P02340 (P53_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cellular tumor antigen p53

Alternative name(s):
Tumor suppressor p53

Gene names

Name:	Tp53
Synonyms:	P53, Trp53

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	387 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression By similarity. Ref.27
Cofactor	Binds 1 zinc ion per subunit.
Subunit structure	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 P53DINP1. 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 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 ubiquination and degradation of TP53. Interacts with DAXX. Interacts (when monomethylated at Lys-376) with L3MBTL1 By similarity. 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 By similarity. Ref.13 Ref.14 Ref.15 Ref.20 Ref.22 Ref.26 Ref.27 Ref.30 Ref.32
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Endoplasmic reticulum By similarity. Nucleus › PML body By similarity. Note: Interaction with BANP promotes nuclear localization. Recruited into PML bodies together with CHEK2 By similarity. Ref.23
Domain	The [KR]-[STA]-K motif is specifically recognized by the SETD7 methyltransferase By similarity.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. 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. Ref.14 Ref.16 Ref.17 Ref.23 Ref.25 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, which leads to proteasomal degradation. Ubiquitination by TOPORS induces degradation. Deubiquitination by USP7, leading to stabilize it By similarity. Ref.23 Ref.27 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 by SUMO1 By similarity.
Involvement in disease	Note=p53 is found in increased amounts in a wide variety of transformed cells. p53 is frequently mutated or inactivated in many types of cancer.
Sequence similarities	Belongs to the p53 family.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle Transcription Transcription regulation
Cellular component	Cytoplasm Endoplasmic reticulum Nucleus
Disease	Disease mutation Tumor suppressor
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	B cell lineage commitment Inferred from mutant phenotype. Source: MGI DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Inferred from genetic interaction. Source: MGI DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis Inferred from mutant phenotype. Source: BHF-UCL DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Inferred from Biological aspect of Ancestor. Source: RefGenome T cell differentiation in thymus Inferred from genetic interaction. Source: MGI T cell lineage commitment Inferred from mutant phenotype. Source: MGI T cell proliferation involved in immune response Inferred from genetic interaction. Source: MGI activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c Inferred from sequence or structural similarity. Source: UniProtKB cell aging Inferred from sequence or structural similarity. Source: UniProtKB cellular response to UV Inferred from genetic interaction. Source: MGI central nervous system development Inferred from genetic interaction. Source: MGI chromosome organization Inferred from genetic interaction. Source: MGI determination of adult lifespan Inferred from mutant phenotype. Source: BHF-UCL double-strand break repair Inferred from mutant phenotype. Source: MGI gastrulation Inferred from genetic interaction. Source: MGI in utero embryonic development Inferred from genetic interaction. Source: MGI mitotic cell cycle arrest Inferred from direct assay. Source: MGI multicellular organism growth Inferred from genetic interaction. Source: MGI negative regulation of DNA replication Inferred from direct assay. Source: MGI negative regulation of apoptotic process Inferred from mutant phenotype. Source: MGI negative regulation of cell growth Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of fibroblast proliferation Inferred from mutant phenotype. Source: MGI negative regulation of neuroblast proliferation Inferred from genetic interaction. Source: MGI negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: BHF-UCL negative regulation of transforming growth factor beta receptor signaling pathway Inferred from mutant phenotype. Source: MGI nucleotide-excision repair Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell aging Inferred from mutant phenotype. Source: BHF-UCL positive regulation of histone deacetylation Inferred from direct assay. Source: MGI positive regulation of neuron apoptosis Inferred from direct assay. Source: MGI positive regulation of peptidyl-tyrosine phosphorylation Inferred from mutant phenotype. Source: BHF-UCL positive regulation of thymocyte apoptosis Inferred from mutant phenotype. Source: BHF-UCL protein import into nucleus, translocation Inferred from direct assay. Source: MGI protein tetramerization Inferred from electronic annotation. Source: InterPro rRNA transcription Inferred from genetic interaction. Source: MGI regulation of mitochondrial membrane permeability Inferred from genetic interaction. Source: MGI release of cytochrome c from mitochondria Inferred from direct assay. Source: MGI response to X-ray Inferred from direct assay. Source: MGI response to drug Inferred from direct assay. Source: MGI response to gamma radiation Inferred from direct assay. Source: MGI somitogenesis Inferred from genetic interaction. Source: MGI
Cellular component	PML body Inferred from electronic annotation. Source: UniProtKB-SubCell chromatin Inferred from Biological aspect of Ancestor. Source: RefGenome cytosol Inferred from direct assay. Source: MGI endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB nucleolus Inferred from sequence or structural similarity. Source: UniProtKB replication fork Inferred from direct assay. Source: MGI transcription factor complex Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB DNA strand annealing activity Inferred from sequence or structural similarity. Source: UniProtKB MDM2 binding Inferred from physical interaction. Source: BHF-UCL RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Inferred from genetic interaction. Source: MGI chromatin binding Inferred from direct assay. Source: MGI copper ion binding Inferred from sequence or structural similarity. Source: UniProtKB damaged DNA binding Inferred from Biological aspect of Ancestor. Source: RefGenome histone deacetylase regulator activity Inferred from direct assay. Source: MGI p53 binding Inferred from Biological aspect of Ancestor. Source: RefGenome sequence-specific DNA binding Inferred from Biological aspect of Ancestor. Source: RefGenome transcription regulatory region DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P03070	7	EBI-474016,EBI-617698	From a different organism.
BCL2L1	Q07817-1	3	EBI-474016,EBI-287195	From a different organism.
Mdm2	P23804	3	EBI-474016,EBI-641788
Mdm2	P23804-1	2	EBI-474016,EBI-3386476
Pin1	Q9QUR7	3	EBI-474016,EBI-2432975
Smarcd1	Q61466	4	EBI-474016,EBI-371529

