apoptosis	GO:0006915							1
Q96EY5	93343	<ul><li>Y->D at 204: Mimics constitutively phosphorylated form and has the ability to interact with CD2AP and CIN85/SH3KBP1 without EGF treatment</li><li>Y->F at 204: Abolishes interaction with CD2AP and CIN85/SH3KBP1</li></ul>							<li>Q9BEA0</li><li>P26224</li><li>P01132</li><li>Q96B97</li><li>P01133</li><li>Q95ND4</li><li>Q9Y5K6</li><li>Q00968</li><li>P07522</li>		1
Q96F24	29982	<ul><li>LL->AA at 144-145: Decreased interaction with nuclear receptors</li></ul>									1
Q96FI4	79661	<ul><li>P->T at 2: Loss of glycosylase and AP lyase activity</li><li>Missing at 2: Loss of glycosylase activity</li><li>E->Q at 3: Loss of glycosylase and AP lyase activity</li><li>K->L at 54: Loss of glycosylase activity</li><li>R->A at 277: Strongly reduced glycosylase activity. Has little effect on AP lyase activity</li></ul>							<li>O66612</li><li>Q972A8</li><li>Q9UZY0</li><li>Q8TXW8</li><li>Q6L1T6</li><li>O15527</li><li>Q9V3I8</li><li>Q58134</li><li>Q6M0G7</li><li>P53397</li><li>O58954</li><li>Q8R689</li><li>Q5UQ00</li><li>Q74MX2</li><li>Q8ZVK6</li><li>Q9X2E1</li><li>O27397</li><li>Q9YE60</li><li>Q5JI79</li><li>O70249</li><li>O29876</li><li>Q97CP1</li><li>Q9HM55</li><li>Q4J929</li><li>Q97ZK2</li><li>O08760</li><li>Q8U2D5</li>		1
Q96FL8	55244	<ul><li>E->Q at 273: No change in subcellular location and abolition of MATE1-dependent TEA transport activity</li></ul>	transport	GO:0006810							1
Q96FT7	55515	<ul><li>G->A at 549: No effect on channel function</li></ul>									1
Q96FW1	55611	<ul><li>D->E at 88: Abolishes hydrolase activity in vitro</li><li>C->A at 91: Prevents RNF128 autoubiquitination, and stabilizes RNF128 in vivo</li><li>C->S at 91: Abolishes hydrolase activity in vitro</li><li>R->L at 176: No effect on RNF128</li><li>C->A at 212: No effect on RNF128</li><li>H->R at 265: Abolishes hydrolase activity in vitro</li></ul>			hydrolase activity	GO:0016787			<li>Q29RU0</li><li>Q8TEB7</li><li>Q5RF74</li>		1
Q96FZ7	79643	<ul><li>G->A at 2: Abolishes myristoylation</li><li>R->E at 49: Does not affect the subcellular location</li><li>Missing at 168-201: Membrane association; releases autoinhibition</li><li>L->D at 170: Abolishes interaction with VPS4A</li><li>V->D at 173: Abolishes interaction with VPS4A</li><li>L->D at 178: Reduces interaction with VPS4A</li></ul>					Membrane	GO:0016020	Q9UN37		1
Q96G25	112950	<ul><li>L->P at 143: Impairs interaction with the Elongin BC complex; when associated with F-147</li><li>C->F at 147: Impairs interaction with the Elongin BC complex; when associated with P-143</li></ul>									1
Q96G27	23559	<ul><li>Y->A at 141: Abolishes interaction with WWOX</li></ul>							<li>Q5F389</li><li>Q5R9W5</li><li>Q9NZC7</li><li>Q9VLU5</li>		1
Q96G74	55593	<ul><li>C->S at 224: Loss of suppression of IFN production</li><li>L->A at 542: Loss of 'K-48'- and 'K-63'-linked polyubiquitin chain binding. Partial loss of TRAF3 deubiquitination; when associated with A-549</li><li>S->A at 549: Loss of 'K-48'- and 'K-63'-linked polyubiquitin chain binding. Partial loss of TRAF3 deubiquitination; when associated with A-542</li></ul>	deubiquitination	GO:0016579	binding	GO:0005488			<li>P28172</li><li>P51526</li><li>Q13114</li>		1
Q96HE7	30001	<ul><li>C->A at 85: Alters protein folding and stability. Loss of regulatory disulfide bond formation and increased activity towards PDI; when associated with A-131</li><li>C->S at 85: Induces a decrease in activity</li><li>C->S at 94: Induces a decrease in activity towards thioredoxin. Loss of activity towards thioredoxin and loss of regulatory disulfide bond formation; when associated with A-99</li><li>C->A at 99: Acts as a weak dominant-negative mutant. Loss of activity towards thioredoxin. Loss of regulatory disulfide bond formation; when associated with A-94</li><li>C->A at 104: No effect. Strongly increased activity towards PDI; when associated with A-131</li><li>C->S at 104: No effect</li><li>C->A at 131: Loss of regulatory disulfide bond formation and increased activity towards PDI. Loss of regulatory disulfide bond formation and strongly increased activity towards PDI; when associated with A-85. Loss of regulatory disulfide bond formation and strongly increased activity towards PDI; when associated with A-104</li><li>C->A at 166: No effect</li><li>C->A,S at 208: No effect</li><li>C->A,S at 241: No effect</li><li>N->A at 280: No effect on activity</li><li>N->A at 384: No effect on activity</li><li>C->A at 391: Alters protein folding. Prevents formation of regulatory disulfide bond and down-regulation of activity. Decreases association with P4HB</li><li>C->A at 394: Retains activity towards PDI. Does not act as a dominant negative mutant. Induces defects in folding. Remains associated with P4HB</li><li>C->A at 397: Acts as a dominant negative mutant; does not induce defects in folding; remains associated with P4HB</li></ul>	protein folding	GO:0006457					<li>Q12730</li><li>Q9PJK3</li><li>P81108</li><li>P81109</li><li>Q5R9M3</li><li>Q98TX1</li><li>P52588</li><li>P52589</li><li>P21610</li><li>Q9ZEE0</li><li>O97508</li><li>P80284</li><li>O14463</li><li>O22022</li><li>Q57755</li><li>P99122</li><li>P42115</li><li>Q05739</li><li>P32474</li><li>P0A4L4</li><li>Q43116</li><li>P0A4L3</li><li>P80579</li><li>O51088</li><li>O84544</li><li>O17486</li><li>P10599</li><li>P81110</li><li>O83889</li><li>Q9JWM8</li><li>P07237</li><li>P21609</li><li>P0A617</li><li>P0A616</li><li>P29429</li><li>Q5HGT9</li><li>P96132</li><li>P51225</li><li>Q9X2T1</li><li>P09102</li><li>P09103</li><li>Q9DGI3</li><li>P08058</li><li>P59527</li><li>Q8CPL5</li><li>P00276</li><li>P17967</li><li>P66928</li><li>P29451</li><li>Q92JR5</li><li>P10639</li><li>P52233</li><li>Q6GHU0</li><li>Q9UW02</li><li>O51890</li><li>P52230</li><li>P52231</li><li>P46843</li><li>P99505</li><li>P66929</li><li>P50254</li><li>O96952</li><li>Q2HWU2</li><li>Q5R5B6</li><li>O97680</li><li>P37395</li><li>Q9Z7P5</li><li>P11232</li><li>P75512</li><li>P05307</li><li>P14930</li><li>P82460</li><li>Q98PL5</li><li>P47370</li><li>P54399</li><li>P55059</li><li>Q00002</li><li>P04785</li><li>O30974</li><li>Q7M1B9</li><li>Q8R4U2</li><li>Q7KQL8</li><li>Q9R6P9</li><li>P57653</li><li>Q9BDJ3</li><li>Q6GA69</li><li>P50338</li><li>P14949</li><li>Q9CM49</li><li>P08628</li><li>P09857</li><li>P08629</li><li>Q9K1N8</li><li>P43785</li><li>Q5HQ29</li><li>P10473</li><li>P21195</li><li>P10472</li><li>P29828</li><li>P33791</li><li>P34723</li><li>P22549</li><li>Q00248</li><li>Q9XF61</li><li>P0A0K6</li><li>P0A0K5</li><li>P0A0K4</li><li>P50413</li><li>P52227</li>		1
Q96HI0	205564	<ul><li>C->A at 713: Abolishes enzymatic activity</li></ul>									1
Q96HS1	192111	<ul><li>E->A at 79: Loss of interaction with KEAP1; when associated with A-80</li><li>S->A at 80: Loss of interaction with KEAP1; when associated with A-79</li></ul>							Q14145		1
Q96J02	83737	<ul><li>C->A at 871: Loss of ubiquitin protein ligase activity</li></ul>							<li>Q9UVR2</li><li>O74196</li><li>P35130</li><li>Q5UQC9</li><li>Q5UQ88</li><li>P16577</li><li>O00103</li><li>O00102</li><li>P35128</li><li>P14682</li><li>P52492</li><li>P25153</li><li>P29340</li><li>P25866</li><li>P27949</li><li>P25867</li><li>P61087</li><li>P25869</li><li>P28263</li><li>P42743</li><li>P61085</li><li>P50623</li><li>P61086</li><li>Q02159</li><li>P35135</li><li>P49427</li><li>P49428</li><li>Q29503</li><li>P21734</li><li>P52487</li><li>P52486</li><li>P52485</li><li>Q5UQ57</li><li>O60015</li><li>P15732</li><li>Q8CFI2</li>		1
Q96JN0	84458	<ul><li>LL->AA at 56-57: Loss of estradiol-dependent interaction with ESR1 and ESR2</li></ul>							<li>Q9XSW2</li><li>Q91250</li><li>Q29040</li><li>P38111</li><li>Q9YHT3</li><li>P50242</li><li>P50241</li><li>P50240</li><li>Q9PVE2</li><li>P06212</li><li>Q95171</li><li>P49885</li><li>Q53AD2</li><li>Q9W6M2</li><li>P49886</li><li>O13012</li><li>O42132</li><li>Q9QZJ5</li><li>Q9TV98</li><li>Q9IAK1</li><li>P49884</li><li>Q9PTU5</li><li>Q91424</li><li>O93511</li><li>P16058</li><li>P03372</li><li>Q92731</li><li>Q9PVZ9</li><li>Q9YH33</li><li>Q9YH32</li><li>P57753</li><li>P57781</li><li>Q9TU15</li><li>P57782</li><li>Q9XSB5</li><li>Q9TTE5</li><li>Q9YHZ7</li>		1
Q96JY6	64236	<ul><li>L->K at 80: Abolishes cell adhesion to collagen and ability to suppress anchorage independent growth</li><li>C->S at 313: Abolishes ability to suppress anchorage independent growth but not cell adhesion to collagen; when associated with S-316</li><li>C->S at 316: Abolishes ability to suppress anchorage independent growth but not cell adhesion to collagen; when associated with S-313</li></ul>	cell adhesion	GO:0007155			collagen	GO:0005581			1
Q96JZ2	84941	<ul><li>PLPP->ALPA at 10-13: No change in the ability to inhibit RE/AP up-regulation in response to TCR/CD28 stimulation</li><li>R->K at 59: Loss of the ability to inhibit RE/AP up-regulation in response to TCR/CD28 stimulation</li><li>P->A at 116: No change in the ability to inhibit RE/AP up-regulation in response to TCR/CD28 stimulation</li><li>Y->F at 135: No change in the ability to inhibit RE/AP up-regulation in response to TCR/CD28 stimulation</li><li>PKSP->AKSA at 192-195: No change in the ability to inhibit RE/AP up-regulation in response to TCR/CD28 stimulation</li><li>Y->F at 341: No change in the ability to inhibit RE/AP up-regulation in response to TCR/CD28 stimulation</li><li>PFAP->AFAA at 346-349: No change in the ability to inhibit RE/AP up-regulation in response to TCR/CD28 stimulation</li></ul>					TCR	GO:0042101	<li>O02757</li><li>P42069</li><li>P31043</li><li>Q28071</li><li>P10747</li>		1
Q96KB5	55872	<ul><li>T->E at 9: TP53-binding</li><li>KK->AA at 64-65: Loss of activity</li><li>T->A at 320: Decrease in the binding to DLG1</li><li>V->A at 322: Decrease in the binding to DLG1</li></ul>			binding	GO:0005488			<li>Q9TUB2</li><li>P56423</li><li>P56424</li><li>O12946</li><li>P25035</li><li>O36006</li><li>Q64662</li><li>O57538</li><li>P10360</li><li>P61260</li><li>Q9W679</li><li>Q9W678</li><li>P13481</li><li>Q9TTA1</li><li>Q95330</li><li>O93379</li><li>P41685</li><li>Q8SPZ3</li><li>P79820</li><li>Q92143</li><li>P04637</li><li>Q29537</li><li>Q29480</li><li>O09185</li><li>Q00366</li><li>P79892</li><li>P51664</li><li>Q9WUR6</li><li>P67939</li><li>Q12959</li><li>P67938</li>		1
Q96KG7	84466	<ul><li>N->A at 927: Does not interact with GULP1; when associated with A-930</li><li>Y->A at 930: Does not interact with GULP1; when associated with A-927</li></ul>									1
Q96KK5	85235	<ul><li>S->A at 2: Blocks the inhibition of transcription by RPS6KA5/MSK1</li></ul>	transcription	GO:0006350					<li>P32048</li><li>Q5R4K3</li><li>Q5F3L1</li><li>O75582</li>		1
Q96KN2	84735	<ul><li>H->A at 132: Loss of activity</li><li>D->A at 165: Loss of activity</li><li>E->A at 200: Loss of activity</li></ul>									1
Q96KS0	112398	<ul><li>H->A at 297: Eliminates hydroxylase activity</li><li>D->A at 299: Eliminates hydroxylase activity</li><li>H->A at 358: Eliminates hydroxylase activity</li><li>R->A at 367: Eliminates hydroxylase activity</li></ul>									1
Q96L50	122769	<ul><li>HIIP->AAA at 341-344: Abolishes interaction with CUL2 and RBX1</li></ul>							<li>Q08273</li><li>P62877</li><li>Q13617</li><li>Q8QG64</li><li>Q5RCF3</li>		1
Q96LC7	89790	<ul><li>Y->F at 667: Abolishes binding to PTPN6</li></ul>			binding	GO:0005488			P29350		1
Q96LD8	123228	<ul><li>D->A at 10: No effect on activity</li><li>W->A at 26: Strongly reduces activity</li><li>D->A,N at 29: Abolishes activity</li><li>V->A at 58: No effect on activity</li><li>F->A at 74: No effect on activity</li><li>P->A at 77: No effect on activity</li><li>N->A at 91: Abolishes activity</li><li>H->N at 102: Abolishes activity</li><li>W->A,H at 103: Strongly reduces activity</li><li>D->A,N at 119: Abolishes activity</li><li>Q->A at 157: No effect on activity</li><li>C->A at 163: Abolishes activity</li></ul>									1
Q96LI5	246175	<ul><li>D->A at 410: Loss of deadenylase activity</li><li>D->A at 489: Loss of deadenylase activity</li><li>H->A at 529: Loss of deadenylase activity</li></ul>									1
Q96LW7	84270	<ul><li>L->A at 17: Abolishes the NF-kappa-B inhibitory activity</li><li>L->A at 65: Abolishes the NF-kappa-B inhibitory activity</li></ul>									1
Q96MF7	286053	<ul><li>C->A at 169: Induces a strong decrease in SUMO ligase activity</li><li>C->A at 185: Induces a strong decrease in SUMO ligase activity</li><li>H->A at 187: Induces a strong decrease in SUMO ligase activity</li><li>C->A at 210: Induces a strong decrease in SUMO ligase activity</li><li>C->A at 215: Induces a strong decrease in SUMO ligase activity</li></ul>			ligase activity	GO:0016874					1
Q96MH2	124790	<ul><li>T->A at 143: Loss of interaction with P-TEFb</li><li>T->D at 143: Loss of interaction with P-TEFb</li></ul>									1
Q96MT3	144165	<ul><li>Missing at 828-831: Abolishes localization to the nuclear membrane</li></ul>	localization	GO:0051179			nuclear membrane	GO:0005635			1
Q96NA2	83547	<ul><li>F->A at 248: Strongly reduces dimerization and localization to late endosomal/lysosomal compartments</li><li>I->A at 251: Abolishes dimerization, interaction with RAB7 and localization to late endosomal/lysosomal compartments</li><li>L->A at 252: Abolishes interaction with RAB7 and localization to late endosomal/lysosomal compartments</li><li>R->A at 255: Abolishes dimerization, interaction with RAB7 and localization to late endosomal/lysosomal compartments</li><li>L->A at 258: Reduces dimerization, interaction with RAB7 and localization to late endosomal/lysosomal compartments</li><li>K->A at 304: Abolishes interaction with RAB7 and localization to late endosomal/lysosomal compartments</li><li>M->A at 305: Abolishes interaction with RAB7 and localization to late endosomal/lysosomal compartments</li><li>L->A at 306: Abolishes interaction with RAB7 and localization to late endosomal/lysosomal compartments</li></ul>	localization	GO:0051179					<li>Q3T0F5</li><li>O04157</li><li>P18067</li><li>O97572</li><li>Q9XER8</li><li>P51149</li><li>Q5R9Y4</li>		1
Q96NY9	80198	<ul><li>GD->AE at 306-307: Loss of activity</li><li>ER->AG at 333-334: Loss of activity</li><li>DD->AA at 338-339: Loss of activity</li></ul>									1
Q96P31	115352	<ul><li>Y->F at 650: Loss of phosphorylation; when associated with F-662; F-692 and F-722. Alters binding with SYK and ZAP70; when associated with F-662</li><li>Y->F at 662: Loss of phosphorylation; when associated with F-650; F-692 and F-722. Alters binding with SYK and ZAP70; when associated with F-650</li><li>Y->F at 692: Loss of phosphorylation; when associated with F-650; F-662 and F-722. Alters binding with PTPN6 and PTPN11; when associated with F-772</li><li>Y->F at 722: Loss of phosphorylation; when associated with F-650; F-662 and F-692. Alters binding with PTPN6 and PTPN11; when associated with F-692</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488			<li>Q00655</li><li>P29350</li><li>P43403</li><li>Q90687</li><li>Q06124</li><li>P43405</li>		1
Q96PC2	117283	<ul><li>K->A at 217: Loss of activity</li><li>S->A at 325: Strongly reduces activity</li></ul>									1
Q96PD5	114770	<ul><li>H->A at 411: No effect on amidase activity</li><li>C->A at 419: Abolishes amidase activity</li><li>H->A at 436: No effect on amidase activity</li><li>W->A at 442: Reduced amidase activity</li><li>Y->A at 447: Abolishes amidase activity</li><li>C->S at 530: Abolishes amidase activity</li></ul>							<li>P22984</li><li>O69768</li><li>P95896</li><li>P27765</li>		1
Q96PH1	79400	<ul><li>E->Q at 49: Loss of binding of 1 calcium molecule. No effect on catalytic activity</li></ul>			<li>binding</li><li>catalytic activity</li>	<li>GO:0005488</li><li>GO:0003824</li>					1
Q96PJ5	83417	<ul><li>Y->F at 451: No effect on function, phosphorylation and interaction with PTPN6 and PTPN11</li><li>Y->F at 463: Loss of function, phosphorylation and interaction with PTPN6 and PTPN11</li><li>Y->F at 493: Loss of interaction with PTPN6 and PTPN11 and partial loss of function and phosphorylation</li></ul>	phosphorylation	GO:0016310					<li>P29350</li><li>Q90687</li><li>Q06124</li>		1
Q96PU5	23327	<ul><li>S->A at 448: Abolishes interaction with 1433F</li><li>C->S at 942: Abolishes activity</li></ul>									1
Q96Q15	23049	<ul><li>D->A at 2331: Loss of function</li></ul>									1
Q96Q27	51676	<ul><li>L->P at 548: No interaction with Elongin BC complex</li><li>LC->PF at 551-552: No interaction with CUL5 or RNF7</li><li>C->P at 552: No interaction with Elongin BC complex</li><li>LPLP->AAAA at 571-574: No interaction with CUL5 or RNF7</li></ul>							<li>Q9UBF6</li><li>Q5RB36</li><li>Q29425</li><li>Q93034</li>		1
Q96Q83	221120	<ul><li>R->A at 122: Decreases activity towards ssDNA by 25%. Loss of activity towards dsDNA</li><li>E->A at 123: Strongly increases activity towards dsDNA, possibly by facilitating access to the active site</li><li>R->A at 131: Loss of activity</li><li>L->A,N at 177: Loss of activity against 1-methyladenine</li><li>L->E,Q at 177: Loss of activity</li><li>L->I at 177: Decreases activity against 1-methyladenine</li><li>L->M at 177: No effect</li><li>N->A at 179: Decreases activity by about 60%</li><li>Y->A at 181: Strong decrease of activity</li><li>D->A at 189: Strongly increases activity towards dsDNA, possibly by facilitating access to the active site</li><li>H->A at 191: Loss of activity</li><li>D->A at 193: Loss of activity</li><li>H->A at 257: Decreases activity by about 65%</li><li>R->A at 269: Strong decrease of activity</li><li>N->A at 271: No effect</li><li>R->A at 275: Loss of activity</li></ul>									1
Q96QE3	79915	<ul><li>S->A at 1169: No effect on the RAD9A interaction after MMS exposure. Resists to DNA damage after MMS exposure</li><li>S->A at 1187: Weakly affects the RAD9A interaction after MMS exposure</li><li>C->G at 1430: Abolishes RB1 binding. Abolishes RB1 binding; when associated with K-1432. Weakly detected after methyl methane-sulfonate (MMS) treatment. Expression detected after MMS treatment; when associated with K-1432. Weakly affects the RAD9A interaction after MMS exposure. No effect on the RAD9A interaction after MMS exposure; when associated with K-1432. Resists to DNA damage after MMS exposure; when associated with K-1432</li><li>E->K at 1432: Abolishes RB1 binding; when associated with G-1430. Expression detected after methyl methane-sulfonate (MMS) treatment; when associated with G-1430. No effect on the RAD9A interaction after MMS exposure; when associated with G-1430. Resists to DNA damage after MMS exposure; when associated with G-1430</li></ul>			binding	GO:0005488			<li>P06400</li><li>Q99638</li><li>Q4R5X9</li>		1
Q96QT4	54822	<ul><li>K->R at 1648: Loss of kinase activity</li><li>G->D at 1799: Loss of kinase activity</li></ul>			kinase activity	GO:0016301					1
Q96QV6	221613	<ul><li>S->A at 2: Blocks the inhibition of transcription by RPS6KA5/MSK1</li></ul>	transcription	GO:0006350					<li>P32048</li><li>Q5R4K3</li><li>Q5F3L1</li><li>O75582</li>		1
Q96RG2	23178	<ul><li>K->R at 1028: Loss of autophosphorylating activity</li><li>T->A at 1161: Loss of catalytic activity</li><li>T->A at 1165: Loss of catalytic activity</li></ul>			catalytic activity	GO:0003824					1
Q96RI0	9002	<ul><li>R->A at 47: No proteolytic cleavage (by thrombin or trypsin)</li><li>R->A at 68: No effect on receptor activation</li></ul>							<li>P24664</li><li>Q59149</li><li>P35050</li><li>P84122</li><li>P23916</li><li>P83348</li>		1
Q96RJ3	115650	<ul><li>C->Y at 24: Abolishes a disulfide bond and thereby changes the specificity, so that both TNFSF13B and TNFSF13 can be bound</li><li>D->A at 26: Strongly reduced affinity for TNFSF13B</li><li>L->A at 28: Strongly reduced affinity for TNFSF13B</li><li>C->S at 35: Abolishes a disulfide bond and thereby changes the specificity, so that both TNFSF13B and TNFSF13 can be bound</li></ul>							<li>Q9Y275</li><li>O75888</li>		1
Q96RN1	116369	<ul><li>P->S at 914: Not a cause of male infertility</li></ul>									1
Q96RN5	51586	<ul><li>E->A at 42: Abrogates interaction with SREBF1</li><li>L->D at 58: Abrogates interaction with SREBF1</li><li>A->D at 60: Abrogates interaction with SREBF1</li></ul>							<li>P36956</li><li>O97676</li><li>Q60416</li>		1
Q96RU3	23048	<ul><li>L->E at 7: Impairs membrane tubulation but does not affect lipid-binding</li><li>K->Q at 33: Impairs lipid-binding and induction of membrane tubulation; when associated with Q-35</li><li>R->Q at 35: Impairs lipid-binding and induction of membrane tubulation; when associated with Q-33</li><li>KK->QQ at 51-52: Impairs lipid-binding and induction of membrane tubulation</li><li>RK->QQ at 113-114: Impairs lipid-binding and induction of membrane tubulation</li><li>Missing at 515-520: Abrogates interaction with TNKS</li><li>R->A at 515: Impairs interaction with TNKS</li><li>D->A at 519: Impairs interaction with TNKS; when associated with A-515</li><li>P->L at 602: Abrogates interaction with DNM1, DNM2 and DNM3</li></ul>			lipid-binding	GO:0008289	membrane	GO:0016020	<li>Q05193</li><li>O95271</li><li>Q9UQ16</li><li>P50570</li><li>P54861</li>		1
Q96S21	57799	<ul><li>LPLP->AAAA at 212-215: Abolishes interaction with RNF7 and CUL5</li><li>HL->AA at 221-222: Abolishes interaction with RNF7</li></ul>							<li>Q9UBF6</li><li>Q5RB36</li><li>Q29425</li><li>Q93034</li>		1
Q96SB4	6732	<ul><li>S->A at 37: No effect on protein phosphorylation</li><li>S->A at 51: Protein phosphorylation impaired at this position</li><li>S->A at 222: No effect on protein phosphorylation</li><li>S->G at 311: No effect on protein phosphorylation</li><li>S->G at 436: No effect on protein phosphorylation</li><li>S->A at 555: Protein phosphorylation impaired at this position</li><li>S->A at 619: No effect on protein phosphorylation</li></ul>	phosphorylation	GO:0016310							1
Q96SD1	64421	<ul><li>D->N,A at 17: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination</li><li>H->A at 33: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination</li><li>H->A at 35: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination</li><li>D->N,A at 37: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination</li><li>H->A at 38: Reduces PRKDC-dependent endonuclease activity, although V(D)J recombination is largely normal</li><li>H->A at 115: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination</li><li>D->N,A at 136: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination</li><li>D->N,A at 165: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination</li><li>H->A at 319: Abolishes PRKDC-dependent endonuclease activity and V(D)J recombination</li><li>S->A at 516: Reduced IR induced phosphorylation; when associated with A-534; A-538; A-548; A-553; A-561 and A-562</li><li>S->A at 534: Reduced IR induced phosphorylation; when associated with A-516; A-538; A-548; A-553; A-561 and A-562</li><li>S->A at 538: Reduced IR induced phosphorylation; when associated with A-516; A-534; A-548; A-553; A-561 and A-562</li><li>S->A at 548: Reduced IR induced phosphorylation; when associated with A-516; A-534; A-538; A-553; A-561 and A-562</li><li>S->A at 553: Reduced IR induced phosphorylation; when associated with A-516; A-534; A-538; A-548; A-561 and A-562</li><li>S->A at 561: Reduced IR induced phosphorylation; when associated with A-516; A-534; A-538; A-548; A-553 and A-562</li><li>S->A at 562: Reduced IR induced phosphorylation; when associated with A-516; A-534; A-538; A-548; A-553 and A-561</li></ul>	phosphorylation	GO:0016310					<li>P04323</li><li>P20825</li><li>P10399</li><li>P78527</li><li>P10978</li><li>P00641</li><li>Q00962</li><li>P38446</li><li>Q8QGX4</li><li>P15629</li><li>P13717</li><li>P05400</li><li>P03554</li><li>Q03269</li><li>P03556</li><li>P03555</li><li>Q03277</li><li>P10394</li><li>Q03278</li><li>Q03275</li><li>Q05118</li><li>Q03276</li><li>P11283</li><li>P16423</li><li>Q03273</li><li>Q03274</li><li>Q03271</li><li>Q03272</li><li>P09523</li><li>P11369</li><li>Q8I7P9</li><li>Q03270</li><li>P11367</li><li>Q02964</li><li>P10400</li><li>P20314</li><li>Q8WN22</li><li>Q03279</li><li>P10401</li>		1
Q96T51	80230	<ul><li>Y->F at 389: Abolishes phosphorylation and endosomal targeting; when associated with F-400</li><li>Y->F at 400: Abolishes phosphorylation and endosomal targeting; when associated with F-389</li></ul>	phosphorylation	GO:0016310							1
Q96T53	619373	<ul><li>H->A at 338: Abolishes ability to acylate ghrelin</li></ul>							<li>Q9EQX0</li><li>Q9BDJ6</li><li>Q6BEG6</li><li>Q9UBU3</li><li>Q9BEF8</li><li>Q6BEG7</li><li>Q9QYH7</li><li>Q9GKY5</li>		1
Q96T88	29128	<ul><li>S->A at 298: Diminishes in vitro phosphorylation by PKA</li><li>S->A at 651: No effect on in vitro phosphorylation by PKA</li><li>S->A at 666: No effect on in vitro phosphorylation by PKA</li></ul>	phosphorylation	GO:0016310	PKA	GO:0004691					1
Q99426	1155	<ul><li>S->A at 65: Reduced phosphorylation by PAK1. Reduced microtubule polymerization and loss of phosphorylation by PAK1; when associated with A-128</li><li>S->A at 128: Reduced phosphorylation by PAK1. Reduced microtubule polymerization and loss of phosphorylation by PAK1; when associated with A-65</li></ul>	<li>phosphorylation</li><li>microtubule polymerization</li>	<li>GO:0016310</li><li>GO:0046785</li>					<li>Q13153</li><li>P38990</li><li>P40494</li><li>Q17850</li>		1
