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Protein

Phosphoethanolamine/phosphocholine phosphatase

Gene

PHOSPHO1

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

Functioni

Phosphatase that has a high activity toward phosphoethanolamine (PEA) and phosphocholine (PCho). Involved in the generation of inorganic phosphate for bone mineralization.

Catalytic activityi

O-phosphoethanolamine + H2O = ethanolamine + phosphate.1 Publication
Phosphocholine + H2O = choline + phosphate.1 Publication

Cofactori

Mg2+1 Publication

Kineticsi

  1. KM=3 µM for PEA1 Publication
  2. KM=11.4 µM for PCho1 Publication

    pH dependencei

    Optimum pH is 6.7.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei32 – 321NucleophileCurated
    Metal bindingi32 – 321MagnesiumCurated
    Active sitei34 – 341Proton donorBy similarity
    Metal bindingi34 – 341MagnesiumBy similarity
    Binding sitei43 – 431SubstrateCurated
    Binding sitei123 – 1231SubstrateCurated
    Metal bindingi203 – 2031MagnesiumCurated

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Mineral balance

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS16266-MONOMER.
    BRENDAi3.1.3.75. 2681.
    ReactomeiR-HSA-1483191. Synthesis of PC.
    R-HSA-1483213. Synthesis of PE.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoethanolamine/phosphocholine phosphatase (EC:3.1.3.75)
    Gene namesi
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:16815. PHOSPHO1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi32 – 321D → N: Abolishes phosphatase activity. 1 Publication
    Mutagenesisi43 – 431D → N: Strongly reduces reactivity toward PEA and PCho substrates. Abolishes phosphatase activity; when associated with N-123. 1 Publication
    Mutagenesisi123 – 1231D → N: Strongly reduces reactivity toward PEA and PCho substrates. Abolishes phosphatase activity; when associated with N-43. 1 Publication
    Mutagenesisi203 – 2031D → S: Abolishes phosphatase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA33276.

    Chemistry

    ChEMBLiCHEMBL6113.
    DrugBankiDB00122. Choline.

    Polymorphism and mutation databases

    BioMutaiPHOSPHO1.
    DMDMi74715842.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 267267Phosphoethanolamine/phosphocholine phosphatasePRO_0000068829Add
    BLAST

    Proteomic databases

    PaxDbiQ8TCT1.
    PeptideAtlasiQ8TCT1.
    PRIDEiQ8TCT1.

    PTM databases

    DEPODiQ8TCT1.
    iPTMnetiQ8TCT1.
    PhosphoSiteiQ8TCT1.

    Expressioni

    Tissue specificityi

    Expressed at sites of mineralization in bone and cartilage. Highly expressed in osteoblast cell line SaOS-2 which produces a mineralized matrix, but not in MG-63 cell line, which do not mineralize.1 Publication

    Gene expression databases

    BgeeiQ8TCT1.
    CleanExiHS_PHOSPHO1.
    ExpressionAtlasiQ8TCT1. baseline and differential.
    GenevisibleiQ8TCT1. HS.

    Organism-specific databases

    HPAiHPA053016.

    Interactioni

    Protein-protein interaction databases

    BioGridi127819. 4 interactions.
    STRINGi9606.ENSP00000406909.

    Chemistry

    BindingDBiQ8TCT1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8TCT1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG3120. Eukaryota.
    ENOG4111NAQ. LUCA.
    GeneTreeiENSGT00390000007741.
    HOGENOMiHOG000231038.
    HOVERGENiHBG080058.
    InParanoidiQ8TCT1.
    KOiK06124.
    OMAiSPGMGDL.
    OrthoDBiEOG7BZVTZ.
    PhylomeDBiQ8TCT1.
    TreeFamiTF300112.

