ID P53_HUMAN Reviewed; 393 AA. AC P04637; Q15086; Q15087; Q15088; Q16535; Q16807; Q16808; Q16809; Q16810; Q16811; Q16848; Q86UG1; Q8J016; Q99659; Q9BTM4; Q9HAQ8; Q9NP68; Q9NPJ2; Q9NZD0; Q9UBI2; Q9UQ61; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 2. DT 02-OCT-2007, entry version 135. DE Cellular tumor antigen p53 (Tumor suppressor p53) (Phosphoprotein p53) (Antigen NY-CO-13). GN Name=TP53; Synonyms=P53; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=85230577; PubMed=4006916; RA Zakut-Houri R., Bienz-Tadmor B., Givol D., Oren M.; RT "Human p53 cellular tumor antigen: cDNA sequence and expression in COS cells."; RL EMBO J. 4:1251-1255(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX MEDLINE=87064416; PubMed=2946935; RA Lamb P., Crawford L.; RT "Characterization of the human p53 gene."; RL Mol. Cell. Biol. 6:1379-1385(1986). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=85267676; PubMed=3894933; RA Harlow E., Williamson N.M., Ralston R., Helfman D.M., Adams T.E.; RT "Molecular cloning and in vitro expression of a cDNA clone for human cellular tumor antigen p53."; RL Mol. Cell. Biol. 5:1601-1610(1985). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=87089826; PubMed=3025664; RA Harris N., Brill E., Shohat O., Prokocimer M., Wolf D., Arai N., Rotter V.; RT "Molecular basis for heterogeneity of the human p53 protein."; RL Mol. Cell. Biol. 6:4650-4656(1986). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89108008; PubMed=2905688; DOI=10.1016/0378-1119(88)90196-5; RA Buchman V.L., Chumakov P.M., Ninkina N.N., Samarina O.P., Georgiev G.P.; RT "A variation in the structure of the protein-coding region of the human p53 gene."; RL Gene 70:245-252(1988). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 101-393. RX MEDLINE=85126934; PubMed=6396087; RA Matlashewski G., Lamb P., Pim D., Peacock J., Crawford L., Benchimol S.; RT "Isolation and characterization of a human p53 cDNA clone: expression of the human p53 gene."; RL EMBO J. 3:3257-3262(1984). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS BURKITT LYMPHOMA, AND VARIANT ARG-72. RX MEDLINE=92007731; PubMed=1915267; RA Farrell P.J., Allan G., Shanahan F., Vousden K.H., Crook T.; RT "p53 is frequently mutated in Burkitt's lymphoma cell lines."; RL EMBO J. 10:2879-2887(1991). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-72 AND LYS-286. RX MEDLINE=93303270; PubMed=8316628; RA Allalunis-Turner M.J., Barron G.M., Day R.S. III, Dobler K.D., Mirzayans R.; RT "Isolation of two cell lines from a human malignant glioma specimen differing in sensitivity to radiation and chemotherapeutic drugs."; RL Radiat. Res. 134:349-354(1993). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-72, AND INTERACTION WITH WWOX. RX MEDLINE=21264809; PubMed=11058590; DOI=10.1074/jbc.M007140200; RA Chang N.-S., Pratt N., Heath J., Schultz L., Sleve D., Carey G.B., Zevotek N.; RT "Hyaluronidase induction of a WW domain-containing oxidoreductase that enhances tumor necrosis factor cytotoxicity."; RL J. Biol. Chem. 276:3361-3370(2001). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Chumakov P.M., Almazov V.P., Jenkins J.R.; RL Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Rozemuller E.H., Tilanus M.G.J.; RT "P53 genomic sequence. Corrections and polymorphism."; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-47; ARG-72; LYS-339 AND ALA-366. RA Livingston R.J., Rieder M.J., Chung M.-W., Ritchie T.K., Olson A.N., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.; RT "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-72 AND LYS-286. RX PubMed=11023613; RA Anderson C.W., Allalunis-Turner M.J.; RT "Human TP53 from the malignant glioma-derived cell lines M059J and M059K has a cancer-associated mutation in exon 8."; RL Radiat. Res. 154:473-476(2000). RN [14] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ARG-72; HIS-273 AND SER-309. RA Azuma K., Shichijo S., Itoh K.; RT "Identification of a tumor-rejection antigen recognized by HLA-B46 restricted CTL."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [15] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-72 AND ALA-278. RC TISSUE=Kidney; 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: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [16] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-379, AND VARIANTS ARG-72 AND ASN-139. RC TISSUE=Lung carcinoma; RX PubMed=14660794; DOI=10.1073/pnas.2536558100; RA Kanashiro C.A., Schally A.V., Groot K., Armatis P., Bernardino A.L., Varga J.L.; RT "Inhibition of mutant p53 expression and growth of DMS-153 small cell lung carcinoma by antagonists of growth hormone-releasing hormone and bombesin."; RL Proc. Natl. Acad. Sci. U.S.A. 100:15836-15841(2003). RN [17] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 126-185. RA Pan X.L., Zhang A.H.; RT "Study on the effect of tumor suppressor gene p53 in arsenism patients."; RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases. RN [18] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 261-298. RC TISSUE=Blood; RA Nimri L.F., Owais W., Momani E.; RT "Detection of P53 gene mutations and serum p53 antibodies associated with cigarette smoking."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [19] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 262-306. RC TISSUE=Ovarian adenocarcinoma; RA Filippini G., Soldati G.; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. RN [20] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 225-260. RC TISSUE=Glial cell, and Glial tumor; RA Thompson-Hehir J., Davies M.P.A., Green J.A., Halliwell N., Joyce K.A., Salisbury J., Sibson D.R., Vergote I., Walker C.; RT "Mutation detection utilizing a novel PCR approach for amplification of the p53 gene from microdissected tissue: application to archival tumor samples."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [21] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 225-260. RA Yavuz A.S., Farner N.L., Yavuz S., Grammer A.C., Girschick H.J., Lipsky P.E.; RT "Bcl6 and P53 gene mutations in tonsillar B cells."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [22] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 332-366. RA Pinto E.M., Mendonca B.B., Latronico A.C.; RT "Allelic variant in intron 9 of TP53 gene."; RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases. RN [23] RP RNA-BINDING. RX MEDLINE=91141509; PubMed=1705009; RA Samad A., Carroll R.B.; RT "The tumor suppressor p53 is bound to RNA by a stable covalent linkage."; RL Mol. Cell. Biol. 11:1598-1606(1991). RN [24] RP ALTERNATIVE SPLICING. RX MEDLINE=96197761; PubMed=8632903; RA Flaman J.-M., Waridel F., Estreicher A., Vannier A., Limacher J.-M., Gilbert D., Iggo R., Frebourg T.; RT "The human tumour suppressor gene p53 is alternatively spliced in normal cells."; RL Oncogene 12:813-818(1996). RN [25] RP NUCLEAR LOCALIZATION SIGNAL. RX MEDLINE=90191730; PubMed=2156209; RA Addison C., Jenkins J.R., Sturzbecher H.