Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (Protein name
), PTEN_HUMAN from NCBI database.
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General Annotation
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Antigen Annotation
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Gene name:
PTEN(MMAC1;TEP1);
Protein name:
Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN;
Alternative:
Phosphatase and tensin homolog;Mutated in multiple advanced cancers 1;
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Monomer. The unphosphorylated form interacts with the second PDZ domain of AIP1 and with DLG1 and MAST2 in vitro. Interacts with MAGI2, MAGI3, MAST1 and MAST3, but neither with MAST4 nor with DLG5. Interaction with MAGI2 increases protein stability. Interacts with NEDD4. Interacts with NDFIP1 and NDFIP2; in the presence of NEDD4 or ITCH, this interaction promotes PTEN ubiquitination. Interacts (via C2 domain) with FRK. Interacts with USP7; the interaction is direct. Interacts with ROCK1.
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. 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.
Subcellular Location:
Cytoplasm
Nucleus
Nucleus
PML body
Monoubiquitinated form is nuclear. Nonubiquitinated form is cytoplasmic. Colocalized with PML and USP7 in PML nuclear bodies.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);FUNCTION;CATALYTIC ACTIVITY;SUBCELLULAR LOCATION;INDUCTION
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);TISSUE SPECIFICITY;VARIANTS GLIOMA SER-15; GLU-36; ARG-42; TRP-57 AND THR-319 DEL
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);VARIANTS GLIOBLASTOMA ARG-129 AND PROSTATE CANCER LEU-134
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]
7.
"Homo sapiens phosphatase and tensin homolog mRNA splicing variants." Yang C.-W.
,
Hsu Y.-F.
Submitted (2011-01) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3)
8.
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L.
,
Schick M.
,
Neubert P.
,
Schatten R.
,
Henze S.
,
Korn B.
Submitted (2004-05) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
NIEHS SNPs program
Submitted (2005-05) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA];VARIANT LEU-290
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
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Cited for: FUNCTION;CATALYTIC ACTIVITY;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
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Cited for: FUNCTION;CATALYTIC ACTIVITY;MUTAGENESIS OF ARG-130;CHARACTERIZATION OF VARIANTS CWS1 SER-124 AND CWS1 GLU-129
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Cited for: FUNCTION;MUTAGENESIS OF ASP-92 AND CYS-124;CHARACTERIZATION OF VARIANT GLU-129
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Cited for: FUNCTION;DOMAIN;CHARACTERIZATION OF VARIANTS THR-319 DEL; GLN-345 AND ILE-348
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Cited for: INTERACTION WITH DLG1 AND MAST2;PHOSPHORYLATION AT THR-401
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Cited for: PHOSPHORYLATION AT SER-370; SER-380; THR-382; THR-383 AND SER-385
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Cited for: PHOSPHORYLATION AT THR-366; SER-370 AND SER-385
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Cited for: INTERACTION WITH STK11;SUBCELLULAR LOCATION;PHOSPHORYLATION BY STK11
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Cited for: INTERACTION WITH MAGI2; MAGI3; MAST1; MAST2 AND MAST3;MUTAGENESIS OF VAL-403;PHOSPHORYLATION
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Cited for: FUNCTION;INTERACTION WITH USP7;UBIQUITINATION AT LYS-13 AND LYS-289;DEUBIQUITINATION BY USP7;SUBCELLULAR LOCATION;MUTAGENESIS OF LYS-13 AND LYS-289
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Cited for: INTERACTION WITH FRK;PHOSPHORYLATION AT TYR-336;MUTAGENESIS OF TYR-336
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Cited for: UBIQUITINATION BY XIAP/BIRC4;SUBCELLULAR LOCATION;INTERACTION WITH XIAP/BIRC4
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Cited for: PHOSPHORYLATION AT THR-366 AND SER-370;MUTAGENESIS OF THR-366 AND SER-370
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS];CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]
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Cited for: ALTERNATIVE INITIATION (ISOFORM ALPHA);CTG START CODON;FUNCTION (ISOFORM ALPHA);SUBCELLULAR LOCATION (ISOFORM ALPHA)
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Cited for: ALTERNATIVE INITIATION (ISOFORM ALPHA);CTG START CODON;SUBCELLULAR LOCATION (ISOFORM ALPHA);MUTAGENESIS OF MET-1
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Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 8-353 IN COMPLEX WITH L(+)-TARTRATE;SUBUNIT;DOMAIN;MUTAGENESIS OF ASP-92; HIS-93; LYS-125; LYS-128; THR-167; GLN-171; 263-LYS--ALA-269 AND 327-LYS--ALA-335
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Cited for: VARIANTS GLIOBLASTOMA TYR-107; PRO-121; ARG-129; ARG-165 AND GLN-345
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Cited for: VARIANTS ENDOMETRIAL HYPERPLASIA ARG-36; LEU-130; CYS-173; ALA-191 AND ILE-348
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Cited for: VARIANTS CWS1 ILE-33 DEL; ARG-123; ARG-124 AND GLU-165
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Cited for: VARIANTS BRRS ASP-34; HIS-68; TYR-105; VAL-135; ARG-170 AND LEU-246
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Cited for: CHARACTERIZATION OF VARIANTS CWS1 SER-124 AND GLU-129
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Cited for: VARIANT CWS1 GLY-47;VARIANTS BRRS ASP-34; HIS-68; TYR-105; VAL-135 AND ARG-170
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Cited for: DISCUSSION OF PTEN INVOLVEMENT IN PROTEUS SYNDROME
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Cited for: INVOLVEMENT IN CHROMOSOME 10Q23 DELETION SYNDROME