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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-Experimental evidence at protein leveli

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

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi170Zinc1
Metal bindingi173Zinc1
Metal bindingi232Zinc1
Metal bindingi236Zinc1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi96 – 286By similarityAdd BLAST191

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: MGI
  • B cell lineage commitment Source: MGI
  • cardiac septum morphogenesis Source: MGI
  • cell aging Source: UniProtKB
  • cell cycle arrest Source: MGI
  • cellular response to DNA damage stimulus Source: MGI
  • cellular response to gamma radiation Source: MGI
  • cellular response to glucose starvation Source: MGI
  • cellular response to ionizing radiation Source: MGI
  • cellular response to UV Source: MGI
  • cellular response to UV-C Source: MGI
  • central nervous system development Source: MGI
  • cerebellum development Source: MGI
  • chromatin assembly Source: MGI
  • chromosome breakage Source: MGI
  • chromosome organization Source: MGI
  • circadian behavior Source: UniProtKB
  • circadian rhythm Source: UniProtKB
  • determination of adult lifespan Source: BHF-UCL
  • DNA damage response, signal transduction by p53 class mediator Source: MGI
  • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: MGI
  • DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: MGI
  • DNA strand renaturation Source: UniProtKB
  • double-strand break repair Source: MGI
  • embryo development ending in birth or egg hatching Source: MGI
  • embryonic organ development Source: MGI
  • entrainment of circadian clock by photoperiod Source: UniProtKB
  • ER overload response Source: MGI
  • gastrulation Source: MGI
  • heart development Source: MGI
  • intrinsic apoptotic signaling pathway by p53 class mediator Source: MGI
  • intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: BHF-UCL
  • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
  • intrinsic apoptotic signaling pathway in response to hypoxia Source: MGI
  • in utero embryonic development Source: MGI
  • mitochondrial DNA repair Source: MGI
  • mitotic cell cycle arrest Source: MGI
  • mitotic G1 DNA damage checkpoint Source: MGI
  • multicellular organism development Source: UniProtKB
  • multicellular organism growth Source: MGI
  • necroptotic process Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of cell growth Source: UniProtKB
  • negative regulation of cell proliferation Source: BHF-UCL
  • negative regulation of DNA replication Source: MGI
  • negative regulation of fibroblast proliferation Source: MGI
  • negative regulation of gene expression Source: MGI
  • negative regulation of glucose catabolic process to lactate via pyruvate Source: MGI
  • negative regulation of macromitophagy Source: MGI
  • negative regulation of mitotic cell cycle Source: MGI
  • negative regulation of neuroblast proliferation Source: MGI
  • negative regulation of proteolysis Source: MGI
  • negative regulation of reactive oxygen species metabolic process Source: MGI
  • negative regulation of telomerase activity Source: MGI
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • negative regulation of transforming growth factor beta receptor signaling pathway Source: MGI
  • neuron apoptotic process Source: MGI
  • nucleotide-excision repair Source: UniProtKB
  • oligodendrocyte apoptotic process Source: UniProtKB
  • oxidative stress-induced premature senescence Source: MGI
  • positive regulation of apoptotic process Source: MGI
  • positive regulation of cardiac muscle cell apoptotic process Source: MGI
  • positive regulation of cell aging Source: BHF-UCL
  • positive regulation of cell cycle arrest Source: MGI
  • positive regulation of execution phase of apoptosis Source: MGI
  • positive regulation of gene expression Source: MGI
  • positive regulation of histone deacetylation Source: MGI
  • positive regulation of intrinsic apoptotic signaling pathway Source: MGI
  • positive regulation of mitochondrial membrane permeability Source: MGI
  • positive regulation of neuron apoptotic process Source: MGI
  • positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • positive regulation of protein oligomerization Source: MGI
  • positive regulation of reactive oxygen species metabolic process Source: MGI
  • positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
  • positive regulation of thymocyte apoptotic process Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
  • positive regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: MGI
  • protein complex assembly Source: MGI
  • protein import into nucleus, translocation Source: MGI
  • protein localization Source: MGI
  • protein stabilization Source: MGI
  • protein tetramerization Source: InterPro
  • regulation of apoptotic process Source: MGI
  • regulation of cell cycle Source: MGI
  • regulation of cell proliferation Source: MGI
  • regulation of cellular senescence Source: MGI
  • regulation of fibroblast apoptotic process Source: MGI
  • regulation of glycolytic process by positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • regulation of intrinsic apoptotic signaling pathway by p53 class mediator Source: MGI
  • regulation of mitochondrial membrane permeability involved in apoptotic process Source: MGI
  • regulation of neuron apoptotic process Source: MGI
  • regulation of thymocyte apoptotic process Source: MGI
  • regulation of tissue remodeling Source: MGI
  • regulation of transcription, DNA-templated Source: MGI
  • regulation of transcription from RNA polymerase II promoter Source: MGI
  • release of cytochrome c from mitochondria Source: MGI
  • replicative senescence Source: MGI
  • response to drug Source: MGI
  • response to gamma radiation Source: MGI
  • response to ischemia Source: MGI
  • response to oxidative stress Source: MGI
  • response to salt stress Source: MGI
  • response to UV Source: MGI
  • response to X-ray Source: MGI
  • rRNA transcription Source: MGI
  • somitogenesis Source: MGI
  • T cell differentiation in thymus Source: MGI
  • T cell lineage commitment Source: MGI
  • T cell proliferation involved in immune response Source: MGI
  • transforming growth factor beta receptor signaling pathway Source: MGI
  • viral process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Apoptosis, Biological rhythms, Cell cycle, Necrosis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

