ID P53_MOUSE Reviewed; 390 AA. AC P02340; Q9QUP3; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2018, sequence version 4. DT 27-NOV-2024, entry version 270. DE RecName: Full=Cellular tumor antigen p53; DE AltName: Full=Tumor suppressor p53; GN Name=Tp53; Synonyms=P53, Trp53; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6092064; DOI=10.1002/j.1460-2075.1984.tb02110.x; RA Bienz B., Zakut-Houri R., Givol D., Oren M.; RT "Analysis of the gene coding for the murine cellular tumour antigen p53."; RL EMBO J. 3:2179-2183(1984). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=6646235; DOI=10.1038/306594a0; RA Zakut-Houri R., Oren M., Bienz B., Lavie V., Hazum S., Givol D.; RT "A single gene and a pseudogene for the cellular tumour antigen p53."; RL Nature 306:594-597(1983). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=6379601; DOI=10.1093/nar/12.14.5609; RA Jenkins J.R., Rudge K., Redmond S., Wade-Evans A.; RT "Cloning and expression analysis of full length mouse cDNA sequences RT encoding the transformation associated protein p53."; RL Nucleic Acids Res. 12:5609-5626(1984). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (CLONES PCD53; P53-M11 AND P53-M8). RX PubMed=3023970; DOI=10.1128/mcb.6.9.3232-3239.1986; RA Arai N., Nomura D., Yokota K., Wolf D., Brill E., Shohat O., Rotter V.; RT "Immunologically distinct p53 molecules generated by alternative RT splicing."; RL Mol. Cell. Biol. 6:3232-3239(1986). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-135. RX PubMed=3329909; RA Chumakov P.M.; RT "Primary structure of DNA complementary to mRNA of murine oncoprotein RT p53."; RL Bioorg. Khim. 13:1691-1694(1987). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=SCID; RA Araki R., Fukumura R., Fujimori A., Tatsumi K., Abe M.; RT "Cell cycle in DNA-PKcs knock-out mice."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=10403253; DOI=10.1038/21913; RA Jimenez G.S., Bryntesson F., Torres-Arzayus M.I., Priestley A., Beeche M., RA Saito S., Sakaguchi K., Appella E., Jeggo P.A., Taccioli G.E., Wahl G.M., RA Hubank M.; RT "DNA-dependent protein kinase is not required for the p53-dependent RT response to DNA damage."; RL Nature 400:81-83(1999). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Mammary carcinoma; RA Araki R., Fukumura R., Fujimori A., Tatsumi K., Abe M.; RT "Characterization of DNA-PKcs null mutant SX9."; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=129/SvJ; TISSUE=Lung fibroblast; RA Fujimori A., Abe M.; RT "p53 in 129-SVJ mice."; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 222-258. RX PubMed=1766680; RA Burns P.A., Kemp C.J., Gannon J.V., Lane D.P., Bremner R., Balmain A.; RT "Loss of heterozygosity and mutational alterations of the p53 gene in skin RT tumours of interspecific hybrid mice."; RL Oncogene 6:2363-2369(1991). RN [12] RP DISCOVERY OF P53. RX PubMed=221923; DOI=10.1073/pnas.76.5.2420; RA DeLeo A.B., Jay G., Appella E., Dubois G.C., Law L.W., Old L.J.; RT "Detection of a transformation-related antigen in chemically induced RT sarcomas and other transformed cells of the mouse."; RL Proc. Natl. Acad. Sci. U.S.A. 76:2420-2424(1979). RN [13] RP INTERACTION WITH E4F1. RX PubMed=10644996; DOI=10.1038/sj.onc.1203250; RA Sandy P., Gostissa M., Fogal V., Cecco L.D., Szalay K., Rooney R.J., RA Schneider C., Del Sal G.; RT "p53 is involved in the p120E4F-mediated growth arrest."; RL Oncogene 19:188-199(2000). RN [14] RP INTERACTION WITH HIPK1, AND PHOSPHORYLATION. RX PubMed=12702766; DOI=10.1073/pnas.0530308100; RA Kondo S., Lu Y., Debbas M., Lin A.W., Sarosi I., Itie A., Wakeham A., RA Tuan J., Saris C., Elliott G., Ma W., Benchimol S., Lowe S.W., Mak T.W., RA Thukral S.K.; RT "Characterization of cells and gene-targeted mice deficient for the p53- RT binding kinase homeodomain-interacting protein kinase 1 (HIPK1)."; RL Proc. Natl. Acad. Sci. U.S.A. 100:5431-5436(2003). RN [15] RP INTERACTION WITH AXIN1, AND IDENTIFICATION IN A COMPLEX WITH HIPK2 AND RP AXIN1. RX PubMed=15526030; DOI=10.1038/sj.emboj.7600475; RA Rui Y., Xu Z., Lin S., Li Q., Rui H., Luo W., Zhou H.-M., Cheung P.-Y., RA Wu Z., Ye Z., Li P., Han J., Lin S.-C.; RT "Axin stimulates p53 functions by activation of HIPK2 kinase through RT multimeric complex formation."; RL EMBO J. 23:4583-4594(2004). RN [16] RP PHOSPHORYLATION AT SER-312 AND SER-389, AND RNA-BINDING. RX PubMed=3006031; DOI=10.1073/pnas.83.4.897; RA Samad A., Anderson C.W., Carroll R.B.; RT "Mapping of phosphomonoester and apparent phosphodiester bonds of the RT oncogene product p53 from simian virus 40-transformed 3T3 cells."; RL Proc. Natl. Acad. Sci. U.S.A. 83:897-901(1986). RN [17] RP PHOSPHORYLATION AT SER-389. RX PubMed=2145148; DOI=10.1002/j.1460-2075.1990.tb07524.x; RA Meek D.W., Simon S., Kikkawa U., Eckhart W.; RT "The p53 tumour suppressor protein is phosphorylated at serine 389 by RT casein kinase II."; RL EMBO J. 9:3253-3260(1990). RN [18] RP PUTATIVE RNA-BINDING. RX PubMed=1406686; DOI=10.1128/mcb.12.11.5145-5151.1992; RA Fontoura B.M., Sorokina E.A., David E., Carroll R.B.; RT "p53 is covalently linked to 5.8S rRNA."; RL Mol. Cell. Biol. 12:5145-5151(1992). RN [19] RP DEACETYLATION BY SIRT1. RX PubMed=11672522; DOI=10.1016/s0092-8674(01)00524-4; RA Luo J., Nikolaev A.Y., Imai S., Chen D., Su F., Shiloh A., Guarente L., RA Gu W.; RT "Negative control of p53 by Sir2alpha promotes cell survival under RT stress."; RL Cell 107:137-148(2001). RN [20] RP INTERACTION WITH USP7. RX PubMed=14719112; RA Lim S.-K., Shin J.-M., Kim Y.-S., Baek K.-H.; RT "Identification and characterization of murine mHAUSP encoding a RT deubiquitinating enzyme that regulates the status of p53 ubiquitination."; RL Int. J. Oncol. 