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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 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-ARNTL/BMAL1-mediated transcriptional activation of PER2 (PubMed:24051492).12 Publications

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi176Zinc1
Metal bindingi179Zinc1
Metal bindingi238Zinc1
Metal bindingi242Zinc1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi102 – 292Add BLAST191

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, DNA-binding, Repressor
Biological processApoptosis, Biological rhythms, Cell cycle, Host-virus interaction, Necrosis, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-111448 Activation of NOXA and translocation to mitochondria
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-6785807 Interleukin-4 and Interleukin-13 signaling
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-8941855 RUNX3 regulates CDKN1A transcription
R-HSA-8943724 Regulation of PTEN gene transcription
R-HSA-983231 Factors involved in megakaryocyte development and platelet production

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
P04637

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P04637

SIGNOR Signaling Network Open Resource

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SIGNORi
P04637

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P04637 Predicted

Transport Classification Database

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

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cellular tumor antigen p53
Alternative name(s):
Antigen NY-CO-13
Phosphoprotein p53
Tumor suppressor p53
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:TP53
Synonyms:P53
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 17

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000141510.16

Human Gene Nomenclature Database

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HGNCi
HGNC:11998 TP53

Online Mendelian Inheritance in Man (OMIM)

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MIMi
191170 gene+phenotype

neXtProt; the human protein knowledge platform

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neXtProti
NX_P04637

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Mitochondrion, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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 descriptionAn 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.
See also OMIM:151623
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_04462182P → L in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs534447939EnsemblClinVar.1
Natural variantiVAR_044661105G → C in 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 dbSNP:rs747342068EnsemblClinVar.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 dbSNP:rs28934873EnsemblClinVar.1
Natural variantiVAR_005881138A → P in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs28934875EnsemblClinVar.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 dbSNP:rs587781288EnsemblClinVar.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 dbSNP:rs28934874EnsemblClinVar.1
Natural variantiVAR_005896151P → T in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs28934874EnsemblClinVar.1
Natural variantiVAR_005897152P → L in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs587782705EnsemblClinVar.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 dbSNP:rs371524413EnsemblClinVar.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 dbSNP:rs587782144EnsemblClinVar.1
Natural variantiVAR_033035163Y → C in LFS; germline mutation and in sporadic cancers; somatic mutation. 2 PublicationsCorresponds to variant dbSNP:rs148924904EnsemblClinVar.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. Corresponds to variant dbSNP:rs1131691043Ensembl.1
Natural variantiVAR_005926173V → M in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs876660754EnsemblClinVar.1
Natural variantiVAR_044911174R → G in LFS; germline mutation and in a sporadic cancer; somatic mutation. Corresponds to variant dbSNP:rs864622115EnsemblClinVar.1
Natural variantiVAR_005929175R → G in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs138729528EnsemblClinVar.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 dbSNP:rs28934578EnsemblClinVar.1
Natural variantiVAR_005930175R → L in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs28934578EnsemblClinVar.1
Natural variantiVAR_044939179H → Y in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs587780070EnsemblClinVar.1
Natural variantiVAR_044943180E → K in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs879253911EnsemblClinVar.1
Natural variantiVAR_044946181R → C in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs587782596EnsemblClinVar.1
Natural variantiVAR_044948181R → H in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs397514495EnsemblClinVar.1
Natural variantiVAR_005948193H → R in LFS; germline mutation and in sporadic cancers; somatic mutation. 2 PublicationsCorresponds to variant dbSNP:rs786201838EnsemblClinVar.1
Natural variantiVAR_045007196R → P in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs483352697EnsemblClinVar.1
Natural variantiVAR_045013197V → M in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs786204041EnsemblClinVar.1
