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Q9PUT6

- PTEN_XENLA

UniProt

Q9PUT6 - PTEN_XENLA

Protein

Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN

Gene

pten

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Tumor suppressor. Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. The lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with AIP1 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including neuron positioning, dendritic development and synapse formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement By similarity.By similarity

    Catalytic activityi

    Phosphatidylinositol 3,4,5-trisphosphate + H2O = phosphatidylinositol 4,5-bisphosphate + phosphate.By similarity
    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.
    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.By similarity

    Cofactori

    Magnesium.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei123 – 1231Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity Source: UniProtKB
    2. lipid binding Source: UniProtKB-KW
    3. magnesium ion binding Source: InterPro
    4. PDZ domain binding Source: UniProtKB
    5. phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity Source: UniProtKB
    6. phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity Source: UniProtKB
    7. phosphatidylinositol-3-phosphatase activity Source: UniProtKB
    8. protein serine/threonine phosphatase activity Source: UniProtKB
    9. protein tyrosine/serine/threonine phosphatase activity Source: InterPro
    10. protein tyrosine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. inositol phosphate dephosphorylation Source: UniProtKB
    3. negative regulation of cell migration Source: UniProtKB
    4. negative regulation of cell proliferation Source: UniProtKB
    5. negative regulation of focal adhesion assembly Source: UniProtKB
    6. negative regulation of protein kinase B signaling Source: UniProtKB
    7. peptidyl-tyrosine dephosphorylation Source: GOC
    8. phosphatidylinositol dephosphorylation Source: UniProtKB
    9. protein dephosphorylation Source: UniProtKB
    10. protein kinase B signaling Source: UniProtKB
    11. regulation of neuron projection development Source: UniProtKB
    12. regulation of protein stability Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Apoptosis, Lipid metabolism, Neurogenesis

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC:3.1.3.16, EC:3.1.3.48, EC:3.1.3.67)
    Alternative name(s):
    Mutated in multiple advanced cancers 1
    Phosphatase and tensin homolog
    Gene namesi
    Name:ptenImported
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-491437. pten.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity. NucleusPML body By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. PML body Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 402402Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTENPRO_0000227539Add
    BLAST

    Post-translational modificationi

    Monoubiquitinated. Deubiquitinated By similarity.By similarity

    Keywords - PTMi

    Ubl conjugation

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ9PUT6.
    SMRiQ9PUT6. Positions 14-350.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 184171Phosphatase tensin-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini189 – 349161C2 tensin-typePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi400 – 4023PDZ-binding

    Sequence similaritiesi

    Contains 1 C2 tensin-type domain.PROSITE-ProRule annotation
    Contains 1 phosphatase tensin-type domain.PROSITE-ProRule annotation

    Phylogenomic databases

    HOVERGENiHBG000239.
    KOiK01110.

    Family and domain databases

    Gene3Di3.90.190.10. 1 hit.
    InterProiIPR017361. Bifunc_PIno_P3_Pase/Pase_PTEN.
    IPR000008. C2_dom.
    IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR014020. Tensin_C2-dom.
    IPR029023. Tensin_lipid_phosphatase_dom.
    IPR016130. Tyr_Pase_AS.
    [Graphical view]
    PfamiPF00782. DSPc. 1 hit.
    PF10409. PTEN_C2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038025. PTEN. 1 hit.
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF52799. SSF52799. 1 hit.
    PROSITEiPS51182. C2_TENSIN. 1 hit.
    PS51181. PPASE_TENSIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9PUT6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTAIIKEFVS RNKRRYQEDG FDLDLTYIYP NIIAMGFPAE RLEGVYRNNI    50
    DDVVRFLDSK HKNHYKIYNL CAERHYDTNK FSCRVAQYPF EDHNPPQLEL 100
    IKPFCEDLDQ LLSENENVAA IHCKAGKGRT GVMICAYLLH RGKFPRAQEA 150
    LDFYGEVRTR DKKGVTIPSQ RRYVYYYSYL LKNSLEYRPV PLLFHKIEFE 200
    TIPMFSGSTC NPQFVVYQLK VKIFTSTAGP KRAEKLMYFD FPQPLPVCGD 250
    IKVEFFHKQN KVMKKEKMFH FWVNTFFIPG PEEYSEKVEN GTLVGEQELD 300
    GIYSTERSDN DKEYLTLALT KNDLDKANKD KANRLFSPNF KVKLFFTKTV 350
    EESSNSEASS STSVTPDVSD NEPDHYRYSD TTDSDPENEP FDEDQITQIT 400
    KV 402
    Length:402
    Mass (Da):46,878
    Last modified:May 1, 2000 - v1
    Checksum:iE61315E2DAB0850F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF144732 mRNA. Translation: AAD46165.1.
    RefSeqiNP_001083831.1. NM_001090362.1.
    UniGeneiXl.561.

    Genome annotation databases

    GeneIDi399142.
    KEGGixla:399142.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF144732 mRNA. Translation: AAD46165.1 .
    RefSeqi NP_001083831.1. NM_001090362.1.
    UniGenei Xl.561.

    3D structure databases

    ProteinModelPortali Q9PUT6.
    SMRi Q9PUT6. Positions 14-350.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 399142.
    KEGGi xla:399142.

    Organism-specific databases

    CTDi 5728.
    Xenbasei XB-GENE-491437. pten.

    Phylogenomic databases

    HOVERGENi HBG000239.
    KOi K01110.

    Family and domain databases

    Gene3Di 3.90.190.10. 1 hit.
    InterProi IPR017361. Bifunc_PIno_P3_Pase/Pase_PTEN.
    IPR000008. C2_dom.
    IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR014020. Tensin_C2-dom.
    IPR029023. Tensin_lipid_phosphatase_dom.
    IPR016130. Tyr_Pase_AS.
    [Graphical view ]
    Pfami PF00782. DSPc. 1 hit.
    PF10409. PTEN_C2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038025. PTEN. 1 hit.
    SUPFAMi SSF49562. SSF49562. 1 hit.
    SSF52799. SSF52799. 1 hit.
    PROSITEi PS51182. C2_TENSIN. 1 hit.
    PS51181. PPASE_TENSIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association."
      Lee J.-O., Yang H., Georgescu M.-M., Di Cristofano A., Maehama T., Shi Y., Dixon J.E., Pandolfi P., Pavletich N.P.
      Cell 99:323-334(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: TestisImported.

    Entry informationi

    Entry nameiPTEN_XENLA
    AccessioniPrimary (citable) accession number: Q9PUT6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 7, 2006
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 83 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3