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Protein

Cellular tumor antigen p53

Gene

Tp53

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

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

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression (By similarity). 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, but seems to have to effect on cell-cycle regulation. Regulates the circadian clock by repressing CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER2 (PubMed:24051492).By similarity4 Publications

Caution

It is uncertain whether Met-1 or Met-4 is the initiator.Curated

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

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi173Zinc1
Metal bindingi176Zinc1
Metal bindingi235Zinc1
Metal bindingi239Zinc1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi99 – 289By 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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-2559580 Oxidative Stress Induced Senescence
R-MMU-2559584 Formation of Senescence-Associated Heterochromatin Foci (SAHF)
R-MMU-2559585 Oncogene Induced Senescence
R-MMU-2559586 DNA Damage/Telomere Stress Induced Senescence
R-MMU-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-MMU-5689880 Ub-specific processing proteases
R-MMU-5689896 Ovarian tumor domain proteases
R-MMU-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-MMU-6804754 Regulation of TP53 Expression
R-MMU-6804756 Regulation of TP53 Activity through Phosphorylation
R-MMU-6804757 Regulation of TP53 Degradation
R-MMU-6804758 Regulation of TP53 Activity through Acetylation
R-MMU-6804759 Regulation of TP53 Activity through Association with Co-factors
R-MMU-6804760 Regulation of TP53 Activity through Methylation
R-MMU-6811555 PI5P Regulates TP53 Acetylation
R-MMU-69473 G2/M DNA damage checkpoint
R-MMU-69481 G2/M Checkpoints
R-MMU-69541 Stabilization of p53
R-MMU-69895 Transcriptional activation of cell cycle inhibitor p21
R-MMU-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-MMU-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_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, 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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 11

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:98834 Trp53

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

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

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Mitochondrion, Nucleus

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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

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

Disease mutation, Tumor suppressor

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4164

<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_00001857091 – 390Cellular tumor antigen p53Add BLAST390

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 residuei12Phosphoserine; by HIPK41 Publication1
Modified residuei18Phosphoserine; by CDK5, PRPK, AMPK, NUAK1 and ATM1 Publication1
Modified residuei21Phosphothreonine; by CK1, VRK1 and VRK2By similarity1
Modified residuei23Phosphoserine; by CHEK2, CK1 and PLK3By similarity1
Modified residuei37Phosphoserine; by MAPKAPK51 Publication1
Modified residuei117N6-acetyllysine; by KAT6ABy similarity1
Modified residuei180Phosphoserine; by AURKBBy similarity1
Modified residuei266Phosphoserine; by AURKBBy similarity1
Modified residuei281Phosphothreonine; 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-linki288Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki289Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei302N6-acetyllysineBy similarity1
Modified residuei312Phosphoserine; by AURKA, CDK1 and CDK2By similarity1
Modified residuei318N6-acetyllysineCombined sources1
Modified residuei367N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei367N6-methyllysine; by SMYD2; alternateBy similarity1
Modified residuei369N6-methyllysine; by SETD7By similarity1
Modified residuei370N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternateBy similarity1
Modified residuei370N6-acetyllysine; alternateBy similarity1
Modified residuei378N6-acetyllysineBy similarity1
Modified residuei379N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei379N6-acetyllysine; by KAT6A; alternateBy similarity1
Modified residuei379N6-methyllysine; by KMT5A; alternateBy similarity1
Cross-linki383Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei389Phosphoserine; 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

