Tp53
entrez
22059
canonical
uniprot
P02340
canonical
ensembl
ENSMUSG00000059552
resolver
ensp
ENSMUSP00000104298
resolver
ensp
ENSMUSP00000127130
resolver
ensp
ENSMUSP00000279808
resolver
ensp
ENSMUSP00000279809
resolver
ensp
ENSMUSP00000279811
resolver
enst
ENSMUST00000108658
resolver
enst
ENSMUST00000171247
resolver
genesymbol
Tp53
resolver
genesymbol
Trp53
resolver
genesymbol_syn
P53
resolver
genesymbol_syn
Trp53
resolver
genesymbol_syn
p53
resolver
uniprot
F6V780
resolver
uniprot
Q3UGQ1
resolver
uniprot
Q549C9
resolver
uniprot
Q80ZA1
resolver
uniprot
Q9QUP3
resolver
uniprot_entry
F6V780_MOUSE
resolver
uniprot_entry
P53_MOUSE
resolver
uniprot_entry
Q3UGQ1_MOUSE
resolver
uniprot_entry
Q549C9_MOUSE
resolver
uniprot_entry
Q80ZA1_MOUSE
resolver
uniprot_sec
Q9QUP3
resolver
amino_acid_sequence
MTAMEESQSDISLELPLSQETFSGLWKLLPPEDILPSPHCMDDLLLPQDVEEFFEGPSEALRVSGAPAAQDPVTETPGPVAPAPATPWPLSSFVPSQKTYQGNYGFHLGFLQSGTAKSVMCTYSPPLNKLFCQLAKTCPVQLWVSATPPAGSRVRAMAIYKKSQHMTEVVRRCPHHERCSDGDGLAPPQHLIRVEGNLYPEYLEDRQTFRHSVVVPYEPPEAGSEYTTIHYKYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRDSFEVRVCACPGRDRRTEEENFRKKEVLCPELPPGSAKRALPTCTSASPPQKKKPLDGEYFTLKIRGRKRFEMFRELNEALELKDAHATEESGDSRAHSSYLKTKKGQSTSRHKKTMVKKVGPDSD
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 (PubMed:19556538, PubMed:20673990, PubMed:22726440). 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 (By similarity). 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, but seems to have to effect on cell-cycle regulation. Regulates the circadian clock by repressing CLOCK-BMAL1-mediated transcriptional activation of PER2 (PubMed:24051492). {ECO:0000250|UniProtKB:P04637, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:20673990, ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:24051492}.
uniprot
proteins
mass_dalton
43458
uniprot
proteins
post_translational_modification
PTM: Phosphorylation on Ser residues mediates transcriptional activation. Phosphorylation at Ser-12 by HIPK4 increases repression activity on BIRC5 promoter. Phosphorylated on Thr-21 by VRK1. Phosphorylated on Ser-23 by CHEK2 in response to DNA damage, which prevents ubiquitination by MDM2. Phosphorylated on Ser-23 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. Stabilized by CDK5-mediated phosphorylation in response to genotoxic and oxidative stresses at Ser-18 leading to accumulation of p53/TP53, particularly in the nucleus, thus inducing the transactivation of p53/TP53 target genes (By similarity). Phosphorylated on Ser-389 following UV but not gamma irradiation. Phosphorylated by HIPK1. Phosphorylation at Ser-18 is required for interaction with DDX3X and gamma-tubulin (By similarity). Phosphorylation at Ser-389 regulates its ability to undergo liquid-liquid phase separation by increasing fluidity of TP53/p53 condensates (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P04637, ECO:0000269|PubMed:12702766, ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:17254968, ECO:0000269|PubMed:18022393, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:2145148, ECO:0000269|PubMed:3006031}.; 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 at Lys-288 and Lys-289, 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 (PubMed:25732823). Polyubiquitinated by C10orf90/FATS, polyubiquitination is 'Lys-48'-linkage independent and non-proteolytic, leading to TP53 stabilization (PubMed:24240685). Also ubiquitinated by the SCF(FBXO22)-KDMA4A complex; leading to proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P04637, ECO:0000269|PubMed:24240685, ECO:0000269|PubMed:25732823}.; PTM: Monomethylated at Lys-369 by SETD7, leading to stabilization and increased transcriptional activation. Monomethylated at Lys-367 by SMYD2, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity. Lys-369 monomethylation prevents interaction with SMYD2 and subsequent monomethylation at Lys-367. Dimethylated at Lys-370 by EHMT1 and EHMT2. Monomethylated at Lys-379 by KMT5A, promoting interaction with L3MBTL1 and leading to repress transcriptional activity. Demethylation of dimethylated Lys-367 by KDM1A prevents interaction with TP53BP1 and represses TP53-mediated transcriptional activation (By similarity). Monomethylated at Arg-330 and dimethylated at Arg-332 and Arg-334 by PRMT5; methylation is increased after DNA damage and might possibly affect TP53 target gene specificity (By similarity). Polyubiquitinated by MUL1 at Lys-27 which leads to proteasomal degradation (By similarity). Deubiquitinated by USP3, leading to stabilization (By similarity). Ubiquitinated by MSL2, promoting its cytoplasmic localization (By similarity). {ECO:0000250|UniProtKB:P04637}.; PTM: Sumoylated with SUMO1. Sumoylated at Lys-383 by UBC9 (By similarity). {ECO:0000250}.; PTM: Acetylation of Lys-379 by CREBBP enhances transcriptional activity. Acetylation of Lys-379 by EP300. Deacetylation of Lys-379 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-378 increases stability. Deacetylation at Lys-378 by SIRT6 decreases its stability, thereby regulating cell senescence. Acetylated at Lys-117 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
10403253
uniprot
proteins
pubmed
10644996
uniprot
proteins
pubmed
11152481
uniprot
proteins
pubmed
11672522
uniprot
proteins
pubmed
11706030
uniprot
proteins
pubmed
12494467
uniprot
proteins
pubmed
12702766
uniprot
proteins
pubmed
1406686
uniprot
proteins
pubmed
14719112
uniprot
proteins
pubmed
15195100
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15526030
uniprot
proteins
pubmed
16717092
uniprot
proteins
pubmed
17139084
uniprot
proteins
pubmed
17254968
uniprot
proteins
pubmed
1766680
uniprot
proteins
pubmed
17719541
uniprot
proteins
pubmed
17876829
uniprot
proteins
pubmed
18022393
uniprot
proteins
pubmed
18978813
uniprot
proteins
pubmed
19151705
uniprot
proteins
pubmed
19556538
uniprot
proteins
pubmed
20673990
uniprot
proteins
pubmed
2145148
uniprot
proteins
pubmed
221923
uniprot
proteins
pubmed
22726440
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
24051492
uniprot
proteins
pubmed
24240685
uniprot
proteins
pubmed
25732823
uniprot
proteins
pubmed
3006031
uniprot
proteins
pubmed
3023970
uniprot
proteins
pubmed
3329909
uniprot
proteins
pubmed
35122041
uniprot
proteins
pubmed
6092064
uniprot
proteins
pubmed
6379601
uniprot
proteins
pubmed
6646235
uniprot
proteins
sequence_length
390
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