-W.; RT "The p53 nuclear localisation signal is structurally linked to a p34cdc2 kinase motif."; RL Oncogene 5:423-426(1990). RN [26] RP MINIMAL REPRESSION DOMAIN. RX MEDLINE=21125692; PubMed=11007800; DOI=10.1074/jbc.M008231200; RA Hong T.M., Chen J.J., Peck K., Yang P.C., Wu C.W.; RT "p53 amino acids 339-346 represent the minimal p53 repression domain."; RL J. Biol. Chem. 276:1510-1515(2001). RN [27] RP INTERACTION WITH ING4. RX MEDLINE=22635239; PubMed=12750254; RA Shiseki M., Nagashima M., Pedeux R.M., Kitahama-Shiseki M., Miura K., Okamura S., Onogi H., Higashimoto Y., Appella E., Yokota J., Harris C.C.; RT "p29ING4 and p28ING5 bind to p53 and p300, and enhance p53 activity."; RL Cancer Res. 63:2373-2378(2003). RN [28] RP PHOSPHORYLATION BY P60/CDC2 AND CYCLIN B/CDC2. RX MEDLINE=90280456; PubMed=2141171; RA Bischoff J.R., Friedman P.N., Marshak D.R., Prives C., Beach D.; RT "Human p53 is phosphorylated by p60-cdc2 and cyclin B-cdc2."; RL Proc. Natl. Acad. Sci. U.S.A. 87:4766-4770(1990). RN [29] RP DEPHOSPHORYLATION BY PP2A. RX MEDLINE=91172186; PubMed=1848668; RA Scheidtmann K.H., Mumby M.C., Rundell K., Walter G.; RT "Dephosphorylation of simian virus 40 large-T antigen and p53 protein by protein phosphatase 2A: inhibition by small-t antigen."; RL Mol. Cell. Biol. 11:1996-2003(1991). RN [30] RP O-GLYCOSYLATION. RX MEDLINE=96197773; PubMed=8632915; RA Shaw P., Freeman J., Bovey R., Iggo R.; RT "Regulation of specific DNA binding by p53: evidence for a role for O-glycosylation and charged residues at the carboxy-terminus."; RL Oncogene 12:921-930(1996). RN [31] RP PHOSPHORYLATION AT THR-18. RX MEDLINE=20406546; PubMed=10951572; DOI=10.1038/sj.onc.1203709; RA Lopez-Borges S., Lazo P.A.; RT "The human vaccinia-related kinase 1 (VRK1) phosphorylates threonine-18 within the mdm-2 binding site of the p53 tumour suppressor protein."; RL Oncogene 19:3656-3664(2000). RN [32] RP ACETYLATION AT LYS-373 AND LYS-382. RX MEDLINE=20123976; PubMed=10656795; DOI=10.1006/jmbi.1999.3415; RA Abraham J., Kelly J., Thibault P., Benchimol S.; RT "Post-translational modification of p53 protein in response to ionizing radiation analyzed by mass spectrometry."; RL J. Mol. Biol. 295:853-864(2000). RN [33] RP DEACETYLATION AT LYS-382 BY SIRT1. RX MEDLINE=21526627; PubMed=11672523; DOI=10.1016/S0092-8674(01)00527-X; RA Vaziri H., Dessain S.K., Ng Eaton E., Imai S., Frye R.A., Pandita T.K., Guarente L., Weinberg R.A.; RT "hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase."; RL Cell 107:149-159(2001). RN [34] RP PHOSPHORYLATION BY PRPK. RX MEDLINE=21570176; PubMed=11546806; DOI=10.1074/jbc.M105669200; RA Abe Y., Matsumoto S., Wei S., Nezu K., Miyoshi A., Kito K., Ueda N., Shigemoto K., Hitsumoto Y., Nikawa J., Enomoto Y.; RT "Cloning and characterization of a p53-related protein kinase expressed in interleukin-2-activated cytotoxic T-cells, epithelial tumor cell lines, and the testes."; RL J. Biol. Chem. 276:44003-44011(2001). RN [35] RP PHOSPHORYLATION AT SER-392. RX PubMed=11239457; DOI=10.1016/S1097-2765(01)00176-9; RA Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H., Goodman R., Lozano G., Zhao Y., Lu H.; RT "A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1."; RL Mol. Cell 7:283-292(2001). RN [36] RP INTERACTION WITH USP7. RX PubMed=12507430; DOI=10.1016/S0092-8674(02)01199-6; RA Hu M., Li P., Li M., Li W., Yao T., Wu J.-W., Gu W., Cohen R.E., Shi Y.; RT "Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde."; RL Cell 111:1041-1054(2002). RN [37] RP IDENTIFICATION IN A COMPLEX WITH CABLES1 AND TP73. RX MEDLINE=21659718; 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 [38] RP INTERACTION WITH HIPK2. RX MEDLINE=22191252; PubMed=11925430; DOI=10.1074/jbc.M200153200; RA Kim E.-J., Park J.-S., Um S.-J.; RT "Identification and characterization of HIPK2 interacting with p73 and modulating functions of the p53 family in vivo."; RL J. Biol. Chem. 277:32020-32028(2002). RN [39] RP INTERACTION WITH HIPK2, PHOSPHORYLATION AT SER-46, AND MUTAGENESIS OF SER-46 AND LYS-382. RX MEDLINE=21638685; PubMed=11740489; DOI=10.1038/ncb715; RA Hofmann T.G., Moeller A., Sirma H., Zentgraf H., Taya Y., Droege W., Will H., Schmitz M.L.; RT "Regulation of p53 activity by its interaction with homeodomain-interacting protein kinase-2."; RL Nat. Cell Biol. 4:1-10(2002). RN [40] RP INTERACTION WITH HIPK2, AND PHOSPHORYLATION AT SER-46. RX MEDLINE=21638694; PubMed=11780126; DOI=10.1038/ncb714; RA D'Orazi G., Cecchinelli B., Bruno T., Manni I., Higashimoto Y., Saito S., Gostissa M., Coen S., Marchetti A., Del Sal G., Piaggio G., Fanciulli M., Appella E., Soddu S.; RT "Homeodomain-interacting protein kinase-2 phosphorylates p53 at Ser 46 and mediates apoptosis."; RL Nat. Cell Biol. 4:11-19(2002). RN [41] RP ACETYLATION AT LYS-305. RX MEDLINE=22726738; PubMed=12724314; DOI=10.1074/jbc.M212574200; RA Wang Y.H., Tsay Y.G., Tan B.C., Lo W.Y., Lee S.C.; RT "Identification and characterization of a novel p300-mediated p53 acetylation site, lysine 305."; RL J. Biol. Chem. 278:25568-25576(2003). RN [42] RP INTERACTION WITH P53DINP1. RX MEDLINE=22863074; PubMed=12851404; DOI=10.1074/jbc.M301979200; RA Tomasini R., Samir A.A., Carrier A., Isnardon D., Cecchinelli B., Soddu S., Malissen B., Dagorn J.-C., Iovanna J.L., Dusetti N.J.; RT "TP53INP1s and homeodomain-interacting protein kinase-2 (HIPK2) are partners in regulating p53 activity."; RL J. Biol. Chem. 278:37722-37729(2003). RN [43] RP NUCLEOCYTOPLASMIC SHUTTLING, AND NUCLEAR EXPORT SIGNAL. RX MEDLINE=22825602; PubMed=12944468; DOI=10.1128/MCB.23.18.6396-6405.2003; RA O'Keefe K., Li H., Zhang Y.; RT "Nucleocytoplasmic shuttling of p53 is essential for MDM2-mediated cytoplasmic degradation but not ubiquitination."; RL Mol. Cell. Biol. 23:6396-6405(2003). RN [44] RP INTERACTION WITH HIPK1. RX MEDLINE=22608637; PubMed=12702766; DOI=10.1073/pnas.0530308100; RA 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.; RT "Characterization of cells and gene-targeted mice deficient for the p53-binding kinase homeodomain-interacting protein kinase 1 (HIPK1)."; RL Proc. Natl. Acad. Sci. U.S.A. 100:5431-5436(2003). RN [45] RP INTERACTION WITH HRMT1L2; EP300 AND CARM1, AND FUNCTION. RX PubMed=15186775; DOI=10.1016/j.cell.2004.05.009; RA An W., Kim J., Roeder R.G.; RT "Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53."; RL Cell 117:735-748(2004). RN [46] RP PHOSPHORYLATION AT THR-55, MUTAGENESIS OF THR-55, AND INTERACTION WITH TAF1. RX PubMed=15053879; DOI=10.1016/S1097-2765(04)00123-6; RA Li H.-H., Li A.G., Sheppard H.M., Liu X.; RT "Phosphorylation on Thr-55 by TAF1 mediates degradation of p53: a role for TAF1 in cell G1 progression."; RL Mol. Cell 13:867-878(2004). RN [47] RP INTERACTION WITH BANP, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-15. RX PubMed=15701641; DOI=10.1074/jbc.M413200200; RA Jalota-Badhwar A., Singh K., Pavithra L., Kaul-Ghanekar R., Jameel S., Chattopadhyay S.; RT "Tumor suppressor SMAR1 activates and stabilizes p53 through its arginine-serine-rich motif."; RL J. Biol. Chem. 280:16019-16029(2005). RN [48] RP INTERACTION WITH WWOX, AND MUTAGENESIS OF SER-46. RX PubMed=16219768; DOI=10.1074/jbc.M505590200; RA Chang N.-S., Doherty J., Ensign A., Schultz L., Hsu L.-J., Hong Q.; RT "WOX1 is essential for tumor necrosis factor-, UV light-, staurosporine-, and p53-mediated cell death, and its tyrosine 33-phosphorylated form binds and stabilizes serine 46-phosphorylated p53."; RL J. Biol. Chem. 280:43100-43108(2005). RN [49] RP UBIQUITINATION, INTERACTION WITH SYVN1, AND SUBCELLULAR LOCATION. RX PubMed=17170702; DOI=10.1038/sj.emboj.7601490; RA Yamasaki S., Yagishita N., Sasaki T., Nakazawa M., Kato Y., Yamadera T., Bae E., Toriyama S., Ikeda R., Zhang L., Fujitani K., Yoo E., Tsuchimochi K., Ohta T., Araya N., Fujita H., Aratani S., Eguchi K., Komiya S., Maruyama I., Higashi N., Sato M., Senoo H., Ochi T., Yokoyama S., Amano T., Kim J., Gay S., Fukamizu A., Nishioka K., Tanaka K., Nakajima T.; RT "Cytoplasmic destruction of p53 by the endoplasmic reticulum-resident ubiquitin ligase 'Synoviolin'."; RL EMBO J. 26:113-122(2007). RN [50] RP REVIEW ON ZINC-BINDING PROPERTIES. RX MEDLINE=21438235; PubMed=11554448; DOI=10.1089/15230860152542961; RA Hainaut P., Mann K.; RT "Zinc binding and redox control of p53 structure and function."; RL Antioxid. Redox Signal. 