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Protein

Cellular tumor antigen p53

Gene

TP53

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. 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 seem to have to 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-ARNTL/BMAL1-mediated transcriptional activation of PER2 (PubMed:24051492).12 Publications

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi176Zinc1
Metal bindingi179Zinc1
Metal bindingi238Zinc1
Metal bindingi242Zinc1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi102 – 292Add BLAST191

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • chaperone binding Source: UniProtKB
  • chromatin binding Source: UniProtKB
  • copper ion binding Source: UniProtKB
  • core promoter sequence-specific DNA binding Source: UniProtKB
  • damaged DNA binding Source: GO_Central
  • DNA binding Source: UniProtKB
  • double-stranded DNA binding Source: GO_Central
  • enzyme binding Source: UniProtKB
  • histone acetyltransferase binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • p53 binding Source: GO_Central
  • protease binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • protein phosphatase 2A binding Source: UniProtKB
  • protein phosphatase binding Source: UniProtKB
  • protein self-association Source: AgBase
  • receptor tyrosine kinase binding Source: BHF-UCL
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: ParkinsonsUK-UCL
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: UniProtKB
  • RNA polymerase II transcription factor binding Source: BHF-UCL
  • sequence-specific DNA binding Source: GO_Central
  • transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding Source: BHF-UCL
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • transcription regulatory region DNA binding Source: BHF-UCL
  • ubiquitin protein ligase binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • base-excision repair Source: UniProtKB
  • cell aging Source: UniProtKB
  • cell cycle arrest Source: UniProtKB
  • cell differentiation Source: UniProtKB
  • cell proliferation Source: UniProtKB
  • cellular protein localization Source: UniProtKB
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to drug Source: UniProtKB
  • cellular response to glucose starvation Source: UniProtKB
  • cellular response to hypoxia Source: UniProtKB
  • cellular response to ionizing radiation Source: BHF-UCL
  • cellular response to UV Source: GO_Central
  • chromatin assembly Source: UniProtKB
  • circadian behavior Source: UniProtKB
  • determination of adult lifespan Source: BHF-UCL
  • DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
  • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  • DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: BHF-UCL
  • DNA strand renaturation Source: UniProtKB
  • entrainment of circadian clock by photoperiod Source: UniProtKB
  • ER overload response Source: MGI
  • intrinsic apoptotic signaling pathway Source: HGNC
  • intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
  • mitotic G1 DNA damage checkpoint Source: BHF-UCL
  • multicellular organism development Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cell growth Source: UniProtKB
  • negative regulation of cell proliferation Source: CACAO
  • negative regulation of fibroblast proliferation Source: UniProtKB
  • negative regulation of helicase activity Source: UniProtKB
  • negative regulation of telomerase activity Source: BHF-UCL
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • nucleotide-excision repair Source: UniProtKB
  • oligodendrocyte apoptotic process Source: UniProtKB
  • oxidative stress-induced premature senescence Source: BHF-UCL
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of cell cycle arrest Source: UniProtKB
  • positive regulation of execution phase of apoptosis Source: AgBase
  • positive regulation of gene expression Source: BHF-UCL
  • positive regulation of histone deacetylation Source: GO_Central
  • positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  • positive regulation of neuron apoptotic process Source: GO_Central
  • positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • positive regulation of protein export from nucleus Source: Reactome
  • positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
  • positive regulation of protein oligomerization Source: UniProtKB
  • positive regulation of reactive oxygen species metabolic process Source: BHF-UCL
  • positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
  • positive regulation of thymocyte apoptotic process Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: Reactome
  • protein complex assembly Source: UniProtKB
  • protein localization Source: UniProtKB
  • protein sumoylation Source: Reactome
  • protein tetramerization Source: UniProtKB
  • Ras protein signal transduction Source: BHF-UCL
  • regulation of apoptotic process Source: MGI
  • regulation of cell cycle G2/M phase transition Source: Reactome
  • regulation of mitochondrial membrane permeability Source: UniProtKB
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • regulation of transcription, DNA-templated Source: UniProtKB
  • replicative senescence Source: BHF-UCL
  • response to antibiotic Source: UniProtKB
  • response to gamma radiation Source: BHF-UCL
  • response to X-ray Source: GO_Central
  • viral process Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Apoptosis, Biological rhythms, Cell cycle, Host-virus interaction, Necrosis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000141510-MONOMER.
ReactomeiR-HSA-111448. Activation of NOXA and translocation to mitochondria.
R-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-139915. Activation of PUMA and translocation to mitochondria.
R-HSA-1912408. Pre-NOTCH Transcription and Translation.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-2559584. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
R-HSA-2559585. Oncogene Induced Senescence.
R-HSA-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-HSA-3232118. SUMOylation of transcription factors.
R-HSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-HSA-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-HSA-5628897. TP53 Regulates Metabolic Genes.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-5689896. Ovarian tumor domain proteases.
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-6803204. TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
R-HSA-6803205. TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
R-HSA-6803207. TP53 Regulates Transcription of Caspase Activators and Caspases.
R-HSA-6803211. TP53 Regulates Transcription of Death Receptors and Ligands.
R-HSA-6804114. TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
R-HSA-6804115. TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
R-HSA-6804116. TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
R-HSA-6804754. Regulation of TP53 Expression.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-6804757. Regulation of TP53 Degradation.
R-HSA-6804758. Regulation of TP53 Activity through Acetylation.
R-HSA-6804759. Regulation of TP53 Activity through Association with Co-factors.
R-HSA-6804760. Regulation of TP53 Activity through Methylation.
R-HSA-6811555. PI5P Regulates TP53 Acetylation.
R-HSA-69473. G2/M DNA damage checkpoint.
R-HSA-69481. G2/M Checkpoints.
R-HSA-69541. Stabilization of p53.
R-HSA-69895. Transcriptional activation of cell cycle inhibitor p21.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP04637.
SIGNORiP04637.