Phosphorylated on Ser-18 upon ultraviolet irradiation; which is enhanced by interaction with BANP (By similarity). Phosphorylation on Ser residues mediates transcriptional activation. Phosphorylation at Ser-12 by HIPK4 increases repression activity on BIRC5 promoter. Phosphorylated on Thr-21 by VRK1. Phosphorylated on Ser-23 by CHEK2 in response to DNA damage, which prevents ubiquitination by MDM2. Phosphorylated on Ser-23 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. Stabilized by CDK5-mediated phosphorylation in response to genotoxic and oxidative stresses at Ser-18 leading to accumulation of p53/TP53, particularly in the nucleus, thus inducing the transactivation of p53/TP53 target genes (By similarity). Phosphorylated on Ser-389 following UV but not gamma irradiation. Phosphorylated by HIPK1.By similarity7 Publications
Deacetylation by SIRT2 impairs its ability to induce transcription activation in a AKT-dependent manner (By similarity). Acetylated. Its deacetylation by SIRT1 impairs its ability to induce proapoptotic program and modulate cell senescence.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 at Lys-288 and Lys-289, 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 (PubMed:25732823). Polyubiquitinated by C10orf90/FATS, polyubiquitination is 'Lys-48'-linkage independent and non-proteolytic, leading to TP53 stabilization (PubMed:24240685).By similarity2 Publications
Monomethylated at Lys-369 by SETD7, leading to stabilization and increased transcriptional activation. Monomethylated at Lys-367 by SMYD2, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity. Lys-369 monomethylation prevents interaction with SMYD2 and subsequent monomethylation at Lys-367. Dimethylated at Lys-370 by EHMT1 and EHMT2. Monomethylated at Lys-379 by KMT5A, promoting interaction with L3MBTL1 and leading to repress transcriptional activity. Demethylation of dimethylated Lys-367 by KDM1A prevents interaction with TP53BP1 and represses TP53-mediated transcriptional activation (By similarity).By similarity
Sumoylated with SUMO1. Sumoylated at Lys-383 by UBC9 (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P02340

MaxQB - The MaxQuant DataBase

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MaxQBi
P02340

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

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PaxDbi
P02340

PRoteomics IDEntifications database

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PRIDEi
P02340

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P02340

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

More...
PhosphoSitePlusi
P02340

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P02340

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

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

Expressed in a circadian manner in the suprachiasmatic nucleus (SCN) of the brain with a peak seen at ZT8.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000059552 Expressed in 258 organ(s), highest expression level in embryo

CleanEx database of gene expression profiles

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CleanExi
MM_TRP53

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P02340 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P02340 MM

<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

Binds DNA as a homotetramer. Interacts with AXIN1 (PubMed:15526030). Probably part of a complex consisting of TP53, HIPK2 and AXIN1 (PubMed:15526030). 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 (PubMed:12702766). Found in a complex with CABLES1 and TP73 (PubMed:11706030). Interacts with HIPK1, HIPK2, and TP53INP1. Interacts with WWOX. Interacts with USP7 and SYVN1 (PubMed:14719112). Interacts with HSP90AB1. Interacts with CHD8; leading to recruit histone H1 and prevent transactivation activity (PubMed:19151705). Interacts with ARMC10, BANP, CDKN2AIP, NUAK1, STK11/LKB1, UHRF2 and E4F (PubMed:10644996). 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 (PubMed:19556538). 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 (PubMed:17719541). 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 (PubMed:24240685).By similarity10 Publications

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>Sitei117Interaction with DNA1

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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
204323, 117 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P02340

Database of interacting proteins

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DIPi
DIP-369N

Protein interaction database and analysis system

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IntActi
P02340, 44 interactors

Molecular INTeraction database

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MINTi
P02340

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000104298

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

Secondary structure

1390
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HU8X-ray2.70A/B/C99-284[»]
2GEQX-ray2.30A/B92-292[»]
2IOIX-ray1.55A92-292[»]
2IOMX-ray2.00A92-292[»]
2IOOX-ray2.02A92-292[»]
2P52X-ray1.50A92-287[»]
3EXJX-ray2.00A/B96-292[»]
3EXLX-ray2.20A96-292[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P02340

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

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SMRi
P02340

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P02340

<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>Regioni4 – 317Interaction with CCAR2By similarityAdd BLAST314
Regioni4 – 45Transcription activation (acidic)Add BLAST42
Regioni63 – 107Interaction with WWOXBy similarityAdd BLAST45
Regioni97 – 367Interaction with HIPK11 PublicationAdd BLAST271
Regioni97 – 297Required for interaction with ZNF385ABy similarityAdd BLAST201
Regioni110 – 233Required for interaction with FBXO42By similarityAdd BLAST124
Regioni113 – 289Interaction with AXIN11 PublicationAdd BLAST177
Regioni256 – 294Interaction with E4F1By similarityAdd BLAST39
Regioni270 – 277Interaction with DNA8
Regioni316 – 357Interaction with HIPK2By similarityAdd BLAST42
Regioni322 – 353OligomerizationAdd BLAST32
Regioni356 – 360Interaction with USP7By similarity5
Regioni365 – 384Basic (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>Motifi302 – 318Bipartite nuclear localization signalBy similarityAdd BLAST17
Motifi336 – 347Nuclear export signalBy similarityAdd BLAST12
Motifi367 – 369[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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000039957