3:611-623(2001). RN [51] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND MASS SPECTROMETRY. RX PubMed=17287340; DOI=10.1073/pnas.0611217104; RA Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; RT "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). RN [52] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND MASS SPECTROMETRY. RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [53] RP STRUCTURE BY NMR OF 319-360. RX MEDLINE=94294808; PubMed=8023159; RA Clore G.M., Omichinski J.G., Sakaguchi K., Zambrano N., Sakamoto H., Appella E., Gronenborn A.M.; RT "High-resolution structure of the oligomerization domain of p53 by multidimensional NMR."; RL Science 265:386-391(1994). RN [54] RP STRUCTURE BY NMR OF 325-355. RX MEDLINE=95292092; PubMed=7773777; DOI=10.1038/nsb1294-877; RA Lee W., Harvey T.S., Yin Y., Yau P., Litchfield D., Arrowsmith C.H.; RT "Solution structure of the tetrameric minimum transforming domain of p53."; RL Nat. Struct. Biol. 1:877-890(1994). RN [55] RP STRUCTURE BY NMR OF 326-354. RX MEDLINE=98026899; PubMed=9321402; DOI=10.1093/emboj/16.20.6230; RA McCoy M., Stavridi E.S., Waterman J.L., Wieczorek A.M., Opella S.J., Halazonetis T.D.; RT "Hydrophobic side-chain size is a determinant of the three-dimensional structure of the p53 oligomerization domain."; RL EMBO J. 16:6230-6236(1997). RN [56] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 94-289. RX MEDLINE=94294806; PubMed=8023157; RA Cho Y., Gorina S., Jeffrey P.D., Pavletich N.P.; RT "Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations."; RL Science 265:346-355(1994). RN [57] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 325-356. RX MEDLINE=95184011; PubMed=7878469; RA Jeffrey P.D., Gorina S., Pavletich N.P.; RT "Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms."; RL Science 267:1498-1502(1995). RN [58] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 13-29 IN COMPLEX WITH MDM2. RX MEDLINE=97081050; PubMed=8875929; DOI=10.1126/science.274.5289.948; RA Kussie P.H., Gorina S., Marechal V., Elenbaas B., Moreau J., Levine A.J., Pavletich N.P.; RT "Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain."; RL Science 274:948-953(1996). RN [59] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 97-287 IN COMPLEX WITH 53BP2. RX MEDLINE=97035414; PubMed=8875926; DOI=10.1126/science.274.5289.1001; RA Gorina S., Pavletich N.P.; RT "Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2."; RL Science 274:1001-1005(1996). RN [60] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 358-367 IN COMPLEX WITH USP7, AND INTERACTION WITH USP7. RX PubMed=16474402; DOI=10.1038/nsmb1067; RA Sheng Y., Saridakis V., Sarkari F., Duan S., Wu T., Arrowsmith C.H., Frappier L.; RT "Molecular recognition of p53 and MDM2 by USP7/HAUSP."; RL Nat. Struct. Mol. Biol. 13:285-291(2006). RN [61] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 360-368 IN COMPLEX WITH USP7, MUTAGENESIS OF PRO-359; GLY-361 AND SER-362, AND INTERACTION WITH USP7. RX PubMed=16402859; DOI=10.1371/journal.pbio.0040027; RA Hu M., Gu L., Li M., Jeffrey P.D., Gu W., Shi Y.; RT "Structural basis of competitive recognition of p53 and MDM2 by HAUSP/USP7: implications for the regulation of the p53-MDM2 pathway."; RL PLoS Biol. 4:228-239(2006). RN [62] RP REVIEW. RX MEDLINE=94090335; PubMed=8266092; RA Harris C.C.; RT "p53: at the crossroads of molecular carcinogenesis and risk assessment."; RL Science 262:1980-1981(1993). RN [63] RP REVIEW ON VARIANTS. RX MEDLINE=91289156; PubMed=1905840; RA Hoolstein M., Sidransky D., Vogelstein B., Harris C.C.; RT "p53 mutations in human cancers."; RL Science 253:49-53(1991). RN [64] RP REVIEW ON VARIANTS. RX MEDLINE=96271983; PubMed=8829653; DOI=10.1002/(SICI)1098-1004(1996)7:3<202::AID-HUMU4>3.3.CO;2-5; RA de Vries E.M.G., Ricke D.O., de Vries T.N., Hartmann A., Blaszyk H., Liao D., Soussi T., Kovach J.S., Sommer S.S.; RT "Database of mutations in the p53 and APC tumor suppressor genes designed to facilitate molecular epidemiological analyses."; RL Hum. Mutat. 7:202-213(1996). RN [65] RP VARIANT ARG-72. RX MEDLINE=91153807; PubMed=1999338; DOI=10.1007/BF00201836; RA Olschwang S., Laurent-Puig P., Vassal A., Salmon R.-J., Thomas G.; RT "Characterization of a frequent polymorphism in the coding sequence of the Tp53 gene in colonic cancer patients and a control population."; RL Hum. Genet. 86:369-370(1991). RN [66] RP VARIANT LFS THR-133. RX MEDLINE=92034774; PubMed=1933902; RA Law J.C., Strong L.C., Chidambaram A., Ferrell R.E.; RT "A germ line mutation in exon 5 of the p53 gene in an extended cancer family."; RL Cancer Res. 51:6385-6387(1991). RN [67] RP VARIANTS LFS CYS-245; TRP-248; PRO-252 AND LYS-258. RX MEDLINE=91057657; PubMed=1978757; RA Malkin D., Li F.P., Strong L.C., Fraumeni J.F. Jr., Nelson C.E., Kim D.H., Kassel J., Gryka M.A., Bischoff F.Z., Tainsky M.A., Friend S.H.; RT "Germ line p53 mutations in a familial syndrome of breast cancer, sarcomas, and other neoplasms."; RL Science 250:1233-1238(1990). RN [68] RP VARIANT LFS ASP-245. RX MEDLINE=91080929; PubMed=2259385; DOI=10.1038/348747a0; RA Srivastava S., Zou Z., Pirollo K., Blattner W., Chang E.H.; RT "Germ-line transmission of a mutated p53 gene in a cancer-prone family with Li-Fraumeni syndrome."; RL Nature 348:747-749(1990). RN [69] RP VARIANT LFS LEU-272. RX MEDLINE=92147883; PubMed=1737852; RA Felix C.A., Nau M.M., Takahashi T., Mitsudomi T., Chiba I., Poplack D.G., Reaman G.H., Cole D.E., Letterio J.J., Whang-Peng J., Knutsen T., Minna J.D.; RT "Hereditary and acquired p53 gene mutations in childhood acute lymphoblastic leukemia."; RL J. Clin. Invest. 89:640-647(1992). RN [70] RP VARIANTS LFS HIS-273 AND VAL-325. RX MEDLINE=92228023; PubMed=1565144; RA Malkin D., Jolly K.W., Barbier N., Look A.T., Friend S.H., Gebhardt M.C., Andersen T.I., Boerresen A.-L., Li F.P., Garber J., Strong L.C.; RT "Germline mutations of the p53 tumor-suppressor gene in children and young adults with second malignant neoplasms."; RL N. Engl. J. Med. 326:1309-1315(1992). RN [71] RP VARIANTS BREAST TUMORS GLN-132; SER-249; LYS-280 AND LYS-285. RX MEDLINE=90295284; PubMed=1694291; RA Bartek J., Iggo R., Gannon J., Lane D.P.; RT "Genetic and immunochemical analysis of mutant p53 in human breast cancer cell lines."; RL Oncogene 5:893-899(1990). RN [72] RP VARIANTS COLON TUMORS PHE-241 AND HIS-273. RX MEDLINE=91017544; PubMed=1699228; RA Rodrigues N.R., Rowan A., Smith M.E.F., Kerr I.B., Bodmer W.F., Gannon J.V., Lane D.P.; RT "p53 mutations in colorectal cancer."; RL Proc. Natl. Acad. Sci. U.S.A. 87:7555-7559(1990). RN [73] RP VARIANTS ESOPHAGUS TUMOR VAL-154; VAL-245; GLN-248; LEU-278 AND SER-278. RX MEDLINE=91088630; PubMed=2263646; RA Hollstein M.C., Metcalf R.A., Welsh J.A., Montesano R., Harris C.C.; RT "Frequent mutation of the p53 gene in human esophageal cancer."; RL Proc. Natl. Acad. Sci. U.S.A. 87:9958-9961(1990). RN [74] RP VARIANTS COLORECTAL CANCER MUTATIONS. RX MEDLINE=91282784; PubMed=1647768; DOI=10.1016/0006-291X(91)90623-F; RA Ishioka C., Sato T., Gamoh M., Suzuki T., Shibata H., Kanamaru R., Wakui A., Yamazaki T.; RT "Mutations of the P53 gene, including an intronic point mutation, in colorectal tumors."; RL Biochem. Biophys. Res. Commun. 177:901-906(1991). RN [75] RP VARIANTS ESOPHAGUS TUMORS LEU-152; ALA-155; HIS-175; PHE-176 AND HIS-273. RX MEDLINE=91330175; PubMed=1868473; RA Casson A.G., Mukhopadhyay T., Cleary K.R., Ro J.Y., Levin B., Roth J.A.; RT "p53 gene mutations in Barrett's epithelium and esophageal cancer."; RL Cancer Res. 51:4495-4499(1991). RN [76] RP VARIANTS HEPATOCELLULAR CARCINOMAS MUTATIONS IN CHINA. RX MEDLINE=91187113; PubMed=1849234; DOI=10.1038/350427a0; RA Hsu I.C., Metcalf R.A., Sun T., Welsh J.A., Wang N.J., Harris C.C.; RT "Mutational hotspot in the p53 gene in human hepatocellular carcinomas."; RL Nature 350:427-428(1991). RN [77] RP VARIANTS HEPATOCELLULAR CARCINOMAS MUTATIONS IN SOUTH AFRICA. RX MEDLINE=91187114; PubMed=1672732; DOI=10.1038/350429a0; RA Bressac B., Kew M., Wands J., Ozturk M.; RT "Selective G to T mutations of p53 gene in hepatocellular carcinoma from southern Africa."; RL Nature 350:429-431(1991). RN [78] RP VARIANTS HNSCC PHE-176; PHE-242; CYS-245; LEU-248 AND HIS-273. RX MEDLINE=93007999; PubMed=1394225; RA Somers K.D., Merrick M.A., Lopez M.E., Incognito L.S., Schechter G.L., Casey G.; RT "Frequent p53 mutations in head and neck cancer."; RL Cancer Res. 52:5997-6000(1992). RN [79] RP VARIANTS ANOGENITAL CARCINOMAS. RX MEDLINE=93010989; PubMed=1327751; RA Crook T., Vousden K.H.; RT "Properties of p53 mutations detected in primary and secondary cervical cancers suggest mechanisms of metastasis and involvement of environmental carcinogens."; RL EMBO J. 11:3935-3940(1992). RN [80] RP VARIANTS ORAL SQUAMOUS CELL CARCINOMA CYS-205; GLU-281 AND LYS-285. RX MEDLINE=93093790; PubMed=1459726; RA Sakai E., Rikimaru K., Ueda M., Matsumoto Y., Ishii N., Enomoto S., Yamamoto H., Tsuchida N.; RT "The p53 tumor-suppressor gene and ras oncogene mutations in oral squamous-cell carcinoma."; RL Int. J. Cancer 52:867-872(1992). RN [81] RP VARIANT PRO-HIS-PRO-178 INS. RX MEDLINE=93265016; PubMed=1303181; DOI=10.1093/hmg/1.3.207; RA Bhatia K., Guiterrez M.I., Magrath I.T.; RT "A novel mutation in the p53 gene in a Burkitt's lymphoma cell line."; RL Hum. Mol. Genet. 