Protein family/group databases

TCDBi1.C.110.1.1. the pore-forming pnc-27 peptide of 32 aas from the p53 tumor suppressor protein (pnc-27) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Cellular tumor antigen p53
Alternative name(s):
Antigen NY-CO-13
Phosphoprotein p53
Tumor suppressor p53
Gene namesi
Name:TP53
Synonyms:P53
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:11998. TP53.

Subcellular locationi

Isoform 1 :
  • Nucleus
  • Cytoplasm

  • Note: Predominantly nuclear but localizes to the cytoplasm when expressed with isoform 4.
Isoform 2 :
  • Nucleus
  • Cytoplasm

  • Note: Localized mainly in the nucleus with minor staining in the cytoplasm.
Isoform 3 :
  • Nucleus
  • Cytoplasm

  • Note: Localized in the nucleus in most cells but found in the cytoplasm in some cells.
Isoform 4 :
  • Nucleus
  • Cytoplasm

  • Note: Predominantly nuclear but translocates to the cytoplasm following cell stress.
Isoform 7 :
  • Nucleus
  • Cytoplasm

  • Note: Localized mainly in the nucleus with minor staining in the cytoplasm.
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.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB-SubCell
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB
  • nuclear chromatin Source: BHF-UCL
  • nuclear matrix Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB
  • protein complex Source: BHF-UCL
  • replication fork Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Esophageal cancer (ESCR)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:133239
Li-Fraumeni syndrome (LFS)9 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal 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 (PubMed:8118819 and PubMed:8718514) 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.
See also OMIM:151623
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04462182P → L in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs534447939dbSNPEnsembl.1
Natural variantiVAR_04465097V → I in familial cancer not matching LFS; germline mutation and in a sporadic cancer; somatic mutation. 1
Natural variantiVAR_044661105G → C in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_044667106S → R in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_005861110R → L in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation; does not induce SNAI1 degradation. 1 PublicationCorresponds to variant rs11540654dbSNPEnsembl.1
Natural variantiVAR_044716126Y → C in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_044740132K → E in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs747342068dbSNPEnsembl.1
Natural variantiVAR_044747133M → R in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_005875133M → T in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant rs28934873dbSNPEnsembl.1
Natural variantiVAR_005881138A → P in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs28934875dbSNPEnsembl.1
Natural variantiVAR_044764138A → S in LFS; germline mutation. 1
Natural variantiVAR_005886141C → Y in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs587781288dbSNPEnsembl.1
Natural variantiVAR_044790144Q → L in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_005895151P → S in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant rs28934874dbSNPEnsembl.1
Natural variantiVAR_005896151P → T in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs28934874dbSNPEnsembl.1
Natural variantiVAR_005897152P → L in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant rs587782705dbSNPEnsembl.1
Natural variantiVAR_044836155T → N in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_044841156R → H in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs371524413dbSNPEnsembl.1
Natural variantiVAR_005906158R → G in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_005907158R → H in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs587782144dbSNPEnsembl.1
Natural variantiVAR_033035163Y → C in LFS; germline mutation and in sporadic cancers; somatic mutation. 2 PublicationsCorresponds to variant rs148924904dbSNPEnsembl.1
Natural variantiVAR_044885167Q → K in LFS; germline mutation and in a sporadic cancer; somatic mutation. 1
Natural variantiVAR_044906172V → F in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_005926173V → M in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_044911174R → G in LFS; germline mutation and in a sporadic cancer; somatic mutation. 1
Natural variantiVAR_005929175R → G in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs138729528dbSNPEnsembl.1
Natural variantiVAR_005932175R → H in LFS; germline mutation and in sporadic cancers; somatic mutation; does not induce SNAI1 degradation; reduces interaction with ZNF385A. 6 PublicationsCorresponds to variant rs28934578dbSNPEnsembl.1
Natural variantiVAR_005930175R → L in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs28934578dbSNPEnsembl.1
Natural variantiVAR_044939179H → Y in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs587780070dbSNPEnsembl.1
Natural variantiVAR_044943180E → K in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_044946181R → C in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs587782596dbSNPEnsembl.1
Natural variantiVAR_044948181R → H in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs397514495dbSNPEnsembl.1
Natural variantiVAR_005937181R → L in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs397514495dbSNPEnsembl.1
Natural variantiVAR_044949181R → P in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_044978189A → V in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs121912665dbSNPEnsembl.1
Natural variantiVAR_005948193H → R in LFS; germline mutation and in sporadic cancers; somatic mutation. 2 PublicationsCorresponds to variant rs786201838dbSNPEnsembl.1
Natural variantiVAR_045007196R → P in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_045010197V → E in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_045013197V → M in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs786204041dbSNPEnsembl.1
Natural variantiVAR_045073210N → Y in a familial cancer not matching LFS; germline mutation. 1
Natural variantiVAR_036506213R → P in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication1
Natural variantiVAR_005955213R → Q in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs587778720dbSNPEnsembl.1
Natural variantiVAR_045114219P → S in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_005957220Y → C in LFS; germline mutation and in sporadic cancers; somatic mutation. 2 PublicationsCorresponds to variant rs121912666dbSNPEnsembl.1
Natural variantiVAR_045151227S → T in LFS; germline mutation and in a sporadic cancer; somatic mutation. 1
Natural variantiVAR_045175233H → D in LFS; germline mutation and in a sporadic cancer; somatic mutation. 1
Natural variantiVAR_005963234Y → C in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs587780073dbSNPEnsembl.1
Natural variantiVAR_045186235N → S in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs144340710dbSNPEnsembl.1
