Tp53
entrez
24842
canonical
uniprot
P10361
canonical
ensembl
ENSRNOG00000010756
resolver
ensembl
ENSRNOG00055030460
resolver
ensembl
ENSRNOG00060028077
resolver
ensembl
ENSRNOG00065000306
resolver
ensembl
ENSRNOG00065026731
resolver
ensp
ENSRNOP00000074031
resolver
ensp
ENSRNOP00000080907
resolver
ensp
ENSRNOP00055043774
resolver
ensp
ENSRNOP00060040833
resolver
ensp
ENSRNOP00065000426
resolver
ensp
ENSRNOP00065037969
resolver
enst
ENSRNOT00000085115
resolver
enst
ENSRNOT00055052973
resolver
enst
ENSRNOT00060048932
resolver
enst
ENSRNOT00065000476
resolver
enst
ENSRNOT00065046290
resolver
genesymbol
Tp53
resolver
genesymbol_syn
P53
resolver
uniprot
O09168
resolver
uniprot
Q4KMA9
resolver
uniprot
Q66HM0
resolver
uniprot_entry
P53_RAT
resolver
uniprot_sec
O09168
resolver
uniprot_sec
Q4KMA9
resolver
uniprot_sec
Q66HM0
resolver
amino_acid_sequence
MEDSQSDMSIELPLSQETFSCLWKLLPPDDILPTTATGSPNSMEDLFLPQDVAELLEGPEEALQVSAPAAQEPGTEAPAPVAPASATPWPLSSSVPSQKTYQGNYGFHLGFLQSGTAKSVMCTYSISLNKLFCQLAKTCPVQLWVTSTPPPGTRVRAMAIYKKSQHMTEVVRRCPHHERCSDGDGLAPPQHLIRVEGNPYAEYLDDRQTFRHSVVVPYEPPEVGSDYTTIHYKYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRDSFEVRVCACPGRDRRTEEENFRKKEEHCPELPPGSAKRALPTSTSSSPQQKKKPLDGEYFTLKIRGRERFEMFRELNEALELKDARAAEESGDSRAHSSYPKTKKGQSTSRHKKPMIKKVGPDSD
uniprot
proteins
disease_involvement
DISEASE: Note=p53 is found in increased amounts in a wide variety of transformed cells. p53 is frequently mutated or inactivated in many types of cancer.
uniprot
proteins
function
FUNCTION: Multifunctional transcription factor that induces cell cycle arrest, DNA repair or apoptosis upon binding to its target DNA sequence. Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Negatively regulates cell division by controlling expression of 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. Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (By similarity). However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (By similarity). In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Regulates the circadian clock by repressing CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER2. {ECO:0000250|UniProtKB:P02340, ECO:0000250|UniProtKB:P04637}.
uniprot
proteins
mass_dalton
43451
uniprot
proteins
post_translational_modification
PTM: Phosphorylation on Ser residues mediates transcriptional activation. Phosphorylation at Ser-9 by HIPK4 increases repression activity on BIRC5 promoter (By similarity). Phosphorylated on Thr-18 by VRK1, which may prevent the interaction with MDM2. Phosphorylated on Ser-20 by CHEK2 in response to DNA damage, which prevents ubiquitination by MDM2. Phosphorylated on Ser-20 by PLK3 in response to reactive oxygen species (ROS), promoting p53/TP53-mediated apoptosis. Probably phosphorylated on by CDK7 in a CAK complex in response to DNA damage. Phosphorylated by HIPK1. Phosphorylated on Ser-390 following UV but not gamma irradiation. Stabilized by CDK5-mediated phosphorylation in response to genotoxic and oxidative stresses at Ser-15, leading to accumulation of p53/TP53, particularly in the nucleus, thus inducing the transactivation of p53/TP53 target genes. Phosphorylated at Ser-313 and Ser-390 by CDK2 in response to DNA-damage (By similarity). Phosphorylation at Ser-15 is required for interaction with DDX3X and gamma-tubulin (By similarity). Phosphorylation at Ser-390 regulates its ability to undergo liquid-liquid phase separation by increasing fluidity of TP53/p53 condensates (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P04637}.; PTM: Monomethylated at Lys-370 by SETD7, leading to stabilization and increased transcriptional activation. Monomethylated at Lys-368 by SMYD2, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity. Lys-370 monomethylation prevents interaction with SMYD2 and subsequent