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 387

387

Cellular tumor antigen p53

PRO_0000185709

Regions

DNA binding

96 – 286

191

By similarity

Region

1 – 42

42

Transcription activation (acidic)

Region

60 – 104

45

Interaction with WWOX By similarity

Region

94 – 364

271

Interaction with HIPK1

Region

107 – 230

124

Required for interaction with FBXO42 By similarity

Region

110 – 286

177

Interaction with AXIN1

Region

253 – 291

39

Interaction with E4F1 By similarity

Region

267 – 274

8

Interaction with DNA

Region

313 – 354

42

Interaction with HIPK2 By similarity

Region

319 – 350

32

Oligomerization

Region

353 – 357

5

Interaction with USP7 By similarity

Region

362 – 381

20

Basic (repression of DNA-binding)

Motif

299 – 315

17

Bipartite nuclear localization signal By similarity

Motif

333 – 344

12

Nuclear export signal By similarity

Motif

364 – 366

3

[KR]-[STA]-K motif

Sites

Metal binding

170

1

Zinc

Metal binding

173

1

Zinc

Metal binding

232

1

Zinc

Metal binding

236

1

Zinc

Site

114

1

Interaction with DNA

Amino acid modifications

Modified residue

9

1

Phosphoserine; by HIPK4 Ref.25

Modified residue

15

1

Phosphoserine; by CDK5, PRPK, AMPK, NUAK1 and ATM Ref.23

Modified residue

18

1

Phosphothreonine; by CK1, VRK1 and VRK2 By similarity

Modified residue

20

1

Phosphoserine; by CHEK2, CK1 and PLK3 By similarity

Modified residue

34

1

Phosphoserine; by MAPKAPK5

Modified residue

93

1

Phosphoserine By similarity

Modified residue

177

1

Phosphoserine; by AURKB By similarity

Modified residue

263

1

Phosphoserine; by AURKB By similarity

Modified residue

278

1

Phosphothreonine; by AURKB By similarity

Modified residue

286

1

N6-acetyllysine By similarity

Modified residue

299

1

N6-acetyllysine By similarity

Modified residue

307

1

Phosphoserine By similarity

Modified residue

309

1

Phosphoserine; by AURKA, CDK1 and CDK2 By similarity

Modified residue

364

1

N6,N6-dimethyllysine; alternate By similarity

Modified residue

364

1

N6-methyllysine; by SMYD2; alternate By similarity

Modified residue

366

1

N6-methyllysine; by SETD7 By similarity

Modified residue

367

1

N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternate By similarity

Modified residue

367

1

N6-acetyllysine; alternate By similarity

Modified residue

376

1

N6-acetyllysine; alternate By similarity

Modified residue

376

1

N6-methyllysine; by SETD8; alternate By similarity

Modified residue

386

1

Phosphoserine; by CK2, CDK2 and NUAK1 By similarity

Cross-link

285

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

286

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

380

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Natural variant

132

1

A → V Can cooperate with an activated Ras to transform fibroblasts. Ref.5

Natural variant

165

1

E → G in clone P53-M11.

Natural variant

188

1

L → R.

Experimental info

Sequence conflict

45

1

Q → R in CAA25323. Ref.3

Sequence conflict

76 – 78

3

PVA → QW in CAA25323. Ref.3

Secondary structure

1

.

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387

Helix Strand Turn

Details...

Helix

102 – 104

3

Beta strand

107 – 109

3

Beta strand

121 – 124

4

Turn

125 – 128

4

Beta strand

129 – 132

4

Beta strand

138 – 143

6

Beta strand

153 – 162

10

Turn

163 – 167

5

Helix

174 – 177

4

Beta strand

184 – 186

3

Beta strand

191 – 196

6

Beta strand

201 – 204

4

Turn

206 – 208

3

Beta strand

211 – 216

6

Beta strand

225 – 233

9

Turn

240 – 245

6

Beta strand

248 – 255

8

Beta strand

261 – 271

11

Helix

275 – 284

10

Sequences

	Sequence		Length	Mass (Da)
	P02340 [UniParc]. Last modified March 18, 2008. Version 3. Checksum: B55EB7B463E1DD9D	FASTA	387	43,155