    Family and domain databases

    Gene3Di3.40.50.1000. 1 hit.
    InterProiIPR023214. HAD-like_dom.
    IPR006383. HAD-SF_hydro_IB_PSP-like.
    IPR016965. Pase_PHOSPHO-typ.
    IPR006384. PyrdxlP_Pase-rel.
    [Graphical view]
    PfamiPF06888. Put_Phosphatase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF031051. PyrdxlP_Pase_PHOSPHO2. 1 hit.
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01489. DKMTPPase-SF. 1 hit.
    TIGR01488. HAD-SF-IB. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q8TCT1-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MSGCFPVSGL RCLSRDGRMA AQGAPRFLLT FDFDETIVDE NSDDSIVRAA
    60 70 80 90 100
    PGQRLPESLR ATYREGFYNE YMQRVFKYLG EQGVRPRDLS AIYEAIPLSP
    110 120 130 140 150
    GMSDLLQFVA KQGACFEVIL ISDANTFGVE SSLRAAGHHS LFRRILSNPS
    160 170 180 190 200
    GPDARGLLAL RPFHTHSCAR CPANMCKHKV LSDYLRERAH DGVHFERLFY
    210 220 230 240 250
    VGDGANDFCP MGLLAGGDVA FPRRGYPMHR LIQEAQKAEP SSFRASVVPW
    260
    ETAADVRLHL QQVLKSC
    Length:267
    Mass (Da):29,713
    Last modified:June 1, 2002 - v1
    Checksum:i539F65C749D39E81
    GO
    Isoform 2 (identifier: Q8TCT1-2) [UniParc]FASTAAdd to basket

    Also known as: PHOSPHO1-3a

    The sequence of this isoform differs from the canonical sequence as follows:
         1-15: MSGCFPVSGLRCLSR → MCQRLWPANQPLPGGLLPRPLSLAPSSSSSCCSPPCSQ

    Show »
    Length:290
    Mass (Da):32,068
    Checksum:iE7E5C497A540C458
    GO
    Isoform 3 (identifier: Q8TCT1-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-15: MSGCFPVSGLRCLSR → MCQRLWPWPANQPLPGGLLPRPLSLAPSSSSSCCSPPCSQ

    Note: No experimental confirmation available.
    Show »
    Length:292
    Mass (Da):32,351
    Checksum:i8D7E3926D78350B5
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1515MSGCF…RCLSR → MCQRLWPANQPLPGGLLPRP LSLAPSSSSSCCSPPCSQ in isoform 2. 1 PublicationVSP_040624Add
    BLAST
    Alternative sequencei1 – 1515MSGCF…RCLSR → MCQRLWPWPANQPLPGGLLP RPLSLAPSSSSSCCSPPCSQ in isoform 3. 1 PublicationVSP_045709Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ457189 mRNA. Translation: CAD29803.1.
    AC004797 Genomic DNA. No translation available.
    BC029931 mRNA. No translation available.
    BC117187 mRNA. Translation: AAI17188.1.
    CCDSiCCDS11547.1. [Q8TCT1-1]
    CCDS45726.1. [Q8TCT1-3]
    RefSeqiNP_001137276.1. NM_001143804.1. [Q8TCT1-3]
    NP_848595.1. NM_178500.3. [Q8TCT1-1]
    XP_005257166.1. XM_005257109.2. [Q8TCT1-1]
    UniGeneiHs.405607.

    Genome annotation databases

    EnsembliENST00000310544; ENSP00000311925; ENSG00000173868. [Q8TCT1-1]
    ENST00000413580; ENSP00000406909; ENSG00000173868. [Q8TCT1-3]
    ENST00000514112; ENSP00000427694; ENSG00000173868. [Q8TCT1-3]
    GeneIDi162466.
    KEGGihsa:162466.
    UCSCiuc002ios.2. human. [Q8TCT1-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ457189 mRNA. Translation: CAD29803.1.
    AC004797 Genomic DNA. No translation available.
    BC029931 mRNA. No translation available.
    BC117187 mRNA. Translation: AAI17188.1.
    CCDSiCCDS11547.1. [Q8TCT1-1]
    CCDS45726.1. [Q8TCT1-3]
    RefSeqiNP_001137276.1. NM_001143804.1. [Q8TCT1-3]
    NP_848595.1. NM_178500.3. [Q8TCT1-1]
    XP_005257166.1. XM_005257109.2. [Q8TCT1-1]
    UniGeneiHs.405607.

    3D structure databases

    ProteinModelPortaliQ8TCT1.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi127819. 4 interactions.
    STRINGi9606.ENSP00000406909.

    Chemistry

    BindingDBiQ8TCT1.
    ChEMBLiCHEMBL6113.
    DrugBankiDB00122. Choline.

