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O08586

- PTEN_MOUSE

UniProt

O08586 - PTEN_MOUSE

Protein

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

Gene

Pten

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement By similarity. 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 correct neuron positioning, dendritic development and synapse formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability.By similarity2 Publications

    Catalytic activityi

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

    Cofactori

    Magnesium.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei124 – 1241Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. activation of mitotic anaphase-promoting complex activity Source: BHF-UCL
    2. aging Source: Ensembl
    3. angiogenesis Source: MGI
    4. apoptotic process Source: UniProtKB-KW
    5. brain morphogenesis Source: BHF-UCL
    6. canonical Wnt signaling pathway Source: Ensembl
    7. cardiac muscle tissue development Source: MGI
    8. cell migration Source: MGI
    9. central nervous system development Source: MGI
    10. central nervous system myelin maintenance Source: BHF-UCL
    11. central nervous system neuron axonogenesis Source: BHF-UCL
    12. dendritic spine morphogenesis Source: BHF-UCL
    13. dentate gyrus development Source: BHF-UCL
    14. endothelial cell migration Source: MGI
    15. forebrain morphogenesis Source: BHF-UCL
    16. heart development Source: MGI
    17. inositol phosphate dephosphorylation Source: UniProtKB
    18. learning or memory Source: BHF-UCL
    19. locomotor rhythm Source: BHF-UCL
    20. locomotory behavior Source: BHF-UCL
    21. long term synaptic depression Source: Ensembl
    22. long-term synaptic potentiation Source: BHF-UCL
    23. male mating behavior Source: BHF-UCL
    24. maternal behavior Source: BHF-UCL
    25. memory Source: Ensembl
    26. multicellular organismal response to stress Source: BHF-UCL
    27. negative regulation of apoptotic process Source: UniProtKB
    28. negative regulation of axonogenesis Source: BHF-UCL
    29. negative regulation of cell aging Source: BHF-UCL
    30. negative regulation of cell migration Source: UniProtKB
    31. negative regulation of cell proliferation Source: UniProtKB
    32. negative regulation of cell size Source: BHF-UCL
    33. negative regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: Ensembl
    34. negative regulation of dendritic spine morphogenesis Source: BHF-UCL
    35. negative regulation of epithelial cell proliferation Source: MGI
    36. negative regulation of excitatory postsynaptic membrane potential Source: BHF-UCL
    37. negative regulation of focal adhesion assembly Source: UniProtKB
    38. negative regulation of myelination Source: MGI
    39. negative regulation of organ growth Source: BHF-UCL
    40. negative regulation of phagocytosis Source: Ensembl
    41. negative regulation of protein kinase B signaling Source: UniProtKB
    42. negative regulation of ribosome biogenesis Source: BHF-UCL
    43. negative regulation of synaptic vesicle clustering Source: BHF-UCL
    44. neuron-neuron synaptic transmission Source: BHF-UCL
    45. phosphatidylinositol dephosphorylation Source: UniProtKB
    46. platelet-derived growth factor receptor signaling pathway Source: Ensembl
    47. positive regulation of apoptotic process Source: Ensembl
    48. positive regulation of apoptotic signaling pathway Source: MGI
    49. positive regulation of cell proliferation Source: BHF-UCL
    50. positive regulation of excitatory postsynaptic membrane potential Source: BHF-UCL
    51. positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: Ensembl
    52. positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
    53. postsynaptic density assembly Source: BHF-UCL
    54. prepulse inhibition Source: BHF-UCL
    55. presynaptic membrane assembly Source: BHF-UCL
    56. prostate gland growth Source: MGI
    57. protein dephosphorylation Source: UniProtKB
    58. protein kinase B signaling Source: UniProtKB
    59. protein stabilization Source: Ensembl
    60. regulation of B cell apoptotic process Source: MGI
    61. regulation of cell cycle Source: MGI
    62. regulation of cellular component size Source: BHF-UCL
    63. regulation of myeloid cell apoptotic process Source: MGI
    64. regulation of neuron projection development Source: UniProtKB
    65. regulation of protein stability Source: UniProtKB
    66. response to arsenic-containing substance Source: Ensembl
    67. response to ATP Source: Ensembl
    68. response to drug Source: Ensembl
    69. response to estradiol Source: Ensembl
    70. response to ethanol Source: Ensembl
    71. response to glucose Source: Ensembl
    72. response to nutrient Source: Ensembl
    73. response to zinc ion Source: Ensembl
    74. rhythmic synaptic transmission Source: BHF-UCL
    75. social behavior Source: BHF-UCL
    76. synapse assembly Source: BHF-UCL
    77. synapse maturation Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Apoptosis, Lipid metabolism, Neurogenesis

