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P02340

- P53_MOUSE

UniProt

P02340 - P53_MOUSE

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Protein
Cellular tumor antigen p53
Gene
Tp53, P53, Trp53
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.3 Publications

Cofactori

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 – 286191 By similarity
Add
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. DNA binding Source: UniProtKB
  3. MDM2/MDM4 family protein binding Source: BHF-UCL
  4. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
  5. RNA polymerase II core promoter sequence-specific DNA binding Source: MGI
  6. chromatin binding Source: MGI
  7. copper ion binding Source: UniProtKB
  8. damaged DNA binding Source: RefGenome
  9. double-stranded DNA binding Source: RefGenome
  10. histone deacetylase regulator activity Source: MGI
  11. p53 binding Source: RefGenome
  12. protein binding Source: UniProtKB
  13. sequence-specific DNA binding Source: RefGenome
  14. sequence-specific DNA binding transcription factor activity Source: MGI

GO - Biological processi

  1. B cell lineage commitment Source: MGI
  2. DNA damage response, signal transduction by p53 class mediator Source: MGI
  3. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: MGI
  4. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: RefGenome
  5. DNA strand renaturation Source: UniProtKB
  6. T cell differentiation in thymus Source: MGI
  7. T cell lineage commitment Source: MGI
  8. T cell proliferation involved in immune response Source: MGI
  9. apoptotic process Source: MGI
  10. cell aging Source: UniProtKB
  11. cellular response to DNA damage stimulus Source: MGI
  12. cellular response to UV Source: MGI
  13. cellular response to ionizing radiation Source: MGI
  14. central nervous system development Source: MGI
  15. cerebellum development Source: MGI
  16. chromosome organization Source: MGI
  17. determination of adult lifespan Source: BHF-UCL
  18. double-strand break repair Source: MGI
  19. embryo development ending in birth or egg hatching Source: MGI
  20. embryonic organ development Source: MGI
  21. gastrulation Source: MGI
  22. in utero embryonic development Source: MGI
  23. intrinsic apoptotic signaling pathway by p53 class mediator Source: MGI
  24. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: BHF-UCL
  25. mitotic G1 DNA damage checkpoint Source: MGI
  26. mitotic cell cycle arrest Source: MGI
  27. multicellular organism growth Source: MGI
  28. multicellular organismal development Source: UniProtKB
  29. necroptotic process Source: MGI
  30. negative regulation of DNA replication Source: MGI
  31. negative regulation of apoptotic process Source: MGI
  32. negative regulation of cell growth Source: UniProtKB
  33. negative regulation of cell proliferation Source: BHF-UCL
  34. negative regulation of fibroblast proliferation Source: MGI
  35. negative regulation of macromitophagy Source: MGI
  36. negative regulation of neuroblast proliferation Source: MGI
  37. negative regulation of reactive oxygen species metabolic process Source: MGI
  38. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  39. negative regulation of transcription, DNA-templated Source: BHF-UCL
  40. negative regulation of transforming growth factor beta receptor signaling pathway Source: MGI
  41. neuron apoptotic process Source: MGI
  42. nucleotide-excision repair Source: UniProtKB
  43. oligodendrocyte apoptotic process Source: UniProtKB
  44. positive regulation of apoptotic process Source: MGI
  45. positive regulation of cardiac muscle cell apoptotic process Source: MGI
  46. positive regulation of cell aging Source: BHF-UCL
  47. positive regulation of histone deacetylation Source: MGI
  48. positive regulation of mitochondrial membrane permeability Source: MGI
  49. positive regulation of neuron apoptotic process Source: MGI
  50. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  51. positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
  52. positive regulation of thymocyte apoptotic process Source: BHF-UCL
  53. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  54. positive regulation of transcription, DNA-templated Source: MGI
  55. protein import into nucleus, translocation Source: MGI
  56. protein tetramerization Source: InterPro
  57. rRNA transcription Source: MGI
  58. regulation of cell cycle Source: MGI
  59. regulation of cell proliferation Source: MGI
  60. regulation of mitochondrial membrane permeability involved in apoptotic process Source: MGI
  61. regulation of neuron apoptotic process Source: MGI
  62. regulation of thymocyte apoptotic process Source: MGI
  63. regulation of tissue remodeling Source: MGI
  64. regulation of transcription from RNA polymerase II promoter Source: MGI
  65. regulation of transcription, DNA-templated Source: MGI
  66. release of cytochrome c from mitochondria Source: MGI
  67. response to UV Source: MGI
  68. response to X-ray Source: MGI
  69. response to drug Source: MGI
  70. response to gamma radiation Source: MGI
  71. response to ischemia Source: MGI
  72. response to oxidative stress Source: MGI
  73. response to salt stress Source: MGI
  74. somitogenesis Source: MGI
  75. transforming growth factor beta receptor signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Apoptosis, Cell cycle, Necrosis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_188819. DNA Damage/Telomere Stress Induced Senescence.
REACT_188970. Oxidative Stress Induced Senescence.
REACT_188971. Oncogene Induced Senescence.
REACT_198649. Factors involved in megakaryocyte development and platelet production.
REACT_209428. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.

