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[1]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
DOI=10.1016/S0092-8674(00)81663-3; PubMed=10555148 [NCBI, ExPASy, EBI, Israel, Japan]
Lee J.-O.,
Yang H.,
Georgescu M.-M.,
Di Cristofano A.,
Maehama T.,
Shi Y.,
Dixon J.E.,
Pandolfi P.,
Pavletich N.P.;
"Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association.";
Cell 99:323-334(1999).
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- FUNCTION: 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. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue (By similarity).
- CATALYTIC ACTIVITY: Phosphatidylinositol 3,4,5-trisphosphate + H2O = phosphatidylinositol 4,5-bisphosphate + phosphate.
- CATALYTIC ACTIVITY: A phosphoprotein + H2O = a protein + phosphate.
- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
- COFACTOR: Magnesium (By similarity).
- SUBUNIT: Monomer (By similarity).
- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
- SIMILARITY: Contains 1 C2 tensin-type domain.
- SIMILARITY: Contains 1 phosphatase tensin-type domain.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 402 AA [This is the length of the unprocessed precursor] |
Molecular weight: 46878 Da [This is the MW of the unprocessed precursor] |
CRC64: E61315E2DAB0850F [This is a checksum on the sequence] |
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10 20 30 40 50 60
MTAIIKEFVS RNKRRYQEDG FDLDLTYIYP NIIAMGFPAE RLEGVYRNNI DDVVRFLDSK
70 80 90 100 110 120
HKNHYKIYNL CAERHYDTNK FSCRVAQYPF EDHNPPQLEL IKPFCEDLDQ LLSENENVAA
130 140 150 160 170 180
IHCKAGKGRT GVMICAYLLH RGKFPRAQEA LDFYGEVRTR DKKGVTIPSQ RRYVYYYSYL
190 200 210 220 230 240
LKNSLEYRPV PLLFHKIEFE TIPMFSGSTC NPQFVVYQLK VKIFTSTAGP KRAEKLMYFD
250 260 270 280 290 300
FPQPLPVCGD IKVEFFHKQN KVMKKEKMFH FWVNTFFIPG PEEYSEKVEN GTLVGEQELD
310 320 330 340 350 360
GIYSTERSDN DKEYLTLALT KNDLDKANKD KANRLFSPNF KVKLFFTKTV EESSNSEASS
370 380 390 400
STSVTPDVSD NEPDHYRYSD TTDSDPENEP FDEDQITQIT KV
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Q9PUT6 in FASTA format |
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