1:207-208(1992). RN [82] RP VARIANTS BURKITT LYMPHOMAS. RX MEDLINE=93064692; PubMed=1437144; RA Duthu A., Debuire B., Romano J.W., Ehrhart J.C., Fiscella M., May E., Appella E., May P.; RT "p53 mutations in Raji cells: characterization and localization relative to other Burkitt's lymphomas."; RL Oncogene 7:2161-2167(1992). RN [83] RP VARIANT NASOPHARYNGEAL CARCINOMA THR-280. RX MEDLINE=92335329; PubMed=1631151; RA Sun Y., Hegamyer G., Heng Y.-J., Hildesheim A., Chen J.-Y., Chen I.-H., Cao Y., Yao K.-T., Colburn N.H.; RT "An infrequent point mutation of the p53 gene in human nasopharyngeal carcinoma."; RL Proc. Natl. Acad. Sci. U.S.A. 89:6516-6520(1992). RN [84] RP VARIANTS HNSCC. RX MEDLINE=93235942; PubMed=7682763; RA Caamano J., Zhang S.Y., Rosvold E.A., Bauer B., Klein-Szanto A.J.P.; RT "p53 alterations in human squamous cell carcinomas and carcinoma cell lines."; RL Am. J. Pathol. 142:1131-1139(1993). RN [85] RP VARIANTS HNSCC. RX MEDLINE=94006220; PubMed=8402617; RA Boyle J.O., Hakim J., Koch W., van der Riet P., Hruban R.H., Roa R.A., Correo R., Eby Y.J., Ruppert J.M., Sidransky D.; RT "The incidence of p53 mutations increases with progression of head and neck cancer."; RL Cancer Res. 53:4477-4480(1993). RN [86] RP VARIANTS COLON TUMORS. RX MEDLINE=93330562; PubMed=8336944; RA Hamelin R., Jego N., Laurent-Puig P., Vidaud M., Thomas G.; RT "Efficient screening of p53 mutations by denaturing gradient gel electrophoresis in colorectal tumors."; RL Oncogene 8:2213-2220(1993). RN [87] RP CHARACTERIZATION OF VARIANT ALA-143. RX MEDLINE=94283378; PubMed=8013454; RA Zhang W., Guo X.-Y., Hu G.-Y., Liu W.-B., Shay J.W., Deisseroth A.B.; RT "A temperature-sensitive mutant of human p53."; RL EMBO J. 13:2535-2544(1994). RN [88] RP VARIANTS LFS HIS-175; ARG-193; GLN-248; CYS-273 AND TYR-275. RX MEDLINE=95193787; PubMed=7887414; RA Frebourg T., Barbier N., Yan Y.-X., Garber J.E., Dreyfus M., Fraumeni J.F. Jr., Li F.P., Friend S.H.; RT "Germ-line p53 mutations in 15 families with Li-Fraumeni syndrome."; RL Am. J. Hum. Genet. 56:608-615(1995). RN [89] RP VARIANT LFS HIS-175. RX MEDLINE=96423319; PubMed=8825920; RA Varley J.M., McGrown G., Thorncroft M., Tricker K.J., Teare M.D., Santibanez-Koref M.F., Houlston R.S., Martin J., Birch J.M., Evans D.G.R.; RT "An extended Li-Fraumeni kindred with gastric carcinoma and a codon 175 mutation in TP53."; RL J. Med. Genet. 32:942-945(1995). RN [90] RP VARIANTS ESOPHAGEAL ADENOCARCINOMA PHE-176; SER-245; TRP-248; TRP-282 AND GLN-286. RX MEDLINE=96233927; PubMed=8829627; DOI=10.1002/(SICI)1098-1004(1996)7:2<109::AID-HUMU4>3.3.CO;2-0; RA Audrezet M.-P., Robaszkiewicz M., Mercier B., Nousbaum J.-B., Hardy E., Bail J.-P., Volant A., Lozac'H P., Gouerou H., Ferec C.; RT "Molecular analysis of the TP53 gene in Barrett's adenocarcinoma."; RL Hum. Mutat. 7:109-113(1996). RN [91] RP VARIANTS COLORECTAL TUMORS. RX MEDLINE=97255965; PubMed=9101296; DOI=10.1002/(SICI)1098-1004(1997)9:4<348::AID-HUMU8>3.3.CO;2-7; RA Guldberg P., Nedergaard T., Nielsen H.J., Olsen A.C., Ahrenkiel V., Zeuthen J.; RT "Single-step DGGE-based mutation scanning of the p53 gene: application to genetic diagnosis of colorectal cancer."; RL Hum. Mutat. 9:348-355(1997). RN [92] RP VARIANT COLORECTAL CARCINOMA ILE-157. RX MEDLINE=98080146; PubMed=9419979; DOI=10.1038/sj.onc.1201668; RA Miyaki M., Nishio J., Konishi M., Kikuchi-Yanoshita R., Tanaka K., Muraoka M., Nagato M., Chong J.-M., Koike M., Terada T., Kawahara Y., Fukutome A., Tomiyama J., Chuganji Y., Momoi M., Utsunomiya J.; RT "Drastic genetic instability of tumors and normal tissues in Turcot syndrome."; RL Oncogene 15:2877-2881(1997). RN [93] RP VARIANTS SER-152; ILE-169; PHE-176; THR-195; CYS-220; ILE-230; CYS-273 AND SER-278. RX MEDLINE=98111377; PubMed=9450901; DOI=10.1002/(SICI)1098-1004(1998)11:1<39::AID-HUMU6>3.0.CO;2-G; RA van Rensburg E.J., Engelbrecht S., van Heerden W.F.P., Kotze M.J., Raubenheimer E.J.; RT "Detection of p53 gene mutations in oral squamous cell carcinomas of a black African population sample."; RL Hum. Mutat. 11:39-44(1998). RN [94] RP VARIANT NON-CLASSICAL LFS CYS-337. RX MEDLINE=98112421; PubMed=9452042; RA Luca J.W., Strong L.C., Hansen M.F.; RT "A germline missense mutation R337C in exon 10 of the human p53 gene."; RL Hum. Mutat. Suppl. 1:S58-S61(1998). RN [95] RP VARIANT LFS ILE-292. RX MEDLINE=99414637; PubMed=10484981; DOI=10.1016/S0165-4608(98)00276-3; RA Gueran S., Tunca Y., Imirzalioglu N.; RT "Hereditary TP53 codon 292 and somatic P16INK4A codon 94 mutations in a Li-Fraumeni syndrome family."; RL Cancer Genet. Cytogenet. 113:145-151(1999). RN [96] RP VARIANT ADCC HIS-337. RX PubMed=11481490; DOI=10.1073/pnas.161479898; RA Ribeiro R.C., Sandrini F., Figueiredo B., Zambetti G.P., Michalkiewicz E., Lafferty A.R., DeLacerda L., Rabin M., Cadwell C., Sampaio G., Cat I., Stratakis C.A., Sandrini R.; RT "An inherited p53 mutation that contributes in a tissue-specific manner to pediatric adrenal cortical carcinoma."; RL Proc. Natl. Acad. Sci. U.S.A. 98:9330-9335(2001). RN [97] RP INVOLVEMENT IN CHOROID PLEXUS PAPILLOMA. RX MEDLINE=22079076; PubMed=12085209; DOI=10.1038/sj.bjc.6600269; RA Rutherford J., Chu C.E., Duddy P.M., Charlton R.S., Chumas P., Taylor G.R., Lu X., Barnes D.M., Camplejohn R.S.; RT "Investigations on a clinically and functionally unusual and novel germline p53 mutation."; RL Br. J. Cancer 86:1592-1596(2002). RN [98] RP VARIANTS PRO-110; VAL-113; VAL-138; CYS-163; HIS-163; THR-195; MET-216; ALA-241; MET-249; SER-251; TYR-259 AND CYS-273. RX PubMed=17224074; DOI=10.1186/bcr1637; RA Chanock S.J., Burdett L., Yeager M., Llaca V., Langeroed A., Presswalla S., Kaaresen R., Strausberg R.L., Gerhard D.S., Kristensen V., Perou C.M., Boerresen-Dale A.L.; RT "Somatic sequence alterations in twenty-one genes selected by expression profile analysis of breast carcinomas."; RL Breast Cancer Res. 9:R5-R5(2007). CC -!- 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. CC -!- COFACTOR: Binds 1 zinc ion per subunit. CC -!- SUBUNIT: Interacts with AXIN1. Probably part of a complex consisting of TP53, HIPK2 and AXIN1 (By similarity). Binds DNA as a homotetramer. Interacts with histone acetyltransferases EP300 and methyltransferases HRMT1L2 and CARM1, and recruits them to promoters. In vitro, the interaction of TP53 with cancer-associated/HPV (E6) viral proteins leads to ubiquitination and degradation of TP53 giving a possible model for cell growth regulation. This complex formation requires an additional factor, E6-AP, which stably associates with TP53 in the presence of E6. C-terminus interacts with TAF1, when TAF1 is part of the TFIID complex. Interacts with ING4 and this interaction may be indirect. Found in a complex with CABLES1 and TP73. Interacts with HIPK1, HIPK2, and P53DINP1. Interacts with WWOX. May interacts with HCV core protein. Interacts with USP7 and SYVN1. Interacts with HSP90AB1 (By similarity). Interacts with BANP. CC -!