24:357-364(2004). RN [21] RP IDENTIFICATION IN A COMPLEX WITH CABLES1 AND TP73. RX PubMed=11706030; DOI=10.1074/jbc.m108535200; RA Tsuji K., Mizumoto K., Yamochi T., Nishimoto I., Matsuoka M.; RT "Differential effect of ik3-1/cables on p53- and p73-induced cell death."; RL J. Biol. Chem. 277:2951-2957(2002). RN [22] RP INTERACTION WITH BANP. RX PubMed=12494467; DOI=10.1002/ijc.10881; RA Kaul R., Mukherjee S., Ahmed F., Bhat M.K., Chhipa R., Galande S., RA Chattopadhyay S.; RT "Direct interaction with and activation of p53 by SMAR1 retards cell-cycle RT progression at G2/M phase and delays tumor growth in mice."; RL Int. J. Cancer 103:606-615(2003). RN [23] RP PHOSPHORYLATION AT SER-18, LYSINE ACETYLATION, UBIQUITINATION, AND RP SUBCELLULAR LOCATION. RX PubMed=15195100; DOI=10.1038/ncb1147; RA Bernardi R., Scaglioni P.P., Bergmann S., Horn H.F., Vousden K.H., RA Pandolfi P.P.; RT "PML regulates p53 stability by sequestering Mdm2 to the nucleolus."; RL Nat. Cell Biol. 6:665-672(2004). RN [24] RP PHOSPHORYLATION AT SER-37. RX PubMed=17254968; DOI=10.1016/j.cell.2006.11.050; RA Sun P., Yoshizuka N., New L., Moser B.A., Li Y., Liao R., Xie C., Chen J., RA Deng Q., Yamout M., Dong M.Q., Frangou C.G., Yates J.R. III, Wright P.E., RA Han J.; RT "PRAK is essential for ras-induced senescence and tumor suppression."; RL Cell 128:295-308(2007). RN [25] RP INTERACTION WITH ZNF385A. RX PubMed=17719541; DOI=10.1016/j.cell.2007.06.013; RA Das S., Raj L., Zhao B., Kimura Y., Bernstein A., Aaronson S.A., Lee S.W.; RT "Hzf Determines cell survival upon genotoxic stress by modulating p53 RT transactivation."; RL Cell 130:624-637(2007). RN [26] RP PHOSPHORYLATION AT SER-12. RX PubMed=18022393; DOI=10.1016/j.febslet.2007.11.022; RA Arai S., Matsushita A., Du K., Yagi K., Okazaki Y., Kurokawa R.; RT "Novel homeodomain-interacting protein kinase family member, HIPK4, RT phosphorylates human p53 at serine 9."; RL FEBS Lett. 581:5649-5657(2007). RN [27] RP INTERACTION WITH CHD8. RX PubMed=19151705; DOI=10.1038/ncb1831; RA Nishiyama M., Oshikawa K., Tsukada Y.I., Nakagawa T., Iemura S., RA Natsume T., Fan Y., Kikuchi A., Skoultchi A.I., Nakayama K.I.; RT "CHD8 suppresses p53-mediated apoptosis through histone H1 recruitment RT during early embryogenesis."; RL Nat. Cell Biol. 11:172-182(2009). RN [28] RP FUNCTION, UBIQUITINATION, AND INTERACTION WITH TRIM24. RX PubMed=19556538; DOI=10.1073/pnas.0813177106; RA Allton K., Jain A.K., Herz H.M., Tsai W.W., Jung S.Y., Qin J., Bergmann A., RA Johnson R.L., Barton M.C.; RT "Trim24 targets endogenous p53 for degradation."; RL Proc. Natl. Acad. Sci. U.S.A. 106:11612-11616(2009). RN [29] RP FUNCTION. RX PubMed=20673990; DOI=10.1016/j.cell.2010.06.040; RA Huarte M., Guttman M., Feldser D., Garber M., Koziol M.J., RA Kenzelmann-Broz D., Khalil A.M., Zuk O., Amit I., Rabani M., Attardi L.D., RA Regev A., Lander E.S., Jacks T., Rinn J.L.; RT "A large intergenic noncoding RNA induced by p53 mediates global gene RT repression in the p53 response."; RL Cell 142:409-419(2010). RN [30] RP FUNCTION. RX PubMed=22726440; DOI=10.1016/j.cell.2012.05.014; RA Vaseva A.V., Marchenko N.D., Ji K., Tsirka S.E., Holzmann S., Moll U.M.; RT "p53 opens the mitochondrial permeability transition pore to trigger RT necrosis."; RL Cell 149:1536-1548(2012). RN [31] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-318, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [32] RP FUNCTION, AND INDUCTION. RX PubMed=24051492; DOI=10.1038/ncomms3444; RA Miki T., Matsumoto T., Zhao Z., Lee C.C.; RT "p53 regulates Period2 expression and the circadian clock."; RL Nat. Commun. 4:2444-2444(2013). RN [33] RP INTERACTION WITH C10ORF90, AND UBIQUITINATION BY C10ORF90. RX PubMed=24240685; DOI=10.1038/onc.2013.494; RA Yan S., Qiu L., Ma K., Zhang X., Zhao Y., Zhang J., Li X., Hao X., Li Z.; RT "FATS is an E2-independent ubiquitin ligase that stabilizes p53 and RT promotes its activation in response to DNA damage."; RL Oncogene 33:5424-5433(2014). RN [34] RP UBIQUITINATION, AND PROTEASOMAL DEGRADATION. RX PubMed=25732823; DOI=10.1016/j.celrep.2015.01.066; RA Qin B., Minter-Dykhouse K., Yu J., Zhang J., Liu T., Zhang H., Lee S., RA Kim J., Wang L., Lou Z.; RT "DBC1 functions as a tumor suppressor by regulating p53 stability."; RL Cell Rep. 10:1324-1334(2015). RN [35] RP INTERACTION WITH ALDOB AND G6PD. RX PubMed=35122041; DOI=10.1038/s43018-020-0086-7; RA Li M., He X., Guo W., Yu H., Zhang S., Wang N., Liu G., Sa R., Shen X., RA Jiang Y., Tang Y., Zhuo Y., Yin C., Tu Q., Li N., Nie X., Li Y., Hu Z., RA Zhu H., Ding J., Li Z., Liu T., Zhang F., Zhou H., Li S., Yue J., Yan Z., RA Cheng S., Tao Y., Yin H.; RT "Aldolase B suppresses hepatocellular carcinogenesis by inhibiting G6PD and RT pentose phosphate pathways."; RL Nat. Cancer 1:735-747(2020). RN [36] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 99-284. RX PubMed=11152481; DOI=10.1074/jbc.m011644200; RA Zhao K., Chai X., Johnston K., Clements A., Marmorstein R.; RT "Crystal structure of the mouse p53 core DNA-binding domain at 2.7 A RT resolution."; RL J. Biol. Chem. 276:12120-12127(2001). RN [37] RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 95-292. RX PubMed=17139084; DOI=10.1107/s090744490603890x; RA Ho W.C., Luo C., Zhao K., Chai X., Fitzgerald M.X., Marmorstein R.; RT "High-resolution structure of the p53 core domain: implications for binding RT small-molecule stabilizing compounds."; RL Acta Crystallogr. D 62:1484-1493(2006). RN [38] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 95-292 IN COMPLEX WITH DNA AND RP ZINC IONS, AND SUBUNIT. RX PubMed=16717092; DOI=10.1074/jbc.m603634200; RA Ho W.C., Fitzgerald M.X., Marmorstein R.; RT "Structure of the p53 core domain dimer bound to DNA."; RL J. Biol. Chem. 281:20494-20502(2006). RN [39] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 95-287. RX PubMed=17876829; DOI=10.1002/prot.21608; RA Kwon E., Kim D.Y., Suh S.W., Kim K.K.; RT "Crystal structure of the mouse p53 core domain in zinc-free state."; RL Proteins 70:280-283(2008). RN [40] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 96-292 IN COMPLEX WITH DNA, AND RP SUBUNIT. RX PubMed=18978813; DOI=10.1038/onc.2008.400; RA Malecka K.A., Ho W.C., Marmorstein R.; RT "Crystal structure of a p53 core tetramer bound to DNA."; RL Oncogene 28:325-333(2009). CC -!