Q99459	988	<ul><li>W->G at 31: Abolishes DNA-binding; when associated with G-53 and G-82</li><li>W->G at 53: Abolishes DNA-binding; when associated with G-31 and G-82</li><li>W->G at 82: Abolishes DNA-binding; when associated with G-31 and G-53</li></ul>			DNA-binding	GO:0003677					1
Q99496	6045	<ul><li>C->W at 51: Strong decrease in HIP2-binding; when associated with S-54</li><li>C->S at 54: Strong decrease in HIP2-binding; when associated with W-51</li><li>H->Y at 69: Loss of HIP2-binding and loss of ubiquitin ligase activity on histone H2A</li><li>R->C at 70: Loss of ubiquitin ligase activity on histone H2A</li></ul>			<li>binding</li><li>ligase activity</li>	<li>GO:0005488</li><li>GO:0016874</li>			<li>P08565</li><li>P68196</li><li>P68197</li><li>O46543</li><li>P68198</li><li>Q05550</li><li>P68199</li><li>P68195</li><li>P27325</li><li>P02264</li><li>P61863</li><li>P61864</li><li>P61862</li><li>P23398</li><li>Q6PV61</li><li>P84589</li><li>Q8MKD1</li><li>P02269</li><li>P14792</li><li>P02268</li><li>P35061</li><li>P59890</li><li>Q9HGX4</li><li>P63049</li><li>P35066</li><li>P02270</li><li>P63051</li><li>P13912</li><li>Q6WV88</li><li>P15174</li><li>Q6CK59</li><li>P62976</li><li>P62977</li><li>P62974</li><li>P62975</li><li>P62972</li><li>P62973</li><li>P14624</li><li>P13117</li><li>P82897</li><li>P19178</li><li>P0C014</li><li>P19177</li><li>P59263</li><li>Q5KMT5</li><li>Q4WWC6</li><li>P61085</li><li>P61086</li><li>P22589</li><li>P62988</li><li>P62989</li><li>P09588</li><li>Q4PEF9</li><li>P59669</li><li>P69326</li><li>Q6WV67</li><li>P69322</li><li>Q6WV66</li><li>P69323</li><li>Q6WV69</li><li>P69324</li><li>Q8X132</li><li>P69325</li><li>O13413</li><li>P19848</li><li>P42739</li><li>Q867C2</li><li>Q9M531</li><li>P62991</li><li>O74268</li><li>Q6C4I6</li><li>P62990</li><li>P21896</li><li>Q867C4</li><li>Q867C3</li><li>Q8SSG3</li><li>P68204</li><li>Q8I0T3</li><li>P68201</li><li>P42740</li><li>Q865C5</li><li>Q2U5A8</li><li>P0C072</li><li>P40280</li><li>P69308</li><li>P69309</li><li>P20685</li><li>P55897</li><li>P40279</li><li>P84056</li><li>P84055</li><li>P46574</li><li>P84057</li><li>P84052</li><li>P50567</li><li>P84051</li><li>P84054</li><li>P69310</li><li>P84053</li><li>P69313</li><li>P69314</li><li>P69311</li><li>P08618</li><li>P69312</li><li>P69317</li><li>P69318</li><li>P69315</li><li>P69316</li><li>Q4HTT1</li><li>P69319</li><li>Q5G578</li><li>P49634</li><li>P49635</li><li>Q875B8</li><li>Q9Y848</li><li>P08844</li><li>P40282</li><li>P23324</li><li>P69321</li><li>P69320</li><li>P13630</li>		1
Q99497	11315	<ul><li>C->A at 46: Reduces protein stability. No effect on oxidation</li><li>C->A at 53: Strongly reduces chaperone activity</li><li>C->A,D at 106: Abolishes oxidation and association with mitochondria. No effect on chaperone activity</li><li>K->R at 130: Partially compensates for loss of stability; when associated with P-166</li></ul>									1
Q99519	4758	<ul><li>Y->A at 412: Correct sorting to the plasma membrane but no endocytosis and internalization</li><li>G->A at 413: Correct sorting to the plasma membrane but no endocytosis and internalization</li><li>L->A at 415: Correct sorting to the plasma membrane but no endocytosis and internalization</li></ul>	endocytosis	GO:0006897			plasma membrane	GO:0005886			1
Q99523	6272	<ul><li>RWRR->GWRA at 74-77: Abrogates propeptide cleavage</li><li>RR->GG at 76-77: Abrogates propeptide cleavage</li><li>Y->A at 792: Reduces endocytosis and Golgi to endosome sorting; when associated with A-795</li><li>L->A at 795: Reduces endocytosis and Golgi to endosome sorting; when associated with A-792</li><li>DD->NN at 823-824: Reduces interaction with GGA1</li><li>S->A at 825: Reduces interaction with GGA1</li><li>DED->NQN at 826-828: Abrogates interaction with GGA1 and impairs localization to the Golgi</li><li>LL->AA at 829-830: Abrogates interaction with GGA1 and impairs localization to the Golgi</li><li>Missing at 829-830: Abrogates interaction with GGA2. Reduces endocytosis and Golgi to endosome sorting; when associated with A-792 and A-795</li></ul>	<li>localization</li><li>endocytosis</li>	<li>GO:0051179</li><li>GO:0006897</li>			endosome	GO:0005768	<li>Q9UJY4</li><li>Q9UJY5</li><li>Q06336</li><li>P38817</li>		1
Q99538	5641	<ul><li>N->D,Q,S at 323: Loss of autoactivation</li></ul>									1
Q99542	4327	<ul><li>E->P at 88: Reduced autolysis rate</li><li>P->V at 90: Reduced autolysis rate</li></ul>									1
Q99558	9020	<ul><li>KK->AA at 429-430: Loss of autophosphorylation</li></ul>	autophosphorylation	GO:0046777							1
Q99638	5883	<ul><li>Y->F at 28: Abolishes phosphorylation by ABL1</li><li>S->A at 272: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-277; A-328; A-341; A-375; A-380 and A-387</li><li>S->A at 277: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-328; A-341; A-375; A-380 and A-387</li><li>S->A at 328: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-341; A-375; A-380 and A-387</li><li>S->A at 341: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-328; A-375; A-380 and A-387</li><li>S->A at 375: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-328; A-341; A-380 and A-387</li><li>S->A at 380: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-328; A-341; A-375 and A-387</li><li>S->A at 387: Complete loss of phosphorylation and no loss of interaction with the 9-1-1 complex; when associated with A-272; A-277; A-328; A-341; A-375 and A-380</li></ul>	phosphorylation	GO:0016310					P00519		1
Q99640	9088	<ul><li>N->A at 238: Loss of kinase activity</li><li>D->A at 251: Loss of kinase activity</li><li>RNL->AAA at 486-488: Loss of CDC2-CCNB1 interaction</li></ul>			kinase activity	GO:0016301			<li>P19026</li><li>Q9DG97</li><li>Q9DG98</li><li>Q60FY0</li><li>P48734</li><li>P06493</li><li>P23111</li><li>P13863</li><li>Q04770</li><li>P15436</li><li>Q9IBG1</li><li>P54119</li><li>P93101</li><li>Q9W739</li><li>Q08301</li><li>Q9DGA2</li><li>Q9DGA5</li><li>Q9DGA4</li><li>Q5RCH1</li><li>Q9DGA0</li><li>P43290</li><li>P14635</li><li>P52389</li><li>P24100</li><li>P51958</li><li>Q41639</li><li>P37882</li><li>Q9DGD3</li>		1
Q99665	3595	<ul><li>Y->F at 678: No loss of STAT4 activation. No loss of SOCS3 binding</li><li>Y->F at 767: No loss of STAT4 activation. No loss of SOCS3 binding</li><li>Y->F at 800: Loss of STAT4 activation. Abolishes SOCS3 binding</li><li>L->A at 801: Abolishes in vitro STAT4 binding to a phosphorylated Y-800 peptide</li><li>P->A at 802: No effect on in vitro STAT4 binding to a phosphorylated Y-800 peptide</li><li>S->A at 803: No effect on in vitro STAT4 binding to a phosphorylated Y-800 peptide</li><li>N->A at 804: No effect on in vitro STAT4 binding to a phosphorylated Y-800 peptide</li></ul>			binding	GO:0005488			<li>Q68AM8</li><li>Q90X67</li><li>Q14765</li><li>O14543</li><li>Q9BEG9</li>		1
Q99683	4217	<ul><li>K->M at 709: Loss of kinase activity. Inhibits activation of JNK and apoptosis mediated by TNFRSF6 and DAXX</li><li>K->R at 709: Loss of kinase activity. Abolishes DAXX-mediated apoptosis</li><li>S->A at 966: Enhanced induction of apoptosis, increased kinase activity, and loss of YWHAG binding</li><li>S->A at 1033: Enhanced induction of apoptosis and increased kinase activity</li></ul>	<li>apoptosis</li><li>induction of apoptosis</li>	<li>GO:0006915</li><li>GO:0006917</li>	<li>binding</li><li>kinase activity</li>	<li>GO:0005488</li><li>GO:0016301</li>			<li>O77736</li><li>Q5RC20</li><li>Q9TSN4</li><li>O18805</li><li>Q9BDN4</li><li>P61981</li><li>P68253</li><li>P68252</li><li>Q966Y3</li><li>P51867</li><li>Q5TJE1</li><li>Q9BDN0</li><li>P92208</li><li>P25445</li><li>Q9BDP2</li><li>Q9UER7</li><li>Q5F3W6</li>		1
Q99704	1796	<ul><li>Y->F at 362: No association with NCK. No association with GAP; when associated with F-398</li><li>Y->F at 398: No association with GAP; when associated with F-362</li></ul>							<li>Q92263</li><li>P20936</li><li>Q92211</li><li>P09851</li><li>Q5PEA9</li><li>P74873</li><li>P16333</li><li>P74851</li><li>P50904</li>		1
Q99708	5932	<ul><li>S->A at 664: Abrogates dissociation of BRCA1</li><li>S->A at 745: Abrogates dissociation of BRCA1</li></ul>							<li>Q864U1</li><li>P38398</li><li>Q95153</li><li>Q6J6J0</li><li>Q6J6I8</li><li>Q9GKK8</li><li>Q6J6I9</li>		1
Q99717	4090	<ul><li>G->S at 419: Loss of phosphorylation</li></ul>	phosphorylation	GO:0016310							1
Q99720	10280	<ul><li>E->G at 123: No effect on ligand-binding</li><li>D->G at 126: Reduces ligand-binding. No effect on subcellular localization</li><li>E->G at 138: No effect on ligand-binding</li><li>E->G at 144: No effect on ligand-binding</li><li>E->G at 150: No effect on ligand-binding</li><li>E->G at 158: No effect on ligand-binding</li><li>E->G at 163: No effect on ligand-binding</li><li>E->G at 172: Reduces ligand-binding. No effect on subcellular localization</li><li>D->G at 188: No effect on ligand-binding</li><li>D->G at 195: No effect on ligand-binding</li><li>E->G at 213: No effect on ligand-binding</li></ul>	localization	GO:0051179	binding	GO:0005488					1
Q99732	9516	<ul><li>Y->A at 23: Abolishes interactions with WWOX</li><li>Y->A at 61: No effect on interaction with WWOX</li></ul>							<li>Q5F389</li><li>Q5R9W5</li><li>Q9NZC7</li><li>Q9VLU5</li>		1
Q99814	2034	<ul><li>C->S at 844: Abolishes hypoxia-inducible transcriptional activation of ctaD</li></ul>							<li>Q8FMT1</li><li>P98059</li><li>Q79VD7</li><li>P16262</li><li>P24010</li><li>P50676</li><li>Q92I67</li><li>P63852</li><li>Q73VC3</li><li>Q08855</li><li>P63853</li><li>Q6NFM3</li><li>O54069</li><li>Q9CBQ5</li><li>P98005</li><li>Q00502</li><li>P31833</li><li>P33517</li><li>Q04440</li><li>Q06473</li>		1
Q99816	7251	<ul><li>V->A at 43: Reduces interaction with ubiquitin; inhibits down-regulation of EGFR</li><li>N->A at 45: Reduces interaction with ubiquitin</li><li>D->A at 46: Reduces interaction with ubiquitin</li><li>Y->A at 63: Reduces interaction with HIV-1 p6; impairs HIV-1 buddding</li><li>F->A at 88: Reduces interaction with ubiquitin; no effect on in interaction with HIV-1 p6</li><li>V->A at 89: No change in interaction with p6; no effect on HIV-1 budding</li><li>M->A at 95: Reduces interaction with VPS37B and HIV-1 p6; abolishes interaction with PDCD6IP; impairs HIV-1 buddding; inhibits down-regulation of EGFR</li><li>V->A at 141: Reduces interaction with HIV-1 p6</li><li>Missing at 158-162: Abolishes interaction with CEP55 and midbody localization; no effect on interaction with ESCRT-I proteins, PDCD6IP and viral proteins</li><li>PPN->AAA at 158-160: Abolishes interaction with CEP55</li><li>RKQF->AAAA at 368-371: Loss of interaction with VPS28. No effect on interaction with VPS37C</li></ul>	localization	GO:0051179			midbody	GO:0030496	<li>P69326</li><li>P08565</li><li>P69322</li><li>P69323</li><li>P69324</li><li>P69325</li><li>P68196</li><li>O46543</li><li>P68197</li><li>P13387</li><li>Q05550</li><li>P68198</li><li>P68199</li><li>P19848</li><li>P42739</li><li>P68195</li><li>Q867C2</li><li>Q02767</li><li>P62991</li><li>P62990</li><li>P61863</li><li>Q3T178</li><li>P61864</li><li>P61862</li><li>Q867C4</li><li>Q867C3</li><li>P23398</li><li>P68204</li><li>P84589</li><li>P55245</li><li>Q8WUM4</li><li>Q865C5</li><li>P42740</li><li>P68201</li><li>Q8MKD1</li><li>P14792</li><li>P63049</li><li>P0C072</li><li>P63051</li><li>P69308</li><li>P69309</li><li>P20685</li><li>P15174</li><li>P62976</li><li>P62977</li><li>P62974</li><li>P62975</li><li>P62972</li><li>P13117</li><li>P14624</li><li>P62973</li><li>P46574</li><li>Q9UK41</li><li>P69310</li><li>P69313</li><li>P69314</li><li>Q53EZ4</li><li>P69311</li><li>P08618</li><li>P69312</li><li>P69317</li><li>P69318</li><li>P69315</li><li>P0C014</li><li>P69316</li><li>P59263</li><li>P69319</li><li>P49634</li><li>P49635</li><li>Q9Y848</li><li>P22589</li><li>P62988</li><li>P62989</li><li>P00533</li><li>P69321</li><li>P23324</li><li>P69320</li><li>P59669</li>		1
Q99856	1820	<ul><li>Y->A at 325: Abolishes DNA-binding</li><li>K->A at 461: Abolishes nuclear targeting</li><li>G->A,P at 527: Impairs DNA-binding but not self-association</li><li>Y->A at 530: Impairs DNA-binding but not self-association</li><li>Y->F at 530: No effect on DNA-binding</li><li>G->A at 532: Impairs DNA-binding</li><li>L->A at 534: Impairs DNA-binding</li></ul>			DNA-binding	GO:0003677					1
Q99878	8331	<ul><li>S->A at 2: Blocks the inhibition of transcription by RPS6KA5/MSK1</li></ul>	transcription	GO:0006350					<li>P32048</li><li>Q5R4K3</li><li>Q5F3L1</li><li>O75582</li>		1
Q99942	6048	<ul><li>C->S at 42: Loss of E3 ubiquitin-protein ligase activity</li></ul>							<li>Q8RSY1</li><li>Q2QCI9</li>		1
Q99962	6456	<ul><li>A->S at 63: Reduced tubulation of liposomes, 3-fold increase in tubule diameter, no effect on liposome binding; when associated with S-66 or with S-66 and Q-70</li><li>A->D at 66: Loss of tubulation of liposomes, no effect on liposome binding</li><li>A->S at 66: Reduced tubulation of liposomes, 3-fold increase in tubule diameter, no effect on liposome binding; when associated with S-63 or with S-63 and Q-70</li><li>A->W at 66: Vesiculation of liposomes, no effect on liposome binding, indol ring located in hydrophobic core of the membrane</li><li>M->Q at 70: Reduced tubulation of liposomes, 3-fold increase in tubule diameter, no effect on liposome binding; when associated with S-63 and S-66</li><li>F->W at 202: No effect. Indol ring not associated with the membrane</li></ul>			binding	GO:0005488	membrane	GO:0016020			1
Q99972	4653	<ul><li>N->S at 57: Loss of higher molecular weight isoform</li></ul>									1
Q99986	7443	<ul><li>S->A at 14: Does not abolish autophosphorylation</li><li>T->A at 102: Does not abolish autophosphorylation</li><li>S->A at 125: Does not abolish autophosphorylation</li><li>S->A at 150: Does not abolish autophosphorylation</li><li>S->A at 158: Does not abolish autophosphorylation</li><li>S->A at 239: Does not abolish autophosphorylation</li><li>T->A at 305: Does not abolish autophosphorylation</li><li>T->A at 312: Does not abolish autophosphorylation</li><li>T->A at 355: Does not abolish autophosphorylation</li><li>T->A at 390: Does not abolish autophosphorylation</li></ul>	autophosphorylation	GO:0046777							1
Q9BQ15	79035	<ul><li>T->A at 117: Loss of phosphorylation by ATM</li><li>T->E at 117: Enhances ATM-dependent signaling</li></ul>	phosphorylation	GO:0016310					<li>Q13315</li><li>Q6PQD5</li><li>Q9M3G7</li>		1
Q9BQF6	57337	<ul><li>F->W at 709: Slightly increased deconjugation activity</li><li>V->E at 713: Reduces deconjugation activity</li></ul>									1
Q9BQG2	83594	<ul><li>Missing at 460-462: Abolishes localization to peroxisomes</li></ul>	localization	GO:0051179			peroxisomes	GO:0005777			1
Q9BR76	57175	<ul><li>S->A at 2: Stronger interaction with the Arp2/3 complex. Does not affect homo-oligomerization. Enhanced ruffling in response to phorbol 12-myristate 13-acetate (PMA) and increased speed in fibroblasts</li><li>S->D at 2: Weaker interaction with the Arp2/3 complex. Does not affect homo-oligomerization. Attenuated PMA-induced ruffling and slower speed in fibroblasts</li></ul>							<li>Q9R045</li><li>P61161</li><li>Q5M7U6</li><li>Q9UUJ1</li>		1
Q9BRA2	84817	<ul><li>C->S at 43: Loss of peroxidase activity</li><li>C->S at 46: Loss of peroxidase activity</li></ul>							<li>P15984</li><li>P16147</li><li>P84714</li>		1
Q9BRG2	10045	<ul><li>Y->F at 95: Loss of phosphorylation</li><li>Y->F at 231: Weak phosphorylation</li></ul>	phosphorylation	GO:0016310							1
Q9BSD7	84284	<ul><li>E->T at 114: Reduced activity, especially towards ATP, GTP and TTP</li><li>G->H at 116: Reduced activity, especially towards ATP, GTP and TTP</li></ul>							<li>Q6S9E0</li><li>P26651</li><li>P53781</li><li>P22893</li><li>P47973</li>		1
Q9BSG0	84279	<ul><li>N->Q at 121: Does not affect glycosylation state. Abolishes N-glycosylation; when associated with Q-171</li><li>N->Q at 171: Abolishes N-glycosylation. Abolishes N-glycosylation; when associated with Q-121</li></ul>									1
Q9BSM1	84759	<ul><li>Y->F at 109: Marked decrease of repressor activity. May be a kinase phosphorylation site</li><li>S->F at 195: Abolishes repressor activity. May be a PKC phosphorylation site</li></ul>	phosphorylation	GO:0016310					<li>P13678</li><li>P13677</li><li>P05130</li><li>P34722</li>		1
Q9BST9	6242	<ul><li>SPV->APA at 561-563: Impairs interaction with TAX1BP3</li></ul>							O14907		1
Q9BT40	51763	<ul><li>Y->A,F at 349: No effect on EGF-induced ruffle localization</li><li>D->A at 361: Significant decrease in EGF-induced ruffle localization</li><li>W->A at 362: Significant decrease in EGF-induced ruffle localization</li><li>Y->A,F at 376: No effect on EGF-induced ruffle localization</li></ul>	localization	GO:0051179			ruffle	GO:0001726	<li>Q9BEA0</li><li>P26224</li><li>P01132</li><li>P01133</li><li>Q95ND4</li><li>Q00968</li><li>P07522</li>		1
Q9BTV5	79187	<ul><li>S->A at 313: In mitosis, remained associated with microtubules; when associated with A-317; A-322 and A-324</li><li>S->D at 313: Reduced ability to associate with microtubules; when associated with D-317; E-322 and D-324</li><li>S->A at 317: In mitosis, remained associated with microtubules; when associated with A-313; A-322 and A-324</li><li>S->D at 317: Reduced ability to associate with microtubules; when associated with D-313; E-322 and D-324</li><li>T->A at 322: In mitosis, remained associated with microtubules; when associated with A-313; A-317 and A-324</li><li>T->E at 322: Reduced ability to associate with microtubules; when associated with D-313; D-317 and D-324</li><li>S->A at 324: In mitosis, remained associated with microtubules; when associated with A-313; A-317 and A-322</li><li>S->D at 324: Reduced ability to associate with microtubules; when associated with D-313; D-317 and E-322</li></ul>	mitosis	GO:0007067			microtubules	GO:0005874			1
Q9BU89	83475	<ul><li>H->A at 56: Abolishes both iron-binding and enzyme activity</li><li>E->A at 57: Abolishes enzyme activity and impairs iron-binding</li><li>H->A at 89: Abolishes both iron-binding and enzyme activity</li><li>E->A at 90: Abolishes both iron-binding and enzyme activity</li><li>H->A at 207: Abolishes both iron-binding and enzyme activity</li><li>E->A at 208: Abolishes enzyme activity and impairs iron-binding</li><li>H->A at 240: Abolishes both iron-binding and enzyme activity</li><li>E->A at 241: Abolishes both iron-binding and enzyme activity</li></ul>			iron-binding	GO:0005506					1
Q9BUB5	8569	<ul><li>K->M at 78: Loss of kinase activity; when associated with D-232</li><li>D->A at 232: Loss of kinase activity; when associated with K-78</li><li>T->A at 250: Loss of kinase activity; when associated with T-255</li><li>T->A at 255: Loss of kinase activity; when associated with T-250</li><li>T->D at 385: Constitutively active</li></ul>			kinase activity	GO:0016301					1
Q9BUF7	92359	<ul><li>N->D at 36: Abolishes N-glycosylation</li><li>Missing at 117-120: Loss of interaction with PARD6A and MPP5</li></ul>							<li>Q5RDQ2</li><li>Q99546</li><li>Q8N3R9</li><li>Q9NPB6</li>		1
Q9BUM1	92579	<ul><li>R->A at 79: Loss of catalytic activity</li><li>H->A at 114: Loss of catalytic activity</li><li>H->A at 167: Loss of catalytic activity</li></ul>			catalytic activity	GO:0003824					1
Q9BUP3	10553	<ul><li>GETG->VETA at 28-31: Loss of proapoptotic and metastatis-inhibiting effect</li><li>R->H at 106: Loss of association with nucleus</li></ul>					nucleus	GO:0005634			1
Q9BV36	79083	<ul><li>E->A at 14: Abolishes RAB27A binding</li><li>R->A at 24: Decreases RAB27A binding</li><li>E->A at 32: Abolishes RAB27A binding</li></ul>			binding	GO:0005488			<li>Q4LE85</li><li>Q1HE58</li><li>P51159</li>		1
Q9BV47	78986	<ul><li>C->A,S at 152: Loss of activity</li></ul>									1
Q9BV57	55256	<ul><li>E->A at 94: Loss of aci-reductone dioxygenase activity</li></ul>							<li>Q9BV57</li><li>Q6AWN0</li><li>Q5ZL43</li><li>Q562C9</li><li>Q3B8C8</li><li>Q99JT9</li><li>Q3ZBL1</li><li>Q6PBX5</li><li>Q6DIY2</li>		1
Q9BVC4	64223	<ul><li>S->D at 72: Impairs interaction with FRAP1</li><li>G->D at 192: Abolishes interaction with FRAP1</li><li>F->S at 320: Impairs interaction with FRAP1</li></ul>							P42345		1
Q9BVN2	23623	<ul><li>L->A at 531: Abrogates nuclear redistribution</li></ul>									1
Q9BWF3	5936	<ul><li>Y->A at 37: Abrogates regulation of alternative splice site selection; when associated with A-39; A-113 and A-115</li><li>F->A at 39: Abrogates regulation of alternative splice site selection; when associated with A-37; A-113 and A-115</li><li>Y->A at 113: Abrogates regulation of alternative splice site selection; when associated with A-37; A-39 and A-115</li><li>F->A at 115: Abrogates regulation of alternative splice site selection; when associated with A-37; A-39 and A-113</li></ul>									1
Q9BX63	83990	<ul><li>K->R at 52: Disrupts BRCA1-mediated double-strand break repair. Loss of ATPase and DNA helicase activities</li><li>S->A at 986: Does not affect the interaction with BRCA1</li><li>S->A at 988: Does not affect the interaction with BRCA1</li><li>T->A at 989: Does not affect the interaction with BRCA1</li><li>S->A at 990: Disrupts the interaction with BRCA1</li><li>P->A at 991: Abolishes phosphorylation of S-990. Impairs the interaction with BRCA1</li><li>T->A at 992: Does not affect the interaction with BRCA1</li><li>F->A at 993: Abolishes phosphorylation of S-990. Impairs the interaction with BRCA1</li><li>T->A at 997: Does not affect the interaction with BRCA1</li><li>S->A at 1001: Does not affect the interaction with BRCA1</li><li>S->A at 1003: Does not affect the interaction with BRCA1</li><li>S->A at 1004: Does not affect the interaction with BRCA1</li><li>S->A at 1007: Does not affect the interaction with BRCA1</li><li>Y->A at 1011: Does not affect the interaction with BRCA1</li><li>T->A at 1013: Does not affect the interaction with BRCA1</li></ul>	<li>phosphorylation</li><li>double-strand break repair</li>	<li>GO:0016310</li><li>GO:0006302</li>					<li>Q8V736</li><li>O67037</li><li>Q9UZ86</li><li>Q68772</li><li>O51934</li><li>P74759</li><li>P37987</li><li>P22657</li><li>Q04575</li><li>Q971T7</li><li>P27328</li><li>P28726</li><li>Q07630</li><li>P27327</li><li>Q9WJB2</li><li>Q3I5J6</li><li>Q66914</li><li>P16342</li><li>Q89273</li><li>P36286</li><li>Q66198</li><li>Q864U1</li><li>P22168</li><li>P19751</li><li>Q8V6W7</li><li>P28897</li><li>Q96725</li><li>P19811</li><li>Q91A29</li><li>O29238</li><li>P09395</li><li>P15402</li><li>Q86117</li><li>P09498</li><li>Q86119</li><li>Q58907</li><li>Q83017</li><li>Q97ZF5</li><li>Q8R979</li><li>Q6F598</li><li>Q08582</li><li>Q91AV2</li><li>P17779</li><li>O58530</li><li>Q6J6I8</li><li>Q6J6I9</li><li>O67226</li><li>Q07518</li><li>P95479</li><li>P38398</li><li>P54634</li><li>Q6J6J0</li><li>Q8ZXT5</li><li>Q9IW06</li><li>Q04544</li><li>Q975P6</li><li>Q9GKK8</li><li>Q8V439</li><li>P17965</li><li>Q91QT2</li><li>Q04561</li><li>Q95153</li><li>Q97ZZ8</li><li>P27411</li><li>P27410</li><li>P27920</li><li>P22591</li><li>Q9PYA3</li><li>P20951</li><li>P15095</li><li>Q9YN02</li><li>P27407</li><li>Q06502</li><li>P18458</li><li>Q05002</li><li>Q9YCB6</li><li>P59641</li><li>Q69014</li><li>Q8B912</li><li>P27409</li><li>Q9YC75</li>		1
Q9BXA6	83983	<ul><li>K->M at 41: Loss of kinase activity</li><li>D->N at 135: Loss of kinase activity</li></ul>			kinase activity	GO:0016301					1
Q9BXA7	83942	<ul><li>T->A at 174: Loss of kinase activity</li><li>T->E at 174: Constitutively active</li></ul>			kinase activity	GO:0016301					1
Q9BXI6	83874	<ul><li>L->LA at 508: Loss of interaction with EBP50 and impaired subcellular localization</li></ul>	localization	GO:0051179					<li>Q28619</li><li>O14745</li><li>P70441</li><li>Q9JJ19</li>		1
Q9BXP8	60676	<ul><li>E->Q at 734: Loss of activity</li></ul>									1
Q9BXS0	84570	<ul><li>R->A at 109: Not secreted</li><li>R->A at 112: Not secreted</li><li>LIKRRLIK->VIKRR at 181-188: Reduces binding to beta amyloid peptide</li><li>Missing at 181-188: Abolishes binding to beta amyloid peptide</li></ul>			binding	GO:0005488					1
Q9BXW4	440738	<ul><li>G->A at 126: No processing of precursor</li></ul>									1
Q9BXW9	2177	<ul><li>S->A at 222: Reduces phosphorylation by ATM. No effect on ubiquitination, foci formation or DNA repair ability, but impairs S-phase checkpoint activation</li><li>K->R at 561: Abolishes ubiquitination; impairs chromatin binding, foci formation and DNA repair. No effect on S-222 phosphorylation by ATM</li><li>S->A at 1257: No effect on phosphorylation by ATM</li><li>S->A at 1401: Reduces phosphorylation by ATM; when associated with A-1404 and A-1418</li><li>S->A at 1404: Reduces phosphorylation by ATM; when associated with A-1401 and A-1418</li><li>S->A at 1418: Reduces phosphorylation by ATM; when associated with A-1401 and A-1404</li></ul>	<li>phosphorylation</li><li>DNA repair</li><li>S-phase</li>	<li>GO:0016310</li><li>GO:0006281</li><li>GO:0051320</li>	chromatin binding	GO:0003682			<li>Q13315</li><li>Q6PQD5</li><li>Q9M3G7</li>		1
Q9BY12	49855	<ul><li>RNL->AAA at 25-27: No effect on CCNA2/CDK2 complex-binding</li><li>RSL->AAA at 198-200: Loss of CCNA2/CDK2 complex-binding</li><li>RAL->AAA at 677-679: No effect on CCNA2/CDK2 complex-binding</li></ul>			binding	GO:0005488			<li>P30274</li><li>P48963</li><li>Q5E9Y0</li><li>P43450</li><li>P24941</li><li>P20248</li><li>O55076</li><li>P43449</li><li>P37881</li>		1