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.

Names & Taxonomyi

Protein namesi
Recommended name:
Cellular tumor antigen p53
Alternative name(s):
Tumor suppressor p53
Gene namesi
Name:Tp53
Synonyms:P53, Trp53
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:98834. Trp53.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: GO_Central
  • cytoplasm Source: UniProtKB
  • cytosol Source: MGI
  • endoplasmic reticulum Source: UniProtKB-SubCell
  • mitochondrial matrix Source: MGI
  • mitochondrion Source: UniProtKB
  • nuclear chromatin Source: MGI
  • nuclear matrix Source: MGI
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: MGI
  • nucleus Source: UniProtKB
  • PML body Source: MGI
  • protein complex Source: MGI
  • replication fork Source: MGI
  • site of double-strand break Source: MGI
  • transcription factor complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Mitochondrion, Nucleus

Pathology & Biotechi

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

ChEMBLiCHEMBL4164.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001857091 – 387Cellular tumor antigen p53Add BLAST387

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei9Phosphoserine; by HIPK41 Publication1
Modified residuei15Phosphoserine; by CDK5, PRPK, AMPK, NUAK1 and ATM1 Publication1
Modified residuei18Phosphothreonine; by CK1, VRK1 and VRK2By similarity1
Modified residuei20Phosphoserine; by CHEK2, CK1 and PLK3By similarity1
Modified residuei34Phosphoserine; by MAPKAPK51 Publication1
Modified residuei114N6-acetyllysine; by KAT6ABy similarity1
Modified residuei177Phosphoserine; by AURKBBy similarity1
Modified residuei263Phosphoserine; by AURKBBy similarity1
Modified residuei278Phosphothreonine; by AURKBBy similarity1
Cross-linki285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki286Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei299N6-acetyllysineBy similarity1
Modified residuei309Phosphoserine; by AURKA, CDK1 and CDK2By similarity1
Modified residuei315N6-acetyllysineCombined sources1
Modified residuei364N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei364N6-methyllysine; by SMYD2; alternateBy similarity1
Modified residuei366N6-methyllysine; by SETD7By similarity1
Modified residuei367N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternateBy similarity1
Modified residuei367N6-acetyllysine; alternateBy similarity1
Modified residuei375N6-acetyllysineBy similarity1
Modified residuei376N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei376N6-acetyllysine; by KAT6A; alternateBy similarity1
Modified residuei376N6-methyllysine; by KMT5A; alternateBy similarity1
Cross-linki380Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei386Phosphoserine; by CK2, CDK2 and NUAK1By similarity1