monomethylation at Lys-368. Dimethylated at Lys-371 by EHMT1 and EHMT2. Monomethylated at Lys-380 by KMT5A, promoting interaction with L3MBTL1 and leading to repress transcriptional activity. Demethylation of dimethylated Lys-368 by KDM1A prevents interaction with TP53BP1 and represses TP53-mediated transcriptional activation (By similarity). Monomethylated at Arg-331 and dimethylated at Arg-333 and Arg-335 by PRMT5; methylation is increased after DNA damage and might possibly affect TP53 target gene specificity (By similarity). {ECO:0000250|UniProtKB:P04637}.; PTM: Sumoylated with SUMO1. Sumoylated at Lys-384 by UBC9 (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by MDM2 and SYVN1, which leads to proteasomal degradation. Ubiquitinated by RFWD3, which works in cooperation with MDM2 and may catalyze the formation of short polyubiquitin chains on p53/TP53 that are not targeted to the proteasome. Ubiquitinated by MKRN1, which leads to proteasomal degradation. Deubiquitinated by USP10, leading to stabilize it. Ubiquitinated by TRIM24, RFFL, RNF34 and RNF125, which leads to proteasomal degradation. Ubiquitination by TOPORS induces degradation. Deubiquitination by USP7, leading to stabilize it. Ubiquitinated by COP1, which leads to proteasomal degradation (By similarity). Ubiquitination and subsequent proteasomal degradation is negatively regulated by CCAR2 (By similarity). Polyubiquitinated by C10orf90/FATS, polyubiquitination is 'Lys-48'-linkage independent and non-proteolytic, leading to TP53 stabilization (By similarity). Polyubiquitinated by MUL1 at Lys-24 which leads to proteasomal degradation (By similarity). Deubiquitinated by USP3, leading to stabilization (By similarity). Ubiquitinated by MSL2, promoting its cytoplasmic localization (By similarity). Also ubiquitinated by the SCF(FBXO22)-KDMA4A complex; leading to proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P02340, ECO:0000250|UniProtKB:P04637}.; PTM: Acetylation of Lys-380 by CREBBP enhances transcriptional activity. Acetylation of Lys-380 by EP300. Deacetylation of Lys-380 by SIRT1 impairs its ability to induce proapoptotic program and modulate cell senescence. Deacetylation by SIRT2 impairs its ability to induce transcription activation in a AKT-dependent manner. Acetylation at Lys-379 increases stability. Deacetylation at Lys-379 by SIRT6 decreases its stability, thereby regulating cell senescence. Acetylated at Lys-118 by KAT5, KAT6A and KAT8; regulating its ability to induce proapoptotic program. {ECO:0000250|UniProtKB:P04637}.; PTM: Lactylation by AARS1 prevents ability to undergo liquid-liquid phase separation (LLPS), thereby inhibiting transcription factor activity. {ECO:0000250|UniProtKB:P04637}.
uniprot
proteins
protein_family
P53 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
22726440
uniprot
proteins
pubmed
3060862
uniprot
proteins
pubmed
8441680
uniprot
proteins
pubmed
8663025
uniprot
proteins
pubmed
9278438
uniprot
proteins
sequence_length
391
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04637}. Nucleus {ECO:0000250|UniProtKB:P04637}. Nucleus, PML body {ECO:0000250|UniProtKB:P04637}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P04637}. Mitochondrion matrix {ECO:0000250|UniProtKB:P04637}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P04637}. Note=Interaction with BANP promotes nuclear localization. Recruited into PML bodies together with CHEK2. Translocates to mitochondria upon oxidative stress. Translocates to mitochondria in response to mitomycin C treatment (By similarity). Competitive inhibition of TP53 interaction with HSPA9/MOT-2 by UBXN2A results in increased protein abundance and subsequent translocation of TP53 to the nucleus (By similarity). {ECO:0000250|UniProtKB:P04637}.
uniprot
proteins