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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_HUMAN              Reviewed;         403 AA.
P60484; B2R904; F2YHV0; O00633; O02679; Q6ICT7;
16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
16-FEB-2004, sequence version 1.
30-AUG-2017, entry version 170.
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, TEP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
SUBCELLULAR LOCATION, AND INDUCTION.
TISSUE=Epithelium;
PubMed=9187108;
Li D.M., Sun H.;
"TEP1, encoded by a candidate tumor suppressor locus, is a novel
protein tyrosine phosphatase regulated by transforming growth factor
beta.";
Cancer Res. 57:2124-2129(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
VARIANTS GLIOMA SER-15; GLU-36; ARG-42; TRP-57 AND THR-319 DEL.
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLIOBLASTOMA
ARG-129 AND PROSTATE CANCER LEU-134.
PubMed=9072974; DOI=10.1126/science.275.5308.1943;
Li J., Yen C., Liaw D., Podsypanina K., Bose S., Wang S.I., Puc J.,
Miliaresis C., Rodgers L., McCombie R., Bigner S.H., Giovanella B.C.,
Ittmann M., Tycko B., Hibshoosh H., Wigler M.H., Parsons R.;
"PTEN, a putative protein tyrosine phosphatase gene mutated in human
brain, breast, and prostate cancer.";
Science 275:1943-1947(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10817502; DOI=10.1054/bjoc.2000.1211;
Hamilton J.A., Stewart L.M.D., Ajayi L., Gray I.C., Gray N.E.,
Roberts K.G., Watson G.J., Kaisary A.V., Snary D.;
"The expression profile for the tumour suppressor gene PTEN and
associated polymorphic markers.";
Br. J. Cancer 82:1671-1676(2000).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Wang S., Li J., Liaw D., Bose S., Podsypanina K., Parsons R.;
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Jensen K., de la Bastide M., Parsons R., Parnell L.D., Dedhia N.,
Gottesman T., Gnoj L., Kaplan N., Lodhi M., Johnson A.F., Shohdy N.,
Hasegawa A., Haberman K., Huang E.N., Schutz K., Calma C., Granat S.,
Wigler M.H., McCombie W.R.;
"Genomic sequence of PTEN/MMAC1.";
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Yang C.-W., Hsu Y.-F.;
"Homo sapiens phosphatase and tensin homolog mRNA splicing variants.";
Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Spleen;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-290.
NIEHS SNPs program;
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
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).
[13]
FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION OF VARIANTS GLIOMA
TRP-57; ENDOMETRIAL CANCER TYR-123; GLIOBLASTOMA ARG-129; CWS1
ARG-129; PROSTATE CANCER LEU-134; GLIOBLASTOMA ARG-165; BREAST CANCER
PRO-167 AND BZ ARG-170.
PubMed=9256433; DOI=10.1073/pnas.94.17.9052;
Myers M.P., Stolarov J.P., Eng C., Li J., Wang S.I., Wigler M.H.,
Parsons R., Tonks N.K.;
"P-TEN, the tumor suppressor from human chromosome 10q23, is a dual-
specificity phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 94:9052-9057(1997).
[14]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=9593664; DOI=10.1074/jbc.273.22.13375;
Maehama T., Dixon J.E.;
"The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second
messenger, phosphatidylinositol 3,4,5-trisphosphate.";
J. Biol. Chem. 273:13375-13378(1998).
[15]
FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-130, AND
CHARACTERIZATION OF VARIANTS CWS1 SER-124 AND CWS1 GLU-129.
PubMed=9811831; DOI=10.1073/pnas.95.23.13513;
Myers M.P., Pass I., Batty I.H., Van der Kaay J., Stolarov J.P.,
Hemmings B.A., Wigler M.H., Downes C.P., Tonks N.K.;
"The lipid phosphatase activity of PTEN is critical for its tumor
suppressor function.";
Proc. Natl. Acad. Sci. U.S.A. 95:13513-13518(1998).
[16]
FUNCTION, MUTAGENESIS OF ASP-92 AND CYS-124, AND CHARACTERIZATION OF
VARIANT GLU-129.
PubMed=9616126; DOI=10.1126/science.280.5369.1614;
Tamura M., Gu J., Matsumoto K., Aota S., Parsons R., Yamada K.M.;
"Inhibition of cell migration, spreading, and focal adhesions by tumor
suppressor PTEN.";
Science 280:1614-1617(1998).
[17]
FUNCTION, DOMAIN, AND CHARACTERIZATION OF VARIANTS THR-319 DEL;
GLN-345 AND ILE-348.
PubMed=10468583; DOI=10.1073/pnas.96.18.10182;
Georgescu M.-M., Kirsch K.H., Akagi T., Shishido T., Hanafusa H.;
"The tumor-suppressor activity of PTEN is regulated by its carboxyl-
terminal region.";
Proc. Natl. Acad. Sci. U.S.A. 96:10182-10187(1999).
[18]
INTERACTION WITH DLG1 AND MAST2, AND PHOSPHORYLATION AT THR-401.
PubMed=10646847;
Adey N.B., Huang L., Ormonde P.A., Baumgard M.L., Pero R.,
Byreddy D.V., Tavtigian S.V., Bartel P.L.;
"Threonine phosphorylation of the MMAC1/PTEN PDZ binding domain both
inhibits and stimulates PDZ binding.";
Cancer Res. 60:35-37(2000).
[19]
INTERACTION WITH MAGI3.
PubMed=10748157; DOI=10.1074/jbc.M909741199;
Wu Y., Dowbenko D., Spencer S., Laura R., Lee J., Gu Q., Lasky L.A.;
"Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of
MAGI3, a novel membrane-associated guanylate kinase.";
J. Biol. Chem. 275:21477-21485(2000).
[20]
INTERACTION WITH AIP1.
PubMed=10760291; DOI=10.1073/pnas.97.8.4233;
Wu X., Hepner K., Castelino-Prabhu S., Do D., Kaye M.B., Yuan X.-J.,
Wood J., Ross C., Sawyers C.L., Whang Y.E.;
"Evidence for regulation of the PTEN tumor suppressor by a membrane-
localized multi-PDZ domain containing scaffold protein MAGI-2.";
Proc. Natl. Acad. Sci. U.S.A. 97:4233-4238(2000).
[21]
PHOSPHORYLATION AT SER-370; SER-380; THR-382; THR-383 AND SER-385.
PubMed=11035045; DOI=10.1074/jbc.M009134200;
Torres J., Pulido R.;
"The tumor suppressor PTEN is phosphorylated by the protein kinase CK2
at its C terminus. Implications for PTEN stability to proteasome-
mediated degradation.";
J. Biol. Chem. 276:993-998(2001).
[22]
FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH AIP1.
PubMed=11707428; DOI=10.1074/jbc.C100556200;
Vazquez F., Grossman S.R., Takahashi Y., Rokas M.V., Nakamura N.,
Sellers W.R.;
"Phosphorylation of the PTEN tail acts as an inhibitory switch by
preventing its recruitment into a protein complex.";
J. Biol. Chem. 276:48627-48630(2001).
[23]
PHOSPHORYLATION AT THR-366; SER-370 AND SER-385.
PubMed=12297295; DOI=10.1016/S0014-5793(02)03274-X;
Miller S., Lou D., Seldin D., Lane W., Neel B.;
"Direct identification of PTEN phosphorylation sites.";
FEBS Lett. 528:145-153(2002).
[24]
INTERACTION WITH NOP53, REGION, AND CHARACTERIZATION OF VARIANTS CWS1
VAL-341; GLU-343 AND GLN-345.
PubMed=15355975; DOI=10.1074/jbc.C400377200;
Okahara F., Ikawa H., Kanaho Y., Maehama T.;
"Regulation of PTEN phosphorylation and stability by a tumor
suppressor candidate protein.";
J. Biol. Chem. 279:45300-45303(2004).
[25]
INTERACTION WITH STK11, SUBCELLULAR LOCATION, AND PHOSPHORYLATION BY
STK11.
PubMed=15987703; DOI=10.1093/hmg/ddi225;
Mehenni H., Lin-Marq N., Buchet-Poyau K., Reymond A., Collart M.A.,
Picard D., Antonarakis S.E.;
"LKB1 interacts with and phosphorylates PTEN: a functional link
between two proteins involved in cancer predisposing syndromes.";
Hum. Mol. Genet. 14:2209-2219(2005).
[26]
INTERACTION WITH MAGI2; MAGI3; MAST1; MAST2 AND MAST3, MUTAGENESIS OF
VAL-403, AND PHOSPHORYLATION.
PubMed=15951562; DOI=10.1074/jbc.M504761200;
Valiente M., Andres-Pons A., Gomar B., Torres J., Gil A., Tapparel C.,
Antonarakis S.E., Pulido R.;
"Binding of PTEN to specific PDZ domains contributes to PTEN protein
stability and phosphorylation by microtubule-associated
serine/threonine kinases.";
J. Biol. Chem. 280:28936-28943(2005).
[27]
INTERACTION WITH NEDD4.
PubMed=17218260; DOI=10.1016/j.cell.2006.11.039;
Wang X., Trotman L.C., Koppie T., Alimonti A., Chen Z., Gao Z.,
Wang J., Erdjument-Bromage H., Tempst P., Cordon-Cardo C.,
Pandolfi P.P., Jiang X.;
"NEDD4-1 is a proto-oncogenic ubiquitin ligase for PTEN.";
Cell 128:129-139(2007).
[28]
FUNCTION, INTERACTION WITH USP7, UBIQUITINATION AT LYS-13 AND LYS-289,
DEUBIQUITINATION BY USP7, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-13
AND LYS-289, AND CHARACTERIZATION OF VARIANT CWS1 GLU-289.
PubMed=18716620; DOI=10.1038/nature07290;
Song M.S., Salmena L., Carracedo A., Egia A., Lo-Coco F.,
Teruya-Feldstein J., Pandolfi P.P.;
"The deubiquitinylation and localization of PTEN are regulated by a
HAUSP-PML network.";
Nature 455:813-817(2008).
[29]
INTERACTION WITH FRK, PHOSPHORYLATION AT TYR-336, AND MUTAGENESIS OF
TYR-336.
PubMed=19345329; DOI=10.1016/j.ccr.2009.02.012;
Yim E.-K., Peng G., Dai H., Hu R., Li K., Lu Y., Mills G.B.,
Meric-Bernstam F., Hennessy B.T., Craven R.J., Lin S.-Y.;
"Rak functions as a tumor suppressor by regulating PTEN protein
stability and function.";
Cancer Cell 15:304-314(2009).