Natural variantiVAR_036506213R → P in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs587778720EnsemblClinVar.1
Natural variantiVAR_005955213R → Q in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs587778720EnsemblClinVar.1
Natural variantiVAR_005957220Y → C in LFS; germline mutation and in sporadic cancers; somatic mutation. 2 PublicationsCorresponds to variant dbSNP:rs121912666EnsemblClinVar.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 dbSNP:rs587780073EnsemblClinVar.1
Natural variantiVAR_045186235N → S in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs144340710EnsemblClinVar.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 dbSNP:rs587782664EnsemblClinVar.1
Natural variantiVAR_045200238C → G in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs1057519981Ensembl.1
Natural variantiVAR_045202238C → S in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_005969241S → F in LFS; germline mutation and in sporadic cancers; somatic mutation. 2 PublicationsCorresponds to variant dbSNP:rs28934573EnsemblClinVar.1
Natural variantiVAR_047183241S → T in LFS; germline mutation and in sporadic cancers; somatic mutation. 1
Natural variantiVAR_045232244G → D in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs1057517983Ensembl.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 dbSNP:rs28934575EnsemblClinVar.1
Natural variantiVAR_005973245G → D in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121912656EnsemblClinVar.1
Natural variantiVAR_005974245G → S in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs28934575EnsemblClinVar.1
Natural variantiVAR_005975245G → V in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121912656EnsemblClinVar.1
Natural variantiVAR_005978246M → V in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs483352695EnsemblClinVar.1
Natural variantiVAR_005983248R → Q in LFS; germline mutation and in sporadic cancers; somatic mutation. 4 PublicationsCorresponds to variant dbSNP:rs11540652EnsemblClinVar.1
Natural variantiVAR_005984248R → W in LFS; germline mutation and in sporadic cancers; somatic mutation. 3 PublicationsCorresponds to variant dbSNP:rs121912651EnsemblClinVar.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 dbSNP:rs121912653EnsemblClinVar.1
Natural variantiVAR_045284257L → Q in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs28934577EnsemblClinVar.1
Natural variantiVAR_005991258E → K in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121912652EnsemblClinVar.1
Natural variantiVAR_045321265L → P in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs879253942EnsemblClinVar.1
Natural variantiVAR_045330267R → Q in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs587780075EnsemblClinVar.1
Natural variantiVAR_005992272V → L in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121912657EnsemblClinVar.1
Natural variantiVAR_005993273R → C in LFS; germline mutation and in sporadic cancers; somatic mutation. 4 PublicationsCorresponds to variant dbSNP:rs121913343EnsemblClinVar.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 dbSNP:rs28934576EnsemblClinVar.1
Natural variantiVAR_036509273R → L in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs28934576EnsemblClinVar.1
Natural variantiVAR_005998275C → Y in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs863224451EnsemblClinVar.1
Natural variantiVAR_006003278P → L in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs876659802EnsemblClinVar.1
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_047202281D → N in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs764146326Ensembl.1
Natural variantiVAR_045384282R → G in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs28934574EnsemblClinVar.1
Natural variantiVAR_006016282R → W in LFS; germline mutation and in sporadic cancers; somatic mutation; does not induce SNAI1 degradation. 2 PublicationsCorresponds to variant dbSNP:rs28934574EnsemblClinVar.1
Natural variantiVAR_006017283R → C in LFS; germline mutation and in sporadic cancers; somatic mutation. Corresponds to variant dbSNP:rs149633775EnsemblClinVar.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 dbSNP:rs55819519EnsemblClinVar.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 dbSNP:rs121912663EnsemblClinVar.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 dbSNP:rs121912659EnsemblClinVar.1
Natural variantiVAR_006041337R → C in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs587782529EnsemblClinVar.1
Natural variantiVAR_035016337R → H in LFS; germline mutation and in sporadic cancers; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121912664EnsemblClinVar.1
Natural variantiVAR_045546344L → P in LFS; germline mutation and in a sporadic cancer; somatic mutation. Corresponds to variant dbSNP:rs121912662EnsemblClinVar.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
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

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DisGeNETi
7157

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
TP53

MalaCards human disease database

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MalaCardsi
TP53
MIMi133239 phenotype
151623 phenotype
191170 gene+phenotype
202300 phenotype
211980 phenotype
260500 phenotype
275355 phenotype
614740 phenotype

Open Targets

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OpenTargetsi
ENSG00000141510