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG005201

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P02340

KEGG Orthology (KO)

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KOi
K04451

Database of Orthologous Groups

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OrthoDBi
257530at2759

Family and domain databases

Conserved Domains Database

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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

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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

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PRINTSi
PR00386 P53SUPPRESSR

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47719 SSF47719, 1 hit
SSF49417 SSF49417, 1 hit

PROSITE; a protein domain and family database

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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>.<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

P02340-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTAMEESQSD ISLELPLSQE TFSGLWKLLP PEDILPSPHC MDDLLLPQDV
60 70 80 90 100
EEFFEGPSEA LRVSGAPAAQ DPVTETPGPV APAPATPWPL SSFVPSQKTY
110 120 130 140 150
QGNYGFHLGF LQSGTAKSVM CTYSPPLNKL FCQLAKTCPV QLWVSATPPA
160 170 180 190 200
GSRVRAMAIY KKSQHMTEVV RRCPHHERCS DGDGLAPPQH LIRVEGNLYP
210 220 230 240 250
EYLEDRQTFR HSVVVPYEPP EAGSEYTTIH YKYMCNSSCM GGMNRRPILT
260 270 280 290 300
IITLEDSSGN LLGRDSFEVR VCACPGRDRR TEEENFRKKE VLCPELPPGS
310 320 330 340 350
AKRALPTCTS ASPPQKKKPL DGEYFTLKIR GRKRFEMFRE LNEALELKDA
360 370 380 390
HATEESGDSR AHSSYLKTKK GQSTSRHKKT MVKKVGPDSD
Length:390
Mass (Da):43,458
Last modified:October 10, 2018 - v4
<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:iED5A607378D921D7
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
Q549C9Q549C9_MOUSE
Cellular tumor antigen p53
Trp53 p53, mCG_20908
390Annotation 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>
Q80ZA1Q80ZA1_MOUSE
Cellular tumor antigen p53
Trp53
381Annotation 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>
A0A158SIS7A0A158SIS7_MOUSE
Cellular tumor antigen p53
Trp53 RP23-56I20.1-001
387Annotation 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>
I7HIK9I7HIK9_MOUSE
Cellular tumor antigen p53
Trp53 RP23-56I20.1-002
378Annotation 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 conflicti48Q → R in CAA25323 (PubMed:6379601).Curated1
Sequence conflicti79 – 81PVA → QW in CAA25323 (PubMed:6379601).Curated3

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 varianti135A → V Can cooperate with an activated Ras to transform fibroblasts. 1 Publication1
Natural varianti168E → G in clone P53-M11. 1
Natural varianti191L → R. 1

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

More...
DDBJi
Links Updated
X00876
, X00877, X00878, X00879, X00880, X00881, X00882, X00883, X00884, X00885 Genomic DNA Translation: CAA25420.1
X01237 mRNA Translation: CAA25625.1
X00741 mRNA Translation: CAA25323.1
M13872 mRNA Translation: AAA39881.1
M13873 mRNA Translation: AAA39882.1
M13874 mRNA Translation: AAA39883.1 Sequence problems.
AB021961 mRNA Translation: BAA82344.1
AF151353 mRNA Translation: AAD39535.1
AB017815 mRNA Translation: BAA82339.1
AB017816 mRNA Translation: BAA82340.1
AB020317 mRNA Translation: BAA82343.1
BC005448 mRNA Translation: AAH05448.1
S77930 Genomic DNA Translation: AAB21108.2

The Consensus CDS (CCDS) project

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CCDSi
CCDS36193.1

Protein sequence database of the Protein Information Resource

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PIRi
A22739 DNMS53
S38824

NCBI Reference Sequences

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RefSeqi
NP_001120705.1, NM_001127233.1
NP_035770.2, NM_011640.3
XP_006533220.1, XM_006533157.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.222

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000108658; ENSMUSP00000104298; ENSMUSG00000059552