[30]
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).
[31]
PHOSPHORYLATION AT THR-366 AND SER-370, AND MUTAGENESIS OF 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).
[32]
INTERACTION WITH NDFIP1 AND NDFIP2.
PubMed=20534535; DOI=10.1073/pnas.0911714107;
Mund T., Pelham H.R.;
"Regulation of PTEN/Akt and MAP kinase signaling pathways by the
ubiquitin ligase activators Ndfip1 and Ndfip2.";
Proc. Natl. Acad. Sci. U.S.A. 107:11429-11434(2010).
[33]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[34]
FUNCTION IN CELL MIGRATION.
PubMed=22279049; DOI=10.1101/gad.177642.111;
Stohr N., Kohn M., Lederer M., Glass M., Reinke C., Singer R.H.,
Huttelmaier S.;
"IGF2BP1 promotes cell migration by regulating MK5 and PTEN
signaling.";
Genes Dev. 26:176-189(2012).
[35]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[36]
ALTERNATIVE INITIATION (ISOFORM ALPHA), CTG START CODON, FUNCTION
(ISOFORM ALPHA), AND SUBCELLULAR LOCATION (ISOFORM ALPHA).
PubMed=23744781; DOI=10.1126/science.1234907;
Hopkins B.D., Fine B., Steinbach N., Dendy M., Rapp Z., Shaw J.,
Pappas K., Yu J.S., Hodakoski C., Mense S., Klein J., Pegno S.,
Sulis M.L., Goldstein H., Amendolara B., Lei L., Maurer M., Bruce J.,
Canoll P., Hibshoosh H., Parsons R.;
"A secreted PTEN phosphatase that enters cells to alter signaling and
survival.";
Science 341:399-402(2013).
[37]
INTERACTION WITH PPP1R16B.
PubMed=25007873; DOI=10.1152/ajprenal.00070.2014;
Obeidat M., Li L., Ballermann B.J.;
"TIMAP promotes angiogenesis by suppressing PTEN-mediated Akt
inhibition in human glomerular endothelial cells.";
Am. J. Physiol. 307:F623-F633(2014).
[38]
ALTERNATIVE INITIATION (ISOFORM ALPHA), CTG START CODON, SUBCELLULAR
LOCATION (ISOFORM ALPHA), AND MUTAGENESIS OF MET-1.
PubMed=24768297; DOI=10.1016/j.cmet.2014.03.023;
Liang H., He S., Yang J., Jia X., Wang P., Chen X., Zhang Z., Zou X.,
McNutt M.A., Shen W.H., Yin Y.;
"PTENalpha, a PTEN isoform translated through alternative initiation,
regulates mitochondrial function and energy metabolism.";
Cell Metab. 19:836-848(2014).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-366, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[40]
INTERACTION WITH NDFIP1, AND 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).
[41]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 8-353 IN COMPLEX WITH
L(+)-TARTRATE, SUBUNIT, DOMAIN, AND MUTAGENESIS OF ASP-92; HIS-93;
LYS-125; LYS-128; THR-167; GLN-171; 263-LYS--ALA-269 AND
327-LYS--ALA-335.
PubMed=10555148; DOI=10.1016/S0092-8674(00)81663-3;
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).
[42]
VARIANT CWS1 ASN-137 INS.
PubMed=9345101; DOI=10.1086/301607;
Tsou H.C., Teng D.H.-F., Ping X.L., Brancolini V., Davis T., Hu R.,
Xie X.X., Gruener A.C., Schrager C.A., Christiano A.M., Eng C.,
Steck P., Ott J., Tavtigian S.V., Peacocke M.;
"The role of MMAC1 mutations in early-onset breast cancer: causative
in association with Cowden syndrome and excluded in BRCA1-negative
cases.";
Am. J. Hum. Genet. 61:1036-1043(1997).
[43]
VARIANTS CWS1 GLU-343 AND LEU-347.
PubMed=9399897; DOI=10.1086/301639;
Lynch E.D., Ostermeyer E.A., Lee M.K., Arena J.F., Ji H., Dann J.,
Swisshelm K., Suchard D., MacLeod P.M., Kvinnsland S., Gjertsen B.T.,
Heimdal K., Lubs H., Moeller P., King M.-C.;
"Inherited mutations in PTEN that are associated with breast cancer,
Cowden disease, and juvenile polyposis.";
Am. J. Hum. Genet. 61:1254-1260(1997).
[44]
VARIANTS GLIOBLASTOMA TYR-107; PRO-121; ARG-129; ARG-165 AND GLN-345.
PubMed=9331071;
Wang S.I., Puc J., Li J., Bruce J.N., Cairns P., Sidransky D.,
Parsons R.;
"Somatic mutations of PTEN in glioblastoma multiforme.";
Cancer Res. 57:4183-4186(1997).
[45]
VARIANTS CWS1 ARG-123 AND ARG-124.
PubMed=9259288; DOI=10.1093/hmg/6.8.1383;
Nelen M.R., van Staveren W.C.G., Peeters E.A.J., Ben-Hassel M.,
Gorlin R.J., Hamm H., Lindboe C.F., Fryns J.-P., Sijmons R.H.,
Woods D.G., Mariman E.C.M., Padberg G.W., Kremer H.;
"Germline mutations in the PTEN/MMAC1 gene in patients with Cowden
disease.";
Hum. Mol. Genet. 6:1383-1387(1997).
[46]
VARIANT CWS1 GLU-129.
PubMed=9140396; DOI=10.1038/ng0597-64;
Liaw D., Marsh D.J., Li J., Dahia P.L.M., Wang S.I., Zheng Z.,
Bose S., Call K.M., Tsou H.C., Peacocke M., Eng C., Parsons R.;
"Germline mutations of the PTEN gene in Cowden disease, an inherited
breast and thyroid cancer syndrome.";
Nat. Genet. 16:64-67(1997).
[47]
VARIANT BRRS ARG-170.
PubMed=9241266; DOI=10.1038/ng0897-333;
Marsh D.J., Dahia P.L.M., Zheng Z., Liaw D., Parsons R., Gorlin R.J.,
Eng C.;
"Germline mutations in PTEN are present in Bannayan-Zonana syndrome.";
Nat. Genet. 16:333-334(1997).
[48]
VARIANTS ENDOMETRIAL HYPERPLASIA ARG-36; LEU-130; CYS-173; ALA-191 AND
ILE-348.
PubMed=9635567;
Maxwell G.L., Risinger J.I., Gumbs C., Shaw H., Bentley R.C.,
Barrett J.C., Berchuck A., Futreal P.A.;
"Mutation of the PTEN tumor suppressor gene in endometrial
hyperplasias.";
Cancer Res. 58:2500-2503(1998).
[49]
VARIANT CWS1 GLU-289.
PubMed=9797362; DOI=10.1016/S0016-5085(98)70078-2;
Chi S.-G., Kim H.-J., Park B.-J., Min H.-J., Park J.-H., Kim Y.-W.,
Dong S.-H., Kim B.-H., Lee J.-I., Chang Y.-W., Chang R., Kim W.-K.,
Yang M.-H.;
"Mutational abrogation of the PTEN/MMAC1 gene in gastrointestinal
polyps in patients with Cowden disease.";
Gastroenterology 115:1084-1089(1998).
[50]
VARIANTS CWS1 HIS-68 AND PRO-112.
PubMed=9600246; DOI=10.1007/s004390050723;
Tsou H.C., Ping X.L., Xie X.X., Gruener A.C., Zhang H., Nini R.,
Swisshelm K., Sybert V., Diamond T.M., Sutphen R., Peacocke M.;
"The genetic basis of Cowden's syndrome: three novel mutations in
PTEN/MMAC1/TEP1.";
Hum. Genet. 102:467-473(1998).
[51]
VARIANTS CWS1 AND BRRS.
PubMed=9467011; DOI=10.1093/hmg/7.3.507;
Marsh D.J., Coulon V., Lunetta K.L., Rocca-Serra P., Dahia P.L.M.,
Zheng Z., Liaw D., Caron S., Duboue B., Lin A.Y., Richardson A.-L.,
Bonnetblanc J.-M., Bressieux J.-M., Cabarrot-Moreau A., Chompret A.,
Demange L., Eeles R.A., Yahanda A.M., Fearon E.R., Fricker J.-P.,
Gorlin R.J., Hodgson S.V., Huson S., Lacombe D., Leprat F., Odent S.,
Toulouse C., Olopade O.I., Sobol H., Tishler S., Woods C.G.,
Robinson B.G., Weber H.C., Parsons R., Peacocke M., Longy M., Eng C.;
"Mutation spectrum and genotype-phenotype analyses in Cowden disease
and Bannayan-Zonana syndrome, two hamartoma syndromes with germline
PTEN mutation.";
Hum. Mol. Genet. 7:507-515(1998).
[52]
VARIANT CWS1 TYR-136.
PubMed=9735393;
Scala S., Bruni P., Lo Muzio L., Mignogna M., Viglietto G., Fusco A.;
"Novel mutation of the PTEN gene in an Italian Cowden's disease
kindred.";
Int. J. Oncol. 13:665-668(1998).
[53]
VARIANT CWS1 PRO-70.
PubMed=9832031; DOI=10.1136/jmg.35.11.881;
Marsh D.J., Dahia P.L.M., Caron S., Kum J.B., Frayling I.M.,
Tomlinson I.P.M., Hughes K.S., Eeles R.A., Hodgson S.V., Murday V.A.,
Houlston R., Eng C.;
"Germline PTEN mutations in Cowden syndrome-like families.";
J. Med. Genet. 35:881-885(1998).
[54]
VARIANT CWS1 ARG-35.
PubMed=9425889; DOI=10.1038/ng0198-12;
Olschwang S., Serova-Sinilnikova O.M., Lenoir G.M., Thomas G.;
"PTEN germ-line mutations in juvenile polyposis coli.";
Nat. Genet. 18:12-14(1998).
[55]
VARIANT CWS1 GLN-130.
PubMed=9915974; DOI=10.1086/302207;
Kurose K., Araki T., Matsunaka T., Takada Y., Emi M.;
"Variant manifestation of Cowden disease in Japan: hamartomatous
polyposis of the digestive tract with mutation of the PTEN gene.";
Am. J. Hum. Genet. 64:308-310(1999).
[56]
VARIANT CWS1/LDD PRO-112.
