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UniProtKB - P10361 (P53_RAT)

Entry version 228 (23 Feb 2022)
Sequence version 1 (01 Jul 1989)
Previous versions | rss
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Protein

Cellular tumor antigen p53

Gene

Tp53

Organism
Rattus norvegicus (Rat)
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. Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (By similarity).

However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (By similarity).

In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Regulates the circadian clock by repressing CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER2.

By similarity

<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+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi174ZincBy similarity1
Metal bindingi177ZincBy similarity1
Metal bindingi236ZincBy similarity1
Metal bindingi240ZincBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi100 – 290By similarityAdd 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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, Necrosis, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-2559580, Oxidative Stress Induced Senescence
R-RNO-2559584, Formation of Senescence-Associated Heterochromatin Foci (SAHF)
R-RNO-2559585, Oncogene Induced Senescence
R-RNO-2559586, DNA Damage/Telomere Stress Induced Senescence
R-RNO-349425, Autodegradation of the E3 ubiquitin ligase COP1
R-RNO-5689880, Ub-specific processing proteases
R-RNO-5689896, Ovarian tumor domain proteases
R-RNO-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-RNO-6804754, Regulation of TP53 Expression
R-RNO-6804756, Regulation of TP53 Activity through Phosphorylation
R-RNO-6804757, Regulation of TP53 Degradation
R-RNO-6804758, Regulation of TP53 Activity through Acetylation
R-RNO-6804759, Regulation of TP53 Activity through Association with Co-factors
R-RNO-6804760, Regulation of TP53 Activity through Methylation
R-RNO-69473, G2/M DNA damage checkpoint
R-RNO-69481, G2/M Checkpoints
R-RNO-69541, Stabilization of p53
R-RNO-69895, Transcriptional activation of cell cycle inhibitor p21
R-RNO-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint
R-RNO-8941855, RUNX3 regulates CDKN1A transcription

<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%5Fand%5Ftaxonomy%5Fsection">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):
Tumor suppressor p53
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 10

Organism-specific databases

Rat genome database

More...RGDi		3889, Tp53

<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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, 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

p53 is found in increased amounts in a wide variety of transformed cells. p53 is frequently mutated or inactivated in many types of cancer.

Keywords - Diseasei

Tumor suppressor

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001857121 – 391Cellular tumor antigen p53Add BLAST391