- FUNCTION: Multifunctional transcription factor that induces cell cycle CC arrest, DNA repair or apoptosis upon binding to its target DNA sequence CC (PubMed:19556538, PubMed:20673990, PubMed:22726440). Acts as a tumor CC suppressor in many tumor types; induces growth arrest or apoptosis CC depending on the physiological circumstances and cell type. Negatively CC regulates cell division by controlling expression of a set of genes CC required for this process. One of the activated genes is an inhibitor CC of cyclin-dependent kinases. Apoptosis induction seems to be mediated CC either by stimulation of BAX and FAS antigen expression, or by CC repression of Bcl-2 expression. Its pro-apoptotic activity is activated CC via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (By CC similarity). However, this activity is inhibited when the interaction CC with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (By CC similarity). In cooperation with mitochondrial PPIF is involved in CC activating oxidative stress-induced necrosis; the function is largely CC independent of transcription. Prevents CDK7 kinase activity when CC associated to CAK complex in response to DNA damage, thus stopping cell CC cycle progression (By similarity). Induces the transcription of long CC intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA- CC p21 participates in TP53-dependent transcriptional repression leading CC to apoptosis, but seems to have to effect on cell-cycle regulation. CC Regulates the circadian clock by repressing CLOCK-BMAL1-mediated CC transcriptional activation of PER2 (PubMed:24051492). CC {ECO:0000250|UniProtKB:P04637, ECO:0000269|PubMed:19556538, CC ECO:0000269|PubMed:20673990, ECO:0000269|PubMed:22726440, CC ECO:0000269|PubMed:24051492}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:16717092}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:16717092}; CC -!- SUBUNIT: Forms homodimers and homotetramers (By similarity). Binds DNA CC as a homotetramer. Interacts with AXIN1 (PubMed:15526030). Probably CC part of a complex consisting of TP53, HIPK2 and AXIN1 CC (PubMed:15526030). Interacts with histone acetyltransferases EP300 and CC methyltransferases HRMT1L2 and CARM1, and recruits them to promoters. CC Interacts (via C-terminus) with TAF1; when TAF1 is part of the TFIID CC complex. Interacts with ING4; this interaction may be indirect CC (PubMed:12702766). Found in a complex with CABLES1 and TP73 CC (PubMed:11706030). Interacts with HIPK1, HIPK2, and TP53INP1. Interacts CC with WWOX. Interacts with USP7 and SYVN1 (PubMed:14719112). Interacts CC with HSP90AB1. Interacts with CHD8; leading to recruit histone H1 and CC prevent transactivation activity (PubMed:19151705). Interacts with CC ARMC10, BANP, CDKN2AIP, NUAK1, STK11/LKB1, UHRF2 and E4F CC (PubMed:10644996). Interacts with YWHAZ; the interaction enhances TP53 CC transcriptional activity. Phosphorylation of YWHAZ on 'Ser-58' inhibits CC this interaction. Interacts (via DNA-binding domain) with MAML1 (via N- CC terminus). Interacts with MKRN1. Interacts with PML (via C-terminus). CC Interacts with MDM2; leading to ubiquitination and proteasomal CC degradation of TP53. Directly interacts with FBXO42; leading to CC ubiquitination and degradation of TP53. Interacts (phosphorylated at CC Ser-18 by ATM) with the phosphatase PP2A-PPP2R5C holoenzyme; regulates CC stress-induced TP53-dependent inhibition of cell proliferation. CC Interacts with PPP2R2A. Interacts with AURKA, DAXX, BRD7 and TRIM24 CC (PubMed:19556538). Interacts (when monomethylated at Lys-379) with CC L3MBTL1. Interacts with GRK5. Binds to the CAK complex (CDK7, cyclin H CC and MAT1) in response to DNA damage. Interacts with CDK5 in neurons. CC Interacts with AURKB, SETD2, UHRF2 and NOC2L. Interacts (via N- CC terminus) with PTK2/FAK1; this promotes ubiquitination by MDM2. CC Interacts with PTK2B/PYK2; this promotes ubiquitination by MDM2. CC Interacts with PRKCG. Interacts with PPIF; the association implicates CC preferentially tetrameric TP53, is induced by oxidative stress and is CC impaired by cyclosporin A (CsA). Interacts with SNAI1; the interaction CC induces SNAI1 degradation via MDM2-mediated ubiquitination and inhibits CC SNAI1-induced cell invasion. Interacts with UBC9. Interacts with CC ZNF385B; the interaction is direct. Interacts (via DNA-binding domain) CC with ZNF385A; the interaction is direct and enhances p53/TP53 CC transactivation functions on cell-cycle arrest target genes, resulting CC in growth arrest (PubMed:17719541). Interacts with ANKRD2. Interacts CC with RFFL and RNF34; involved in p53/TP53 ubiquitination. Interacts CC with MTA1 and COP1. Interacts with CCAR2 (via N-terminus). Interacts CC with MORC3. Interacts (via C-terminus) with POU4F2 (via C-terminus). CC Interacts (via oligomerization region) with NOP53; the interaction is CC direct and may prevent the MDM2-mediated proteasomal degradation of CC TP53. Interacts with AFG1L; mediates mitochondrial translocation of CC TP53. Interacts with UBD (By similarity). Interacts with TAF6 (By CC similarity). Interacts with C10orf90/FATS; the interaction inhibits CC binding of TP53 and MDM2 (PubMed:24240685). Interacts with NUPR1; CC interaction is stress-dependent. Forms a complex with EP300 and NUPR1; CC this complex binds CDKN1A promoter leading to transcriptional induction CC of CDKN1A (By similarity). Interacts with PRMT5 in response to DNA CC damage; the interaction is TTC5/STRAP dependent (By similarity). CC Interacts with PPP1R13L (via SH3 domain and ANK repeats); the CC interaction inhibits pro-apoptotic activity of p53/TP53 (By CC similarity). Interacts with PPP1R13B/ASPP1 and TP53BP2/ASPP2; the CC interactions promotes pro-apoptotic activity (By similarity). When CC phosphorylated at Ser-18, interacts with DDX3X and gamma-tubulin (By CC similarity). Interacts with KAT7/HBO1; leading to inhibit histone CC acetyltransferase activity of KAT7/HBO1 (By similarity). Interacts (via CC N-terminus) with E3 ubiquitin-protein ligase MUL1; the interaction CC results in ubiquitination of cytoplasmic TP53 at Lys-27 and subsequent CC proteasomal degradation (By similarity). Interacts with S100A4; this CC interaction promotes TP53 degradation (By similarity). Interacts with CC TTC5/STRAP; the interaction may result in increased mitochondrial- CC dependent apoptosis (By similarity). Interacts with NQO1; this CC interaction is NADH-dependent, stabilizes TP53 in response to oxidative