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Entry version 188 (16 Oct 2019)
Sequence version 1 (15 Jul 1998)
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Protein

Cellular tumor antigen p53

Gene

TP53

Organism
Macaca mulatta (Rhesus macaque)
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 transcript 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_section">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 bindingi176ZincBy similarity1
Metal bindingi179ZincBy similarity1
Metal bindingi238ZincBy similarity1
Metal bindingi242ZincBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi102 – 292By 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

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

<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):
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>OrganismiMacaca mulatta (Rhesus macaque)
<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 identifieri9544 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca
<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
  • UP000006718 <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 16

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...
VGNCi
VGNC:78627 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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; 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

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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001857061 – 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 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
Modified residuei33Phosphoserine; by CDK5 and CDK7By similarity1
Modified residuei37Phosphoserine; by MAPKAPK5By similarity1
Modified residuei46Phosphoserine; by CDK5, DYRK2, HIPK2 and PKC/PRKCGBy similarity1
Modified residuei55Phosphothreonine; by TAF1By similarity1
Modified residuei55Phosphothreonine; by TAF1 and GRK5By similarity1
Modified residuei120N6-acetyllysine; by KAT6ABy similarity1
Modified residuei183Phosphoserine; by AURKBBy similarity1
Modified residuei269Phosphoserine; by AURKBBy similarity1
Modified residuei284Phosphothreonine; by AURKBBy similarity1
<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)By similarity
Cross-linki292Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei305N6-acetyllysineBy similarity1
Modified residuei315Phosphoserine; by AURKA, CDK1 and CDK2By similarity1
Modified residuei321N6-acetyllysineBy similarity1
Modified residuei333Omega-N-methylarginineBy similarity1
Modified residuei335Symmetric dimethylarginineBy similarity1
Modified residuei337Symmetric dimethylarginineBy similarity1
Modified residuei370N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei370N6-methyllysine; by SMYD2; alternateBy similarity1
Modified residuei372N6-methyllysine; by SETD7By similarity1
Modified residuei373N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternateBy similarity1
Modified residuei373N6-acetyllysine; alternateBy similarity1
Modified residuei381N6-acetyllysineBy similarity1
Modified residuei382N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei382N6-acetyllysine; by KAT6A; alternateBy similarity1
Modified residuei382N6-methyllysine; by KMT5A; alternateBy similarity1
Cross-linki386Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei392Phosphoserine; by CK2, CDK2 and NUAK1By similarity1

<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. Its 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).By similarity
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. Phosphorylated on Thr-55 by TAF1 which promotes MDM2-mediated TP53 degradation. Phosphorylated on Ser-33 by CDK7 in a CAK complex in response to DNA damage. Phosphorylated by HIPK1. 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. 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 similarity).By similarity
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. Demethylation of dimethylated Lys-370 by KDM1A prevents interaction with TP53BP1 and represses TP53-mediated transcriptional activation (By similarity). Monomethylated at Arg-333 and dimethylated at Arg-335 and Arg-337 by PRMT5; methylation is increased after DNA damage and might possibly affect TP53 target gene specificity (By similarity).By similarity
Sumoylated with SUMO1. Sumoylated at Lys-386 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).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

<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
ENSMMUG00000008639 Expressed in 13 organ(s), highest expression level in CD4-positive helper T cell

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P56424 baseline

<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

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.

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-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.

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-apototic activity (By similarity).

By similarity

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 DNABy similarity1

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9544.ENSMMUP00000035274

<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
P56424

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 – 320Interaction with CCAR2By similarityAdd BLAST320
Regioni1 – 83Interaction with HRMT1L2By similarityAdd BLAST83
Regioni1 – 44Transcription activation (acidic)Add BLAST44
Regioni66 – 110Interaction with WWOXBy similarityAdd BLAST45
Regioni100 – 370Interaction with HIPK1By similarityAdd BLAST271
Regioni100 – 300Required for interaction with ZNF385ABy similarityAdd BLAST201
Regioni113 – 236Required for interaction with FBXO42By similarityAdd BLAST124
Regioni116 – 292Interaction with AXIN1By similarityAdd BLAST177
Regioni256 – 294Interaction with E4F1By similarityAdd BLAST39
Regioni273 – 280Interaction with DNABy similarity8
Regioni300 – 393Interaction with CARM1By similarityAdd BLAST94
Regioni319 – 360Interaction with HIPK2By similarityAdd BLAST42
Regioni325 – 356OligomerizationAdd BLAST32
Regioni359 – 363Interaction with USP7By similarity5
Regioni368 – 387Basic (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>Motifi305 – 321Bipartite nuclear localization signalBy similarityAdd BLAST17
Motifi339 – 350Nuclear export signalBy similarityAdd BLAST12
Motifi370 – 372[KR]-[STA]-K motif3