Natural variantiVAR_045189236Y → C in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_005965237M → I in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs587782664dbSNPEnsembl.1
Natural variantiVAR_045200238C → G in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_045202238C → S in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_005967238C → Y in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs730882005dbSNPEnsembl.1
Natural variantiVAR_005969241S → F in LFS; germline mutation and in sporadic cancers; somatic mutation. 2 PublicationsCorresponds to variant rs28934573dbSNPEnsembl.1
Natural variantiVAR_047183241S → T in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_045224242C → Y in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs121912655dbSNPEnsembl.1
Natural variantiVAR_045232244G → D in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs28934572dbSNPEnsembl.1
Natural variantiVAR_045236244G → V in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_005972245G → C in LFS; germline mutation and in sporadic cancers; somatic mutation. 2 PublicationsCorresponds to variant rs28934575dbSNPEnsembl.1
Natural variantiVAR_005973245G → D in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant rs121912656dbSNPEnsembl.1
Natural variantiVAR_005974245G → S in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant rs28934575dbSNPEnsembl.1
Natural variantiVAR_005975245G → V in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant rs121912656dbSNPEnsembl.1
Natural variantiVAR_005978246M → V in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs483352695dbSNPEnsembl.1
Natural variantiVAR_005983248R → Q in LFS; germline mutation and in sporadic cancers; somatic mutation. 4 PublicationsCorresponds to variant rs11540652dbSNPEnsembl.1
Natural variantiVAR_005984248R → W in LFS; germline mutation and in sporadic cancers; somatic mutation. 3 PublicationsCorresponds to variant rs121912651dbSNPEnsembl.1
Natural variantiVAR_045258251I → M in LFS; germline mutation. 1
Natural variantiVAR_005988252L → P in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant rs121912653dbSNPEnsembl.1
Natural variantiVAR_045284257L → Q in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs28934577dbSNPEnsembl.1
Natural variantiVAR_005991258E → K in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant rs121912652dbSNPEnsembl.1
Natural variantiVAR_045321265L → P in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_045330267R → Q in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs587780075dbSNPEnsembl.1
Natural variantiVAR_045351272V → A in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_005992272V → L in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant rs121912657dbSNPEnsembl.1
Natural variantiVAR_005993273R → C in LFS; germline mutation and in sporadic cancers; somatic mutation. 4 PublicationsCorresponds to variant rs121913343dbSNPEnsembl.1
Natural variantiVAR_005994273R → G in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_005995273R → H in LFS; germline mutation and in sporadic cancers; somatic mutation; abolishes sequence-specific DNA binding; does not induce SNAI1 degradation. 9 PublicationsCorresponds to variant rs28934576dbSNPEnsembl.1
Natural variantiVAR_036509273R → L in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant rs28934576dbSNPEnsembl.1
Natural variantiVAR_045357273R → S in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs121913343dbSNPEnsembl.1
Natural variantiVAR_005998275C → Y in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication1
Natural variantiVAR_006003278P → L in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication1
Natural variantiVAR_006004278P → S in LFS; germline mutation and in sporadic cancers; somatic mutation. 3 Publications1
Natural variantiVAR_006005278P → T in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_006007280R → K in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation; no effect on interaction with CCAR2. 2 Publications1
Natural variantiVAR_047202281D → N in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs764146326dbSNPEnsembl.1
Natural variantiVAR_006014281D → V in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs587781525dbSNPEnsembl.1
Natural variantiVAR_045384282R → G in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs28934574dbSNPEnsembl.1
Natural variantiVAR_045387282R → Q in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation. 2 Publications1
Natural variantiVAR_006016282R → W in LFS; germline mutation and in sporadic cancers; somatic mutation; does not induce SNAI1 degradation. 2 PublicationsCorresponds to variant rs28934574dbSNPEnsembl.1
Natural variantiVAR_006017283R → C in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs149633775dbSNPEnsembl.1
Natural variantiVAR_006024285E → Q in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_006026286E → A in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_045411290R → H in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant rs55819519dbSNPEnsembl.1
Natural variantiVAR_045412290R → L in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_015819292K → I in LFS; germline mutation and in a sporadic cancer; somatic mutation. 1 PublicationCorresponds to variant rs121912663dbSNPEnsembl.1
Natural variantiVAR_045471305K → M in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_045475306R → P in LFS; germline mutation and in a sporadic cancer; somatic mutation. 1
Natural variantiVAR_006038309P → S in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 Publication1
Natural variantiVAR_006039325G → V in LFS; germline mutation. 1 PublicationCorresponds to variant rs28934271dbSNPEnsembl.1
Natural variantiVAR_006041337R → C in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant rs587782529dbSNPEnsembl.1
Natural variantiVAR_035016337R → H in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant rs121912664dbSNPEnsembl.1
Natural variantiVAR_045546344L → P in LFS; germline mutation and in a sporadic cancer; somatic mutation. Corresponds to variant rs121912662dbSNPEnsembl.1
Natural variantiVAR_045568365H → Y in a familial cancer not matching LFS; germline mutation and in a sporadic cancer; somatic mutation. Corresponds to variant rs267605075dbSNPEnsembl.1
Natural variantiVAR_022317366S → A in a familial cancer not matching LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant rs17881470dbSNPEnsembl.1
Squamous cell carcinoma of the head and neck (HNSCC)
The gene represented in this entry is involved in disease pathogenesis.
Disease descriptionA non-melanoma skin cancer affecting the head and neck. The hallmark of cutaneous SCC is malignant transformation of normal epidermal keratinocytes.
See also OMIM:275355
Lung cancer (LNCR)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:211980
Papilloma of choroid plexus (CPP)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:260500
Adrenocortical carcinoma (ADCC)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:202300
Basal cell carcinoma 7 (BCC7)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:614740

