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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) (Mutated in multiple advanced cancers 1) (Phosphatase and tensin homolog)

 PTEN_MOUSE              Reviewed;         403 AA.
O08586; Q3UFB0; Q542G1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
30-AUG-2017, entry version 175.
RecName: Full=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;
AltName: Full=Mutated in multiple advanced cancers 1;
AltName: Full=Phosphatase and tensin homolog;
Name=Pten; Synonyms=Mmac1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9090379; DOI=10.1038/ng0497-356;
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.;
"Identification of a candidate tumour suppressor gene, MMAC1, at
chromosome 10q23.3 that is mutated in multiple advanced cancers.";
Nat. Genet. 15:356-363(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Sympathetic ganglion, Testis, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION.
PubMed=10339565; DOI=10.1073/pnas.96.11.6199;
Sun H., Lesche R., Li D.M., Liliental J., Zhang H., Gao J.,
Gavrilova N., Mueller B., Liu X., Wu H.;
"PTEN modulates cell cycle progression and cell survival by regulating
phosphatidylinositol 3,4,5,-trisphosphate and Akt/protein kinase B
signaling pathway.";
Proc. Natl. Acad. Sci. U.S.A. 96:6199-6204(1999).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
UBIQUITINATION BY XIAP/BIRC4, SUBCELLULAR LOCATION, AND INTERACTION
WITH XIAP/BIRC4.
PubMed=19473982; DOI=10.1074/jbc.C109.009522;
Van Themsche C., Leblanc V., Parent S., Asselin E.;
"X-linked inhibitor of apoptosis protein (XIAP) regulates PTEN
ubiquitination, content, and compartmentalization.";
J. Biol. Chem. 284:20462-20466(2009).
[7]
FUNCTION.
PubMed=19778506; DOI=10.1016/j.neuron.2009.08.008;
Kim J.Y., Duan X., Liu C.Y., Jang M.H., Guo J.U., Pow-anpongkul N.,
Kang E., Song H., Ming G.L.;
"DISC1 regulates new neuron development in the adult brain via
modulation of AKT-mTOR signaling through KIAA1212.";
Neuron 63:761-773(2009).
[8]
PHOSPHORYLATION AT SER-380; THR-382 AND THR-383, AND INTERACTION WITH
ROCK1.
PubMed=20008297; DOI=10.1182/blood-2009-08-237222;
Vemula S., Shi J., Hanneman P., Wei L., Kapur R.;
"ROCK1 functions as a suppressor of inflammatory cell migration by
regulating PTEN phosphorylation and stability.";
Blood 115:1785-1796(2010).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294 AND SER-385, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
PHOSPHORYLATION AT THR-366 AND SER-370.
PubMed=20940307; DOI=10.1074/jbc.M110.166462;
Xu D., Yao Y., Jiang X., Lu L., Dai W.;
"Regulation of PTEN stability and activity by Plk3.";
J. Biol. Chem. 285:39935-39942(2010).
[11]
SUBCELLULAR LOCATION.
PubMed=25801959; DOI=10.1093/jmcb/mjv020;
Howitt J., Low L.H., Putz U., Doan A., Lackovic J., Goh C.P.,
Gunnersen J., Silke J., Tan S.S.;
"Ndfip1 represses cell proliferation by controlling Pten localization
and signaling specificity.";
J. Mol. Cell Biol. 7:119-131(2015).
-!- FUNCTION: 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. {ECO:0000250,
ECO:0000269|PubMed:10339565, ECO:0000269|PubMed:19778506}.
-!- CATALYTIC ACTIVITY: Phosphatidylinositol 3,4,5-trisphosphate +
H(2)O = phosphatidylinositol 4,5-bisphosphate + phosphate.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- SUBUNIT: Monomer. The unphosphorylated form interacts with the
second PDZ domain of AIP1 (By similarity). 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 (By similarity). 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 (PubMed:20008297). Interacts with XIAP/BIRC4
(PubMed:19473982). Interacts with STK11; the interaction
phosphorylates PTEN (By similarity). Interacts with PPP1R16B (By
similarity). Interacts with NOP53; regulates PTEN phosphorylation
and increases its stability (By similarity).
{ECO:0000250|UniProtKB:P60484, ECO:0000269|PubMed:19473982,
ECO:0000269|PubMed:20008297}.