	10 20 30 40 50 60 MEESQSDISL ELPLSQETFS GLWKLLPPED ILPSPHCMDD LLLPQDVEEF FEGPSEALRV 70 80 90 100 110 120 SGAPAAQDPV TETPGPVAPA PATPWPLSSF VPSQKTYQGN YGFHLGFLQS GTAKSVMCTY 130 140 150 160 170 180 SPPLNKLFCQ LAKTCPVQLW VSATPPAGSR VRAMAIYKKS QHMTEVVRRC PHHERCSDGD 190 200 210 220 230 240 GLAPPQHLIR VEGNLYPEYL EDRQTFRHSV VVPYEPPEAG SEYTTIHYKY MCNSSCMGGM 250 260 270 280 290 300 NRRPILTIIT LEDSSGNLLG RDSFEVRVCA CPGRDRRTEE ENFRKKEVLC PELPPGSAKR 310 320 330 340 350 360 ALPTCTSASP PQKKKPLDGE YFTLKIRGRK RFEMFRELNE ALELKDAHAT EESGDSRAHS 370 380 SYLKTKKGQS TSRHKKTMVK KVGPDSD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 6092064] [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: 6646235] [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: 6379601] [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: 3023970] [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: 3329909] [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: 10403253] [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: 15489334] [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: 1766680] [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: 221923] [Abstract] Cited for: DISCOVERY OF P53.
[13]	"p53 is involved in the p120E4F-mediated growth arrest." Sandy P., Gostissa M., Fogal V., Cecco L.D., Szalay K., Rooney R.J., Schneider C., Del Sal G. Oncogene 19:188-199(2000) [PubMed: 10644996] [Abstract] 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: 12702766] [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: 15526030] [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: 3006031] [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: 2145148] [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: 1406686] [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: 11672522] [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: 14719112] [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: 11706030] [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: 12494467] [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: 15195100] [Abstract] Cited for: PHOSPHORYLATION AT SER-15, LYSINE ACETYLATION, UBIQUITINATION, SUBCELLULAR LOCATION.
[24]	"PRAK is essential for ras-induced senescence and tumor suppression." Sun P., Yoshizuka N., New L., Moser B.A., Li Y., Liao R., Xie C., Chen J., Deng Q., Yamout M., Dong M.Q., Frangou C.G., Yates J.R. III, Wright P.E., Han J. Cell 128:295-308(2007) [PubMed: 17254968] [Abstract] Cited for: PHOSPHORYLATION AT SER-34.
[25]	"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: 18022393] [Abstract] Cited for: PHOSPHORYLATION AT SER-9.
[26]	"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: 19151705] [Abstract] Cited for: INTERACTION WITH CHD8.
[27]	"Trim24 targets endogenous p53 for degradation." Allton K., Jain A.K., Herz H.M., Tsai W.W., Jung S.Y., Qin J., Bergmann A., Johnson R.L., Barton M.C. Proc. Natl. Acad. Sci. U.S.A. 106:11612-11616(2009) [PubMed: 19556538] [Abstract] Cited for: FUNCTION, UBIQUITINATION, INTERACTION WITH TRIM24.
[28]	"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: 11152481] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 96-281.
[29]	"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: 17139084] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 92-289.
[30]	"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: 16717092] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 92-289 IN COMPLEX WITH DNA AND ZINC IONS, SUBUNIT.
[31]	"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: 17876829] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 92-284.
[32]	"Crystal structure of a p53 core tetramer bound to DNA." Malecka K.A., Ho W.C., Marmorstein R. Oncogene 28:325-333(2009) [PubMed: 18978813] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 93-289 IN COMPLEX WITH DNA, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00406306.