- INTERACTION: CC Q13535:ATR; NbExp=1; IntAct=EBI-366083, EBI-968983; CC Q07817-1:BCL2L1; NbExp=2; IntAct=EBI-366083, EBI-287195; CC P51813:BMX; NbExp=1; IntAct=EBI-366083, EBI-696657; CC Q9BX70:BTBD2; NbExp=1; IntAct=EBI-366083, EBI-710091; CC Q8TDN4:CABLES1; NbExp=1; IntAct=EBI-366083, EBI-604615; CC Q9ESJ1:Cables1 (xeno); NbExp=1; IntAct=EBI-366083, EBI-604411; CC P17676:CEBPB; NbExp=3; IntAct=EBI-366083, EBI-969696; CC Q92793:CREBBP; NbExp=3; IntAct=EBI-366083, EBI-81215; CC Q09472:EP300; NbExp=1; IntAct=EBI-366083, EBI-447295; CC Q86XK2:FBXO11; NbExp=3; IntAct=EBI-366083, EBI-1047804; CC Q9BVP2:GNL3; NbExp=1; IntAct=EBI-366083, EBI-641642; CC P42858:HD; NbExp=2; IntAct=EBI-366083, EBI-466029; CC Q13547:HDAC1; NbExp=1; IntAct=EBI-366083, EBI-301834; CC Q86Z02:HIPK1; NbExp=1; IntAct=EBI-366083, EBI-692891; CC P09429:HMGB1; NbExp=1; IntAct=EBI-366083, EBI-389432; CC Q8N9B5:JMY; NbExp=1; IntAct=EBI-366083, EBI-866435; CC Q15759:MAPK11; NbExp=1; IntAct=EBI-366083, EBI-298304; CC Q15759-2:MAPK11; NbExp=1; IntAct=EBI-366083, EBI-303766; CC Q8IW41:MAPKAPK5; NbExp=1; IntAct=EBI-366083, EBI-1201460; CC Q00987:MDM2; NbExp=2; IntAct=EBI-366083, EBI-389668; CC Q8WYJ1:MDM2; NbExp=1; IntAct=EBI-366083, EBI-782738; CC P56273:mdm2 (xeno); NbExp=1; IntAct=EBI-366083, EBI-541233; CC P23511:NFYA; NbExp=2; IntAct=EBI-366083, EBI-389739; CC P06748:NPM1; NbExp=3; IntAct=EBI-366083, EBI-78579; CC P06748-1:NPM1; NbExp=1; IntAct=EBI-366083, EBI-354150; CC P09874:PARP1; NbExp=1; IntAct=EBI-366083, EBI-355676; CC Q96KB5:PBK; NbExp=2; IntAct=EBI-366083, EBI-536853; CC O75925:PIAS1; NbExp=1; IntAct=EBI-366083, EBI-629434; CC Q8N2W9:PIAS4; NbExp=1; IntAct=EBI-366083, EBI-473160; CC P29590:PML; NbExp=1; IntAct=EBI-366083, EBI-295890; CC P36873-1:PPP1CC; NbExp=2; IntAct=EBI-366083, EBI-356289; CC Q06609:RAD51; NbExp=1; IntAct=EBI-366083, EBI-297202; CC P27694:RPA1; NbExp=1; IntAct=EBI-366083, EBI-621389; CC Q8WTS6:SETD7; NbExp=3; IntAct=EBI-366083, EBI-1268586; CC Q96ST3:SIN3A; NbExp=2; IntAct=EBI-366083, EBI-347218; CC P20226:TBP; NbExp=1; IntAct=EBI-366083, EBI-355371; CC Q13625:TP53BP2; NbExp=1; IntAct=EBI-366083, EBI-77642; CC Q05086:UBE3A; NbExp=1; IntAct=EBI-366083, EBI-954357; CC Q7Z6Z7:UREB1; NbExp=2; IntAct=EBI-366083, EBI-625934; CC Q93009:USP7; NbExp=4; IntAct=EBI-366083, EBI-302474; CC Q14191:WRN; NbExp=2; IntAct=EBI-366083, EBI-368417; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Endoplasmic reticulum. Note=Interaction with BANP promotes nuclear localization. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P04637-1; Sequence=Displayed; CC Name=2; Synonyms=I9RET; CC IsoId=P04637-2; Sequence=VSP_006535, VSP_006536; CC Note=Seems to be non-functional. Expressed in quiescent lymphocytes; CC -!- DOMAIN: The nuclear export signal acts as a transcriptional repression domain. CC -!- PTM: Acetylated. Acetylation of Lys-382 by CREBBP enhances transcriptional activity. Deacetylation of Lys-382 by SIRT1 impairs its ability to induce proapoptotic program and modulate cell senescence. CC -!- PTM: Phosphorylation on Ser residues mediates transcriptional activation. Phosphorylated by HIPK1 (By similarity). Phosphorylated on Thr-18 by VRK1, which may prevent the interaction with MDM2. Phosphorylated on Thr-55 by TAF1, which promotes MDM2-mediated degradation. Phosphorylated on Ser-46 by HIPK2 upon UV irradiation. Phosphorylation on Ser-46 is required for acetylation by CREBBP. Phosphorylated on Ser-392 following UV but not gamma irradiation. Phosphorylated upon DNA damage, probably by ATM or ATR. Phosphorylated on Ser-15 upon ultraviolet irradiation; which is enhanced by interaction with BANP. CC -!- PTM: Dephosphorylated by PP2A. SV40 small T antigen inhibits the dephosphorylation by the AC form of PP2A. CC -!- PTM: May be O-glycosylated in the C-terminal basic region. Studied in EB-1 cell line. CC -!- PTM: Ubiquitinated by SYVN1, which leads to proteasomal degradation. CC -!- DISEASE: TP53 is found in increased amounts in a wide variety of transformed cells. TP53 is frequently mutated or inactivated in about 60% of cancers. CC -!- DISEASE: Defects in TP53 are involved in esophageal squamous cell carcinoma (ESCC) [MIM:133239]. ESCC is a tumor of the esophagus. CC -!- DISEASE: Defects in TP53 are a cause of Li-Fraumeni syndrome (LFS) [MIM:151623]. LFS is an autosomal dominant familial cancer syndrome that in its classic form is defined by the existence of both a proband with a sarcoma and two other first-degree relatives with a cancer by age 45 years. In these families the affected relatives develop a diverse set of malignancies at unusually early ages. The spectrum of cancers in LFS includes breast carcinomas, soft-tissue sarcomas, brain tumors, osteosarcoma, leukemia and adreno-cortical carcinoma. Other possible component tumors of LFS are melanoma, gonadal cell tumors and carcinomas of the lung, pancreas and prostate. CC -!- DISEASE: Defects in TP53 may be associated with nasopharyngeal carcinoma [MIM:161550]; also known as nasopharyngeal cancer. CC -!- DISEASE: Defects in TP53 are found in Barrett metaplasia; also known as Barrett esophagus. It is a condition in which the normally stratified squamous epithelium of the lower esophagus is replaced by a metaplastic columnar epithelium. The condition develops as a complication in approximately 10% of patients with chronic gastroesophageal reflux disease and predisposes to the development of esophageal adenocarcinoma. CC -!- DISEASE: Defects in TP53 are involved in head and neck squamous cell carcinomas (HNSCC) [MIM:275355]. CC -!- DISEASE: Defects in TP53 are involved in oral squamous cell carcinoma (OSCC). Cigarette smoke is a prime mutagenic agent in cancer of the aerodigestive tract. CC -!- DISEASE: Defects in TP53 are a cause of lung cancer [MIM:211980]. CC -!- DISEASE: Defects in TP53 are a cause of choroid plexus papilloma [MIM:260500]. Choroid plexus papilloma is a slow-growing benign tumor of the choroid plexus that often invades the leptomeninges. In children it is usually in a lateral ventricle but in adults it is more often in the fourth ventricle. Hydrocephalus is common, either from obstruction or from tumor secretion of cerebrospinal fluid. If it undergoes malignant transformation it is called a choroid plexus carcinoma. Primary choroid plexus tumors are rare and usually occur in early childhood. CC -!- DISEASE: Defects in TP53 are a cause of one form of hereditary adrenocortical carcinoma (ADCC) [MIM:202300]. ADCC is a rare childhood tumor, representing about 0.4% of childhood tumors, with a high incidence of associated tumors. ADCC occurs with increased frequency in patients with the Beckwith-Wiedemann syndrome [MIM:130650] and is a component tumor in Li-Fraumeni syndrome [MIM:151623]. CC -!- SIMILARITY: Belongs to the p53 family. CC -!- WEB RESOURCE: Name=IARC TP53 mutation database; Note=Somatic and germline TP53 mutations in human cancers; URL="http://www-p53.iarc.fr/"; CC -!- WEB RESOURCE: Name=p53 web site at the Institut Curie; URL="http://p53.free.fr/"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/P53ID88.html"; CC -!- WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=TP53"; CC -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and polymorphism database; URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=TP53"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=P53 entry; URL="http://en.wikipedia.org/wiki/P53"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X02469; CAA26306.1; -; mRNA. DR EMBL; M13121; AAA59987.1; -; Genomic_DNA. DR EMBL; M13112; AAA59987.1; JOINED; Genomic_DNA. DR EMBL; M13113; AAA59987.1; JOINED; Genomic_DNA. DR EMBL; M13114; AAA59987.1; JOINED; Genomic_DNA. DR EMBL; M13115; AAA59987.1; JOINED; Genomic_DNA. DR EMBL; M13116; AAA59987.1; JOINED; Genomic_DNA. DR EMBL; M13117; AAA59987.1; JOINED; Genomic_DNA. DR EMBL; M13118; AAA59987.1; JOINED; Genomic_DNA. DR EMBL; M13119; AAA59987.1; JOINED; Genomic_DNA. DR EMBL; M13120; AAA59987.1; JOINED; Genomic_DNA. DR EMBL; K03199; AAA59989.1; -; mRNA. DR EMBL; M14694; AAA61211.1; -; mRNA. DR EMBL; M14695; AAA61212.1; -; mRNA. DR EMBL; M22898; AAA59988.1; -; Genomic_DNA. DR EMBL; M22882; AAA59988.1; JOINED; Genomic_DNA. DR EMBL; M22883; AAA59988.1; JOINED; Genomic_DNA. DR EMBL; M22884; AAA59988.1; JOINED; Genomic_DNA. DR EMBL; M22887; AAA59988.1; JOINED; Genomic_DNA. DR EMBL; M22888; AAA59988.1; JOINED; Genomic_DNA. DR EMBL; M22894; AAA59988.1; JOINED; Genomic_DNA. DR EMBL; M22895; AAA59988.1; JOINED; Genomic_DNA. DR EMBL; M22896; AAA59988.1; JOINED; Genomic_DNA. DR EMBL; M22897; AAA59988.1; JOINED; Genomic_DNA. DR EMBL; X01405; CAA25652.1; -; mRNA. DR EMBL; X60011; CAA42626.1; -; mRNA. DR EMBL; X60012; CAA42627.1; ALT_TERM; mRNA. DR EMBL; X60013; CAA42628.1; -; mRNA. DR EMBL; X60014; CAA42629.1; -; mRNA. DR