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 HIPK4By similarity1
Modified residuei15Phosphoserine; by CDK5, PRPK, AMPK, NUAK1 and ATMBy similarity1
Modified residuei18Phosphothreonine; by CK1, VRK1 and VRK2By similarity1
Modified residuei20Phosphoserine; by CHEK2, CK1 and PLK3By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki24Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei39Phosphoserine; by MAPKAPK5By similarity1
Modified residuei118N6-acetyllysine; by KAT6ABy similarity1
Modified residuei181Phosphoserine; by AURKBBy similarity1
Modified residuei267Phosphoserine; by AURKBBy similarity1
Modified residuei282Phosphothreonine; by AURKBBy similarity1
Cross-linki289Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki290Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei303N6-acetyllysineBy similarity1
Modified residuei313Phosphoserine; by AURKA, CDK1 and CDK2By similarity1
Modified residuei319N6-acetyllysineBy similarity1
Modified residuei331Omega-N-methylarginineBy similarity1
Modified residuei333Symmetric dimethylarginineBy similarity1
Modified residuei335Symmetric dimethylarginineBy similarity1
Modified residuei368N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei368N6-methyllysine; by SMYD2; alternateBy similarity1
Modified residuei370N6-methyllysine; by SETD7By similarity1
Modified residuei371N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternateBy similarity1
Modified residuei371N6-acetyllysine; alternateBy similarity1
Modified residuei379N6-acetyllysineBy similarity1
Modified residuei380N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei380N6-acetyllysine; by KAT6A; alternateBy similarity1
Modified residuei380N6-methyllysine; by KMT5A; alternateBy similarity1
Cross-linki384Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei390Phosphoserine; by CK2, CDK2 and NUAK1By similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Phosphorylation on Ser residues mediates transcriptional activation. Phosphorylation at Ser-9 by HIPK4 increases repression activity on BIRC5 promoter (By similarity). Phosphorylated on Thr-18 by VRK1, which may prevent the interaction with MDM2. Phosphorylated on Ser-20 by CHEK2 in response to DNA damage, which prevents ubiquitination by MDM2. Phosphorylated on Ser-20 by PLK3 in response to reactive oxygen species (ROS), promoting p53/TP53-mediated apoptosis. Probably phosphorylated on by CDK7 in a CAK complex in response to DNA damage. Phosphorylated by HIPK1. Phosphorylated on Ser-390 following UV but not gamma irradiation. Stabilized by CDK5-mediated phosphorylation in response to genotoxic and oxidative stresses at Ser-15, leading to accumulation of p53/TP53, particularly in the nucleus, thus inducing the transactivation of p53/TP53 target genes. Phosphorylated at Ser-313 and Ser-390 by CDK2 in response to DNA-damage (By similarity). Phosphorylation at Ser-15 is required for interaction with DDX3X and gamma-tubulin (By similarity).By similarity
Monomethylated at Lys-370 by SETD7, leading to stabilization and increased transcriptional activation. Monomethylated at Lys-368 by SMYD2, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity. Lys-370 monomethylation prevents interaction with SMYD2 and subsequent monomethylation at Lys-368. Dimethylated at Lys-371 by EHMT1 and EHMT2. Monomethylated at Lys-380 by KMT5A, promoting interaction with L3MBTL1 and leading to repress transcriptional activity. Demethylation of dimethylated Lys-368 by KDM1A prevents interaction with TP53BP1 and represses TP53-mediated transcriptional activation (By similarity). Monomethylated at Arg-331 and dimethylated at Arg-333 and Arg-335 by PRMT5; methylation is increased after DNA damage and might possibly affect TP53 target gene specificity (By similarity).By similarity
Sumoylated with SUMO1. Sumoylated at Lys-384 by UBC9 (By similarity).By similarity
Ubiquitinated by MDM2 and SYVN1, which leads to proteasomal degradation. Ubiquitinated by RFWD3, which works in cooperation with MDM2 and may catalyze the formation of short polyubiquitin chains on p53/TP53 that are not targeted to the proteasome. Ubiquitinated by MKRN1, which leads to proteasomal degradation. Deubiquitinated by USP10, leading to stabilize it. Ubiquitinated by TRIM24, RFFL, RNF34 and RNF125, which leads to proteasomal degradation. Ubiquitination by TOPORS induces degradation. Deubiquitination by USP7, leading to stabilize it. Ubiquitinated by COP1, which leads to proteasomal degradation (By similarity). Ubiquitination and subsequent proteasomal degradation is negatively regulated by CCAR2 (By similarity). Polyubiquitinated by C10orf90/FATS, polyubiquitination is 'Lys-48'-linkage independent and non-proteolytic, leading to TP53 stabilization (By similarity). Polyubiquitinated by MUL1 at Lys-24 which leads to proteasomal degradation (By similarity).By similarity
Acetylated. Acetylation by CREBBP enhances transcriptional activity. Acetylation by EP300. Deacetylation 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.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...PaxDbi		P10361

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P10361

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

More...PhosphoSitePlusi		P10361

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSRNOG00000010756, Expressed in thymus and 22 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P10361, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P10361, RN

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Forms homodimers and homotetramers (By similarity). Binds DNA as a homotetramer.

Interacts with AXIN1. Probably part of a complex consisting of TP53, HIPK2 and AXIN1 (By similarity).

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.

Interacts with USP7 and SYVN1.

Interacts with HSP90AB1 (PubMed:8663025).

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-380) with L3MBTL1.

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.

Interacts (via C-terminus) with POU4F2 (via C-terminus).

Interacts (via oligomerization region) with NOP53; the interaction is direct and may prevent the MDM2-mediated proteasomal degradation of TP53.

Interacts with AFG1L; mediates mitochondrial translocation of TP53.

Interacts with UBD (By similarity).

Interacts with TAF6 (By similarity). Binds DNA as a homotetramer.

