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Q15181

- IPYR_HUMAN

UniProt

Q15181 - IPYR_HUMAN

Protein

Inorganic pyrophosphatase

Gene

PPA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    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

    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

    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

    ArrayExpressiQ15181.
    BgeeiQ15181.
    CleanExiHS_PPA1.
    GenevestigatoriQ15181.

    Organism-specific databases

    HPAiHPA019878.
    HPA020096.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi111460. 20 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.

    Q15181-1 [UniParc]FASTAAdd to Basket

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    MSGFSTEERA APFSLEYRVF LKNEKGQYIS PFHDIPIYAD KDVFHMVVEV    50
    PRWSNAKMEI ATKDPLNPIK QDVKKGKLRY VANLFPYKGY IWNYGAIPQT 100
    WEDPGHNDKH TGCCGDNDPI DVCEIGSKVC ARGEIIGVKV LGILAMIDEG 150
    ETDWKVIAIN VDDPDAANYN DINDVKRLKP GYLEATVDWF RRYKVPDGKP 200
    ENEFAFNAEF KDKDFAIDII KSTHDHWKAL VTKKTNGKGI SCMNTTLSES 250
    PFKCDPDAAR AIVDALPPPC ESACTVPTDV DKWFHHQKN 289
    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. 20 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

    ArrayExpressi Q15181.
    Bgeei Q15181.
    CleanExi HS_PPA1.
    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

    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 1, 2014
    This is version 146 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