PubMed=10051160;
DOI=10.1002/(SICI)1096-8628(19990212)82:4<290::AID-AJMG3>3.0.CO;2-0;
Sutphen R., Diamond T.M., Minton S.E., Peacocke M., Tsou H.C.,
Root A.W.;
"Severe Lhermitte-Duclos disease with unique germline mutation of
PTEN.";
Am. J. Med. Genet. 82:290-293(1999).
[57]
VARIANTS CWS1 ILE-33 DEL; ARG-123; ARG-124 AND GLU-165.
PubMed=10234502; DOI=10.1038/sj.ejhg.5200289;
Nelen M.R., Kremer H., Konings I.B.M., Schoute F., van Essen A.J.,
Koch R., Woods C.G., Fryns J.-P., Hamel B.C.J., Hoefsloot L.H.,
Peeters E.A.J., Padberg G.W.;
"Novel PTEN mutations in patients with Cowden disease: absence of
clear genotype-phenotype correlations.";
Eur. J. Hum. Genet. 7:267-273(1999).
[58]
VARIANTS BRRS ASP-34; HIS-68; TYR-105; VAL-135; ARG-170 AND LEU-246.
PubMed=10400993; DOI=10.1093/hmg/8.8.1461;
Marsh D.J., Kum J.B., Lunetta K.L., Bennett M.J., Gorlin R.J.,
Ahmed S.F., Bodurtha J., Crowe C., Curtis M.A., Dasouki M., Dunn T.,
Feit H., Geraghty M.T., Graham J.M. Jr., Hodgson S.V., Hunter A.,
Korf B.R., Manchester D., Miesfeldt S., Murday V.A., Nathanson K.L.,
Parisi M., Pober B., Romano C., Tolmie J.L., Trembath R., Winter R.M.,
Zackai E.H., Zori R.T., Weng L.-P., Dahia P.L.M., Eng C.;
"PTEN mutation spectrum and genotype-phenotype correlations in
Bannayan-Riley-Ruvalcaba syndrome suggest a single entity with Cowden
syndrome.";
Hum. Mol. Genet. 8:1461-1472(1999).
[59]
CHARACTERIZATION OF VARIANTS ASN-10; CYS-16; GLU-20; SER-27; ARG-61;
HIS-68; CWS1 TYR-71; CWS1 TYR-93; BRRS PHE-105; BRRS TYR-107; PRO-112;
ARG-112; PRO-121; ARG-124; ARG-129; GLU-129; GLY-130; CWS1 LEU-130;
GLN-130; ILE-133; LEU-134; TYR-136; CYS-155; ARG-165; ASN-170;
ARG-170; CYS-173; HIS-173; PRO-173; ASN-174; PHE-227; CYS-251;
GLU-289; GLY-331; VAL-341; ASN-342; GLU-343; GLN-345; LEU-347; GLY-369
AND ILE-401.
PubMed=10866302;
Han S.-Y., Kato H., Kato S., Suzuki T., Shibata H., Ishii S.,
Shiiba K., Matsuno S., Kanamaru R., Ishioka C.;
"Functional evaluation of PTEN missense mutations using in vitro
phosphoinositide phosphatase assay.";
Cancer Res. 60:3147-3151(2000).
[60]
VARIANTS MULTIPLE CANCERS LEU-119 AND LEU-158.
PubMed=10807691; DOI=10.1136/jmg.37.5.336;
De Vivo I., Gertig D.M., Nagase S., Hankinson S.E., O'Brien R.,
Speizer F.E., Parsons R., Hunter D.J.;
"Novel germline mutations in the PTEN tumour suppressor gene found in
women with multiple cancers.";
J. Med. Genet. 37:336-341(2000).
[61]
VARIANTS MALIGNANT MELANOMA ASN-19 AND ILE-217.
PubMed=10978354; DOI=10.1136/jmg.37.9.653;
Celebi J.T., Shendrik I., Silvers D.N., Peacocke M.;
"Identification of PTEN mutations in metastatic melanoma specimens.";
J. Med. Genet. 37:653-657(2000).
[62]
CHARACTERIZATION OF VARIANTS CWS1 SER-124 AND GLU-129.
PubMed=11230179; DOI=10.1093/hmg/10.6.599;
Weng L.-P., Brown J.L., Eng C.;
"PTEN coordinates G1 arrest by down-regulating cyclin D1 via its
protein phosphatase activity and up-regulating p27 via its lipid
phosphatase activity in a breast cancer model.";
Hum. Mol. Genet. 10:599-604(2001).
[63]
VARIANT VATER ASP-61.
PubMed=11748304; DOI=10.1136/jmg.38.12.820;
Reardon W., Zhou X.-P., Eng C.;
"A novel germline mutation of the PTEN gene in a patient with
macrocephaly, ventricular dilatation, and features of VATER
association.";
J. Med. Genet. 38:820-823(2001).
[64]
VARIANT CWS1 GLY-47, AND VARIANTS BRRS ASP-34; HIS-68; TYR-105;
VAL-135 AND ARG-170.
PubMed=11494117; DOI=10.1038/sj.neo.7900154;
Marsh D.J., Theodosopoulos G., Howell V., Richardson A.-L., Benn D.E.,
Proos A.L., Eng C., Robinson B.G.;
"Rapid mutation scanning of genes associated with familial cancer
syndromes using denaturing high-performance liquid chromatography.";
Neoplasia 3:236-244(2001).
[65]
VARIANT GLM2 GLN-234, AND CHARACTERIZATION OF VARIANT GLM2 GLN-234.
PubMed=12085208; DOI=10.1038/sj.bjc.6600206;
Staal F.J.T., van der Luijt R.B., Baert M.R.M., van Drunen J.,
van Bakel H., Peters E., de Valk I., van Amstel H.K.P.,
Taphoorn M.J.B., Jansen G.H., van Veelen C.W.M., Burgering B.,
Staal G.E.J.;
"A novel germline mutation of PTEN associated with brain tumours of
multiple lineages.";
Br. J. Cancer 86:1586-1591(2002).
[66]
VARIANT HNSCC GLY-121.
PubMed=11801303; DOI=10.1016/S0165-4608(01)00509-X;
Poetsch M., Lorenz G., Kleist B.;
"Detection of new PTEN/MMAC1 mutations in head and neck squamous cell
carcinomas with loss of chromosome 10.";
Cancer Genet. Cytogenet. 132:20-24(2002).
[67]
DISCUSSION OF PTEN INVOLVEMENT IN PROTEUS SYNDROME.
PubMed=12471211; DOI=10.1136/jmg.39.12.937;
Smith J.M., Kirk E.P.E., Theodosopoulos G., Marshall G.M., Walker J.,
Rogers M., Field M., Brereton J.J., Marsh D.J.;
"Germline mutation of the tumour suppressor PTEN in Proteus
syndrome.";
J. Med. Genet. 39:937-940(2002).
[68]
VARIANTS MCEPHAS ARG-93; SER-241 AND GLY-252.
PubMed=15805158; DOI=10.1136/jmg.2004.024646;
Butler M.G., Dasouki M.J., Zhou X.-P., Talebizadeh Z., Brown M.,
Takahashi T.N., Miles J.H., Wang C.H., Stratton R., Pilarski R.,
Eng C.;
"Subset of individuals with autism spectrum disorders and extreme
macrocephaly associated with germline PTEN tumour suppressor gene
mutations.";
J. Med. Genet. 42:318-321(2005).
[69]
INVOLVEMENT IN CHROMOSOME 10Q23 DELETION SYNDROME.
PubMed=17436248; DOI=10.1086/513607;
Balciuniene J., Feng N., Iyadurai K., Hirsch B., Charnas L.,
Bill B.R., Easterday M.C., Staaf J., Oseth L., Czapansky-Beilman D.,
Avramopoulos D., Thomas G.H., Borg A., Valle D., Schimmenti L.A.,
Selleck S.B.;
"Recurrent 10q22-q23 deletions: a genomic disorder on 10q associated
with cognitive and behavioral abnormalities.";
Am. J. Hum. Genet. 80:938-947(2007).
[70]
VARIANT VAL-132.
PubMed=16752378; DOI=10.1002/ajmg.a.31273;
Tekin M., Hismi B.O., Fitoz S., Yalcinkaya F., Ekim M., Kansu A.,
Ertem M., Deda G., Tutar E., Arsan S., Zhou X.-P., Pilarski R.,
Eng C., Akar N.;
"A germline PTEN mutation with manifestations of prenatal onset and
verrucous epidermal nevus.";
Am. J. Med. Genet. A 140:1472-1475(2006).
[71]
VARIANTS MCEPHAS ILE-131 AND ASN-167.
PubMed=23160955; DOI=10.1126/science.1227764;
O'Roak B.J., Vives L., Fu W., Egertson J.D., Stanaway I.B.,
Phelps I.G., Carvill G., Kumar A., Lee C., Ankenman K., Munson J.,
Hiatt J.B., Turner E.H., Levy R., O'Day D.R., Krumm N., Coe B.P.,
Martin B.K., Borenstein E., Nickerson D.A., Mefford H.C., Doherty D.,
Akey J.M., Bernier R., Eichler E.E., Shendure J.;
"Multiplex targeted sequencing identifies recurrently mutated genes in
autism spectrum disorders.";
Science 338:1619-1622(2012).
[72]
VARIANT MCEPHAS 65-TYR--VAL-403 DEL.
PubMed=26637798; DOI=10.1016/j.neuron.2015.11.009;
D'Gama A.M., Pochareddy S., Li M., Jamuar S.S., Reiff R.E., Lam A.T.,
Sestan N., Walsh C.A.;
"Targeted DNA Sequencing from Autism Spectrum Disorder Brains
Implicates Multiple Genetic Mechanisms.";
Neuron 88:910-917(2015).
[73]
VARIANT PROSTATE CANCER GLY-126, CHARACTERIZATION OF VARIANT GLY-126,
MUTAGENESIS OF ALA-126, AND FUNCTION.
PubMed=26504226; DOI=10.1073/pnas.1422504112;
Costa H.A., Leitner M.G., Sos M.L., Mavrantoni A., Rychkova A.,
Johnson J.R., Newton B.W., Yee M.C., De La Vega F.M., Ford J.M.,
Krogan N.J., Shokat K.M., Oliver D., Halaszovich C.R.,
Bustamante C.D.;
"Discovery and functional characterization of a neomorphic PTEN
mutation.";
Proc. Natl. Acad. Sci. U.S.A. 112:13976-13981(2015).
-!- 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 (PubMed:26504226). 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. In
motile cells, suppresses the formation of lateral pseudopods and
thereby promotes cell polarization and directed movement.