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi15S → A: Loss of interaction with PPP2R5C, PPP2CA AND PPP2R1A. 1 Publication1
Mutagenesisi18T → A: No effect on interaction with MDM2 and increase in protein levels after DNA damage. 1 Publication1
Mutagenesisi20S → A: Abolishes phosphorylation site. Abolishes increase in protein levels after DNA damage. 1 Publication1
Mutagenesisi20S → D: Constitutively increased TP53 protein levels. 1 Publication1
Mutagenesisi22 – 23LW → QS: Loss of interaction with MDM2, leading to constitutively increased TP53 protein levels. 1 Publication2
Mutagenesisi37S → D: Abolihes phosphorylation by MAPKAPK5. 1 Publication1
Mutagenesisi46S → A: Abolishes phosphorylation by DYRK2 and HIPK2 and acetylation of K-382 by CREBBP. 3 Publications1
Mutagenesisi46Missing : Alters interaction with WWOX. 3 Publications1
Mutagenesisi55T → A: Blocks phosphorylation by TAF1. 1 Publication1
Mutagenesisi183S → A: Abolishes strongly phosphorylation. 1 Publication1
Mutagenesisi183S → E: Inhibits slightly its transcriptional activity. 1 Publication1
Mutagenesisi248R → S: Does not induce SNAI1 degradation. 1 Publication1
Mutagenesisi269S → A: Abolishes phosphorylation. 1 Publication1
Mutagenesisi269S → E: Inhibits strongly its transcriptional activity. 1 Publication1
Mutagenesisi284T → E: Inhibits strongly its transcriptional activity. 1
Mutagenesisi291 – 292KK → RR: Abolishes polyubiquitination by MKRN1. 1 Publication2
Mutagenesisi319K → A: Loss of nuclear localization; when associated with A-320 and A-321. 1 Publication1
Mutagenesisi320K → A: Loss of nuclear localization; when associated with A-319 and A-321. 1 Publication1
Mutagenesisi321K → A: Loss of nuclear localization; when associated with A-319 and A-320. 1 Publication1
Mutagenesisi359P → D: Abolishes binding to USP7. 1 Publication1
Mutagenesisi361G → E: Abolishes binding to USP7. 1 Publication1
Mutagenesisi362S → A: Abolishes binding to USP7. 1 Publication1
Mutagenesisi370K → R: Induces a decrease in methylation by SMYD2. 1 Publication1
Mutagenesisi372K → R: Induces a decrease in protein stabilization. 1 Publication1
Mutagenesisi373K → R: Abolishes dimethylation by EHMT1 and EHMT2. 1 Publication1
Mutagenesisi382K → A: Abolishes acetylation by CREBBP. 4 Publications1
Mutagenesisi382K → R: Abolishes monomethylation by KMT5A. 4 Publications1
Mutagenesisi383L → A: Abolishes S-315 phosphorylation by CDK2/cyclin A. 1 Publication1
Mutagenesisi385F → A: Reduced SUMO1 conjugation. 2 Publications1
Mutagenesisi386K → A: Abolishes SUMO1 conjugation, in vitro and in vivo. 2 Publications1
Mutagenesisi387T → A: No effect SUMO1 conjugation. 1 Publication1
Mutagenesisi388E → A: Abolishes SUMO1 conjugation. 1 Publication1