    Enzyme and pathway databases

    ReactomeiREACT_196473. Synthesis of IP3 and IP4 in the cytosol.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_198973. Synthesis of PIPs at the plasma membrane.
    REACT_214733. Negative regulation of the PI3K/AKT network.
    REACT_225145. Downstream TCR signaling.

    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:Pten
    Synonyms:Mmac1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:109583. Pten.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity. NucleusPML body By similarity
    Note: Monoubiquitinated form is nuclear By similarity. Nonubiquitinated form is cytoplasmic. Colocalized with PML and USP7 in PML nuclear bodies. XIAP/BIRC4 promotes its nuclear localization.By similarity1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic side of plasma membrane Source: Ensembl
    3. dendritic spine Source: Ensembl
    4. mitochondrion Source: Ensembl
    5. myelin sheath adaxonal region Source: BHF-UCL
    6. neuron projection Source: BHF-UCL
    7. nucleus Source: MGI
    8. PML body Source: UniProtKB-SubCell
    9. postsynaptic membrane Source: Ensembl
    10. Schmidt-Lanterman incisure Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 403402Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTENPRO_0000215905Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonineBy similarity
    Cross-linki13 – 13Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki289 – 289Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei336 – 3361Phosphotyrosine; by FRKBy similarity
    Modified residuei366 – 3661Phosphothreonine; by GSK3-beta and PLK31 Publication
    Modified residuei370 – 3701Phosphoserine; by CK2 and PLK31 Publication
    Modified residuei380 – 3801Phosphoserine; by ROCK11 Publication
    Modified residuei382 – 3821Phosphothreonine; by ROCK11 Publication
    Modified residuei383 – 3831Phosphothreonine; by ROCK11 Publication
    Modified residuei385 – 3851Phosphoserine; alternate1 Publication
    Modified residuei385 – 3851Phosphoserine; by CK2; alternateBy similarity
    Modified residuei401 – 4011PhosphothreonineBy similarity

    Post-translational modificationi

    Constitutively phosphorylated by CK2 under normal conditions. Phosphorylation results in an inhibited activity towards PIP3. Phosphorylation can both inhibit or promote PDZ-binding. Phosphorylation at Tyr-336 by FRK/PTK5 protects this protein from ubiquitin-mediated degradation probably by inhibiting its binding to NEDD4 By similarity. Phosphorylation by PLK3 promotes its stability and prevents its degradation by the proteasome. Phosphorylation by ROCK1 is essential for its stability and activity.By similarity4 Publications
    Monoubiquitinated; monoubiquitination is increased in presence of retinoic acid. Deubiquitinated by USP7; leading to its nuclear exclusion. Monoubiquitination of one of either Lys-13 and Lys-289 amino acid is sufficient to modulate PTEN compartmentalization By similarity. Ubiquitinated by XIAP/BIRC4.By similarity1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO08586.
    PaxDbiO08586.
    PRIDEiO08586.

    PTM databases

    PhosphoSiteiO08586.

    Expressioni

    Gene expression databases

    ArrayExpressiO08586.
    BgeeiO08586.
    CleanExiMM_PTEN.
    GenevestigatoriO08586.