PIR

DNMS53. A22739.
S38824.

RefSeq

NP_001120705.1. NM_001127233.1.
NP_035770.2. NM_011640.3.

UniGene

Mm.222.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HU8	X-ray	2.70	A/B/C	96-281	[»]
2GEQ	X-ray	2.30	A/B	92-289	[»]
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	92-284	[»]
3EXJ	X-ray	2.00	A/B	93-289	[»]
3EXL	X-ray	2.20	A	93-289	[»]

ProteinModelPortal

P02340.

SMR

P02340. Positions 13-55, 88-350.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-369N.

IntAct

P02340. 23 interactions.

MINT

MINT-120104.

STRING

P02340.

PTM databases

PhosphoSite

P02340.

Proteomic databases

PRIDE

P02340.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000005371; ENSMUSP00000005371; ENSMUSG00000059552.

GeneID

22059.

KEGG

mmu:22059.

Organism-specific databases

CTD

22059.

MGI

MGI:98834. Trp53.

Phylogenomic databases

HOVERGEN

HBG005201.

InParanoid

P02340.

OrthoDB

EOG45757H.

Gene expression databases

ArrayExpress

P02340.

Bgee

P02340.

CleanEx

MM_TRP53.

Genevestigator

P02340.

GermOnline

ENSMUSG00000059552. Mus musculus.

Family and domain databases

InterPro

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]

Gene3D

G3DSA:2.60.40.720. p53_RUNT_DNA_bd. 1 hit.
G3DSA:4.10.170.10. p53_tetrameristn. 1 hit.

KO

K04451.

PANTHER

PTHR11447. Trp53. 1 hit.

Pfam

PF00870. P53. 1 hit.
PF08563. P53_TAD. 1 hit.
PF07710. P53_tetramer. 1 hit.
[Graphical view]

PRINTS

PR00386. P53SUPPRESSR.

SUPFAM

SSF49417. P53_like_DNA_bnd. 1 hit.
SSF47719. p53_tetrameristn. 1 hit.

PROSITE

PS00348. P53. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

SOURCE

Search...

Entry information

Entry name

P53_MOUSE

Accession

Primary (citable) accession number: P02340
Secondary accession number(s): Q9QUP3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	March 18, 2008
Last modified:	January 25, 2012
This is version 157 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program