TP53
entrez
7157
canonical
uniprot
P04637
canonical
ensembl
ENSG00000141510
resolver
ensp
ENSP00000269305
resolver
ensp
ENSP00000352610
resolver
ensp
ENSP00000391127
resolver
ensp
ENSP00000391478
resolver
ensp
ENSP00000398846
resolver
ensp
ENSP00000424104
resolver
ensp
ENSP00000426252
resolver
ensp
ENSP00000477531
resolver
ensp
ENSP00000478219
resolver
ensp
ENSP00000478499
resolver
ensp
ENSP00000480868
resolver
ensp
ENSP00000481179
resolver
ensp
ENSP00000481401
resolver
ensp
ENSP00000481638
resolver
ensp
ENSP00000482222
resolver
ensp
ENSP00000482537
resolver
ensp
ENSP00000484375
resolver
ensp
ENSP00000484409
resolver
ensp
ENSP00000593626
resolver
ensp
ENSP00000745782
resolver
enst
ENST00000610623
resolver
enst
ENST00000618944
resolver
enst
ENST00000619186
resolver
genesymbol
TP53
resolver
genesymbol_syn
P53
resolver
hgnc
HGNC:11998
resolver
uniprot
A0A087WT22
resolver
uniprot
A0A087WXZ1
resolver
uniprot
A0A087X1Q1
resolver
uniprot
H2EHT1
resolver
uniprot
K7PPA8
resolver
uniprot
Q15086
resolver
uniprot
Q15087
resolver
uniprot
Q15088
resolver
uniprot
Q16535
resolver
uniprot
Q16807
resolver
uniprot
Q16808
resolver
uniprot
Q16809
resolver
uniprot
Q16810
resolver
uniprot
Q16811
resolver
uniprot
Q16848
resolver
uniprot
Q2XN98
resolver
uniprot
Q3LRW1
resolver
uniprot
Q3LRW2
resolver
uniprot
Q3LRW3
resolver
uniprot
Q3LRW4
resolver
uniprot
Q3LRW5
resolver
uniprot
Q53GA5
resolver
uniprot
Q86UG1
resolver
uniprot
Q8J016
resolver
uniprot
Q99659
resolver
uniprot
Q9BTM4
resolver
uniprot
Q9HAQ8
resolver
uniprot
Q9NP68
resolver
uniprot
Q9NPJ2
resolver
uniprot
Q9NZD0
resolver
uniprot
Q9UBI2
resolver
uniprot
Q9UQ61
resolver
uniprot_entry
A0A087WT22_HUMAN
resolver
uniprot_entry
A0A087WXZ1_HUMAN
resolver
uniprot_entry
A0A087X1Q1_HUMAN
resolver
uniprot_entry
H2EHT1_HUMAN
resolver
uniprot_entry
K7PPA8_HUMAN
resolver
uniprot_entry
P53_HUMAN
resolver
uniprot_entry
Q53GA5_HUMAN
resolver
uniprot_sec
Q15086
resolver
uniprot_sec
Q15087
resolver
uniprot_sec
Q15088
resolver
uniprot_sec
Q16535
resolver
uniprot_sec
Q16807
resolver
uniprot_sec
Q16808
resolver
uniprot_sec
Q16809
resolver
uniprot_sec
Q16810
resolver
uniprot_sec
Q16811
resolver
uniprot_sec
Q16848
resolver
uniprot_sec
Q2XN98
resolver
uniprot_sec
Q3LRW1
resolver
uniprot_sec
Q3LRW2
resolver
uniprot_sec
Q3LRW3
resolver
uniprot_sec
Q3LRW4
resolver
uniprot_sec
Q3LRW5
resolver
uniprot_sec
Q86UG1
resolver
uniprot_sec
Q8J016
resolver
uniprot_sec
Q99659
resolver
uniprot_sec
Q9BTM4
resolver
uniprot_sec
Q9HAQ8
resolver
uniprot_sec
Q9NP68
resolver
uniprot_sec
Q9NPJ2
resolver
uniprot_sec
Q9NZD0
resolver
uniprot_sec
Q9UBI2
resolver
uniprot_sec
Q9UQ61
resolver
amino_acid_sequence
MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD
uniprot
proteins
disease_involvement
DISEASE: Note=TP53 is found in increased amounts in a wide variety of transformed cells. TP53 is frequently mutated or inactivated in about 60% of cancers. TP53 defects are found in Barrett metaplasia a condition in which the normally stratified squamous epithelium of the lower esophagus is replaced by a metaplastic columnar epithelium. The condition develops as a complication in approximately 10% of patients with chronic gastroesophageal reflux disease and predisposes to the development of esophageal adenocarcinoma.; DISEASE: Esophageal cancer (ESCR) [MIM:133239]: A malignancy of the esophagus. The most common types are esophageal squamous cell carcinoma and adenocarcinoma. Cancer of the esophagus remains a devastating disease because it is usually not detected until it has progressed to an advanced incurable stage. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Li-Fraumeni syndrome (LFS) [MIM:151623]: An autosomal dominant familial cancer syndrome that in its classic form is defined by the existence of a proband affected by a sarcoma before 45 years with a first degree relative affected by any tumor before 45 years and another first degree relative with any tumor before 45 years or a sarcoma at any age. Other clinical definitions for LFS have been proposed and called Li-Fraumeni like syndrome (LFL). In these families affected relatives develop a diverse set of malignancies at unusually early ages. Four types of cancers account for 80% of tumors occurring in TP53 germline mutation carriers: breast cancers, soft tissue and bone sarcomas, brain tumors (astrocytomas) and adrenocortical carcinomas. Less frequent tumors include choroid plexus carcinoma or papilloma before the age of 15, rhabdomyosarcoma before the age of 5, leukemia, Wilms tumor, malignant phyllodes tumor, colorectal and gastric cancers. {ECO:0000269|PubMed:10484981, ECO:0000269|PubMed:1565144, ECO:0000269|PubMed:1737852, ECO:0000269|PubMed:1933902, ECO:0000269|PubMed:1978757, ECO:0000269|PubMed:2259385, ECO:0000269|PubMed:36108750, ECO:0000269|PubMed:7887414, ECO:0000269|PubMed:8825920, ECO:0000269|PubMed:9452042}. Note=The disease is caused by variants 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. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Lung cancer (LNCR) [MIM:211980]: A common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Papilloma of choroid plexus (CPP) [MIM:260500]: A benign tumor of neuroectodermal origin that generally occurs in childhood, but has also been reported in adults. Although generally found within the ventricular system, choroid plexus papillomas can arise ectopically in the brain parenchyma or disseminate throughout the neuraxis. Patients present with signs and symptoms of increased intracranial pressure including headache, hydrocephalus, papilledema, nausea, vomiting, cranial nerve deficits, gait impairment, and seizures. {ECO:0000269|PubMed:12085209}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Adrenocortical carcinoma (ADCC) [MIM:202300]: A malignant neoplasm of the adrenal cortex and a rare childhood tumor. It occurs with increased frequency in patients with Beckwith-Wiedemann syndrome and Li-Fraumeni syndrome. {ECO:0000269|PubMed:11481490}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Basal cell carcinoma 7 (BCC7) [MIM:614740]: A common malignant skin neoplasm that typically appears on hair-bearing skin, most commonly on sun-exposed areas. It is slow growing and rarely metastasizes, but has potentialities for local invasion and destruction. It usually develops as a flat, firm, pale area that is small, raised, pink or red, translucent, shiny, and waxy, and the area may bleed following minor injury. Tumor size can vary from a few millimeters to several centimeters in diameter. {ECO:0000269|PubMed:21946351}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Bone marrow failure syndrome 5 (BMFS5) [MIM:618165]: A form of bone marrow failure syndrome, a heterogeneous group of life-threatening disorders characterized by hematopoietic defects in association with a range of variable extra-hematopoietic manifestations. BMFS5 is an autosomal dominant form characterized by infantile onset of severe red cell anemia requiring transfusion. Additional features include hypogammaglobulinemia, poor growth with microcephaly, developmental delay, and seizures. {ECO:0000269|PubMed:30146126}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Multifunctional transcription factor that induces cell cycle arrest, DNA repair or apoptosis upon binding to its target DNA sequence (PubMed:11025664, PubMed:12524540, PubMed:12810724, PubMed:15186775, PubMed:15340061, PubMed:17317671, PubMed:17349958, PubMed:19556538, PubMed:20673990, PubMed:20959462, PubMed:22726440, PubMed:24051492, PubMed:24652652, PubMed:35618207, PubMed:36634798, PubMed:38653238, PubMed:9840937). Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type (PubMed:11025664, PubMed:12524540, PubMed:12810724, PubMed:15186775, PubMed:15340061, PubMed:17189187, PubMed:17317671, PubMed:17349958, PubMed:19556538, PubMed:20673990, PubMed:20959462, PubMed:22726440, PubMed:24051492, PubMed:24652652, PubMed:38653238, PubMed:9840937). Negatively regulates cell division by controlling expression of a set of genes required for this process (PubMed:11025664, PubMed:12524540, PubMed:12810724, PubMed:15186775, PubMed:15340061, PubMed:17317671, PubMed:17349958, PubMed:19556538, PubMed:20673990, PubMed:20959462, PubMed:22726440, PubMed:24051492, PubMed:24652652, PubMed:9840937). 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 (PubMed:12524540, PubMed:17189187). Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (PubMed:12524540). However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (PubMed:12524540). In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. 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. 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. Regulates the circadian clock by repressing CLOCK-BMAL1-mediated transcriptional activation of PER2 (PubMed:24051492). {ECO:0000269|PubMed:11025664, ECO:0000269|PubMed:12524540, ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:15186775, ECO:0000269|PubMed:15340061, ECO:0000269|PubMed:17189187, ECO:0000269|PubMed:17317671, ECO:0000269|PubMed:17349958, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:20673990, ECO:0000269|PubMed:20959462, ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:24051492, ECO:0000269|PubMed:24652652, ECO:0000269|PubMed:35618207, ECO:0000269|PubMed:36634798, ECO:0000269|PubMed:38653238, ECO:0000269|PubMed:9840937}.