Interacts with AXIN1. Probably part of a complex consisting of TP53, HIPK2 and AXIN1.

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.

Interacts with USP7 and SYVN1.

Interacts with HSP90AB1.

Interacts with CHD8; leading to recruit histone H1 and prevent transactivation activity.

Interacts with ARMC10, BANP, CDKN2AIP, NUAK1, STK11/LKB1, UHRF2 and E4F.

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-18 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-379) with L3MBTL1.

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 (By similarity).

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.

Interacts (via C-terminus) with POU4F2 (via C-terminus).

Interacts (via oligomerization region) with NOP53; the interaction is direct and may prevent the MDM2-mediated proteasomal degradation of TP53.

Interacts with AFG1L; mediates mitochondrial translocation of TP53.

Interacts with UBD (By similarity).

Interacts with TAF6 (By similarity).

Interacts with C10orf90/FATS; the interaction inhibits binding of TP53 and MDM2 (By similarity).

Interacts with NUPR1; interaction is stress-dependent.

Forms a complex with EP300 and NUPR1; this complex binds CDKN1A promoter leading to transcriptional induction of CDKN1A (By similarity).

Interacts with PRMT5 in response to DNA damage; the interaction is STRAP dependent (By similarity).

Interacts with PPP1R13L (via SH3 domain and ANK repeats); the interaction inhibits pro-apoptotic activity of p53/TP53 (By similarity).

Interacts with PPP1R13B/ASPP1 and TP53BP2/ASPP2; the interactions promotes pro-apoptotic activity (By similarity). When phosphorylated at Ser-15, interacts with DDX3X and gamma-tubulin (By similarity).

Interacts with KAT7/HBO1; leading to inhibit histone acetyltransferase activity of KAT7/HBO1 (By similarity).

Interacts (via N-terminus) with E3 ubiquitin-protein ligase MUL1; the interaction results in ubiquitination of cytoplasmic TP53 at Lys-24 and subsequent proteasomal degradation (By similarity).

Interacts with S100A4; this interaction promotes TP53 degradation (By similarity).

Interacts with TTC5/STRAP; the interaction may result in increased mitochondrial-dependent apoptosis (By similarity).

By similarity1 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>Sitei118Interaction with DNABy similarity1

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		246960, 11 interactors

Database of interacting proteins

More...DIPi		DIP-46016N

Protein interaction database and analysis system

More...IntActi		P10361, 5 interactors

Molecular INTeraction database

More...MINTi		P10361

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000047840

<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

3D structure databases

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

More...SMRi		P10361

Database of comparative protein structure models

More...ModBasei		Search...

<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 – 318Interaction with CCAR2By similarityAdd BLAST318
Regioni1 – 47Transcription activation (acidic)Add BLAST47
Regioni64 – 108Interaction with WWOXBy similarityAdd BLAST45
Regioni65 – 90DisorderedSequence analysisAdd BLAST26
Regioni98 – 368Interaction with HIPK1By similarityAdd BLAST271
Regioni98 – 298Required for interaction with ZNF385ABy similarityAdd BLAST201
Regioni111 – 234Required for interaction with FBXO42By similarityAdd BLAST124
Regioni114 – 290Interaction with AXIN1By similarityAdd BLAST177
Regioni254 – 292Interaction with E4F1By similarityAdd BLAST39
Regioni271 – 278Interaction with DNABy similarity8
Regioni281 – 324DisorderedSequence analysisAdd BLAST44
Regioni317 – 358Interaction with HIPK2By similarityAdd BLAST42
Regioni323 – 354OligomerizationAdd BLAST32
Regioni350 – 391DisorderedSequence analysisAdd BLAST42
Regioni357 – 361Interaction with USP7By similarity5
Regioni366 – 385Basic (repression of DNA-binding)Add BLAST20

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi303 – 319Bipartite nuclear localization signalBy similarityAdd BLAST17
Motifi337 – 348Nuclear export signalBy similarityAdd BLAST12
Motifi368 – 370[KR]-[STA]-K motif3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi281 – 298Basic and acidic residuesSequence analysisAdd BLAST18
Compositional biasi304 – 318Polar residuesSequence analysisAdd BLAST15
Compositional biasi350 – 366Basic and acidic residuesSequence analysisAdd BLAST17