Keywords - Diseasei

Disease mutation, Li-Fraumeni syndrome, Tumor suppressor

Organism-specific databases

DisGeNETi7157.
MalaCardsiTP53.
MIMi133239. phenotype.
151623. phenotype.
191170. gene+phenotype.
202300. phenotype.
211980. phenotype.
260500. phenotype.
275355. phenotype.
614740. phenotype.
OpenTargetsiENSG00000141510.
Orphaneti1501. Adrenocortical carcinoma.
67038. B-cell chronic lymphocytic leukemia.
3318. Essential thrombocythemia.
1333. Familial pancreatic carcinoma.
251579. Giant cell glioblastoma.
251576. Gliosarcoma.
524. Li-Fraumeni syndrome.
2807. Papilloma of choroid plexus.
99860. Precursor B-cell acute lymphoblastic leukemia.
PharmGKBiPA36679.

Chemistry databases

ChEMBLiCHEMBL4096.
DrugBankiDB00945. Acetylsalicylic acid.

Polymorphism and mutation databases

BioMutaiTP53.
DMDMi269849759.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001857031 – 393Cellular tumor antigen p53Add BLAST393

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei9Phosphoserine; by HIPK41 Publication1
Modified residuei15Phosphoserine; by CDK5, PRPK, AMPK, NUAK1 and ATM8 Publications1
Modified residuei18Phosphothreonine; by CK1, VRK1 and VRK23 Publications1
Modified residuei20Phosphoserine; by CHEK2, CK1 and PLK35 Publications1
Modified residuei33Phosphoserine; by CDK5 and CDK72 Publications1
Modified residuei37Phosphoserine; by MAPKAPK51 Publication1
Modified residuei46Phosphoserine; by CDK5, DYRK2, HIPK2 and PKC/PRKCG5 Publications1
Modified residuei55Phosphothreonine; by TAF1 and GRK52 Publications1
Modified residuei120N6-acetyllysine; by KAT6A1 Publication1
Modified residuei183Phosphoserine; by AURKB1 Publication1
Modified residuei269Phosphoserine; by AURKB1 Publication1
Modified residuei284Phosphothreonine; by AURKB1 Publication1
Cross-linki291Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki292Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei305N6-acetyllysine1 Publication1
Modified residuei315Phosphoserine; by AURKA, CDK1 and CDK22 Publications1
Modified residuei321N6-acetyllysineBy similarity1
Modified residuei370N6,N6-dimethyllysine; alternate2 Publications1
Modified residuei370N6-methyllysine; by SMYD2; alternate2 Publications1
Modified residuei372N6-methyllysine; by SETD72 Publications1
Modified residuei373N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternate1 Publication1
Modified residuei373N6-acetyllysine; alternate1 Publication1
Modified residuei381N6-acetyllysineCombined sources1
Modified residuei382N6,N6-dimethyllysine; alternate3 Publications1
Modified residuei382N6-acetyllysine; by KAT6A; alternateCombined sources3 Publications1
Modified residuei382N6-methyllysine; by KMT5A; alternate3 Publications1
Cross-linki386Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)3 Publications
Modified residuei392Phosphoserine; by CK2, CDK2 and NUAK15 Publications1