uniprot
proteins
mass_dalton
43653
uniprot
proteins
mutagenesis
MUTAGEN 15; /note="S->A: Loss of interaction with PPP2R5C, PPP2CAANDPPP2R1A."; /evidence="ECO:0000269|PubMed:17967874"; MUTAGEN 18; /note="T->A: No effect on interaction with MDM2 and increase in protein levels after DNA damage."; /evidence="ECO:0000269|PubMed:10570149"; MUTAGEN 20; /note="S->A: Abolishes phosphorylation site. Abolishes increase in protein levels after DNA damage."; /evidence="ECO:0000269|PubMed:10570149"; MUTAGEN 20; /note="S->D: Constitutively increased TP53 protein levels."; /evidence="ECO:0000269|PubMed:10570149"; MUTAGEN 22..23; /note="LW->QS: Loss of interaction with MDM2, leading to constitutively increased TP53 protein levels."; /evidence="ECO:0000269|PubMed:10570149"; MUTAGEN 24; /note="K->R: Abolishes ubiquitination by MUL1."; /evidence="ECO:0000269|PubMed:21597459"; MUTAGEN 37; /note="S->D: Abolishes phosphorylation by MAPKAPK5."; /evidence="ECO:0000269|PubMed:17254968"; MUTAGEN 46; /note="S->A: Abolishes phosphorylation by DYRK2 and HIPK2 and acetylation of K-382 by CREBBP."; /evidence="ECO:0000269|PubMed:11740489, ECO:0000269|PubMed:16219768, ECO:0000269|PubMed:17349958"; MUTAGEN 46; /note="Missing: Alters interaction with WWOX."; /evidence="ECO:0000269|PubMed:11740489, ECO:0000269|PubMed:16219768, ECO:0000269|PubMed:17349958"; MUTAGEN 55; /note="T->A: Blocks phosphorylation by TAF1."; /evidence="ECO:0000269|PubMed:15053879"; MUTAGEN 183; /note="S->A: Abolishes strongly phosphorylation."; /evidence="ECO:0000269|PubMed:20959462"; MUTAGEN 183; /note="S->E: Inhibits slightly its transcriptional activity."; /evidence="ECO:0000269|PubMed:20959462"; MUTAGEN 248; /note="R->S: Does not induce SNAI1 degradation."; /evidence="ECO:0000269|PubMed:20385133"; MUTAGEN 269; /note="S->A: Abolishes phosphorylation."; /evidence="ECO:0000269|PubMed:20959462"; MUTAGEN 269; /note="S->E: Inhibits strongly its transcriptional activity."; /evidence="ECO:0000269|PubMed:20959462"; MUTAGEN 284; /note="T->E: Inhibits strongly its transcriptional activity."; /evidence="ECO:0000269|PubMed:20959462"; MUTAGEN 291..292; /note="KK->RR: Abolishes polyubiquitination by MKRN1."; /evidence="ECO:0000269|PubMed:19536131"; MUTAGEN 319; /note="K->A: Loss of nuclear localization; when associated with A-320 and A-321."; /evidence="ECO:0000269|PubMed:2156209"; MUTAGEN 320; /note="K->A: Loss of nuclear localization; when associated with A-319 and A-321."; /evidence="ECO:0000269|PubMed:2156209"; MUTAGEN 321; /note="K->A: Loss of nuclear localization; when associated with A-319 and A-320."; /evidence="ECO:0000269|PubMed:2156209"; MUTAGEN 333..337; /note="RGRER->KGKEK: Reduced methylation by PRMT5. Reduced nuclear localization. Decreased binding to promoters of target genes. Reduced transcriptional activity. Decrease in cell cycle arrest."; /evidence="ECO:0000269|PubMed:19011621"; MUTAGEN 359; /note="P->D: Abolishes binding to USP7."; /evidence="ECO:0000269|PubMed:16402859"; MUTAGEN 361; /note="G->E: Abolishes binding to USP7."; /evidence="ECO:0000269|PubMed:16402859"; MUTAGEN 362; /note="S->A: Abolishes binding to USP7."; /evidence="ECO:0000269|PubMed:16402859"; MUTAGEN 370; /note="K->R: Induces a decrease in methylation by SMYD2."; /evidence="ECO:0000269|PubMed:17108971"; MUTAGEN 372; /note="K->R: Induces a decrease in protein stabilization."; /evidence="ECO:0000269|PubMed:15525938"; MUTAGEN 373; /note="K->R: Abolishes dimethylation by EHMT1 and EHMT2."; /evidence="ECO:0000269|PubMed:20118233"; MUTAGEN 381; /note="K->Q: Mimics acetylation, leading to increased stability."; /evidence="ECO:0000269|PubMed:29474172"; MUTAGEN 381; /note="K->R: Decreased acetylation."; /evidence="ECO:0000269|PubMed:29474172"; MUTAGEN 382; /note="K->A: Abolishes acetylation by