Interacts with AXIN1. Probably part of a complex consisting of TP53, HIPK2 and AXIN1 (By similarity). Binds DNA as a homotetramer. Interacts with histone acetyltransferases EP300 and methyltransferases HRMT1L2 and CARM1, and recruits them to promoters. In vitro, the interaction of TP53 with cancer-associated/HPV (E6) viral proteins leads to ubiquitination and degradation of TP53 giving a possible model for cell growth regulation. This complex formation requires an additional factor, E6-AP, which stably associates with TP53 in the presence of E6. Interacts (via C-terminus) with TAF1; when TAF1 is part of the TFIID complex. Interacts with ING4; this interaction may be indirect. Found in a complex with CABLES1 and TP73. Interacts with HIPK1, HIPK2, and P53DINP1. Interacts with WWOX. May interact with HCV core protein. Interacts with USP7 and SYVN1. Interacts with HSP90AB1. Interacts with CHD8; leading to recruit histone H1 and prevent transactivation activity (By similarity). Interacts with ARMC10, BANP, CDKN2AIP, NUAK1, STK11/LKB1 and E4F1. Interacts with YWHAZ; the interaction enhances TP53 transcriptional activity. Phosphorylation of YWHAZ on 'Ser-58' inhibits this interaction. Interacts (via DNA-binding domain) with MAML1 (via N-terminus). Interacts with MKRN1. Interacts with PML (via C-terminus). Interacts with MDM2; leading to ubiquitination and proteasomal degradation of TP53. Directly interacts with FBXO42; leading to ubiquination and degradation of TP53. Interacts (phosphorylated at Ser-15 by ATM) with the phosphatase PP2A-PPP2R5C holoenzyme; regulates stress-induced TP53-dependent inhibition of cell proliferation. Interacts with PPP2R2A. Interacts with AURKA, DAXX, BRD7 and TRIM24. Interacts (when monomethylated at Lys-382) with L3MBTL1. Isoform 1 interacts with isoform 2 and with isoform 4. Interacts with GRK5. Binds to the CAK complex (CDK7, cyclin H and MAT1) in response to DNA damage. Interacts with CDK5 in neurons.
Function:
Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Implicated in Notch signaling cross-over. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Isoform 2 enhances the transactivation activity of isoform 1 from some but not all TP53-inducible promoters. Isoform 4 suppresses transactivation activity and impairs growth suppression mediated by isoform 1. Isoform 7 inhibits isoform 1-mediated apoptosis.
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1);VARIANT GLY-76
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);VARIANTS SPORADIC CANCERS
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA];VARIANT LYS-286
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);INTERACTION WITH WWOX
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 7; 8 AND 9);SUBCELLULAR LOCATION;TISSUE SPECIFICITY;ALTERNATIVE PROMOTER USAGE;ALTERNATIVE SPLICING;INDUCTION;VARIANT ARG-72
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]
11.
"P53 genomic sequence. Corrections and polymorphism." Rozemuller E.H.
,
Tilanus M.G.J.
Submitted (1997-03) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]
12.
NIEHS SNPs program
Submitted (2004-11) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA];VARIANTS SER-47; LYS-339 AND ALA-366
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA];VARIANT LYS-286
14.
"Identification of a tumor-rejection antigen recognized by HLA-B46 restricted CTL." Azuma K.
,
Shichijo S.
,
Itoh K.
Submitted (2002-03) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);VARIANTS HIS-273 AND SER-309
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1);VARIANT ARG-72
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA];VARIANT ARG-72
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1);VARIANT ALA-278
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-379 (ISOFORM 1);VARIANTS ASN-139 AND PRO-155
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 101-393
21.
"Study on the effect of tumor suppressor gene p53 in arsenism patients." Pan X.L.
,
Zhang A.H.
Submitted (2003-09) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 126-185
22.
"Detection of P53 gene mutations and serum p53 antibodies associated with cigarette smoking." Nimri L.F.
,
Owais W.
,
Momani E.