<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
ENOG410IITK Eukaryota
ENOG410ZSWV LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00950000183153

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000039957

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P56424

KEGG Orthology (KO)

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KOi
K04451

Identification of Orthologs from Complete Genome Data

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OMAi
FHKKGEP

Database of Orthologous Groups

More...
OrthoDBi
257530at2759

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

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Gene3Di
2.60.40.720, 1 hit
4.10.170.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR008967 p53-like_TF_DNA-bd
IPR012346 p53/RUNT-type_TF_DNA-bd_sf
IPR011615 p53_DNA-bd
IPR040926 p53_TAD2
IPR036674 p53_tetramer_sf
IPR010991 p53_tetrameristn
IPR013872 p53_transactivation_domain
IPR002117 p53_tumour_suppressor

The PANTHER Classification System

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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
PF18521 TAD2, 1 hit

Protein Motif fingerprint database; a protein domain database

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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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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 4 potential isoforms that are computationally mapped.Show allAlign All

P56424-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEEPQSDPSI EPPLSQETFS DLWKLLPENN VLSPLPSQAV DDLMLSPDDL
60 70 80 90 100
AQWLTEDPGP DEAPRMSEAA PPMAPTPAAP TPAAPAPAPS WPLSSSVPSQ
110 120 130 140 150
KTYHGSYGFR LGFLHSGTAK SVTCTYSPDL NKMFCQLAKT CPVQLWVDST
160 170 180 190 200
PPPGSRVRAM AIYKQSQHMT EVVRRCPHHE RCSDSDGLAP PQHLIRVEGN
210 220 230 240 250
LRVEYSDDRN TFRHSVVVPY EPPEVGSDCT TIHYNYMCNS SCMGGMNRRP
260 270 280 290 300
ILTIITLEDS SGNLLGRNSF EVRVCACPGR DRRTEEENFR KKGEPCHQLP
310 320 330 340 350
PGSTKRALPN NTSSSPQPKK KPLDGEYFTL QIRGRERFEM FRELNEALEL
360 370 380 390
KDAQAGKEPA GSRAHSSHLK SKKGQSTSRH KKFMFKTEGP DSD
Length:393
Mass (Da):43,655
Last modified:July 15, 1998 - 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:iE212E5E4FE650103
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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F7F8L3F7F8L3_MACMU
Cellular tumor antigen p53
TP53
341Annotation 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>
A0A1I7Q490A0A1I7Q490_MACMU
Cellular tumor antigen p53
TP53
402Annotation 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>
A0A1D5Q594A0A1D5Q594_MACMU
Cellular tumor antigen p53
TP53
292Annotation 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>
A0A1D5RL03A0A1D5RL03_MACMU
Cellular tumor antigen p53
TP53
346Annotation 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>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L20442 mRNA Translation: AAA17994.1
U48956 Genomic DNA Translation: AAB91534.1

NCBI Reference Sequences

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RefSeqi
NP_001040616.1, NM_001047151.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMMUT00000067326; ENSMMUP00000053928; ENSMMUG00000008639

Database of genes from NCBI RefSeq genomes

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GeneIDi
716170

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mcc:716170

<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
L20442 mRNA Translation: AAA17994.1
U48956 Genomic DNA Translation: AAB91534.1
RefSeqiNP_001040616.1, NM_001047151.2

3D structure databases

SMRiP56424
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9544.ENSMMUP00000035274

Genome annotation databases

EnsembliENSMMUT00000067326; ENSMMUP00000053928; ENSMMUG00000008639
GeneIDi716170
KEGGimcc:716170

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7157
VGNCiVGNC:78627 TP53

Phylogenomic databases

eggNOGiENOG410IITK Eukaryota
ENOG410ZSWV LUCA
GeneTreeiENSGT00950000183153
HOGENOMiHOG000039957
InParanoidiP56424
KOiK04451
OMAiFHKKGEP
OrthoDBi257530at2759
TreeFamiTF106101

Gene expression databases

BgeeiENSMMUG00000008639 Expressed in 13 organ(s), highest expression level in CD4-positive helper T cell
ExpressionAtlasiP56424 baseline

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
IPR040926 p53_TAD2
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
PF18521 TAD2, 1 hit
PRINTSiPR00386 P53SUPPRESSR
SUPFAMiSSF47719 SSF47719, 1 hit
SSF49417 SSF49417, 1 hit
PROSITEiView protein in PROSITE
PS00348 P53, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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_MACMU
<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: P56424
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: October 16, 2019
This is version 188 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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