CREBBP."; /evidence="ECO:0000269|PubMed:10884347, ECO:0000269|PubMed:11740489, ECO:0000269|PubMed:17707234, ECO:0000269|PubMed:20870725"; MUTAGEN 382; /note="K->R: Abolishes monomethylation by KMT5A."; /evidence="ECO:0000269|PubMed:10884347, ECO:0000269|PubMed:11740489, ECO:0000269|PubMed:17707234, ECO:0000269|PubMed:20870725"; MUTAGEN 383; /note="L->A: Abolishes S-315 phosphorylation by CDK2/cyclin A."; /evidence="ECO:0000269|PubMed:10884347"; MUTAGEN 385; /note="F->A: Reduced SUMO1 conjugation."; /evidence="ECO:0000269|PubMed:10884347, ECO:0000269|PubMed:11124955"; MUTAGEN 386; /note="K->A: Abolishes SUMO1 conjugation, in vitro and in vivo."; /evidence="ECO:0000269|PubMed:11124955, ECO:0000269|Ref.37"; MUTAGEN 387; /note="T->A: No effect SUMO1 conjugation."; /evidence="ECO:0000269|PubMed:11124955"; MUTAGEN 388; /note="E->A: Abolishes SUMO1 conjugation."; /evidence="ECO:0000269|PubMed:11124955"; MUTAGEN 392; /note="S->D: Mimics phosphorylation; promotes ability to undergo liquid-liquid phase separation."; /evidence="ECO:0000269|PubMed:35618207"; MUTAGEN 392; /note="S->E: Abolished ability to undergo liquid-liquid phase separation."; /evidence="ECO:0000269|PubMed:31953488
uniprot
proteins
post_translational_modification
PTM: Acetylation of Lys-382 by CREBBP enhances transcriptional activity (PubMed:10656795, PubMed:15448695, PubMed:20228809, PubMed:23431171). Acetylation of Lys-382 by EP300 (PubMed:10656795, PubMed:15448695, PubMed:20228809, PubMed:23431171). Deacetylation of Lys-382 by SIRT1 impairs its ability to induce proapoptotic program and modulate cell senescence (PubMed:10656795, PubMed:15448695, PubMed:20228809, PubMed:23431171). Deacetylation by SIRT2 impairs its ability to induce transcription activation in a AKT-dependent manner (PubMed:10656795, PubMed:15448695, PubMed:20228809, PubMed:23431171, PubMed:29681526). Acetylation at Lys-381 increases stability (PubMed:29474172). Deacetylation at Lys-381 by SIRT6 decreases its stability, thereby regulating cell senescence (PubMed:29474172). Acetylated at Lys-120 by KAT5, KAT6A and KAT8; regulating its ability to induce proapoptotic program (PubMed:17189187, PubMed:19854137, PubMed:23431171). {ECO:0000269|PubMed:10656795, ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:17189187, ECO:0000269|PubMed:19854137, ECO:0000269|PubMed:20228809, ECO:0000269|PubMed:23431171, ECO:0000269|PubMed:29474172, ECO:0000269|PubMed:29681526}.; PTM: Lactylation by AARS1 prevents ability to undergo liquid-liquid phase separation (LLPS), thereby inhibiting transcription factor activity. {ECO:0000269|PubMed:38653238}.; PTM: Phosphorylation on Ser residues mediates transcriptional activation. Phosphorylated by HIPK1 (By similarity). Phosphorylation at Ser-9 by HIPK4 increases repression activity on BIRC5 promoter. Phosphorylated on Thr-18 by VRK1, which may prevent the interaction with MDM2 (PubMed:10951572, PubMed:31527692). 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. Phosphorylated on Thr-55 by TAF1, which promotes MDM2-mediated degradation. Phosphorylated on Ser-33 by CDK7 in a CAK complex in response to DNA damage. Phosphorylated on Ser-46 by HIPK2 upon UV irradiation. Phosphorylation on Ser-46 is required for acetylation by CREBBP. Phosphorylated on Ser-392 following UV but not gamma irradiation. Phosphorylated by NUAK1 at Ser-15 and Ser-392; was initially thought to be mediated by STK11/LKB1 but it was later shown that it is indirect and that STK11/LKB1-dependent phosphorylation is probably mediated by downstream NUAK1 (PubMed:21317932). It is unclear whether AMP directly mediates phosphorylation at Ser-15. Phosphorylated on Thr-18 by isoform 1 and isoform 2 of VRK2. Phosphorylation on Thr-18 by isoform 2 of VRK2 results in a reduction in ubiquitination by MDM2 and an