Database of genes from NCBI RefSeq genomes

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GeneIDi
22059

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:22059

UCSC genome browser

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UCSCi
uc007jql.2 mouse

<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
X00876
, X00877, X00878, X00879, X00880, X00881, X00882, X00883, X00884, X00885 Genomic DNA Translation: CAA25420.1
X01237 mRNA Translation: CAA25625.1
X00741 mRNA Translation: CAA25323.1
M13872 mRNA Translation: AAA39881.1
M13873 mRNA Translation: AAA39882.1
M13874 mRNA Translation: AAA39883.1 Sequence problems.
AB021961 mRNA Translation: BAA82344.1
AF151353 mRNA Translation: AAD39535.1
AB017815 mRNA Translation: BAA82339.1
AB017816 mRNA Translation: BAA82340.1
AB020317 mRNA Translation: BAA82343.1
BC005448 mRNA Translation: AAH05448.1
S77930 Genomic DNA Translation: AAB21108.2
CCDSiCCDS36193.1
PIRiA22739 DNMS53
S38824
RefSeqiNP_001120705.1, NM_001127233.1
NP_035770.2, NM_011640.3
XP_006533220.1, XM_006533157.3
UniGeneiMm.222

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HU8X-ray2.70A/B/C99-284[»]
2GEQX-ray2.30A/B92-292[»]
2IOIX-ray1.55A92-292[»]
2IOMX-ray2.00A92-292[»]
2IOOX-ray2.02A92-292[»]
2P52X-ray1.50A92-287[»]
3EXJX-ray2.00A/B96-292[»]
3EXLX-ray2.20A96-292[»]
ProteinModelPortaliP02340
SMRiP02340
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204323, 117 interactors
CORUMiP02340
DIPiDIP-369N
IntActiP02340, 44 interactors
MINTiP02340
STRINGi10090.ENSMUSP00000104298

Chemistry databases

ChEMBLiCHEMBL4164

PTM databases

iPTMnetiP02340
PhosphoSitePlusiP02340
SwissPalmiP02340

Proteomic databases

EPDiP02340
MaxQBiP02340
PaxDbiP02340
PRIDEiP02340

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000108658; ENSMUSP00000104298; ENSMUSG00000059552
GeneIDi22059
KEGGimmu:22059
UCSCiuc007jql.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
22059
MGIiMGI:98834 Trp53

Phylogenomic databases

eggNOGiENOG410IITK Eukaryota
ENOG410ZSWV LUCA
HOGENOMiHOG000039957
HOVERGENiHBG005201
InParanoidiP02340
KOiK04451
OrthoDBi257530at2759

Enzyme and pathway databases

ReactomeiR-MMU-2559580 Oxidative Stress Induced Senescence
R-MMU-2559584 Formation of Senescence-Associated Heterochromatin Foci (SAHF)
R-MMU-2559585 Oncogene Induced Senescence
R-MMU-2559586 DNA Damage/Telomere Stress Induced Senescence
R-MMU-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-MMU-5689880 Ub-specific processing proteases
R-MMU-5689896 Ovarian tumor domain proteases
R-MMU-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-MMU-6804754 Regulation of TP53 Expression
R-MMU-6804756 Regulation of TP53 Activity through Phosphorylation
R-MMU-6804757 Regulation of TP53 Degradation
R-MMU-6804758 Regulation of TP53 Activity through Acetylation
R-MMU-6804759 Regulation of TP53 Activity through Association with Co-factors
R-MMU-6804760 Regulation of TP53 Activity through Methylation
R-MMU-6811555 PI5P Regulates TP53 Acetylation
R-MMU-69473 G2/M DNA damage checkpoint
R-MMU-69481 G2/M Checkpoints
R-MMU-69541 Stabilization of p53
R-MMU-69895 Transcriptional activation of cell cycle inhibitor p21
R-MMU-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-MMU-8941855 RUNX3 regulates CDKN1A transcription

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Trp53 mouse
EvolutionaryTraceiP02340

Protein Ontology

More...
PROi
PR:P02340

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000059552 Expressed in 258 organ(s), highest expression level in embryo
CleanExiMM_TRP53
ExpressionAtlasiP02340 baseline and differential
GenevisibleiP02340 MM

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

More...
ProtoNeti
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_MOUSE
<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: P02340
Secondary accession number(s): Q9QUP3
<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 21, 1986
Last sequence update: October 10, 2018
Last modified: January 16, 2019
This is version 235 of the entry and version 4 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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