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: Chromosome 11

Organism-specific databases

MGIiMGI:98834. Trp53.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity. Endoplasmic reticulum By similarity. Mitochondrion matrix By similarity
Note: Interaction with BANP promotes nuclear localization. Translocates to mitochondria upon oxidative stress By similarity.1 Publication

GO - Cellular componenti

  1. chromatin Source: RefGenome
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: MGI
  4. endoplasmic reticulum Source: UniProtKB-SubCell
  5. mitochondrial matrix Source: MGI
  6. mitochondrion Source: UniProtKB
  7. nucleolus Source: UniProtKB
  8. nucleus Source: UniProtKB
  9. replication fork Source: MGI
  10. transcription factor complex Source: RefGenome
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 p53
PRO_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 VRK2 By similarity
Modified residuei20 – 201Phosphoserine; by CHEK2, CK1 and PLK3 By similarity
Modified residuei34 – 341Phosphoserine; by MAPKAPK51 Publication
Modified residuei114 – 1141N6-acetyllysine; by KAT6A By similarity
Modified residuei177 – 1771Phosphoserine; by AURKB By similarity
Modified residuei263 – 2631Phosphoserine; by AURKB By similarity
Modified residuei278 – 2781Phosphothreonine; by AURKB By 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-acetyllysine By similarity
Modified residuei309 – 3091Phosphoserine; by AURKA, CDK1 and CDK2 By similarity
Modified residuei315 – 3151N6-acetyllysine1 Publication
Modified residuei364 – 3641N6,N6-dimethyllysine; alternate By similarity
Modified residuei364 – 3641N6-methyllysine; by SMYD2; alternate By similarity
Modified residuei366 – 3661N6-methyllysine; by SETD7 By similarity
Modified residuei367 – 3671N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternate By similarity
Modified residuei367 – 3671N6-acetyllysine; alternate By similarity
Modified residuei375 – 3751N6-acetyllysine By similarity
Modified residuei376 – 3761N6,N6-dimethyllysine; alternate By similarity
Modified residuei376 – 3761N6-acetyllysine; by KAT6A; alternate By similarity
Modified residuei376 – 3761N6-methyllysine; by SETD8; alternate By similarity
Cross-linki380 – 380Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Modified residuei386 – 3861Phosphoserine; by CK2, CDK2 and NUAK1 By 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 HIPK1.6 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.
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 and RFFL, which leads to proteasomal degradation. Ubiquitination by TOPORS induces degradation. Deubiquitination by USP7, leading to stabilize it By similarity.2 Publications
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.
Sumoylated with SUMO1. Sumoylated at Lys-380 by UBC9 By similarity.

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP02340.

PTM databases

PhosphoSiteiP02340.

Expressioni

Gene expression databases

ArrayExpressiP02340.
BgeeiP02340.
CleanExiMM_TRP53.
GenevestigatoriP02340.

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 (via RING-type zinc finger); involved in p53/TP53 ubiquitination By similarity.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P0307012EBI-474016,EBI-617698From a different organism.
BCL2L1Q07817-13EBI-474016,EBI-287195From a different organism.
Mdm2P238043EBI-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. 80 interactions.
DIPiDIP-369N.
IntActiP02340. 36 interactions.
MINTiMINT-120104.
STRINGi10090.ENSMUSP00000104298.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP02340.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 4242Transcription activation (acidic)
Add
BLAST
Regioni60 – 10445Interaction with WWOX By similarity
Add
BLAST
Regioni94 – 364271Interaction with HIPK1
Add
BLAST
Regioni94 – 294201Required for interaction with ZNF385A By similarity
Add
BLAST
Regioni107 – 230124Required for interaction with FBXO42 By similarity
Add
BLAST
Regioni110 – 286177Interaction with AXIN1
Add
BLAST
Regioni253 – 29139Interaction with E4F1 By similarity
Add
BLAST
Regioni267 – 2748Interaction with DNA
Regioni313 – 35442Interaction with HIPK2 By similarity
Add
BLAST
Regioni319 – 35032Oligomerization
Add
BLAST
Regioni353 – 3575Interaction with USP7 By similarity
Regioni362 – 38120Basic (repression of DNA-binding)
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi299 – 31517Bipartite nuclear localization signal By similarity
Add
BLAST
Motifi333 – 34412Nuclear export signal By similarity
Add
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.