{ECO:0000269|PubMed:26504226}.
-!- FUNCTION: Isoform alpha: Functional kinase, like isoform 1 it
antagonizes the PI3K-AKT/PKB signaling pathway. Plays a role in
mitochondrial energetic metabolism by promoting COX activity and
ATP production, via collaboration with isoform 1 in increasing
protein levels of PINK1.
-!- 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 and with DLG1 and MAST2 in vitro
(PubMed:10646847, PubMed:10760291, PubMed:11707428). Interacts
with MAGI2, MAGI3, MAST1 and MAST3, but neither with MAST4 nor
with DLG5; interaction with MAGI2 increases protein stability
(PubMed:10748157, PubMed:15951562). Interacts with NEDD4
(PubMed:17218260). Interacts with NDFIP1 and NDFIP2; in the
presence of NEDD4 or ITCH, this interaction promotes PTEN
ubiquitination (PubMed:25801959, PubMed:20534535). Interacts (via
C2 domain) with FRK (PubMed:19345329). Interacts with USP7; the
interaction is direct (PubMed:18716620). Interacts with ROCK1 (By
similarity). Interacts with XIAP/BIRC4 (PubMed:19473982).
Interacts with STK11; the interaction phosphorylates PTEN
(PubMed:15987703). Interacts with PPP1R16B (PubMed:25007873).
Interacts with NOP53; regulates PTEN phosphorylation and increases
its stability (PubMed:15355975). {ECO:0000250|UniProtKB:O08586,
ECO:0000269|PubMed:10555148, ECO:0000269|PubMed:10646847,
ECO:0000269|PubMed:10748157, ECO:0000269|PubMed:10760291,
ECO:0000269|PubMed:11707428, ECO:0000269|PubMed:15355975,
ECO:0000269|PubMed:15951562, ECO:0000269|PubMed:15987703,
ECO:0000269|PubMed:17218260, ECO:0000269|PubMed:18716620,
ECO:0000269|PubMed:19345329, ECO:0000269|PubMed:19473982,
ECO:0000269|PubMed:20534535, ECO:0000269|PubMed:25007873,
ECO:0000269|PubMed:25801959}.
-!- INTERACTION:
Self; NbExp=9; IntAct=EBI-696162, EBI-696162;
P35226:BMI1; NbExp=3; IntAct=EBI-696162, EBI-2341576;
P30260:CDC27; NbExp=7; IntAct=EBI-696162, EBI-994813;
Q16643:DBN1; NbExp=5; IntAct=EBI-696162, EBI-351394;
Q62696:Dlg1 (xeno); NbExp=2; IntAct=EBI-696162, EBI-389325;
P42685:FRK; NbExp=7; IntAct=EBI-696162, EBI-1383583;
O88382:Magi2 (xeno); NbExp=3; IntAct=EBI-696162, EBI-696179;
Q9JK71:Magi3 (xeno); NbExp=3; IntAct=EBI-696162, EBI-696226;
Q9R1L5:Mast1 (xeno); NbExp=3; IntAct=EBI-696162, EBI-491771;
Q60592:Mast2 (xeno); NbExp=4; IntAct=EBI-696162, EBI-493888;
O60307:MAST3; NbExp=3; IntAct=EBI-696162, EBI-311420;
Q9Y6Q9:NCOA3; NbExp=2; IntAct=EBI-696162, EBI-81196;
P46934:NEDD4; NbExp=4; IntAct=EBI-696162, EBI-726944;
P09619:PDGFRB; NbExp=3; IntAct=EBI-696162, EBI-641237;
P62136:PPP1CA; NbExp=2; IntAct=EBI-696162, EBI-357253;
Q06830:PRDX1; NbExp=7; IntAct=EBI-696162, EBI-353193;
O14745:SLC9A3R1; NbExp=7; IntAct=EBI-696162, EBI-349787;
Q15599:SLC9A3R2; NbExp=5; IntAct=EBI-696162, EBI-1149760;
Q9JHL1:Slc9a3r2 (xeno); NbExp=2; IntAct=EBI-696162, EBI-538451;
O43791:SPOP; NbExp=4; IntAct=EBI-696162, EBI-743549;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15987703,
ECO:0000269|PubMed:18716620, ECO:0000269|PubMed:19473982,
ECO:0000269|PubMed:25801959, ECO:0000269|PubMed:9187108}. Nucleus
{ECO:0000269|PubMed:15987703, ECO:0000269|PubMed:18716620,
ECO:0000269|PubMed:19473982, ECO:0000269|PubMed:25801959}.
Nucleus, PML body {ECO:0000269|PubMed:18716620}.
Note=Monoubiquitinated form is nuclear. Nonubiquitinated form is
cytoplasmic. Colocalized with PML and USP7 in PML nuclear bodies
(PubMed:18716620). XIAP/BIRC4 promotes its nuclear localization
(PubMed:19473982). {ECO:0000269|PubMed:18716620,
ECO:0000269|PubMed:19473982}.
-!- SUBCELLULAR LOCATION: Isoform alpha: Secreted
{ECO:0000269|PubMed:23744781, ECO:0000269|PubMed:24768297}.
Note=May be secreted via a classical signal peptide and reenter
into cells with the help of a poly-Arg motif.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=3;
Name=1; Synonyms=55kDa;
IsoId=P60484-1; Sequence=Displayed;
Name=alpha; Synonyms=70kDa, PTEN-long;
IsoId=P60484-2; Sequence=VSP_055420;
Note=Produced by alternative initiation at a CTG start codon of
isoform 1. May contain a signal peptide at positions 1-21.;
Name=3;
IsoId=P60484-3; Sequence=VSP_055421, VSP_055422, VSP_055423;
-!- TISSUE SPECIFICITY: Expressed at a relatively high level in all
adult tissues, including heart, brain, placenta, lung, liver,
muscle, kidney and pancreas. {ECO:0000269|PubMed:9090379}.
-!- INDUCTION: Down-regulated by TGFB1. {ECO:0000269|PubMed:9187108}.
-!- DOMAIN: The C2 domain binds phospholipid membranes in vitro in a
Ca(2+)-independent manner; this binding is important for its tumor
suppressor function. {ECO:0000269|PubMed:10468583,
ECO:0000269|PubMed:10555148}.
-!- PTM: Constitutively phosphorylated by CK2 under normal conditions.
Phosphorylated in vitro by MAST1, MAST2, MAST3 and STK11.
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. Phosphorylation by ROCK1 is essential for its stability
and activity. Phosphorylation by PLK3 promotes its stability and
prevents its degradation by the proteasome.
{ECO:0000269|PubMed:10646847, ECO:0000269|PubMed:11035045,
ECO:0000269|PubMed:11707428, ECO:0000269|PubMed:12297295,
ECO:0000269|PubMed:15951562, ECO:0000269|PubMed:15987703,
ECO:0000269|PubMed:18716620, ECO:0000269|PubMed:19345329,
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. Ubiquitinated by XIAP/BIRC4.
{ECO:0000269|PubMed:18716620, ECO:0000269|PubMed:19473982}.
-!- DISEASE: Cowden syndrome 1 (CWS1) [MIM:158350]: An autosomal
dominant hamartomatous polyposis syndrome with age-related
penetrance. Cowden syndrome is characterized by hamartomatous
lesions affecting derivatives of ectodermal, mesodermal and
endodermal layers, macrocephaly, facial trichilemmomas (benign
tumors of the hair follicle infundibulum), acral keratoses,
papillomatous papules, and elevated risk for development of
several types of malignancy, particularly breast carcinoma in
women and thyroid carcinoma in both men and women. Colon cancer
and renal cell carcinoma have also been reported. Hamartomas can
be found in virtually every organ, but most commonly in the skin,
gastrointestinal tract, breast and thyroid.
{ECO:0000269|PubMed:10051160, ECO:0000269|PubMed:10234502,
ECO:0000269|PubMed:11230179, ECO:0000269|PubMed:11494117,
ECO:0000269|PubMed:15355975, ECO:0000269|PubMed:18716620,
ECO:0000269|PubMed:9140396, ECO:0000269|PubMed:9259288,
ECO:0000269|PubMed:9345101, ECO:0000269|PubMed:9399897,
ECO:0000269|PubMed:9425889, ECO:0000269|PubMed:9467011,
ECO:0000269|PubMed:9600246, ECO:0000269|PubMed:9735393,
ECO:0000269|PubMed:9797362, ECO:0000269|PubMed:9811831,
ECO:0000269|PubMed:9832031, ECO:0000269|PubMed:9915974}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Lhermitte-Duclos disease (LDD) [MIM:158350]: A rare
disease characterized by the occurrence of a slowly enlarging mass
within the cerebellar cortex corresponding histologically to a
cerebellar hamartoma. It manifests, most commonly in the third and
fourth decades of life, with increased intracranial pressure,
headache, nausea, cerebellar dysfunction, occlusive hydrocephalus,
ataxia, visual disturbances and other cranial nerve palsies.
Various associated abnormalities may be present such as
megalencephaly, microgyria, hydromyelia, polydactyly, partial
gigantism, macroglossia. LDD is part of the PTEN hamartoma tumor
syndromes spectrum that also includes Cowden syndrome. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Bannayan-Riley-Ruvalcaba syndrome (BRRS) [MIM:153480]: A
rare hamartomatous disorder characterized by macrocephaly and
multiple hemangiomas as well as subcutaneous and visceral lipomas.
It belongs to the family of hamartomatous polyposis syndromes that
includes Peutz Jeghers syndrome, juvenile polyposis, and Cowden
syndrome. {ECO:0000269|PubMed:10400993,
ECO:0000269|PubMed:11494117, ECO:0000269|PubMed:9241266,
ECO:0000269|PubMed:9467011}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Squamous cell carcinoma of the head and neck (HNSCC)
[MIM:275355]: A non-melanoma skin cancer affecting the head and
neck. The hallmark of cutaneous SCC is malignant transformation of
normal epidermal keratinocytes. {ECO:0000269|PubMed:11801303}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Endometrial cancer (ENDMC) [MIM:608089]: A malignancy of
endometrium, the mucous lining of the uterus. Most endometrial
cancers are adenocarcinomas, cancers that begin in cells that make
and release mucus and other fluids. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Note=PTEN mutations are found in a subset of patients
with Proteus syndrome, a genetically heterogeneous condition. The
molecular diagnosis of PTEN mutation positive cases classifies
Proteus syndrome patients as part of the PTEN hamartoma syndrome
spectrum. As such, patients surviving the early years of Proteus
syndrome are likely at a greater risk of developing malignancies.
