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O08586

- PTEN_MOUSE

UniProt

O08586 - PTEN_MOUSE

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Protein

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

Gene
Pten, Mmac1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.2 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 intermediate Reviewed prediction

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
Complete GO annotation...

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.1 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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By 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-acetylthreonine By 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 FRK By 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; alternate By similarity
Modified residuei401 – 4011Phosphothreonine By 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.2 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/BIRC4.1 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.2 Publications

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.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501Missing in BAE28651. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 143 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

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