EMBL; X60015; CAA42630.1; -; mRNA. DR EMBL; X60016; CAA42631.1; -; mRNA. DR EMBL; X60017; CAA42632.1; -; mRNA. DR EMBL; X60018; CAA42633.1; -; mRNA. DR EMBL; X60019; CAA42634.1; -; mRNA. DR EMBL; X60020; CAA42635.1; -; mRNA. DR EMBL; AF135121; AAD28535.1; -; Genomic_DNA. DR EMBL; AF135120; AAD28535.1; JOINED; Genomic_DNA. DR EMBL; AF307851; AAG28785.1; -; mRNA. DR EMBL; X54156; CAA38095.1; -; Genomic_DNA. DR EMBL; U94788; AAC12971.1; -; Genomic_DNA. DR EMBL; AF136271; AAD28628.1; -; Genomic_DNA. DR EMBL; AF136270; AAD28628.1; JOINED; Genomic_DNA. DR EMBL; AB082923; BAC16799.1; -; mRNA. DR EMBL; AY838896; AAV80424.1; -; Genomic_DNA. DR EMBL; BC003596; AAH03596.1; -; mRNA. DR EMBL; AY429684; AAR10356.1; -; mRNA. DR EMBL; AY390341; AAQ90158.1; -; Genomic_DNA. DR EMBL; AY359814; AAR13239.1; -; Genomic_DNA. DR EMBL; U63714; AAB39322.1; -; Genomic_DNA. DR EMBL; AF209136; AAF36362.1; -; Genomic_DNA. DR EMBL; AF209128; AAF36354.1; -; Genomic_DNA. DR EMBL; AF209129; AAF36355.1; -; Genomic_DNA. DR EMBL; AF209130; AAF36356.1; -; Genomic_DNA. DR EMBL; AF209131; AAF36357.1; -; Genomic_DNA. DR EMBL; AF209132; AAF36358.1; -; Genomic_DNA. DR EMBL; AF209133; AAF36359.1; -; Genomic_DNA. DR EMBL; AF209134; AAF36360.1; -; Genomic_DNA. DR EMBL; AF209135; AAF36361.1; -; Genomic_DNA. DR EMBL; AF209148; AAF36374.1; -; Genomic_DNA. DR EMBL; AF209149; AAF36375.1; -; Genomic_DNA. DR EMBL; AF209150; AAF36376.1; -; Genomic_DNA. DR EMBL; AF209151; AAF36377.1; -; Genomic_DNA. DR EMBL; AF209152; AAF36378.1; -; Genomic_DNA. DR EMBL; AF209153; AAF36379.1; -; Genomic_DNA. DR EMBL; AF209154; AAF36380.1; -; Genomic_DNA. DR EMBL; AF209155; AAF36381.1; -; Genomic_DNA. DR EMBL; AF209156; AAF36382.1; -; Genomic_DNA. DR EMBL; AF210309; AAF63442.1; -; Genomic_DNA. DR EMBL; AF210308; AAF63442.1; JOINED; Genomic_DNA. DR EMBL; AF210310; AAF63443.1; -; Genomic_DNA. DR EMBL; AF240684; AAK76358.1; -; Genomic_DNA. DR EMBL; AF240685; AAK76359.1; -; Genomic_DNA. DR EMBL; AY270155; AAP30003.1; -; Genomic_DNA. DR PIR; A25224; DNHU53. DR RefSeq; NP_000537.3; -. DR UniGene; Hs.654481; -. DR PDB; 1A1U; NMR; A/C=324-358. DR PDB; 1AIE; X-ray; @=326-356. DR PDB; 1C26; X-ray; A=325-356. DR PDB; 1DT7; NMR; X/Y=367-388. DR PDB; 1GZH; X-ray; A/C=-. DR PDB; 1H26; X-ray; E=376-386. DR PDB; 1HS5; NMR; A/B=324-357. DR PDB; 1JSP; NMR; A=367-386. DR PDB; 1KZY; X-ray; A/B=95-289. DR PDB; 1OLG; NMR; A/B/C/D=319-360. DR PDB; 1OLH; NMR; A/B/C/D=319-360. DR PDB; 1PES; NMR; A/B/C/D=325-355. DR PDB; 1PET; NMR; A/B/C/D=325-355. DR PDB; 1SAE; NMR; A/B/C/D=319-360. DR PDB; 1SAF; NMR; A/B/C/D=319-360. DR PDB; 1SAG; NMR; A/B/C/D=319-360. DR PDB; 1SAH; NMR; A/B/C/D=319-360. DR PDB; 1SAI; NMR; A/B/C/D=319-360. DR PDB; 1SAJ; NMR; A/B/C/D=319-360. DR PDB; 1SAK; NMR; A/B/C/D=319-360. DR PDB; 1SAL; NMR; A/B/C/D=319-360. DR PDB; 1TSR; X-ray; A/B/C=94-312. DR PDB; 1TUP; X-ray; A/B/C=94-312. DR PDB; 1UOL; X-ray; A/B=94-312. DR PDB; 1YCQ; X-ray; B=13-29. DR PDB; 1YCR; X-ray; B=15-29. DR PDB; 1YCS; X-ray; A=94-292. DR PDB; 2B3G; X-ray; B=33-60. DR PDB; 2BIM; X-ray; A/B=94-312. DR PDB; 2BIN; X-ray; A=94-312. DR PDB; 2BIO; X-ray; A=94-312. DR PDB; 2BIP; X-ray; A=94-312. DR PDB; 2BIQ; X-ray; A=94-312. DR PDB; 2F1X; X-ray; A/B=360-368. DR PDB; 2FEJ; NMR; A=94-297. DR PDB; 2FOJ; X-ray; B=363-367. DR PDB; 2FOO; X-ray; B=358-363. DR PDB; 2J1W; X-ray; A/B=94-312. DR PDB; 2J1X; X-ray; A/B=94-312. DR PDB; 2J1Y; X-ray; A/B/C/D=94-293. DR PDB; 2J1Z; X-ray; A/B=94-312. DR PDB; 2J20; X-ray; A/B=94-312. DR PDB; 2J21; X-ray; A/B=94-312. DR PDB; 3SAK; NMR; A/B/C/D=319-360. DR DisProt; DP00086; -. DR DIP; DIP:368N; -. DR IntAct; P04637; -. DR TRANSFAC; T00671; -. DR SWISS-2DPAGE; P04637; HUMAN. DR Ensembl; ENSG00000141510; Homo sapiens. DR GeneID; 7157; -. DR KEGG; hsa:7157; -. DR H-InvDB; HIX0013510; -. DR HGNC; HGNC:11998; TP53. DR HPA; CAB002973; -. DR MIM; 133239; phenotype. DR MIM; 151623; phenotype. DR MIM; 161550; phenotype. DR MIM; 191170; gene+phenotype. DR MIM; 202300; phenotype. DR MIM; 211980; phenotype. DR MIM; 260500; phenotype. DR MIM; 275355; phenotype. DR Orphanet; 1501; Adrenocortical carcinoma. DR Orphanet; 70482; Esophageal carcinoma. DR Orphanet; 33402; Hepatocellular carcinoma of childhood. DR Orphanet; 524; Li-Fraumeni syndrome. DR Orphanet; 1333; Pancreatic carcinoma. DR Orphanet; 2807; Papilloma of choroid plexus. DR Orphanet; 67037; Squamous cell carcinoma of head and neck. DR PharmGKB; PA36679; -. DR Reactome; REACT_1538; Cell Cycle Checkpoints. DR LinkHub; P04637; -. DR ArrayExpress; P04637; -. DR GermOnline; ENSG00000141510; Homo sapiens. DR GO; GO:0005626; C:insoluble fraction; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB. DR GO; GO:0000739; F:DNA strand annealing activity; IDA:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0004518; F:nuclease activity; TAS:ProtInc. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB. DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB. DR GO; GO:0003700; F:transcription factor activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; TAS:UniProtKB. DR GO; GO:0006284; P:base-excision repair; TAS:UniProtKB. DR GO; GO:0008635; P:caspase activation via cytochrome c; IDA:UniProtKB. DR GO; GO:0007569; P:cell aging; IMP:UniProtKB. DR GO; GO:0007050; P:cell cycle arrest; TAS:UniProtKB. DR GO; GO:0008283; P:cell proliferation; TAS:UniProtKB. DR GO; GO:0042149; P:cellular response to glucose starvation; IDA:MGI. DR GO; GO:0042771; P:DNA damage response, signal transduction by...; IDA:MGI. DR GO; GO:0006983; P:ER overload response; IDA:MGI. DR GO; GO:0007275; P:multicellular organismal development; IMP:UniProtKB. DR GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB. DR GO; GO:0051097; P:negative regulation of helicase activity; TAS:UniProtKB. DR GO; GO:0006289; P:nucleotide-excision repair; IMP:UniProtKB. DR GO; GO:0008104; P:protein localization; IDA:UniProtKB. DR GO; GO:0051262; P:protein tetramerization; TAS:UniProtKB. DR GO; GO:0046902; P:regulation of mitochondrial membrane permea...; TAS:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IDA:UniProtKB. DR InterPro; IPR002117; p53. DR InterPro; IPR011615; p53_DNA_bd. DR InterPro; IPR012346; p53_RUNT_DNA_bd. DR InterPro; IPR013872; p53_TAD. DR InterPro; IPR010991; p53_tetrameristn. DR InterPro; IPR015551; Trp53. DR Gene3D; G3DSA:2.60.40.720; p53_RUNT_DNA_bd; 1. DR Gene3D; G3DSA:4.10.170.10; p53_tetrameristn; 1. DR PANTHER; PTHR11447; Trp53; 1. DR Pfam; PF00870; P53; 1. DR Pfam; PF08563; P53_TAD; 1. DR Pfam; PF07710; P53_tetramer; 1. DR PRINTS; PR00386; P53SUPPRESSR. DR ProDom; PD002681; P53; 1. DR PROSITE; PS00348; P53; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; Anti-oncogene; Apoptosis; Cell cycle; Covalent protein-RNA linkage; Cytoplasm; Disease mutation; DNA-binding; Endoplasmic reticulum; Glycoprotein; Host-virus interaction; Li-Fraumeni syndrome; Metal-binding; Nucleus; Phosphorylation; Polymorphism; Transcription; Transcription regulation; Ubl conjugation; Zinc. FT CHAIN 1 393 Cellular tumor antigen p53. FT /FTId=PRO_0000185703. FT DNA_BIND 102 292 FT REGION 1 83 Interaction with HRMT1L2. FT REGION 1 44 Transcription activation (acidic). FT REGION 66 110 Interaction with WWOX. FT REGION 100 370 Interaction with HIPK1 (By similarity). FT REGION 116 292 Interaction with AXIN1 (By similarity). FT REGION 241 248 Interacts with the 53BP2 SH3 domain. FT REGION 300 393 Interaction with CARM1. FT REGION 319 360 Interaction with HIPK2. FT REGION 325 356 Oligomerization. FT REGION 359 363 Interaction with USP7. FT REGION 368 387 Basic (repression of DNA-binding). FT MOTIF 305 321 Bipartite nuclear localization signal. FT MOTIF 339 350 Nuclear export signal. FT METAL 176 176 Zinc. FT METAL 179 179 Zinc. FT METAL 238 238 Zinc. FT METAL 242 242 Zinc. FT MOD_RES 15 15 Phosphoserine; by PRPK. FT MOD_RES 18 18 Phosphothreonine; by VRK1. FT MOD_RES 46 46 Phosphoserine; by HIPK2. FT MOD_RES 55 55 Phosphothreonine; by TAF1. FT MOD_RES 99 99 Phosphoserine. FT MOD_RES 305 305 N6-acetyllysine. FT MOD_RES 315 315 Phosphoserine; by CDC2. FT MOD_RES 373 373 N6-acetyllysine. FT MOD_RES 382 382 