Post-translational modificationi

Phosphorylated on Ser-15 upon ultraviolet irradiation; which is enhanced by interaction with BANP (By similarity). Phosphorylation on Ser residues mediates transcriptional activation. Phosphorylation at Ser-9 by HIPK4 increases repression activity on BIRC5 promoter. Phosphorylated on Thr-18 by VRK1. Phosphorylated on Ser-20 by CHEK2 in response to DNA damage, which prevents ubiquitination by MDM2. Phosphorylated on Ser-20 by PLK3 in response to reactive oxygen species (ROS), promoting p53/TP53-mediated apoptosis. 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-15 leading to accumulation of p53/TP53, particularly in the nucleus, thus inducing the transactivation of p53/TP53 target genes (By similarity). Phosphorylated on Ser-386 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-285 and Lys-286, which leads to proteasomal degradation. Deubiquitinated by USP10, leading to stabilize it. Ubiquitinated by TRIM24, RFFL and RNF34, which leads to proteasomal degradation. Ubiquitination by TOPORS induces degradation. Deubiquitination by USP7, leading to stabilize it. Ubiquitinated by RFWD2, which leads to proteasomal degradation (By similarity). Ubiquitination and subsequent proteasomal degradation is negatively regulated by CCAR2 (PubMed:25732823).By similarity1 Publication
Monomethylated at Lys-366 by SETD7, leading to stabilization and increased transcriptional activation. Monomethylated at Lys-364 by SMYD2, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity. Lys-366 monomethylation prevents interaction with SMYD2 and subsequent monomethylation at Lys-364. Dimethylated at Lys-367 EHMT1 and EHMT2. Monomethylated at Lys-376 KMT5A, promoting interaction with L3MBTL1 and leading to repress transcriptional activity. Demethylation of dimethylated Lys-364 by KDM1A prevents interaction with TP53BP1 and represses TP53-mediated transcriptional activation (By similarity).By similarity
Sumoylated with SUMO1. Sumoylated at Lys-380 by UBC9 (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP02340.
MaxQBiP02340.
PaxDbiP02340.
PRIDEiP02340.

PTM databases

iPTMnetiP02340.
PhosphoSitePlusiP02340.
SwissPalmiP02340.

Expressioni

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

BgeeiENSMUSG00000059552.
CleanExiMM_TRP53.
ExpressionAtlasiP02340. baseline and differential.
GenevisibleiP02340. MM.

Interactioni

Subunit structurei

Binds DNA as a homotetramer. Found in a complex with CABLES1 and TP73. Interacts with histone acetyltransferases EP300 and methyltransferases HRMT1L2 and CARM1, and recruits them to promoters. The C-terminus interacts with TAF1, when TAF1 is part of the TFIID complex. Interacts with HIPK1, HIPK2, AXIN1, and TP53INP1. Part of a complex consisting of TP53, HIPK2 and AXIN1. Interacts with WWOX. Interacts with USP7 and SYVN1. Interacts with HSP90AB1. Interacts with YWHAZ; the interaction enhances TP53 transcriptional activity. Phosphorylation of YWHAZ on 'Ser-58' inhibits this interaction. Interacts with AURKB, SETD2, UHRF2 and NOC2L. 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 with DAXX. Interacts (when monomethylated at Lys-376) with L3MBTL1. Interacts with BANP, CDKN2AIP, NUAK1, STK11/LKB1 and E4F1. Interacts with CHD8, leading to recruit histone H1 and prevent transactivation activity. Interacts with AURKA, TRIM24 and BRD7. Interacts with GRK5. Binds to the CAK complex (CDK7, cyclin H and MAT1) in response to DNA damage. Interacts with CDK5 in neurons. Phosphorylated at Ser-309 and Ser-386 by CDK2 in response to DNA-damage. 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. Forms a complex with UBC9 and PRKRA. Interacts with ZNF385B; the interaction is direct. Interacts (via DNA-binding domain) with ZNF385A; the interaction is direct and enhances p53/TP53 transactivation functions on cell-cycle arrest target genes, resulting in growth arrest. Interacts with ANKRD2. Interacts with RFFL and RNF34; involved in p53/TP53 ubiquitination. Interacts with MTA1 and RFWD2. Interacts with CCAR2 (via N-terminus). Interacts with MORC3.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei114Interaction with DNA1

Binary interactionsi

WithEntry#Exp.IntActNotes
P0307012EBI-474016,EBI-617698From a different organism.
BCL2L1Q07817-13EBI-474016,EBI-287195From a different organism.
Ep300B2RWS62EBI-474016,EBI-3953360
Mdm2P238045EBI-474016,EBI-641788
Mdm2P23804-12EBI-474016,EBI-3386476
Pin1Q9QUR73EBI-474016,EBI-2432975
PolgP540992EBI-474016,EBI-863636
PpifQ99KR72EBI-474016,EBI-6455001
PtenO085864EBI-474016,EBI-1186266
Smarcd1Q614664EBI-474016,EBI-371529
Sod2P096712EBI-474016,EBI-1635071
UbcP629912EBI-474016,EBI-413074

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204323. 86 interactors.
DIPiDIP-369N.
IntActiP02340. 37 interactors.
MINTiMINT-120104.
STRINGi10090.ENSMUSP00000104298.