-!- DISEASE: Glioma 2 (GLM2) [MIM:613028]: Gliomas are benign or
malignant central nervous system neoplasms derived from glial
cells. They comprise astrocytomas and glioblastoma multiforme that
are derived from astrocytes, oligodendrogliomas derived from
oligodendrocytes and ependymomas derived from ependymocytes.
{ECO:0000269|PubMed:12085208}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: VACTERL association with hydrocephalus (VACTERL-H)
[MIM:276950]: VACTERL is an acronym for vertebral anomalies, anal
atresia, congenital cardiac disease, tracheoesophageal fistula,
renal anomalies, radial dysplasia, and other limb defects.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Prostate cancer (PC) [MIM:176807]: A malignancy
originating in tissues of the prostate. Most prostate cancers are
adenocarcinomas that develop in the acini of the prostatic ducts.
Other rare histopathologic types of prostate cancer that occur in
approximately 5% of patients include small cell carcinoma,
mucinous carcinoma, prostatic ductal carcinoma, transitional cell
carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid
cystic carcinoma (basaloid), signet-ring cell carcinoma and
neuroendocrine carcinoma. {ECO:0000269|PubMed:26504226,
ECO:0000269|PubMed:9072974}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Macrocephaly/autism syndrome (MCEPHAS) [MIM:605309]:
Patients have autism spectrum disorders and macrocephaly, with
head circumferences ranging from +2.5 to +8 SD for age and sex
(average head circumference +4.0 SD).
{ECO:0000269|PubMed:15805158, ECO:0000269|PubMed:23160955,
ECO:0000269|PubMed:26637798}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=A microdeletion of chromosome 10q23 involving BMPR1A
and PTEN is a cause of chromosome 10q23 deletion syndrome, which
shows overlapping features of the following three disorders:
Bannayan-Zonana syndrome, Cowden disease and juvenile polyposis
syndrome.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PTENID158.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/pten/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; U96180; AAB66902.1; -; mRNA.
EMBL; U92436; AAC51182.1; -; mRNA.
EMBL; U93051; AAC51183.1; -; mRNA.
EMBL; AF143315; AAD38372.1; -; Genomic_DNA.
EMBL; AF143312; AAD38372.1; JOINED; Genomic_DNA.
EMBL; AF143313; AAD38372.1; JOINED; Genomic_DNA.
EMBL; AF143314; AAD38372.1; JOINED; Genomic_DNA.
EMBL; AF000734; AAC08699.1; -; Genomic_DNA.
EMBL; AF000726; AAC08699.1; JOINED; Genomic_DNA.
EMBL; AF000727; AAC08699.1; JOINED; Genomic_DNA.
EMBL; AF000728; AAC08699.1; JOINED; Genomic_DNA.
EMBL; AF000729; AAC08699.1; JOINED; Genomic_DNA.
EMBL; AF000730; AAC08699.1; JOINED; Genomic_DNA.
EMBL; AF000731; AAC08699.1; JOINED; Genomic_DNA.
EMBL; AF000732; AAC08699.1; JOINED; Genomic_DNA.
EMBL; AF000733; AAC08699.1; JOINED; Genomic_DNA.
EMBL; AF067844; AAD13528.1; -; Genomic_DNA.
EMBL; JF268690; ADZ48535.1; -; mRNA.
EMBL; CR450306; CAG29302.1; -; mRNA.
EMBL; AK313581; BAG36351.1; -; mRNA.
EMBL; DQ073384; AAY57327.1; -; Genomic_DNA.
EMBL; CH471066; EAW50174.1; -; Genomic_DNA.
EMBL; BC005821; AAH05821.1; -; mRNA.
CCDS; CCDS31238.1; -. [P60484-1]
RefSeq; NP_000305.3; NM_000314.6. [P60484-1]
RefSeq; NP_001291646.2; NM_001304717.2.
RefSeq; NP_001291647.1; NM_001304718.1.
UniGene; Hs.500466; -.
UniGene; Hs.729457; -.
PDB; 1D5R; X-ray; 2.10 A; A=8-353.
PDB; 2KYL; NMR; -; B=391-403.
PDB; 4O1V; X-ray; 2.00 A; B=354-368.
PDB; 5BUG; X-ray; 2.40 A; A/B/C/D=14-351.
PDB; 5BZX; X-ray; 2.50 A; A/B/C/D=14-351.
PDB; 5BZZ; X-ray; 2.20 A; A/B/C/D=14-351.
PDBsum; 1D5R; -.
PDBsum; 2KYL; -.
PDBsum; 4O1V; -.
PDBsum; 5BUG; -.
PDBsum; 5BZX; -.
PDBsum; 5BZZ; -.
ProteinModelPortal; P60484; -.
SMR; P60484; -.
BioGrid; 111700; 280.
DIP; DIP-35019N; -.
ELM; P60484; -.
IntAct; P60484; 52.
MINT; MINT-127351; -.
STRING; 9606.ENSP00000361021; -.
BindingDB; P60484; -.
ChEMBL; CHEMBL2052032; -.
GuidetoPHARMACOLOGY; 2497; -.
SwissLipids; SLP:000000849; -.
DEPOD; P60484; -.
iPTMnet; P60484; -.
PhosphoSitePlus; P60484; -.
BioMuta; PTEN; -.
DMDM; 42560209; -.
EPD; P60484; -.
MaxQB; P60484; -.
PaxDb; P60484; -.
PeptideAtlas; P60484; -.
PRIDE; P60484; -.
DNASU; 5728; -.
Ensembl; ENST00000371953; ENSP00000361021; ENSG00000171862. [P60484-1]
GeneID; 5728; -.
KEGG; hsa:5728; -.
UCSC; uc001kfb.4; human. [P60484-1]
CTD; 5728; -.
DisGeNET; 5728; -.
GeneCards; PTEN; -.
GeneReviews; PTEN; -.
HGNC; HGNC:9588; PTEN.
HPA; CAB004076; -.
HPA; HPA031335; -.
MalaCards; PTEN; -.
MIM; 137800; phenotype.
MIM; 153480; phenotype.
MIM; 158350; phenotype.
MIM; 176807; phenotype.
MIM; 275355; phenotype.
MIM; 276950; phenotype.
MIM; 601728; gene.
MIM; 605309; phenotype.
MIM; 608089; phenotype.
MIM; 612242; phenotype.
MIM; 613028; phenotype.
neXtProt; NX_P60484; -.
OpenTargets; ENSG00000171862; -.
Orphanet; 109; Bannayan-Riley-Ruvalcaba syndrome.
Orphanet; 201; Cowden syndrome.
Orphanet; 145; Hereditary breast and ovarian cancer syndrome.
Orphanet; 79076; Juvenile polyposis of infancy.
Orphanet; 65285; Lhermitte-Duclos disease.
Orphanet; 210548; Macrocephaly-autism syndrome.
Orphanet; 744; Proteus syndrome.
Orphanet; 2969; Proteus-like syndrome.
Orphanet; 137608; Segmental outgrowth - lipomatosis - arteriovenous malformation - epidermal nevus.
Orphanet; 67037; Squamous cell carcinoma of head and neck.
PharmGKB; PA33942; -.
eggNOG; KOG2283; Eukaryota.
eggNOG; COG2453; LUCA.
GeneTree; ENSGT00760000119113; -.
HOGENOM; HOG000008008; -.
HOVERGEN; HBG000239; -.
InParanoid; P60484; -.
KO; K01110; -.
OMA; PFDEEQH; -.
OrthoDB; EOG091G09VG; -.
PhylomeDB; P60484; -.
TreeFam; TF324513; -.
BioCyc; MetaCyc:HS10404-MONOMER; -.
BRENDA; 3.1.3.16; 2681.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol.
Reactome; R-HSA-199418; Negative regulation of the PI3K/AKT network.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
SignaLink; P60484; -.
SIGNOR; P60484; -.
ChiTaRS; PTEN; human.
EvolutionaryTrace; P60484; -.
GeneWiki; PTEN_(gene); -.
GenomeRNAi; 5728; -.
PMAP-CutDB; P60484; -.
PRO; PR:P60484; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000171862; -.
CleanEx; HS_PTEN; -.
CleanEx; HS_TEP1; -.
ExpressionAtlas; P60484; baseline and differential.
Genevisible; P60484; HS.
GO; GO:0016324; C:apical plasma membrane; IMP:UniProtKB.
GO; GO:0042995; C:cell projection; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0035749; C:myelin sheath adaxonal region; ISS:BHF-UCL.
GO; GO:0043005; C:neuron projection; ISS:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
GO; GO:0043220; C:Schmidt-Lanterman incisure; ISS:BHF-UCL.
GO; GO:0010997; F:anaphase-promoting complex binding; IPI:BHF-UCL.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0051717; F:inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity; IDA:UniProtKB.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IEA:Ensembl.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; IDA:UniProtKB.
GO; GO:0051800; F:phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity; IDA:UniProtKB.
GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IDA:UniProtKB.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:BHF-UCL.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; IEA:Ensembl.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
GO; GO:1990782; F:protein tyrosine kinase binding; IEA:Ensembl.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:MGI.
GO; GO:0030534; P:adult behavior; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
GO; GO:0048854; P:brain morphogenesis; ISS:BHF-UCL.
GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:BHF-UCL.
GO; GO:0048738; P:cardiac muscle tissue development; IEA:Ensembl.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0008283; P:cell proliferation; TAS:UniProtKB.
GO; GO:0071257; P:cellular response to electrical stimulus; IMP:BHF-UCL.
GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
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; ISS:UniProtKB.
GO; GO:0032286; P:central nervous system myelin maintenance; ISS:BHF-UCL.
GO; GO:0021955; P:central nervous system neuron axonogenesis; ISS:BHF-UCL.
GO; GO:0060997; P:dendritic spine morphogenesis; ISS:BHF-UCL.
GO; GO:0021542; P:dentate gyrus development; ISS:BHF-UCL.
GO; GO:0043542; P:endothelial cell migration; IEA:Ensembl.
GO; GO:0048853; P:forebrain morphogenesis; ISS:BHF-UCL.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0046855; P:inositol phosphate dephosphorylation; IDA:UniProtKB.
GO; GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
GO; GO:0007611; P:learning or memory; ISS:BHF-UCL.
GO; GO:0045475; P:locomotor rhythm; ISS:BHF-UCL.
GO; GO:0007626; P:locomotory behavior; ISS:BHF-UCL.
GO; GO:0060292; P:long term synaptic depression; IEA:Ensembl.
GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
GO; GO:0060179; P:male mating behavior; IEA:Ensembl.
GO; GO:0042711; P:maternal behavior; IEA:Ensembl.
GO; GO:0007613; P:memory; IEA:Ensembl.
GO; GO:0033555; P:multicellular organismal response to stress; ISS:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0048681; P:negative regulation of axon regeneration; IEA:Ensembl.
GO; GO:0050771; P:negative regulation of axonogenesis; ISS:BHF-UCL.
GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0090344; P:negative regulation of cell aging; IEA:Ensembl.
GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0045792; P:negative regulation of cell size; ISS: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; IDA:BHF-UCL.
GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; ISS:BHF-UCL.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:BHF-UCL.
GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; ISS:BHF-UCL.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; IMP:UniProtKB.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:BHF-UCL.
GO; GO:0051548; P:negative regulation of keratinocyte migration; IMP:BHF-UCL.
GO; GO:0031642; P:negative regulation of myelination; IEA:Ensembl.
GO; GO:0046621; P:negative regulation of organ growth; ISS:BHF-UCL.
GO; GO:0050765; P:negative regulation of phagocytosis; IEA:Ensembl.
GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; TAS:BHF-UCL.
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; IDA:BHF-UCL.
GO; GO:2000272; P:negative regulation of receptor activity; IEA:Ensembl.
GO; GO:0090071; P:negative regulation of ribosome biogenesis; IEA:Ensembl.
GO; GO:2000808; P:negative regulation of synaptic vesicle clustering; ISS:BHF-UCL.
GO; GO:1903690; P:negative regulation of wound healing, spreading of epidermal cells; IMP:BHF-UCL.
GO; GO:0007270; P:neuron-neuron synaptic transmission; ISS:BHF-UCL.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS: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; IDA:BHF-UCL.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IMP:BHF-UCL.
GO; GO:1903984; P:positive regulation of TRAIL-activated apoptotic signaling pathway; IMP:BHF-UCL.
GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; IDA:BHF-UCL.
GO; GO:0097107; P:postsynaptic density assembly; ISS:BHF-UCL.
GO; GO:0060134; P:prepulse inhibition; ISS:BHF-UCL.
GO; GO:0097105; P:presynaptic membrane assembly; ISS:BHF-UCL.
GO; GO:0060736; P:prostate gland growth; IEA:Ensembl.
GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
GO; GO:0002902; P:regulation of B cell apoptotic process; IEA:Ensembl.
GO; GO:0032535; P:regulation of cellular component size; ISS:BHF-UCL.
GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:UniProtKB.
GO; GO:0033032; P:regulation of myeloid cell apoptotic process; IEA:Ensembl.
GO; GO:0010975; P:regulation of neuron projection development; ISS:UniProtKB.
GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IEA:Ensembl.
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; ISS:BHF-UCL.
GO; GO:0035176; P:social behavior; ISS:BHF-UCL.
GO; GO:0007416; P:synapse assembly; ISS:BHF-UCL.
GO; GO:0060074; P:synapse maturation; ISS:BHF-UCL.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
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;
3D-structure; Acetylation; Alternative initiation;
Alternative splicing; Apoptosis; Autism spectrum disorder;
Complete proteome; Cytoplasm; Disease mutation; Hydrolase;
Isopeptide bond; Lipid metabolism; Lipid-binding; Neurogenesis;
Nucleus; Phosphoprotein; Polymorphism; Protein phosphatase;
Reference proteome; Secreted; Tumor suppressor; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 403 Phosphatidylinositol 3,4,5-trisphosphate
3-phosphatase and dual-specificity
protein phosphatase PTEN.
/FTId=PRO_0000215904.
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:0000269|PubMed:15355975}.
REGION 401 403 PDZ domain-binding.
ACT_SITE 124 124 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00590}.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 294 294 Phosphoserine.
{ECO:0000250|UniProtKB:O08586}.
MOD_RES 336 336 Phosphotyrosine; by FRK.
{ECO:0000269|PubMed:19345329}.
MOD_RES 366 366 Phosphothreonine; by GSK3-beta and PLK3.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:12297295,
ECO:0000269|PubMed:20940307}.
MOD_RES 370 370 Phosphoserine; by CK2 and PLK3.
{ECO:0000269|PubMed:11035045,
ECO:0000269|PubMed:12297295,
ECO:0000269|PubMed:20940307}.
MOD_RES 380 380 Phosphoserine; by ROCK1 and CK2.
{ECO:0000269|PubMed:11035045}.
MOD_RES 382 382 Phosphothreonine; by ROCK1 and CK2.
{ECO:0000269|PubMed:11035045}.
MOD_RES 383 383 Phosphothreonine; by ROCK1 and CK2.
{ECO:0000269|PubMed:11035045}.
MOD_RES 385 385 Phosphoserine; by CK2.
{ECO:0000269|PubMed:11035045,
ECO:0000269|PubMed:12297295}.
MOD_RES 401 401 Phosphothreonine.
{ECO:0000269|PubMed:10646847}.
CROSSLNK 13 13 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:18716620}.
CROSSLNK 289 289 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:18716620}.
VAR_SEQ 1 1 M -> MERGGEAAAAAAAAAAAPGRGSESPVTISRAGNAGE
LVSPLLLPPTRRRRRRHIQGPGPVLNLPSAAAAPPVARAPE
AAGGGSRSEDYSSSPHSAAAAARPLAAEEKQAQSLQPSSSR
RSSHYPAAVQSQAAAERGASATAKSRAISILQKKPRHQQLL
PSLSSFFFSHRLPDM (in isoform alpha).
{ECO:0000305}.
/FTId=VSP_055420.
VAR_SEQ 55 70 RFLDSKHKNHYKIYNL -> S (in isoform 3).
{ECO:0000303|Ref.7}.
/FTId=VSP_055421.
VAR_SEQ 165 190 GVTIPSQRRYVYYYSYLLKNHLDYRP -> ADPTGGIPDKG
IIVIGDGSSMDVIAP (in isoform 3).
{ECO:0000303|Ref.7}.
/FTId=VSP_055422.
VAR_SEQ 191 403 Missing (in isoform 3).
{ECO:0000303|Ref.7}.
/FTId=VSP_055423.
VARIANT 10 10 S -> N (retains phosphatase activity
towards Ins(1,3,4,5)P4 and
PtdIns(3,4,5)P3; retains the ability to
bind phospholipid membranes).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026248.
VARIANT 15 15 R -> S (in glioma).
{ECO:0000269|PubMed:9090379}.
/FTId=VAR_007457.
VARIANT 16 16 Y -> C (loss of phosphatase activity
towards Ins(1,3,4,5)P4; retains the
ability to bind phospholipid membranes).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026249.
VARIANT 19 19 D -> N (in malignant melanoma; somatic
mutation; dbSNP:rs121909233).
{ECO:0000269|PubMed:10978354}.
/FTId=VAR_018100.
VARIANT 20 20 G -> E (reduced phosphatase activity
towards Ins(1,3,4,5)P4; retains
phosphatase activity towards
PtdIns(3,4,5)P3).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026250.
VARIANT 27 27 Y -> S (loss of phosphatase activity
towards Ins(1,3,4,5)P4).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026251.
VARIANT 33 33 Missing (in CWS1).
{ECO:0000269|PubMed:10234502}.
/FTId=VAR_008733.
VARIANT 34 34 A -> D (in BRRS).
{ECO:0000269|PubMed:10400993,
ECO:0000269|PubMed:11494117}.
/FTId=VAR_008734.
VARIANT 35 35 M -> R (in CWS1; dbSNP:rs121909225).
{ECO:0000269|PubMed:9425889}.
/FTId=VAR_008036.
VARIANT 36 36 G -> E (in glioma).
{ECO:0000269|PubMed:9090379}.
/FTId=VAR_007458.
VARIANT 36 36 G -> R (in endometrial hyperplasia;
dbSNP:rs786204854).
{ECO:0000269|PubMed:9635567}.
/FTId=VAR_026252.
VARIANT 42 42 L -> R (in glioma; retains phosphatase
activity towards Ins(1,3,4,5)P4 and
PtdIns(3,4,5)P3; retains the ability to
bind phospholipid membranes).
{ECO:0000269|PubMed:9090379}.
/FTId=VAR_007459.
VARIANT 47 47 R -> G (in CWS1; dbSNP:rs786204855).
{ECO:0000269|PubMed:11494117}.
/FTId=VAR_011587.
VARIANT 57 57 L -> W (in glioma; loss of protein
phosphatase activity; dbSNP:rs786202398).
{ECO:0000269|PubMed:9090379,
ECO:0000269|PubMed:9256433}.
/FTId=VAR_007460.
VARIANT 61 61 H -> D (in VATER; dbSNP:rs121909236).
{ECO:0000269|PubMed:11748304}.
/FTId=VAR_018101.
VARIANT 61 61 H -> R (loss of phosphatase activity
towards Ins(1,3,4,5)P4;
dbSNP:rs398123316).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026253.
VARIANT 65 403 Missing (in MCEPHAS).
{ECO:0000269|PubMed:26637798}.
/FTId=VAR_078705.
VARIANT 67 67 I -> R (in CWS1).
/FTId=VAR_007461.
VARIANT 68 68 Y -> H (in CWS1 and BRRS; loss of
phosphatase activity towards
Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3;
retains the ability to bind phospholipid
membranes; dbSNP:rs398123317).
{ECO:0000269|PubMed:10400993,
ECO:0000269|PubMed:10866302,
ECO:0000269|PubMed:11494117,
ECO:0000269|PubMed:9600246}.
/FTId=VAR_007462.
VARIANT 70 70 L -> P (in CWS1; dbSNP:rs121909226).
{ECO:0000269|PubMed:9832031}.
/FTId=VAR_018102.
VARIANT 71 71 C -> Y (in CWS1; loss of phosphatase
activity towards Ins(1,3,4,5)P4).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026254.
VARIANT 93 93 H -> R (in MCEPHAS; dbSNP:rs121909238).
{ECO:0000269|PubMed:15805158}.
/FTId=VAR_032634.
VARIANT 93 93 H -> Y (in CWS1).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026255.
VARIANT 105 105 C -> F (in BRRS; loss of phosphatase
activity towards Ins(1,3,4,5)P4).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026256.
VARIANT 105 105 C -> Y (in BRRS; dbSNP:rs587782343).
{ECO:0000269|PubMed:10400993,
ECO:0000269|PubMed:11494117}.
/FTId=VAR_008735.