Q9BY41	55869	<ul><li>HH->AA at 142-143: Strongly reduces histone deacetylase activity</li></ul>							O22446		1
Q9BY49	55825	<ul><li>Missing at 303: Abolishes localization to peroxisomes</li></ul>	localization	GO:0051179			peroxisomes	GO:0005777			1
Q9BY66	8284	<ul><li>H->A at 534: Abolishes enzymatic activity; when associated with A-536</li><li>E->A at 536: Abolishes enzymatic activity; when associated with A-534</li></ul>									1
Q9BYC5	2530	<ul><li>R->A,K at 365: Complete loss of activity</li><li>R->A,K at 366: Decreases activity to 3%</li></ul>									1
Q9BYE7	84108	<ul><li>S->A at 30: Abolishes phosphorylation</li><li>S->A at 57: Does not abolish phosphorylation</li><li>S->A at 59: Does not abolish phosphorylation</li><li>S->A at 69: Does not abolish phosphorylation</li></ul>	phosphorylation	GO:0016310							1
Q9BYF1	59272	<ul><li>QAK->KAE at 24-26: Slightly inhibits interaction with SARS-CoV spike glycoprotein</li><li>K->D at 31: Abolishes interaction with SARS-CoV spike glycoprotein</li><li>E->A at 37: No effect on interaction with SARS-CoV spike glycoprotein</li><li>D->A at 38: No effect on interaction with SARS-CoV spike glycoprotein</li><li>Y->A at 41: Strongly inhibits interaction with SARS-CoV spike glycoprotein</li><li>K->D at 68: Slightly inhibits interaction with SARS-CoV spike glycoprotein</li><li>MYP->NFS at 82-84: Inhibits interaction with SARS-CoV spike glycoprotein</li><li>E->P at 110: No effect on interaction with SARS-CoV spike glycoprotein</li><li>PD->SM at 135-136: No effect on interaction with SARS-CoV spike glycoprotein</li><li>E->R at 160: No effect on interaction with SARS-CoV spike glycoprotein</li><li>R->D at 192: No effect on interaction with SARS-CoV spike glycoprotein</li><li>R->D at 219: No effect on interaction with SARS-CoV spike glycoprotein</li><li>H->Q at 239: No effect on interaction with SARS-CoV spike glycoprotein</li><li>K->D at 309: No effect on interaction with SARS-CoV spike glycoprotein</li><li>E->A at 312: No effect on interaction with SARS-CoV spike glycoprotein</li><li>T->A at 324: No effect on interaction with SARS-CoV spike glycoprotein</li><li>NVQ->DDR at 338-340: No effect on interaction with SARS-CoV spike glycoprotein</li><li>D->A at 350: No effect on interaction with SARS-CoV spike glycoprotein</li><li>K->H,A,D at 353: Abolishes interaction with SARS-CoV spike glycoprotein</li><li>D->A at 355: Strongly inhibits interaction with SARS-CoV spike glycoprotein</li><li>R->A at 357: Strongly inhibits interaction with SARS-CoV spike glycoprotein</li><li>L->K,A at 359: No effect on interaction with SARS-CoV spike glycoprotein</li><li>M->A at 383: Slightly inhibits interaction with SARS-CoV spike glycoprotein</li><li>P->A at 389: Slightly inhibits interaction with SARS-CoV spike glycoprotein</li><li>R->A at 393: Slightly inhibits interaction with SARS-CoV spike glycoprotein</li><li>SPD->PSN at 425-427: Slightly inhibits interaction with SARS-CoV spike glycoprotein</li><li>KGE->QDK at 465-467: No effect on interaction with SARS-CoV spike glycoprotein</li><li>R->S at 559: Slightly inhibits interaction with SARS-CoV spike glycoprotein</li><li>F->T at 603: No effect on interaction with SARS-CoV spike glycoprotein</li></ul>							<li>P13642</li><li>P08163</li><li>P26636</li><li>P49591</li><li>Q9GMB8</li>		1
Q9BYG3	84365	<ul><li>S->A at 230: Loss of phosphorylation site</li><li>T->A at 234: Loss of phosphorylation site. Abrogates interaction with MKI67</li><li>P->A at 235: Reduces phosphorylation at T-234</li><li>T->A at 238: Loss of phosphorylation site. Abrogates interaction with MKI67</li><li>P->A at 239: Reduces phosphorylation at T-234 and T-238</li></ul>	phosphorylation	GO:0016310					P46013		1
Q9BYN0	140809	<ul><li>C->S at 99: No effect on association with PRDX1, PRDX2, PRDX3 or PRDX4</li></ul>							<li>P35705</li><li>Q5E947</li><li>P52552</li><li>Q8K3U7</li><li>Q6DV14</li><li>Q5RC63</li><li>Q6B4U9</li><li>Q13162</li><li>Q9JKY1</li><li>Q9BGI2</li><li>Q9BGI3</li><li>P30048</li><li>Q2PFZ3</li><li>Q5REY3</li><li>P32119</li><li>Q06830</li>		1
Q9BYW2	29072	<ul><li>R->H at 1625: Loss of methyltransferase activity</li><li>R->A at 2475: Does not affect interaction with hyperphosphorylated POLR2A</li><li>K->A at 2476: Does not affect interaction with hyperphosphorylated POLR2A</li><li>Q->A at 2480: Does not affect interaction with hyperphosphorylated POLR2A</li><li>F->A at 2481: Does not affect interaction with hyperphosphorylated POLR2A</li><li>V->A at 2483: Impairs interaction with hyperphosphorylated POLR2A</li><li>F->L at 2505: Impairs interaction with hyperphosphorylated POLR2A</li><li>K->A at 2506: Impairs interaction with hyperphosphorylated POLR2A</li><li>R->A at 2510: Impairs interaction with hyperphosphorylated POLR2A</li><li>H->A at 2514: Impairs interaction with hyperphosphorylated POLR2A</li><li>G->A,T at 2515: Does not affect interaction with hyperphosphorylated POLR2A</li><li>E->A at 2528: Increases interaction with hyperphosphorylated POLR2A; when associated with A-2531</li><li>E->A at 2531: Increases interaction with hyperphosphorylated POLR2A; when associated with A-2528</li></ul>							<li>Q00020</li><li>P03588</li><li>P03589</li><li>Q83270</li><li>P28931</li><li>P06011</li><li>P24928</li><li>P17769</li><li>P20122</li><li>Q66121</li><li>O40976</li><li>P28726</li><li>P11414</li><li>P27752</li><li>Q83264</li>		1
Q9BYX4	64135	<ul><li>D->A at 251: No cleavage and no acceleration of DNA degradation</li><li>E->A at 444: No acceleration of DNA degradation, no binding to ATP, and no helicase activity</li></ul>	DNA degradation	GO:0006308	binding	GO:0005488			<li>Q8V736</li><li>O67037</li><li>Q9UZ86</li><li>Q68772</li><li>O51934</li><li>P74759</li><li>P37987</li><li>P22657</li><li>Q04575</li><li>Q971T7</li><li>P27328</li><li>P28726</li><li>Q07630</li><li>P27327</li><li>Q9WJB2</li><li>Q3I5J6</li><li>Q66914</li><li>P16342</li><li>Q89273</li><li>P36286</li><li>Q66198</li><li>P22168</li><li>P19751</li><li>Q8V6W7</li><li>P28897</li><li>Q96725</li><li>P19811</li><li>Q91A29</li><li>O29238</li><li>P09395</li><li>P15402</li><li>Q86117</li><li>P09498</li><li>Q86119</li><li>Q58907</li><li>Q83017</li><li>Q97ZF5</li><li>Q8R979</li><li>Q6F598</li><li>Q08582</li><li>Q91AV2</li><li>P17779</li><li>O58530</li><li>O67226</li><li>Q07518</li><li>P95479</li><li>P54634</li><li>Q8ZXT5</li><li>Q9IW06</li><li>Q04544</li><li>Q975P6</li><li>Q8V439</li><li>P17965</li><li>Q91QT2</li><li>Q04561</li><li>Q97ZZ8</li><li>P27411</li><li>P27410</li><li>P27920</li><li>P22591</li><li>Q9PYA3</li><li>P20951</li><li>P15095</li><li>Q9YN02</li><li>P27407</li><li>Q06502</li><li>P18458</li><li>Q05002</li><li>Q9YCB6</li><li>P59641</li><li>Q69014</li><li>Q8B912</li><li>P27409</li><li>Q9YC75</li>		1
Q9BZB8	64506	<ul><li>T->A at 172: Does not affect its localization</li><li>T->D at 172: Does not affect its localization</li><li>F->A at 314: Abolishes stress granule assembly and correct localization in dcp1 bodies</li><li>H->A at 545: Abolishes stress granule assembly and correct localization in dcp1 bodies</li></ul>	localization	GO:0051179					<li>P47820</li><li>P09470</li><li>P22967</li><li>Q50JE5</li><li>Q8CFN1</li>		1
Q9BZI7	65109	<ul><li>K->E at 52: Abolishes interaction with RENT2</li><li>VVIRRL->AVARRA at 53-58: Abolishes interaction with RENT2</li><li>R->E at 56: Does not abolish interaction with RENT2</li><li>YVF->DVD at 117-119: Abolishes interaction with RENT2</li><li>R->A at 430: Reduces NMD</li><li>R->A at 432: Reduces NMD</li><li>Missing at 434-447: Abolishes NMD</li><li>K->A at 434: Reduces NMD</li><li>D->A at 435: Reduces NMD</li><li>R->A at 436: Reduces NMD</li><li>L->F at 441: Reduces NMD</li></ul>							Q9HAU5		1
Q9BZM5	80328	<ul><li>SAG->TPV at 208-210: Secreted</li><li>SSG->TPV at 216-218: Not secreted</li></ul>									1
Q9BZQ4	23057	<ul><li>H->A at 24: Reduces activity by 95%</li><li>W->G at 92: Reduces activity by 95%</li></ul>									1
Q9BZX4	152015	<ul><li>L->A at 18: Abolishes interaction with AKAP3</li></ul>							<li>O75969</li><li>O77797</li>		1
Q9C000	22861	<ul><li>GK->EA at 339-340: Abolishes binding to ATP</li><li>K->L,S at 340: No effect</li></ul>			binding	GO:0005488					1
Q9C035	85363	<ul><li>R->A,G,H,P,Q,S at 332: Increases strongly cell restriction against HIV-1 and SIVmac infection</li><li>R->D,E,L at 332: Increases strongly cell restriction against HIV-1 infection</li><li>R->K at 332: No effect on HIV-1 and SIVmac infection</li></ul>									1
Q9C0D3	79699	<ul><li>L->S at 18: Abolishes interaction with TCEB1</li></ul>							<li>Q15369</li><li>Q2KII4</li>		1
Q9C0H2	80727	<ul><li>T->A at 128: Does not affect N-glycosylation state</li><li>T->A at 146: Does not affect N-glycosylation state</li><li>T->A at 353: Abolishes N-glycosylation</li><li>R->Q at 367: Induces a stronger permeability to cations</li><li>H->D at 370: Shows a different ion selectivity</li></ul>									1
Q9GZM8	81565	<ul><li>S->A at 198: Abrogates mitotic phosphorylation; when associated with V-219; A-231; A-242 and V-245. Abrogates phosphorylation by CDK5; when associated with A-219 and A-231</li><li>S->E at 198: Enhances interaction with PAFAH1B1 and impairs centrosomal localization; when associated with E-219; E-231; E-242 and E-245</li><li>T->A at 219: Abrogates phosphorylation by CDK5; when associated with A-198 and A-231</li><li>T->E at 219: Enhances interaction with PAFAH1B1 and impairs centrosomal localization; when associated with E-198; E-231; E-242 and E-245</li><li>T->V at 219: Abrogates mitotic phosphorylation; when associated with A-198; A-231; A-242 and V-245</li><li>S->A at 231: Abrogates mitotic phosphorylation; when associated with A-198; V-219; A-242 and V-245. Abrogates phosphorylation by CDK5; when associated with A-198 and A-219</li><li>S->E at 231: Enhances interaction with PAFAH1B1 and impairs centrosomal localization; when associated with E-198; E-219; E-242 and E-245</li><li>S->A at 242: Abrogates mitotic phosphorylation; when associated with A-198; V-219; A-231 and V-245</li><li>S->E at 242: Enhances interaction with PAFAH1B1 and impairs centrosomal localization; when associated with E-198; E-219; E-231 and E-245</li><li>T->E at 245: Enhances interaction with PAFAH1B1 and impairs centrosomal localization; when associated with E-198; E-219; E-231 and E-242</li><li>T->V at 245: Abrogates mitotic phosphorylation; when associated with A-198; V-219; A-231 and A-242</li><li>C->A at 273: Abolishes oligopeptidase activity</li></ul>	<li>phosphorylation</li><li>localization</li>	<li>GO:0016310</li><li>GO:0051179</li>					<li>Q02399</li><li>Q5REG7</li><li>Q8HXX0</li><li>Q9GL51</li><li>P43033</li><li>Q00535</li><li>P43034</li><li>Q9PTR5</li><li>Q5IS43</li>		1
Q9GZN2	60436	<ul><li>T->V at 182: Decrease of phosphorylation. Strong decrease of phosphorylation; when associated with V-186</li><li>T->V at 186: Decrease of phosphorylation. Strong decrease of phosphorylation; when associated with V-182</li></ul>	phosphorylation	GO:0016310							1
Q9GZP0	80310	<ul><li>R->A at 247: Abolishes cleavage into active form; when associated with A-249</li><li>R->A at 249: Abolishes cleavage into active form; when associated with A-247</li></ul>									1
Q9GZQ8	81631	<ul><li>G->A at 120: No processing of precursor</li><li>K->A at 122: No effect on processing of precursor</li></ul>									1
Q9GZR1	26054	<ul><li>C->S at 1030: Abolishes enzymatic activity</li></ul>									1
Q9GZT3	81892	<ul><li>R->A at 7: Impairs corepressor activity; when associated with 13-A-A-14</li><li>RR->AA at 13-14: Impairs corepressor activity; when associated with A-7</li><li>RR->AA at 24-25: Impairs SRA-mediated repression; when associated with A-62</li><li>L->A at 62: Impairs SRA-mediated repression; when associated with 24-A-A-25</li></ul>							P68191		1
Q9GZT9	54583	<ul><li>Y->F at 303: No effect</li><li>R->A at 383: Reduces enzyme activity by 95%</li></ul>									1
Q9GZY0	56001	<ul><li>E->A at 598: Has no effect on FG-nucleoporin binding</li><li>W->A at 599: Suppresses FG-nucleoporin binding</li><li>N->A at 600: Has no effect on FG-nucleoporin binding</li></ul>			binding	GO:0005488					1
Q9GZY6	7462	<ul><li>Y->F at 58: No change in phosphorylation upon BCR activation</li><li>Y->F at 84: No change in phosphorylation upon BCR activation</li><li>Y->F at 95: Slightly reduces phosphorylation upon BCR activation</li><li>Y->F at 110: No change in phosphorylation upon BCR activation</li><li>Y->F at 118: No change in phosphorylation upon BCR activation</li><li>Y->F at 136: Slightly reduces phosphorylation upon BCR activation</li><li>Y->F at 193: Reduces phosphorylation upon BCR activation</li><li>Y->F at 233: Strongly reduces phosphorylation upon BCR activation</li></ul>	phosphorylation	GO:0016310					P11274		1
Q9H093	81788	<ul><li>K->R at 81: Loss of autophosphorylation, kinase activity and of anti-apoptotic activity</li><li>T->A at 208: Prevents phosphorylation and activation by STK11 complex</li></ul>	<li>phosphorylation</li><li>autophosphorylation</li>	<li>GO:0016310</li><li>GO:0046777</li>	kinase activity	GO:0016301			<li>Q15831</li><li>Q0GGW5</li>		1
Q9H0C8	80895	<ul><li>D->A at 152: Losing of more than 90% of activity</li><li>H->D at 154: Losing of more than 90% of activity</li><li>H->L at 154: Losing of more than 90% of activity</li></ul>									1
Q9H0H5	29127	<ul><li>R->A at 385: Abolishes GAP activity towards RAC1 and CDC42 and induces multiple blebs during cytokinesis</li></ul>	cytokinesis	GO:0000910					<li>P20936</li><li>O14426</li><li>P60953</li><li>P60952</li><li>Q9SSX0</li><li>Q92211</li><li>P80236</li><li>P63000</li><li>Q90694</li><li>O94103</li><li>Q92263</li><li>Q17031</li><li>Q9HF56</li><li>P09851</li><li>Q5PEA9</li><li>Q38912</li><li>P74873</li><li>O04369</li><li>P13362</li><li>P19073</li><li>P74851</li><li>P62999</li><li>P50904</li><li>P62998</li>		1
Q9H0K1	23235	<ul><li>T->A at 175: Prevents phosphorylation and activation by STK11 complex</li><li>T->E at 175: Constitutively active</li></ul>	phosphorylation	GO:0016310					<li>Q15831</li><li>Q0GGW5</li>		1
Q9H0M0	11059	<ul><li>E->A at 614: Reduces ubiquitin transfer</li><li>H->A at 621: Strongly reduces ubiquitin transfer</li><li>D->A at 675: Reduces ubiquitin transfer</li><li>E->A at 798: Reduces ubiquitin transfer. Strongly reduces ubiquitin transfer; when associated with A-845</li><li>M->P at 804: Strongly reduces ubiquitin transfer; when associated with P-806</li><li>E->P at 806: Strongly reduces ubiquitin transfer; when associated with P-804</li><li>R->A at 845: No effect</li><li>Q->A at 848: Abolishes ubiquitin transfer; when associated with A-855</li><li>R->A at 855: Abolishes ubiquitin transfer; when associated with A-848</li></ul>							<li>P69326</li><li>P08565</li><li>P69322</li><li>P69323</li><li>P69324</li><li>P69325</li><li>P68196</li><li>O46543</li><li>P68197</li><li>Q05550</li><li>P68198</li><li>P68199</li><li>P19848</li><li>P42739</li><li>P68195</li><li>Q867C2</li><li>P62991</li><li>P62990</li><li>P61863</li><li>P61864</li><li>P61862</li><li>Q867C4</li><li>Q867C3</li><li>P23398</li><li>P68204</li><li>P84589</li><li>Q865C5</li><li>P42740</li><li>P68201</li><li>Q8MKD1</li><li>P14792</li><li>P63049</li><li>P0C072</li><li>P63051</li><li>P69308</li><li>P69309</li><li>P20685</li><li>P15174</li><li>P62976</li><li>P62977</li><li>P62974</li><li>P62975</li><li>P62972</li><li>P13117</li><li>P14624</li><li>P62973</li><li>P46574</li><li>P69310</li><li>P69313</li><li>P69314</li><li>P69311</li><li>P08618</li><li>P69312</li><li>P69317</li><li>P69318</li><li>P69315</li><li>P0C014</li><li>P69316</li><li>P59263</li><li>P69319</li><li>P49634</li><li>P49635</li><li>Q9Y848</li><li>P22589</li><li>P62988</li><li>P62989</li><li>P69321</li><li>P23324</li><li>P69320</li><li>P59669</li>		1
Q9H0P0	51251	<ul><li>D->N at 88: Loss of nucleotidase and phosphotransferase activity</li><li>F->A at 89: Increases Km for CMP 45-fold. Reduces nucleotidase and phosphotransferase activity by 99%</li><li>D->N at 90: Loss of nucleotidase and phosphotransferase activity</li><li>E->D at 135: No effect on nucleotidase activity. Reduces phosphotransferase activity by 99%</li><li>F->A at 233: Reduces nucleotidase and phosphotransferase activity by 97%</li></ul>			nucleotidase activity	GO:0008252			<li>P21941</li><li>P05099</li>		1
Q9H0U4	81876	<ul><li>Q->L at 67: No effect on GDI1 binding. Reduces, in vitro, but not, in vivo prenylation. No effect on interaction with REP1/CHM Much lower GDP/GTP ratio</li><li>I->N at 73: Abolishes interaction with REP1/CHM. No prenylation. Much lower GDP/GTP ratio</li><li>Y->D at 78: Abolishes interaction with REP1/CHM and GDI1. No prenylation. Much lower GDP/GTP ratio. No membrane association</li><li>A->D at 81: Abolishes interaction with REP1/CHM. No prenylation. Lowers GDP/GTP ratio by half</li><li>L->R at 103: No effect on prenylation</li><li>A->D at 110: No effect on prenylation</li><li>K->E at 137: No effect on prenylation</li><li>G->N at 144: No effect on prenylation</li></ul>			binding	GO:0005488	membrane	GO:0016020	<li>P24386</li><li>Q9FE22</li><li>P03871</li><li>P60028</li><li>Q7YQM0</li><li>O97555</li><li>Q9SFC6</li><li>P21856</li><li>Q99109</li><li>P52195</li><li>P39958</li><li>P13741</li><li>P13775</li><li>P31150</li><li>P13778</li><li>Q8HXX7</li><li>P13777</li><li>P13776</li>		1
Q9H0V9	81562	<ul><li>RKR->SSS at 344-346: Loss of ER retention</li></ul>					ER	GO:0005783			1
Q9H1B7	64207	<ul><li>C->A at 715: Loss of transcription activity</li></ul>	transcription	GO:0006350							1
Q9H1D0	55503	<ul><li>D->A at 542: Abolishes channel activity</li><li>T->A at 702: Abolishes phosphorylation by PKC/PRKCA, achieves faster channel inactivation and no effect on binding to calmodulin</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488			<li>Q40302</li><li>Q8STF0</li><li>P04353</li><li>P41040</li><li>P04352</li><li>P04409</li><li>Q9GRJ1</li><li>P61860</li><li>P02594</li><li>P02595</li><li>P61861</li><li>P48976</li><li>O82018</li><li>P93171</li><li>P62184</li><li>P62144</li><li>P62145</li><li>Q5RAD2</li><li>P07463</li><li>P24044</li><li>P11121</li><li>P62149</li><li>P06787</li><li>O02367</li><li>Q6IT78</li><li>P05935</li><li>P05933</li><li>O16305</li><li>Q6PI52</li><li>P05934</li><li>Q6YNX6</li><li>Q7Y052</li><li>Q95NR9</li><li>P62157</li><li>P11118</li><li>P62156</li><li>P62155</li><li>P21251</li><li>Q5EHV7</li><li>P62154</li><li>P62152</li><li>P62151</li><li>P17252</li><li>Q7T3T2</li><li>P69097</li><li>P69098</li><li>P60206</li><li>Q9U6D3</li><li>Q9HFY6</li><li>P60205</li><li>P62158</li><li>P60204</li><li>O96102</li><li>P62201</li><li>P18061</li><li>P34722</li><li>P11120</li><li>Q8X187</li><li>P93087</li><li>O60041</li><li>Q05055</li><li>P62204</li><li>P62160</li><li>P62203</li><li>P62202</li><li>P61859</li><li>P17928</li><li>P15094</li><li>Q95NI4</li><li>Q9UWF0</li><li>P62162</li><li>P02598</li><li>P62161</li><li>P02599</li><li>Q71UH6</li><li>Q71UH5</li><li>O97341</li><li>P04464</li><li>P27165</li><li>P13678</li><li>P05130</li><li>P13677</li><li>P10102</li><li>Q39752</li><li>P84339</li><li>P27166</li><li>P23286</li><li>O94739</li><li>P27161</li><li>P41041</li><li>Q6R520</li>		1
Q9H1K0	64145	<ul><li>NPF->APA at 626-628: Reduces the interaction with EHD1. Abolishes the interaction with EHD1; when associated with 662-APA-664</li><li>NPF->APA at 662-664: Reduces the interaction with EHD1. Abolishes the interaction with EHD1; when associated with 626-APA-628</li></ul>							<li>Q07075</li><li>P16406</li><li>Q95334</li><li>P50123</li><li>Q9H4M9</li>		1
Q9H1R2	128853	<ul><li>C->S at 85: Loss of phosphatase activity</li></ul>							<li>Q5X1E5</li><li>Q7M7K5</li><li>Q7MAZ9</li><li>Q8XBL4</li><li>Q88A53</li><li>Q5P3T0</li><li>Q7MBF4</li><li>Q8Z3M9</li><li>Q5PC82</li><li>Q5ZRX9</li><li>Q821A6</li><li>Q87SK9</li><li>Q9JZ88</li><li>Q9CP21</li><li>Q82U82</li><li>Q9I5V3</li><li>Q5F8K9</li><li>Q63YC3</li><li>Q8Y395</li><li>Q6LV05</li><li>Q8ZLY4</li><li>Q6FA38</li><li>Q9PDL7</li><li>Q62EU1</li><li>Q9JUB2</li><li>Q5WT58</li><li>Q665U9</li><li>Q57JQ5</li><li>Q9KPC6</li><li>Q8P5D4</li><li>Q8CWL6</li><li>Q8PPG9</li><li>P06961</li><li>P45269</li><li>Q9L7A3</li><li>Q88QU2</li><li>Q6D160</li><li>Q8ZI64</li><li>Q60CQ4</li><li>Q87DS9</li><li>Q65Q41</li><li>Q5E2K7</li><li>Q8CXX6</li>		1
Q9H1Y0	9474	<ul><li>K->R at 130: Loss of conjugation</li></ul>	conjugation	GO:0000746							1
Q9H211	81620	<ul><li>RRL->AAA at 68-70: Abolishes binding of cyclin A-dependent protein kinases</li></ul>			binding	GO:0005488			<li>P00513</li><li>P30274</li><li>P51943</li><li>P25848</li><li>P20248</li><li>Q92161</li><li>P43449</li><li>P37881</li>		1
Q9H227	57733	<ul><li>V->Y at 168: No change in temperature or pH dependence. Decrease in specific activity</li><li>F->S at 225: Decrease in specific activity</li><li>Y->F,A at 308: Decrease in specific activity</li></ul>									1
Q9H2G2	9748	<ul><li>K->R at 63: Loss of activity</li></ul>									1
Q9H2G4	64061	<ul><li>S->A at 20: Impairs effect on cell proliferation; when associated with A-340</li><li>T->A at 340: Impairs effect on cell proliferation; when associated with A-20</li></ul>	cell proliferation	GO:0008283							1
Q9H2K8	51347	<ul><li>T->A at 181: No autophosphorylation and no kinase activity; when associated with F-183</li><li>Y->F at 183: No autophosphorylation and no kinase activity; when associated with A-181</li></ul>	autophosphorylation	GO:0046777	kinase activity	GO:0016301					1
Q9H2S9	64375	<ul><li>PED->AAA at 425-427: No effect on CTBP2 interaction</li></ul>							P56545		1
Q9H2U1	170506	<ul><li>E->A at 335: Loss of ATPase activity resulting in loss of mRNA deadenylation and decay</li></ul>			ATPase activity	GO:0016887					1
Q9H2X6	28996	<ul><li>K->A at 228: Locates in the nucleoplasm, no effect on interaction with RANBP9</li><li>K->R at 228: Abolishes enzymatic activity, no effect on interaction with TP53 and TP73 or on BMP-induced transcriptional activation. Enhances BMP-induced transcriptional activation; when associated with 359-AAF-361</li><li>STY->AAF at 359-361: Enhances BMP-induced transcriptional activation; when associated with R-228</li></ul>					nucleoplasm	GO:0005654	<li>Q9TUB2</li><li>Q9XSK8</li><li>P56423</li><li>P56424</li><li>O12946</li><li>P25035</li><li>P35855</li><li>O36006</li><li>Q64662</li><li>O57538</li><li>P10360</li><li>P61260</li><li>Q9W679</li><li>Q9W678</li><li>P13481</li><li>Q9TTA1</li><li>Q96S59</li><li>Q95330</li><li>O93379</li><li>P41685</li><li>Q96P70</li><li>Q8SPZ3</li><li>Q92143</li><li>P79820</li><li>P04637</li><li>Q29537</li><li>Q29480</li><li>O09185</li><li>Q00366</li><li>P79892</li><li>O15350</li><li>P51664</li><li>Q9WUR6</li><li>P67939</li><li>P67938</li>		1
Q9H300	55486	<ul><li>S->D at 65: Strongly reduces the beta cleavage; when associated with D-69 and D-70</li><li>T->D at 69: Strongly reduces the beta cleavage; when associated with D-65 and D-70</li><li>S->D at 70: Strongly reduces the beta cleavage; when associated with D-65 and D-69</li><li>R->E at 76: Abolishes the beta cleavage</li><li>R->G at 76: Abolishes the beta cleavage</li><li>S->E at 77: Abolishes the beta cleavage</li><li>A->E at 78: Abolishes the beta cleavage</li><li>L->E at 79: Abolishes the beta cleavage</li></ul>									1
Q9H307	5411	<ul><li>L->P at 8: Abolishes interaction with KRT18</li><li>L->P at 19: Abolishes interaction with KRT18</li><li>PE->AA at 502-503: Abolishes interaction with CTBP1 and shows moderate relief of CTBP1-mediated repression</li></ul>							<li>Q13363</li><li>P05783</li>		1
Q9H310	57127	<ul><li>F->A at 419: Loss of interaction with ANK3. Intracellular retention; when associated with A-420 and A-421</li><li>L->A at 420: Partial loss of interaction with ANK3. Intracellular retention; when associated with A-419 and A-421</li><li>D->A at 421: Partial loss of interaction with ANK3. Intracellular retention; when associated with A-419 and A-420</li></ul>					Intracellular	GO:0005622	<li>Q12955</li><li>O90760</li>		1
Q9H3D4	8626	<ul><li>F->A at 55: Abrogates transcriptional activity and interaction with transactivation inhibition domain; when associated with A-59 and A-62</li><li>W->A at 59: Abrogates transcriptional activity and interaction with transactivation inhibition domain; when associated with A-55 and A-62</li><li>L->A at 62: Abrogates transcriptional activity and interaction with transactivation inhibition domain; when associated with A-55 and A-59</li></ul>									1
Q9H3N1	81542	<ul><li>C->S at 56: Loss of reductase activity; when associated with S-59</li><li>C->S at 59: Loss of reductase activity; when associated with S-56</li></ul>									1
Q9H3S5	93183	<ul><li>D->A at 49: Almost abolishes enzyme activity</li><li>D->A at 51: Abolishes enzyme activity</li></ul>									1
Q9H3U1	55898	<ul><li>K->E at 33: Abolishes interaction with HSP90AB1; when associated with D-40. No effect on interaction with PGR</li><li>A->D at 40: Abolishes interaction with HSP90AB1; when associated with E-33. No effect on interaction with PGR</li><li>K->E at 70: Abolishes interaction with HSP90AB1; when associated with D-77. No effect on interaction with PGR</li><li>A->D at 77: Abolishes interaction with HSP90AB1; when associated with E-70. No effect on interaction with PGR</li></ul>							<li>P30947</li><li>Q04619</li><li>P06401</li><li>Q76LV1</li><li>Q9GLW0</li><li>Q9EQZ5</li><li>Q9GKX8</li><li>P06186</li><li>Q28590</li><li>P08238</li><li>P07812</li><li>Q8AYI2</li><li>P79373</li>		1