Structurei

Secondary structure

1387
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi99 – 101Combined sources3
Beta strandi104 – 106Combined sources3
Helixi113 – 116Combined sources4
Beta strandi117 – 121Combined sources5
Turni122 – 125Combined sources4
Beta strandi126 – 129Combined sources4
Beta strandi134 – 140Combined sources7
Beta strandi150 – 159Combined sources10
Turni160 – 164Combined sources5
Helixi171 – 175Combined sources5
Beta strandi181 – 183Combined sources3
Beta strandi188 – 193Combined sources6
Beta strandi198 – 201Combined sources4
Turni203 – 205Combined sources3
Beta strandi208 – 213Combined sources6
Beta strandi222 – 230Combined sources9
Helixi235 – 237Combined sources3
Helixi239 – 242Combined sources4
Beta strandi245 – 252Combined sources8
Beta strandi258 – 268Combined sources11
Helixi272 – 283Combined sources12
Turni285 – 287Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HU8X-ray2.70A/B/C96-281[»]
2GEQX-ray2.30A/B89-289[»]
2IOIX-ray1.55A89-289[»]
2IOMX-ray2.00A89-289[»]
2IOOX-ray2.02A89-289[»]
2P52X-ray1.50A89-284[»]
3EXJX-ray2.00A/B93-289[»]
3EXLX-ray2.20A93-289[»]
ProteinModelPortaliP02340.
SMRiP02340.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02340.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 314Interaction with CCAR2By similarityAdd BLAST314
Regioni1 – 42Transcription activation (acidic)Add BLAST42
Regioni60 – 104Interaction with WWOXBy similarityAdd BLAST45
Regioni94 – 364Interaction with HIPK11 PublicationAdd BLAST271
Regioni94 – 294Required for interaction with ZNF385ABy similarityAdd BLAST201
Regioni107 – 230Required for interaction with FBXO42By similarityAdd BLAST124
Regioni110 – 286Interaction with AXIN11 PublicationAdd BLAST177
Regioni253 – 291Interaction with E4F1By similarityAdd BLAST39
Regioni267 – 274Interaction with DNA8
Regioni313 – 354Interaction with HIPK2By similarityAdd BLAST42
Regioni319 – 350OligomerizationAdd BLAST32
Regioni353 – 357Interaction with USP7By similarity5
Regioni362 – 381Basic (repression of DNA-binding)Add BLAST20

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi299 – 315Bipartite nuclear localization signalBy similarityAdd BLAST17
Motifi333 – 344Nuclear export signalBy similarityAdd BLAST12
Motifi364 – 366[KR]-[STA]-K motif3

Domaini

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

Sequence similaritiesi

Belongs to the p53 family.Curated

Phylogenomic databases

eggNOGiENOG410IITK. Eukaryota.
ENOG410ZSWV. LUCA.
GeneTreeiENSGT00390000015092.
HOGENOMiHOG000039957.
HOVERGENiHBG005201.
InParanoidiP02340.
KOiK04451.