-!- INTERACTION:
P49452:Cenpc; NbExp=2; IntAct=EBI-1186266, EBI-1186252;
Q9JHL1:Slc9a3r2; NbExp=3; IntAct=EBI-1186266, EBI-538451;
P02340:Tp53; NbExp=4; IntAct=EBI-1186266, EBI-474016;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19473982,
ECO:0000269|PubMed:25801959}. Nucleus
{ECO:0000269|PubMed:19473982, ECO:0000269|PubMed:25801959}.
Nucleus, PML body {ECO:0000250|UniProtKB:P60484}.
Note=Monoubiquitinated form is nuclear (By similarity).
Nonubiquitinated form is cytoplasmic (By similarity). Colocalized
with PML and USP7 in PML nuclear bodies (By similarity).
XIAP/BIRC4 promotes its nuclear localization (PubMed:19473982).
{ECO:0000250|UniProtKB:P60484, ECO:0000269|PubMed:19473982}.
-!- PTM: 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. {ECO:0000250, ECO:0000269|PubMed:19473982,
ECO:0000269|PubMed:20008297, ECO:0000269|PubMed:20940307}.
-!- PTM: 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.
{ECO:0000250, ECO:0000269|PubMed:19473982}.
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EMBL; U92437; AAC53118.1; -; mRNA.
EMBL; AK076980; BAC36545.1; -; mRNA.
EMBL; AK088717; BAC40525.1; -; mRNA.
EMBL; AK148736; BAE28651.1; -; mRNA.
EMBL; BC021445; AAH21445.1; -; mRNA.
CCDS; CCDS29753.1; -.
RefSeq; NP_032986.1; NM_008960.2.
UniGene; Mm.245395; -.
ProteinModelPortal; O08586; -.
SMR; O08586; -.
BioGrid; 202449; 21.
DIP; DIP-38740N; -.
IntAct; O08586; 20.
MINT; MINT-128418; -.
STRING; 10090.ENSMUSP00000013807; -.
iPTMnet; O08586; -.
PhosphoSitePlus; O08586; -.
EPD; O08586; -.
MaxQB; O08586; -.
PaxDb; O08586; -.
PeptideAtlas; O08586; -.
PRIDE; O08586; -.
Ensembl; ENSMUST00000013807; ENSMUSP00000013807; ENSMUSG00000013663.
GeneID; 19211; -.
KEGG; mmu:19211; -.
UCSC; uc008hfr.1; mouse.
CTD; 5728; -.
MGI; MGI:109583; Pten.
eggNOG; KOG2283; Eukaryota.
eggNOG; COG2453; LUCA.
GeneTree; ENSGT00760000119113; -.
HOGENOM; HOG000008008; -.
HOVERGEN; HBG000239; -.
InParanoid; O08586; -.
KO; K01110; -.
OMA; PFDEEQH; -.
OrthoDB; EOG091G09VG; -.
PhylomeDB; O08586; -.
TreeFam; TF324513; -.
Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol.
Reactome; R-MMU-199418; Negative regulation of the PI3K/AKT network.
Reactome; R-MMU-202424; Downstream TCR signaling.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-5689896; Ovarian tumor domain proteases.
ChiTaRS; Pten; mouse.
PRO; PR:O08586; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000013663; -.
CleanEx; MM_PTEN; -.
Genevisible; O08586; MM.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0042995; C:cell projection; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0035749; C:myelin sheath adaxonal region; IDA:BHF-UCL.
GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
GO; GO:0043220; C:Schmidt-Lanterman incisure; IDA:BHF-UCL.
GO; GO:0010997; F:anaphase-promoting complex binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0051717; F:inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity; ISS:UniProtKB.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IEA:Ensembl.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; IDA:MGI.
GO; GO:0051800; F:phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity; ISS:UniProtKB.
GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; ISS:UniProtKB.
GO; GO:0004721; F:phosphoprotein phosphatase activity; ISO:MGI.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
GO; GO:1990782; F:protein tyrosine kinase binding; IEA:Ensembl.
GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:MGI.
GO; GO:0030534; P:adult behavior; IMP:CACAO.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0001525; P:angiogenesis; IMP:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0048854; P:brain morphogenesis; IMP:BHF-UCL.
GO; GO:0060070; P:canonical Wnt signaling pathway; ISO:MGI.
GO; GO:0048738; P:cardiac muscle tissue development; IMP:MGI.
GO; GO:0016477; P:cell migration; IMP:MGI.
GO; GO:0036294; P:cellular response to decreased oxygen levels; IDA:MGI.
GO; GO:0071257; P:cellular response to electrical stimulus; ISO:MGI.
GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IDA:MGI.
GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEA:Ensembl.
GO; GO:0044320; P:cellular response to leptin stimulus; IEA:Ensembl.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
GO; GO:0007417; P:central nervous system development; IMP:MGI.
GO; GO:0032286; P:central nervous system myelin maintenance; IMP:BHF-UCL.
GO; GO:0021955; P:central nervous system neuron axonogenesis; IMP:BHF-UCL.
GO; GO:0060997; P:dendritic spine morphogenesis; IMP:BHF-UCL.
GO; GO:0021542; P:dentate gyrus development; IMP:BHF-UCL.
GO; GO:0043542; P:endothelial cell migration; IMP:MGI.
GO; GO:0048853; P:forebrain morphogenesis; IMP:BHF-UCL.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0046855; P:inositol phosphate dephosphorylation; ISS:UniProtKB.
GO; GO:0007611; P:learning or memory; IMP:BHF-UCL.
GO; GO:0045475; P:locomotor rhythm; IMP:BHF-UCL.
GO; GO:0007626; P:locomotory behavior; IMP:BHF-UCL.
GO; GO:0060292; P:long term synaptic depression; IEA:Ensembl.
GO; GO:0060291; P:long-term synaptic potentiation; IMP:BHF-UCL.
GO; GO:0060179; P:male mating behavior; IMP:BHF-UCL.
GO; GO:0042711; P:maternal behavior; IMP:BHF-UCL.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0033555; P:multicellular organismal response to stress; IMP:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0048681; P:negative regulation of axon regeneration; IMP:ParkinsonsUK-UCL.
GO; GO:0050771; P:negative regulation of axonogenesis; IMP:BHF-UCL.
GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IGI:BHF-UCL.
GO; GO:0090344; P:negative regulation of cell aging; IMP:BHF-UCL.
GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
GO; GO:0045792; P:negative regulation of cell size; IMP:BHF-UCL.
GO; GO:0031658; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle; ISO:MGI.
GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; IMP:BHF-UCL.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISO:MGI.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:MGI.
GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; IMP:BHF-UCL.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISS:UniProtKB.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
GO; GO:0051548; P:negative regulation of keratinocyte migration; ISO:MGI.
GO; GO:0031642; P:negative regulation of myelination; IMP:MGI.
GO; GO:0046621; P:negative regulation of organ growth; IMP:BHF-UCL.
GO; GO:0050765; P:negative regulation of phagocytosis; IEA:Ensembl.
GO; GO:1901017; P:negative regulation of potassium ion transmembrane transporter activity; IEA:Ensembl.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:BHF-UCL.
GO; GO:2000272; P:negative regulation of receptor activity; IEA:Ensembl.
GO; GO:0090071; P:negative regulation of ribosome biogenesis; IMP:BHF-UCL.
GO; GO:2000808; P:negative regulation of synaptic vesicle clustering; IMP:BHF-UCL.
GO; GO:1903690; P:negative regulation of wound healing, spreading of epidermal cells; ISO:MGI.
GO; GO:0007270; P:neuron-neuron synaptic transmission; IMP:BHF-UCL.
GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISS:UniProtKB.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IMP:MGI.
GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:MGI.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IMP:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
GO; GO:2000060; P:positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; ISO:MGI.
GO; GO:1903984; P:positive regulation of TRAIL-activated apoptotic signaling pathway; ISO:MGI.
GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; IMP:BHF-UCL.
GO; GO:0097107; P:postsynaptic density assembly; IMP:BHF-UCL.
GO; GO:0060134; P:prepulse inhibition; IMP:BHF-UCL.
GO; GO:0097105; P:presynaptic membrane assembly; IMP:BHF-UCL.
GO; GO:0060736; P:prostate gland growth; IMP:MGI.
GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; IMP:UniProtKB.
GO; GO:0050821; P:protein stabilization; ISO:MGI.
GO; GO:0048679; P:regulation of axon regeneration; IGI:MGI.
GO; GO:0002902; P:regulation of B cell apoptotic process; IMP:MGI.
GO; GO:0051726; P:regulation of cell cycle; IGI:MGI.
GO; GO:0032535; P:regulation of cellular component size; IMP:BHF-UCL.
GO; GO:0060341; P:regulation of cellular localization; IMP:CACAO.
GO; GO:0033032; P:regulation of myeloid cell apoptotic process; IMP:MGI.
GO; GO:0010975; P:regulation of neuron projection development; IMP:UniProtKB.
GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IMP:MGI.
GO; GO:0014823; P:response to activity; IEA:Ensembl.
GO; GO:0046685; P:response to arsenic-containing substance; IEA:Ensembl.
GO; GO:0033198; P:response to ATP; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
GO; GO:0060024; P:rhythmic synaptic transmission; IMP:BHF-UCL.
GO; GO:0035176; P:social behavior; IMP:BHF-UCL.
GO; GO:0007416; P:synapse assembly; IMP:BHF-UCL.
GO; GO:0060074; P:synapse maturation; IMP:BHF-UCL.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR017361; Bifunc_PIno_P3_Pase/Pase_PTEN.
InterPro; IPR000008; C2_dom.
InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR014020; Tensin_C2-dom.
InterPro; IPR029023; Tensin_phosphatase.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
Pfam; PF00782; DSPc; 1.
Pfam; PF10409; PTEN_C2; 1.
PIRSF; PIRSF038025; PTEN; 1.
SMART; SM01326; PTEN_C2; 1.
SMART; SM00404; PTPc_motif; 1.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF52799; SSF52799; 1.
PROSITE; PS51182; C2_TENSIN; 1.
PROSITE; PS51181; PPASE_TENSIN; 1.
1: Evidence at protein level;
Acetylation; Apoptosis; Complete proteome; Cytoplasm; Hydrolase;
Isopeptide bond; Lipid metabolism; Neurogenesis; Nucleus;
Phosphoprotein; Protein phosphatase; Reference proteome;
Tumor suppressor; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P60484}.
CHAIN 2 403 Phosphatidylinositol 3,4,5-trisphosphate
3-phosphatase and dual-specificity
protein phosphatase PTEN.
/FTId=PRO_0000215905.
DOMAIN 14 185 Phosphatase tensin-type.
{ECO:0000255|PROSITE-ProRule:PRU00590}.
DOMAIN 190 350 C2 tensin-type. {ECO:0000255|PROSITE-
ProRule:PRU00589}.
REGION 338 348 Required for interaction with NOP53.
{ECO:0000250|UniProtKB:P60484}.
REGION 401 403 PDZ domain-binding. {ECO:0000250}.
ACT_SITE 124 124 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00590}.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000250|UniProtKB:P60484}.
MOD_RES 294 294 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 336 336 Phosphotyrosine; by FRK.
{ECO:0000250|UniProtKB:P60484}.
MOD_RES 366 366 Phosphothreonine; by GSK3-beta and PLK3.
{ECO:0000269|PubMed:20940307}.
MOD_RES 370 370 Phosphoserine; by CK2 and PLK3.
{ECO:0000269|PubMed:20940307}.
MOD_RES 380 380 Phosphoserine; by ROCK1.
{ECO:0000269|PubMed:20008297}.
MOD_RES 382 382 Phosphothreonine; by ROCK1.
{ECO:0000269|PubMed:20008297}.
MOD_RES 383 383 Phosphothreonine; by ROCK1.
{ECO:0000269|PubMed:20008297}.
MOD_RES 385 385 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 401 401 Phosphothreonine.
{ECO:0000250|UniProtKB:P60484}.
CROSSLNK 13 13 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P60484}.
CROSSLNK 289 289 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P60484}.
CONFLICT 50 50 Missing (in Ref. 2; BAE28651).
{ECO:0000305}.
SEQUENCE 403 AA; 47152 MW; 75F97C3DD6843BA9 CRC64;
MTAIIKEIVS RNKRRYQEDG FDLDLTYIYP NIIAMGFPAE RLEGVYRNNI DDVVRFLDSK
HKNHYKIYNL CAERHYDTAK FNCRVAQYPF EDHNPPQLEL IKPFCEDLDQ WLSEDDNHVA
AIHCKAGKGR TGVMICAYLL HRGKFLKAQE ALDFYGEVRT RDKKGVTIPS QRRYVYYYSY
LLKNHLDYRP VALLFHKMMF ETIPMFSGGT CNPQFVVCQL KVKIYSSNSG PTRREDKFMY
FEFPQPLPVC GDIKVEFFHK QNKMLKKDKM FHFWVNTFFI PGPEETSEKV ENGSLCDQEI
DSICSIERAD NDKEYLVLTL TKNDLDKANK DKANRYFSPN FKVKLYFTKT VEEPSNPEAS
SSTSVTPDVS DNEPDHYRYS DTTDSDPENE PFDEDQHSQI TKV


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