Q9H400	54923	<ul><li>Y->F at 145: No change in binding to LCK, CSK or FYN</li><li>Y->F at 167: Abolishes binding to CSK</li><li>Y->F at 200: Reduces binding to CSK</li><li>Y->F at 235: No change in binding to LCK, CSK or FYN</li><li>Y->F at 254: Abolishes binding to LCK and reduces binding to FYN</li></ul>			binding	GO:0005488			<li>Q5PXS1</li><li>P42683</li><li>P06239</li><li>Q05876</li><li>P41239</li><li>Q0VBZ0</li><li>Q95KR7</li><li>P06241</li><li>P41240</li><li>P27446</li>		1
Q9H427	60598	<ul><li>R->Y at 138: No effect on lack of functional expression</li><li>LAAKC->HRAKK at 141-145: No effect on lack of functional expression</li><li>W->R at 151: No effect on lack of functional expression</li><li>C->D at 153: No effect on lack of functional expression</li></ul>									1
Q9H492	84557	<ul><li>G->A at 120: No processing of precursor</li></ul>									1
Q9H4D5	56000	<ul><li>L->R at 300: Inactivates CRM1 binding; when associated with R-302</li><li>L->R at 302: Inactivates CRM1 binding; when associated with R-300</li></ul>			binding	GO:0005488			<li>O14980</li><li>P30822</li>		1
Q9H4E7	50619	<ul><li>L->N at 18: Abolishes interaction with RAC1</li><li>LKV->NKS at 31-33: Abolishes interaction with RAC1</li><li>Y->F at 210: Loss of phosphorylation by LCK and abolition of PtdInsP3 binding</li><li>KR->AA at 225-226: Abolishes PtdInsP3 binding</li><li>RR->AA at 230-231: Abolishes PtdInsP3 binding</li><li>R->C at 236: Abolishes PtdInsP3 binding</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488			<li>Q5PXS1</li><li>P42683</li><li>P06239</li><li>Q95KR7</li><li>Q9SSX0</li><li>Q38912</li><li>O04369</li><li>P13362</li><li>P80236</li><li>P62999</li><li>P63000</li><li>P62998</li>		1
Q9H4P4	10193	<ul><li>C->S at 34: Loss of activity; when associated with Q-36</li><li>H->Q at 36: Loss of activity; when associated with S-34</li><li>D->V at 56: Loss of activity</li></ul>									1
Q9H4X1	28984	<ul><li>T->A at 111: Loss of phosphorylation. Reduced stimulation of CDC2 activity</li></ul>	phosphorylation	GO:0016310					<li>Q9W739</li><li>Q9DGA2</li><li>Q9DGA5</li><li>P19026</li><li>Q5RCH1</li><li>Q9DG98</li><li>P06493</li><li>P48734</li><li>P43290</li><li>P23111</li><li>P13863</li><li>Q04770</li><li>P52389</li><li>P15436</li><li>P24100</li><li>P51958</li><li>Q41639</li><li>P54119</li><li>P93101</li><li>Q9DGD3</li>		1
Q9H5Q4	64216	<ul><li>G->A at 105: Abolishes methyltransferase activity</li></ul>							<li>Q00020</li><li>P03588</li><li>P03589</li><li>Q83270</li><li>P28931</li><li>P06011</li><li>P17769</li><li>P20122</li><li>Q66121</li><li>O40976</li><li>P28726</li><li>P27752</li><li>Q83264</li>		1
Q9H5V8	64866	<ul><li>Y->F at 734: Impaired association with SRC</li><li>Y->F at 762: Impaired association with protein kinase PRKCG but not with SRC</li></ul>							<li>P00513</li><li>P00523</li><li>P12931</li><li>P25848</li><li>P05129</li><li>P05128</li><li>P10829</li>		1
Q9H611	80119	<ul><li>K->A at 234: Loss of ATPase activity. Lower activity for single-stranded DNA</li></ul>			ATPase activity	GO:0016887					1
Q9H6P5	55617	<ul><li>D->A at 233: 0.1% enzymatic activity; no intramolecular processing</li><li>T->A at 234: Complete loss of enzymatic activity; no intramolecular processing</li></ul>									1
Q9H6Q3	84174	<ul><li>G->A at 2: Abolishes localization to membranes</li></ul>	localization	GO:0051179			membranes	GO:0016020			1
Q9H6Y7	26001	<ul><li>I->A at 232: Drastically increased stability; reduction in auto-ubiquitination activity; loss of cell delay/arrest in G1</li><li>W->A at 260: Drastically increased stability; reduction in auto-ubiquitination activity; loss of cell delay/arrest in G1</li></ul>									1
Q9H6Z9	112399	<ul><li>H->A at 135: Eliminates hydroxylase activity</li><li>D->A at 137: Eliminates hydroxylase activity</li><li>H->A at 196: Eliminates hydroxylase activity</li></ul>									1
Q9H7Z7	80142	<ul><li>C->S at 110: Loss of function</li><li>C->S at 113: Does not strongly affect enzyme activity</li></ul>									1
Q9H8N7	55893	<ul><li>L->A at 109: No change in subcellular location; when associated with A-113</li><li>L->A at 113: No change in subcellular location; when associated with A-109</li><li>M->A at 169: No shuttle from the nucleus to the cytoplasm; when associated with A-172</li><li>M->A at 172: No shuttle from the nucleus to the cytoplasm; when associated with A-169</li></ul>					<li>cytoplasm</li><li>nucleus</li>	<li>GO:0005737</li><li>GO:0005634</li>			1
Q9H8Y8	26003	<ul><li>T->A at 222: Abolishes mitotic phosphorylation; when associated with A-225</li><li>T->A at 225: Abolishes mitotic phosphorylation; when associated with A-222</li></ul>	phosphorylation	GO:0016310							1
Q9H9H5	79929	<ul><li>C->G at 5: Loss of Golgi colocalization and gain of microtubule colocalization; when associated with C-10 and C-11</li><li>C->G at 10: Loss of Golgi colocalization and gain of microtubule colocalization; when associated with C-5 and C-11</li><li>C->G at 11: Loss of Golgi colocalization and gain of microtubule colocalization; when associated with C-5 and C-10</li></ul>					microtubule	GO:0005874			1
Q9HAJ7	79685	<ul><li>RK->KS at 88-89: Impairs nuclear localization</li><li>RRYKRHYK->AAAAA at 120-127: Abolishes nucleolar localization</li></ul>	localization	GO:0051179							1
Q9HAU4	64750	<ul><li>F->A at 29: Increases autoubiquitination; when associated with A-30</li><li>F->A at 30: Increases autoubiquitination; when associated with A-29</li><li>T->A at 56: Increases autoubiquitination; when associated with A-57</li><li>L->A at 57: Increases autoubiquitination; when associated with A-56</li><li>Missing at 251-284: Abolishes interaction with SMAD2 and SMAD7</li><li>Missing at 297-330: Abolishes interaction with SMAD7</li><li>W->A at 535: Loss of catalytic activity</li><li>W->D at 535: Loss of catalytic activity</li><li>H->A at 547: Partial loss of catalytic activity</li><li>H->F,I at 547: Activates autocatalytic activity</li><li>Y->A at 581: Loss of catalytic activity</li><li>C->A at 716: Increases Smad7-bound TGF-beta receptors in membrane rafts</li><li>C->G at 716: Loss of activity. Loss of ability to ubiquitinate SMAD1 and SMAD2 and no down-regulation of SMAD1 and SMAD2 protein levels</li></ul>			catalytic activity	GO:0003824	membrane	GO:0016020	<li>O35253</li><li>Q15796</li><li>O15105</li><li>Q1JQA2</li><li>Q1W668</li><li>Q15797</li><li>O88406</li><li>Q9I962</li>		1
Q9HAU5	26019	<ul><li>RK->EE at 796-797: Strongly impairs RNA-binding</li><li>D->K at 847: Does not abolish interaction with RENT3B</li><li>ED->KR at 851-852: Does not abolish interaction with RENT3B. Does not abolish interaction with RENT3B; when associated with D-854</li><li>R->D at 854: Does not abolish interaction with RENT3B; when associated with K-851 and R-852</li><li>E->R at 858: Abolishes interaction with RENT3B</li><li>Y->A at 894: Does not impair RNA-binding; when associated with A-932</li><li>Y->A at 932: Does not impair RNA-binding; when associated with A-894</li></ul>			RNA-binding	GO:0003723			Q9BZI7		1
Q9HAV5	60401	<ul><li>E->R at 256: Abolishes TRAF6 association</li></ul>							Q9Y4K3		1
Q9HAW4	63967	<ul><li>T->A at 916: Impairs interaction with CHEK1</li><li>S->A at 945: Impairs interaction with CHEK1</li><li>S->A at 982: No effect on interaction with CHEK1</li></ul>							<li>O14757</li><li>Q8AYC9</li>		1
Q9HAZ1	57396	<ul><li>K->R at 189: Loss of function</li></ul>									1
Q9HB21	59338	<ul><li>R->L at 28: No effect on phosphatidylinositide binding</li><li>AVM->GGG at 203-205: Abolishes phosphatidylinositide binding</li><li>AVM->GLV at 203-205: Binds both PtdIns3,4P2 and PtdIns3,4,5P3</li><li>AV->GG at 203-204: Binds both PtdIns3,4P2 and PtdIns3,4,5P3</li><li>A->G at 203: Binds both PtdIns3,4P2 and PtdIns3,4,5P3</li><li>V->L at 204: No effect</li><li>M->V at 205: No effect</li><li>N->T at 207: No effect</li><li>R->L at 211: Abolishes phosphatidylinositide binding</li></ul>			binding	GO:0005488					1
Q9HBA0	59341	<ul><li>RLRRDR->ELEEDE at 816-821: Loss of calmodulin binding; when associated with A-828</li><li>RWSS->AASA at 821-824: Loss of calmodulin binding</li><li>W->A at 822: Loss of Ca(2+) dependent current potentiation</li><li>R->A at 828: Loss of calmodulin binding; when associated with 816-ELEEDE-821</li></ul>			binding	GO:0005488			<li>Q40302</li><li>Q8STF0</li><li>P04353</li><li>P41040</li><li>P04352</li><li>Q9GRJ1</li><li>P61860</li><li>P02594</li><li>P02595</li><li>P61861</li><li>P48976</li><li>O82018</li><li>P93171</li><li>P62184</li><li>P62144</li><li>P62145</li><li>Q5RAD2</li><li>P07463</li><li>P24044</li><li>P11121</li><li>P62149</li><li>P06787</li><li>O02367</li><li>Q6IT78</li><li>P05935</li><li>P05933</li><li>O16305</li><li>Q6PI52</li><li>P05934</li><li>Q6YNX6</li><li>Q7Y052</li><li>Q95NR9</li><li>P11118</li><li>P62157</li><li>P62156</li><li>P21251</li><li>P62155</li><li>Q5EHV7</li><li>P62154</li><li>P62152</li><li>P62151</li><li>Q7T3T2</li><li>P69097</li><li>P69098</li><li>P60206</li><li>Q9U6D3</li><li>Q9HFY6</li><li>P60205</li><li>P62158</li><li>P60204</li><li>O96102</li><li>P62201</li><li>P18061</li><li>P11120</li><li>Q8X187</li><li>P93087</li><li>O60041</li><li>Q05055</li><li>P62204</li><li>P62160</li><li>P62203</li><li>P62202</li><li>P61859</li><li>P17928</li><li>P15094</li><li>Q95NI4</li><li>Q9UWF0</li><li>P62162</li><li>P02598</li><li>P62161</li><li>P02599</li><li>Q71UH6</li><li>Q71UH5</li><li>O97341</li><li>P04464</li><li>P27165</li><li>Q39752</li><li>P84339</li><li>P27166</li><li>P23286</li><li>O94739</li><li>P27161</li><li>P41041</li><li>Q6R520</li>		1
Q9HBF4	53349	<ul><li>T->R at 616: Partially restore PtdIns3P binding; when associated with R-733</li><li>K->A at 617: Drastically reduce PtdIns3P binding; when associated with A-619 and A-621. Abolishes PtdIns3P binding; when associated with A-734; A-736 and A-738</li><li>H->A at 619: Drastically reduce PtdIns3P binding; when associated with A-617 and A-621. Abolishes PtdIns3P binding; when associated with A-734; A-736 and A-738</li><li>R->A at 621: Drastically reduce PtdIns3P binding; when associated with A-617 and A-619. Abolishes PtdIns3P binding; when associated with A-734; A-736 and A-738</li><li>C->S at 654: Abolishes PtdIns3P binding; when associated with S-770</li><li>S->R at 733: Partially restored PtdIns3P binding; when associated with R-616</li><li>K->A at 734: Drastically reduce PtdIns3P binding; when associated with A-736 and A-738. Abolishes PtdIns3P binding; when associated with A-617; A-619 and A-621</li><li>H->A at 736: Drastically reduce PtdIns3P binding; when associated with A-734 and A-738. Abolishes PtdIns3P binding; when associated with A-617; A-619 and A-621</li><li>R->A at 738: Drastically reduce PtdIns3P binding; when associated with A-734 and A-736. Abolishes PtdIns3P binding; when associated with A-617; A-619 and A-621</li><li>C->S at 770: Abolishes PtdIns3P binding; when associated with S-654</li></ul>			binding	GO:0005488					1
Q9HBH9	2872	<ul><li>T->A at 244: Loss of kinase activity; when associated with T-249</li><li>T->A at 249: Loss of kinase activity; when associated with T-244</li><li>T->D at 379: Constitutively active</li></ul>			kinase activity	GO:0016301					1
Q9HBW0	9170	<ul><li>D->A at 348: Abolishes interaction with MAGI3</li><li>S->A at 349: Abolishes interaction with MAGI3</li><li>T->A at 350: Does not affect interaction with MAGI3</li><li>L->A at 351: Abolishes interaction with MAGI3</li></ul>									1
Q9HBX9	59350	<ul><li>D->Y at 637: Leads to constitutive increase of basal cAMP</li></ul>									1
Q9HBY0	50508	<ul><li>P->H at 413: Loss of catalytic activity</li></ul>			catalytic activity	GO:0003824					1
Q9HBY8	10110	<ul><li>S->D at 416: Increased activation</li></ul>									1
Q9HC16	60489	<ul><li>E->Q at 67: Decreases cytidine deaminase activity</li><li>H->A at 81: Decreases cytidine deaminase activity</li><li>E->Q at 85: Does not decrease cytidine deaminase activity</li><li>C->A at 97: Decreases cytidine deaminase activity</li><li>C->A,S at 100: Decreases cytidine deaminase activity</li><li>D->K at 128: Complete loss of VIF-induced degradation</li><li>C->S at 221: Does not decrease cytidine deaminase activity</li><li>H->A at 257: Decreases cytidine deaminase activity</li><li>E->Q at 259: Decreases cytidine deaminase activity</li><li>C->A at 288: Decreases cytidine deaminase activity</li><li>C->A,S at 291: Decreases cytidine deaminase activity</li><li>E->Q at 323: Does not decrease cytidine deaminase activity</li></ul>							<li>Q9KSM5</li><li>P47298</li><li>Q8ZG08</li><li>Q7MK48</li><li>Q06549</li><li>Q7N6K3</li><li>Q65RG8</li><li>Q3IBX5</li><li>Q8X648</li><li>P56389</li><li>Q9S3M0</li><li>Q4QK60</li><li>Q32EM3</li><li>P44325</li><li>P32320</li><li>P47718</li><li>Q6D3B4</li><li>Q57MF5</li><li>Q5E4R6</li><li>Q6LRI0</li><li>Q322V3</li><li>Q66C79</li><li>Q3Z062</li><li>P19079</li><li>P0ABF6</li><li>Q9CP11</li><li>Q8EDG1</li><li>Q87Q52</li><li>P0ABF7</li><li>Q7VMJ6</li><li>Q9KD53</li><li>Q8DA31</li><li>Q5PE68</li><li>P53348</li><li>Q8FFV3</li><li>P75051</li><li>Q8ZNM0</li><li>Q8Z5A8</li>		1
Q9HC29	64127	<ul><li>K->R at 305: No activation</li></ul>									1
Q9HC84	727897	<ul><li>W->A at 1791: Poorly secreted</li></ul>									1
Q9HC98	10783	<ul><li>K->M at 74: Loss of autophosphorylation and of kinase activity and induction of apoptosis; when associated with M-75</li><li>K->M at 75: Loss of autophosphorylation and of kinase activity and induction of apoptosis; when associated with M-74</li></ul>	<li>autophosphorylation</li><li>induction of apoptosis</li>	<li>GO:0046777</li><li>GO:0006917</li>	kinase activity	GO:0016301					1
Q9HCD5	57727	<ul><li>I->A at 342: Abolishes E2-inducible strong interaction with ESR1, but not basal interaction</li><li>LL->AA at 348-349: Abolishes interaction with ESR1</li></ul>			E2	GO:0004840			<li>Q9TV98</li><li>Q9QZJ5</li><li>P49884</li><li>Q91424</li><li>Q91250</li><li>Q29040</li><li>P38111</li><li>Q9YHT3</li><li>P50242</li><li>P50241</li><li>P03372</li><li>P16058</li><li>Q9YH33</li><li>Q9PVZ9</li><li>P50240</li><li>P06212</li><li>P57753</li><li>Q53AD2</li><li>P49885</li><li>P49886</li><li>Q9YHZ7</li><li>O42132</li>		1
Q9HCE7	57154	<ul><li>C->A at 725: Loss of ubiquitination capacity</li></ul>									1
Q9HCN6	51206	<ul><li>K->A at 61: Increases collagen binding</li><li>K->E at 79: Dramatically reduces collagen binding</li><li>R->A at 80: Reduces collagen binding</li><li>N->A at 92: Reduces collagen binding (65 to 70%)</li><li>S->A at 94: Reduces collagen binding (65 to 70%)</li><li>L->H at 95: No effect on collagen binding</li><li>R->A at 186: Reduces collagen binding</li></ul>			collagen binding	GO:0005518					1
Q9HCR9	50940	<ul><li>D->A at 355: Induces a decrease in enzyme activity due to the inability of cGMP to bind and stimulate enzyme activity</li></ul>									1
Q9HCU8	57804	<ul><li>I->A at 7: Abolishes interaction with PCNA; when associated with 10-AA-11</li><li>SY->A at 10-11: Abolishes interaction with PCNA; when associated with A-7</li></ul>							<li>O16852</li><li>Q9HJQ0</li><li>Q6B6N4</li><li>Q8PX25</li><li>P61074</li><li>O29912</li><li>Q9DDF1</li><li>Q43124</li><li>Q57697</li><li>P18248</li><li>O02115</li><li>P53358</li><li>O01377</li><li>Q6LWJ8</li><li>Q9MAY3</li><li>Q00268</li><li>Q00265</li><li>Q8TUF7</li><li>Q9DEA3</li><li>P17070</li><li>O58398</li><li>Q9M7Q7</li><li>O10308</li><li>P31008</li><li>P17917</li><li>P61258</li><li>P17918</li><li>P11038</li><li>P15873</li><li>Q7T6Y0</li><li>Q03392</li><li>P22177</li><li>P04961</li><li>Q979S2</li><li>P57761</li><li>O73947</li><li>Q9W644</li><li>Q9UWR9</li><li>Q9PTP1</li><li>Q74MV1</li><li>Q8TWK3</li><li>O82134</li><li>Q9HN45</li><li>Q6KZF1</li><li>O82797</li><li>P12004</li><li>P24314</li><li>Q9UYX8</li><li>Q9P9H8</li><li>Q43266</li><li>O27367</li>		1
Q9HD26	57120	<ul><li>L->V at 175: No effect on subcellular location; when associated with V-182; V-189 and V-196</li><li>L->V at 182: No effect on subcellular location; when associated with V-175; V-189 and V-196</li><li>L->V at 189: No effect on subcellular location; when associated with V-175; V-182 and V-196</li><li>L->V at 196: No effect on subcellular location; when associated with V-175; V-182 and V-189</li></ul>									1
Q9HD40	51091	<ul><li>K->A at 284: Loss of activity</li></ul>									1
Q9HD43	5794	<ul><li>D->A at 986: Loss of activity. Acts as a dominant negative mutant</li><li>C->S at 1020: Loss of activity. No induction of apoptosis</li></ul>	induction of apoptosis	GO:0006917							1
Q9NNX6	30835	<ul><li>LL->AA at 14-15: Loss of antigen internalization by endocytosis</li><li>D->A at 320: Loss of binding to ICAM3 and HIV-1 gp120</li><li>E->A at 324: Loss of binding to ICAM3 and HIV-1 gp120</li><li>E->Q at 347: Loss of binding to ICAM3 and HIV-1 gp120</li><li>N->D at 349: Loss of binding to ICAM3 and HIV-1 gp120</li><li>N->A at 350: Loss of binding to ICAM3 and HIV-1 gp120</li><li>D->A at 355: Loss of binding to ICAM3 and HIV-1 gp120</li><li>N->D at 365: Loss of binding to ICAM3 and HIV-1 gp120</li><li>D->A at 366: Loss of binding to ICAM3 and HIV-1 gp120</li></ul>	endocytosis	GO:0006897	binding	GO:0005488			<li>P32942</li><li>Q5NKU6</li><li>Q28125</li>		1
Q9NP77	29101	<ul><li>C->S at 12: Abolishes phosphatase activity</li></ul>							<li>Q5X1E5</li><li>Q7M7K5</li><li>Q7MAZ9</li><li>Q8XBL4</li><li>Q88A53</li><li>Q5P3T0</li><li>Q7MBF4</li><li>Q8Z3M9</li><li>Q5PC82</li><li>Q5ZRX9</li><li>Q821A6</li><li>Q87SK9</li><li>Q9JZ88</li><li>Q9CP21</li><li>Q82U82</li><li>Q9I5V3</li><li>Q5F8K9</li><li>Q63YC3</li><li>Q8Y395</li><li>Q6LV05</li><li>Q8ZLY4</li><li>Q6FA38</li><li>Q9PDL7</li><li>Q62EU1</li><li>Q9JUB2</li><li>Q5WT58</li><li>Q665U9</li><li>Q57JQ5</li><li>Q9KPC6</li><li>Q8P5D4</li><li>Q8CWL6</li><li>Q8PPG9</li><li>P06961</li><li>P45269</li><li>Q9L7A3</li><li>Q88QU2</li><li>Q6D160</li><li>Q8ZI64</li><li>Q60CQ4</li><li>Q87DS9</li><li>Q65Q41</li><li>Q5E2K7</li><li>Q8CXX6</li>		1
Q9NPB6	50855	<ul><li>K->A at 19: Loss of interaction with PRKCI</li><li>R->A at 28: Slight decrease of interaction with PRKCI. Loss of interaction with PRKCI; when associated with A-89</li><li>R->A at 89: Slight decrease of interaction with PRKCI. Loss of interaction with PRKCI; when associated with A-28</li></ul>							<li>Q5R4K9</li><li>P41743</li>		1
Q9NPC3	57820	<ul><li>C->A at 28: Abrogates induction of filamentous growth in yeast; when associated with A-30 and A-33</li><li>H->A at 30: Abrogates induction of filamentous growth in yeast; when associated with A-28 and A-33</li><li>C->A at 33: Abrogates induction of filamentous growth in yeast; when associated with A-28 and A-30</li></ul>	filamentous growth	GO:0030447							1
Q9NPF2	50515	<ul><li>K->Q at 125: Abolishes enzyme activity but does not affect stability of the protein</li><li>N->S at 205: Induces a weak decrease in enzyme activity but has no effect on stability of the protein. Unstable protein; when associated with S-223 and S-321</li><li>N->S at 223: Induces a weak decrease in enzyme activity but has no effect on stability of the protein. Unstable protein; when associated with S-205 and S-321</li><li>N->S at 321: Induces a strong decrease in enzyme activity but has no effect on stability of the protein. Unstable protein; when associated with S-205 and S-223</li><li>N->S at 342: Induces a strong decrease in enzyme activity has no effect on stability of the protein</li></ul>									1
Q9NPH0	51205	<ul><li>H->A at 59: Decreased activity</li></ul>									1
Q9NPH5	50507	<ul><li>R->RGT at 304: Partial loss of catalytic activity. No effect on CYBA localization</li><li>Missing at 575-578: Partial loss of catalytic activity. No effect on CYBA localization</li></ul>	localization	GO:0051179	catalytic activity	GO:0003824			<li>Q95MN4</li><li>P52650</li><li>Q95L73</li><li>P13498</li><li>Q9N2H0</li><li>O46521</li>		1
Q9NPI5	27231	<ul><li>D->A at 35: Loss of activity</li><li>E->A at 100: Loss of activity</li></ul>									1
Q9NPI6	55802	<ul><li>D->A at 20: Lowers decapping activity</li><li>R->A at 59: Lowers decapping activity</li></ul>									1
Q9NPI8	2188	<ul><li>L->R at 209: Reduced monoubiquitination of FANCD2</li><li>F->R at 251: Reduced monoubiquitination of FANCD2</li><li>Y->A at 287: Strongly reduced monoubiquitination of FANCD2; when associated with A-289; A-339; A-341 and A-344</li><li>L->A at 289: Strongly reduced monoubiquitination of FANCD2; when associated with A-287; A-339; A-341 and A-344</li><li>F->A at 339: Strongly reduced monoubiquitination of FANCD2; when associated with A-287; A-289; A-341 and A-344</li><li>V->A at 341: Strongly reduced monoubiquitination of FANCD2; when associated with A-287; A-289; A-339 and A-344</li><li>L->A at 344: Strongly reduced monoubiquitination of FANCD2; when associated with A-287; A-289; A-339 and A-341</li></ul>							Q9BXW9		1
Q9NPJ4	100132235	<ul><li>P->A at 101: Abolishes the interaction with the nuclear receptors; when associated with A-104</li><li>P->A at 104: Abolishes the interaction with the nuclear receptors; when associated with A-101</li></ul>									1
Q9NQ94	29974	<ul><li>F->A at 59: Greatly reduced RNA binding</li><li>F->A at 100: Greatly reduced RNA binding</li><li>F->A at 139: Greatly reduced RNA binding</li><li>F->A at 183: Greatly reduced RNA binding</li><li>Y->A at 234: Slightly reduced RNA binding</li><li>F->A at 270: Slightly reduced RNA binding</li></ul>			RNA binding	GO:0003723					1
Q9NQB0	6934	<ul><li>DD->AA at 10-11: Reduces CTNNB1 binding</li><li>D->A at 16: Abolishes CTNNB1 binding</li><li>E->A at 17: Reduces CTNNB1 binding</li><li>I->A at 19: Reduces transcription activation</li><li>F->A at 21: Reduces transcription activation</li><li>DE->AA at 23-24: Reduces CTNNB1 binding</li><li>E->A at 24: Reduces CTNNB1 binding, and abolishes CTNNB1 binding; when associated with A-26; A-28 and A-29</li><li>E->A at 26: Abolishes CTNNB1 binding; when associated with A-24; A-28 and A-29</li><li>E->A at 28: Abolishes CTNNB1 binding; when associated with A-24; A-26 and A-29</li><li>E->A at 29: Reduces CTNNB1 binding, and abolishes CTNNB1 binding; when associated with A-24; A-26 and A-28</li><li>L->A at 48: Abolishes CTNNB1 binding</li><li>K->R at 320: Loss of sumoylation. No effect on localization to nuclear bodies</li><li>E->A at 322: Loss of sumoylation</li></ul>	<li>sumoylation</li><li>localization</li><li>transcription</li>	<li>GO:0016925</li><li>GO:0051179</li><li>GO:0006350</li>	binding	GO:0005488			P35222		1
Q9NQC7	1540	<ul><li>S->A at 457: Abolishes binding to TRAF2</li><li>C->S at 601: Loss of deubiquitinating activity</li><li>H->N at 871: Loss of deubiquitinating activity</li></ul>			binding	GO:0005488			Q12933		1
Q9NQE9	135114	<ul><li>H->A at 145: Abolishes hydrolase activity</li></ul>			hydrolase activity	GO:0016787					1
Q9NQR1	387893	<ul><li>Y->A,F at 286: Strongly reduces affinity for histone H4 and abolishes methyltransferase activity</li><li>E->A at 300: Strongly reduces affinity for histone H4</li><li>C->A at 311: Strongly reduces affinity for histone H4</li><li>R->G at 336: Abolishes methyltransferase activity</li><li>H->A at 340: Strongly decreases methyltransferase activity</li><li>Y->A at 375: Strongly reduces affinity for histone H4 and methyltransferase activity</li><li>Y->F at 375: Alters methyltransferase activity, so that both monomethylation and dimethylation take place</li><li>D->A,N at 379: Abolishes histone H4 binding and methyltransferase activity</li><li>Missing at 385-393: Abolishes methyltransferase activity</li><li>H->A,E at 388: Strongly reduces affinity for histone H4</li><li>H->F at 388: Increases affinity for histone H4</li></ul>			binding	GO:0005488			<li>Q76FE7</li><li>P82888</li><li>Q6LAF1</li><li>P91882</li><li>Q6LAF3</li><li>Q27443</li><li>Q8MTV8</li><li>Q76FD9</li><li>P08436</li><li>P35059</li><li>P35057</li><li>P91890</li><li>Q6WZ83</li><li>P83865</li><li>P84048</li><li>P84049</li><li>P84044</li><li>Q7K8C0</li><li>Q7KQD1</li><li>P84045</li><li>P62779</li><li>P84046</li><li>P62778</li><li>P84047</li><li>P84040</li><li>P62777</li><li>P84041</li><li>P62776</li><li>Q8I0Y4</li><li>P84042</li><li>P84043</li><li>P84050</li><li>Q43083</li><li>Q6WV90</li><li>P62782</li><li>P62781</li><li>P62784</li><li>Q8NIG3</li><li>P62783</li><li>P28931</li><li>P62780</li><li>Q9HDF5</li><li>P62789</li><li>Q7LKT3</li><li>P62788</li><li>Q27765</li><li>Q6WV73</li><li>P20122</li><li>P62787</li><li>Q6WV74</li><li>P17769</li><li>P59259</li><li>Q7M3Z5</li><li>O40976</li><li>P27752</li><li>P91849</li><li>Q6ZXX3</li><li>P03588</li><li>P03589</li><li>P09322</li><li>Q76H85</li><li>P62796</li><li>P62797</li><li>P62798</li><li>P62799</li><li>P28726</li><li>P62790</li><li>P62791</li><li>P62792</li><li>P62793</li><li>P62794</li><li>P62795</li><li>Q6WV72</li><li>Q00020</li><li>P80739</li><li>P80738</li><li>Q66121</li><li>Q9U7D0</li><li>P27996</li><li>P90516</li><li>Q8T7J8</li><li>P62803</li><li>P62802</li><li>P62801</li><li>P62800</li><li>Q76MU7</li><li>P02309</li><li>Q8J1L3</li><li>Q6V9I2</li><li>P62806</li><li>P50566</li><li>P62804</li><li>P62805</li><li>P04915</li><li>Q76FF5</li><li>Q8SQP4</li><li>P04914</li><li>Q76FF1</li><li>Q83270</li><li>P06011</li><li>Q6PMI5</li><li>P62887</li><li>Q83264</li><li>P40287</li><li>Q71V09</li>		1
Q9NQR9	57818	<ul><li>N->A at 50: No effect on N-glycosylation</li><li>N->A at 92: Loss of N-glycosylation</li><li>N->A at 287: No effect on N-glycosylation</li></ul>									1