increase in acetylation by EP300. Stabilized by CDK5-mediated phosphorylation in response to genotoxic and oxidative stresses at Ser-15, Ser-33 and Ser-46, leading to accumulation of p53/TP53, particularly in the nucleus, thus inducing the transactivation of p53/TP53 target genes. Phosphorylated by DYRK2 at Ser-46 in response to genotoxic stress. Phosphorylated at Ser-315 and Ser-392 by CDK2 in response to DNA-damage. Phosphorylation at Ser-15 is required for interaction with DDX3X and gamma-tubulin (PubMed:28842590). Phosphorylation at Ser-392 regulates its ability to undergo liquid-liquid phase separation by increasing fluidity of TP53/p53 condensates (PubMed:35618207). {ECO:0000250, ECO:0000269|PubMed:10570149, ECO:0000269|PubMed:10606744, ECO:0000269|PubMed:10884347, ECO:0000269|PubMed:10951572, ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:11447225, ECO:0000269|PubMed:11546806, ECO:0000269|PubMed:11551930, ECO:0000269|PubMed:11554766, ECO:0000269|PubMed:11740489, ECO:0000269|PubMed:11780126, ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:14702041, ECO:0000269|PubMed:15053879, ECO:0000269|PubMed:15866171, ECO:0000269|PubMed:16377624, ECO:0000269|PubMed:16704422, ECO:0000269|PubMed:1705009, ECO:0000269|PubMed:17108107, ECO:0000269|PubMed:17254968, ECO:0000269|PubMed:17349958, ECO:0000269|PubMed:17591690, ECO:0000269|PubMed:17967874, ECO:0000269|PubMed:18022393, ECO:0000269|PubMed:20041275, ECO:0000269|PubMed:20124405, ECO:0000269|PubMed:20959462, ECO:0000269|PubMed:21317932, ECO:0000269|PubMed:2141171, ECO:0000269|PubMed:22214662, ECO:0000269|PubMed:28842590, ECO:0000269|PubMed:31527692, ECO:0000269|PubMed:9372954}.; PTM: Dephosphorylated by PP2A-PPP2R5C holoenzyme at Thr-55. SV40 small T antigen inhibits the dephosphorylation by the AC form of PP2A.; PTM: May be O-glycosylated in the C-terminal basic region. Studied in EB-1 cell line. {ECO:0000269|PubMed:8632915}.; PTM: Ubiquitinated by MDM2 and SYVN1, which leads to proteasomal degradation (PubMed:10722742, PubMed:12810724, PubMed:15340061, PubMed:17170702, PubMed:19880522, PubMed:29681526). 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 (PubMed:10722742, PubMed:12810724, PubMed:20173098). Ubiquitinated by MKRN1 at Lys-291 and Lys-292, which leads to proteasomal degradation (PubMed:19536131). Deubiquitinated by USP10, leading to its stabilization (PubMed:20096447). Ubiquitinated by TRIM24, RFFL, RNF34 and RNF125, which leads to proteasomal degradation (PubMed:19556538). Ubiquitination by TOPORS induces degradation (PubMed:19473992). Deubiquitination by USP7, leading to stabilization (PubMed:15053880). Isoform 4 is monoubiquitinated in an MDM2-independent manner (PubMed:15340061). Ubiquitinated by COP1, which leads to proteasomal degradation (PubMed:19837670). 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 (By similarity). Polyubiquitinated by MUL1 at Lys-24 which leads to proteasomal degradation (PubMed:21597459). Deubiquitinated by USP3, leading to stabilization (PubMed:28807825). Ubiquitinated by MSL2, promoting its cytoplasmic localization (PubMed:19033443). Also ubiquitinated by the SCF(FBXO22)-KDMA4A complex; leading to proteasomal degradation (PubMed:26868148). {ECO:0000250|UniProtKB:P02340, ECO:0000269|PubMed:10722742, ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:15053880, ECO:0000269|PubMed:15340061, ECO:0000269|PubMed:17170702, ECO:0000269|PubMed:18206965, ECO:0000269|PubMed:19033443, ECO:0000269|PubMed:19473992, ECO:0000269|PubMed:19536131, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:19837670, ECO:0000269|PubMed:19880522, ECO:0000269|PubMed:20096447, ECO:0000269|PubMed:20173098, ECO:0000269|PubMed:21597459, ECO:0000269|PubMed:25591766, ECO:0000269|PubMed:25732823, ECO:0000269|PubMed:26868148, ECO:0000269|PubMed:28807825, ECO:0000269|PubMed:29681526}.; PTM: Monomethylated at Lys-372 by SETD7, leading to stabilization and increased transcriptional activation (PubMed:15525938, PubMed:16415881). Monomethylated at Lys-370 by SMYD2, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity (PubMed:17108971). Lys-372 monomethylation prevents interaction with SMYD2 and subsequent monomethylation at Lys-370 (PubMed:17108971). Dimethylated at Lys-373 by EHMT1 and EHMT2 (PubMed:20118233). Monomethylated at Lys-382 by KMT5A, promoting interaction with L3MBTL1 and leading to repress transcriptional activity (PubMed:17707234). Dimethylation at Lys-370 and Lys-382 diminishes p53 ubiquitination, through stabilizing association with the methyl reader PHF20 (PubMed:22864287). Demethylation of dimethylated Lys-370 by KDM1A prevents interaction with TP53BP1 and represses TP53-mediated transcriptional activation (PubMed:17805299). Monomethylated at Arg-333 and dimethylated at Arg-335 and Arg-337 by PRMT5; methylation is increased after DNA damage and might possibly affect TP53 target gene specificity (PubMed:19011621). {ECO:0000269|PubMed:15525938, ECO:0000269|PubMed:16415881, ECO:0000269|PubMed:17108971, ECO:0000269|PubMed:17707234, ECO:0000269|PubMed:17805299, ECO:0000269|PubMed:19011621, ECO:0000269|PubMed:20118233, ECO:0000269|PubMed:22864287}.; PTM: Sumoylated with SUMO1. Sumoylated at Lys-386 by UBC9. {ECO:0000269|PubMed:11124955, ECO:0000269|PubMed:22214662, ECO:0000269|Ref.37}.
uniprot
proteins
protein_family
P53 family
uniprot
proteins
pubmed
10484981
uniprot
proteins
pubmed
10549356
uniprot
proteins
pubmed
10551826
uniprot
proteins
pubmed
10570149
uniprot
proteins
pubmed
10606744
uniprot
proteins
pubmed
10644996
uniprot
proteins
pubmed
10656795
uniprot
proteins
pubmed
10722742
uniprot
proteins
pubmed
10884347
uniprot
proteins
pubmed
10951572
uniprot
proteins
pubmed
11007800
uniprot
proteins
pubmed
11023613
uniprot
proteins
pubmed
11025664
uniprot
proteins
pubmed
11058590
uniprot
proteins
pubmed
11124955
uniprot
proteins
pubmed
11239457
uniprot
proteins
pubmed
11447225
uniprot
proteins
pubmed
11481490
uniprot
proteins
pubmed
11546806
uniprot
proteins
pubmed
11551930
uniprot
proteins
pubmed
11554448
uniprot
proteins
pubmed
11554766
uniprot
proteins
pubmed
11672523
uniprot
proteins
pubmed
11706030
uniprot
proteins
pubmed
11740489
uniprot
proteins
pubmed
11780126
uniprot
proteins
pubmed
11925430
uniprot
proteins
pubmed
12085209
uniprot
proteins
pubmed
12507430
uniprot
proteins
pubmed
12524540
uniprot
proteins
pubmed
12702766
uniprot
proteins
pubmed
12724314
uniprot
proteins
pubmed
12750254
uniprot
proteins
pubmed
12810724
uniprot
proteins
pubmed
12851404
uniprot
proteins
pubmed
12944468
uniprot
proteins
pubmed
1303181
uniprot
proteins
pubmed
1327751
uniprot
proteins
pubmed
1394225
uniprot
proteins
pubmed
1437144
uniprot
proteins
pubmed
14534297
uniprot
proteins
pubmed
1459726
uniprot
proteins
pubmed
14660794
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14702041
uniprot
proteins
pubmed
15053879
uniprot
proteins
pubmed
15053880
uniprot
proteins
pubmed
15109303
uniprot
proteins
pubmed
15136035
uniprot
proteins
pubmed
15186775
uniprot
proteins
pubmed
15340061
uniprot
proteins
pubmed
15448695
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15525938
uniprot
proteins
pubmed
1565144
uniprot
proteins
pubmed
15687255
uniprot
proteins
pubmed
15701641
uniprot
proteins
pubmed
15855171
uniprot
proteins
pubmed
15866171
uniprot
proteins
pubmed
16131611
uniprot
proteins
pubmed
16219768
uniprot
proteins
pubmed
1631151
uniprot
proteins
pubmed
16322561
uniprot
proteins
pubmed
16376338
uniprot
proteins
pubmed
16377624
uniprot
proteins
pubmed
16402859
uniprot
proteins
pubmed
16415881
uniprot
proteins
pubmed
16474402
uniprot
proteins
pubmed