CC stress and protects it from ubiquitin-independent degradation by the CC 20S proteasome (By similarity). Interacts with DAZAP2 at TP53 target CC gene promoters; the interaction is triggered by DNA damage and leads to CC modulation of the expression of a subset of TP53 target genes, reducing CC DNA damage-induced cell death by limiting the expression of cell death- CC mediating TP53 target genes (By similarity). Interacts (via N-terminus) CC with ZNF768 (via zinc-finger domains); interaction might be facilitated CC by TP53 oligomerization state (By similarity). Forms a ternary complex CC with ALDOB and G6PD; this interaction is direct. ALDOB stabilizes the CC complex inhibiting G6PD activity and keeping oxidative pentose CC phosphate metabolism in check. Interacts with MORN3; the interactions CC mediate post-transcriptional modifications of TP53 by MDM2 and SIRT1 CC (By similarity). Interacts with HSPA9/MOT-2; the interaction promotes CC the degradation of TP53 (By similarity). {ECO:0000250|UniProtKB:P04637, CC ECO:0000250|UniProtKB:P10361, ECO:0000269|PubMed:10644996, CC ECO:0000269|PubMed:11706030, ECO:0000269|PubMed:12494467, CC ECO:0000269|PubMed:12702766, ECO:0000269|PubMed:14719112, CC ECO:0000269|PubMed:15526030, ECO:0000269|PubMed:17719541, CC ECO:0000269|PubMed:19151705, ECO:0000269|PubMed:19556538, CC ECO:0000269|PubMed:24240685, ECO:0000269|PubMed:35122041}. CC -!- INTERACTION: CC P02340; P97302: Bach1; NbExp=4; IntAct=EBI-474016, EBI-2552417; CC P02340; B2RWS6: Ep300; NbExp=3; IntAct=EBI-474016, EBI-3953360; CC P02340; P23804: Mdm2; NbExp=9; IntAct=EBI-474016, EBI-641788; CC P02340; P23804-1: Mdm2; NbExp=2; IntAct=EBI-474016, EBI-3386476; CC P02340; Q9QUR7: Pin1; NbExp=3; IntAct=EBI-474016, EBI-2432975; CC P02340; P54099: Polg; NbExp=2; IntAct=EBI-474016, EBI-863636; CC P02340; Q99KR7: Ppif; NbExp=2; IntAct=EBI-474016, EBI-6455001; CC P02340; O08586: Pten; NbExp=4; IntAct=EBI-474016, EBI-1186266; CC P02340; Q61466: Smarcd1; NbExp=4; IntAct=EBI-474016, EBI-371529; CC P02340; P09671: Sod2; NbExp=2; IntAct=EBI-474016, EBI-1635071; CC P02340; Q64127: Trim24; NbExp=2; IntAct=EBI-474016, EBI-307947; CC P02340; P62991: Ubc; NbExp=4; IntAct=EBI-474016, EBI-413074; CC P02340; Q07817-1: BCL2L1; Xeno; NbExp=3; IntAct=EBI-474016, EBI-287195; CC P02340; P03070; Xeno; NbExp=20; IntAct=EBI-474016, EBI-617698; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04637}. Nucleus CC {ECO:0000250|UniProtKB:P04637}. Nucleus, PML body CC {ECO:0000250|UniProtKB:P04637}. Endoplasmic reticulum CC {ECO:0000250|UniProtKB:P04637}. Mitochondrion matrix CC {ECO:0000250|UniProtKB:P04637}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000250|UniProtKB:P04637}. CC Note=Interaction with BANP promotes nuclear localization. Recruited CC into PML bodies together with CHEK2. Translocates to mitochondria upon CC oxidative stress. Translocates to mitochondria in response to mitomycin CC C treatment (By similarity). Competitive inhibition of TP53 interaction CC with HSPA9/MOT-2 by UBXN2A results in increased protein abundance and CC subsequent translocation of TP53 to the nucleus (By similarity). CC {ECO:0000250|UniProtKB:P04637}. CC -!- INDUCTION: Expressed in a circadian manner in the suprachiasmatic CC nucleus (SCN) of the brain with a peak seen at ZT8. CC {ECO:0000269|PubMed:24051492}. CC -!- DOMAIN: The N-terminal and C-terminal disordered regions undergo CC liquid-liquid phase separation (LLPS) following homotetramerization and CC activation. Post-translational modifications, such as phosphorylation CC or lactylation affect the ability to undergo LLPS. CC {ECO:0000250|UniProtKB:P04637}. CC -!- DOMAIN: The nuclear export signal acts as a transcriptional repression CC domain. The TADI and TADII motifs (residues 17 to 25 and 48 to 56) CC correspond both to 9aaTAD motifs which are transactivation domains CC present in a large number of yeast and animal transcription factors. CC {ECO:0000250|UniProtKB:P04637}. CC -!- PTM: Phosphorylation on Ser residues mediates transcriptional CC activation. Phosphorylation at Ser-12 by HIPK4 increases repression CC activity on BIRC5 promoter. Phosphorylated on Thr-21 by VRK1. CC Phosphorylated on Ser-23 by CHEK2 in response to DNA damage, which CC prevents ubiquitination by MDM2. Phosphorylated on Ser-23 by PLK3 in CC response to reactive oxygen species (ROS), promoting p53/TP53-mediated CC apoptosis. Probably phosphorylated on by CDK7 in a CAK complex in CC response to DNA damage. Stabilized by CDK5-mediated phosphorylation in CC response to genotoxic and oxidative stresses at Ser-18 leading to CC accumulation of p53/TP53, particularly in the nucleus, thus inducing CC the transactivation of p53/TP53 target genes (By similarity). CC Phosphorylated on Ser-389 following UV but not gamma irradiation. CC Phosphorylated by HIPK1. Phosphorylation at Ser-18 is required for CC interaction with DDX3X and gamma-tubulin (By similarity). CC Phosphorylation at Ser-389 regulates its ability to undergo liquid- CC liquid phase separation by increasing fluidity of TP53/p53 condensates CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P04637, CC ECO:0000269|PubMed:12702766, ECO:0000269|PubMed:15195100, CC ECO:0000269|PubMed:17254968, ECO:0000269|PubMed:18022393, CC ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:2145148, CC ECO:0000269|PubMed:3006031}. CC -!- PTM: Ubiquitinated by MDM2 and SYVN1, which leads to proteasomal CC degradation. Ubiquitinated by RFWD3, which works in cooperation with CC MDM2 and may catalyze the formation of short polyubiquitin chains on CC p53/TP53 that are not targeted to the proteasome. Ubiquitinated by CC MKRN1 at Lys-288 and Lys-289, which leads to proteasomal degradation. CC Deubiquitinated by USP10, leading to stabilize it. Ubiquitinated by CC TRIM24, RFFL, RNF34 and RNF125, which leads to proteasomal degradation. CC Ubiquitination by TOPORS induces degradation. Deubiquitination by USP7, CC leading to stabilize it. Ubiquitinated by COP1, which leads to CC proteasomal degradation (By similarity). Ubiquitination and subsequent CC proteasomal degradation is negatively regulated by CCAR2 CC (PubMed:25732823). Polyubiquitinated by C10orf90/FATS, CC polyubiquitination is 'Lys-48'-linkage independent and non-proteolytic, CC leading to TP53 stabilization (PubMed:24240685). CC {ECO:0000250|UniProtKB:P04637, ECO:0000269|PubMed:24240685, CC ECO:0000269|PubMed:25732823}. CC -!