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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)LengthDescriptionGraphical viewFeature identifierActions
Sitei114 – 1141Interaction with DNA
Metal bindingi170 – 1701Zinc
Metal bindingi173 – 1731Zinc
Metal bindingi232 – 2321Zinc
Metal bindingi236 – 2361Zinc

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi96 – 286191By similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: MGI
  • B cell lineage commitment Source: MGI
  • cell aging Source: UniProtKB
  • cell cycle arrest Source: MGI
  • cellular protein localization Source: MGI
  • cellular response to DNA damage stimulus 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
  • 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 organismal 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 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 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 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 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
  • transcription from RNA polymerase II promoter Source: GOC
  • 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

ReactomeiREACT_271804. Stabilization of p53.
REACT_280010. Factors involved in megakaryocyte development and platelet production.
REACT_299120. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_305463. Oxidative Stress Induced Senescence.
REACT_316610. DNA Damage/Telomere Stress Induced Senescence.
REACT_339940. Oncogene Induced Senescence.
REACT_341685. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

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
ProteomesiUP000000589 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
  • 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 387387Cellular tumor antigen p53PRO_0000185709Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91Phosphoserine; by HIPK41 Publication
Modified residuei15 – 151Phosphoserine; by CDK5, PRPK, AMPK, NUAK1 and ATM1 Publication
Modified residuei18 – 181Phosphothreonine; by CK1, VRK1 and VRK2By similarity
Modified residuei20 – 201Phosphoserine; by CHEK2, CK1 and PLK3By similarity
Modified residuei34 – 341Phosphoserine; by MAPKAPK51 Publication
Modified residuei114 – 1141N6-acetyllysine; by KAT6ABy similarity
Modified residuei177 – 1771Phosphoserine; by AURKBBy similarity
Modified residuei263 – 2631Phosphoserine; by AURKBBy similarity
Modified residuei278 – 2781Phosphothreonine; by AURKBBy similarity
Cross-linki285 – 285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki286 – 286Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei299 – 2991N6-acetyllysineBy similarity
Modified residuei309 – 3091Phosphoserine; by AURKA, CDK1 and CDK2By similarity
Modified residuei315 – 3151N6-acetyllysine1 Publication
Modified residuei364 – 3641N6,N6-dimethyllysine; alternateBy similarity
Modified residuei364 – 3641N6-methyllysine; by SMYD2; alternateBy similarity
Modified residuei366 – 3661N6-methyllysine; by SETD7By similarity
Modified residuei367 – 3671N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternateBy similarity
Modified residuei367 – 3671N6-acetyllysine; alternateBy similarity
Modified residuei375 – 3751N6-acetyllysineBy similarity
Modified residuei376 – 3761N6,N6-dimethyllysine; alternateBy similarity
Modified residuei376 – 3761N6-acetyllysine; by KAT6A; alternateBy similarity
Modified residuei376 – 3761N6-methyllysine; by SETD8; alternateBy similarity
Cross-linki380 – 380Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei386 – 3861Phosphoserine; by CK2, CDK2 and NUAK1By similarity

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 SETD8, 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

MaxQBiP02340.
PRIDEiP02340.

PTM databases

PhosphoSiteiP02340.

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

BgeeiP02340.
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 (By similarity). 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 (By similarity). Interacts with KAT6A (By similarity). Interacts with UBC9 (By similarity). Forms a complex with UBC9 and PRKRA (By similarity). Interacts with ZNF385B; the interaction is direct (By similarity). 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 (By similarity). Interacts with RFFL and RNF34; involved in p53/TP53 ubiquitination. Interacts with MTA1 and RFWD2. Interacts with CCAR2 (via N-terminus) (By similarity).By similarity

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

Protein-protein interaction databases

BioGridi204323. 84 interactions.
DIPiDIP-369N.
IntActiP02340. 37 interactions.
MINTiMINT-120104.
STRINGi10090.ENSMUSP00000104298.