Post-translational modificationi

Acetylated. Acetylation of Lys-382 by CREBBP enhances transcriptional activity. Deacetylation of Lys-382 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.3 Publications
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. 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 on Ser-15 upon ultraviolet irradiation; which is enhanced by interaction with BANP. Phosphorylated by NUAK1 at Ser-15 and Ser-392; was intially 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.By similarity32 Publications
Dephosphorylated by PP2A-PPP2R5C holoenzyme at Thr-55. SV40 small T antigen inhibits the dephosphorylation by the AC form of PP2A.
May be O-glycosylated in the C-terminal basic region. Studied in EB-1 cell line.1 Publication
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-291 and Lys-292, which leads to proteasomal degradation. Deubiquitinated by USP10, leading to its stabilization. Ubiquitinated by TRIM24, RFFL and RNF34, which leads to proteasomal degradation. Ubiquitination by TOPORS induces degradation. Deubiquitination by USP7, leading to stabilization. Isoform 4 is monoubiquitinated in an MDM2-independent manner. Ubiquitinated by RFWD2, which leads to proteasomal degradation. Ubiquitination and subsequent proteasomal degradation is negatively regulated by CCAR2.3 Publications
Monomethylated at Lys-372 by SETD7, leading to stabilization and increased transcriptional activation. Monomethylated at Lys-370 by SMYD2, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity. Lys-372 monomethylation prevents interaction with SMYD2 and subsequent monomethylation at Lys-370. Dimethylated at Lys-373 by EHMT1 and EHMT2. Monomethylated at Lys-382 by KMT5A, promoting interaction with L3MBTL1 and leading to repress transcriptional activity. Dimethylation at Lys-370 and Lys-382 diminishes p53 ubiquitination, through stabilizing association with the methyl reader PHF20. Demethylation of dimethylated Lys-370 by KDM1A prevents interaction with TP53BP1 and represses TP53-mediated transcriptional activation.
Sumoylated with SUMO1. Sumoylated at Lys-386 by UBC9.3 Publications

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP04637.
MaxQBiP04637.
PaxDbiP04637.
PeptideAtlasiP04637.
PRIDEiP04637.

2D gel databases

SWISS-2DPAGEP04637.

PTM databases

iPTMnetiP04637.
PhosphoSitePlusiP04637.

Miscellaneous databases

PMAP-CutDBP04637.

Expressioni

Tissue specificityi

Ubiquitous. Isoforms are expressed in a wide range of normal tissues but in a tissue-dependent manner. Isoform 2 is expressed in most normal tissues but is not detected in brain, lung, prostate, muscle, fetal brain, spinal cord and fetal liver. Isoform 3 is expressed in most normal tissues but is not detected in lung, spleen, testis, fetal brain, spinal cord and fetal liver. Isoform 7 is expressed in most normal tissues but is not detected in prostate, uterus, skeletal muscle and breast. Isoform 8 is detected only in colon, bone marrow, testis, fetal brain and intestine. Isoform 9 is expressed in most normal tissues but is not detected in brain, heart, lung, fetal liver, salivary gland, breast or intestine.1 Publication

Inductioni

Up-regulated in response to DNA damage. Isoform 2 is not induced in tumor cells in response to stress.2 Publications

Gene expression databases

BgeeiENSG00000141510.
ExpressionAtlasiP04637. baseline and differential.
GenevisibleiP04637. HS.

Organism-specific databases

HPAiCAB002973.
CAB039238.
CAB039239.
CAB072876.
HPA051244.

Interactioni

Subunit structurei

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 TP53INP1. 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, UHRF2 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 ubiquitination 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. Interacts with AURKB, SETD2, UHRF2 and NOC2L. Interacts (via N-terminus) with PTK2/FAK1; this promotes ubiquitination by MDM2. Interacts with PTK2B/PYK2; this promotes ubiquitination by MDM2. Interacts with PRKCG. Interacts with PPIF; the association implicates preferentially tetrameric TP53, is induced by oxidative stress and is impaired by cyclosporin A (CsA). Interacts with human cytomegalovirus/HHV-5 protein UL123. Interacts with SNAI1; the interaction induces SNAI1 degradation via MDM2-mediated ubiquitination and inhibits SNAI1-induced cell invasion. Interacts with KAT6A. Interacts with UBC9. Interacts with ZNF385B; the interaction is direct. Interacts (via DNA-binding domain) with ZNF385A; the interaction is direct and enhances p53/TP53 transactivation functions on cell-cycle arrest target genes, resulting in growth arrest. Interacts with ANKRD2. Interacts with RFFL and RNF34; involved in p53/TP53 ubiquitination. Interacts with MTA1 and RFWD2. Interacts with CCAR2 (via N-terminus). Interacts (via N-terminus) with human adenovirus 5 E1B-55K protein; this interaction leads to the inhibition of TP53 function and/or its degradation (PubMed:25772236). Interacts with MORC3 (PubMed:17332504).By similarity69 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei120Interaction with DNA1