- PTM: Monomethylated at Lys-369 by SETD7, leading to stabilization and CC increased transcriptional activation. Monomethylated at Lys-367 by CC SMYD2, leading to decreased DNA-binding activity and subsequent CC transcriptional regulation activity. Lys-369 monomethylation prevents CC interaction with SMYD2 and subsequent monomethylation at Lys-367. CC Dimethylated at Lys-370 by EHMT1 and EHMT2. Monomethylated at Lys-379 CC by KMT5A, promoting interaction with L3MBTL1 and leading to repress CC transcriptional activity. Demethylation of dimethylated Lys-367 by CC KDM1A prevents interaction with TP53BP1 and represses TP53-mediated CC transcriptional activation (By similarity). Monomethylated at Arg-330 CC and dimethylated at Arg-332 and Arg-334 by PRMT5; methylation is CC increased after DNA damage and might possibly affect TP53 target gene CC specificity (By similarity). Polyubiquitinated by MUL1 at Lys-27 which CC leads to proteasomal degradation (By similarity). Deubiquitinated by CC USP3, leading to stabilization (By similarity). Ubiquitinated by MSL2, CC promoting its cytoplasmic localization (By similarity). CC {ECO:0000250|UniProtKB:P04637}. CC -!- PTM: Sumoylated with SUMO1. Sumoylated at Lys-383 by UBC9 (By CC similarity). {ECO:0000250}. CC -!- PTM: Acetylation of Lys-379 by CREBBP enhances transcriptional CC activity. Acetylation of Lys-379 by EP300. Deacetylation of Lys-379 by CC SIRT1 impairs its ability to induce proapoptotic program and modulate CC cell senescence. Deacetylation by SIRT2 impairs its ability to induce CC transcription activation in a AKT-dependent manner. Acetylation at Lys- CC 378 increases stability. Deacetylation at Lys-378 by SIRT6 decreases CC its stability, thereby regulating cell senescence. Acetylated at Lys- CC 117 by KAT5, KAT6A and KAT8; regulating its ability to induce CC proapoptotic program. {ECO:0000250|UniProtKB:P04637}. CC -!- PTM: Lactylation by AARS1 prevents ability to undergo liquid-liquid CC phase separation (LLPS), thereby inhibiting transcription factor CC activity. {ECO:0000250|UniProtKB:P04637}. CC -!- DISEASE: Note=p53 is found in increased amounts in a wide variety of CC transformed cells. p53 is frequently mutated or inactivated in many CC types of cancer. CC -!- SIMILARITY: Belongs to the p53 family. {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X00876; CAA25420.1; -; Genomic_DNA. DR EMBL; X00877; CAA25420.1; JOINED; Genomic_DNA. DR EMBL; X00878; CAA25420.1; JOINED; Genomic_DNA. DR EMBL; X00879; CAA25420.1; JOINED; Genomic_DNA. DR EMBL; X00880; CAA25420.1; JOINED; Genomic_DNA. DR EMBL; X00881; CAA25420.1; JOINED; Genomic_DNA. DR EMBL; X00882; CAA25420.1; JOINED; Genomic_DNA. DR EMBL; X00883; CAA25420.1; JOINED; Genomic_DNA. DR EMBL; X00884; CAA25420.1; JOINED; Genomic_DNA. DR EMBL; X00885; CAA25420.1; JOINED; Genomic_DNA. DR EMBL; X01237; CAA25625.1; -; mRNA. DR EMBL; X00741; CAA25323.1; -; mRNA. DR EMBL; M13872; AAA39881.1; -; mRNA. DR EMBL; M13873; AAA39882.1; -; mRNA. DR EMBL; M13874; AAA39883.1; ALT_SEQ; mRNA. DR EMBL; AB021961; BAA82344.1; -; mRNA. DR EMBL; AF151353; AAD39535.1; -; mRNA. DR EMBL; AB017815; BAA82339.1; -; mRNA. DR EMBL; AB017816; BAA82340.1; -; mRNA. DR EMBL; AB020317; BAA82343.1; -; mRNA. DR EMBL; BC005448; AAH05448.1; -; mRNA. DR EMBL; S77930; AAB21108.2; -; Genomic_DNA. DR CCDS; CCDS36193.1; -. DR PIR; A22739; DNMS53. DR PIR; S38824; S38824. DR RefSeq; NP_001120705.1; NM_001127233.1. DR RefSeq; NP_035770.2; NM_011640.3. DR RefSeq; XP_006533220.1; XM_006533157.3. DR PDB; 1HU8; X-ray; 2.70 A; A/B/C=99-284. DR PDB; 2GEQ; X-ray; 2.30 A; A/B=92-292. DR PDB; 2IOI; X-ray; 1.55 A; A=92-292. DR PDB; 2IOM; X-ray; 2.00 A; A=92-292. DR PDB; 2IOO; X-ray; 2.02 A; A=92-292. DR PDB; 2P52; X-ray; 1.50 A; A=92-287. DR PDB; 3EXJ; X-ray; 2.00 A; A/B=96-292. DR PDB; 3EXL; X-ray; 2.20 A; A=96-292. DR PDBsum; 1HU8; -. DR PDBsum; 2GEQ; -. DR PDBsum; 2IOI; -. DR PDBsum; 2IOM; -. DR PDBsum; 2IOO; -. DR PDBsum; 2P52; -. DR PDBsum; 3EXJ; -. DR PDBsum; 3EXL; -. DR AlphaFoldDB; P02340; -. DR SMR; P02340; -. DR BioGRID; 204323; 139. DR CORUM; P02340; -. DR DIP; DIP-369N; -. DR IntAct; P02340; 50. DR MINT; P02340; -. DR STRING; 10090.ENSMUSP00000104298; -. DR ChEMBL; CHEMBL4164; -. DR GlyGen; P02340; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P02340; -. DR PhosphoSitePlus; P02340; -. DR SwissPalm; P02340; -. DR PaxDb; 10090-ENSMUSP00000104298; -. DR ProteomicsDB; 294305; -. DR ABCD; P02340; 20 sequenced antibodies. DR Antibodypedia; 3525; 9364 antibodies from 65 providers. DR DNASU; 22059; -. DR Ensembl; ENSMUST00000108658.10; ENSMUSP00000104298.4; ENSMUSG00000059552.14. DR GeneID; 22059; -. DR KEGG; mmu:22059; -. DR UCSC; uc007jql.2; mouse. DR AGR; MGI:98834; -. DR CTD; 22059; -. DR MGI; MGI:98834; Trp53. DR VEuPathDB; HostDB:ENSMUSG00000059552; -. DR eggNOG; ENOG502QVY3; Eukaryota. DR GeneTree; ENSGT00950000183153; -. DR HOGENOM; CLU_019621_0_0_1; -. DR InParanoid; P02340; -. DR OMA; HKKGEPC; -. DR OrthoDB; 2902631at2759; -. DR Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence. DR Reactome; R-MMU-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF). DR Reactome; R-MMU-2559585; Oncogene Induced Senescence. DR Reactome; R-MMU-2559586; DNA Damage/Telomere Stress Induced Senescence. DR Reactome; R-MMU-349425; Autodegradation of the E3 ubiquitin ligase COP1. DR Reactome; R-MMU-5689880; Ub-specific processing proteases. DR Reactome; R-MMU-5689896; Ovarian tumor domain proteases. DR Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks. DR Reactome; R-MMU-6804754; Regulation of TP53 Expression. DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation. DR Reactome; R-MMU-6804757; Regulation of TP53 Degradation. DR Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation. DR Reactome; R-MMU-6804759; Regulation of TP53 Activity through Association with Co-factors. DR Reactome; R-MMU-6804760; Regulation of TP53 Activity through Methylation. DR