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

MEESQSDISL ELPLSQETFS GLWKLLPPED ILPSPHCMDD LLLPQDVEEF    50
FEGPSEALRV SGAPAAQDPV TETPGPVAPA PATPWPLSSF VPSQKTYQGN 100
YGFHLGFLQS GTAKSVMCTY SPPLNKLFCQ LAKTCPVQLW VSATPPAGSR 150
VRAMAIYKKS QHMTEVVRRC PHHERCSDGD GLAPPQHLIR VEGNLYPEYL 200
EDRQTFRHSV VVPYEPPEAG SEYTTIHYKY MCNSSCMGGM NRRPILTIIT 250
LEDSSGNLLG RDSFEVRVCA CPGRDRRTEE ENFRKKEVLC PELPPGSAKR 300
ALPTCTSASP PQKKKPLDGE YFTLKIRGRK RFEMFRELNE ALELKDAHAT 350
EESGDSRAHS SYLKTKKGQS TSRHKKTMVK KVGPDSD 387
Length:387
Mass (Da):43,155
Last modified:March 18, 2008 - v3
Checksum:iB55EB7B463E1DD9D
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451Q → R in CAA25323. 1 Publication
Sequence conflicti76 – 783PVA → QW in CAA25323. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006533157.1.
XP_006533221.1. XM_006533158.1.
UniGeneiMm.222.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A22739. DNMS53.
S38824.
RefSeqi NP_001120705.1. NM_001127233.1.
NP_035770.2. NM_011640.3.
XP_006533220.1. XM_006533157.1.
XP_006533221.1. XM_006533158.1.
UniGenei Mm.222.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HU8 X-ray 2.70 A/B/C 96-281 [» ]
2GEQ X-ray 2.30 A/B 89-289 [» ]
2IOI X-ray 1.55 A 92-289 [» ]
2IOM X-ray 2.00 A 92-289 [» ]
2IOO X-ray 2.02 A 92-289 [» ]
2P52 X-ray 1.50 A 89-284 [» ]
3EXJ X-ray 2.00 A/B 93-289 [» ]
3EXL X-ray 2.20 A 93-289 [» ]
ProteinModelPortali P02340.
SMRi P02340. Positions 88-350.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204323. 80 interactions.
DIPi DIP-369N.
IntActi P02340. 36 interactions.
MINTi MINT-120104.
STRINGi 10090.ENSMUSP00000104298.

Chemistry

ChEMBLi CHEMBL4164.

PTM databases

PhosphoSitei P02340.

Proteomic databases

PRIDEi P02340.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000005371 ; ENSMUSP00000005371 ; ENSMUSG00000059552 .
GeneIDi 22059.
KEGGi mmu:22059.
UCSCi uc007jql.2. mouse.

Organism-specific databases

CTDi 22059.
MGIi MGI:98834. Trp53.

Phylogenomic databases

eggNOGi NOG80479.
GeneTreei ENSGT00390000015092.
HOGENOMi HOG000039957.
HOVERGENi HBG005201.
InParanoidi P02340.
KOi K04451.
OrthoDBi EOG7JQBNW.

Enzyme and pathway databases

Reactomei REACT_188819. DNA Damage/Telomere Stress Induced Senescence.
REACT_188970. Oxidative Stress Induced Senescence.
REACT_188971. Oncogene Induced Senescence.
REACT_198649. Factors involved in megakaryocyte development and platelet production.
REACT_209428. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.

Miscellaneous databases

EvolutionaryTracei P02340.
NextBioi 301858.
PROi P02340.
SOURCEi Search...

Gene expression databases

ArrayExpressi P02340.
Bgeei P02340.
CleanExi MM_TRP53.
Genevestigatori P02340.

Family and domain databases

Gene3Di 2.60.40.720. 1 hit.
4.10.170.10. 1 hit.
InterProi IPR008967. 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 ]
PANTHERi PTHR11447. PTHR11447. 1 hit.
Pfami PF00870. P53. 1 hit.
PF08563. P53_TAD. 1 hit.
PF07710. P53_tetramer. 1 hit.
[Graphical view ]
PRINTSi PR00386. P53SUPPRESSR.
SUPFAMi SSF47719. SSF47719. 1 hit.
SSF49417. SSF49417. 1 hit.
PROSITEi PS00348. P53. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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.
  33. "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.
  34. "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.
  35. "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.
  36. "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: September 3, 2014
This is version 186 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

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