Q9NQW6	54443	<ul><li>R->A at 32: Abrogates interaction with CD2AP</li><li>R->A at 41: Abrogates ubiquitin-mediated proteolysis; when associated with A-44</li><li>L->A at 44: Abrogates ubiquitin-mediated proteolysis; when associated with A-41</li></ul>							<li>P69326</li><li>P08565</li><li>P69322</li><li>P69323</li><li>P69324</li><li>P69325</li><li>P68196</li><li>O46543</li><li>P68197</li><li>Q05550</li><li>P68198</li><li>P68199</li><li>P19848</li><li>P42739</li><li>P68195</li><li>Q867C2</li><li>P62991</li><li>P62990</li><li>P61863</li><li>P61864</li><li>P61862</li><li>Q867C4</li><li>Q867C3</li><li>P23398</li><li>P68204</li><li>P84589</li><li>Q865C5</li><li>P42740</li><li>P68201</li><li>Q8MKD1</li><li>P14792</li><li>P63049</li><li>P0C072</li><li>P63051</li><li>P69308</li><li>P69309</li><li>P20685</li><li>Q9Y5K6</li><li>P15174</li><li>P62976</li><li>P62977</li><li>P62974</li><li>P62975</li><li>P62972</li><li>P13117</li><li>P14624</li><li>P62973</li><li>P46574</li><li>P69310</li><li>P69313</li><li>P69314</li><li>P69311</li><li>P08618</li><li>P69312</li><li>P69317</li><li>P69318</li><li>P69315</li><li>P0C014</li><li>P69316</li><li>P59263</li><li>P69319</li><li>P49634</li><li>P49635</li><li>Q9Y848</li><li>P22589</li><li>P62988</li><li>P62989</li><li>P69321</li><li>P23324</li><li>P69320</li><li>P59669</li>		1
Q9NQX7	81618	<ul><li>KR->AA at 241-242: Completely abrogates proteolytic processing</li></ul>									1
Q9NR12	9260	<ul><li>GF->AA at 15-16: Loss of binding to TPM2</li><li>H->A at 63: Loss of binding to TPM2</li></ul>			binding	GO:0005488			<li>P07951</li><li>P40414</li><li>P19352</li><li>P58776</li><li>Q9U5M4</li>		1
Q9NR20	8798	<ul><li>K->R at 133: Loss of kinase activity</li></ul>			kinase activity	GO:0016301					1
Q9NR22	56341	<ul><li>G->A at 2: Loss of cell membrane localization</li></ul>	localization	GO:0051179			cell membrane	GO:0005886			1
Q9NR71	56624	<ul><li>S->A at 258: Impairs enzyme activity</li><li>D->A at 352: Abolishes enzyme activity</li><li>S->A at 354: Abolishes enzyme activity</li><li>C->A at 362: Abolishes enzyme activity</li><li>S->A at 374: Impairs enzyme activity</li><li>S->A at 396: No effect</li><li>S->A at 595: Impairs enzyme activity</li><li>S->A at 729: Impairs enzyme activity</li></ul>									1
Q9NR83	56731	<ul><li>L->A at 257: Nuclear; when associated with A-260</li><li>L->A at 260: Nuclear; when associated with A-257</li><li>F->A at 273: Cytoplasmic; when associated with A-276</li><li>L->A at 276: Cytoplasmic; when associated with A-273</li></ul>									1
Q9NRA1	56034	<ul><li>C->S at 124: Loss of mitogenic activity of CUB domain in coronary artery smooth muscle cells</li><li>R->A at 231: Essential for cleavage by PLAT</li><li>K->A at 232: Not essential for cleavage by PLAT</li><li>R->A at 234: Not essential for cleavage by PLAT</li></ul>							<li>P00750</li><li>Q28198</li>		1
Q9NRA8	56478	<ul><li>Y->A at 30: Abolishes interaction with EIF4E</li><li>RR->NS at 195-196: Abolishes the nuclear localization</li></ul>	localization	GO:0051179					<li>Q9P974</li><li>P63074</li><li>Q9P975</li><li>Q9N0T5</li><li>P29338</li><li>P48598</li><li>Q75AV8</li><li>P06730</li><li>P48597</li><li>O77210</li><li>P07260</li><li>Q5UQG4</li><li>Q9PW28</li><li>P63073</li>		1
Q9NRD5	9463	<ul><li>KD->AA at 27-28: Abolishes interaction with other proteins, but not with itself</li></ul>									1
Q9NRF2	25970	<ul><li>F->R at 29: Abolishes self-association and interaction with INSR and IGF1R</li><li>A->D at 34: Abolishes self-association and interaction with INSR and IGF1R</li><li>A->D at 38: Abolishes self-association and interaction with INSR and IGF1R</li><li>F->A at 41: Abolishes self-association and interaction with INSR and IGF1R</li><li>A->D at 42: Abolishes self-association and interaction with INSR and IGF1R</li><li>Y->A at 48: Abolishes self-association and interaction with INSR and IGF1R</li><li>F->A at 68: Abolishes self-association and interaction with INSR and IGF1R</li><li>F->A at 72: Abolishes self-association and interaction with INSR and IGF1R</li><li>R->A at 555: Abolishes self-association and interaction with INSR and IGF1R</li></ul>							<li>P08069</li><li>Q28516</li><li>P06213</li><li>Q29000</li><li>Q05688</li>		1
Q9NRH2	54861	<ul><li>T->A,E at 173: Prevents phosphorylation and activation by STK11 complex</li></ul>	phosphorylation	GO:0016310					<li>Q15831</li><li>Q0GGW5</li>		1
Q9NRI5	27185	<ul><li>L->P at 815: Impairs interaction with NDEL1; when associated with P-822</li><li>L->P at 822: Impairs interaction with NDEL1; when associated with P-815</li></ul>							<li>O46480</li><li>Q5ZKH4</li><li>Q4R4S6</li><li>Q9GZM8</li><li>Q5R8T7</li>		1
Q9NRM7	26524	<ul><li>S->C at 83: Fails to localize at the centromere during interphase</li><li>S->E at 83: Fails to localize at the centromere during interphase</li><li>K->A at 697: Loss of kinase activity, autophosphorylation and tumor suppressor activity</li><li>S->A at 872: Loss of tumor suppressor activity</li></ul>	<li>autophosphorylation</li><li>interphase</li>	<li>GO:0046777</li><li>GO:0051325</li>	kinase activity	GO:0016301					1
Q9NRP7	27148	<ul><li>K->R at 33: No effect on nuclear localization of GLI1 or GLI2 or on GLI-mediated transcription</li></ul>	<li>transcription</li><li>localization</li>	<li>GO:0006350</li><li>GO:0051179</li>					<li>P10070</li><li>P55878</li><li>P08151</li>		1
Q9NRR8	56882	<ul><li>CC->AA at 10-11: Prevents targeting to the activated TCR</li><li>P->A at 33: Abolishes interaction with CDC42, induces a decrease in blocking CDC42-induced JNK activation but does not affect targeting to the activated TCR; when associated with A-38 and A-41</li><li>H->A at 38: Abolishes interaction with CDC42, induces a decrease in blocking CDC42-induced JNK activation but does not affect targeting to the activated TCR; when associated with A-33 and A-41</li><li>H->A at 41: Abolishes interaction with CDC42, induces a decrease in blocking CDC42-induced JNK activation but does not affect targeting to the activated TCR; when associated with A-33 and A-38</li><li>Q->A at 62: Abolishes interaction with CDC42 and induces a decrease in blocking CDC42-induced JNK activation; when associated with A-66</li><li>K->A at 66: Abolishes interaction with CDC42 and induces a decrease in blocking CDC42-induced JNK activation; when associated with A-62</li></ul>					TCR	GO:0042101	<li>Q90694</li><li>O94103</li><li>O14426</li><li>Q966Y3</li><li>P60953</li><li>Q17031</li><li>P60952</li><li>P92208</li><li>Q9HF56</li><li>P19073</li>		1
Q9NS18	51022	<ul><li>C->S at 68: Abolishes absorption at 320 nm and 420 nm suggesting the loss of 2Fe-2S-binding</li><li>S->P at 78: Specifically increases the specific activity but decreases affinity for glutathionylated substrates</li><li>C->S at 80: Strongly impairs enzymatic activity</li><li>C->S at 153: Abolishes absorption at 320 nm and 420 nm suggesting the loss of 2Fe-2S-binding</li></ul>			binding	GO:0005488					1
Q9NS37	58487	<ul><li>D->A at 221: Significantly reduced binding to HCFC1</li><li>H->A at 222: Significantly reduced binding to HCFC1</li><li>Y->A at 224: Significantly reduced binding to HCFC1</li></ul>			binding	GO:0005488			<li>P51611</li><li>P51610</li>		1
Q9NS56	10210	<ul><li>K->R at 76: No effect on sumoylation</li><li>W->A at 131: Abrogates E3 ubiquitin-protein ligase activity</li><li>K->R at 301: No effect on sumoylation</li><li>K->R at 485: No effect on sumoylation</li><li>K->R at 560: Strongly reduces sumoylation</li><li>K->R at 921: No effect on sumoylation</li></ul>	sumoylation	GO:0016925					<li>Q8RSY1</li><li>Q2QCI9</li>		1
Q9NSA0	55867	<ul><li>N->Q at 39: No visible effect on N-glycosylation. Loss of N-glycosylation and of cell surface location; when associated with Q-56; Q-63 and Q-99</li><li>H->A at 47: Reduced cell surface expression and estrone sulfate transport. Reduced cell surface expression and estrone sulfate transport; when associated with A-52; A-83; A-305 and A-469</li><li>H->A at 52: Slightly reduced estrone sulfate transport. Reduced cell surface expression and estrone sulfate transport; when associated with A-47; A-83; A-305 and A-469</li><li>N->Q at 56: No visible effect on N-glycosylation. Loss of N-glycosylation and of cell surface expression; when associated with Q-39; Q-63 and Q-99</li><li>N->Q at 63: No visible effect on N-glycosylation. Loss of N-glycosylation and of cell surface expression; when associated with Q-39; Q-56 and Q-99</li><li>H->A at 83: Reduced cell surface expression and estrone sulfate transport; when associated with A-47; A-52; A-305 and A-469</li><li>N->Q at 99: No visible effect on N-glycosylation. Loss of N-glycosylation and of cell surface expression; when associated with Q-39; Q-56 and Q-63</li><li>G->L,S,V at 241: Strongly reduced cell surface expression and estrone sulfate transport</li><li>H->A at 305: Reduced cell surface expression and estrone sulfate transport; when associated with A-47; A-52; A-83 and A-469</li><li>G->L,S,V at 400: Strongly reduced cell surface expression and estrone sulfate transport</li><li>H->A at 469: Slightly reduced estrone sulfate transport. Reduced cell surface expression and estrone sulfate transport; when associated with A-47; A-52; A-83 and A-305</li></ul>	sulfate transport	GO:0008272			cell surface	GO:0009928,GO:0009986			1
Q9NT62	64422	<ul><li>C->S at 264: Instead of the formation of an intermediate complex with a thiol ester bond between ATG3 (E2-like enzyme) and GABARAPL1/APG8L (substrate), a stable complex with an O-ester bond is formed</li></ul>			E2	GO:0004840			<li>Q5ABQ7</li><li>Q755K1</li><li>Q5RF21</li><li>P40344</li><li>Q6CL19</li><li>Q51LD2</li><li>P60518</li><li>Q9H0R8</li><li>Q9NT62</li><li>Q8HYB6</li><li>Q5K9X6</li><li>Q6C4Q9</li><li>Q6BSC4</li><li>Q6FQJ2</li>		1
Q9NTG7	23410	<ul><li>R->G,Q at 7: Suppresses targeting to mitochondrion; when associated with G-13 or Q-13</li><li>R->G,Q at 13: Suppresses targeting to mitochondrion; when associated with G-7 or Q-7</li><li>R->G,Q at 17: Reduces targeting to mitochondrion; when associated with G-21 or Q-21</li><li>R->G,Q at 21: Reduces targeting to mitochondrion; when associated with G-17 or Q-17</li><li>RR->GG at 99-100: Abolishes processing by MPP (in vitro)</li><li>N->A at 229: Loss of function</li><li>H->Y at 248: Loss of function</li></ul>					mitochondrion	GO:0005739	<li>Q6WEB5</li><li>P10522</li><li>P37301</li><li>P27573</li><li>P06907</li><li>P29677</li><li>P25189</li><li>P20938</li>		1
Q9NTK5	29789	<ul><li>F->A at 127: Loss of ATP-binding</li><li>N->A at 230: Loss of ATP-binding</li><li>LSE->KSD at 231-233: Retention of ATP-binding specificity</li></ul>			ATP-binding	GO:0005524					1
Q9NUD9	55650	<ul><li>W->L at 66: Loss of function</li><li>D->A at 67: Loss of function</li><li>PP->TA at 293-294: N-glycosylated due to the creation of an acceptor site for N-glycosylation</li><li>Q->A at 308: Induces a reduces enzyme activity</li><li>W->L at 312: Loss of function</li></ul>									1
Q9NUT2	11194	<ul><li>GK->AR at 512-513: Renders the protein instable</li></ul>									1
Q9NUW8	55775	<ul><li>H->A at 263: Loss of activity</li><li>K->A at 265: Abolishes hydrolysis of the covalent intermediate between the active site nucleophile and DNA</li><li>K->S at 265: Reduces the activity to nearly undetectable levels</li><li>N->A at 283: No effect</li><li>Q->A at 294: Slightly reduced hydrolysis of the covalent intermediate between the active site nucleophile and DNA</li><li>H->A at 493: 3000-fold reduction in activity; abolishes hydrolysis of the covalent intermediate between the active site nucleophile and DNA</li><li>H->N at 493: 15000-fold reduction in activity</li><li>K->A at 495: Abolishes hydrolysis of the covalent intermediate between the active site nucleophile and DNA</li><li>K->S at 495: 125-fold reduction in activity</li><li>N->A at 516: Reduced hydrolysis of the covalent intermediate between the active site nucleophile and DNA</li><li>E->A at 538: Abolishes hydrolysis of the covalent intermediate between the active site nucleophile and DNA</li></ul>									1
Q9NV58	25897	<ul><li>C->S at 132: Abolishes interaction with VCP and E3 ligase activity toward mutant SOD1; when associated with S-135</li><li>C->S at 135: Abolishes interaction with VCP and E3 ligase activity toward mutant SOD1; when associated with S-132</li></ul>			ligase activity	GO:0016874			<li>Q9SQL5</li><li>P00445</li><li>P00443</li><li>P00442</li><li>Q8HXQ1</li><li>P00441</li><li>Q01853</li><li>Q8HXQ0</li><li>Q8HXQ3</li><li>Q8HXQ2</li><li>Q8HXQ4</li><li>Q8HXP9</li><li>Q711T9</li><li>Q5FB29</li><li>Q751L8</li><li>P33431</li><li>P80566</li><li>Q96VL0</li><li>P55072</li><li>Q6CPE2</li><li>P09670</li><li>Q8HXP8</li><li>P42660</li><li>Q8J0N3</li><li>Q8J0N2</li><li>Q6T3B0</li><li>P60052</li><li>Q52RN5</li><li>Q9C0N4</li><li>O46412</li><li>P54774</li><li>Q6FWL5</li><li>Q7M1R5</li><li>O42724</li><li>Q8WNN6</li><li>P68638</li><li>P68639</li><li>P03974</li><li>P09212</li><li>P04178</li><li>P93258</li><li>O94178</li><li>Q42684</li><li>Q6C662</li><li>O59924</li><li>P46462</li>		1
Q9NVJ2	55207	<ul><li>L->A at 2: Diffuse cytoplasmic distribution and loss of localization to lysosomes. No effect on acetylation</li><li>L->F at 2: No effect on localization and acetylation</li><li>ISRLLDWF->ASRAL at 5-12: Diffuse cytoplasmic distribution and loss of localization to lysosomes. No effect on acetylation</li><li>T->N at 34: Preferentially binds GDP. Alters chromosome segregation</li><li>Missing at 49-58: Alters chromosome segregation</li><li>W->R at 70: Preferentially binds GTP</li><li>Missing at 74-85: Alters chromosome segregation</li><li>Q->L at 75: Prevents GTP hydrolysis. No effect on localization. Alters lysosomes cellular distribution and motility</li><li>N->I at 130: Loss of GTP/GDP-binding. Affects chromosome segregation</li></ul>	<li>GTP hydrolysis</li><li>chromosome segregation</li><li>localization</li>	<li>GO:0006184</li><li>GO:0007059</li><li>GO:0051179</li>	GDP-binding	GO:0019003	lysosomes	GO:0005764			1
Q9NVN8	54552	<ul><li>KK->AA at 9-10: Loss of nucleolar localization; when associated with 34-A-A-35. Loss of nuclear location; when associated with 19-A-A-20</li><li>KK->AA at 19-20: Loss of nuclear location; when associated with 9-A-A-10. Loss of nuclear location; when associated with 34-A-A-35</li><li>KK->AA at 34-35: Loss of nucleolar localization; when associated with 9-A-A-10. Loss of nuclear location; when associated with 19-A-A-20</li><li>RDP->AAA at 145-147: Loss of GTP binding. Loss of nucleolar localization. No effect on nuclear localization</li><li>PG->AA at 309-310: Loss of nucleolar localization. No effect on nuclear localization</li></ul>	localization	GO:0051179	GTP binding	GO:0005525					1
Q9NW38	55120	<ul><li>C->A at 307: Abolishes ubiquitin ligase activity</li><li>C->A at 310: Abolishes ubiquitin ligase activity</li></ul>			ligase activity	GO:0016874			<li>P69326</li><li>P08565</li><li>P69322</li><li>P69323</li><li>P69324</li><li>P69325</li><li>P68196</li><li>O46543</li><li>P68197</li><li>Q05550</li><li>P68198</li><li>P68199</li><li>P19848</li><li>P42739</li><li>P68195</li><li>Q867C2</li><li>P62991</li><li>P62990</li><li>P61863</li><li>P61864</li><li>P61862</li><li>Q867C4</li><li>Q867C3</li><li>P23398</li><li>P68204</li><li>P84589</li><li>Q865C5</li><li>P42740</li><li>P68201</li><li>Q8MKD1</li><li>P14792</li><li>P63049</li><li>P0C072</li><li>P63051</li><li>P69308</li><li>P69309</li><li>P20685</li><li>P15174</li><li>P62976</li><li>P62977</li><li>P62974</li><li>P62975</li><li>P62972</li><li>P13117</li><li>P14624</li><li>P62973</li><li>P46574</li><li>P69310</li><li>P69313</li><li>P69314</li><li>P69311</li><li>P08618</li><li>P69312</li><li>P69317</li><li>P69318</li><li>P69315</li><li>P0C014</li><li>P69316</li><li>P59263</li><li>P69319</li><li>P49634</li><li>P49635</li><li>Q9Y848</li><li>P22589</li><li>P62988</li><li>P62989</li><li>P69321</li><li>P23324</li><li>P69320</li><li>P59669</li>		1
Q9NWB1	54715	<ul><li>H->A at 120: Reduces RNA-binding affinity 160-fold</li><li>F->A,I,R at 126: Reduces RNA-binding affinity 1500-fold</li><li>F->H,W at 126: Reduces RNA-binding affinity 15-fold</li><li>F->Y at 126: No effect on RNA-binding</li><li>F->A at 158: Reduces RNA-binding affinity 700-fold</li><li>F->A at 160: Reduces RNA-binding affinity 30'000-fold</li></ul>			RNA-binding	GO:0003723					1
Q9NWB7	55081	<ul><li>K->D at 409: Impairs the interaction with HIP1</li></ul>							<li>O00291</li><li>P06775</li>		1
Q9NWM0	54498	<ul><li>C->R at 320: No change in enzymatic activity</li></ul>									1
Q9NWQ8	55824	<ul><li>Y->F at 105: No effect on interaction with FYN or CSK</li><li>Y->F at 163: No effect on interaction with FYN or CSK</li><li>Y->F at 181: No effect on interaction with FYN or CSK</li><li>Y->F at 227: No effect on interaction with FYN or CSK</li><li>Y->F at 299: No effect on interaction with FYN or CSK</li><li>Y->F at 317: No effect on interaction with FYN. Abolishes interaction with CSK</li><li>Y->F at 341: No effect on interaction with FYN or CSK</li><li>Y->F at 359: No effect on interaction with FYN or CSK</li><li>Y->F at 387: No effect on interaction with FYN or CSK</li><li>Y->F at 417: No effect on interaction with FYN or CSK</li></ul>							<li>Q05876</li><li>P41239</li><li>Q0VBZ0</li><li>P41240</li><li>P06241</li><li>P27446</li>		1
Q9NWT6	55662	<ul><li>H->A at 199: Prevents suppression of HIF CAD activity</li><li>D->A at 201: Prevents suppression of HIF CAD activity</li></ul>									1
Q9NWW0	54985	<ul><li>DHPY->AAPA at 76-79: Loss of interaction with HCFC1</li><li>LRL->ARA at 117-119: Reduces nuclear export</li></ul>	nuclear export	GO:0051168					<li>P51611</li><li>P51610</li>		1
Q9NWW6	54981	<ul><li>K->A at 16: Loss of activity</li><li>D->A at 36: Loss of activity</li><li>D->A at 56: Loss of activity</li><li>E->A at 98: Loss of activity</li><li>D->A at 138: Almost no effect</li></ul>									1
Q9NWZ3	51135	<ul><li>K->A at 213: Loss of kinase activity</li></ul>			kinase activity	GO:0016301					1
Q9NX46	54936	<ul><li>E->A,Q at 41: Significant loss of activity</li><li>DD->NN at 77-78: Complete loss of activity</li><li>D->N at 77: Complete loss of activity</li><li>S->A at 148: Complete loss of activity</li><li>Y->A at 149: Significant loss of activity</li><li>N->A at 151: Partial loss of activity</li><li>H->Q at 182: Complete loss of activity</li><li>EE->QQ at 238-239: Slight reduction in activity</li><li>EE->QQ at 261-262: Slight reduction in activity</li><li>D->E at 314: Complete loss of activity</li><li>D->N at 314: Significant loss of activity</li><li>T->A at 317: Complete loss of activity</li><li>T->S at 317: Partial loss of activity</li></ul>									1
Q9NX52	54933	<ul><li>W->A at 121: Reduces protease activity</li><li>R->A at 122: Abolishes protease activity</li><li>N->A at 139: Reduces protease activity</li><li>G->A at 185: Abolishes protease activity</li><li>S->A,G at 187: Abolishes protease activity</li><li>H->A at 250: Abolishes protease activity</li></ul>							<li>P19028</li><li>Q9QBZ5</li><li>P24107</li><li>Q9QBZ1</li><li>Q79666</li><li>P15833</li><li>P03362</li><li>P18042</li><li>Q8AII1</li><li>P03363</li><li>P04024</li><li>P04023</li><li>P10978</li><li>O93215</li><li>P26810</li><li>Q1A249</li><li>P03356</li><li>P03355</li><li>O41798</li><li>P20892</li><li>Q9Y6I0</li><li>P10210</li><li>Q9QBY3</li><li>P03353</li><li>P16901</li><li>Q74120</li><li>Q09SZ9</li><li>Q89928</li><li>Q73368</li><li>P84454</li><li>Q9WC63</li><li>P20825</li><li>Q9IDV9</li><li>P0C211</li><li>P0C210</li><li>P51518</li><li>Q4U0X6</li><li>P12451</li><li>P07570</li><li>P28936</li><li>O89940</li><li>P24740</li><li>P26809</li><li>P26808</li><li>Q0R5R3</li><li>Q0R5R2</li><li>P18802</li><li>P10394</li><li>P19561</li><li>P16423</li><li>P63119</li><li>P19560</li><li>Q75002</li><li>P04589</li><li>P04587</li><li>P04588</li><li>Q9QSR3</li><li>O91080</li><li>P16046</li><li>P17757</li><li>P12497</li><li>P12499</li><li>P12498</li><li>P03311</li><li>P20875</li><li>P20876</li><li>P10273</li><li>Q9WC54</li><li>P10272</li><li>P10271</li><li>P10270</li><li>P19199</li><li>P05962</li><li>P18096</li><li>P10265</li><li>P04584</li><li>P11227</li><li>P04585</li><li>Q76634</li><li>Q8I7P9</li><li>Q9Q720</li><li>P14078</li><li>P31822</li><li>P11365</li><li>P35963</li><li>P14074</li><li>P05959</li><li>P63131</li><li>P04323</li><li>P10274</li><li>P21407</li><li>O89290</li><li>P35956</li><li>P05960</li><li>P05961</li><li>Q1A267</li><li>P63122</li><li>P63123</li><li>P63124</li><li>P63125</li><li>P63120</li><li>P63121</li><li>P03366</li><li>P03367</li><li>P03369</li><li>P63127</li><li>P63128</li><li>P63129</li><li>Q77373</li><li>P03370</li><li>P27502</li><li>P21414</li>		1
Q9NXH3	54866	<ul><li>KK->EE at 21-22: Reduces inhibitory activity by 57%</li><li>W->A at 25: Reduces inhibitory activity by 13%</li><li>T->E at 58: Reduces inhibitory activity by 16%. Reduces phosphorylation</li></ul>	phosphorylation	GO:0016310							1
Q9NY25	23601	<ul><li>K->I at 16: Abolishes interaction with TYROBP</li></ul>							<li>Q95J79</li><li>Q9TU45</li><li>Q8WNQ8</li><li>O43914</li>		1
Q9NY37	51802	<ul><li>A->C at 443: Slightly activates the channel</li><li>A->F,T at 443: Activates the channel</li></ul>									1
Q9NY46	6328	<ul><li>Y->A at 1970: Abolishes interaction with NEDD4L</li></ul>							<li>Q5RBF2</li><li>Q96PU5</li>		1
Q9NYG5	100131844	<ul><li>C->S at 23: Greatly reduces autoubiquitination activity; in isoform 1</li><li>C->S at 26: Greatly reduces autoubiquitination activity; in isoform 1</li><li>C->S at 34: Slightly reduces autoubiquitination activity; in isoform 1</li><li>C->S at 37: Slightly reduces autoubiquitination activity; in isoform 1</li><li>C->S at 44: Slightly reduces autoubiquitination activity; in isoform 1</li><li>C->S at 51: Greatly reduces autoubiquitination activity; in isoform 1</li><li>H->S at 53: Greatly reduces autoubiquitination activity; in isoform 1</li><li>H->S at 56: Greatly reduces autoubiquitination activity; in isoform 1</li><li>H->S at 58: Slightly reduces autoubiquitination activity; in isoform 1</li><li>C->S at 59: Greatly reduces autoubiquitination activity; in isoform 1</li><li>C->S at 73: Greatly reduces autoubiquitination activity; in isoform 1</li><li>C->S at 76: Greatly reduces autoubiquitination activity; in isoform 1</li></ul>									1
Q9NYL2	51776	<ul><li>K->M at 45: Loss of kinase activity</li><li>T->A at 161: Loss of autophosphorylation activity</li><li>T->A at 162: Slight loss of autophosphorylation activity</li><li>S->A at 165: Loss of autophosphorylation activity</li></ul>	autophosphorylation	GO:0046777	kinase activity	GO:0016301					1
Q9NYP9	54069	<ul><li>C->A at 85: Abolishes location at the centromere</li><li>C->A at 88: Abolishes location at the centromere</li><li>C->A at 134: No effect</li><li>C->A at 141: Abolishes location at the centromere</li><li>C->A at 144: Abolishes location at the centromere</li></ul>									1
Q9NYS0	28512	<ul><li>T->A at 38: Loss of function</li></ul>									1
Q9NYU2	56886	<ul><li>Missing at 1452-1457: Inactive</li><li>D->A at 1452: Inactive</li><li>Q->A at 1453: 4% active</li><li>D->A at 1454: Inactive</li><li>L->A at 1455: 2% active</li><li>P->A at 1456: 41% active</li><li>N->A at 1457: 7% active</li></ul>									1
Q9NZ20	50487	<ul><li>N->S at 167: Loss of glycosylation</li><li>H->Q at 184: Loss of PGE2 synthesis</li><li>N->S at 280: Loss of glycosylation</li></ul>									1
Q9NZ42	55851	<ul><li>E->S at 10: Induces a N-linked glycosylation on N-8</li><li>A->N at 46: No effect</li><li>S->N at 93: Induces a N-linked glycosylation</li></ul>	N-linked glycosylation	GO:0006487							1
Q9NZ45	55847	<ul><li>C->S at 72: Abolishes absorption in the 300-500 nm range</li><li>C->S at 74: Abolishes absorption in the 300-500 nm range</li><li>C->S at 83: Abolishes absorption in the 300-500 nm range</li><li>D->N at 84: Does not affect absorption in the 300-500 nm range</li><li>H->C at 87: Affects absorption in the 300-500 nm range but it is not reduced. Increased stability of the 2Fe-2S cluster at low pH</li><li>H->Q at 87: Abolishes absorption in the 300-500 nm range</li></ul>									1
Q9NZ52	23163	<ul><li>N->A at 194: Loss of interaction with ARF1 and Golgi localization</li><li>S->P at 199: Loss of interaction with ARF1 and Golgi localization</li><li>T->P at 217: Loss of interaction with ARF1 and Golgi localization</li><li>L->P at 247: Loss of UBC-binding and ubiquitination</li><li>K->M at 258: No effect. Confers an affinity to RABEP1 identical to GGA1; when associated with N-283</li><li>L->S at 262: Loss of UBC-binding and ubiquitination</li><li>L->A at 276: Loss of UBC-binding and ubiquitination</li><li>L->S at 276: Loss of UBC-binding and ubiquitination</li><li>L->R at 280: Loss of UBC-binding and ubiquitination</li><li>S->N at 283: Can bind RABEP1. Confers an affinity to RABEP1 identical to GGA1; when associated with M-258</li><li>D->G at 284: Loss of UBC-binding and ubiquitination</li><li>Y->H at 293: Loss of UBC-binding and ubiquitination</li><li>DEELL->AAAAA at 391-395: Increased binding to IGF2R</li></ul>	localization	GO:0051179	binding	GO:0005488			<li>Q8L7G0</li><li>P84080</li><li>P22274</li><li>P11076</li><li>Q06336</li><li>O23778</li><li>Q5UQC9</li><li>Q867C2</li><li>P61209</li><li>Q75A26</li><li>P84077</li><li>Q4R5P2</li><li>Q867C4</li><li>Q867C3</li><li>P36397</li><li>Q15276</li><li>P27949</li><li>Q9UJY5</li><li>Q94650</li><li>P11717</li><li>P25869</li><li>P49076</li><li>P61210</li><li>O48649</li><li>P62988</li><li>P08169</li><li>Q96361</li><li>Q25761</li><li>P51821</li><li>P51822</li>		1