Submitted (2003-08) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 261-298;VARIANT GLN-282
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 262-306;VARIANT VAL-262
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Cited for: NUCLEAR LOCALIZATION SIGNAL;MUTAGENESIS OF LYS-319; LYS-320 AND LYS-321
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Cited for: BIPARTITE NUCLEAR LOCALIZATION SIGNAL;CHARACTERIZATION OF VARIANT ASN-305
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Cited for: PHOSPHORYLATION AT SER-15 AND SER-20;INDUCTION BY DNA DAMAGE;CHARACTERIZATION OF LFS VARIANT HIS-273;MUTAGENESIS OF THR-18; SER-20 AND 22-LEU-TRP-23;SUBCELLULAR LOCATION;INTERACTION WITH PML AND MDM2
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Cited for: PHOSPHORYLATION AT SER-315 AND SER-392 BY CDK2;MUTAGENESIS OF LYS-382; LEU-383 AND PHE-385
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Cited for: FUNCTION;INTERACTION WITH PML;SUBCELLULAR LOCATION
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Cited for: SUMOYLATION AT LYS-386;SUBCELLULAR LOCATION;MUTAGENESIS OF PHE-385; LYS-386; THR-387 AND GLU-388
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Cited for: IDENTIFICATION IN A COMPLEX WITH CABLES1 AND TP73
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Cited for: INTERACTION WITH HIPK2;PHOSPHORYLATION AT SER-46;MUTAGENESIS OF SER-46 AND LYS-382
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Cited for: INTERACTION WITH HIPK2;PHOSPHORYLATION AT SER-46
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Cited for: FUNCTION;SUBCELLULAR LOCATION;INTERACTION WITH CHEK2 AND PML;UBIQUITINATION BY MDM2;PHOSPHORYLATION AT SER-20
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Cited for: NUCLEOCYTOPLASMIC SHUTTLING;NUCLEAR EXPORT SIGNAL
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Cited for: INTERACTION WITH HRMT1L2; EP300 AND CARM1;FUNCTION
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Cited for: PHOSPHORYLATION AT THR-55;MUTAGENESIS OF THR-55;INTERACTION WITH TAF1
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Cited for: ALTERNATIVE SPLICING (ISOFORM 4);FUNCTION;SUBCELLULAR LOCATION;UBIQUITINATION
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Cited for: INTERACTION WITH AURKA;PHOSPHORYLATION AT SER-315
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Cited for: INTERACTION WITH BANP;SUBCELLULAR LOCATION;PHOSPHORYLATION AT SER-15
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Cited for: INTERACTION WITH STK11/LKB1;PHOSPHORYLATION AT SER-15 AND SER-392
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Cited for: PHOSPHORYLATION AT SER-46;INTERACTION WITH PRKCG
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Cited for: PHOSPHORYLATION AT SER-37;MUTAGENESIS OF SER-37
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Cited for: INTERACTION WITH ZNF385A;CHARACTERIZATION OF VARIANTS ALA-143; HIS-175 AND PRO-175
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Cited for: UBIQUITINATION;INTERACTION WITH SYVN1;SUBCELLULAR LOCATION
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Cited for: INTERACTION WITH PPP2CA; PPP2R1A; PPP2R2A AND PPP2R5C
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Cited for: PHOSPHORYLATION AT SER-15; SER-33 AND SER-46;INTERACTION WITH CDK5;SUBCELLULAR LOCATION
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Cited for: FUNCTION;PHOSPHORYLATION AT SER-46;MUTAGENESIS OF SER-46
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: INTERACTION WITH PPP2CA; PPP2R1A AND PPP2R5C;PHOSPHORYLATION AT SER-15 BY ATM;MUTAGENESIS OF SER-15
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: INTERACTION WITH MKRN1;MUTAGENESIS OF 291-LYS-LYS-292;UBIQUITINATION AT LYS-291 AND LYS-292 BY MKRN1
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Cited for: FUNCTION;UBIQUITINATION;INTERACTION WITH TRIM24
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Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-381 AND LYS-382;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: INTERACTION WITH SNAI1;CHARACTERIZATION OF VARIANTS LEU-110; PRO-155; HIS-175; SER-232; SER-249; HIS-273 AND TRP-282;MUTAGENESIS OF ARG-248
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Cited for: INTERACTION WITH PTK2B/PYK2 AND MDM2;UBIQUITINATION;SUBCELLULAR LOCATION
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Cited for: PHOSPHORYLATION AT THR-55;INTERACTION WITH GRK5