Structurei

Secondary structure

1
387
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi99 – 1013Combined sources
Beta strandi104 – 1063Combined sources
Helixi113 – 1164Combined sources
Beta strandi117 – 1215Combined sources
Turni122 – 1254Combined sources
Beta strandi126 – 1294Combined sources
Beta strandi134 – 1407Combined sources
Beta strandi150 – 15910Combined sources
Turni160 – 1645Combined sources
Helixi171 – 1755Combined sources
Beta strandi181 – 1833Combined sources
Beta strandi188 – 1936Combined sources
Beta strandi198 – 2014Combined sources
Turni203 – 2053Combined sources
Beta strandi208 – 2136Combined sources
Beta strandi222 – 2309Combined sources
Helixi235 – 2373Combined sources
Helixi239 – 2424Combined sources
Beta strandi245 – 2528Combined sources
Beta strandi258 – 26811Combined sources
Helixi272 – 28312Combined sources
Turni285 – 2873Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HU8X-ray2.70A/B/C96-281[»]
2GEQX-ray2.30A/B89-289[»]
2IOIX-ray1.55A92-289[»]
2IOMX-ray2.00A92-289[»]
2IOOX-ray2.02A92-289[»]
2P52X-ray1.50A89-284[»]
3EXJX-ray2.00A/B93-289[»]
3EXLX-ray2.20A93-289[»]
ProteinModelPortaliP02340.
SMRiP02340. Positions 88-350.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02340.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 314314Interaction with CCAR2By similarityAdd
BLAST
Regioni1 – 4242Transcription activation (acidic)Add
BLAST
Regioni60 – 10445Interaction with WWOXBy similarityAdd
BLAST
Regioni94 – 364271Interaction with HIPK1Add
BLAST
Regioni94 – 294201Required for interaction with ZNF385ABy similarityAdd
BLAST
Regioni107 – 230124Required for interaction with FBXO42By similarityAdd
BLAST
Regioni110 – 286177Interaction with AXIN1Add
BLAST
Regioni253 – 29139Interaction with E4F1By similarityAdd
BLAST
Regioni267 – 2748Interaction with DNA
Regioni313 – 35442Interaction with HIPK2By similarityAdd
BLAST
Regioni319 – 35032OligomerizationAdd
BLAST
Regioni353 – 3575Interaction with USP7By similarity
Regioni362 – 38120Basic (repression of DNA-binding)Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi299 – 31517Bipartite nuclear localization signalBy similarityAdd
BLAST
Motifi333 – 34412Nuclear export signalBy similarityAdd
BLAST
Motifi364 – 3663[KR]-[STA]-K motif

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

eggNOGiNOG80479.
GeneTreeiENSGT00390000015092.
HOGENOMiHOG000039957.
HOVERGENiHBG005201.
InParanoidiP02340.
KOiK04451.
OrthoDBiEOG7JQBNW.

Family and domain databases

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451Q → R in CAA25323 (PubMed:6379601).Curated
Sequence conflicti76 – 783PVA → QW in CAA25323 (PubMed:6379601).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti132 – 1321A → V Can cooperate with an activated Ras to transform fibroblasts. 1 Publication
Natural varianti165 – 1651E → G in clone P53-M11.
Natural varianti188 – 1881L → R.

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_006533157.2.
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_006533157.2.
UniGeneiMm.222.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HU8X-ray2.70A/B/C96-281[»]
2GEQX-ray2.30A/B89-289[»]
2IOIX-ray1.55A92-289[»]
2IOMX-ray2.00A92-289[»]
2IOOX-ray2.02A92-289[»]
2P52X-ray1.50A89-284[»]
3EXJX-ray2.00A/B93-289[»]
3EXLX-ray2.20A93-289[»]
ProteinModelPortaliP02340.
SMRiP02340. Positions 88-350.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204323. 84 interactions.
DIPiDIP-369N.
IntActiP02340. 37 interactions.
MINTiMINT-120104.
STRINGi10090.ENSMUSP00000104298.

Chemistry

ChEMBLiCHEMBL4164.

PTM databases

PhosphoSiteiP02340.

Proteomic databases

MaxQBiP02340.
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

eggNOGiNOG80479.
GeneTreeiENSGT00390000015092.
HOGENOMiHOG000039957.
HOVERGENiHBG005201.
InParanoidiP02340.
KOiK04451.
OrthoDBiEOG7JQBNW.

Enzyme and pathway databases

ReactomeiREACT_271804. Stabilization of p53.
REACT_280010. Factors involved in megakaryocyte development and platelet production.
REACT_299120. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_305463. Oxidative Stress Induced Senescence.
REACT_316610. DNA Damage/Telomere Stress Induced Senescence.
REACT_339940. Oncogene Induced Senescence.
REACT_341685. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

Miscellaneous databases

EvolutionaryTraceiP02340.
NextBioi301858.
PROiP02340.
SOURCEiSearch...

Gene expression databases

BgeeiP02340.
CleanExiMM_TRP53.
ExpressionAtlasiP02340. baseline and differential.
GenevisibleiP02340. MM.