    PTM databases

    DEPODiQ8TCT1.
    iPTMnetiQ8TCT1.
    PhosphoSiteiQ8TCT1.

    Polymorphism and mutation databases

    BioMutaiPHOSPHO1.
    DMDMi74715842.

    Proteomic databases

    PaxDbiQ8TCT1.
    PeptideAtlasiQ8TCT1.
    PRIDEiQ8TCT1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000310544; ENSP00000311925; ENSG00000173868. [Q8TCT1-1]
    ENST00000413580; ENSP00000406909; ENSG00000173868. [Q8TCT1-3]
    ENST00000514112; ENSP00000427694; ENSG00000173868. [Q8TCT1-3]
    GeneIDi162466.
    KEGGihsa:162466.
    UCSCiuc002ios.2. human. [Q8TCT1-1]

    Organism-specific databases

    CTDi162466.
    GeneCardsiPHOSPHO1.
    HGNCiHGNC:16815. PHOSPHO1.
    HPAiHPA053016.
    neXtProtiNX_Q8TCT1.
    PharmGKBiPA33276.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG3120. Eukaryota.
    ENOG4111NAQ. LUCA.
    GeneTreeiENSGT00390000007741.
    HOGENOMiHOG000231038.
    HOVERGENiHBG080058.
    InParanoidiQ8TCT1.
    KOiK06124.
    OMAiSPGMGDL.
    OrthoDBiEOG7BZVTZ.
    PhylomeDBiQ8TCT1.
    TreeFamiTF300112.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS16266-MONOMER.
    BRENDAi3.1.3.75. 2681.
    ReactomeiR-HSA-1483191. Synthesis of PC.
    R-HSA-1483213. Synthesis of PE.

    Miscellaneous databases

    GenomeRNAii162466.
    PROiQ8TCT1.

    Gene expression databases

    BgeeiQ8TCT1.
    CleanExiHS_PHOSPHO1.
    ExpressionAtlasiQ8TCT1. baseline and differential.
    GenevisibleiQ8TCT1. HS.

    Family and domain databases

    Gene3Di3.40.50.1000. 1 hit.
    InterProiIPR023214. HAD-like_dom.
    IPR006383. HAD-SF_hydro_IB_PSP-like.
    IPR016965. Pase_PHOSPHO-typ.
    IPR006384. PyrdxlP_Pase-rel.
    [Graphical view]
    PfamiPF06888. Put_Phosphatase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF031051. PyrdxlP_Pase_PHOSPHO2. 1 hit.
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01489. DKMTPPase-SF. 1 hit.
    TIGR01488. HAD-SF-IB. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Chromosomal localization of the chicken and mammalian orthologues of the orphan phosphatase PHOSPHO1 gene."
      Houston B., Paton I.R., Burt D.W., Farquharson C.
      Anim. Genet. 33:451-454(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Identification of a novel splice variant of the haloacid dehalogenase: PHOSPHO1."
      Roberts S.J., Owen H.C., Farquharson C.
      Biochem. Biophys. Res. Commun. 371:872-876(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
    3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-111 (ISOFORM 3).
      Tissue: Colon and Medulla oblongata.
    5. "Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities."
      Roberts S.J., Stewart A.J., Sadler P.J., Farquharson C.
      Biochem. J. 382:59-65(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
    6. "PHOSPHO1 -- a novel phosphatase specifically expressed at sites of mineralisation in bone and cartilage."
      Houston B., Stewart A.J., Farquharson C.
      Bone 34:629-637(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "Comparative modelling of human PHOSPHO1 reveals a new group of phosphatases within the haloacid dehalogenase superfamily."
      Stewart A.J., Schmid R., Blindauer C.A., Paisey S.J., Farquharson C.
      Protein Eng. 16:889-895(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SIMILARITY TO HAD-LIKE HYDROLASE SUPERFAMILY.
    8. Cited for: MUTAGENESIS OF ASP-32; ASP-43; ASP-123 AND ASP-203.

    Entry informationi

    Entry nameiPHOP1_HUMAN
    AccessioniPrimary (citable) accession number: Q8TCT1
    Secondary accession number(s): E9PAM0, Q17RU6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2006
    Last sequence update: June 1, 2002
    Last modified: July 6, 2016
    This is version 107 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.