Binary interactionsi

WithEntry#Exp.IntActNotes
itself11EBI-366083,EBI-366083
P0307019EBI-366083,EBI-617698From a different organism.
P266639EBI-366083,EBI-6838571From a different organism.
Q7L7W22EBI-366083,EBI-7210801
Q8QW272EBI-366083,EBI-6863726From a different organism.
ARIH2O953765EBI-366083,EBI-711158
ASH2LQ9UBL35EBI-366083,EBI-540797
AXIN1O151694EBI-366083,EBI-710484
BANPQ8N9N53EBI-366083,EBI-744695
BCL2P104155EBI-366083,EBI-77694
BCL2L1Q07817-118EBI-366083,EBI-287195
BCRP112742EBI-366083,EBI-712838
BHLHE40O145035EBI-366083,EBI-711810
BRD7Q9NPI18EBI-366083,EBI-711221
BTBD2Q9BX702EBI-366083,EBI-710091
Cables1Q9ESJ13EBI-366083,EBI-604411From a different organism.
CCDC106Q9BWC93EBI-366083,EBI-711501
CDKN1AP389363EBI-366083,EBI-375077
CEBPBP176764EBI-366083,EBI-969696
CREBBPQ927939EBI-366083,EBI-81215
CrebbpP454816EBI-366083,EBI-296306From a different organism.
CSE1LP550605EBI-366083,EBI-286709
CSNK2A1P684002EBI-366083,EBI-347804
CUL7Q149995EBI-366083,EBI-308606
CUL9Q8IWT34EBI-366083,EBI-311123
CXXC1Q9P0U47EBI-366083,EBI-949911
DAXXQ9UER712EBI-366083,EBI-77321
DDX17Q928413EBI-366083,EBI-746012
DDX5P178446EBI-366083,EBI-351962
DUSP26Q9BV479EBI-366083,EBI-2924519
DVL2O146414EBI-366083,EBI-740850
E6P031263EBI-366083,EBI-1177242From a different organism.
E6P064633EBI-366083,EBI-1186926From a different organism.
EP300Q0947210EBI-366083,EBI-447295
FBXO11Q86XK24EBI-366083,EBI-1047804
FOXO3O435242EBI-366083,EBI-1644164
GSK3BP498413EBI-366083,EBI-373586
GTF2H1P327805EBI-366083,EBI-715539
HDAC1Q135477EBI-366083,EBI-301834
HIPK1Q86Z022EBI-366083,EBI-692891
HNRNPKP619782EBI-366083,EBI-304185
HNRNPKP61978-22EBI-366083,EBI-7060731
HSPA1LP349312EBI-366083,EBI-354912
HSPA9P386466EBI-366083,EBI-354932
HSPB1P047923EBI-366083,EBI-352682
HTTP428584EBI-366083,EBI-466029
HUWE1Q7Z6Z73EBI-366083,EBI-625934
IFI16Q16666-23EBI-366083,EBI-6273540
Ifi205bQ086192EBI-366083,EBI-8064290From a different organism.
KAT5Q929933EBI-366083,EBI-399080
KAT8Q9H7Z62EBI-366083,EBI-896414
KMT2EQ8IZD24EBI-366083,EBI-2689959
LAMA4Q163632EBI-366083,EBI-711505
MAGEA2BP433566EBI-366083,EBI-5650739
MAGEC2Q9UBF13EBI-366083,EBI-5651487
MAP1BP468216EBI-366083,EBI-764611
MAPK11Q157592EBI-366083,EBI-298304
MAPKAPK5Q8IW412EBI-366083,EBI-1201460
MDM2Q0098765EBI-366083,EBI-389668
MDM4O1515114EBI-366083,EBI-398437
MKRN1Q9UHC78EBI-366083,EBI-373524
MPDZO759703EBI-366083,EBI-821405
MT1AP047313EBI-366083,EBI-8045030
NCLP193382EBI-366083,EBI-346967
NCOR2Q9Y6187EBI-366083,EBI-80830
NFYAP2351111EBI-366083,EBI-389739
NFYBP252086EBI-366083,EBI-389728
NOC2LQ9Y3T98EBI-366083,EBI-751547
NPM1P067486EBI-366083,EBI-78579
NPM1P06748-13EBI-366083,EBI-354150
NR0B2Q154663EBI-366083,EBI-3910729
NR4A1P227366EBI-366083,EBI-721550
NRDCO438476EBI-366083,EBI-2371631
NSP1P890556EBI-366083,EBI-9522973From a different organism.
NUAK1O602855EBI-366083,EBI-1046789
OTUB1Q96FW18EBI-366083,EBI-1058491
PARD3Q8TEW03EBI-366083,EBI-81968
PARP1P098743EBI-366083,EBI-355676
PBKQ96KB57EBI-366083,EBI-536853
PIAS1O759254EBI-366083,EBI-629434
PIAS2O759282EBI-366083,EBI-348555
PIAS4Q8N2W92EBI-366083,EBI-473160
PIN1Q1352612EBI-366083,EBI-714158
PLK1P533506EBI-366083,EBI-476768
PMLP295904EBI-366083,EBI-295890
PPIFP304054EBI-366083,EBI-5544229
PPP1CCP36873-12EBI-366083,EBI-356289
PPP1R13LQ8WUF511EBI-366083,EBI-5550163
PPP2R1AP301533EBI-366083,EBI-302388
PPP2R5CQ133624EBI-366083,EBI-1266156
PRKCDQ056554EBI-366083,EBI-704279
PSME3P612897EBI-366083,EBI-355546
PTK2Q0539713EBI-366083,EBI-702142
RAD51Q066092EBI-366083,EBI-297202
RCHY1Q96PM57EBI-366083,EBI-947779
RPS3P233964EBI-366083,EBI-351193
RYBPQ8N4883EBI-366083,EBI-752324
S100A1P232972EBI-366083,EBI-743686
S100A2P290342EBI-366083,EBI-752230
S100A4P264477EBI-366083,EBI-717058
S100BP042712EBI-366083,EBI-458391
SAFBQ154245EBI-366083,EBI-348298
SETD7Q8WTS66EBI-366083,EBI-1268586
SFNP319474EBI-366083,EBI-476295
SIN3AQ96ST32EBI-366083,EBI-347218
SIRT1Q96EB613EBI-366083,EBI-1802965
Sirt1Q923E44EBI-366083,EBI-1802585From a different organism.
SMAD2Q157967EBI-366083,EBI-1040141
SNAI1O958632EBI-366083,EBI-1045459
SREBF2Q127723EBI-366083,EBI-465059
SRPK1Q96SB43EBI-366083,EBI-539478
SYVN1Q86TM65EBI-366083,EBI-947849
TBPP202262EBI-366083,EBI-355371
TCF4P158842EBI-366083,EBI-533224
TOE1Q96GM83EBI-366083,EBI-717460
TP53BP1Q128882EBI-366083,EBI-396540
TP53BP2Q136255EBI-366083,EBI-77642
TP63Q9H3D45EBI-366083,EBI-2337775
Tp63O888982EBI-366083,EBI-2338025From a different organism.
TPT1P136935EBI-366083,EBI-1783169
TWIST1Q1567210EBI-366083,EBI-1797287
Twist1P266874EBI-366083,EBI-6123119From a different organism.
UBCP0CG4815EBI-366083,EBI-3390054
UBE3AQ050863EBI-366083,EBI-954357
UHRF2Q96PU43EBI-366083,EBI-625304
USP42Q9H9J42EBI-366083,EBI-2513638
USP42Q9H9J4-22EBI-366083,EBI-9118105
USP7Q9300917EBI-366083,EBI-302474
VDRP114736EBI-366083,EBI-286357
VRK1Q999869EBI-366083,EBI-1769146
WRNQ141915EBI-366083,EBI-368417
XRCC6P129562EBI-366083,EBI-353208
YWHAGP619815EBI-366083,EBI-359832
YWHAZP631042EBI-366083,EBI-347088
ZNF420Q8TAQ54EBI-366083,EBI-3923307
znf585bQ9PST73EBI-366083,EBI-1782562From a different organism.