Reactome; R-MMU-6811555; PI5P Regulates TP53 Acetylation. DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint. DR Reactome; R-MMU-69481; G2/M Checkpoints. DR Reactome; R-MMU-69541; Stabilization of p53. DR Reactome; R-MMU-69895; Transcriptional activation of cell cycle inhibitor p21. DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint. DR Reactome; R-MMU-8941855; RUNX3 regulates CDKN1A transcription. DR Reactome; R-MMU-9833482; PKR-mediated signaling. DR BioGRID-ORCS; 22059; 15 hits in 120 CRISPR screens. DR ChiTaRS; Trp53; mouse. DR EvolutionaryTrace; P02340; -. DR PRO; PR:P02340; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; P02340; protein. DR Bgee; ENSMUSG00000059552; Expressed in embryonic post-anal tail and 235 other cell types or tissues. DR ExpressionAtlas; P02340; baseline and differential. DR GO; GO:0005813; C:centrosome; ISS:UniProtKB. DR GO; GO:0000785; C:chromatin; ISS:ARUK-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0043073; C:germ cell nucleus; IDA:MGI. DR GO; GO:0005759; C:mitochondrial matrix; IDA:MGI. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0016363; C:nuclear matrix; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:ARUK-UCL. DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell. DR GO; GO:0005657; C:replication fork; IDA:MGI. DR GO; GO:0035861; C:site of double-strand break; IDA:MGI. DR GO; GO:0017053; C:transcription repressor complex; IEA:Ensembl. DR GO; GO:0036310; F:ATP-dependent DNA/DNA annealing activity; ISS:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB. DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl. DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:MGI. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl. DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl. DR GO; GO:0035033; F:histone deacetylase regulator activity; IDA:MGI. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; IPI:BHF-UCL. DR GO; GO:0140693; F:molecular condensate scaffold activity; ISS:UniProtKB. DR GO; GO:0140677; F:molecular function activator activity; IEA:Ensembl. DR GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:Ensembl. DR GO; GO:0002039; F:p53 binding; IEA:Ensembl. DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB. DR GO; GO:0002020; F:protease binding; IEA:Ensembl. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl. DR GO; GO:0051721; F:protein phosphatase 2A binding; IEA:Ensembl. DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:Ensembl. DR GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl. DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; IEA:Ensembl. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IDA:MGI. DR GO; GO:0002326; P:B cell lineage commitment; IMP:MGI. DR GO; GO:0048539; P:bone marrow development; IEA:Ensembl. DR GO; GO:0010659; P:cardiac muscle cell apoptotic process; IMP:MGI. DR GO; GO:0060411; P:cardiac septum morphogenesis; IGI:MGI. DR GO; GO:0008283; P:cell population proliferation; IGI:MGI. DR GO; GO:0072717; P:cellular response to actinomycin D; IEA:Ensembl. DR GO; GO:0071480; P:cellular response to gamma radiation; IDA:MGI. DR GO; GO:0042149; P:cellular response to glucose starvation; ISO:MGI. DR GO; GO:0071479; P:cellular response to ionizing radiation; IDA:CAFA. DR GO; GO:0033554; P:cellular response to stress; IGI:MGI. DR GO; GO:0034644; P:cellular response to UV; IDA:CAFA. DR GO; GO:0071494; P:cellular response to UV-C; IGI:MGI. DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0090398; P:cellular senescence; ISS:UniProtKB. DR GO; GO:0007417; P:central nervous system development; IGI:MGI. DR GO; GO:0021549; P:cerebellum development; IDA:MGI. DR GO; GO:0051276; P:chromosome organization; IGI:MGI. DR GO; GO:0048512; P:circadian behavior; IMP:UniProtKB. DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB. DR GO; GO:0008340; P:determination of adult lifespan; IMP:BHF-UCL. DR GO; GO:0006974; P:DNA damage response; IDA:MGI. DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IDA:MGI. DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; IGI:MGI. DR GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IDA:MGI. DR GO; GO:0006302; P:double-strand break repair; IMP:MGI. DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:MGI. DR GO; GO:0048568; P:embryonic organ development; IGI:MGI. DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IMP:UniProtKB. DR GO; GO:0006983; P:ER overload response; ISO:MGI. DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI. DR GO; GO:0007369; P:gastrulation; IGI:MGI. DR GO; GO:0014009; P:glial cell proliferation; IGI:MGI. DR GO; GO:0019661; P:glucose catabolic process to lactate via pyruvate; IMP:MGI. DR GO; GO:0007507; P:heart development; IGI:MGI. DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IEA:Ensembl. DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI. DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IDA:MGI. DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IDA:CAFA. DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL. DR GO; GO:1990144; P:intrinsic apoptotic signaling pathway in response to hypoxia; IMP:MGI. DR GO; GO:0043504; P:mitochondrial DNA repair; IMP:MGI. DR GO; GO:0000423; P:mitophagy; IMP:MGI. DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IMP:MGI. DR GO; GO:0009299; P:mRNA transcription; IEA:Ensembl. DR GO; GO:0035264; P:multicellular organism growth; IGI:MGI. DR GO; GO:0070266; P:necroptotic process; IGI:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI. DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:BHF-UCL. DR GO; GO:0008156; P:negative regulation of DNA replication; IDA:MGI. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:MGI. DR GO; GO:1903451; P:negative regulation of G1 to G0 transition; IEA:Ensembl. DR GO; GO:0010629; P:negative regulation of gene expression; IGI:MGI. DR GO; GO:0060253; P:negative regulation of glial cell proliferation; IGI:MGI. DR GO; GO:1904024; P:negative regulation of glucose catabolic process to lactate via pyruvate; IMP:MGI. DR GO; GO:1903799; P:negative regulation of miRNA processing; IGI:MGI. DR GO; GO:1901525; P:negative regulation of mitophagy; IMP:MGI. DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IGI:MGI. DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IGI:MGI. DR GO; GO:1905856; P:negative regulation of pentose-phosphate shunt; IEA:Ensembl. DR GO; GO:0045861; P:negative regulation of proteolysis; IMP:MGI. DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:MGI. DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IGI:MGI. DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:MGI. DR GO; GO:0007405; P:neuroblast proliferation; IGI:MGI. DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI. DR GO; GO:0006289; P:nucleotide-excision repair; ISS:UniProtKB. DR GO; GO:0097252; P:oligodendrocyte apoptotic process; ISS:UniProtKB. DR GO; GO:0090403; P:oxidative stress-induced premature senescence; IEA:Ensembl. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI. DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IMP:MGI. DR GO; GO:2000774; P:positive regulation of cellular senescence; IMP:BHF-UCL. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IEA:Ensembl. DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB. DR GO; GO:1902895; P:positive regulation of miRNA transcription; IEA:Ensembl. DR GO; GO:0035794; P:positive regulation of mitochondrial membrane permeability; IGI:MGI. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IDA:MGI. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL. DR GO; GO:0062100; P:positive regulation of programmed necrotic cell death; IMP:ARUK-UCL. DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IEA:Ensembl. DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IEA:Ensembl. DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IEA:Ensembl. DR GO; GO:0070245; P:positive regulation of thymocyte apoptotic process; IMP:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0006606; P:protein import into nucleus; IDA:MGI. DR GO; GO:0050821; P:protein stabilization; IGI:MGI. DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro. DR GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl. DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:MGI. DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI. DR GO; GO:0051726; P:regulation of cell cycle; IMP:MGI. DR GO; GO:1902749; P:regulation of cell cycle G2/M phase transition; IEA:Ensembl. DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI. DR GO; GO:2000772; P:regulation of cellular senescence; IGI:MGI. DR GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; IGI:MGI. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:2000269; P:regulation of fibroblast apoptotic process; IGI:MGI. DR GO; GO:1902253; P:regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IMP:MGI. DR GO; GO:1902108; P:regulation of mitochondrial membrane permeability involved in apoptotic process; IGI:MGI. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IDA:MGI. DR GO; GO:0043523; P:regulation of neuron apoptotic process; IGI:MGI. DR GO; GO:0070243; P:regulation of thymocyte apoptotic process; IGI:MGI. DR GO; GO:0034103; P:regulation of tissue remodeling; IMP:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:MGI. DR GO; GO:0090399; P:replicative senescence; IEA:Ensembl. DR GO; GO:0010332; P:response to gamma radiation; IDA:MGI. DR GO; GO:0002931; P:response to ischemia; IMP:MGI. DR GO; GO:0006979; P:response to oxidative stress; IMP:MGI. DR GO; GO:0009651; P:response to salt stress; IGI:MGI. DR GO; GO:0009411; P:response to UV; IDA:MGI. DR GO; GO:0010165; P:response to X-ray; IDA:MGI. DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:MGI. DR GO; GO:0009303; P:rRNA transcription; IGI:MGI. DR GO; GO:0072331; P:signal transduction by p53 class mediator; IMP:MGI. DR GO; GO:0001756; P:somitogenesis; IGI:MGI. DR GO; GO:0072089; P:stem cell proliferation; IGI:MGI. DR GO; GO:0033077; P:T cell differentiation in thymus; IGI:MGI. DR GO; GO:0002360; P:T cell lineage commitment; IMP:MGI. DR GO; GO:0002309; P:T cell proliferation involved in immune response; IGI:MGI. DR GO; GO:0070242; P:thymocyte apoptotic process; IMP:MGI. DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IEA:Ensembl. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IGI:MGI. DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IEA:Ensembl. DR GO; GO:0060333; P:type II interferon-mediated signaling pathway; IMP:CAFA. DR GO; GO:0016032; P:viral process; IEA:Ensembl. DR CDD; cd08367; P53; 1. DR FunFam; 2.60.40.720:FF:000003; Cellular tumor antigen p53; 1. DR FunFam; 4.10.170.10:FF:000003; Cellular tumor antigen p53; 1. DR Gene3D; 2.60.40.720; -; 1. DR Gene3D; 6.10.50.20; -; 1. DR Gene3D; 4.10.170.10; p53-like tetramerisation domain; 1. DR InterPro; IPR008967; p53-like_TF_DNA-bd_sf. DR InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf. DR InterPro; IPR011615; p53_DNA-bd. DR InterPro; IPR036674; p53_tetramer_sf. DR InterPro; IPR010991; p53_tetrameristn. DR InterPro; IPR013872; p53_transactivation_domain. DR InterPro; IPR002117; p53_tumour_suppressor. DR PANTHER; PTHR11447; CELLULAR TUMOR ANTIGEN P53; 1. DR PANTHER; PTHR11447:SF6; CELLULAR TUMOR ANTIGEN P53; 1. DR Pfam; PF00870; P53; 1. DR Pfam; PF08563; P53_TAD; 1. DR Pfam; PF07710; P53_tetramer; 1. DR PRINTS; PR00386; P53SUPPRESSR. DR SUPFAM; SSF47719; p53 tetramerization domain; 1. DR SUPFAM; SSF49417; p53-like transcription factors; 1. DR PROSITE; PS00348; P53; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Apoptosis; Biological rhythms; KW Cell cycle; Cytoplasm; Cytoskeleton; Disease variant; DNA-binding; KW Endoplasmic reticulum; Isopeptide bond; Metal-binding; Methylation; KW Mitochondrion; Necrosis; Nucleus; Phosphoprotein; Reference proteome; KW Repressor; Transcription; Transcription regulation; Tumor suppressor; KW Ubl conjugation; Zinc. FT CHAIN 1..390 FT /note="Cellular tumor antigen p53" FT /id="PRO_0000185709" FT DNA_BIND 99..289 FT /evidence="ECO:0000250|UniProtKB:P04637" FT REGION 4..317 FT /note="Interaction with CCAR2" FT /evidence="ECO:0000250|UniProtKB:P04637" FT REGION 4..45 FT /note="Transcription activation (acidic)" FT REGION 63..107 FT /note="Interaction with WWOX" FT /evidence="ECO:0000250" FT REGION 97..367 FT /note="Interaction with HIPK1" FT /evidence="ECO:0000269|PubMed:12702766" FT