VARIANT 107 107 D -> Y (in BRRS and glioblastoma; loss of
phosphatase activity towards
Ins(1,3,4,5)P4).
{ECO:0000269|PubMed:10866302,
ECO:0000269|PubMed:9331071}.
/FTId=VAR_026257.
VARIANT 112 112 L -> P (in CWS1 and LDD; loss of
phosphatase activity towards
Ins(1,3,4,5)P4; dbSNP:rs121909230).
{ECO:0000269|PubMed:10051160,
ECO:0000269|PubMed:10866302,
ECO:0000269|PubMed:9600246}.
/FTId=VAR_007807.
VARIANT 112 112 L -> R (loss of phosphatase activity
towards Ins(1,3,4,5)P4).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026258.
VARIANT 119 119 V -> L (in multiple cancers;
dbSNP:rs139767111).
{ECO:0000269|PubMed:10807691}.
/FTId=VAR_011588.
VARIANT 121 121 A -> G (in HNSCC; dbSNP:rs121909237).
{ECO:0000269|PubMed:11801303}.
/FTId=VAR_018103.
VARIANT 121 121 A -> P (in glioblastoma; loss of
phosphatase activity towards
Ins(1,3,4,5)P4).
{ECO:0000269|PubMed:10866302,
ECO:0000269|PubMed:9331071}.
/FTId=VAR_026259.
VARIANT 123 123 H -> R (in CWS1; dbSNP:rs121909222).
{ECO:0000269|PubMed:10234502,
ECO:0000269|PubMed:9259288}.
/FTId=VAR_007463.
VARIANT 123 123 H -> Y (in endometrial cancer; loss of
protein phosphatase activity;
dbSNP:rs786204931).
{ECO:0000269|PubMed:9256433}.
/FTId=VAR_026260.
VARIANT 124 124 C -> R (in CWS1; dbSNP:rs121909223).
{ECO:0000269|PubMed:10234502,
ECO:0000269|PubMed:10866302,
ECO:0000269|PubMed:9259288}.
/FTId=VAR_007464.
VARIANT 124 124 C -> S (in CWS1; phosphatase-dead protein
with neither lipid nor protein
phosphatase activity).
{ECO:0000269|PubMed:11230179,
ECO:0000269|PubMed:9811831}.
/FTId=VAR_018104.
VARIANT 126 126 A -> G (in a patient with prostate
cancer; reduced phosphatase activity
towards PtdIns(3,4,5); shifts its
activity from phosphatidylinositol
phosphate 3-phosphatase to
phosphatidylinositol phosphate 5-
phosphatase; disrupts PI3K/ATK signaling;
reduced cell migration).
{ECO:0000269|PubMed:26504226}.
/FTId=VAR_076551.
VARIANT 129 129 G -> E (in CWS1; no lipid phosphatase
activity but retains protein phosphatase
activity; retains ability to inhibit
focal adhesion formation;
dbSNP:rs121909218).
{ECO:0000269|PubMed:10866302,
ECO:0000269|PubMed:11230179,
ECO:0000269|PubMed:9140396,
ECO:0000269|PubMed:9616126,
ECO:0000269|PubMed:9811831}.
/FTId=VAR_007465.
VARIANT 129 129 G -> R (in glioblastoma; severely reduced
protein phosphatase activity; loss of
phosphatase activity towards
Ins(1,3,4,5)P4; dbSNP:rs786204929).
{ECO:0000269|PubMed:10866302,
ECO:0000269|PubMed:9072974,
ECO:0000269|PubMed:9256433,
ECO:0000269|PubMed:9331071}.
/FTId=VAR_007466.
VARIANT 130 130 R -> G (loss of phosphatase activity
towards Ins(1,3,4,5)P4 and
PtdIns(3,4,5)P3; dbSNP:rs121909224).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026261.
VARIANT 130 130 R -> L (in CWS1 and endometrial
hyperplasia; loss of phosphatase activity
towards Ins(1,3,4,5)P4; retains ability
to bind phospholipid membranes).
{ECO:0000269|PubMed:10866302,
ECO:0000269|PubMed:9635567}.
/FTId=VAR_007467.
VARIANT 130 130 R -> Q (in CWS1; loss of phosphatase
activity towards Ins(1,3,4,5)P4; retains
ability to bind phospholipid membranes;
dbSNP:rs121909229).
{ECO:0000269|PubMed:10866302,
ECO:0000269|PubMed:9915974}.
/FTId=VAR_007468.
VARIANT 131 131 T -> I (in MCEPHAS; dbSNP:rs397514560).
{ECO:0000269|PubMed:23160955}.
/FTId=VAR_076762.
VARIANT 132 132 G -> V (in one patient with clinical
findings suggesting hamartoma tumor
syndrome; dbSNP:rs121909241).
{ECO:0000269|PubMed:16752378}.
/FTId=VAR_032635.
VARIANT 133 133 V -> I (loss of phosphatase activity
towards Ins(1,3,4,5)P3).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026262.
VARIANT 134 134 M -> L (in prostate cancer; no effect on
protein phosphatase activity; reduced
phosphatase activity towards
Ins(1,3,4,5)P3 but retains
PtdIns(3,4,5)P3 phosphatase activity).
{ECO:0000269|PubMed:10866302,
ECO:0000269|PubMed:9072974,
ECO:0000269|PubMed:9256433}.
/FTId=VAR_007469.
VARIANT 135 135 I -> V (in BRRS; dbSNP:rs587782360).
{ECO:0000269|PubMed:10400993,
ECO:0000269|PubMed:11494117}.
/FTId=VAR_008736.
VARIANT 136 136 C -> Y (in CWS1; loss of phosphatase
activity towards Ins(1,3,4,5)P3;
dbSNP:rs786204859).
{ECO:0000269|PubMed:10866302,
ECO:0000269|PubMed:9735393}.
/FTId=VAR_007808.
VARIANT 137 137 A -> AN (in CWS1).
{ECO:0000269|PubMed:9345101}.
/FTId=VAR_008737.
VARIANT 155 155 Y -> C (in CWS1; loss of phosphatase
activity towards Ins(1,3,4,5)P4).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026263.
VARIANT 158 158 V -> L (in multiple cancers).
{ECO:0000269|PubMed:10807691}.
/FTId=VAR_011589.
VARIANT 165 165 G -> E (in CWS1).
{ECO:0000269|PubMed:10234502}.
/FTId=VAR_008739.
VARIANT 165 165 G -> R (in glioblastoma; severely reduced
protein phosphatase activity; loss of
phosphatase activity towards
Ins(1,3,4,5)P4; retains ability to bind
phospholipid membranes).
{ECO:0000269|PubMed:10866302,
ECO:0000269|PubMed:9256433,
ECO:0000269|PubMed:9331071}.
/FTId=VAR_026264.
VARIANT 165 165 G -> V (in CWS1; dbSNP:rs786204863).
/FTId=VAR_008738.
VARIANT 167 167 T -> N (in MCEPHAS; dbSNP:rs397514559).
{ECO:0000269|PubMed:23160955}.
/FTId=VAR_076763.
VARIANT 167 167 T -> P (in breast cancer; severely
reduced protein phosphatase activity).
{ECO:0000269|PubMed:9256433}.
/FTId=VAR_026265.
VARIANT 170 170 S -> N (loss of phosphatase activity
towards Ins(1,3,4,5)P4; retains ability
to bind phospholipid membranes).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026266.
VARIANT 170 170 S -> R (in BRRS; severely reduced protein
phosphatase activity; loss of phosphatase
activity towards Ins(1,3,4,5)P4;
dbSNP:rs121909221).
{ECO:0000269|PubMed:10400993,
ECO:0000269|PubMed:10866302,
ECO:0000269|PubMed:11494117,
ECO:0000269|PubMed:9241266,
ECO:0000269|PubMed:9256433}.
/FTId=VAR_007470.
VARIANT 173 173 R -> C (in endometrial hyperplasia; loss
of phosphatase activity towards
Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3;
retains ability to bind phospholipid
membranes; dbSNP:rs121913293).
{ECO:0000269|PubMed:10866302,
ECO:0000269|PubMed:9635567}.
/FTId=VAR_026267.
VARIANT 173 173 R -> H (loss of phosphatase activity
towards Ins(1,3,4,5)P4;
dbSNP:rs121913294).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026268.
VARIANT 173 173 R -> P (loss of phosphatase activity
towards Ins(1,3,4,5)P4;
dbSNP:rs121913294).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026269.
VARIANT 174 174 Y -> N (loss of phosphatase activity
towards Ins(1,3,4,5)P4;
dbSNP:rs587782316).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026270.
VARIANT 191 191 V -> A (in endometrial hyperplasia).
{ECO:0000269|PubMed:9635567}.
/FTId=VAR_026271.
VARIANT 217 217 V -> I (in malignant melanoma; somatic
mutation; dbSNP:rs121909234).
{ECO:0000269|PubMed:10978354}.
/FTId=VAR_018105.
VARIANT 227 227 S -> F (reduced phosphatase activity
towards Ins(1,3,4,5)P4 but retains
PtdIns(3,4,5)P3 phosphatase activity).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026272.
VARIANT 234 234 R -> Q (in GLM2; the patient also
suffered from benign meningioma; not
capable of inducing apoptosis; induced
increased cell proliferation; led to high
constitutive AKT1 activation which could
not be increased further by stimulation
with insulin; dbSNP:rs121909235).
{ECO:0000269|PubMed:12085208}.
/FTId=VAR_018106.
VARIANT 241 241 F -> S (in MCEPHAS; dbSNP:rs121909240).
{ECO:0000269|PubMed:15805158}.
/FTId=VAR_032636.
VARIANT 246 246 P -> L (in BRRS; dbSNP:rs587782350).
{ECO:0000269|PubMed:10400993}.
/FTId=VAR_008740.
VARIANT 251 251 G -> C (loss of phosphatase activity
towards Ins(1,3,4,5)P4; retains ability
to bind phospholipid membranes).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026273.
VARIANT 252 252 D -> G (in MCEPHAS; dbSNP:rs121909239).
{ECO:0000269|PubMed:15805158}.
/FTId=VAR_032637.
VARIANT 289 289 K -> E (in CWS1; reduced phosphatase
activity towards Ins(1,3,4,5)P4; retains
ability to bind phospholipid membranes;
predominantly nuclear;
dbSNP:rs562015640).
{ECO:0000269|PubMed:10866302,
ECO:0000269|PubMed:18716620,
ECO:0000269|PubMed:9797362}.
/FTId=VAR_008741.