Family and domain databases

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...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the gene coding for the murine cellular tumour antigen p53."
    Bienz B., Zakut-Houri R., Givol D., Oren M.
    EMBO J. 3:2179-2183(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "A single gene and a pseudogene for the cellular tumour antigen p53."
    Zakut-Houri R., Oren M., Bienz B., Lavie V., Hazum S., Givol D.
    Nature 306:594-597(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning and expression analysis of full length mouse cDNA sequences encoding the transformation associated protein p53."
    Jenkins J.R., Rudge K., Redmond S., Wade-Evans A.
    Nucleic Acids Res. 12:5609-5626(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Immunologically distinct p53 molecules generated by alternative splicing."
    Arai N., Nomura D., Yokota K., Wolf D., Brill E., Shohat O., Rotter V.
    Mol. Cell. Biol. 6:3232-3239(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (CLONES PCD53; P53-M11 AND P53-M8).
  5. "Primary structure of DNA complementary to mRNA of murine oncoprotein p53."
    Chumakov P.M.
    Bioorg. Khim. 13:1691-1694(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-132.
  6. "Cell cycle in DNA-PKcs knock-out mice."
    Araki R., Fukumura R., Fujimori A., Tatsumi K., Abe M.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: SCID.
  7. "DNA-dependent protein kinase is not required for the p53-dependent response to DNA damage."
    Jimenez G.S., Bryntesson F., Torres-Arzayus M.I., Priestley A., Beeche M., Saito S., Sakaguchi K., Appella E., Jeggo P.A., Taccioli G.E., Wahl G.M., Hubank M.
    Nature 400:81-83(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  8. "Characterization of DNA-PKcs null mutant SX9."
    Araki R., Fukumura R., Fujimori A., Tatsumi K., Abe M.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Mammary carcinoma.
  9. "p53 in 129-SVJ mice."
    Fujimori A., Abe M.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129/SvJ.
    Tissue: Lung fibroblast.
  10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary gland.
  11. "Loss of heterozygosity and mutational alterations of the p53 gene in skin tumours of interspecific hybrid mice."
    Burns P.A., Kemp C.J., Gannon J.V., Lane D.P., Bremner R., Balmain A.
    Oncogene 6:2363-2369(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 219-255.
  12. "Detection of a transformation-related antigen in chemically induced sarcomas and other transformed cells of the mouse."
    DeLeo A.B., Jay G., Appella E., Dubois G.C., Law L.W., Old L.J.
    Proc. Natl. Acad. Sci. U.S.A. 76:2420-2424(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISCOVERY OF P53.
  13. Cited for: INTERACTION WITH E4F1.
  14. "Characterization of cells and gene-targeted mice deficient for the p53-binding kinase homeodomain-interacting protein kinase 1 (HIPK1)."
    Kondo S., Lu Y., Debbas M., Lin A.W., Sarosi I., Itie A., Wakeham A., Tuan J., Saris C., Elliott G., Ma W., Benchimol S., Lowe S.W., Mak T.W., Thukral S.K.
    Proc. Natl. Acad. Sci. U.S.A. 100:5431-5436(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIPK1, PHOSPHORYLATION.
  15. "Axin stimulates p53 functions by activation of HIPK2 kinase through multimeric complex formation."
    Rui Y., Xu Z., Lin S., Li Q., Rui H., Luo W., Zhou H.-M., Cheung P.-Y., Wu Z., Ye Z., Li P., Han J., Lin S.-C.
    EMBO J. 23:4583-4594(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AXIN1, IDENTIFICATION IN A COMPLEX WITH HIPK2 AND AXIN1.
  16. "Mapping of phosphomonoester and apparent phosphodiester bonds of the oncogene product p53 from simian virus 40-transformed 3T3 cells."
    Samad A., Anderson C.W., Carroll R.B.
    Proc. Natl. Acad. Sci. U.S.A. 83:897-901(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-309 AND SER-386, RNA-BINDING.
  17. "The p53 tumour suppressor protein is phosphorylated at serine 389 by casein kinase II."
    Meek D.W., Simon S., Kikkawa U., Eckhart W.
    EMBO J. 9:3253-3260(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-386.
  18. "p53 is covalently linked to 5.8S rRNA."
    Fontoura B.M., Sorokina E.A., David E., Carroll R.B.
    Mol. Cell. Biol. 12:5145-5151(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PUTATIVE RNA-BINDING.
  19. "Negative control of p53 by Sir2alpha promotes cell survival under stress."
    Luo J., Nikolaev A.Y., Imai S., Chen D., Su F., Shiloh A., Guarente L., Gu W.
    Cell 107:137-148(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEACETYLATION BY SIRT1.
  20. "Identification and characterization of murine mHAUSP encoding a deubiquitinating enzyme that regulates the status of p53 ubiquitination."
