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Q15181

- IPYR_HUMAN

UniProt

Q15181 - IPYR_HUMAN

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Protein

Inorganic pyrophosphatase

Gene

PPA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Diphosphate + H2O = 2 phosphate.

Cofactori

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi116 – 1161Magnesium 1By similarity
Metal bindingi121 – 1211Magnesium 1By similarity
Metal bindingi121 – 1211Magnesium 2By similarity
Metal bindingi153 – 1531Magnesium 1By similarity

GO - Molecular functioni

  1. inorganic diphosphatase activity Source: Reactome
  2. magnesium ion binding Source: InterPro

GO - Biological processi

  1. diphosphate metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. phosphate-containing compound metabolic process Source: ProtInc
  4. tRNA aminoacylation for protein translation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi3.6.1.1. 2681.
ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Inorganic pyrophosphatase (EC:3.6.1.1)
Alternative name(s):
Pyrophosphate phospho-hydrolase
Short name:
PPase
Gene namesi
Name:PPA1
Synonyms:IOPPP, PP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:9226. PPA1.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33550.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 289288Inorganic pyrophosphatasePRO_0000137567Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Modified residuei57 – 571N6-acetyllysine1 Publication
Modified residuei228 – 2281N6-acetyllysine1 Publication
Modified residuei250 – 2501Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15181.
PaxDbiQ15181.
PeptideAtlasiQ15181.
PRIDEiQ15181.

2D gel databases

REPRODUCTION-2DPAGEIPI00015018.

PTM databases

PhosphoSiteiQ15181.

Expressioni

Tissue specificityi

Expressed ubiquitously.1 Publication

Gene expression databases

BgeeiQ15181.
CleanExiHS_PPA1.
ExpressionAtlasiQ15181. baseline and differential.
GenevestigatoriQ15181.

Organism-specific databases

HPAiHPA019878.
HPA020096.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi111460. 21 interactions.
IntActiQ15181. 9 interactions.
MINTiMINT-3030968.
STRINGi9606.ENSP00000362329.

Structurei

3D structure databases

ProteinModelPortaliQ15181.
SMRiQ15181. Positions 4-284.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PPase family.Curated

Phylogenomic databases

eggNOGiCOG0221.
HOGENOMiHOG000195569.
HOVERGENiHBG000491.
InParanoidiQ15181.
KOiK01507.
OMAiWFYYQKN.
OrthoDBiEOG7R2BKH.
PhylomeDBiQ15181.
TreeFamiTF300887.

Family and domain databases

Gene3Di3.90.80.10. 1 hit.
InterProiIPR008162. Pyrophosphatase.
[Graphical view]
PANTHERiPTHR10286. PTHR10286. 1 hit.
PfamiPF00719. Pyrophosphatase. 1 hit.
[Graphical view]
SUPFAMiSSF50324. SSF50324. 1 hit.
PROSITEiPS00387. PPASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q15181 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGFSTEERA APFSLEYRVF LKNEKGQYIS PFHDIPIYAD KDVFHMVVEV
60 70 80 90 100
PRWSNAKMEI ATKDPLNPIK QDVKKGKLRY VANLFPYKGY IWNYGAIPQT
110 120 130 140 150
WEDPGHNDKH TGCCGDNDPI DVCEIGSKVC ARGEIIGVKV LGILAMIDEG
160 170 180 190 200
ETDWKVIAIN VDDPDAANYN DINDVKRLKP GYLEATVDWF RRYKVPDGKP
210 220 230 240 250
ENEFAFNAEF KDKDFAIDII KSTHDHWKAL VTKKTNGKGI SCMNTTLSES
260 270 280
PFKCDPDAAR AIVDALPPPC ESACTVPTDV DKWFHHQKN
Length:289
Mass (Da):32,660
Last modified:May 30, 2000 - v2
Checksum:iE3973C9E6F8CA5CD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121P → A in AAD24964. 1 PublicationCurated
Sequence conflicti84 – 841L → I in CAA88494. 1 PublicationCurated
Sequence conflicti96 – 972AI → TL in CAA88494. 1 PublicationCurated
Sequence conflicti105 – 11410GHNDKHTGCC → HEKDKSTNCF in CAA88494. 1 PublicationCurated
Sequence conflicti129 – 14012VCARG…IGVKV → ILSCGEVIHVKI in CAA88494. 1 PublicationCuratedAdd
BLAST
Sequence conflicti146 – 1461M → L in CAA88494. 1 PublicationCurated
Sequence conflicti156 – 1561V → L in CAA88494. 1 PublicationCurated
Sequence conflicti161 – 1622VD → AN in CAA88494. 1 PublicationCurated
Sequence conflicti165 – 1739DAANYNDIN → EASKFHDID in CAA88494. 1 PublicationCurated
Sequence conflicti177 – 1782RL → KF in CAA88494. 1 PublicationCurated
Sequence conflicti187 – 1882VD → LN in CAA88494. 1 PublicationCurated
Sequence conflicti192 – 1921R → L in CAA88494. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571K → N in a breast cancer sample; somatic mutation. 1 Publication
VAR_036358