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
1501 Adrenocortical carcinoma
210159 Adult hepatocellular carcinoma
67038 B-cell chronic lymphocytic leukemia
251899 Choroid plexus carcinoma
3318 Essential thrombocythemia
1333 Familial pancreatic carcinoma
251579 Giant cell glioblastoma
251576 Gliosarcoma
145 Hereditary breast and ovarian cancer syndrome
524 Li-Fraumeni syndrome
668 Osteosarcoma
2807 Papilloma of choroid plexus
99860 Precursor B-cell acute lymphoblastic leukemia
70573 Small cell lung cancer

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA36679

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4096

Drug and drug target database

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DrugBanki
DB08363 1-(9-ethyl-9H-carbazol-3-yl)-N-methylmethanamine
DB00945 Acetylsalicylic acid
DB05404 AZD 3355

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
TP53

Domain mapping of disease mutations (DMDM)

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DMDMi
269849759

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001857031 – 393Cellular tumor antigen p53Add BLAST393

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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 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.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 (PubMed:10722742, PubMed:12810724, PubMed:15340061, PubMed:17170702, PubMed:19880522). 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).By similarity15 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

Encyclopedia of Proteome Dynamics

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EPDi
P04637

MaxQB - The MaxQuant DataBase

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MaxQBi
P04637

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P04637

PeptideAtlas

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PeptideAtlasi
P04637

PRoteomics IDEntifications database

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PRIDEi
P04637

ProteomicsDB human proteome resource

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ProteomicsDBi
51728
51729 [P04637-2]
51730 [P04637-3]
51731 [P04637-4]
51732 [P04637-5]
51733 [P04637-6]
51734 [P04637-7]
51735 [P04637-8]
51736 [P04637-9]

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P04637

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P04637

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P04637

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P04637

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000141510 Expressed in 170 organ(s), highest expression level in epithelium of mammary gland

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P04637 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P04637 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB002973
CAB039238
CAB039239
CAB072876
HPA051244

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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. 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 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 COP1. Interacts with CCAR2 (via N-terminus). Interacts with MORC3 (PubMed:17332504). Interacts (via C-terminus) with POU4F2 isoform 1 (via C-terminus) (PubMed:17145718). Interacts (via oligomerization region) with NOP53; the interaction is direct and may prevent the MDM2-mediated proteasomal degradation of TP53 (PubMed:22522597). Interacts with AFG1L; mediates mitochondrial translocation of TP53 (PubMed:27323408). Interacts with UBD (PubMed:25422469). Interacts with TAF6 isoform 1 and isoform 4 (PubMed:20096117). Interacts with C10orf90/FATS; the interaction inhibits binding of TP53 and MDM2 (By similarity).By similarity62 Publications
(Microbial infection) Interacts with cancer-associated/HPV E6 viral proteins leading 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 E6.1 Publication
(Microbial infection) Interacts with human cytomegalovirus/HHV-5 protein UL123.1 Publication
(Microbial infection) Interacts (via N-terminus) with human adenovirus 5 E1B-55K protein; this interaction leads to the inhibition of TP53 function and/or its degradation.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei120Interaction with DNA1