Q9NZ53	50512	<ul><li>Y->F at 97: Remains sulfated. Not sulfated and reduced rolling of Jurkat T-cells by more than 50%; when associated with F-118. The rolling of Jurkat T-cells is reduced by more than 80%; when associated with F-118 and A-124</li><li>Y->F at 118: Remains sulfated. Not sulfated and reduced rolling of Jurkat T-cells by more than 50%; when associated with F-97. The rolling of Jurkat T-cells is reduced by more than 80%; when associated with F-97 and A-124</li><li>T->A at 124: Not sialylated O-linked</li></ul>									1
Q9NZC7	51741	<ul><li>K->T at 28: No effect on interaction with TP53. Abolishes interaction with MAPK8; when associated with V-29</li><li>D->V at 29: No effect on interaction with TP53. Abolishes interaction with MAPK8; when associated with T-28</li><li>Y->F at 33: Loss of phosphorylation</li><li>Y->R at 33: Abolishes interaction with TP53, TP73, MAPK8 and ERBB4. Partial loss of interaction with TFAP2C. Loss of phosphorylation. Loss of the proaptotic activity</li><li>WEHP->FEHA at 44-47: Abolishes interaction with LITAF</li><li>Y->R at 61: No effect on interaction with TP73</li><li>YLDP->ALDA at 85-88: No effect on interaction with LITAF</li></ul>	phosphorylation	GO:0016310					<li>Q9TUB2</li><li>Q8QGW7</li><li>Q9XSK8</li><li>P56423</li><li>P56424</li><li>Q15303</li><li>O12946</li><li>P25035</li><li>O36006</li><li>Q64662</li><li>O57538</li><li>P10360</li><li>P61260</li><li>Q9W679</li><li>Q9W678</li><li>P13481</li><li>Q9TTA1</li><li>Q95330</li><li>O93379</li><li>P41685</li><li>Q8SPZ3</li><li>P79820</li><li>Q92143</li><li>P04637</li><li>Q29537</li><li>Q29480</li><li>O09185</li><li>Q99732</li><li>Q00366</li><li>P79892</li><li>O15350</li><li>P51664</li><li>Q9WUR6</li><li>P67939</li><li>Q92754</li><li>P45983</li><li>P67938</li>		1
Q9NZD2	51228	<ul><li>I->N at 45: 18% decrease in activity</li><li>D->V at 48: Significant inactivation; 15% residual activity</li><li>N->I at 52: Significant inactivation; 15% residual activity</li><li>K->I at 55: No loss of activity; 90-97% residual activity</li><li>W->A at 96: Almost complete inactivation; 1-3% residual activity</li><li>W->F at 96: Partial inactivation; 63% residual activity</li><li>F->S at 103: About 25% decrease in activity</li><li>L->R at 136: Significant inactivation; 5% residual activity</li><li>H->L at 140: Almost complete inactivation; 1-3% residual activity</li><li>F->S at 148: About 50% decrease in activity</li><li>L->R at 165: 46% decrease in activity</li><li>F->S at 183: No loss of activity; 90% residual activity</li><li>Y->L at 207: No loss of activity; 90-97% residual activity</li></ul>									1
Q9NZD8	51324	<ul><li>S->A at 109: Abolishes interaction with CD4</li></ul>							<li>Q08339</li><li>P05542</li><li>Q29037</li><li>P01730</li><li>P79185</li><li>P16004</li><li>Q08340</li><li>P16003</li><li>P79184</li><li>P33705</li><li>Q9XS78</li><li>P46630</li><li>Q08338</li><li>Q08336</li>		1
Q9NZI8	10642	<ul><li>K->E at 213: Decreases RNA-binding affinity, decreases cytoplasmic granular formation and increases nuclear localization; when associated with E-294 and E-423</li><li>K->E at 294: Decreases RNA-binding affinity, decreases cytoplasmic granular formation and increases nuclear localization; when associated with E-213 and E-423</li><li>L->A at 318: Diminishes export activity</li><li>L->A at 320: Diminishes export activity</li><li>K->E at 423: Decreases RNA-binding affinity, decreases cytoplasmic granular formation and increases nuclear localization; when associated with E-294 and E-213</li><li>E->A at 485: Loss of export activity</li><li>V->A at 486: Loss of export activity</li><li>L->A at 488: Loss of export activity</li><li>I->A at 492: Loss of export activity</li><li>K->E at 505: Decreases RNA-binding affinity, loss of cytoplasmic granular formation, increases nuclear localization</li></ul>	localization	GO:0051179	RNA-binding	GO:0003723					1
Q9NZJ0	51514	<ul><li>R->A at 246: Blocks association with DDB1</li></ul>							<li>Q16531</li><li>Q6QNU4</li><li>Q6E7D1</li><li>P33194</li>		1
Q9NZM1	26509	<ul><li>NPF->SPL at 238-240: Reduces interaction with EHD2</li></ul>							<li>Q08558</li><li>Q9NZN4</li><li>Q9NZN3</li>		1
Q9NZN9	23746	<ul><li>R->W at 53: No interaction with NUB1</li><li>M->T at 79: No interaction with NUB1</li><li>V->I at 96: No interaction with NUB1</li><li>A->P at 197: No significant effect on interaction with NUB1</li><li>I->N at 206: No significant effect on interaction with NUB1</li><li>G->S at 262: No interaction with NUB1</li><li>R->L at 302: No interaction with NUB1</li></ul>							<li>Q8MJ87</li><li>P32860</li><li>Q9Y5A7</li>		1
Q9NZP8	51279	<ul><li>S->A at 436: Unable to cleave HP</li></ul>									1
Q9NZV8	3751	<ul><li>PTPP->ATAA at 601-604: Abolishes interaction with FLNC</li></ul>							Q14315		1
Q9P032	29078	<ul><li>K->A at 73: Reduces interaction with calmodulin. Does not promote MMP-9 secretion</li></ul>	secretion	GO:0046903					<li>Q40302</li><li>Q8STF0</li><li>P04353</li><li>P41040</li><li>P04352</li><li>P14780</li><li>P41245</li><li>P41246</li><li>O18733</li><li>Q9GRJ1</li><li>P61860</li><li>P02594</li><li>P02595</li><li>P61861</li><li>P48976</li><li>O82018</li><li>P50282</li><li>P93171</li><li>P62184</li><li>P62144</li><li>P62145</li><li>Q5RAD2</li><li>P07463</li><li>P24044</li><li>P11121</li><li>P62149</li><li>P06787</li><li>O02367</li><li>Q6IT78</li><li>P05935</li><li>P05933</li><li>O16305</li><li>Q6PI52</li><li>P05934</li><li>Q6YNX6</li><li>Q7Y052</li><li>Q95NR9</li><li>P11118</li><li>P62157</li><li>P62156</li><li>P21251</li><li>P62155</li><li>Q5EHV7</li><li>P62154</li><li>P62152</li><li>P62151</li><li>Q7T3T2</li><li>P69097</li><li>P69098</li><li>P60206</li><li>Q9U6D3</li><li>Q9HFY6</li><li>P60205</li><li>P62158</li><li>P60204</li><li>O96102</li><li>P62201</li><li>P18061</li><li>P11120</li><li>Q8X187</li><li>P93087</li><li>O60041</li><li>Q05055</li><li>P62204</li><li>P62160</li><li>P62203</li><li>P62202</li><li>P61859</li><li>P17928</li><li>P15094</li><li>Q95NI4</li><li>Q9UWF0</li><li>P62162</li><li>P02598</li><li>P62161</li><li>P02599</li><li>Q71UH6</li><li>Q71UH5</li><li>P52176</li><li>O97341</li><li>P04464</li><li>P27165</li><li>Q39752</li><li>P84339</li><li>P27166</li><li>P23286</li><li>O94739</li><li>P27161</li><li>P41041</li><li>Q6R520</li>		1
Q9P0K1	53616	<ul><li>S->A at 834: Abolishes interactions with YWHAB and YWHAZ; when associated with A-857</li><li>S->A at 857: Abolishes interactions with YWHAB and YWHAZ; when associated with A-834</li></ul>							<li>P63103</li><li>P29361</li><li>Q4R572</li><li>Q5ZKC9</li><li>P68251</li><li>P68250</li><li>Q5R651</li><li>Q5ZLQ6</li><li>P31946</li><li>P63104</li>		1
Q9P0L2	4139	<ul><li>T->A at 215: Prevents phosphorylation and activation by STK11 complex</li><li>T->E at 215: Constitutively active</li></ul>	phosphorylation	GO:0016310					<li>Q15831</li><li>Q0GGW5</li>		1
Q9P0R6	51527	<ul><li>L->P at 130: Loss of interaction with GSK3B</li></ul>							<li>Q5YJC2</li><li>P49841</li>		1
Q9P0U3	29843	<ul><li>D->A at 441: No effect on SUMO2 processing and SUMO2 deconjugating activities</li><li>W->A at 465: Impairs SUMO2 processing and SUMO2 deconjugating activities</li><li>D->A at 468: Slightly impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity</li><li>F->A at 496: Impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity</li><li>R->A at 511: Impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity</li><li>W->A at 512: Impairs SUMO2 processing and SUMO2 deconjugating activities</li><li>H->A at 529: Impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity</li><li>V->A at 532: No effect on SUMO2 processing and SUMO2 deconjugating activities</li><li>H->A at 533: Abolishes SUMO2 processing and SUMO2 deconjugating activities</li><li>W->A at 534: Abolishes SUMO2 processing and SUMO2 deconjugating activities</li><li>D->A at 550: Abolishes SUMO2 processing and SUMO2 deconjugating activities</li><li>Q->A at 597: Abolishes SUMO2 processing and SUMO2 deconjugating activities</li><li>C->A,S at 603: Abolishes SUMO2 processing and SUMO2 deconjugating activities</li><li>C->S at 603: Exclusively nuclear</li></ul>							<li>Q6LDZ8</li><li>P61958</li><li>P61956</li><li>P61955</li>		1
Q9P0U4	30827	<ul><li>C->A at 169: Complete loss of DNA binding activity. No effect on localization in nuclear speckles</li><li>C->A at 208: Complete loss of DNA binding activity. No effect on localization in nuclear speckles</li></ul>	localization	GO:0051179	DNA binding	GO:0003677	nuclear speckles	GO:0016607			1
Q9P0V3	23677	<ul><li>W->A at 92: Loss of function. Loss of targeting to the clathrin-coated pits and vesicles. Loss of interaction with DNM2. No effect on localization to the plasma membrane</li></ul>	localization	GO:0051179			<li>coated pits</li><li>plasma membrane</li>	<li>GO:0005905</li><li>GO:0005886</li>	P50570		1
Q9P0W2	10362	<ul><li>K->I at 116: Loss of DNA binding activity of the BHC histone deacetylase complex</li></ul>			DNA binding	GO:0003677			O22446		1
Q9P126	51266	<ul><li>K->A at 150: Substantial reduction in rhodocytin binding</li><li>K->A at 171: Significant reduction in rhodocytin binding</li><li>E->A at 184: Significant reduction in rhodocytin binding</li><li>E->A at 187: Significant reduction in rhodocytin binding</li><li>D->A at 188: Significant reduction in rhodocytin binding</li><li>K->A at 190: Significant reduction in rhodocytin binding</li><li>N->A at 192: Significant reduction in rhodocytin binding</li></ul>			binding	GO:0005488					1
Q9P212	51196	<ul><li>H->L at 1452: Loss of the phospholipase C enzymatic activity. Still activates HRAS and the MAP kinase pathway</li><li>Q->E at 2140: Increases 2.8-fold the affinity for HRAS</li><li>Q->E at 2148: Decreases 17.5-fold the affinity for HRAS</li><li>Q->K at 2148: Increases 1.4-fold the affinity for HRAS</li><li>R->L at 2150: Abolishes interaction with HRAS</li><li>K->L at 2171: No effect on HRAS-binding</li><li>Y->L at 2174: Reduces HRAS-binding</li></ul>			binding	GO:0005488			<li>Q60529</li><li>P01112</li>		1
Q9P246	57620	<ul><li>D->A at 80: No effect on inhibitory activity; when associated with A-91</li><li>E->A at 91: No effect on inhibitory activity; when associated with A-80</li></ul>									1
Q9UBD6	51458	<ul><li>F->L at 74: Reduction of ammonia transport</li><li>V->I at 137: Reduction of ammonia transport</li><li>D->N at 177: Loss of function</li><li>F->V at 235: Reduction of ammonia transport</li></ul>	transport	GO:0006810							1
Q9UBG0	9902	<ul><li>N->D at 472: Reduced sugar-binding activity</li><li>Y->A at 1452: No alteration of distribution and trafficking</li><li>E->A at 1464: Increased cell surface distribution</li><li>LV->AA at 1468-1469: Reduction of endocytotic activity; distribution almost restricted to the cell surface</li></ul>			sugar-binding	GO:0005529	cell surface	GO:0009928,GO:0009986			1
Q9UBK5	10870	<ul><li>D->A at 57: Abolishes stable interaction with NKG2D</li></ul>							<li>P26718</li><li>P61252</li><li>Q9MZ37</li><li>Q9MZJ7</li>		1
Q9UBK9	8409	<ul><li>L->P at 50: Causes dislocation from the centrosome; when associated with L-59</li><li>L->P at 59: Causes dislocation from the centrosome; when associated with L-50</li></ul>					centrosome	GO:0005813			1
Q9UBN7	10013	<ul><li>H->A at 216: Reduces histone deacetylase activity</li><li>H->A at 611: Reduces histone deacetylase activity</li></ul>							O22446		1
Q9UBP5	23493	<ul><li>G->P at 54: Impairs transcriptional repression</li></ul>									1
Q9UBP9	51454	<ul><li>L->P at 176: Loss of dimerization; when associated with P-183</li><li>L->P at 183: Loss of dimerization; when associated with P-176</li></ul>									1
Q9UBQ0	51699	<ul><li>D->A at 8: Loss of protein phosphatase activity</li><li>N->A at 39: Loss of protein phosphatase activity</li><li>N->D at 39: No effect on protein phosphatase activity</li><li>D->A,N at 62: Loss of protein phosphatase activity</li><li>H->A at 86: Loss of protein phosphatase activity</li><li>H->A at 117: Loss of protein phosphatase activity</li></ul>							<li>Q5X1E5</li><li>Q7M7K5</li><li>Q7MAZ9</li><li>Q8XBL4</li><li>Q88A53</li><li>Q5P3T0</li><li>Q7MBF4</li><li>Q8Z3M9</li><li>Q5PC82</li><li>Q5ZRX9</li><li>Q821A6</li><li>Q87SK9</li><li>Q9JZ88</li><li>Q9CP21</li><li>Q82U82</li><li>Q9I5V3</li><li>Q5F8K9</li><li>Q63YC3</li><li>Q8Y395</li><li>Q6LV05</li><li>Q8ZLY4</li><li>Q6FA38</li><li>Q9PDL7</li><li>Q62EU1</li><li>Q9JUB2</li><li>Q5WT58</li><li>Q665U9</li><li>Q57JQ5</li><li>Q9KPC6</li><li>Q8P5D4</li><li>Q8CWL6</li><li>Q8PPG9</li><li>P06961</li><li>P45269</li><li>Q9L7A3</li><li>Q88QU2</li><li>Q6D160</li><li>Q8ZI64</li><li>Q60CQ4</li><li>Q87DS9</li><li>Q65Q41</li><li>Q5E2K7</li><li>Q8CXX6</li>		1
Q9UBS4	51726	<ul><li>H->Q at 53: Loss of HSPA5-binding, but no effect on interaction with denatured substrates</li><li>C->S at 169: Drastic loss of interaction with denatured substrates</li><li>C->S at 171: Drastic loss of interaction with denatured substrates</li><li>C->S at 193: Drastic loss of interaction with denatured substrates</li><li>C->S at 196: Drastic loss of interaction with denatured substrates</li></ul>			binding	GO:0005488			<li>Q90593</li><li>P07823</li><li>Q3S4T7</li><li>P11021</li><li>P34935</li><li>P16392</li>		1
Q9UBS8	9604	<ul><li>C->S at 220: Loss of interaction with UBE2E2 and of autoubiquitination</li></ul>							Q96LR5		1
Q9UBT6	51426	<ul><li>D->A at 198: Loss of DNA polymerase activity; when associated with A-199</li><li>E->A at 199: Loss of DNA polymerase activity; when associated with D-198</li></ul>							<li>Q9YUS3</li><li>O59610</li><li>Q9YUS2</li><li>P56689</li><li>P06538</li><li>Q69025</li><li>Q9HH84</li><li>P04495</li><li>P43139</li><li>Q56366</li><li>P77933</li><li>P03261</li><li>P19894</li><li>P52025</li><li>P03158</li><li>Q6S6P1</li><li>Q85428</li><li>P09252</li><li>O64235</li><li>P03198</li><li>P52367</li><li>P28859</li><li>P74918</li><li>P52342</li><li>O72539</li><li>P20311</li><li>O70736</li><li>P28857</li><li>P28858</li><li>P20509</li><li>Q9HH05</li><li>Q88469</li><li>P61875</li><li>P61876</li><li>O72540</li><li>Q05254</li><li>Q64751</li><li>P06950</li><li>P06856</li><li>P05664</li><li>Q83948</li><li>P05468</li><li>P08546</li><li>O71121</li><li>Q37882</li><li>P19822</li><li>P10479</li><li>Q58295</li><li>P87553</li><li>P30321</li><li>P30320</li><li>P10582</li><li>P21402</li><li>Q51334</li><li>O33845</li><li>P42489</li><li>P18131</li><li>O27276</li><li>P09804</li><li>P24907</li><li>P41712</li><li>Q84173</li><li>P48311</li><li>P33793</li><li>O57191</li><li>P04415</li><li>P03680</li><li>P00581</li><li>Q5UQR0</li><li>Q90162</li><li>P87503</li><li>Q37989</li><li>P04292</li><li>P30318</li><li>P04293</li><li>P30317</li><li>Q65946</li><li>Q38087</li><li>P07917</li><li>O29753</li><li>P07918</li><li>P30319</li><li>P06225</li><li>P27172</li><li>P30314</li><li>P09854</li>		1
Q9UBU8	10933	<ul><li>V->E at 208: Abolishes binding to MRFAP1</li><li>E->R at 234: No effect on MRFAP1 binding</li><li>Y->A at 251: No effect on MRFAP1 binding</li><li>N->C at 254: Reduces binding to MRFAP1</li></ul>			binding	GO:0005488					1
Q9UBU9	10482	<ul><li>ERE->AAA at 306-308: Decreases the export of mRNAs from the nucleus</li><li>W->A at 594: Suppresses FG-nucleoporin binding</li><li>D->R at 595: Suppresses FG-nucleoporin binding</li><li>F->A at 617: Suppresses FG-nucleoporin binding</li></ul>			binding	GO:0005488	nucleus	GO:0005634			1
Q9UBY8	2055	<ul><li>KK->RR at 283-284: Localizes to the Golgi complex</li></ul>					Golgi complex	GO:0005794			1
Q9UBZ9	51455	<ul><li>D->A at 570: Abolishes transferase activity; when associated with A-571</li><li>E->A at 571: Abolishes transferase activity; when associated with A-570</li></ul>			transferase activity	GO:0016740					1
Q9UDY8	10892	<ul><li>C->A at 464: Slight decrease in NF-kappa-B activation</li><li>E->A at 653: Abolishes binding to TRAF6</li><li>E->A at 806: Abolishes binding to TRAF6</li></ul>			binding	GO:0005488			Q9Y4K3		1
Q9UEE5	9263	<ul><li>K->A at 90: Loss of activity and of apoptotic function</li></ul>									1
Q9UER7	1616	<ul><li>K->A at 630: Abolishes sumoylation</li><li>K->A at 631: Abolishes sumoylation</li><li>S->A at 668: No translocation to the cytosol upon glucose deprivation</li><li>S->A at 671: No effect on cytosol translocation. upon glucose deprivation</li></ul>	sumoylation	GO:0016925			cytosol	GO:0005829			1
Q9UGI0	54764	<ul><li>C->A at 10: Abolishes the binding to ubiquitin chains but not the deubiquitinating activity; when associated with 14-LV-15; A-90; 94-LV-95; A-155 and 159-LV-160</li><li>TY->LV at 14-15: Abolishes the binding to ubiquitin chains but not the deubiquitinating activity; when associated with A-10; A-90; 94-LV-95; A-155 and 159-LV-160</li><li>C->A at 90: Abolishes the binding to ubiquitin chains but not the deubiquitinating activity; when associated with A-10; 14-LV-15; 94-LV-95; A-155 and 159-LV-160</li><li>TY->LV at 94-95: Abolishes the binding to ubiquitin chains but not the deubiquitinating activity; when associated with A-10; 14-LV-15; A-90; A-155 and 159-LV-160</li><li>C->A at 155: Abolishes the binding to ubiquitin chains but not the deubiquitinating activity; when associated with A-10; 14-LV-15; A-90; 94-LV-95 and 159-LV-160</li><li>TY->LV at 159-160: Abolishes the binding to ubiquitin chains but not the deubiquitinating activity; when associated with A-10; 14-LV-15; A-90; 94-LV-95; and A-155</li><li>C->S at 443: Abolishes the deubiquitinating activity but not the binding to ubiquitin chains</li></ul>			binding	GO:0005488			<li>P69326</li><li>P08565</li><li>P69322</li><li>P69323</li><li>P69324</li><li>P69325</li><li>P68196</li><li>O46543</li><li>P68197</li><li>Q05550</li><li>P68198</li><li>P68199</li><li>P19848</li><li>P19987</li><li>P42739</li><li>P68195</li><li>Q867C2</li><li>P62991</li><li>P62990</li><li>P61863</li><li>P61864</li><li>P61862</li><li>Q867C4</li><li>Q867C3</li><li>P23398</li><li>P68204</li><li>P84589</li><li>Q865C5</li><li>P42740</li><li>P68201</li><li>Q8MKD1</li><li>P14792</li><li>P63049</li><li>P0C072</li><li>P63051</li><li>P69308</li><li>P69309</li><li>P20685</li><li>P15174</li><li>P62976</li><li>P62977</li><li>P62974</li><li>P62975</li><li>P62972</li><li>P13117</li><li>P14624</li><li>P62973</li><li>P46574</li><li>P69310</li><li>P69313</li><li>P69314</li><li>P69311</li><li>P08618</li><li>P69312</li><li>P69317</li><li>P69318</li><li>P69315</li><li>P0C014</li><li>P69316</li><li>P59263</li><li>P69319</li><li>P49634</li><li>P49635</li><li>Q9Y848</li><li>P22589</li><li>P62988</li><li>P62989</li><li>P69321</li><li>P23324</li><li>P69320</li><li>P59669</li>		1
Q9UGK3	55620	<ul><li>Y->F at 22: Small decrease in tyrosine phosphorylation</li><li>Y->F at 250: Loss of tyrosine phosphorylation</li><li>Y->F at 310: Decrease in tyrosine phosphorylation</li><li>Y->F at 322: Decrease in tyrosine phosphorylation</li></ul>	phosphorylation	GO:0016310							1
Q9UGL1	10765	<ul><li>H->A at 335: Slightly impairs transcription repression ability</li><li>H->Y at 499: Abolishes enzymatic activity</li><li>H->A at 1200: Impairs transcription repression ability and interaction with HDAC4</li></ul>	transcription	GO:0006350					<li>P56524</li><li>P83038</li>		1
Q9UGP5	27343	<ul><li>K->A at 312: Reduces dRP lyase activity by over 90%</li><li>Y->A at 505: No effect on polymerase activity. Reduces terminal transferase activitites</li><li>F->G,R at 506: Strongly reduces polymerase and terminal transferase activitites</li></ul>			lyase activity	GO:0016829			<li>P09838</li><li>O57486</li><li>P06526</li><li>O02789</li><li>P42118</li><li>Q92089</li><li>P36195</li><li>P04053</li>		1
Q9UH65	23075	<ul><li>RR->EE at 223-224: Abolishes binding to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid and the localization to the loose actin filament arrays</li><li>R->C at 230: Reduced binding to phosphatidylinositol 3,4-bisphosphate and reduced association with actin filament</li><li>W->A at 297: Abolishes binding to plasma membrane</li><li>Missing at 526-585: Affects targeting to loose actin filament arrays</li></ul>	localization	GO:0051179	binding	GO:0005488	plasma membrane	GO:0005886	<li>Q92192</li><li>Q92193</li><li>P53499</li><li>P26183</li><li>P53498</li><li>O13419</li><li>Q9P4D1</li><li>P48465</li><li>P53455</li><li>Q39596</li><li>Q39758</li><li>P26182</li><li>P80709</li><li>Q9UVX4</li><li>O17320</li><li>P53689</li><li>P78711</li><li>P30161</li><li>P17128</li><li>P45521</li><li>P45520</li><li>P20904</li><li>P81085</li><li>Q6TCF2</li><li>Q99023</li><li>Q75D00</li><li>P51775</li><li>P10365</li><li>P60011</li><li>P60010</li><li>Q8SWN8</li><li>O16808</li><li>P02577</li><li>P10989</li><li>P68555</li><li>Q05214</li><li>Q8X119</li><li>O65316</li><li>O65315</li><li>O65314</li><li>P53491</li><li>P91754</li><li>P13363</li><li>P11426</li><li>O81221</li><li>Q11212</li><li>P50138</li><li>P53477</li><li>P53476</li><li>P60009</li><li>P53502</li><li>Q2U7A3</li><li>P53500</li><li>Q9UVZ8</li><li>P14235</li><li>O00937</li><li>Q9UVF3</li><li>Q24733</li><li>P90689</li><li>P24902</li><li>O74258</li>		1
Q9UHC3	9311	<ul><li>V->A at 528: No effect on interaction with LIN7B, MAGI1 and GOPC</li><li>T->A at 529: Loss of interaction with LIN7B, MAGI1</li><li>Q->A at 530: Loss of interaction with GOPC. No effect on interaction LIN7B and MAGI1</li><li>L->A at 531: Loss of interaction with LIN7B, MAGI1 and GOPC</li></ul>							<li>Q9HD26</li><li>Q96QZ7</li><li>Q9HAP6</li><li>Q5RD32</li>		1
Q9UHD2	29110	<ul><li>K->A at 38: Loss of TANK-mediated NF-kappa-B activation</li><li>S->A at 172: Loss of kinase activity</li><li>S->E at 172: Decreased kinase activity</li></ul>			kinase activity	GO:0016301			Q92844		1
Q9UHG2	27344	<ul><li>V->A at 235: Reduces inhibition of PCSK1</li><li>L->A at 236: Greatly reduces inhibition of PCSK1</li><li>G->A at 237: Reduces inhibition of PCSK1</li><li>L->A at 240: Reduces inhibition of PCSK1</li><li>R->A at 241: Reduces inhibition of PCSK1</li><li>V->A at 242: Reduces inhibition of PCSK1</li><li>K->A at 243: Abolishes inhibition of PCSK1</li><li>R->A at 244: Abolishes inhibition of PCSK1</li><li>L->A at 245: Reduces inhibition of PCSK1</li><li>E->A at 246: Reduces inhibition of PCSK1</li></ul>							<li>Q9GLR1</li><li>P29120</li>		1
Q9UHL9	9569	<ul><li>Missing at 898-959: Cytoplasmic localization</li></ul>	localization	GO:0051179							1
Q9UHR4	55971	<ul><li>K->E at 141: Loss ability to induce the formation of actin clusters; when associated with K-142; R-145 and K-146</li><li>K->E at 142: Loss ability to induce the formation of actin clusters; when associated with K-141; R-145 and K-146</li><li>R->E at 145: Loss ability to induce the formation of actin clusters; when associated with K-141; K-142 and K-146</li><li>K->E at 146: Loss ability to induce the formation of actin clusters; when associated with K-141; K-142 and R-145</li><li>Missing at 488-511: Loss ability to induce the formation of actin clusters; induce the formation of long filipodia</li></ul>							<li>Q92192</li><li>Q92193</li><li>P53499</li><li>P26183</li><li>P53498</li><li>O13419</li><li>Q9P4D1</li><li>P48465</li><li>P53455</li><li>Q39596</li><li>Q39758</li><li>P26182</li><li>P80709</li><li>Q9UVX4</li><li>O17320</li><li>P53689</li><li>P78711</li><li>P30161</li><li>P17128</li><li>P45521</li><li>P45520</li><li>P20904</li><li>P81085</li><li>Q6TCF2</li><li>Q99023</li><li>Q75D00</li><li>P51775</li><li>P10365</li><li>P60011</li><li>P60010</li><li>Q8SWN8</li><li>O16808</li><li>P02577</li><li>P10989</li><li>P68555</li><li>Q05214</li><li>Q8X119</li><li>O65316</li><li>O65315</li><li>O65314</li><li>P53491</li><li>P91754</li><li>P13363</li><li>P11426</li><li>O81221</li><li>Q11212</li><li>P50138</li><li>P53477</li><li>P53476</li><li>P60009</li><li>P53502</li><li>Q2U7A3</li><li>P53500</li><li>Q9UVZ8</li><li>P14235</li><li>O00937</li><li>Q9UVF3</li><li>Q24733</li><li>P90689</li><li>P24902</li><li>O74258</li>		1
Q9UHX3	30817	<ul><li>S->A at 518: Abolishes cleavage</li></ul>									1
Q9UIB8	8832	<ul><li>T->A at 55: Loss of dimerization</li><li>Y->A at 62: No effect</li><li>Y->D at 62: Loss of dimerization</li><li>T->A at 77: Loss of dimerization</li><li>H->A at 78: Loss of dimerization</li><li>D->A at 110: Loss of dimerization</li><li>N->A at 112: Loss of dimerization</li><li>T->A at 119: Loss of dimerization</li><li>Y->F at 279: Reduced tyrosine phosphorylation, reduced binding of SH2D1B and loss of binding of SH2D1A</li><li>Y->F at 316: Reduced tyrosine phosphorylation and reduced binding of SH2D1B. Loss of phosphorylation and loss of binding of SH2D1A and SH2D1B; when associated with F-279</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488			<li>O60880</li><li>O14796</li>		1