1647768
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
16704422
uniprot
proteins
pubmed
1672732
uniprot
proteins
pubmed
16793544
uniprot
proteins
pubmed
16845383
uniprot
proteins
pubmed
1694291
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
1699228
uniprot
proteins
pubmed
17015838
uniprot
proteins
pubmed
1705009
uniprot
proteins
pubmed
17108107
uniprot
proteins
pubmed
17108971
uniprot
proteins
pubmed
17121812
uniprot
proteins
pubmed
17145718
uniprot
proteins
pubmed
17170702
uniprot
proteins
pubmed
17189187
uniprot
proteins
pubmed
17224074
uniprot
proteins
pubmed
17245430
uniprot
proteins
pubmed
17254968
uniprot
proteins
pubmed
17311302
uniprot
proteins
pubmed
17317671
uniprot
proteins
pubmed
17332504
uniprot
proteins
pubmed
17349958
uniprot
proteins
pubmed
1737852
uniprot
proteins
pubmed
17467953
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17591690
uniprot
proteins
pubmed
17707234
uniprot
proteins
pubmed
17719541
uniprot
proteins
pubmed
17805299
uniprot
proteins
pubmed
17904127
uniprot
proteins
pubmed
17954561
uniprot
proteins
pubmed
17967874
uniprot
proteins
pubmed
18022393
uniprot
proteins
pubmed
18206965
uniprot
proteins
pubmed
18249187
uniprot
proteins
pubmed
18453682
uniprot
proteins
pubmed
1848668
uniprot
proteins
pubmed
1849234
uniprot
proteins
pubmed
18585004
uniprot
proteins
pubmed
18650397
uniprot
proteins
pubmed
1868473
uniprot
proteins
pubmed
18690848
uniprot
proteins
pubmed
18996393
uniprot
proteins
pubmed
19011621
uniprot
proteins
pubmed
19033443
uniprot
proteins
pubmed
1905840
uniprot
proteins
pubmed
1915267
uniprot
proteins
pubmed
1933902
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19473992
uniprot
proteins
pubmed
19509332
uniprot
proteins
pubmed
19515728
uniprot
proteins
pubmed
19536131
uniprot
proteins
pubmed
19556538
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19776115
uniprot
proteins
pubmed
1978757
uniprot
proteins
pubmed
19837670
uniprot
proteins
pubmed
19854137
uniprot
proteins
pubmed
19880522
uniprot
proteins
pubmed
1999338
uniprot
proteins
pubmed
20041275
uniprot
proteins
pubmed
20096117
uniprot
proteins
pubmed
20096447
uniprot
proteins
pubmed
20118233
uniprot
proteins
pubmed
20124405
uniprot
proteins
pubmed
20142040
uniprot
proteins
pubmed
20173098
uniprot
proteins
pubmed
20228809
uniprot
proteins
pubmed
20364130
uniprot
proteins
pubmed
20385133
uniprot
proteins
pubmed
20660729
uniprot
proteins
pubmed
20673990
uniprot
proteins
pubmed
20870725
uniprot
proteins
pubmed
20959462
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21317932
uniprot
proteins
pubmed
2141171
uniprot
proteins
pubmed
2156209
uniprot
proteins
pubmed
21597459
uniprot
proteins
pubmed
2175676
uniprot
proteins
pubmed
21946351
uniprot
proteins
pubmed
21952639
uniprot
proteins
pubmed
22214662
uniprot
proteins
pubmed
22522597
uniprot
proteins
pubmed
2259385
uniprot
proteins
pubmed
2263646
uniprot
proteins
pubmed
22726440
uniprot
proteins
pubmed
22864287
uniprot
proteins
pubmed
22914926
uniprot
proteins
pubmed
22945289
uniprot
proteins
pubmed
23431171
uniprot
proteins
pubmed
23752197
uniprot
proteins
pubmed
24051492
uniprot
proteins
pubmed
24625977
uniprot
proteins
pubmed
24652652
uniprot
proteins
pubmed
25168243
uniprot
proteins
pubmed
25422469
uniprot
proteins
pubmed
25591766
uniprot
proteins
pubmed
25732823
uniprot
proteins
pubmed
25772236
uniprot
proteins
pubmed
26634371
uniprot
proteins
pubmed
26868148
uniprot
proteins
pubmed
27323408
uniprot
proteins
pubmed
27657329
uniprot
proteins
pubmed
28807825
uniprot
proteins
pubmed
28842590
uniprot
proteins
pubmed
2905688
uniprot
proteins
pubmed
2946935
uniprot
proteins
pubmed
29474172
uniprot
proteins
pubmed
29681526
uniprot
proteins
pubmed
30146126
uniprot
proteins
pubmed
3025664
uniprot
proteins
pubmed
31527692
uniprot
proteins
