Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q15181 (IPYR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inorganic pyrophosphatase

EC=3.6.1.1
Alternative name(s):
Pyrophosphate phospho-hydrolase
Short name=PPase
Gene names
Name:PPA1
Synonyms:IOPPP, PP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length289 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Diphosphate + H2O = 2 phosphate.

Cofactor

Binds 4 magnesium ions per subunit. Other metal ions can support activity, but at a lower rate. Two magnesium ions are required for the activation of the enzyme and are present before substrate binds, two additional magnesium ions form complexes with substrate and product By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Expressed ubiquitously. Ref.1

Sequence similarities

Belongs to the PPase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 289288Inorganic pyrophosphatase
PRO_0000137567

Sites

Metal binding1161Magnesium 1 By similarity
Metal binding1211Magnesium 1 By similarity
Metal binding1211Magnesium 2 By similarity
Metal binding1531Magnesium 1 By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.11 Ref.15 Ref.16
Modified residue571N6-acetyllysine Ref.12
Modified residue2281N6-acetyllysine Ref.12
Modified residue2501Phosphoserine Ref.13

Natural variations

Natural variant571K → N in a breast cancer sample; somatic mutation. Ref.17
VAR_036358

Experimental info

Sequence conflict121P → A in AAD24964. Ref.8
Sequence conflict841L → I in CAA88494. Ref.10
Sequence conflict96 – 972AI → TL in CAA88494. Ref.10
Sequence conflict105 – 11410GHNDKHTGCC → HEKDKSTNCF in CAA88494. Ref.10
Sequence conflict129 – 14012VCARG…IGVKV → ILSCGEVIHVKI in CAA88494. Ref.10
Sequence conflict1461M → L in CAA88494. Ref.10
Sequence conflict1561V → L in CAA88494. Ref.10
Sequence conflict161 – 1622VD → AN in CAA88494. Ref.10
Sequence conflict165 – 1739DAANYNDIN → EASKFHDID in CAA88494. Ref.10
Sequence conflict177 – 1782RL → KF in CAA88494. Ref.10
Sequence conflict187 – 1882VD → LN in CAA88494. Ref.10
Sequence conflict1921R → L in CAA88494. Ref.10

Sequences

Sequence LengthMass (Da)Tools
Q15181 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: E3973C9E6F8CA5CD

FASTA28932,660
        10         20         30         40         50         60 
MSGFSTEERA APFSLEYRVF LKNEKGQYIS PFHDIPIYAD KDVFHMVVEV PRWSNAKMEI 

        70         80         90        100        110        120 
ATKDPLNPIK QDVKKGKLRY VANLFPYKGY IWNYGAIPQT WEDPGHNDKH TGCCGDNDPI 

       130        140        150        160        170        180 
DVCEIGSKVC ARGEIIGVKV LGILAMIDEG ETDWKVIAIN VDDPDAANYN DINDVKRLKP 

       190        200        210        220        230        240 
GYLEATVDWF RRYKVPDGKP ENEFAFNAEF KDKDFAIDII KSTHDHWKAL VTKKTNGKGI 

       250        260        270        280 
SCMNTTLSES PFKCDPDAAR AIVDALPPPC ESACTVPTDV DKWFHHQKN 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression profile of human inorganic pyrophosphatase."
Fairchild T.A., Patejunas G.
Biochim. Biophys. Acta 1447:133-136(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Heart.
[2]"Putative inorganic pyrophosphatase."
Saito T., Hattori A., Miyajima N.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"Cloning of a human inorganic pyrophosphatase cDNA."
Kanni L., Johansson M., Karlsson A.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Cloning and characterization of a novel human cDNA homology to bovine inorganic pyrophosphatase mRNA."
Dai F.Y., Yu L., Hu P.R., Xin Y.R., Xu Y.F., Zhao S.Y.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Adrenal gland.
[6]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Lymph and Uterus.
[8]"Cloning, expression, affinity purification and characterization of polyhistidine-tagged cytosolic Saccharomyces cerevisiae and human inorganic pyrophosphatases for differential screening of compounds for antifungal activity."
Rumsfeld J., Ziegelbauer K., Spaltmann F.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-286.
[9]Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 10-18; 26-41; 58-70; 80-88; 110-128; 140-191; 193-221 AND 239-253, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[10]"Partial sequence of the human inorganic pyrophosphatase."
Lacroix J., Vigneron M., Kedinger C.
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 83-196.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57 AND LYS-228, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-57.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF154065 mRNA. Translation: AAD34643.1.
AB026723 mRNA. Translation: BAA84702.1.
AF217186 mRNA. Translation: AAG36780.1.
AF092439 mRNA. Translation: AAP97214.1.
AF119665 mRNA. Translation: AAF17222.1.
AL731540 Genomic DNA. Translation: CAI13692.1.
BC001022 mRNA. Translation: AAH01022.3.
BC061581 mRNA. Translation: AAH61581.2.
BC105034 mRNA. Translation: AAI05035.1.
BC105036 mRNA. Translation: AAI05037.1.
BC107882 mRNA. Translation: AAI07883.1.
AF108211 mRNA. Translation: AAD24964.1.
Z48605 mRNA. Translation: CAA88494.1.
RefSeqNP_066952.1. NM_021129.3.
UniGeneHs.437403.

3D structure databases

ProteinModelPortalQ15181.
SMRQ15181. Positions 4-284.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111460. 20 interactions.
IntActQ15181. 9 interactions.
MINTMINT-3030968.
STRING9606.ENSP00000362329.

PTM databases

PhosphoSiteQ15181.

Polymorphism databases

DMDM8247940.

2D gel databases

REPRODUCTION-2DPAGEIPI00015018.

Proteomic databases

PaxDbQ15181.
PeptideAtlasQ15181.
PRIDEQ15181.

Protocols and materials databases

DNASU5464.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373232; ENSP00000362329; ENSG00000180817.
GeneID5464.
KEGGhsa:5464.
UCSCuc001jqv.1. human.

Organism-specific databases

CTD5464.
GeneCardsGC10M071962.
H-InvDBHIX0032502.
HGNCHGNC:9226. PPA1.
HPAHPA019878.
HPA020096.
MIM179030. gene.
neXtProtNX_Q15181.
PharmGKBPA33550.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0221.
HOGENOMHOG000195569.
HOVERGENHBG000491.
InParanoidQ15181.
KOK01507.
OMAWFYYQKN.
OrthoDBEOG7R2BKH.
PhylomeDBQ15181.
TreeFamTF300887.

Enzyme and pathway databases

BRENDA3.6.1.1. 2681.
ReactomeREACT_21259. Pyrophosphate hydrolysis.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ15181.
BgeeQ15181.
CleanExHS_PPA1.
GenevestigatorQ15181.

Family and domain databases

Gene3D3.90.80.10. 1 hit.
InterProIPR008162. Pyrophosphatase.
[Graphical view]
PANTHERPTHR10286. PTHR10286. 1 hit.
PfamPF00719. Pyrophosphatase. 1 hit.
[Graphical view]
SUPFAMSSF50324. SSF50324. 1 hit.
PROSITEPS00387. PPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPA1. human.
GenomeRNAi5464.
NextBio21148.
PROQ15181.
SOURCESearch...

Entry information

Entry nameIPYR_HUMAN
AccessionPrimary (citable) accession number: Q15181
Secondary accession number(s): Q2M348 expand/collapse secondary AC list , Q5SQT7, Q6P7P4, Q9UQJ5, Q9Y5B1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2000
Last modified: April 16, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM