MASCOT Search Results
Protein View: IPYR_HUMAN
Inorganic pyrophosphatase OS=Homo sapiens GN=PPA1 PE=1 SV=2
AC Q15181; Q2M348; Q5SQT7; Q6P7P4; Q9UQJ5; Q9Y5B1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 09-DEC-2015, entry version 158.
DE RecName: Full=Inorganic pyrophosphatase;
DE EC=3.6.1.1;
DE AltName: Full=Pyrophosphate phospho-hydrolase;
DE Short=PPase;
GN Name=PPA1; Synonyms=IOPPP, PP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=10542310; DOI=10.1016/S0167-4781(99)00175-X;
RA Fairchild T.A., Patejunas G.;
RT "Cloning and expression profile of human inorganic pyrophosphatase.";
RL Biochim. Biophys. Acta 1447:133-136(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Saito T., Hattori A., Miyajima N.;
RT "Putative inorganic pyrophosphatase.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kanni L., Johansson M., Karlsson A.;
RT "Cloning of a human inorganic pyrophosphatase cDNA.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Dai F.Y., Yu L., Hu P.R., Xin Y.R., Xu Y.F., Zhao S.Y.;
RT "Cloning and characterization of a novel human cDNA homology to bovine
RT inorganic pyrophosphatase mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lymph, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-286.
RA Rumsfeld J., Ziegelbauer K., Spaltmann F.;
RT "Cloning, expression, affinity purification and characterization of
RT polyhistidine-tagged cytosolic Saccharomyces cerevisiae and human
RT inorganic pyrophosphatases for differential screening of compounds for
RT antifungal activity.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PROTEIN SEQUENCE OF 10-18; 26-41; 58-70; 80-88; 110-128; 140-191;
RP 193-221 AND 239-253, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 83-196.
RA Lacroix J., Vigneron M., Kedinger C.;
RT "Partial sequence of the human inorganic pyrophosphatase.";
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57 AND LYS-228, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.M111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA Meinnel T., Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA Wang L., Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT liver phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-57.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- CATALYTIC ACTIVITY: Diphosphate + H(2)O = 2 phosphate.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 4 Mg(2+) ions per subunit. Other metal ions can support
CC activity, but at a lower rate. Two Mg(2+) ions are required for
CC the activation of the enzyme and are present before substrate
CC binds, two additional Mg(2+) ions form complexes with substrate
CC and product. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC {ECO:0000269|PubMed:10542310}.
CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000305}.
DR EMBL; AF154065; AAD34643.1; -; mRNA.
DR EMBL; AB026723; BAA84702.1; -; mRNA.
DR EMBL; AF217186; AAG36780.1; -; mRNA.
DR EMBL; AF092439; AAP97214.1; -; mRNA.
DR EMBL; AF119665; AAF17222.1; -; mRNA.
DR EMBL; AL731540; CAI13692.1; -; Genomic_DNA.
DR EMBL; BC001022; AAH01022.3; -; mRNA.
DR EMBL; BC061581; AAH61581.2; -; mRNA.
DR EMBL; BC105034; AAI05035.1; -; mRNA.
DR EMBL; BC105036; AAI05037.1; -; mRNA.
DR EMBL; BC107882; AAI07883.1; -; mRNA.
DR EMBL; AF108211; AAD24964.1; -; mRNA.
DR EMBL; Z48605; CAA88494.1; -; mRNA.
DR CCDS; CCDS7299.1; -.
DR RefSeq; NP_066952.1; NM_021129.3.
DR UniGene; Hs.437403; -.
DR ProteinModelPortal; Q15181; -.
DR SMR; Q15181; 4-284.
DR BioGrid; 111460; 33.
DR IntAct; Q15181; 9.
DR MINT; MINT-3030968; -.
DR STRING; 9606.ENSP00000362329; -.
DR PhosphoSite; Q15181; -.
DR BioMuta; PPA1; -.
DR DMDM; 8247940; -.
DR REPRODUCTION-2DPAGE; IPI00015018; -.
DR PaxDb; Q15181; -.
DR PeptideAtlas; Q15181; -.
DR PRIDE; Q15181; -.
DR DNASU; 5464; -.
DR Ensembl; ENST00000373232; ENSP00000362329; ENSG00000180817.
DR GeneID; 5464; -.
DR KEGG; hsa:5464; -.
DR UCSC; uc001jqv.1; human.
DR CTD; 5464; -.
DR GeneCards; PPA1; -.
DR H-InvDB; HIX0032502; -.
DR HGNC; HGNC:9226; PPA1.
DR HPA; HPA019878; -.
DR HPA; HPA020096; -.
DR MIM; 179030; gene.
DR neXtProt; NX_Q15181; -.
DR PharmGKB; PA33550; -.
DR eggNOG; KOG1626; Eukaryota.