VARIANT 290 290 V -> L (in dbSNP:rs35600253).
{ECO:0000269|Ref.10}.
/FTId=VAR_025167.
VARIANT 319 319 Missing (in glioma; reduced tumor
suppressor activity; fails to inactivate
AKT/PKB). {ECO:0000269|PubMed:10468583,
ECO:0000269|PubMed:9090379}.
/FTId=VAR_026274.
VARIANT 331 331 D -> G (in CWS1; reduced phosphatase
activity towards Ins(1,3,4,5)P4; retains
ability to bind phospholipid membranes).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026275.
VARIANT 341 341 F -> V (in CWS1; loss of interaction with
NOP53; decreased phosphorylation at S-
380; decreased stability; loss of
phosphatase activity towards
Ins(1,3,4,5)P4).
{ECO:0000269|PubMed:10866302,
ECO:0000269|PubMed:15355975}.
/FTId=VAR_026276.
VARIANT 342 342 K -> N (in CWS1; reduced phosphatase
activity towards Ins(1,3,4,5)P4 but
PtdIns(3,4,5)P3 phosphatase activity is
similar to wild-type; dbSNP:rs398123314).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026277.
VARIANT 343 343 V -> E (in CWS1; loss of interaction with
NOP53; decreased phosphorylation at S-
380; decreased stability; loss of
phosphatase activity towards
Ins(1,3,4,5)P4).
{ECO:0000269|PubMed:10866302,
ECO:0000269|PubMed:15355975,
ECO:0000269|PubMed:9399897}.
/FTId=VAR_008742.
VARIANT 345 345 L -> Q (in glioblastoma; reduced tumor
suppressor activity; loss of interaction
with NOP53; decreased phosphorylation at
S-380; decreased stability; loss of
phosphatase activity towards
Ins(1,3,4,5)P4; reduced ability to
inactivate AKT/PKB; retains ability to
bind phospholipid membranes).
{ECO:0000269|PubMed:10468583,
ECO:0000269|PubMed:10866302,
ECO:0000269|PubMed:15355975,
ECO:0000269|PubMed:9331071}.
/FTId=VAR_026278.
VARIANT 347 347 F -> L (in CWS1; reduced phosphatase
activity towards Ins(1,3,4,5)P4).
{ECO:0000269|PubMed:10866302,
ECO:0000269|PubMed:9399897}.
/FTId=VAR_008743.
VARIANT 348 348 T -> I (in endometrial hyperplasia;
reduced phosphatase activity towards
PtdIns(3,4,5)P3; mildly reduced tumor
suppressor activity; reduced ability to
inactivate AKT/PKB).
{ECO:0000269|PubMed:10468583,
ECO:0000269|PubMed:9635567}.
/FTId=VAR_026279.
VARIANT 369 369 V -> G (retains Ins(1,3,4,5)P4 and
PtdIns(3,4,5)P3 phosphatase activity;
retains ability to bind phospholipid
membranes).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026280.
VARIANT 401 401 T -> I (retains Ins(1,3,4,5)P4 and
PtdIns(3,4,5)P3 phosphatase activity;
retains ability to bind phospholipid
membranes).
{ECO:0000269|PubMed:10866302}.
/FTId=VAR_026281.
MUTAGEN 1 1 M->I: Expression is restricted to isoform
alpha. {ECO:0000269|PubMed:24768297}.
MUTAGEN 13 13 K->E: Nuclear. Cytoplasmic; when
associated with E-289. Shows less tumor
suppressive ability; when associated with
E-289. {ECO:0000269|PubMed:18716620}.
MUTAGEN 92 92 D->A: 700-fold reduction in phosphatase
activity towards PtdIns(3,4,5)P3. Loss of
protein phosphatase activity. Unable to
inhibit focal adhesion formation.
{ECO:0000269|PubMed:10555148,
ECO:0000269|PubMed:9616126}.
MUTAGEN 93 93 H->A: 75% reduction in phosphatase
activity towards PtdIns(3,4,5)P3. Modest
reduction in phosphatase activity towards
PtdIns(3,4)P2.
{ECO:0000269|PubMed:10555148}.
MUTAGEN 124 124 C->A: Loss of protein phosphatase
activity. Unable to inhibit focal
adhesion formation.
{ECO:0000269|PubMed:9616126}.
MUTAGEN 125 125 K->M: Reduced phosphatase activity
towards PtdIns(3,4,5)P3, PtdIns(3,4)P2
and PtdIns(3)P.
{ECO:0000269|PubMed:10555148}.
MUTAGEN 126 126 A->P: Does not reduce phosphatase
activity towards PtdIns(3,4,5)P3 and
PtdIns(3,4)P2.
{ECO:0000269|PubMed:26504226}.
MUTAGEN 126 126 A->S: Does not reduce phosphatase
activity towards PtdIns(3,4,5)P3 and
PtdIns(3,4)P2.
{ECO:0000269|PubMed:26504226}.
MUTAGEN 126 126 A->V: Does not reduce phosphatase
activity towards PtdIns(3,4,5)P3 and
PtdIns(3,4)P2.
{ECO:0000269|PubMed:26504226}.
MUTAGEN 128 128 K->M: 85% reduction in phosphatase
activity towards PtdIns(3,4,5)P3.
{ECO:0000269|PubMed:10555148}.
MUTAGEN 128 128 K->R: Does not reduce phosphatase
activity towards PtdIns(3,4,5)P3.
{ECO:0000269|PubMed:10555148}.
MUTAGEN 130 130 R->M: Does not affect the ability to
inhibit AKT/PKB activation.
{ECO:0000269|PubMed:9811831}.
MUTAGEN 167 167 T->A,D: 60% reduction in phosphatase
activity towards PtdIns(3,4,5)P3.
{ECO:0000269|PubMed:10555148}.
MUTAGEN 171 171 Q->A,E: 75% reduction in phosphatase
activity towards PtdIns(3,4,5)P3.
{ECO:0000269|PubMed:10555148}.
MUTAGEN 263 269 KMLKKDK->AAGAADA: Reduces the growth
suppression activity and cells show
anchorage-independent growth. Reduces
binding to phospholipid membranes in
vitro. Phosphatase activity towards
PtdIns(3,4,5)P3 is not affected.
{ECO:0000269|PubMed:10555148}.
MUTAGEN 289 289 K->E: Cytoplasmic; when associated with
E-13. Shows less tumor suppressive
ability; when associated with E-13.
{ECO:0000269|PubMed:18716620}.
MUTAGEN 327 335 KANKDKANR->AAGADAANA: Reduces growth
suppression activity and promotes
anchorage-independent growth. Reduces
binding to phospholipid membranes in
vitro; phosphatase activity towards
PtdIns(3,4,5)P3 is not affected.
{ECO:0000269|PubMed:10555148}.
MUTAGEN 336 336 Y->F: Significantly lower phosphatase
activity, reduced protein stability and
decreased growth-inhibitory effect.
{ECO:0000269|PubMed:19345329}.
MUTAGEN 366 366 T->A: Decreased stability.
{ECO:0000269|PubMed:20940307}.
MUTAGEN 370 370 S->A: Decreased stability.
{ECO:0000269|PubMed:20940307}.
MUTAGEN 401 401 T->A: Loss of DLG1-binding. No effect on
MAGI2- and MAST2-binding.
MUTAGEN 402 402 K->A: No effect on MAGI2-, MAST2- and
DLG1-binding.
MUTAGEN 402 402 K->W: Loss of DLG1-, MAGI2-, MAGI3- and
MAST2-binding. Decrease of protein
stability.
MUTAGEN 403 403 V->A: Loss of DLG1-, MAGI2-, MAGI3-,
MAST1-, MAST2- and MAST3-binding.
{ECO:0000269|PubMed:15951562}.
TURN 19 22 {ECO:0000244|PDB:1D5R}.
STRAND 23 29 {ECO:0000244|PDB:1D5R}.
STRAND 32 35 {ECO:0000244|PDB:1D5R}.
STRAND 39 41 {ECO:0000244|PDB:1D5R}.
STRAND 44 47 {ECO:0000244|PDB:5BZZ}.
HELIX 50 60 {ECO:0000244|PDB:1D5R}.
STRAND 61 63 {ECO:0000244|PDB:1D5R}.
STRAND 65 73 {ECO:0000244|PDB:1D5R}.
HELIX 78 80 {ECO:0000244|PDB:5BZZ}.
STRAND 81 83 {ECO:0000244|PDB:5BZZ}.
STRAND 85 90 {ECO:0000244|PDB:1D5R}.
HELIX 98 100 {ECO:0000244|PDB:1D5R}.
HELIX 101 112 {ECO:0000244|PDB:1D5R}.
TURN 113 115 {ECO:0000244|PDB:1D5R}.
STRAND 118 123 {ECO:0000244|PDB:1D5R}.
STRAND 125 128 {ECO:0000244|PDB:1D5R}.
HELIX 129 141 {ECO:0000244|PDB:1D5R}.
HELIX 148 159 {ECO:0000244|PDB:1D5R}.
STRAND 161 163 {ECO:0000244|PDB:1D5R}.
HELIX 169 184 {ECO:0000244|PDB:1D5R}.
STRAND 192 202 {ECO:0000244|PDB:1D5R}.
STRAND 206 209 {ECO:0000244|PDB:5BZZ}.
STRAND 213 219 {ECO:0000244|PDB:1D5R}.
STRAND 222 226 {ECO:0000244|PDB:1D5R}.
STRAND 232 235 {ECO:0000244|PDB:1D5R}.
STRAND 238 259 {ECO:0000244|PDB:1D5R}.
STRAND 262 264 {ECO:0000244|PDB:5BZZ}.
STRAND 268 276 {ECO:0000244|PDB:1D5R}.
HELIX 277 279 {ECO:0000244|PDB:1D5R}.
STRAND 280 284 {ECO:0000244|PDB:5BZZ}.
STRAND 310 312 {ECO:0000244|PDB:5BZX}.
STRAND 315 321 {ECO:0000244|PDB:1D5R}.
HELIX 322 324 {ECO:0000244|PDB:1D5R}.
HELIX 328 330 {ECO:0000244|PDB:1D5R}.
STRAND 335 337 {ECO:0000244|PDB:1D5R}.
STRAND 342 349 {ECO:0000244|PDB:1D5R}.
STRAND 395 403 {ECO:0000244|PDB:2KYL}.
SEQUENCE 403 AA; 47166 MW; 75F97C3DD6802BA9 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 PFDEDQHTQI TKV


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