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS7299.1.
RefSeqiNP_066952.1. NM_021129.3.
UniGeneiHs.437403.

Genome annotation databases

EnsembliENST00000373232; ENSP00000362329; ENSG00000180817.
GeneIDi5464.
KEGGihsa:5464.
UCSCiuc001jqv.1. human.

Polymorphism databases

DMDMi8247940.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS7299.1.
RefSeqi NP_066952.1. NM_021129.3.
UniGenei Hs.437403.

3D structure databases

ProteinModelPortali Q15181.
SMRi Q15181. Positions 4-284.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111460. 21 interactions.
IntActi Q15181. 9 interactions.
MINTi MINT-3030968.
STRINGi 9606.ENSP00000362329.

PTM databases

PhosphoSitei Q15181.

Polymorphism databases

DMDMi 8247940.

2D gel databases

REPRODUCTION-2DPAGE IPI00015018.

Proteomic databases

MaxQBi Q15181.
PaxDbi Q15181.
PeptideAtlasi Q15181.
PRIDEi Q15181.

Protocols and materials databases

DNASUi 5464.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373232 ; ENSP00000362329 ; ENSG00000180817 .
GeneIDi 5464.
KEGGi hsa:5464.
UCSCi uc001jqv.1. human.

Organism-specific databases

CTDi 5464.
GeneCardsi GC10M071962.
H-InvDB HIX0032502.
HGNCi HGNC:9226. PPA1.
HPAi HPA019878.
HPA020096.
MIMi 179030. gene.
neXtProti NX_Q15181.
PharmGKBi PA33550.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0221.
HOGENOMi HOG000195569.
HOVERGENi HBG000491.
InParanoidi Q15181.
KOi K01507.
OMAi WFYYQKN.
OrthoDBi EOG7R2BKH.
PhylomeDBi Q15181.
TreeFami TF300887.

Enzyme and pathway databases

BRENDAi 3.6.1.1. 2681.
Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

Miscellaneous databases

ChiTaRSi PPA1. human.
GenomeRNAii 5464.
NextBioi 21148.
PROi Q15181.
SOURCEi Search...

Gene expression databases

Bgeei Q15181.
CleanExi HS_PPA1.
ExpressionAtlasi Q15181. baseline and differential.
Genevestigatori Q15181.

Family and domain databases

Gene3Di 3.90.80.10. 1 hit.
InterProi IPR008162. Pyrophosphatase.
[Graphical view ]
PANTHERi PTHR10286. PTHR10286. 1 hit.
Pfami PF00719. Pyrophosphatase. 1 hit.
[Graphical view ]
SUPFAMi SSF50324. SSF50324. 1 hit.
PROSITEi PS00387. PPASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-57.

Entry informationi

Entry nameiIPYR_HUMAN
AccessioniPrimary (citable) accession number: Q15181
Secondary accession number(s): Q2M348
, Q5SQT7, Q6P7P4, Q9UQJ5, Q9Y5B1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2000
Last modified: October 29, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3