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
itself24EBI-366083,EBI-366083
P0307020EBI-366083,EBI-617698From Simian virus 40.
P266639EBI-366083,EBI-6838571From Hepatitis C virus genotype 1b (isolate BK).
Q7L7W22EBI-366083,EBI-7210801
Q8QW272EBI-366083,EBI-6863726From Hepatitis C virus subtype 1b.
AIMP2Q131556EBI-366083,EBI-745226
ARIH2O953765EBI-366083,EBI-711158
ARRB1P494075EBI-366083,EBI-743313
Arrb1P290663EBI-366083,EBI-4303019From Rattus norvegicus.
ASH2LQ9UBL37EBI-366083,EBI-540797
ATG7O95352-24EBI-366083,EBI-15980880
AXIN1O151694EBI-366083,EBI-710484
BANPQ8N9N53EBI-366083,EBI-744695
BCL2P104155EBI-366083,EBI-77694
BCL2L1Q07817-126EBI-366083,EBI-287195
BCRP112742EBI-366083,EBI-712838
BHLHE40O1450311EBI-366083,EBI-711810
BRCA2P515877EBI-366083,EBI-79792
BRD7Q9NPI19EBI-366083,EBI-711221
BTBD2Q9BX702EBI-366083,EBI-710091
BTRCQ9Y2972EBI-366083,EBI-307461
Cables1Q9ESJ13EBI-366083,EBI-604411From Mus musculus.
CCDC106Q9BWC93EBI-366083,EBI-711501
CDKN1AP389363EBI-366083,EBI-375077
CEBPBP176764EBI-366083,EBI-969696
CREBBPQ9279311EBI-366083,EBI-81215
CrebbpP454819EBI-366083,EBI-296306From Mus musculus.
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
DROSHAQ9NRR45EBI-366083,EBI-528367
DUSP26Q9BV479EBI-366083,EBI-2924519
DVL2O146414EBI-366083,EBI-740850
E6P031265EBI-366083,EBI-1177242From Human papillomavirus type 16.
E6P064633EBI-366083,EBI-1186926From Human papillomavirus type 18.
EP300Q0947220EBI-366083,EBI-447295
ETS2P150364EBI-366083,EBI-1646991
FBXO11Q86XK24EBI-366083,EBI-1047804
FOXO3O435242EBI-366083,EBI-1644164
GSK3BP498413EBI-366083,EBI-373586
GTF2H1P327805EBI-366083,EBI-715539
HDAC1Q135477EBI-366083,EBI-301834
HIPK1Q86Z022EBI-366083,EBI-692891
HMGB1P094299EBI-366083,EBI-389432
HNRNPKP619782EBI-366083,EBI-304185
HNRNPKP61978-22EBI-366083,EBI-7060731
HSP82P028298EBI-366083,EBI-8659From Saccharomyces cerevisiae (strain ATCC 204508 / S288c).
HSPA1LP349312EBI-366083,EBI-354912
HSPA9P386466EBI-366083,EBI-354932
HSPB1P047923EBI-366083,EBI-352682
HTTP428584EBI-366083,EBI-466029
HUWE1Q7Z6Z73EBI-366083,EBI-625934
IFI16Q16666-26EBI-366083,EBI-6273540
Ifi205bQ086192EBI-366083,EBI-8064290From a different organism.
IKBKBO149202EBI-366083,EBI-81266
IP6K2Q9UHH94EBI-366083,EBI-747509
JMJD6Q6NYC17EBI-366083,EBI-8464037
KAT5Q929933EBI-366083,EBI-399080
KAT8Q9H7Z62EBI-366083,EBI-896414
KDM1AO60341-16EBI-366083,EBI-15599570
KMT2EQ8IZD24EBI-366083,EBI-2689959
LAMA4Q163632EBI-366083,EBI-711505
MAGEA2BP433567EBI-366083,EBI-5650739
MAGEC2Q9UBF13EBI-366083,EBI-5651487
MAP1BP468216EBI-366083,EBI-764611
MAPK11Q157592EBI-366083,EBI-298304
MAPKAPK5Q8IW412EBI-366083,EBI-1201460
MDM2Q0098793EBI-366083,EBI-389668
MDM4O1515119EBI-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
NOL3O609363EBI-366083,EBI-740992
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 Rotavirus sp..
NUAK1O602855EBI-366083,EBI-1046789
NUMBP497575EBI-366083,EBI-915016
OTUB1Q96FW18EBI-366083,EBI-1058491
PARD3Q8TEW03EBI-366083,EBI-81968
PARP1P098743EBI-366083,EBI-355676
PBKQ96KB57EBI-366083,EBI-536853
PHBP352326EBI-366083,EBI-354213
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
PPP1R13LQ8WUF512EBI-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
RBPJQ063305EBI-366083,EBI-632552
RCHY1Q96PM511EBI-366083,EBI-947779
RFWD3Q6PCD55EBI-366083,EBI-2129159
RING1Q065877EBI-366083,EBI-752313
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
SETD7Q8WTS611EBI-366083,EBI-1268586
SFNP319474EBI-366083,EBI-476295
SIN3AQ96ST32EBI-366083,EBI-347218
SIRT1Q96EB618EBI-366083,EBI-1802965
Sirt1Q923E44EBI-366083,EBI-1802585From Mus musculus.
SMAD2Q157967EBI-366083,EBI-1040141
SMYD2Q9NRG46EBI-366083,EBI-1055671
Smyd2Q8R5A03EBI-366083,EBI-15612527From Mus musculus.
SNAI1O958632EBI-366083,EBI-1045459
SOX4Q069454EBI-366083,EBI-6672525
SP1P080473EBI-366083,EBI-298336
SREBF2Q127723EBI-366083,EBI-465059
SRPK1Q96SB43EBI-366083,EBI-539478
SUMO1P631653EBI-366083,EBI-80140
SYVN1Q86TM65EBI-366083,EBI-947849
TBPP202262EBI-366083,EBI-355371
TCF4P158842EBI-366083,EBI-533224
TOE1Q96GM83EBI-366083,EBI-717460
TP53BP1Q128886EBI-366083,EBI-396540
TP53BP1Q12888-117EBI-366083,EBI-8022649
TP53BP2Q136257EBI-366083,EBI-77642
TP63Q9H3D45EBI-366083,EBI-2337775
Tp63O888982EBI-366083,EBI-2338025From Mus musculus.
TPT1P136937EBI-366083,EBI-1783169
TRIM24O151643EBI-366083,EBI-2130378
TWIST1Q1567210EBI-366083,EBI-1797287
Twist1P266874EBI-366083,EBI-6123119From Mus musculus.
UBCP0CG4815EBI-366083,EBI-3390054
UBE3AQ050866EBI-366083,EBI-954357
UHRF2Q96PU43EBI-366083,EBI-625304
USP42Q9H9J42EBI-366083,EBI-2513638
USP42Q9H9J4-22EBI-366083,EBI-9118105
USP7Q9300918EBI-366083,EBI-302474
VDRP114736EBI-366083,EBI-286357
VRK1Q9998611EBI-366083,EBI-1769146
WRNQ141915EBI-366083,EBI-368417
XPO1O149803EBI-366083,EBI-355867
XRCC6P129562EBI-366083,EBI-353208
YWHAGP619815EBI-366083,EBI-359832
YWHAZP631042EBI-366083,EBI-347088
ZNF420Q8TAQ54EBI-366083,EBI-3923307
znf585bQ9PST73EBI-366083,EBI-1782562From Xenopus laevis.