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The [KR]-[STA]-K motif is specifically recognized by the SETD7 methyltransferase.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the p53 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502QVY3, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00950000183153

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_019621_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P10361

Identification of Orthologs from Complete Genome Data

More...OMAi		FHKKGEP

Database of Orthologous Groups

More...OrthoDBi		257530at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P10361

TreeFam database of animal gene trees

More...TreeFami		TF106101

Family and domain databases

Conserved Domains Database

More...CDDi		cd08367, P53, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.40.720, 1 hit
4.10.170.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR008967, p53-like_TF_DNA-bd
IPR012346, p53/RUNT-type_TF_DNA-bd_sf
IPR011615, p53_DNA-bd
IPR036674, p53_tetramer_sf
IPR010991, p53_tetrameristn
IPR013872, p53_transactivation_domain
IPR002117, p53_tumour_suppressor

The PANTHER Classification System

More...PANTHERi		PTHR11447, PTHR11447, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00870, P53, 1 hit
PF08563, P53_TAD, 1 hit
PF07710, P53_tetramer, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00386, P53SUPPRESSR

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47719, SSF47719, 1 hit
SSF49417, SSF49417, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00348, P53, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

P10361-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEDSQSDMSI ELPLSQETFS CLWKLLPPDD ILPTTATGSP NSMEDLFLPQ 
        60         70         80         90        100
DVAELLEGPE EALQVSAPAA QEPGTEAPAP VAPASATPWP LSSSVPSQKT 
       110        120        130        140        150
YQGNYGFHLG FLQSGTAKSV MCTYSISLNK LFCQLAKTCP VQLWVTSTPP 
       160        170        180        190        200
PGTRVRAMAI YKKSQHMTEV VRRCPHHERC SDGDGLAPPQ HLIRVEGNPY 
       210        220        230        240        250
AEYLDDRQTF RHSVVVPYEP PEVGSDYTTI HYKYMCNSSC MGGMNRRPIL 
       260        270        280        290        300
TIITLEDSSG NLLGRDSFEV RVCACPGRDR RTEEENFRKK EEHCPELPPG 
       310        320        330        340        350
SAKRALPTST SSSPQQKKKP LDGEYFTLKI RGRERFEMFR ELNEALELKD 
       360        370        380        390 
ARAAEESGDS RAHSSYPKTK KGQSTSRHKK PMIKKVGPDS D
Length:391
Mass (Da):43,451
Last modified:July 1, 1989 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE62522313A5C872F
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q9EQL0Q9EQL0_RAT
Cellular tumor antigen p53
Tp53 rCG_34931
271Annotation score:

Annotation score:3 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>
A0A0G2KBB2A0A0G2KBB2_RAT
Cellular tumor antigen p53
Tp53
170Annotation score:

Annotation score:2 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>
A0A0G2KB75A0A0G2KB75_RAT
Cellular tumor antigen p53
Tp53
170Annotation score:

Annotation score:2 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti174C → W in AAA41788 (PubMed:8441680).Curated1

Natural variant

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 varianti103G → S. 1
Natural varianti256E → G. 1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X13058 mRNA Translation: CAA31457.1
L07910 L07909 Genomic DNA Translation: AAA41788.1
U90328 mRNA Translation: AAB80959.1
BC081788 mRNA Translation: AAH81788.2
BC098663 mRNA Translation: AAH98663.1

Protein sequence database of the Protein Information Resource

More...PIRi		S02192

NCBI Reference Sequences

More...RefSeqi		NP_112251.2, NM_030989.3
XP_006246656.1, XM_006246594.3
XP_006246657.1, XM_006246595.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000046490; ENSRNOP00000047840; ENSRNOG00000010756
ENSRNOT00000085115; ENSRNOP00000074031; ENSRNOG00000010756