    Interactioni

    Subunit structurei

    Monomer. The unphosphorylated form interacts with the second PDZ domain of AIP1. Interacts with MAGI2, MAGI3, MAST1 and MAST3, but neither with MAST4 nor with DLG5; interaction with MAGI2 increases protein stability By similarity. Interacts with NEDD4. Interacts with NDFIP1 and NDFIP2; in the presence of NEDD4 or ITCH, this interaction promotes PTEN ubiquitination By similarity. Interacts (via C2 domain) with FRK By similarity. Interacts with USP7; the interaction is direct By similarity. Interacts with ROCK1. Interacts with XIAP/BIRC4. Interacts with STK11; the interaction phosphorylates PTEN By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CenpcP494522EBI-1186266,EBI-1186252
    Slc9a3r2Q9JHL13EBI-1186266,EBI-538451
    Tp53P023404EBI-1186266,EBI-474016

    Protein-protein interaction databases

    BioGridi202449. 6 interactions.
    DIPiDIP-38740N.
    IntActiO08586. 8 interactions.
    MINTiMINT-128418.

    Structurei

    3D structure databases

    ProteinModelPortaliO08586.
    SMRiO08586. Positions 14-351.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 185172Phosphatase tensin-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini190 – 350161C2 tensin-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni401 – 4033PDZ domain-bindingBy similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG2453.
    GeneTreeiENSGT00620000087779.
    HOGENOMiHOG000008008.
    HOVERGENiHBG000239.
    InParanoidiQ3UFB0.
    KOiK01110.
    OMAiKEYLILT.
    OrthoDBiEOG7R2BJ5.
    PhylomeDBiO08586.
    TreeFamiTF324513.

    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.

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

    O08586-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTAIIKEIVS RNKRRYQEDG FDLDLTYIYP NIIAMGFPAE RLEGVYRNNI    50
    DDVVRFLDSK HKNHYKIYNL CAERHYDTAK FNCRVAQYPF EDHNPPQLEL 100
    IKPFCEDLDQ WLSEDDNHVA AIHCKAGKGR TGVMICAYLL HRGKFLKAQE 150
    ALDFYGEVRT RDKKGVTIPS QRRYVYYYSY LLKNHLDYRP VALLFHKMMF 200
    ETIPMFSGGT CNPQFVVCQL KVKIYSSNSG PTRREDKFMY FEFPQPLPVC 250
    GDIKVEFFHK QNKMLKKDKM FHFWVNTFFI PGPEETSEKV ENGSLCDQEI 300
    DSICSIERAD NDKEYLVLTL TKNDLDKANK DKANRYFSPN FKVKLYFTKT 350
    VEEPSNPEAS SSTSVTPDVS DNEPDHYRYS DTTDSDPENE PFDEDQHSQI 400
    TKV 403
    Length:403
    Mass (Da):47,152
    Last modified:July 1, 1997 - v1
    Checksum:i75F97C3DD6843BA9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti50 – 501Missing in BAE28651. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U92437 mRNA. Translation: AAC53118.1.
    AK076980 mRNA. Translation: BAC36545.1.
    AK088717 mRNA. Translation: BAC40525.1.
    AK148736 mRNA. Translation: BAE28651.1.
    BC021445 mRNA. Translation: AAH21445.1.
    CCDSiCCDS29753.1.
    RefSeqiNP_032986.1. NM_008960.2.
    UniGeneiMm.245395.

    Genome annotation databases

    EnsembliENSMUST00000013807; ENSMUSP00000013807; ENSMUSG00000013663.
    GeneIDi19211.
    KEGGimmu:19211.
    UCSCiuc008hfr.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U92437 mRNA. Translation: AAC53118.1 .
    AK076980 mRNA. Translation: BAC36545.1 .
    AK088717 mRNA. Translation: BAC40525.1 .
    AK148736 mRNA. Translation: BAE28651.1 .
    BC021445 mRNA. Translation: AAH21445.1 .
    CCDSi CCDS29753.1.
    RefSeqi NP_032986.1. NM_008960.2.
    UniGenei Mm.245395.