GO - Molecular functioni

  • chaperone binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • histone acetyltransferase binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • p53 binding Source: GO_Central
  • protease binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • protein phosphatase 2A binding Source: UniProtKB
  • protein phosphatase binding Source: UniProtKB
  • protein self-association Source: AgBase
  • receptor tyrosine kinase binding Source: BHF-UCL
  • RNA polymerase II transcription factor binding Source: BHF-UCL
  • transcription factor binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113010. 995 interactors.
DIPiDIP-368N.
IntActiP04637. 416 interactors.
MINTiMINT-91013.
STRINGi9606.ENSP00000269305.

Chemistry databases

BindingDBiP04637.

Structurei

Secondary structure

1393
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 6Combined sources4
Turni8 – 10Combined sources3
Helixi19 – 23Combined sources5
Beta strandi27 – 29Combined sources3
Helixi30 – 32Combined sources3
Beta strandi33 – 35Combined sources3
Helixi36 – 38Combined sources3
Helixi41 – 44Combined sources4
Helixi47 – 55Combined sources9
Turni105 – 108Combined sources4
Beta strandi110 – 112Combined sources3
Beta strandi119 – 121Combined sources3
Beta strandi124 – 127Combined sources4
Turni128 – 131Combined sources4
Beta strandi132 – 135Combined sources4
Beta strandi141 – 146Combined sources6
Beta strandi156 – 165Combined sources10
Helixi166 – 168Combined sources3
Helixi177 – 180Combined sources4
Beta strandi181 – 183Combined sources3
Beta strandi187 – 189Combined sources3
Beta strandi194 – 199Combined sources6
Beta strandi204 – 207Combined sources