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: FUNCTION;INTERACTION WITH AURKB AND NOC2L;PHOSPHORYLATION AT SER-183; SER-269 AND THR-284;CHARACTERIZATION OF VARIANT ALA-284;MUTAGENESIS OF SER-183 AND SER-269;IDENTIFICATION BY MASS SPECTROMETRY
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Cited for: INTERACTION WITH NUAK1;PHOSPHORYLATION AT SER-15 AND SER-392
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Cited for: FUNCTION;SUBCELLULAR LOCATION;INTERACTION WITH PPIF
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Cited for: INTERACTION WITH UBC9;PHOSPHORYLATION AT SER-392;SUMOYLATION AT LYS-386
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Cited for: INTERACTION WITH KAT6A;ACETYLATION AT LYS-120 AND LYS-382
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Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 94-289
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Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 325-356
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Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 13-29 IN COMPLEX WITH MDM2
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Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 97-287 IN COMPLEX WITH 53BP2
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Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 94-312 IN COMPLEX WITH ZINC IONS;SUBUNIT
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Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 94-293 IN COMPLEX WITH DNA AND ZINC IONS;SUBUNIT
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Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 358-367 IN COMPLEX WITH USP7;INTERACTION WITH USP7
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Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 360-368 IN COMPLEX WITH USP7;MUTAGENESIS OF PRO-359; GLY-361 AND SER-362;INTERACTION WITH USP7
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Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 377-386;METHYLATION AT LYS-382;MUTAGENESIS OF LYS-382;INTERACTION WITH L3MBTL1
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Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 94-312 IN COMPLEX WITH ZINC IONS
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Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 94-292 OF VARIANT GLN-282
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Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 94-312 OF VARIANT CYS-202 IN COMPLEX WITH ZINC IONS AND PHIKAN083
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Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 94-293 OF VARIANT SER-249 IN COMPLEX WITH DNA
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Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 94-310 IN COMPLEX WITH ZINC IONS
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Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 94-312 OF VARIANT CYS-220 IN COMPLEX WITH ZINC IONS
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Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 94-293 IN COMPLEX WITH DNA AND ZINC IONS;SUBUNIT
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Cited for: VARIANTS LFS CYS-245; TRP-248; PRO-252 AND LYS-258
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Cited for: VARIANTS SPORADIC CANCERS GLN-132; SER-249; LYS-280 AND LYS-285
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Cited for: VARIANTS SPORADIC CANCER VAL-154; VAL-245; GLN-248; LEU-278 AND SER-278
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Cited for: VARIANTS SPORADIC CANCERS LEU-152; ALA-155; HIS-175; PHE-176 AND HIS-273
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Cited for: VARIANTS SPORADIC CANCERS PHE-176; PHE-242; CYS-245; LEU-248 AND HIS-273
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Cited for: VARIANTS SPORADIC CANCERS CYS-205; GLU-281 AND LYS-285
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Cited for: VARIANTS SPORADIC CANCERS SER-151; PRO-156; LYS-174; ARG-194; CYS-220; GLN-248; LEU-248 AND HIS-273
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Cited for: VARIANTS LFS HIS-175; ARG-193; GLN-248; CYS-273 AND TYR-275
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Cited for: VARIANTS SPORADIC CANCERS PHE-176; SER-245; TRP-248; TRP-282 AND GLN-286
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Cited for: VARIANTS SER-152; ILE-169; PHE-176; THR-195; CYS-220; ILE-230; CYS-273 AND SER-278
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Cited for: VARIANTS PRO-110; VAL-113; VAL-138; CYS-163; HIS-163; THR-195; MET-216; ALA-241; MET-249; SER-251; TYR-259 AND CYS-273