    3D structure databases

    ProteinModelPortali O08586.
    SMRi O08586. Positions 14-351.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202449. 6 interactions.
    DIPi DIP-38740N.
    IntActi O08586. 8 interactions.
    MINTi MINT-128418.

    PTM databases

    PhosphoSitei O08586.

    Proteomic databases

    MaxQBi O08586.
    PaxDbi O08586.
    PRIDEi O08586.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000013807 ; ENSMUSP00000013807 ; ENSMUSG00000013663 .
    GeneIDi 19211.
    KEGGi mmu:19211.
    UCSCi uc008hfr.1. mouse.

    Organism-specific databases

    CTDi 5728.
    MGIi MGI:109583. Pten.

    Phylogenomic databases

    eggNOGi COG2453.
    GeneTreei ENSGT00620000087779.
    HOGENOMi HOG000008008.
    HOVERGENi HBG000239.
    InParanoidi Q3UFB0.
    KOi K01110.
    OMAi KEYLILT.
    OrthoDBi EOG7R2BJ5.
    PhylomeDBi O08586.
    TreeFami TF324513.

    Enzyme and pathway databases

    Reactomei REACT_196473. Synthesis of IP3 and IP4 in the cytosol.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_198973. Synthesis of PIPs at the plasma membrane.
    REACT_214733. Negative regulation of the PI3K/AKT network.
    REACT_225145. Downstream TCR signaling.

    Miscellaneous databases

    ChiTaRSi PTEN. mouse.
    NextBioi 295956.
    PROi O08586.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O08586.
    Bgeei O08586.
    CleanExi MM_PTEN.
    Genevestigatori O08586.

    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. "Identification of a candidate tumour suppressor gene, MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers."
      Steck P.A., Pershouse M.A., Jasser S.A., Lin H., Yung W.K.A., Ligon A.H., Langford L.A., Baumgard M.L., Hattier T., Davis T., Frye C., Hu R., Swedlund B., Teng D.H.-F., Tavtigian S.V.
      Nat. Genet. 15:356-363(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Sympathetic ganglion, Testis and Thymus.
    3. "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].
      Strain: Czech II.
      Tissue: Mammary gland.
    4. "PTEN modulates cell cycle progression and cell survival by regulating phosphatidylinositol 3,4,5,-trisphosphate and Akt/protein kinase B signaling pathway."
      Sun H., Lesche R., Li D.M., Liliental J., Zhang H., Gao J., Gavrilova N., Mueller B., Liu X., Wu H.
      Proc. Natl. Acad. Sci. U.S.A. 96:6199-6204(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "X-linked inhibitor of apoptosis protein (XIAP) regulates PTEN ubiquitination, content, and compartmentalization."
      Van Themsche C., Leblanc V., Parent S., Asselin E.
      J. Biol. Chem. 284:20462-20466(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY XIAP/BIRC4, SUBCELLULAR LOCATION, INTERACTION WITH XIAP/BIRC4.
    7. "DISC1 regulates new neuron development in the adult brain via modulation of AKT-mTOR signaling through KIAA1212."
      Kim J.Y., Duan X., Liu C.Y., Jang M.H., Guo J.U., Pow-anpongkul N., Kang E., Song H., Ming G.L.
      Neuron 63:761-773(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "ROCK1 functions as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability."
      Vemula S., Shi J., Hanneman P., Wei L., Kapur R.
      Blood 115:1785-1796(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-380; THR-382 AND THR-383, INTERACTION WITH ROCK1.
    9. "Regulation of PTEN stability and activity by Plk3."
      Xu D., Yao Y., Jiang X., Lu L., Dai W.
      J. Biol. Chem. 285:39935-39942(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-366 AND SER-370.

    Entry informationi

    Entry nameiPTEN_MOUSE
    AccessioniPrimary (citable) accession number: O08586
    Secondary accession number(s): Q3UFB0, Q542G1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 144 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3