    Lim S.-K., Shin J.-M., Kim Y.-S., Baek K.-H.
    Int. J. Oncol. 24:357-364(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH USP7.
  21. "Differential effect of ik3-1/cables on p53- and p73-induced cell death."
    Tsuji K., Mizumoto K., Yamochi T., Nishimoto I., Matsuoka M.
    J. Biol. Chem. 277:2951-2957(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH CABLES1 AND TP73.
  22. "Direct interaction with and activation of p53 by SMAR1 retards cell-cycle progression at G2/M phase and delays tumor growth in mice."
    Kaul R., Mukherjee S., Ahmed F., Bhat M.K., Chhipa R., Galande S., Chattopadhyay S.
    Int. J. Cancer 103:606-615(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BANP.
  23. "PML regulates p53 stability by sequestering Mdm2 to the nucleolus."
    Bernardi R., Scaglioni P.P., Bergmann S., Horn H.F., Vousden K.H., Pandolfi P.P.
    Nat. Cell Biol. 6:665-672(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-15, LYSINE ACETYLATION, UBIQUITINATION, SUBCELLULAR LOCATION.
  24. Cited for: PHOSPHORYLATION AT SER-34.
  25. "Hzf Determines cell survival upon genotoxic stress by modulating p53 transactivation."
    Das S., Raj L., Zhao B., Kimura Y., Bernstein A., Aaronson S.A., Lee S.W.
    Cell 130:624-637(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZNF385A.
  26. "Novel homeodomain-interacting protein kinase family member, HIPK4, phosphorylates human p53 at serine 9."
    Arai S., Matsushita A., Du K., Yagi K., Okazaki Y., Kurokawa R.
    FEBS Lett. 581:5649-5657(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-9.
  27. "CHD8 suppresses p53-mediated apoptosis through histone H1 recruitment during early embryogenesis."
    Nishiyama M., Oshikawa K., Tsukada Y.I., Nakagawa T., Iemura S., Natsume T., Fan Y., Kikuchi A., Skoultchi A.I., Nakayama K.I.
    Nat. Cell Biol. 11:172-182(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHD8.
  28. Cited for: FUNCTION, UBIQUITINATION, INTERACTION WITH TRIM24.
  29. "A large intergenic noncoding RNA induced by p53 mediates global gene repression in the p53 response."
    Huarte M., Guttman M., Feldser D., Garber M., Koziol M.J., Kenzelmann-Broz D., Khalil A.M., Zuk O., Amit I., Rabani M., Attardi L.D., Regev A., Lander E.S., Jacks T., Rinn J.L.
    Cell 142:409-419(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  30. "p53 opens the mitochondrial permeability transition pore to trigger necrosis."
    Vaseva A.V., Marchenko N.D., Ji K., Tsirka S.E., Holzmann S., Moll U.M.
    Cell 149:1536-1548(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  31. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  32. "p53 regulates Period2 expression and the circadian clock."
    Miki T., Matsumoto T., Zhao Z., Lee C.C.
    Nat. Commun. 4:2444-2444(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  33. "DBC1 functions as a tumor suppressor by regulating p53 stability."
    Qin B., Minter-Dykhouse K., Yu J., Zhang J., Liu T., Zhang H., Lee S., Kim J., Wang L., Lou Z.
    Cell Rep. 10:1324-1334(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, PROTEASOMAL DEGRADATION.
  34. "Crystal structure of the mouse p53 core DNA-binding domain at 2.7 A resolution."
    Zhao K., Chai X., Johnston K., Clements A., Marmorstein R.
    J. Biol. Chem. 276:12120-12127(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 96-281.
  35. "High-resolution structure of the p53 core domain: implications for binding small-molecule stabilizing compounds."
    Ho W.C., Luo C., Zhao K., Chai X., Fitzgerald M.X., Marmorstein R.
    Acta Crystallogr. D 62:1484-1493(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 92-289.
  36. "Structure of the p53 core domain dimer bound to DNA."
    Ho W.C., Fitzgerald M.X., Marmorstein R.
    J. Biol. Chem. 281:20494-20502(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 92-289 IN COMPLEX WITH DNA AND ZINC IONS, SUBUNIT.
  37. "Crystal structure of the mouse p53 core domain in zinc-free state."
    Kwon E., Kim D.Y., Suh S.W., Kim K.K.
    Proteins 70:280-283(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 92-284.
  38. "Crystal structure of a p53 core tetramer bound to DNA."
    Malecka K.A., Ho W.C., Marmorstein R.
    Oncogene 28:325-333(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 93-289 IN COMPLEX WITH DNA, SUBUNIT.

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: June 24, 2015
This is version 196 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

External Data

Dasty 3

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 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.