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Entry version 182 (16 Oct 2019)
Sequence version 1 (01 Nov 1995)
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Protein

Cellular tumor antigen p53

Gene

TP53

Organism
Felis catus (Cat) (Felis silvestris catus)
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 bindingi168ZincBy similarity1
Metal bindingi171ZincBy similarity1
Metal bindingi231ZincBy similarity1
Metal bindingi235ZincBy 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 bindingi94 – 285By similarityAdd BLAST192

<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:TRP53
<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>OrganismiFelis catus (Cat) (Felis silvestris catus)
<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 identifieri9685 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis
<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
  • UP000011712 <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 E1

<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_00001857011 – 386Cellular tumor antigen p53Add BLAST386

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 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 residuei112N6-acetyllysine; by KAT6ABy similarity1
Modified residuei262Phosphoserine; by AURKBBy similarity1
Modified residuei277Phosphothreonine; 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-linki284Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei298N6-acetyllysineBy similarity1
Modified residuei314N6-acetyllysineBy similarity1
Modified residuei326Omega-N-methylarginineBy similarity1
Modified residuei328Symmetric dimethylarginineBy similarity1
Modified residuei330Symmetric dimethylarginineBy similarity1
Modified residuei363N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei363N6-methyllysine; by SMYD2; alternateBy similarity1
Modified residuei365N6-methyllysine; by SETD7By similarity1
Modified residuei366N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternateBy similarity1
Modified residuei366N6-acetyllysine; alternateBy similarity1
Modified residuei374N6-acetyllysineBy similarity1
Modified residuei375N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei375N6-acetyllysine; by KAT6A; alternateBy similarity1
Modified residuei375N6-methyllysine; by KMT5A; alternateBy similarity1
Cross-linki379Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei385Phosphoserine; 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

Phosphorylation on Ser residues mediates transcriptional activation. 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 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-385 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-385 by CDK2 in response to DNA-damage (By similarity).By similarity
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
Monomethylated at Lys-365 by SETD7, leading to stabilization and increased transcriptional activation. Monomethylated at Lys-363 by SMYD2, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity. Lys-365 monomethylation prevents interaction with SMYD2 and subsequent monomethylation at Lys-363. Dimethylated at Lys-366 by EHMT1 and EHMT2. Monomethylated at Lys-375 by KMT5A, promoting interaction with L3MBTL1 and leading to repress transcriptional activity. Demethylation of dimethylated Lys-363 by KDM1A prevents interaction with TP53BP1 and represses TP53-mediated transcriptional activation (By similarity). Monomethylated at Arg-326 and dimethylated at Arg-328 and Arg-330 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-379 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
ENSFCAG00000009623 Expressed in 3 organ(s), highest expression level in liver

<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-375) 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>Sitei112Interaction with DNABy similarity1

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9685.ENSFCAP00000008925

<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
P41685

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 – 313Interaction with CCAR2By similarityAdd BLAST313
Regioni1 – 44Transcription activation (acidic)Add BLAST44
Regioni63 – 102Interaction with WWOXBy similarityAdd BLAST40
Regioni92 – 363Interaction with HIPK1By similarityAdd BLAST272
Regioni92 – 293Required for interaction with ZNF385ABy similarityAdd BLAST202
Regioni105 – 229Required for interaction with FBXO42By similarityAdd BLAST125
Regioni108 – 285Interaction with AXIN1By similarityAdd BLAST178
Regioni249 – 287Interaction with E4F1By similarityAdd BLAST39
Regioni266 – 273Interaction with DNABy similarity8
Regioni312 – 353Interaction with HIPK2By similarityAdd BLAST42
Regioni318 – 349OligomerizationAdd BLAST32
Regioni352 – 356Interaction with USP7By similarity5
Regioni361 – 380Basic (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>Motifi298 – 314Bipartite nuclear localization signalBy similarityAdd BLAST17
Motifi332 – 343Nuclear export signalBy similarityAdd BLAST12
Motifi363 – 365[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

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InParanoidi
P41685

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

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OrthoDBi
257530at2759

TreeFam database of animal gene trees

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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
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

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_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 2 potential isoforms that are computationally mapped.Show allAlign All

P41685-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQEPPLELTI EPPLSQETFS ELWNLLPENN VLSSELSSAM NELPLSEDVA
60 70 80 90 100
NWLDEAPDDA SGMSAVPAPA APAPATPAPA ISWPLSSFVP SQKTYPGAYG
110 120 130 140 150
FHLGFLQSGT AKSVTCTYSP PLNKLFCQLA KTCPVQLWVR SPPPPGTCVR
160 170 180 190 200
AMAIYKKSEF MTEVVRRCPH HERCPDSSDG LAPPQHLIRV EGNLHAKYLD
210 220 230 240 250
DRNTFRHSVV VPYEPPEVGS DCTTIHYNFM CNSSCMGGMN RRPIITIITL
260 270 280 290 300
EDSNGKLLGR NSFEVRVCAC PGRDRRTEEE NFRKKGEPCP EPPPGSTKRA
310 320 330 340 350
LPPSTSSTPP QKKKPLDGEY FTLQIRGRER FEMFRELNEA LELKDAQSGK
360 370 380
EPGGSRAHSS HLKAKKGQST SRHKKPMLKR EGLDSD
Length:386
Mass (Da):42,692
Last modified:November 1, 1995 - 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:iD08B43BA1BC8EB78
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A337SFG8A0A337SFG8_FELCA
Cellular tumor antigen p53
TP53
518Annotation 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>
A0A2K5TIV2A0A2K5TIV2_FELCA
Cellular tumor antigen p53
TP53
489Annotation 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>

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 conflicti285K → R in BAA03927 (PubMed:8286534).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
D26608 mRNA Translation: BAA05653.1
D16460 mRNA Translation: BAA03927.1

NCBI Reference Sequences

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RefSeqi
NP_001009294.1, NM_001009294.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSFCAT00000055487; ENSFCAP00000049466; ENSFCAG00000009623

Database of genes from NCBI RefSeq genomes

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GeneIDi
493847

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
fca:493847

<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
D26608 mRNA Translation: BAA05653.1
D16460 mRNA Translation: BAA03927.1
RefSeqiNP_001009294.1, NM_001009294.1

3D structure databases

SMRiP41685
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9685.ENSFCAP00000008925

Genome annotation databases

EnsembliENSFCAT00000055487; ENSFCAP00000049466; ENSFCAG00000009623
GeneIDi493847
KEGGifca:493847

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
7157

Phylogenomic databases

eggNOGiENOG410IITK Eukaryota
ENOG410ZSWV LUCA
GeneTreeiENSGT00950000183153
HOGENOMiHOG000039957
InParanoidiP41685
KOiK04451
OMAiFHKKGEP
OrthoDBi257530at2759
TreeFamiTF106101

Gene expression databases

BgeeiENSFCAG00000009623 Expressed in 3 organ(s), highest expression level in liver

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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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_FELCA
<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: P41685
<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: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 16, 2019
This is version 182 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
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