P02340 (P53_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 157.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Cellular tumor antigen p53 Alternative name(s): Tumor suppressor p53 | ||||
| Gene names |
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| 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
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 | ||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||
| 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
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References
| « Hide '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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| EMBL GenBank DDBJ | X00876 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 |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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 |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with