Family and domain databases

CDDicd08367. P53. 1 hit.
Gene3Di2.60.40.720. 1 hit.
4.10.170.10. 1 hit.
InterProiIPR008967. p53-like_TF_DNA-bd.
IPR012346. p53/RUNT-type_TF_DNA-bd.
IPR011615. p53_DNA-bd.
IPR010991. p53_tetrameristn.
IPR013872. p53_transactivation_domain.
IPR002117. p53_tumour_suppressor.
[Graphical view]
PANTHERiPTHR11447. PTHR11447. 1 hit.
PfamiPF00870. P53. 1 hit.
PF08563. P53_TAD. 1 hit.
PF07710. P53_tetramer. 1 hit.
[Graphical view]
PRINTSiPR00386. P53SUPPRESSR.
SUPFAMiSSF47719. SSF47719. 1 hit.
SSF49417. SSF49417. 1 hit.
PROSITEiPS00348. P53. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P02340-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEESQSDISL ELPLSQETFS GLWKLLPPED ILPSPHCMDD LLLPQDVEEF
60 70 80 90 100
FEGPSEALRV SGAPAAQDPV TETPGPVAPA PATPWPLSSF VPSQKTYQGN
110 120 130 140 150
YGFHLGFLQS GTAKSVMCTY SPPLNKLFCQ LAKTCPVQLW VSATPPAGSR
160 170 180 190 200
VRAMAIYKKS QHMTEVVRRC PHHERCSDGD GLAPPQHLIR VEGNLYPEYL
210 220 230 240 250
EDRQTFRHSV VVPYEPPEAG SEYTTIHYKY MCNSSCMGGM NRRPILTIIT
260 270 280 290 300
LEDSSGNLLG RDSFEVRVCA CPGRDRRTEE ENFRKKEVLC PELPPGSAKR
310 320 330 340 350
ALPTCTSASP PQKKKPLDGE YFTLKIRGRK RFEMFRELNE ALELKDAHAT
360 370 380
EESGDSRAHS SYLKTKKGQS TSRHKKTMVK KVGPDSD
Length:387
Mass (Da):43,155
Last modified:March 18, 2008 - v3
Checksum:iB55EB7B463E1DD9D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti45Q → R in CAA25323 (PubMed:6379601).Curated1
Sequence conflicti76 – 78PVA → QW in CAA25323 (PubMed:6379601).Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti132A → V Can cooperate with an activated Ras to transform fibroblasts. 1 Publication1
Natural varianti165E → G in clone P53-M11. 1
Natural varianti188L → R.1

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.
PIRiA22739. DNMS53.
S38824.
RefSeqiNP_001120705.1. NM_001127233.1.
NP_035770.2. NM_011640.3.
XP_006533220.1. XM_006533157.3.
UniGeneiMm.222.

Genome annotation databases

EnsembliENSMUST00000005371; ENSMUSP00000005371; ENSMUSG00000059552.
GeneIDi22059.
KEGGimmu:22059.
UCSCiuc007jql.2. mouse.

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.
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/C96-281[»]
2GEQX-ray2.30A/B89-289[»]
2IOIX-ray1.55A89-289[»]
2IOMX-ray2.00A89-289[»]
2IOOX-ray2.02A89-289[»]
2P52X-ray1.50A89-284[»]
3EXJX-ray2.00A/B93-289[»]
3EXLX-ray2.20A93-289[»]
ProteinModelPortaliP02340.
SMRiP02340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204323. 86 interactors.
DIPiDIP-369N.
IntActiP02340. 37 interactors.
MINTiMINT-120104.
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

EnsembliENSMUST00000005371; ENSMUSP00000005371; ENSMUSG00000059552.
GeneIDi22059.
KEGGimmu:22059.
UCSCiuc007jql.2. mouse.

Organism-specific databases

CTDi22059.
MGIiMGI:98834. Trp53.

Phylogenomic databases

eggNOGiENOG410IITK. Eukaryota.
ENOG410ZSWV. LUCA.
GeneTreeiENSGT00390000015092.
HOGENOMiHOG000039957.
HOVERGENiHBG005201.
InParanoidiP02340.
KOiK04451.

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.

Miscellaneous databases

EvolutionaryTraceiP02340.
PROiP02340.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000059552.
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.
InterProiIPR008967. p53-like_TF_DNA-bd.
IPR012346. p53/RUNT-type_TF_DNA-bd.
IPR011615. p53_DNA-bd.
IPR010991. p53_tetrameristn.
IPR013872. p53_transactivation_domain.
IPR002117. p53_tumour_suppressor.
[Graphical view]
PANTHERiPTHR11447. PTHR11447. 1 hit.
PfamiPF00870. P53. 1 hit.
PF08563. P53_TAD. 1 hit.
PF07710. P53_tetramer. 1 hit.
[Graphical view]
PRINTSiPR00386. P53SUPPRESSR.
SUPFAMiSSF47719. SSF47719. 1 hit.
SSF49417. SSF49417. 1 hit.
PROSITEiPS00348. P53. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiP53_MOUSE
AccessioniPrimary (citable) accession number: P02340
Secondary accession number(s): Q9QUP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 18, 2008
Last modified: November 30, 2016
This is version 212 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.