REGION 97..297 FT /note="Required for interaction with ZNF385A" FT /evidence="ECO:0000250" FT REGION 110..233 FT /note="Required for interaction with FBXO42" FT /evidence="ECO:0000250" FT REGION 113..289 FT /note="Interaction with AXIN1" FT /evidence="ECO:0000269|PubMed:15526030" FT REGION 256..294 FT /note="Interaction with E4F1" FT /evidence="ECO:0000250" FT REGION 270..277 FT /note="Interaction with DNA" FT REGION 316..357 FT /note="Interaction with HIPK2" FT /evidence="ECO:0000250" FT REGION 322..353 FT /note="Oligomerization" FT REGION 348..390 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 356..360 FT /note="Interaction with USP7" FT /evidence="ECO:0000250" FT REGION 365..384 FT /note="Basic (repression of DNA-binding)" FT MOTIF 302..318 FT /note="Bipartite nuclear localization signal" FT /evidence="ECO:0000250" FT MOTIF 336..347 FT /note="Nuclear export signal" FT /evidence="ECO:0000250" FT MOTIF 367..369 FT /note="[KR]-[STA]-K motif" FT COMPBIAS 348..365 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 173 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:16717092" FT BINDING 176 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:16717092" FT BINDING 235 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:16717092" FT BINDING 239 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:16717092" FT SITE 117 FT /note="Interaction with DNA" FT /evidence="ECO:0000269|PubMed:16717092" FT MOD_RES 12 FT /note="Phosphoserine; by HIPK4" FT /evidence="ECO:0000269|PubMed:18022393" FT MOD_RES 18 FT /note="Phosphoserine; by CDK5, PRPK, AMPK, NUAK1 and ATM" FT /evidence="ECO:0000269|PubMed:15195100" FT MOD_RES 21 FT /note="Phosphothreonine; by CK1, VRK1 and VRK2" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 23 FT /note="Phosphoserine; by CHEK2, CK1 and PLK3" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 37 FT /note="Phosphoserine; by MAPKAPK5" FT /evidence="ECO:0000269|PubMed:17254968" FT MOD_RES 117 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 117 FT /note="N6-lactoyllysine" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 136 FT /note="N6-lactoyllysine" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 180 FT /note="Phosphoserine; by AURKB" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 266 FT /note="Phosphoserine; by AURKB" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 281 FT /note="Phosphothreonine; by AURKB" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 302 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 312 FT /note="Phosphoserine; by AURKA, CDK1 and CDK2" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 318 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 330 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 332 FT /note="Symmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 334 FT /note="Symmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 367 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 367 FT /note="N6-methyllysine; by SMYD2; alternate" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 369 FT /note="N6-methyllysine; by SETD7" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 370 FT /note="N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternate" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 370 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 378 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 379 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 379 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 379 FT /note="N6-methyllysine; by KMT5A; alternate" FT /evidence="ECO:0000250|UniProtKB:P04637" FT MOD_RES 389 FT /note="Phosphoserine; by CK2, CDK2 and NUAK1" FT /evidence="ECO:0000250|UniProtKB:P04637" FT CROSSLNK 27 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P04637" FT CROSSLNK 288 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P04637" FT CROSSLNK 289 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P04637" FT CROSSLNK 348 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P04637" FT CROSSLNK 383 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000250" FT VARIANT 135 FT /note="A -> V (can cooperate with an activated Ras to FT transform fibroblasts)" FT /evidence="ECO:0000269|PubMed:3329909" FT VARIANT 168 FT /note="E -> G (in clone P53-M11)" FT VARIANT 191 FT /note="L -> R" FT CONFLICT 48 FT /note="Q -> R (in Ref. 3; CAA25323)" FT /evidence="ECO:0000305" FT CONFLICT 79..81 FT /note="PVA -> QW (in Ref. 3; CAA25323)" FT /evidence="ECO:0000305" FT HELIX 102..104 FT /evidence="ECO:0007829|PDB:2P52" FT STRAND 107..109 FT /evidence="ECO:0007829|PDB:2P52" FT HELIX 116..119 FT /evidence="ECO:0007829|PDB:3EXJ" FT STRAND 120..124 FT /evidence="ECO:0007829|PDB:2P52" FT TURN 125..128 FT /evidence="ECO:0007829|PDB:2P52" FT STRAND 129..132 FT /evidence="ECO:0007829|PDB:2P52" FT STRAND 137..143 FT /evidence="ECO:0007829|PDB:2P52" FT STRAND 153..162 FT /evidence="ECO:0007829|PDB:2P52" FT TURN 163..167 FT /evidence="ECO:0007829|PDB:2P52" FT HELIX 174..178 FT /evidence="ECO:0007829|PDB:2P52" FT STRAND 184..186 FT /evidence="ECO:0007829|PDB:2P52" FT STRAND 191..196 FT /evidence="ECO:0007829|PDB:2P52" FT STRAND 201..204 FT /evidence="ECO:0007829|PDB:2P52" FT TURN 206..208 FT /evidence="ECO:0007829|PDB:2P52" FT STRAND 211..216 FT /evidence="ECO:0007829|PDB:2P52" FT STRAND 225..233 FT /evidence="ECO:0007829|PDB:2P52" FT HELIX 238..240 FT /evidence="ECO:0007829|PDB:2P52" FT HELIX 242..245 FT /evidence="ECO:0007829|PDB:2P52" FT STRAND 248..255 FT /evidence="ECO:0007829|PDB:2P52" FT STRAND 261..271 FT /evidence="ECO:0007829|PDB:2P52" FT HELIX 275..286 FT /evidence="ECO:0007829|PDB:2P52" FT TURN 288..290 FT /evidence="ECO:0007829|PDB:3EXJ" SQ SEQUENCE 390 AA; 43458 MW; ED5A607378D921D7 CRC64; MTAMEESQSD ISLELPLSQE TFSGLWKLLP PEDILPSPHC MDDLLLPQDV EEFFEGPSEA LRVSGAPAAQ DPVTETPGPV APAPATPWPL SSFVPSQKTY QGNYGFHLGF LQSGTAKSVM CTYSPPLNKL FCQLAKTCPV QLWVSATPPA GSRVRAMAIY KKSQHMTEVV RRCPHHERCS DGDGLAPPQH LIRVEGNLYP EYLEDRQTFR HSVVVPYEPP EAGSEYTTIH YKYMCNSSCM GGMNRRPILT IITLEDSSGN LLGRDSFEVR VCACPGRDRR TEEENFRKKE VLCPELPPGS AKRALPTCTS ASPPQKKKPL DGEYFTLKIR GRKRFEMFRE LNEALELKDA HATEESGDSR AHSSYLKTKK GQSTSRHKKT MVKKVGPDSD //