DR eggNOG; COG0221; LUCA.
DR HOGENOM; HOG000195569; -.
DR HOVERGEN; HBG000491; -.
DR InParanoid; Q15181; -.
DR KO; K01507; -.
DR OMA; GHKDENT; -.
DR OrthoDB; EOG7R2BKH; -.
DR PhylomeDB; Q15181; -.
DR TreeFam; TF300887; -.
DR BRENDA; 3.6.1.1; 2681.
DR Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation.
DR ChiTaRS; PPA1; human.
DR GenomeRNAi; 5464; -.
DR NextBio; 21148; -.
DR PRO; PR:Q15181; -.
DR Proteomes; UP000005640; Chromosome 10.
DR Bgee; Q15181; -.
DR CleanEx; HS_PPA1; -.
DR ExpressionAtlas; Q15181; baseline and differential.
DR Genevisible; Q15181; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0004427; F:inorganic diphosphatase activity; EXP:Reactome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0071344; P:diphosphate metabolic process; TAS:Reactome.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; TAS:ProtInc.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
DR Gene3D; 3.90.80.10; -; 1.
DR InterPro; IPR008162; Pyrophosphatase.
DR PANTHER; PTHR10286; PTHR10286; 1.
DR Pfam; PF00719; Pyrophosphatase; 1.
DR SUPFAM; SSF50324; SSF50324; 1.
DR PROSITE; PS00387; PPASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Magnesium; Metal-binding; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
FT ECO:0000244|PubMed:22223895,
FT ECO:0000244|PubMed:22814378}.
FT CHAIN 2 289 Inorganic pyrophosphatase.
FT /FTId=PRO_0000137567.
FT METAL 116 116 Magnesium 1. {ECO:0000250}.
FT METAL 121 121 Magnesium 1. {ECO:0000250}.
FT METAL 121 121 Magnesium 2. {ECO:0000250}.
FT METAL 153 153 Magnesium 1. {ECO:0000250}.
FT MOD_RES 2 2 N-acetylserine.
FT {ECO:0000244|PubMed:19413330,
FT ECO:0000244|PubMed:22223895,
FT ECO:0000244|PubMed:22814378}.
FT MOD_RES 57 57 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 228 228 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 250 250 Phosphoserine.
FT {ECO:0000244|PubMed:20068231}.
FT VARIANT 57 57 K -> N (in a breast cancer sample;
FT somatic mutation).
FT {ECO:0000269|PubMed:16959974}.
FT /FTId=VAR_036358.
FT CONFLICT 12 12 P -> A (in Ref. 8; AAD24964).
FT {ECO:0000305}.
FT CONFLICT 84 84 L -> I (in Ref. 10; CAA88494).
FT {ECO:0000305}.
FT CONFLICT 96 97 AI -> TL (in Ref. 10; CAA88494).
FT {ECO:0000305}.
FT CONFLICT 105 114 GHNDKHTGCC -> HEKDKSTNCF (in Ref. 10;
FT CAA88494). {ECO:0000305}.
FT CONFLICT 129 140 VCARGEIIGVKV -> ILSCGEVIHVKI (in Ref. 10;
FT CAA88494). {ECO:0000305}.
FT CONFLICT 146 146 M -> L (in Ref. 10; CAA88494).
FT {ECO:0000305}.
FT CONFLICT 156 156 V -> L (in Ref. 10; CAA88494).
FT {ECO:0000305}.
FT CONFLICT 161 162 VD -> AN (in Ref. 10; CAA88494).
FT {ECO:0000305}.
FT CONFLICT 165 173 DAANYNDIN -> EASKFHDID (in Ref. 10;
FT CAA88494). {ECO:0000305}.
FT CONFLICT 177 178 RL -> KF (in Ref. 10; CAA88494).
FT {ECO:0000305}.
FT CONFLICT 187 188 VD -> LN (in Ref. 10; CAA88494).
FT {ECO:0000305}.
FT CONFLICT 192 192 R -> L (in Ref. 10; CAA88494).
FT {ECO:0000305}.
SQ SEQUENCE 289 AA; 32660 MW; E3973C9E6F8CA5CD CRC64;
MSGFSTEERA APFSLEYRVF LKNEKGQYIS PFHDIPIYAD KDVFHMVVEV PRWSNAKMEI
ATKDPLNPIK QDVKKGKLRY VANLFPYKGY IWNYGAIPQT WEDPGHNDKH TGCCGDNDPI
DVCEIGSKVC ARGEIIGVKV LGILAMIDEG ETDWKVIAIN VDDPDAANYN DINDVKRLKP
GYLEATVDWF RRYKVPDGKP ENEFAFNAEF KDKDFAIDII KSTHDHWKAL VTKKTNGKGI
SCMNTTLSES PFKCDPDAAR AIVDALPPPC ESACTVPTDV DKWFHHQKN