Database of genes from NCBI RefSeq genomes

More...GeneIDi		24842

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:24842

UCSC genome browser

More...UCSCi		RGD:3889, rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13058 mRNA Translation: CAA31457.1
L07910 L07909 Genomic DNA Translation: AAA41788.1
U90328 mRNA Translation: AAB80959.1
BC081788 mRNA Translation: AAH81788.2
BC098663 mRNA Translation: AAH98663.1
PIRiS02192
RefSeqiNP_112251.2, NM_030989.3
XP_006246656.1, XM_006246594.3
XP_006246657.1, XM_006246595.3

3D structure databases

SMRiP10361
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi246960, 11 interactors
DIPiDIP-46016N
IntActiP10361, 5 interactors
MINTiP10361
STRINGi10116.ENSRNOP00000047840

PTM databases

iPTMnetiP10361
PhosphoSitePlusiP10361

Proteomic databases

PaxDbiP10361

Genome annotation databases

EnsembliENSRNOT00000046490; ENSRNOP00000047840; ENSRNOG00000010756
ENSRNOT00000085115; ENSRNOP00000074031; ENSRNOG00000010756
GeneIDi24842
KEGGirno:24842
UCSCiRGD:3889, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7157
RGDi3889, Tp53

Phylogenomic databases

eggNOGiENOG502QVY3, Eukaryota
GeneTreeiENSGT00950000183153
HOGENOMiCLU_019621_0_0_1
InParanoidiP10361
OMAiFHKKGEP
OrthoDBi257530at2759
PhylomeDBiP10361
TreeFamiTF106101

Enzyme and pathway databases

ReactomeiR-RNO-2559580, Oxidative Stress Induced Senescence
R-RNO-2559584, Formation of Senescence-Associated Heterochromatin Foci (SAHF)
R-RNO-2559585, Oncogene Induced Senescence
R-RNO-2559586, DNA Damage/Telomere Stress Induced Senescence
R-RNO-349425, Autodegradation of the E3 ubiquitin ligase COP1
R-RNO-5689880, Ub-specific processing proteases
R-RNO-5689896, Ovarian tumor domain proteases
R-RNO-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-RNO-6804754, Regulation of TP53 Expression
R-RNO-6804756, Regulation of TP53 Activity through Phosphorylation
R-RNO-6804757, Regulation of TP53 Degradation
R-RNO-6804758, Regulation of TP53 Activity through Acetylation
R-RNO-6804759, Regulation of TP53 Activity through Association with Co-factors
R-RNO-6804760, Regulation of TP53 Activity through Methylation
R-RNO-69473, G2/M DNA damage checkpoint
R-RNO-69481, G2/M Checkpoints
R-RNO-69541, Stabilization of p53
R-RNO-69895, Transcriptional activation of cell cycle inhibitor p21
R-RNO-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint
R-RNO-8941855, RUNX3 regulates CDKN1A transcription

Miscellaneous databases

Protein Ontology

More...PROi		PR:P10361

Gene expression databases

BgeeiENSRNOG00000010756, Expressed in thymus and 22 other tissues
ExpressionAtlasiP10361, baseline and differential
GenevisibleiP10361, RN

Family and domain databases

CDDicd08367, P53, 1 hit
Gene3Di2.60.40.720, 1 hit
4.10.170.10, 1 hit
InterProiView protein in InterPro
IPR008967, p53-like_TF_DNA-bd
IPR012346, p53/RUNT-type_TF_DNA-bd_sf
IPR011615, p53_DNA-bd
IPR036674, p53_tetramer_sf
IPR010991, p53_tetrameristn
IPR013872, p53_transactivation_domain
IPR002117, p53_tumour_suppressor
PANTHERiPTHR11447, PTHR11447, 1 hit
PfamiView protein in Pfam
PF00870, P53, 1 hit
PF08563, P53_TAD, 1 hit
PF07710, P53_tetramer, 1 hit
PRINTSiPR00386, P53SUPPRESSR
SUPFAMiSSF47719, SSF47719, 1 hit
SSF49417, SSF49417, 1 hit
PROSITEiView protein in PROSITE
PS00348, P53, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiP53_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P10361
Secondary accession number(s): O09168, Q4KMA9, Q66HM0
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: February 23, 2022
This is version 228 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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