pubmed
31953488
uniprot
proteins
pubmed
32144153
uniprot
proteins
pubmed
32442400
uniprot
proteins
pubmed
33591310
uniprot
proteins
pubmed
34404770
uniprot
proteins
pubmed
34523970
uniprot
proteins
pubmed
35122041
uniprot
proteins
pubmed
35618207
uniprot
proteins
pubmed
36108750
uniprot
proteins
pubmed
36634798
uniprot
proteins
pubmed
38653238
uniprot
proteins
pubmed
3894933
uniprot
proteins
pubmed
4006916
uniprot
proteins
pubmed
6396087
uniprot
proteins
pubmed
7682763
uniprot
proteins
pubmed
7773777
uniprot
proteins
pubmed
7878469
uniprot
proteins
pubmed
7887414
uniprot
proteins
pubmed
8013454
uniprot
proteins
pubmed
8023157
uniprot
proteins
pubmed
8023159
uniprot
proteins
pubmed
8118819
uniprot
proteins
pubmed
8266092
uniprot
proteins
pubmed
8316628
uniprot
proteins
pubmed
8336944
uniprot
proteins
pubmed
8402617
uniprot
proteins
pubmed
8632903
uniprot
proteins
pubmed
8632915
uniprot
proteins
pubmed
8718514
uniprot
proteins
pubmed
8825920
uniprot
proteins
pubmed
8829627
uniprot
proteins
pubmed
8829653
uniprot
proteins
pubmed
8875926
uniprot
proteins
pubmed
8875929
uniprot
proteins
pubmed
9101296
uniprot
proteins
pubmed
9321402
uniprot
proteins
pubmed
9372954
uniprot
proteins
pubmed
9419979
uniprot
proteins
pubmed
9450901
uniprot
proteins
pubmed
9452042
uniprot
proteins
pubmed
9840937
uniprot
proteins
sequence_length
393
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15340061, ECO:0000269|PubMed:17170702, ECO:0000269|PubMed:19011621, ECO:0000269|PubMed:19033443, ECO:0000269|PubMed:21597459, ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:22914926, ECO:0000269|PubMed:24625977, ECO:0000269|PubMed:26634371}. Nucleus {ECO:0000269|PubMed:15340061, ECO:0000269|PubMed:17170702, ECO:0000269|PubMed:17591690, ECO:0000269|PubMed:18206965, ECO:0000269|PubMed:19011621, ECO:0000269|PubMed:21597459, ECO:0000269|PubMed:22914926, ECO:0000269|PubMed:24625977, ECO:0000269|PubMed:26634371}. Nucleus, PML body {ECO:0000269|PubMed:11025664, ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:36108750}. Endoplasmic reticulum {ECO:0000269|PubMed:17170702}. Mitochondrion matrix {ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:25168243, ECO:0000269|PubMed:27323408}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:28842590}. Note=Recruited into PML bodies together with CHEK2 (PubMed:12810724). Translocates to mitochondria upon oxidative stress (PubMed:22726440). Translocates to mitochondria in response to mitomycin C treatment (PubMed:27323408). Competitive inhibition of TP53 interaction with HSPA9/MOT-2 by UBXN2A results in increased protein abundance and subsequent translocation of TP53 to the nucleus (PubMed:24625977). {ECO:0000269|PubMed:12810724, ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:24625977, ECO:0000269|PubMed:27323408}.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000269|PubMed:23752197}. Cytoplasm. Note=Predominantly nuclear but localizes to the cytoplasm when expressed with isoform 4.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. Cytoplasm. Note=Localized mainly in the nucleus with minor staining in the cytoplasm.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus. Cytoplasm. Note=Localized in the nucleus in most cells but found in the cytoplasm in some cells.; SUBCELLULAR LOCATION: [Isoform 4]: Nucleus. Cytoplasm. Note=Predominantly nuclear but translocates to the cytoplasm following cell stress.; SUBCELLULAR LOCATION: [Isoform 7]: Nucleus. Cytoplasm. Note=Localized mainly in the nucleus with minor staining in the cytoplasm.; SUBCELLULAR LOCATION: [Isoform 8]: Nucleus. Cytoplasm. Note=Localized in both nucleus and cytoplasm in most cells. In some cells, forms foci in the nucleus that are different from nucleoli.; SUBCELLULAR LOCATION: [Isoform 9]: Cytoplasm.
uniprot
proteins