Q9UIK4	23604	<ul><li>K->A at 52: Loss of activity, apoptotic function and of autophosphorylation</li><li>Missing at 299-330: Loss of ca(2+)-calmodulin binding, increase in activity, loss of autophosphorylation</li><li>S->A at 299: No effect on Ca(2+)-calmodulin independent phosphorylation or apoptotic activity</li><li>S->A at 318: Loss of Ca(2+)-calmodulin independent phosphorylation, increase in apoptotic activity</li><li>S->D at 318: Abolishes apoptotic activity</li><li>S->A at 320: No effect on Ca(2+)-calmodulin independent phosphorylation or apoptotic activity</li><li>S->A at 323: No effect on Ca(2+)-calmodulin independent phosphorylation or apoptotic activity</li><li>T->A at 329: No effect on Ca(2+)-calmodulin independent phosphorylation or apoptotic activity</li></ul>	<li>phosphorylation</li><li>autophosphorylation</li>	<li>GO:0016310</li><li>GO:0046777</li>	binding	GO:0005488			<li>Q40302</li><li>Q8STF0</li><li>P04353</li><li>P41040</li><li>P04352</li><li>Q9GRJ1</li><li>P61860</li><li>P02594</li><li>P02595</li><li>P61861</li><li>P48976</li><li>O82018</li><li>P93171</li><li>P62184</li><li>P62144</li><li>P62145</li><li>Q5RAD2</li><li>P07463</li><li>P24044</li><li>P11121</li><li>P62149</li><li>P06787</li><li>O02367</li><li>Q6IT78</li><li>P05935</li><li>P05933</li><li>O16305</li><li>Q6PI52</li><li>P05934</li><li>Q6YNX6</li><li>Q7Y052</li><li>Q95NR9</li><li>P11118</li><li>P62157</li><li>P62156</li><li>P21251</li><li>P62155</li><li>Q5EHV7</li><li>P62154</li><li>P62152</li><li>P62151</li><li>Q7T3T2</li><li>P69097</li><li>P69098</li><li>P60206</li><li>Q9U6D3</li><li>Q9HFY6</li><li>P60205</li><li>P62158</li><li>P60204</li><li>O96102</li><li>P62201</li><li>P18061</li><li>P11120</li><li>Q8X187</li><li>P93087</li><li>O60041</li><li>Q05055</li><li>P62204</li><li>P62160</li><li>P62203</li><li>P62202</li><li>P61859</li><li>P17928</li><li>P15094</li><li>Q95NI4</li><li>Q9UWF0</li><li>P62162</li><li>P02598</li><li>P62161</li><li>P02599</li><li>Q71UH6</li><li>Q71UH5</li><li>O97341</li><li>P04464</li><li>P27165</li><li>Q39752</li><li>P84339</li><li>P27166</li><li>P23286</li><li>O94739</li><li>P27161</li><li>P41041</li><li>Q6R520</li>		1
Q9UIM3	63943	<ul><li>K->A at 287: Abolishes HSP90AB1 binding; when associated with A-291</li><li>R->A at 291: Abolishes HSP90AB1 binding; when associated with A-287</li></ul>			binding	GO:0005488			<li>P30947</li><li>Q04619</li><li>Q76LV1</li><li>P08238</li><li>Q9GKX8</li>		1
Q9UIS9	4152	<ul><li>R->A at 22: Abolishes binding to methylated DNA</li><li>R->A at 30: Strongly reduces binding to methylated DNA</li><li>D->A at 32: Strongly reduces binding to methylated DNA</li><li>Y->A at 34: Reduces binding to methylated DNA</li><li>R->A at 44: Abolishes binding to methylated DNA</li><li>S->A at 45: Slightly reduces binding to methylated DNA</li><li>Y->A at 52: No effect</li><li>F->A at 64: Disrupts tertiary structure and abolishes DNA binding</li><li>K->A at 499: Abolishes sumoylation; when associated with A-538</li><li>E->A at 501: Abolishes sumoylation; when associated with A-540</li><li>K->A at 538: Abolishes sumoylation; when associated with A-499</li><li>E->A at 540: Abolishes sumoylation; when associated with A-501</li><li>I->R at 576: Abolishes interaction with AFT7IP and subsequent transcription repression activity</li></ul>	<li>sumoylation</li><li>transcription</li>	<li>GO:0016925</li><li>GO:0006350</li>	<li>binding</li><li>DNA binding</li>	<li>GO:0005488</li><li>GO:0003677</li>					1
Q9UJ41	27342	<ul><li>A->G at 196: Reduces affinity for ubiquitin 3-fold</li><li>D->A at 530: Strongly reduced activity</li><li>P->A at 534: Strongly reduced activity</li><li>Y->A at 571: Strongly reduced activity</li><li>T->A at 574: Strongly reduced activity</li></ul>							<li>P69326</li><li>P08565</li><li>P69322</li><li>P69323</li><li>P69324</li><li>P69325</li><li>P68196</li><li>O46543</li><li>P68197</li><li>Q05550</li><li>P68198</li><li>P68199</li><li>P19848</li><li>P42739</li><li>P68195</li><li>Q867C2</li><li>P62991</li><li>P62990</li><li>P61863</li><li>P61864</li><li>P61862</li><li>Q867C4</li><li>Q867C3</li><li>P23398</li><li>P68204</li><li>P84589</li><li>Q865C5</li><li>P42740</li><li>P68201</li><li>Q8MKD1</li><li>P14792</li><li>P63049</li><li>P0C072</li><li>P63051</li><li>P69308</li><li>P69309</li><li>P20685</li><li>P15174</li><li>P62976</li><li>P62977</li><li>P62974</li><li>P62975</li><li>P62972</li><li>P13117</li><li>P14624</li><li>P62973</li><li>P46574</li><li>P69310</li><li>P69313</li><li>P69314</li><li>P69311</li><li>P08618</li><li>P69312</li><li>P69317</li><li>P69318</li><li>P69315</li><li>P0C014</li><li>P69316</li><li>P59263</li><li>P69319</li><li>P49634</li><li>P49635</li><li>Q9Y848</li><li>P22589</li><li>P62988</li><li>P62989</li><li>P69321</li><li>P23324</li><li>P69320</li><li>P59669</li>		1
Q9UJU6	28988	<ul><li>D->A at 361: Abolishes cleavage by caspase-3</li></ul>									1
Q9UJY4	23062	<ul><li>LIDLE->AADAA at 349-353: Partial loss of clathrin-binding</li></ul>			clathrin-binding	GO:0030276					1
Q9UJY5	26088	<ul><li>N->A at 92: Abolishes interaction with IGF2R</li><li>L->A at 182: Abolishes interaction with ARF1, UBC and TSG101</li><li>N->A at 194: Abolishes interaction with ARF1 and RABEP1</li><li>I->A at 197: Abolishes interaction with ARF1, UBC and TSG101</li><li>K->A at 198: Abolishes interaction with ARF1</li><li>M->A at 200: Abolishes interaction with ARF1</li><li>D->A at 204: Abolishes interaction with ARF1</li><li>M->K at 259: Abolishes interaction with RABEP1</li><li>R->A at 260: No effect on interaction with RABEP1</li><li>R->E at 260: Abolishes interaction with RABEP1 and UBC</li><li>F->A at 264: Abolishes interaction with RABEP1</li><li>A->D at 267: Abolishes interaction with RABEP1 and UBC</li><li>L->A at 277: Abolishes interaction with RABEP1, UBC and TSG101</li><li>L->A at 281: Abolishes interaction with RABEP1</li><li>N->A at 284: Abolishes interaction with RABEP1</li><li>N->S at 284: Abolishes interaction with RABEP1</li><li>S->A at 355: Increased interaction with IGF2R. Reduced phosphorylation</li><li>S->D at 355: Abolishes interaction with IGF2R</li><li>LLDDE->AADAA at 356-360: Partial loss of clathrin-binding</li><li>D->A at 358: Increased interaction with IGF2R</li><li>LM->AA at 361-362: Increased interaction with IGF2R</li><li>A->D at 563: Abolishes interaction with CCDC91</li><li>V->D at 564: Abolishes interaction with CCDC91</li><li>V->E at 570: Abolishes interaction with CCDC91</li><li>L->E at 572: Abolishes interaction with CCDC91</li></ul>	phosphorylation	GO:0016310	clathrin-binding	GO:0030276			<li>Q99816</li><li>Q8L7G0</li><li>P84080</li><li>P22274</li><li>P11076</li><li>O23778</li><li>Q5UQC9</li><li>Q867C2</li><li>Q7Z6B0</li><li>P61209</li><li>Q75A26</li><li>P84077</li><li>Q867C4</li><li>Q4R5P2</li><li>Q867C3</li><li>P36397</li><li>Q15276</li><li>P27949</li><li>Q94650</li><li>P11717</li><li>P25869</li><li>P49076</li><li>P61210</li><li>O48649</li><li>P62988</li><li>P08169</li><li>Q96361</li><li>P51821</li><li>Q25761</li><li>Q5RCA7</li><li>P51822</li>		1
Q9UK55	51156	<ul><li>Y->A at 408: Loss of inhibitory activity</li></ul>									1
Q9UK73	10116	<ul><li>D->A at 342: Prevents cleavage by a caspase-3-like protease</li><li>D->A at 356: Does not affect cleavage by a caspase-3-like protease</li></ul>							<li>P19028</li><li>Q9QBZ5</li><li>P24107</li><li>Q9QBZ1</li><li>Q79666</li><li>P15833</li><li>P03362</li><li>P18042</li><li>Q8AII1</li><li>P03363</li><li>P04024</li><li>P04023</li><li>P10978</li><li>O93215</li><li>P26810</li><li>Q1A249</li><li>P03356</li><li>P03355</li><li>O41798</li><li>P20892</li><li>Q9Y6I0</li><li>P10210</li><li>Q9QBY3</li><li>P03353</li><li>P16901</li><li>Q74120</li><li>Q09SZ9</li><li>Q89928</li><li>Q73368</li><li>P84454</li><li>Q9WC63</li><li>P20825</li><li>Q9IDV9</li><li>P0C211</li><li>P0C210</li><li>P51518</li><li>Q4U0X6</li><li>P12451</li><li>P07570</li><li>P28936</li><li>O89940</li><li>P24740</li><li>P26809</li><li>P26808</li><li>Q0R5R3</li><li>Q0R5R2</li><li>P18802</li><li>P10394</li><li>P19561</li><li>P16423</li><li>P63119</li><li>P19560</li><li>Q75002</li><li>P04589</li><li>P04587</li><li>P04588</li><li>Q9QSR3</li><li>O91080</li><li>P16046</li><li>P17757</li><li>P12497</li><li>P12499</li><li>P12498</li><li>P03311</li><li>P20875</li><li>P20876</li><li>P10273</li><li>Q9WC54</li><li>P10272</li><li>P10271</li><li>P10270</li><li>P19199</li><li>P05962</li><li>P18096</li><li>P10265</li><li>P04584</li><li>P11227</li><li>P04585</li><li>Q76634</li><li>Q8I7P9</li><li>Q9Q720</li><li>P14078</li><li>P31822</li><li>P11365</li><li>P35963</li><li>P14074</li><li>P05959</li><li>P63131</li><li>P04323</li><li>P10274</li><li>P21407</li><li>O89290</li><li>P35956</li><li>P05960</li><li>P05961</li><li>Q1A267</li><li>P63122</li><li>P63123</li><li>P63124</li><li>P63125</li><li>P63120</li><li>P63121</li><li>P03366</li><li>P03367</li><li>P03369</li><li>P63127</li><li>P63128</li><li>P63129</li><li>Q77373</li><li>P03370</li><li>P27502</li><li>P21414</li>		1
Q9UKB5	55966	<ul><li>L->A at 303: Mistargeting to the apical membrane</li><li>Y->A at 350: Mistargeting to the apical membrane</li><li>Y->A at 368: Mistargeting to the apical membrane</li><li>Y->A at 380: Mistargeting to the apical membrane</li><li>LI->HV at 396-397: Mistargeting to the apical membrane</li><li>L->A at 396: Mistargeting to the apical membrane</li></ul>					membrane	GO:0016020			1
Q9UKF6	51692	<ul><li>DH->KA at 75-76: Loss of endonuclease activity</li><li>K->R at 462: Reduced sumoylation; when associated with R-465 and R-545</li><li>K->R at 465: Reduced sumoylation; when associated with R-462 and R-545</li><li>K->R at 545: Reduced sumoylation; when associated with R-462 and R-465</li></ul>	sumoylation	GO:0016925					<li>P04323</li><li>P20825</li><li>P10399</li><li>P10978</li><li>P00641</li><li>Q00962</li><li>P38446</li><li>P15629</li><li>P13717</li><li>P05400</li><li>P03554</li><li>P03556</li><li>Q03269</li><li>P03555</li><li>Q03277</li><li>P10394</li><li>Q03278</li><li>Q03275</li><li>Q05118</li><li>Q03276</li><li>P11283</li><li>P16423</li><li>Q03273</li><li>Q03274</li><li>Q03271</li><li>Q03272</li><li>P09523</li><li>P11369</li><li>Q8I7P9</li><li>Q03270</li><li>P11367</li><li>Q02964</li><li>P10400</li><li>P20314</li><li>Q03279</li><li>P10401</li>		1
Q9UKI8	9874	<ul><li>D->A at 607: Loss of kinase activity</li><li>S->A at 743: Loss of kinase inhibition in response to DNA damage</li><li>S->D at 743: Loss of kinase inhibition in response to DNA damage</li><li>S->E at 743: Loss of kinase inhibition in response to DNA damage</li></ul>			kinase activity	GO:0016301					1
Q9UKJ1	29992	<ul><li>Y->F at 269: Greatly diminishes interaction with PTPN6</li></ul>							P29350		1
Q9UKJ5	26511	<ul><li>CGCLCCCC->SGSLS at 88-95: Loss of palmitoylation. Abolishes membrane association</li></ul>					membrane	GO:0016020			1
Q9UKT4	26271	<ul><li>E->A at 143: Delays degradation</li><li>S->E at 145: Degraded in similar manner to wild-type</li><li>S->N at 145: Not mitotically degraded. Shows impaired interaction with BTRC and reduced phosphate incorporation; when associated with N-149</li><li>S->A at 148: Degraded in similar manner to wild-type</li><li>S->E at 149: Degraded in similar manner to wild-type</li><li>S->N at 149: Not mitotically degraded. Shows impaired interaction with BTRC and reduced phosphate incorporation; when associated with N-145</li><li>S->A at 182: Shows impaired interaction with BTRC</li><li>KRNPKVD->AAAAAA at 210-216: Loss of interaction with EVI5</li><li>C->S at 401: Reduced inhibition of APC</li></ul>							<li>Q9Y297</li><li>P25054</li><li>O60447</li>		1
Q9UKV3	22985	<ul><li>D->A at 1093: Abolishes cleavage by CASP3 and chromatin condensation activity</li></ul>					chromatin	GO:0000785	<li>Q8MKI5</li><li>Q8MJU1</li><li>Q5IS99</li><li>Q2PFV2</li><li>Q60431</li><li>Q8MJC3</li><li>Q95ND5</li><li>P42574</li><li>Q5IS54</li><li>Q08DY9</li>		1
Q9UL54	9344	<ul><li>K->A at 57: Loss of kinase activity</li></ul>			kinase activity	GO:0016301					1
Q9ULC4	28985	<ul><li>T->A at 81: No phosphorylation by MAPK1; decreased stability of MCTS1 protein; Significant cell growth reduction</li><li>S->A at 118: No phosphorylation by CDC2; No cell growth alteration</li></ul>	phosphorylation	GO:0016310					<li>Q9W739</li><li>Q9DGA2</li><li>Q9DGA5</li><li>P19026</li><li>Q5RCH1</li><li>Q9DG98</li><li>P06493</li><li>P48734</li><li>P43290</li><li>P23111</li><li>P13863</li><li>P46196</li><li>Q04770</li><li>P52389</li><li>P15436</li><li>P28482</li><li>P24100</li><li>P51958</li><li>Q41639</li><li>P54119</li><li>P93101</li><li>Q9DGD3</li><li>Q5Z9J0</li>		1
Q9UM07	23569	<ul><li>R->A at 374: Strongly reduces enzymatic activity</li><li>C->A at 645: Abolishes enzymatic activity</li></ul>									1
Q9UMR2	11269	<ul><li>E->Q at 243: Loss of activity</li></ul>									1
Q9UMR5	9374	<ul><li>S->A at 111: Abolishes enzymatic activity</li><li>D->A at 228: Abolishes enzymatic activity</li><li>H->A at 283: Abolishes enzymatic activity</li><li>H->A at 287: No effect on enzymatic activity</li></ul>									1
Q9UMX1	51684	<ul><li>E->A at 106: No effect on down-regulation of GLI1 activity</li><li>D->A at 111: No effect on down-regulation of GLI1 activity</li><li>T->A,D at 128: No effect on down-regulation of GLI1 activity</li><li>E->A at 152: No effect on down-regulation of GLI1 activity</li><li>D->A at 159: Abolishes down-regulation of GLI1 activity. Has only slight effect on GLI1 binding</li><li>E->A at 181: No effect on down-regulation of GLI1 activity</li><li>E->A at 221: No effect on down-regulation of GLI1 activity</li><li>D->A at 262: No effect on down-regulation of GLI1 activity</li></ul>			binding	GO:0005488			<li>P55878</li><li>P08151</li>		1
Q9UN19	27071	<ul><li>R->K at 61: No change in BCR-induced NFAT activation</li><li>K->L at 173: No interaction with 3-phosphoinositides</li><li>R->C at 184: No membrane association</li><li>K->E at 197: No membrane association</li><li>W->L at 250: No interaction with 3-phosphoinositides</li></ul>					membrane	GO:0016020	P11274		1
Q9UN37	27183	<ul><li>V->A,D at 13: Diminishes interaction with IST1</li><li>V->D at 13: Abolishes interaction with CHMP6, no effect on interaction with CHMP1A</li><li>V->D at 13: Greatly diminishes localization to punctate class E compartments; when associated with Q-173</li><li>L->A,D at 64: Abolishes interaction with CHMP1B; diminishes interaction with IST1</li><li>L->D at 64: Greatly diminishes localization to punctate class E compartments and partially restores HIV-1 release; when associated with Q-173</li><li>L->D at 64: Modestly reduces interaction with CHMP6</li><li>E->D at 68: Diminshes interaction with CHMP1B</li><li>K->Q at 173: Defective in ATP-binding. Causes membrane association. Induces vacuolation of endosomal compartments and impairs cholesterol sorting. Inhibits HIV-1 release</li><li>K->Q at 173: Greatly diminishes localization to punctate class E compartments and partially restores HIV-1 release; when associated with D-64</li><li>K->Q at 173: Greatly diminishes localization to punctate class E compartments; when associated with D-173</li><li>WL->AA at 201-202: Strongly impairs HIV-1 release</li><li>G->A at 203: Impairs HIV-1 release</li><li>E->Q at 228: Defective in ATP-hydrolysis. Causes membrane association. Induces vacuolation of endosomal compartments and impairs cholesterol and protein sorting. Inhibits HIV-1 release. Increases binding to CHMP1</li></ul>	<li>ATP-hydrolysis</li><li>localization</li>	<li>GO:0006200</li><li>GO:0051179</li>	<li>binding</li><li>ATP-binding</li>	<li>GO:0005488</li><li>GO:0005524</li>	membrane	GO:0016020	<li>Q5ZKX1</li><li>Q5ZL55</li><li>Q5E994</li><li>Q9HD42</li><li>Q7LBR1</li><li>P53843</li><li>Q96FZ7</li><li>Q5R861</li><li>Q5R605</li>		1
Q9UNE0	10913	<ul><li>E->K at 379: Reduces activation of NF-kappa-B</li></ul>									1
Q9UNH5	8556	<ul><li>D->A at 251: Loss of phosphatase activity</li><li>C->S at 278: Loss of phosphatase activity</li><li>R->A at 284: Loss of phosphatase activity</li><li>M->A at 362: Inappropriate nucleolar localization; when associated with A-364</li><li>I->A at 364: Inappropriate nucleolar localization; when associated with A-362</li></ul>	localization	GO:0051179					<li>Q5X1E5</li><li>Q7M7K5</li><li>Q7MAZ9</li><li>Q8XBL4</li><li>Q88A53</li><li>Q5P3T0</li><li>Q7MBF4</li><li>Q8Z3M9</li><li>Q5PC82</li><li>Q5ZRX9</li><li>Q821A6</li><li>Q87SK9</li><li>Q9JZ88</li><li>Q9CP21</li><li>Q82U82</li><li>Q9I5V3</li><li>Q5F8K9</li><li>Q63YC3</li><li>Q8Y395</li><li>Q6LV05</li><li>Q8ZLY4</li><li>Q6FA38</li><li>Q9PDL7</li><li>Q62EU1</li><li>Q9JUB2</li><li>Q5WT58</li><li>Q665U9</li><li>Q57JQ5</li><li>Q9KPC6</li><li>Q8P5D4</li><li>Q8CWL6</li><li>Q8PPG9</li><li>P06961</li><li>P45269</li><li>Q9L7A3</li><li>Q88QU2</li><li>Q6D160</li><li>Q8ZI64</li><li>Q60CQ4</li><li>Q87DS9</li><li>Q65Q41</li><li>Q5E2K7</li><li>Q8CXX6</li>		1
Q9UNQ0	9429	<ul><li>K->M at 86: Inactive and altered subcellular location</li><li>N->Q at 418: No effect</li><li>R->D at 482: Decreases ATPase activity</li><li>R->G,N,S,T at 482: Increases ATPase activity</li><li>R->K,I,M,Y at 482: No change in ATPase activity</li><li>R->T,Y at 482: Decreases transport activity</li><li>N->Q at 557: No effect</li><li>N->Q at 596: Loss of glycosylation</li></ul>	transport	GO:0006810	ATPase activity	GO:0016887					1
Q9UNW1	9562	<ul><li>H->A at 370: Greatly diminishes phosphatase activity</li></ul>							<li>Q5X1E5</li><li>Q7M7K5</li><li>Q7MAZ9</li><li>Q8XBL4</li><li>Q88A53</li><li>Q5P3T0</li><li>Q7MBF4</li><li>Q8Z3M9</li><li>Q5PC82</li><li>Q5ZRX9</li><li>Q821A6</li><li>Q87SK9</li><li>Q9JZ88</li><li>Q9CP21</li><li>Q82U82</li><li>Q9I5V3</li><li>Q5F8K9</li><li>Q63YC3</li><li>Q8Y395</li><li>Q6LV05</li><li>Q8ZLY4</li><li>Q6FA38</li><li>Q9PDL7</li><li>Q62EU1</li><li>Q9JUB2</li><li>Q5WT58</li><li>Q665U9</li><li>Q57JQ5</li><li>Q9KPC6</li><li>Q8P5D4</li><li>Q8CWL6</li><li>Q8PPG9</li><li>P06961</li><li>P45269</li><li>Q9L7A3</li><li>Q88QU2</li><li>Q6D160</li><li>Q8ZI64</li><li>Q60CQ4</li><li>Q87DS9</li><li>Q65Q41</li><li>Q5E2K7</li><li>Q8CXX6</li>		1
Q9UP65	8605	<ul><li>R->A at 54: Abolishes enzyme activity</li><li>S->A at 82: Abolishes enzyme activity</li><li>D->A at 385: Abolishes enzyme activity</li><li>R->A at 402: Abolishes enzyme activity</li></ul>									1
Q9UPN9	51592	<ul><li>C->A at 125: Abolishes E3 activity but does not affect interaction with SMAD4; when associated with A-128</li><li>C->A at 128: Abolishes E3 activity but does not affect interaction with SMAD4; when associated with A-125</li></ul>							<li>Q1HE26</li><li>Q13485</li><li>Q9GKQ9</li>		1
Q9UPQ3	116987	<ul><li>C->S at 647: Loss of GAP activity</li><li>R->K at 652: Loss of GAP activity. No effect on AP-3-binding</li></ul>			binding	GO:0005488			<li>Q92263</li><li>P20936</li><li>Q92211</li><li>P09851</li><li>Q5PEA9</li><li>P74873</li><li>P74851</li><li>P50904</li>		1
Q9UPQ8	22845	<ul><li>G->D at 443: Abolishes kinase activity</li><li>D->A at 451: Reduces kinase activity</li><li>K->A at 470: Reduces kinase activity. Significant reduction in binding affinity for CTP; when associated with A-471</li><li>K->A at 471: Reduces kinase activity. Significant reduction in binding affinity for CTP</li><li>T->A at 472: Reduces kinase activity. Significant reduction in binding affinity for CTP</li><li>E->A at 474: No effect on kinase activity</li><li>G->A at 475: No effect on kinase activity</li></ul>			<li>binding</li><li>kinase activity</li>	<li>GO:0005488</li><li>GO:0016301</li>			<li>P38152</li><li>P53007</li><li>P49587</li><li>P34519</li><li>P32089</li><li>P79110</li>		1
Q9UPR3	23381	<ul><li>D->A at 860: Abolishes stimulation of RENT1 dephosphorylation</li></ul>	dephosphorylation	GO:0016311					<li>Q98TR3</li><li>Q92900</li>		1
Q9UPZ9	22858	<ul><li>K->R at 33: Loss of activity and autophosphorylation; when associated with R-34; R-36 and R-38</li><li>K->R at 34: Loss of activity and autophosphorylation; when associated with R-33; R-36 and R-38</li><li>K->R at 36: Loss of activity and autophosphorylation; when associated with R-33; R-34 and R-38</li><li>K->R at 38: Loss of activity and autophosphorylation; when associated with R-33; R-34 and R-36</li><li>T->A at 157: Reduction of activity and loss of autophosphorylation. Loss of activity and autophosphorylation; when associated with F-159</li><li>Y->F at 159: Reduction of activity and loss of autophosphorylation. Loss of activity and autophosphorylation; when associated with A-157</li></ul>	autophosphorylation	GO:0046777							1
Q9UQ80	5036	<ul><li>KYK->AYA at 20-22: Loss of nucleolar localization</li><li>S->A at 363: No effect on in vitro phosphorylation by PKC</li><li>RK->AA at 364-365: Only partial nucleolar localization</li><li>T->A at 366: Decreases in vitro phosphorylation by PKC</li></ul>	<li>phosphorylation</li><li>localization</li>	<li>GO:0016310</li><li>GO:0051179</li>					<li>P13678</li><li>P13677</li><li>P05130</li><li>P34722</li>		1
Q9UQ84	9156	<ul><li>D->A at 78: Abrogates double-stranded DNA exonuclease activity and endonuclease activity against 5'-overhanging flap structures. Also reduces DNA-binding to 5'-overhanging flap structures</li><li>D->A at 173: Abrogates double-stranded DNA exonuclease activity and endonuclease activity against 5'-overhanging flap structures. No effect on DNA-binding to 5'-overhanging flap structures</li><li>D->A at 225: Abrogates double-stranded DNA exonuclease activity and endonuclease activity against 5'-overhanging flap structures. Also enhances DNA-binding to 5'-overhanging flap structures</li><li>K->A,T at 418: Complete loss of nuclear localization</li><li>R->A at 419: Complete loss of nuclear localization</li></ul>	localization	GO:0051179	DNA-binding	GO:0003677			<li>P04323</li><li>P20825</li><li>P10399</li><li>P10978</li><li>P00641</li><li>P20321</li><li>Q00962</li><li>P38446</li><li>P15629</li><li>P00638</li><li>P13717</li><li>P05400</li><li>P03554</li><li>Q03269</li><li>P03556</li><li>P03555</li><li>Q03277</li><li>P10394</li><li>Q03278</li><li>Q03275</li><li>Q05118</li><li>Q03276</li><li>P11283</li><li>P16423</li><li>Q03273</li><li>Q03274</li><li>Q03271</li><li>Q03272</li><li>P09523</li><li>P11369</li><li>Q8I7P9</li><li>Q03270</li><li>P03697</li><li>P11367</li><li>Q02964</li><li>P10400</li><li>P20314</li><li>Q03279</li><li>P10401</li>		1
Q9UQB8	10458	<ul><li>K->E at 142: Abolishes actin-bundling and filopodia formation; when associated with E-143; E-146 and E147</li><li>K->E at 143: Abolishes actin-bundling and filopodia formation; when associated with E-142; E-146 and E147</li><li>K->E at 146: Abolishes actin-bundling and filopodia formation; when associated with E-142; E-143 and E147</li><li>K->E at 147: Abolishes actin-bundling and filopodia formation; when associated with E-142; E-143 and E146</li><li>I->N at 267: Loss of interaction with CDC42. Loss of stimulation of neurite growth</li><li>F->A at 427: Loss of interaction with ENAH and no induction of filopodia; when associated with A-428</li><li>P->A at 428: Loss of interaction with ENAH and no induction of filopodia; when associated with A-427</li></ul>	neurite growth	GO:0007399					<li>Q92192</li><li>Q92193</li><li>P53499</li><li>P26183</li><li>P53498</li><li>O13419</li><li>Q9P4D1</li><li>P48465</li><li>P53455</li><li>Q39596</li><li>Q39758</li><li>P26182</li><li>P80709</li><li>Q9UVX4</li><li>O17320</li><li>P53689</li><li>P78711</li><li>Q17031</li><li>P30161</li><li>P17128</li><li>Q9HF56</li><li>P45521</li><li>P45520</li><li>P20904</li><li>P81085</li><li>Q6TCF2</li><li>Q99023</li><li>Q75D00</li><li>P51775</li><li>P10365</li><li>P60011</li><li>P60010</li><li>Q8SWN8</li><li>O16808</li><li>P02577</li><li>P10989</li><li>P68555</li><li>Q05214</li><li>Q8X119</li><li>O65316</li><li>O65315</li><li>O65314</li><li>P53491</li><li>P91754</li><li>P13363</li><li>P60953</li><li>P11426</li><li>P60952</li><li>O81221</li><li>Q11212</li><li>P50138</li><li>P53477</li><li>P53476</li><li>Q90694</li><li>O94103</li><li>P60009</li><li>P53502</li><li>Q2U7A3</li><li>P53500</li><li>Q9UVZ8</li><li>P14235</li><li>O00937</li><li>Q9UVF3</li><li>O14426</li><li>Q24733</li><li>P90689</li><li>P24902</li><li>O74258</li><li>Q8N8S7</li><li>P19073</li>		1
Q9UQC9	9635	<ul><li>N->Q at 150: Reduction in size by around 2 kDa</li><li>N->Q at 292: No change in size</li><li>N->Q at 522: Reduction in size by around 2 kDa</li><li>N->Q at 637: No change in size</li><li>N->Q at 822: Reduction in size by around 2 kDa</li><li>N->Q at 938: No change in size</li></ul>									1
Q9UQF0	30816	<ul><li>RNK->AAA at 314-316: Complete loss of cleavage between SU and TM. Loss of fusiogenic function</li><li>R->T at 317: Complete loss of cleavage between SU and TM. Loss of fusiogenic function</li><li>C->A at 405: Loss of fusiogenic function. No effect on cleavage between SU and TM</li></ul>									1
Q9UQF2	9479	<ul><li>R->G at 160: Abolishes MAPK9 interaction</li><li>P->G at 161: Abolishes MAPK9 interaction</li><li>P->A at 704: No effect on KNS2 binding</li><li>Y->A at 709: Abolishes KNS2 binding</li></ul>			binding	GO:0005488			<li>Q5R581</li><li>P45984</li><li>O00139</li><li>P79996</li><li>Q07866</li>		1
Q9UQK1	5507	<ul><li>V->A at 85: No effect on interaction with EPM2A; when associated with A-87</li><li>F->A at 87: No effect on interaction with EPM2A; when associated with A-85</li><li>D->A at 247: No interaction with EPM2A; when associated with A-250</li><li>D->A at 250: No interaction with EPM2A; when associated with A-247</li></ul>							O95278		1