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
113010, 1079 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P04637

Database of interacting proteins

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DIPi
DIP-368N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P04637

Protein interaction database and analysis system

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IntActi
P04637, 468 interactors

Molecular INTeraction database

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MINTi
P04637

STRING: functional protein association networks

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STRINGi
9606.ENSP00000269305

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P04637

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1393
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Database of protein disorder

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DisProti
DP00086

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P04637

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P04637

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P04637

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 320Interaction with CCAR21 PublicationAdd BLAST320
Regioni1 – 83Interaction with HRMT1L21 PublicationAdd BLAST83
Regioni1 – 44Transcription activation (acidic)Add BLAST44
Regioni66 – 110Interaction with WWOXAdd BLAST45
Regioni100 – 370Interaction with HIPK1By similarityAdd BLAST271
Regioni100 – 300Required for interaction with ZNF385A1 PublicationAdd BLAST201
Regioni113 – 236Required for interaction with FBXO421 PublicationAdd BLAST124
Regioni116 – 292Interaction with AXIN1By similarityAdd BLAST177
Regioni241 – 248Interaction with the 53BP2 SH3 domain8
Regioni256 – 294Interaction with E4F11 PublicationAdd BLAST39
Regioni273 – 280Interaction with DNA8
Regioni300 – 393Interaction with CARM11 Publication