Q9UQL6	10014	<ul><li>S->A at 259: Reduces CaMK-dependent phosphorylation and the subsequent nuclear export. Abolishes nuclear export; when associated with A-498</li><li>S->A at 279: No effect</li><li>S->A at 498: Reduces CaMK-dependent phosphorylation and the subsequent nuclear export. Abolishes nuclear export; when associated with A-259</li><li>S->A at 661: No effect</li><li>S->A at 713: No effect</li><li>V->A at 1086: Reduces CaMK-dependent nuclear export</li><li>L->A at 1092: Reduces CaMK-dependent nuclear export</li></ul>	<li>phosphorylation</li><li>nuclear export</li>	<li>GO:0016310</li><li>GO:0051168</li>							1
Q9Y233	10846	<ul><li>D->A at 554: Loss of activity and of zinc binding</li><li>D->N at 554: Reduces activity 1000-fold</li></ul>			zinc binding	GO:0008270					1
Q9Y239	10392	<ul><li>V->Q at 41: Abolishes caspase-9 activation and interaction with RICK</li><li>K->R at 208: Reduces caspase-9 activation</li></ul>							O43353		1
Q9Y243	10000	<ul><li>T->A at 305: No activation after pervanadate treatment</li><li>T->D at 305: 2-fold increase of phosphorylation steady state level, no activation after pervanadate treatment</li><li>T->A at 447: No effect</li><li>T->D at 447: No effect</li><li>S->A at 472: 67% decrease of activity after pervanadate treatment</li><li>S->D at 472: 1.4-fold increase of phosphorylation steady state level, 50% decrease of activity after pervanadate treatment</li></ul>	phosphorylation	GO:0016310							1
Q9Y251	10855	<ul><li>Y->A,E at 156: Alteration of the correct processing of heparanase which results in the cleavage at an upstream site in the linker peptide and no activation of proheparanase</li><li>Y->V at 156: Normal processing</li><li>K->A at 158: No association with GS-modified heparin; when associated with K-158</li><li>K->A at 161: Two-fold increase in the level of secretion upon addition of GS-modified heparin. No association with GS-modified heparin; when associated with K-161</li><li>N->Q at 162: Faster electrophoretic migration typical of a size reduction and important decrease of secretion. Larger size reduction; when associated with Q-178; Q-200; Q-217; Q-238 and Q-459</li><li>N->Q at 178: Faster electrophoretic migration typical of a size reduction and important decrease of secretion. Larger size reduction; when associated with Q-162; Q-200; Q-217; Q-238 and Q-459</li><li>N->Q at 200: Faster electrophoretic migration typical of a size reduction and partial decrease in secretion. Larger size reduction; when associated with Q-162; Q-178; Q-217; Q-238 and Q-459</li><li>N->Q at 217: Faster electrophoretic migration typical of a size reduction and partial decrease in secretion. Larger size reduction; when associated with Q-162; Q-178; Q-200; Q-238 and Q-459</li><li>E->A at 225: Loss of heparanase activity</li><li>N->Q at 238: Faster electrophoretic migration typical of a size reduction. Larger size reduction and important decrease of secretion; when associated with Q-162; Q-178; Q-200; Q-217 and Q-459</li><li>E->A at 343: Loss of heparanase activity</li><li>D->A at 367: Strong decrease in heparanase activity</li><li>E->A at 378: No reduction in heparanase activity</li><li>E->A at 396: No reduction in heparanase activity</li><li>N->Q at 459: Faster electrophoretic migration typical of a size reduction. Larger size reduction and important decrease of secretion; when associated with Q-162; Q-178; Q-200; Q-217 and Q-238</li></ul>	secretion	GO:0046903	heparanase activity	GO:0030305			<li>P11140</li><li>P02879</li><li>P93543</li><li>P28590</li><li>Q06077</li><li>Q06076</li>		1
Q9Y253	5429	<ul><li>Y->A,F at 52: Reduces DNA polymerase activity</li><li>Y->E at 52: Reduces DNA polymerase activity. Increases fidelity of replication and reduces translesion bypass</li></ul>							<li>Q9YUS3</li><li>O59610</li><li>Q9YUS2</li><li>P56689</li><li>P06538</li><li>Q69025</li><li>Q9HH84</li><li>P04495</li><li>P43139</li><li>Q56366</li><li>P77933</li><li>P03261</li><li>P19894</li><li>P52025</li><li>P03158</li><li>Q6S6P1</li><li>Q85428</li><li>P09252</li><li>O64235</li><li>P03198</li><li>P52367</li><li>P28859</li><li>P74918</li><li>P52342</li><li>O72539</li><li>P20311</li><li>O70736</li><li>P28857</li><li>P28858</li><li>P20509</li><li>Q9HH05</li><li>Q88469</li><li>P61875</li><li>P61876</li><li>O72540</li><li>Q05254</li><li>Q64751</li><li>P06950</li><li>P06856</li><li>P05664</li><li>Q83948</li><li>P05468</li><li>P08546</li><li>O71121</li><li>Q37882</li><li>P19822</li><li>P10479</li><li>Q58295</li><li>P87553</li><li>P30321</li><li>P30320</li><li>P10582</li><li>P21402</li><li>Q51334</li><li>O33845</li><li>P42489</li><li>P18131</li><li>O27276</li><li>P09804</li><li>P24907</li><li>P41712</li><li>Q84173</li><li>P48311</li><li>P33793</li><li>O57191</li><li>P04415</li><li>P03680</li><li>P00581</li><li>Q5UQR0</li><li>Q90162</li><li>P87503</li><li>Q37989</li><li>P04292</li><li>P30318</li><li>P04293</li><li>P30317</li><li>Q65946</li><li>Q38087</li><li>P07917</li><li>O29753</li><li>P07918</li><li>P30319</li><li>P06225</li><li>P27172</li><li>P30314</li><li>P09854</li>		1
Q9Y257	9424	<ul><li>C->A at 53: No channel activity</li></ul>									1
Q9Y265	8607	<ul><li>D->N at 302: Inhibition of MYC- and CTNNB1-mediated transformation</li></ul>							<li>P01110</li><li>Q9MZT9</li><li>Q9MZT7</li><li>Q9MZT8</li><li>P10395</li><li>Q9MZT6</li><li>Q28566</li><li>P35222</li><li>P68272</li><li>P68271</li><li>P12523</li><li>P22555</li><li>P01109</li><li>P01106</li><li>P49032</li><li>P49033</li><li>Q28350</li><li>Q2HJ27</li><li>Q9MZU0</li><li>Q17103</li><li>P06646</li><li>Q29031</li><li>P0C0N8</li><li>P49709</li><li>P23583</li><li>P06295</li><li>P21438</li><li>P0C0N9</li>		1
Q9Y266	10726	<ul><li>S->A at 274: Abolishes phosphorylation by PLK1; when associated with A-326</li><li>S->A at 326: Abolishes phosphorylation by PLK1; when associated with A-274</li></ul>	phosphorylation	GO:0016310					P53350		1
Q9Y272	51655	<ul><li>C->S at 11: Suppresses NO-induced activation</li></ul>									1
Q9Y294	25842	<ul><li>ED->AA at 36-37: Abrogates interaction with HIRA and induction of senescence-associated heterochromatin foci</li><li>D->A at 37: Abrogates interaction with CHAF1B and HIRA</li><li>D->R at 54: Reduces interaction with histone H3</li><li>VGP->AAA at 62-64: Abrogates interaction with HIRA and induction of senescence-associated heterochromatin foci</li><li>V->R at 94: Abrogates interaction with histone H3 and histone H4</li><li>R->E at 108: Reduces interaction with histone H3</li></ul>	senescence	GO:0007568,GO:0010149			heterochromatin	GO:0000792	<li>Q76FE7</li><li>Q98RY4</li><li>P82888</li><li>P07041</li><li>Q6LAF1</li><li>Q6LAF3</li><li>P91882</li><li>Q8MTV8</li><li>Q27443</li><li>Q76FD9</li><li>P08436</li><li>P35059</li><li>Q7XYZ0</li><li>P35057</li><li>Q5DWI3</li><li>P91890</li><li>Q6WZ83</li><li>P83865</li><li>Q9P427</li><li>P84048</li><li>P84049</li><li>P83864</li><li>Q7KQD1</li><li>Q7K8C0</li><li>P84044</li><li>P84045</li><li>P62779</li><li>P84046</li><li>P62778</li><li>P84047</li><li>P62777</li><li>P84040</li><li>Q8I0Y4</li><li>P62776</li><li>P90543</li><li>P84041</li><li>P84042</li><li>P84043</li><li>Q43083</li><li>P84050</li><li>P08437</li><li>Q6WV90</li><li>P62782</li><li>P62781</li><li>Q8NIG3</li><li>P62784</li><li>P62783</li><li>P62780</li><li>Q9HDF5</li><li>Q7LKT3</li><li>P62789</li><li>Q06196</li><li>P08898</li><li>Q6WV73</li><li>Q27765</li><li>P79987</li><li>P62788</li><li>Q6WV74</li><li>Q9HDN1</li><li>P23753</li><li>P62787</li><li>P59259</li><li>Q7M3Z5</li><li>Q2UCQ0</li><li>P84239</li><li>P84238</li><li>P84237</li><li>P84236</li><li>P84235</li><li>P61835</li><li>P91849</li><li>Q6ZXX3</li><li>P61834</li><li>P61833</li><li>P61832</li><li>P61831</li><li>P61830</li><li>P54198</li><li>Q76H85</li><li>P09322</li><li>P62796</li><li>P62797</li><li>P02299</li><li>P62798</li><li>P62799</li><li>Q757N1</li><li>P62790</li><li>O42611</li><li>P62791</li><li>P62792</li><li>P62793</li><li>P61836</li><li>P62794</li><li>Q6WV72</li><li>P62795</li><li>P80739</li><li>P80738</li><li>Q9U7D0</li><li>P27996</li><li>Q9U7D1</li><li>Q13112</li><li>Q8T7J8</li><li>P90516</li><li>P62803</li><li>P62802</li><li>P62801</li><li>P62800</li><li>Q76MU7</li><li>P02309</li><li>Q8J1L3</li><li>Q6V9I2</li><li>P50566</li><li>P62806</li><li>P50564</li><li>P62804</li><li>P62805</li><li>Q8SQP4</li><li>Q76FF5</li><li>P04915</li><li>P04914</li><li>Q76FF1</li><li>Q6PMI5</li><li>P62887</li><li>P80553</li><li>P40285</li><li>Q71V09</li><li>P40287</li><li>P22843</li>		1
Q9Y2C4	9941	<ul><li>S->D at 137: No effect on catalytic activity</li><li>H->A at 140: Abolishes catalytic activity</li></ul>			catalytic activity	GO:0003824					1
Q9Y2G2	22900	<ul><li>L->R at 366: Inhibits homodimer formation</li></ul>									1
Q9Y2H1	23012	<ul><li>T->A at 75: Decreased kinase activity. Reduced binding of S100B</li><li>K->A at 119: Loss of autophosphorylation and kinase activity</li><li>S->A at 282: Loss of autophosphorylation and kinase activity</li><li>T->A at 442: Decreased kinase activity</li></ul>	autophosphorylation	GO:0046777	<li>binding</li><li>kinase activity</li>	<li>GO:0005488</li><li>GO:0016301</li>			<li>P02638</li><li>Q6YNR6</li><li>P04271</li>		1
Q9Y2H2	22876	<ul><li>D->A at 460: Loss of phosphatase activity</li></ul>							<li>Q5X1E5</li><li>Q7M7K5</li><li>Q7MAZ9</li><li>Q8XBL4</li><li>Q88A53</li><li>Q5P3T0</li><li>Q7MBF4</li><li>Q8Z3M9</li><li>Q5PC82</li><li>Q5ZRX9</li><li>Q821A6</li><li>Q87SK9</li><li>Q9JZ88</li><li>Q9CP21</li><li>Q82U82</li><li>Q9I5V3</li><li>Q5F8K9</li><li>Q63YC3</li><li>Q8Y395</li><li>Q6LV05</li><li>Q8ZLY4</li><li>Q6FA38</li><li>Q9PDL7</li><li>Q62EU1</li><li>Q9JUB2</li><li>Q5WT58</li><li>Q665U9</li><li>Q57JQ5</li><li>Q9KPC6</li><li>Q8P5D4</li><li>Q8CWL6</li><li>Q8PPG9</li><li>P06961</li><li>P45269</li><li>Q9L7A3</li><li>Q88QU2</li><li>Q6D160</li><li>Q8ZI64</li><li>Q60CQ4</li><li>Q87DS9</li><li>Q65Q41</li><li>Q5E2K7</li><li>Q8CXX6</li>		1
Q9Y2I1	11188	<ul><li>R->A at 49: Inhibits targeting to endosomes</li><li>Y->A at 50: Inhibits targeting to endosomes</li></ul>					endosomes	GO:0005768			1
Q9Y2K2	23387	<ul><li>T->A at 163: Prevents phosphorylation and activation by STK11 complex</li></ul>	phosphorylation	GO:0016310					<li>Q15831</li><li>Q0GGW5</li>		1
Q9Y2K7	22992	<ul><li>H->A at 212: Abolishes histone demethylase activity</li></ul>							Q9UBB5		1
Q9Y2N7	64344	<ul><li>K->R at 467: No loss of ubiquitination. Reduced ubiquitination when associated with R-570</li><li>P->A at 492: Reduced ubiquitination</li><li>K->R at 570: No loss of ubiquitination. Reduced ubiquitination when associated with R-467</li></ul>									1
Q9Y2W2	51729	<ul><li>R->A at 192: Loss of PQBP1-binding; when associated with A-197 and A-198</li><li>R->A at 197: Loss of PQBP1-binding; when associated with A-192 and A-198</li><li>K->A at 198: Loss of PQBP1-binding; when associated with A-192 and A-197</li></ul>			binding	GO:0005488			O60828		1
Q9Y2W7	30818	<ul><li>D->A at 61: Abolishes cleavage by caspase-3</li><li>D->A at 64: Abolishes cleavage by caspase-3</li></ul>									1
Q9Y336	27180	<ul><li>R->K at 120: Loss of sialic acid binding</li></ul>			binding	GO:0005488					1
Q9Y371	51100	<ul><li>V->M at 8: Abolishes interaction with BAX</li></ul>							<li>Q07815</li><li>Q07812</li><li>Q07814</li><li>O02703</li><li>P55269</li>		1
Q9Y385	51465	<ul><li>C->S at 91: Loss of catalytic activity. Slows down degradation of misfolded proteins from the ER</li></ul>			catalytic activity	GO:0003824	ER	GO:0005783			1
Q9Y397	51114	<ul><li>C->S at 169: Abolishes palmitoyltransferase activity</li></ul>			palmitoyltransferase activity	GO:0016409					1
Q9Y3B8	25996	<ul><li>D->A at 168: Abolishes activity</li></ul>									1
Q9Y3C8	51506	<ul><li>C->S at 116: Instead of the formation of an intermediate complex with a thiol ester bond between UFC1 (E2-like enzyme) and UFM1 (substrate), a stable complex with an O-ester bond is formed</li></ul>			E2	GO:0004840			<li>Q5R4N5</li><li>Q5ZMK7</li><li>Q5E953</li><li>P61960</li><li>Q2KJG2</li><li>Q9Y3C8</li><li>Q4R4I2</li>		1
Q9Y3D6	51024	<ul><li>L->P at 14: Approximately 40% of cells display fragmented mitochondria</li><li>L->P at 42: Less than 15% of cells display fragmented mitochondria</li><li>L->P at 58: Less than 15% of cells display fragmented mitochondria</li><li>L->P at 77: Less than 15% of cells display fragmented mitochondria. Shows greatly reduced binding to DNM1L</li><li>L->P at 91: Less than 15% of cells display fragmented mitochondria. Shows greatly reduced binding to DNM1L</li><li>L->P at 110: Approximately 40% of cells display fragmented mitochondria. No change in binding to DNM1L</li><li>K->A at 149: Protein localizes to both mitochondrion and endoplasmic reticulum. Protein localizes to endoplasmic reticulum only; when associated with A-151</li><li>K->A at 151: Protein localizes to both mitochondrion and endoplasmic reticulum. Protein localizes to endoplasmic reticulum only; when associated with A-149</li></ul>			binding	GO:0005488	<li>mitochondrion</li><li>endoplasmic reticulum</li>	<li>GO:0005739</li><li>GO:0005783</li>	O00429		1
Q9Y3M8	90627	<ul><li>R->A at 699: Loss of RhoGAP activity</li><li>K->E at 736: Loss of RhoGAP activity</li><li>R->E at 740: Loss of RhoGAP activity</li></ul>									1
Q9Y3P8	27240	<ul><li>N->Q at 26: Abolishes glycosylation</li><li>Y->F at 90: Reduces interaction with GRB2. Abolishes interaction with GRB2; when associated with F-188</li><li>Y->F at 127: No effect on interaction with PTPN11 or GRB2</li><li>Y->F at 148: Reduces interaction with PTPN11, no effect on inhibition of NF-AT activation</li><li>Y->F at 169: Abolishes interaction with CSK and impairs inhibition of NF-AT activation</li><li>Y->F at 188: Reduces interaction with GRB2. Abolishes interaction with GRB2; when associated with F-90</li></ul>							<li>Q5R4J7</li><li>Q07883</li><li>P62993</li><li>P41239</li><li>Q0VBZ0</li><li>Q90687</li><li>Q06124</li><li>P41240</li>		1
Q9Y3V2	25950	<ul><li>YP->AA at 61-62: Abolishes enhancement of IKBA sumoylation</li></ul>	sumoylation	GO:0016925					<li>Q91974</li><li>P25963</li><li>Q08353</li>		1
Q9Y463	9149	<ul><li>K->R at 140: Abolishes kinase activity</li><li>Y->F at 271: Abolishes kinase activity; when associated with F-273</li><li>Y->F at 273: Abolishes kinase activity; when associated with F-271</li></ul>			kinase activity	GO:0016301					1
Q9Y4C1	55818	<ul><li>H->Y at 1120: Abolishes histone demethylase activity</li></ul>							Q9UBB5		1
Q9Y4C5	9435	<ul><li>C->S at 59: Does not affect homodimerization. Abolishes homodimerization but not enzyme activity; when associated with S-39</li><li>C->S at 86: Induces migration in both homodimeric and monomeric forms. Abolishes homodimerization but not enzyme activity; when associated with S-12</li><li>R->A at 174: Induces a strong decrease in enzyme activity</li><li>R->A at 296: Induces a strong decrease in enzyme activity</li><li>K->A at 304: Loss of function</li><li>R->A at 332: Loss of function</li><li>R->A at 341: Induces a strong decrease in enzyme activity</li><li>K->A at 518: Has weak or no effect</li><li>D->A at 519: Has weak or no effect</li><li>L->A at 520: Has weak or no effect</li><li>S->A at 521: No effect</li><li>K->A at 522: No effect</li><li>T->A at 523: Has weak or no effect</li><li>L->A,T at 524: Induces a strong decrease in enzyme activity</li><li>L->A at 525: Induces a strong decrease in enzyme activity</li><li>L->T at 525: Has weak or no effect</li><li>R->A at 526: Has weak or no effect</li><li>K->A at 527: No effect</li><li>P->A at 528: Has weak or no effect</li><li>R->A at 529: No effect</li><li>L->A,T at 530: Induces a strong decrease in enzyme activity</li></ul>									1
Q9Y4H4	63940	<ul><li>A->D at 121: Restores G(i) alpha binding and GDI activity of the GoLoco 2 domain</li></ul>			<li>binding</li><li>GDI</li>	<li>GO:0005488</li><li>GO:0005092</li>					1
Q9Y4K4	11183	<ul><li>K->R at 49: Loss of kinase activity and ability to activate JNK family</li></ul>			kinase activity	GO:0016301			<li>Q966Y3</li><li>P92208</li>		1
Q9Y4P1	23192	<ul><li>C->S at 74: Complete loss of protease activity</li><li>W->A at 142: Strongly reduced protease activity</li><li>R->A at 229: Strongly reduced protease activity</li><li>D->A at 278: Complete loss of protease activity</li><li>H->A at 280: Complete loss of protease activity</li></ul>							<li>P19028</li><li>Q9QBZ5</li><li>P24107</li><li>Q9QBZ1</li><li>Q79666</li><li>P15833</li><li>P03362</li><li>P18042</li><li>Q8AII1</li><li>P03363</li><li>P04024</li><li>P04023</li><li>P10978</li><li>O93215</li><li>P26810</li><li>Q1A249</li><li>P03356</li><li>P03355</li><li>O41798</li><li>P20892</li><li>Q9Y6I0</li><li>P10210</li><li>Q9QBY3</li><li>P03353</li><li>P16901</li><li>Q74120</li><li>Q09SZ9</li><li>Q89928</li><li>Q73368</li><li>P84454</li><li>Q9WC63</li><li>P20825</li><li>Q9IDV9</li><li>P0C211</li><li>P0C210</li><li>P51518</li><li>Q4U0X6</li><li>P12451</li><li>P07570</li><li>P28936</li><li>O89940</li><li>P24740</li><li>P26809</li><li>P26808</li><li>Q0R5R3</li><li>Q0R5R2</li><li>P18802</li><li>P10394</li><li>P19561</li><li>P16423</li><li>P63119</li><li>P19560</li><li>Q75002</li><li>P04589</li><li>P04587</li><li>P04588</li><li>Q9QSR3</li><li>O91080</li><li>P16046</li><li>P17757</li><li>P12497</li><li>P12499</li><li>P12498</li><li>P03311</li><li>P20875</li><li>P20876</li><li>P10273</li><li>Q9WC54</li><li>P10272</li><li>P10271</li><li>P10270</li><li>P19199</li><li>P05962</li><li>P18096</li><li>P10265</li><li>P04584</li><li>P11227</li><li>P04585</li><li>Q76634</li><li>Q8I7P9</li><li>Q9Q720</li><li>P14078</li><li>P31822</li><li>P11365</li><li>P35963</li><li>P14074</li><li>P05959</li><li>P63131</li><li>P04323</li><li>P10274</li><li>P21407</li><li>O89290</li><li>P35956</li><li>P05960</li><li>P05961</li><li>Q1A267</li><li>P63122</li><li>P63123</li><li>P63124</li><li>P63125</li><li>P63120</li><li>P63121</li><li>P03366</li><li>P03367</li><li>P03369</li><li>P63127</li><li>P63128</li><li>P63129</li><li>Q77373</li><li>P03370</li><li>P27502</li><li>P21414</li>		1
Q9Y4X5	25820	<ul><li>QI->HV at 187-188: No loss of interaction with UBE2L3</li><li>I->A at 188: Loss of interaction with UBE2L3</li><li>C->A,H at 208: Loss of interaction with UBE2L3</li><li>Y->A at 258: No loss of interaction with UBE2L3</li></ul>							<li>Q3MHP1</li><li>P68036</li>		1
Q9Y572	11035	<ul><li>K->A at 50: Abolishes kinase activity</li><li>K->D at 50: Abolishes kinase activity</li></ul>			kinase activity	GO:0016301					1
Q9Y5A7	51667	<ul><li>A->V at 448: No effect on NEDD8-binding</li><li>L->A at 453: Partial inhibition of NEDD8-binding</li><li>L->A at 464: Partial inhibition of NEDD8-binding</li><li>L->A at 468: Partial inhibition of NEDD8-binding</li><li>L->A at 587: Suppression of NEDD8-binding; when associated with A-464; A-468 and A-591. Suppression of NEDD8-buster function; when associated with A-591</li><li>L->A at 591: Suppression of NEDD8-binding; when associated with A-464; A-468 and A-587. Suppression of NEDD8-buster function; when associated with A-587</li></ul>			binding	GO:0005488			<li>Q15843</li><li>Q9SHE7</li><li>P0C031</li><li>Q4PLJ0</li><li>P0C030</li><li>P61282</li><li>P0C032</li>		1
Q9Y5K5	51377	<ul><li>C->A at 88: Abolishes enzymatic activity</li></ul>									1
Q9Y5P4	10087	<ul><li>S->A at 132: Abolishes the phosphorylation. Strongly reduces the interaction with phosphatidylinositol 4-phosphate. Increases the ceramide transfer activity</li><li>D->A at 324: Impairs the endoplasmic reticulum-to-Golgi ceramide trafficking and abolishes the interaction with VAPA</li></ul>	phosphorylation	GO:0016310			endoplasmic reticulum	GO:0005783	<li>Q9P0L0</li><li>Q5R601</li>		1
Q9Y5Q5	10699	<ul><li>S->A at 985: Loss of activity</li></ul>									1
Q9Y5S9	9939	<ul><li>EE->RR at 82-83: Impaired nonsense-mediated decay activity</li><li>LDR->RDE at 106-108: Complete loss of nonsense-mediated decay activity</li><li>L->R at 118: Complete loss of nonsense-mediated decay activity</li><li>CF->KA at 149-150: Complete loss of nonsense-mediated decay activity</li></ul>									1
Q9Y5T5	10600	<ul><li>C->S at 205: Loss of enzyme activity</li></ul>									1
Q9Y5U4	51141	<ul><li>D->A at 149: Loss of ability to suppress the cleavage of SREBP2 and to accelerate the degradation of HMGCR</li></ul>							<li>P16393</li><li>Q60429</li><li>Q5R6N3</li><li>P00347</li><li>Q1W675</li><li>Q12772</li><li>Q29512</li><li>P04035</li><li>P09610</li>		1
Q9Y5Y6	6768	<ul><li>H->A at 656: Abolishes catalytic activity</li><li>D->A at 711: Abolishes catalytic activity</li><li>S->A at 805: Abolishes catalytic activity</li></ul>			catalytic activity	GO:0003824					1
Q9Y662	9953	<ul><li>K->A at 146: Reduces activity by 99.6%</li><li>K->A at 147: Reduces activity by 99.6%</li><li>R->E at 151: Reduces activity by 99.8%</li><li>E->Q at 155: Reduces activity by 17%</li><li>R->S at 158: Reduces activity by 44%</li><li>E->Q at 169: Reduces activity by 99.9%</li><li>H->F at 171: Loss of activity</li><li>D->N at 174: Reduces activity by 99%</li><li>R->E at 175: Reduces activity by 32%</li><li>K->A at 179: Reduces activity by 99.5%</li><li>K->A at 200: Reduces activity by 99.9%</li><li>Q->A at 240: Reduces activity by 99.6%</li><li>H->A at 347: No effect</li><li>K->A at 351: Reduces activity by 99.8%</li><li>K->A at 353: Reduces activity by 99.9%</li><li>R->E at 355: Reduces activity by 99.2%</li></ul>									1
Q9Y663	9955	<ul><li>K->A at 161: 99.6% loss of enzymatic activity</li><li>K->A at 162: 99.6% loss of enzymatic activity; no HSV1 entry activity</li><li>R->E at 166: 99.8% loss of enzymatic activity</li><li>E->Q at 170: 17% loss of enzymatic activity</li><li>R->S at 173: 44.1% loss of enzymatic activity</li><li>G->A at 182: No effect on enzymatic activity</li><li>E->Q at 184: 99.9% loss of enzymatic activity</li><li>H->F at 186: Abolishes enzymatic activity</li><li>D->N at 189: 99.1% loss of enzymatic activity</li><li>R->E at 190: 32% loss of enzymatic activity</li><li>K->A at 194: 99.5% loss of enzymatic activity</li><li>K->A at 215: 99.9% loss of enzymatic activity</li><li>S->A at 218: 23.3% loss of enzymatic activity</li><li>E->Q at 224: 47.6% loss of enzymatic activity</li><li>Q->A at 255: 99.6% loss of enzymatic activity</li><li>K->A at 259: 48.3% loss of enzymatic activity</li><li>I->A at 288: 65% loss of enzymatic activity</li><li>K->A at 293: 33.6% loss of enzymatic activity</li><li>H->A at 362: No effect on enzymatic activity</li><li>G->A at 365: 43% loss of enzymatic activity</li><li>K->A at 366: 99.8% loss of enzymatic activity</li><li>K->A at 368: 99.9% loss of enzymatic activity</li><li>R->E at 370: 99.2% loss of enzymatic activity</li></ul>							Q02887		1
Q9Y678	22820	<ul><li>W->S at 776: Loss of interaction with ZNF289/ARFGAP2</li></ul>									1
Q9Y691	10242	<ul><li>FIW->GGG at 2-4: Abolishes inactivation of KCNMA1 channel</li></ul>							<li>Q8AYS8</li><li>O18866</li><li>O18867</li><li>Q28204</li><li>Q28265</li><li>Q9BG98</li><li>Q12791</li>		1
Q9Y6B2	23741	<ul><li>L->S at 178: Abolishes RB1 binding</li><li>C->G at 180: Abolishes RB1 binding</li><li>E->Q at 182: Abolishes RB1 binding</li></ul>			binding	GO:0005488			P06400		1
Q9Y6E0	8428	<ul><li>T->A at 18: Loss of phosphorylation by PKA</li></ul>	phosphorylation	GO:0016310	PKA	GO:0004691					1
Q9Y6H6	10008	<ul><li>D->N at 90: Decreases current 4-fold in KCNH2/KCNE3 channel</li></ul>							<li>Q9Y6H6</li><li>Q9TSZ3</li><li>Q9PT84</li><li>O08703</li><li>Q12809</li><li>Q8WNY2</li><li>Q9TUI4</li>		1
Q9Y6I3	29924	<ul><li>S->A at 357: Abolishes phosphorylation by CDC2</li><li>S->D at 357: Abolishes phosphorylation by CDC2 and reduces REPS2 binding</li></ul>	phosphorylation	GO:0016310	binding	GO:0005488			<li>Q9W739</li><li>Q9DGA2</li><li>Q9DGA5</li><li>P19026</li><li>Q5RCH1</li><li>Q9DG98</li><li>P06493</li><li>P48734</li><li>P43290</li><li>P23111</li><li>Q8NFH8</li><li>P13863</li><li>Q04770</li><li>P52389</li><li>P15436</li><li>P24100</li><li>P51958</li><li>Q41639</li><li>P54119</li><li>P93101</li><li>Q9DGD3</li>		1
Q9Y6J0	23523	<ul><li>L->A,K,W at 2172: Abrogates binding to MEF2B</li></ul>			binding	GO:0005488			Q02080		1
Q9Y6J6	9992	<ul><li>K->H at 75: Increases tail current in KCNH2/KCNE2 channel</li></ul>							<li>Q9Y6J6</li><li>Q9TSZ3</li><li>Q9PT84</li><li>O08703</li><li>Q9BDR0</li><li>Q12809</li><li>Q8WNY2</li><li>Q9TUI4</li>		1
Q9Y6K0	10390	<ul><li>K->M at 138: Induces a reduction in both cholinephosphotransferase and ethanolaminephosphotransferase activities</li><li>N->G at 144: No effect</li><li>S->Q,C at 146: No effect</li><li>G->C,S,A at 156: Induces a reduction in cholinephosphotransferase activity and abolishes ethanolaminephosphotransferase activity</li><li>T->A at 214: Alters the profile of diacylglycerol utilization and results in modest reduction in enzyme activity</li><li>E->A,D at 215: Induces a strong reduction in enzyme activity without altering diacylglycerol specificity</li><li>E->Q at 215: Induces a strong reduction in enzyme activity and alters diacylglycerol specificity</li><li>V->A at 216: Alters the profile of diacylglycerol utilization and results in modest reduction in enzyme activity</li><li>I->A at 221: Alters the profile of diacylglycerol utilization and results in modest reduction in enzyme activity</li><li>L->A at 226: Does not affect either the enzyme activity or the diacylglycerol specificity</li><li>V->A at 228: Does not affect either the enzyme activity or the diacylglycerol specificity</li></ul>							P22140		1
Q9Y6K9	8517	<ul><li>S->A at 68: Increases formation of homodimers</li><li>S->E at 68: Abolishes interaction with IKBKB; abolishes TNF-alpha induced NF-kappa-B act