N6-acetyllysine. FT MOD_RES 392 392 O-(5'-phospho-RNA)-serine. FT MOD_RES 392 392 Phosphoserine; by CK2. FT VAR_SEQ 332 341 IRGRERFEMF -> DGTSFQKENC (in isoform 2). FT /FTId=VSP_006535. FT VAR_SEQ 342 393 Missing (in isoform 2). FT /FTId=VSP_006536. FT VARIANT 7 7 D -> H (in a skin tumor). FT /FTId=VAR_005851. FT VARIANT 35 35 L -> F (in a liver tumor). FT /FTId=VAR_005852. FT VARIANT 43 43 L -> S (in a renal tumor). FT /FTId=VAR_005853. FT VARIANT 47 47 P -> S (in dbSNP:rs1800371). FT /FTId=VAR_014632. FT VARIANT 53 53 W -> C (in a leukemia and a lymphoma). FT /FTId=VAR_005854. FT VARIANT 60 60 P -> S (in a leukemia and a lymphoma). FT /FTId=VAR_005855. FT VARIANT 72 72 P -> R (in dbSNP:rs1042522). FT /FTId=VAR_005856. FT VARIANT 79 79 A -> T (in clone P53-H-1). FT /FTId=VAR_005857. FT VARIANT 87 87 P -> Q (in a brain tumor). FT /FTId=VAR_005858. FT VARIANT 94 94 S -> T (in a colon tumor). FT /FTId=VAR_005859. FT VARIANT 110 110 R -> C (in a liver and an uterus tumor). FT /FTId=VAR_005860. FT VARIANT 110 110 R -> L (in a liver tumor). FT /FTId=VAR_005861. FT VARIANT 110 110 R -> P (in a breast tumor). FT /FTId=VAR_005862. FT VARIANT 113 113 F -> C (in a lung tumor). FT /FTId=VAR_005863. FT VARIANT 113 113 F -> V (in a breast cancer sample; somatic mutation). FT /FTId=VAR_033033. FT VARIANT 125 125 T -> M (in a lung tumor). FT /FTId=VAR_005864. FT VARIANT 126 126 Y -> D (in a colorectal tumor). FT /FTId=VAR_005865. FT VARIANT 126 126 Y -> N (in a leukemia and a lymphoma). FT /FTId=VAR_005866. FT VARIANT 127 127 S -> F (in a lung tumor). FT /FTId=VAR_005867. FT VARIANT 128 128 P -> S (in a breast tumor). FT /FTId=VAR_005868. FT VARIANT 129 129 A -> D (in a sarcoma). FT /FTId=VAR_005869. FT VARIANT 130 130 L -> R (in a liver tumor). FT /FTId=VAR_005870. FT VARIANT 131 131 N -> K (in a colon tumor). FT /FTId=VAR_005872. FT VARIANT 131 131 N -> S (in a liver tumor). FT /FTId=VAR_005871. FT VARIANT 132 132 K -> M (in a sarcoma). FT /FTId=VAR_005873. FT VARIANT 132 132 K -> Q (in a breast tumor). FT /FTId=VAR_005874. FT VARIANT 133 133 M -> T (in LFS). FT /FTId=VAR_005875. FT VARIANT 135 135 C -> F (in a colon tumor). FT /FTId=VAR_005877. FT VARIANT 135 135 C -> S (in a colon tumor). FT /FTId=VAR_005876. FT VARIANT 136 136 Q -> E (in a breast tumor). FT /FTId=VAR_005878. FT VARIANT 136 136 Q -> K (in a colon tumor). FT /FTId=VAR_005879. FT VARIANT 137 137 L -> Q (in a liver tumor). FT /FTId=VAR_005880. FT VARIANT 138 138 A -> P (in a lung tumor). FT /FTId=VAR_005881. FT VARIANT 138 138 A -> V (in a breast cancer sample; somatic mutation). FT /FTId=VAR_033034. FT VARIANT 139 139 K -> N (in a breast, an ovary tumor, a leukemia and a lymphoma). FT /FTId=VAR_005882. FT VARIANT 141 141 C -> F (in a breast tumor). FT /FTId=VAR_005885. FT VARIANT 141 141 C -> G (in an ovary tumor). FT /FTId=VAR_005884. FT VARIANT 141 141 C -> Y (in many types of tumors). FT /FTId=VAR_005886. FT VARIANT 143 143 V -> A (in a colon tumor; strong DNA binding ability at 32.5 degrees Celsius; strong reduction of transcriptional activity at 37.5 degrees Celsius). FT /FTId=VAR_005887. FT VARIANT 144 144 Q -> P (in a leukemia and a lymphoma). FT /FTId=VAR_005888. FT VARIANT 145 145 L -> P (in a brain tumor). FT /FTId=VAR_005889. FT VARIANT 145 145 L -> Q (in an esophagus tumor). FT /FTId=VAR_005890. FT VARIANT 147 147 V -> D (in an ovary tumor). FT /FTId=VAR_005891. FT VARIANT 147 147 V -> G (in a prostate tumor). FT /FTId=VAR_005892. FT VARIANT 149 149 S -> P (in a breast tumor). FT /FTId=VAR_005893. FT VARIANT 151 151 P -> A (in a brain and a colon tumor). FT /FTId=VAR_005894. FT VARIANT 151 151 P -> S (in many types of tumors). FT /FTId=VAR_005895. FT VARIANT 151 151 P -> T (in a breast tumor). FT /FTId=VAR_005896. FT VARIANT 152 152 P -> L (in an esophagus tumor). FT /FTId=VAR_005897. FT VARIANT 152 152 P -> S (in oral squamous cell carcinoma). FT /FTId=VAR_005898. FT VARIANT 153 153 P -> T (in a colon tumor). FT /FTId=VAR_005899. FT VARIANT 154 154 G -> V (in esophagus tumor). FT /FTId=VAR_005900. FT VARIANT 155 155 T -> A (in an esophagus tumor). FT /FTId=VAR_005901. FT VARIANT 156 156 R -> P (in an osteosarcoma cell line). FT /FTId=VAR_005902. FT VARIANT 157 157 V -> D (in a liver tumor). FT /FTId=VAR_005903. FT VARIANT 157 157 V -> F (in a South African hepatocellular carcinoma). FT /FTId=VAR_005904. FT VARIANT 157 157 V -> I (in colorectal carcinoma; from a patient with Turcot syndrome). FT /FTId=VAR_012977. FT VARIANT 158 158 R -> C (in a noninvasive head and neck tumor). FT /FTId=VAR_005905. FT VARIANT 158 158 R -> G (in a brain and a lung tumor). FT /FTId=VAR_005906. FT VARIANT 158 158 R -> H (in many types of tumors). FT /FTId=VAR_005907. FT VARIANT 160 160 M -> I (in a lung and a skin tumor). FT /FTId=VAR_005908. FT VARIANT 161 161 A -> S (in a brain tumor). FT /FTId=VAR_005909. FT VARIANT 162 162 I -> S (in a brain tumor). FT /FTId=VAR_005910. FT VARIANT 162 162 I -> V (in an ovary tumor). FT /FTId=VAR_005911. FT VARIANT 163 163 Y -> C (in a breast cancer sample; somatic mutation). FT /FTId=VAR_033035. FT VARIANT 163 163 Y -> H (in HNSCC and a breast cancer sample; somatic mutation). FT /FTId=VAR_005912. FT VARIANT 164 164 K -> N (in a lung tumor). FT /FTId=VAR_005913. FT VARIANT 164 164 K -> Q (in a breast tumor). FT /FTId=VAR_005914. FT VARIANT 165 165 Q -> L (in a breast tumor). FT /FTId=VAR_005915. FT VARIANT 165 165 Q -> R (in an ovary tumor). FT /FTId=VAR_005916. FT VARIANT 166 166 S -> L (in a lung tumor). FT /FTId=VAR_005917. FT VARIANT 168 168 H -> R (in a brain tumor). FT /FTId=VAR_005918. FT VARIANT 169 169 M -> I (in oral squamous cell carcinoma). FT /FTId=VAR_005919. FT VARIANT 169 169 M -> T (in a noninvasive head and neck tumor). FT /FTId=VAR_005920. FT VARIANT 170 170 T -> M (in a colon tumor). FT /FTId=VAR_005921. FT VARIANT 170 170 T -> S (in a colon tumor). FT /FTId=VAR_005922. FT VARIANT 172 172 V -> A (in a prostate tumor). FT /FTId=VAR_005923. FT VARIANT 173 173 V -> E (in a colon tumor). FT /FTId=VAR_005924. FT VARIANT 173 173 V -> L (in a cervical carcinoma). FT /FTId=VAR_005925. FT VARIANT 173 173 V -> M (in a colon tumor). FT /FTId=VAR_005926. FT VARIANT 174 174 R -> H (in the cell line Detroit 562 of squamous cell carcinoma). FT /FTId=VAR_005927. FT VARIANT 175 175 R -> C (in a colon and an uterus tumor). FT /FTId=VAR_005928. FT VARIANT 175 175 R -> G (in a brain tumor). FT /FTId=VAR_005929. FT VARIANT 175 175 R -> H (in LFS and colon/esophagus/ gastric tumors). FT /FTId=VAR_005932. FT VARIANT 175 175 R -> L (in a breast and a colon tumor). FT /FTId=VAR_005930. FT VARIANT 175 175 R -> P (in a cervical carcinoma). FT /FTId=VAR_005931. FT VARIANT 176 176 C -> F (in esophagus tumors and many types of tumors). FT /FTId=VAR_005933. FT VARIANT 176 176 C -> W (in a lung tumor). FT /FTId=VAR_005934. FT VARIANT 177 177 P -> L (in a skin tumor). FT /FTId=VAR_005935. FT VARIANT 178 178 H -> HPHP (in a Burkitt lymphoma). FT /FTId=VAR_005936. FT VARIANT 181 181 R -> L (in a cervical carcinoma). FT /FTId=VAR_005937. FT VARIANT 182 182 C -> S (in a stomach tumor). FT /FTId=VAR_005938. FT VARIANT 184 184 D -> Y (in a leukemia and a lymphoma). FT /FTId=VAR_005939. FT VARIANT 186 186 D -> Y (in a breast tumor). FT /FTId=VAR_005940. FT VARIANT 187 187 G -> C (in a breast tumor). FT /FTId=VAR_005941. FT VARIANT 187 187 G -> S (in a leukemia and a lymphoma). FT /FTId=VAR_005942. FT VARIANT 189 189 A -> P (in an ovary tumor). FT /FTId=VAR_005943. FT VARIANT 190 190 P -> L (in a colorectal tumor). FT /FTId=VAR_005944. FT VARIANT 191 191 P -> T (in a colon tumor). FT /FTId=VAR_005945. FT VARIANT 192 192 Q -> R (in a colon tumor). FT /FTId=VAR_005946. FT VARIANT 193 193 H -> D (in an uterus tumor). FT /FTId=VAR_005947. FT VARIANT 193 193 H -> R (in LFS). FT /FTId=VAR_005948. FT VARIANT 194 194 L -> P (in a colon tumor). FT /FTId=VAR_005949. FT VARIANT 194 194 L -> R (in the cell line HU 281 of squamous cell carcinoma). FT /FTId=VAR_005950. FT VARIANT 195 195 I -> T (in oral squamous cell carcinoma and a breast cancer sample; somatic mutation). FT /FTId=VAR_005951. FT VARIANT 198 198 E -> K (in HNSCC). FT /FTId=VAR_005952. FT VARIANT 205 205 Y -> C (in oral squamous cell carcinoma). FT /FTId=VAR_005953. FT VARIANT 205 205 Y -> D (in HNSCC). FT /FTId=VAR_005954. FT VARIANT 213 213 R -> Q (in a Burkitt lymphoma and a colorectal tumor). FT /FTId=VAR_005955. FT VARIANT 216 216 V -> M (in HNSCC and a breast cancer sample; somatic mutation). FT /FTId=VAR_005956. FT VARIANT 220 220 Y -> C (in oral squamous cell carcinoma). FT /FTId=VAR_005957. FT VARIANT 220 220 Y -> H (in a colon tumor). FT /FTId=VAR_005958. FT VARIANT 220 220 Y -> S (in HNSCC). FT /FTId=VAR_005959. FT VARIANT 228 228 D -> E (in HNSCC). FT /FTId=VAR_005960. FT VARIANT 230 230 T -> I (in oral squamous cell carcinoma). FT /FTId=VAR_005961. FT VARIANT 232 232 I -> T (in an anal tumor). FT /FTId=VAR_005962. FT VARIANT 234 234 Y -> C (in HNSCC). FT /FTId=VAR_005963. FT VARIANT 234 234 Y -> H (in a Burkitt's lymphoma). FT /FTId=VAR_005964. FT VARIANT 237 237 M -> I (in a colon tumor). FT /FTId=VAR_005965. FT VARIANT 238 238 C -> F (in an anal tumor). FT /FTId=VAR_005966. FT VARIANT 238 238 C -> Y (in a colorectal tumor). FT /FTId=VAR_005967. FT VARIANT 240 240 S -> I (in an anal tumor). FT /FTId=VAR_005968. FT VARIANT 241 241 S -> A (in a breast cancer sample; somatic mutation). FT /FTId=VAR_033036. FT VARIANT 241 241 S -> F (in a colon tumor). FT /FTId=VAR_005969. FT VARIANT 242 242 C -> F (in a skin tumor). FT /FTId=VAR_005970. FT VARIANT 245 245 G -> A (in a renal tumor). FT /FTId=VAR_005971. FT VARIANT 245 245 G -> C (in LFS, colon and larynx tumors). FT /FTId=VAR_005972. FT VARIANT 245 245 G -> D (in LFS and a colon tumor). FT /FTId=VAR_005973. FT VARIANT 245 245 G -> S (in esophageal adenocarcinoma and many types of tumors). FT /FTId=VAR_005974. FT VARIANT 245 245 G -> V (in HNSCC). FT /FTId=VAR_005975. FT VARIANT 246 246 M -> R (in a liver tumor). FT /FTId=VAR_005976. FT VARIANT 246 246 M -> T (in a leukemia and a lymphoma). FT /FTId=VAR_005977. FT VARIANT 246 246 M -> V (in many types of tumors). FT /FTId=VAR_005978. FT VARIANT 247 247 N -> I (in a lung tumor). FT /FTId=VAR_005980. FT VARIANT 248 248 R -> G (in an endocrine tumor). FT /FTId=VAR_005981. FT VARIANT 248 248 R -> L (in tumors of hypopharynx, larynx and tonsil). FT /FTId=VAR_005982. FT VARIANT 248 248 R -> Q (in LFS and many types of tumors). FT /FTId=VAR_005983. FT VARIANT 248 248 R -> W (in LFS, esophageal adenocarcinoma and many types of tumors). FT /FTId=VAR_005984. FT VARIANT 249 249 R -> G (in a breast tumor). FT /FTId=VAR_005985. FT VARIANT 249 249 R -> M (in a breast cancer sample; somatic mutation). FT /FTId=VAR_033037. FT VARIANT 249 249 R -> S (in many types of tumors). FT /FTId=VAR_005986. FT VARIANT 251 251 I -> N (in HNSCC). FT /FTId=VAR_005987. FT VARIANT 251 251 I -> S (in a breast cancer sample; somatic mutation). FT /FTId=VAR_033038. FT VARIANT 252 252 L -> P (in LFS and many types of tumors). FT /FTId=VAR_005988. FT VARIANT 254 254 I -> N (in a breast tumor). FT /FTId=VAR_017908. FT VARIANT 254 254 I -> T (in a colon tumor). FT /FTId=VAR_017909. FT VARIANT 257 257 L -> P (in HNSCC). FT /FTId=VAR_005989. FT VARIANT 258 258 E -> D (in a colorectal tumor). FT /FTId=VAR_005990. FT VARIANT 258 258 E -> K (in LFS). FT /FTId=VAR_005991. FT VARIANT 259 259 D -> Y (in a breast cancer sample; somatic mutation). FT /FTId=VAR_033039. FT VARIANT 272 272 V -> L (in LFS). FT /FTId=VAR_005992. FT VARIANT 273 273 R -> C (in LFS, colorectal tumor, oral squamous cell carcinoma and a breast cancer sample; somatic mutation). FT /FTId=VAR_005993. FT VARIANT 273 273 R -> G (in HNSCC). FT /FTId=VAR_005994. FT VARIANT 273 273 R -> H (in LFS, colon and esophagus tumors). FT /FTId=VAR_005995. FT VARIANT 274 274 V -> F (in a colorectal tumor). FT /FTId=VAR_005997. FT VARIANT 275 275 C -> W (in a breast and a stomach tumor). FT /FTId=VAR_005999. FT VARIANT 275 275 C -> Y (in LFS and tumors of brain, lung, kidney, stomach). FT /FTId=VAR_005998. FT VARIANT 277 277 C -> G (in a lung tumor). FT /FTId=VAR_006000. FT VARIANT 278 278 P -> A (in a breast tumor). FT /FTId=VAR_006001. FT VARIANT 278 278 P -> H (in a leukemia and a lymphoma). FT /FTId=VAR_006002. FT VARIANT 278 278 P -> L (in an esophagus and a lung tumor). FT /FTId=VAR_006003. FT VARIANT 278 278 P -> S (in oral squamous cell carcinoma). FT /FTId=VAR_006004. FT VARIANT 278 278 P -> T (in HNSCC; same patient as mutation His-281). FT /FTId=VAR_006005. FT VARIANT 279 279 G -> E (in a colorectal tumor). FT /FTId=VAR_006006. FT VARIANT 280 280 R -> I (in a colorectal tumor). FT /FTId=VAR_006008. FT VARIANT 280 280 R -> K (in a breast tumor). FT /FTId=VAR_006007. FT VARIANT 280 280 R -> T (in a nasopharyngeal carcinoma cell line; unknown pathogenic significance). FT /FTId=VAR_006009. FT VARIANT 281 281 D -> A (in a leukemia and a lymphoma). FT /FTId=VAR_006010. FT VARIANT 281 281 D -> E (in many types of tumors). FT /FTId=VAR_006011. FT VARIANT 281 281 D -> G (in many types of tumors). FT /FTId=VAR_006012. FT VARIANT 281 281 D -> H (in HNSCC; same patient as mutation Thr-278). FT /FTId=VAR_006013. FT VARIANT 281 281 D -> V (in a colorectal tumor). FT /FTId=VAR_006014. FT VARIANT 282 282 R -> L (in a breast tumor). FT /FTId=VAR_006015. FT VARIANT 282 282 R -> W (in esophageal adenocarcinoma and many types of tumors). FT /FTId=VAR_006016. FT VARIANT 283 283 R -> C (in a colon tumor). FT /FTId=VAR_006017. FT VARIANT 283 283 R -> G (in a lung tumor). FT /FTId=VAR_006018. FT VARIANT 283 283 R -> H (in a colon tumor). FT /FTId=VAR_006019. FT VARIANT 283 283 R -> P (in a breast and a lung tumor). FT /FTId=VAR_006020. FT VARIANT 284 284 T -> A (in a colorectal tumor). FT /FTId=VAR_006021. FT VARIANT 284 284 T -> P (in a lung tumor). FT /FTId=VAR_006022. FT VARIANT 285 285 E -> K (in many types of tumors). FT /FTId=VAR_006023. FT VARIANT 285 285 E -> Q (in an uterus tumor). FT /FTId=VAR_006024. FT VARIANT 285 285 E -> V (in a liver tumor). FT /FTId=VAR_006025. FT VARIANT 286 286 E -> A (in LFS). FT /FTId=VAR_006026. FT VARIANT 286 286 E -> D (in a liver tumor). FT /FTId=VAR_006027. FT VARIANT 286 286 E -> G (in tumors of colon, lung, head and neck). FT /FTId=VAR_006028. FT VARIANT 286 286 E -> K (in many types of tumors). FT /FTId=VAR_006029. FT VARIANT 286 286 E -> Q (in esophageal adenocarcinoma). FT /FTId=VAR_006030. FT VARIANT 292 292 K -> I (in LFS). FT /FTId=VAR_015819. FT VARIANT 296 296 H -> P (in HNSCC). FT /FTId=VAR_006031. FT VARIANT 300 300 P -> R (in a skin tumor). FT /FTId=VAR_006032. FT VARIANT 301 301 P -> L (in a colon tumor). FT /FTId=VAR_006033. FT VARIANT 302 302 G -> E (in a colon tumor). FT /FTId=VAR_006034. FT VARIANT 302 302 G -> V (in a colon tumor). FT /FTId=VAR_006035. FT VARIANT 306 306 R -> Q (in a sarcoma). FT /FTId=VAR_006036. FT VARIANT 307 307 A -> T (in a breast tumor). FT /FTId=VAR_006037. FT VARIANT 309 309 P -> S (in a colon tumor). FT /FTId=VAR_006038. FT VARIANT 325 325 G -> V (in LFS). FT /FTId=VAR_006039. FT VARIANT 334 334 G -> V (in a lung tumor). FT /FTId=VAR_006040. FT VARIANT 337 337 R -> C (in LFS; non-classical form; also found in a liver tumor). FT /FTId=VAR_006041. FT VARIANT 337 337 R -> H (in ADCC). FT /FTId=VAR_035016. FT VARIANT 339 339 E -> K. FT /FTId=VAR_022316. FT VARIANT 366 366 S -> A. FT /FTId=VAR_022317. FT MUTAGEN 46 46 Missing: Alters interaction with WWOX. FT MUTAGEN 46 46 S->A: Abolishes phosphorylation by HIPK2 and acetylation of K-382 by CREBBP. FT MUTAGEN 55 55 T->A: Blocks phosphorylation by TAF1. FT MUTAGEN 135 135 C->Y: Decreased E6-mediated binding to E6-AP. FT MUTAGEN 359 359 P->D: Abolishes binding to USP7. FT MUTAGEN 361 361 G->E: Abolishes binding to USP7. FT MUTAGEN 362 362 S->A: Abolishes binding to USP7. FT MUTAGEN 382 382 K->A: Abolishes acetylation by CREBBP. FT CONFLICT 76 76 A -> G (in Ref. 2; AAA59987). FT CONFLICT 155 155 T -> P (in Ref. 16). FT CONFLICT 254 254 I -> D (in Ref. 7; CAA42635). FT CONFLICT 262 262 G -> V (in Ref. 19). FT CONFLICT 282 282 R -> Q (in Ref. 18). FT HELIX 19 23 FT HELIX 36 38 FT HELIX 41 44 FT HELIX 47 55 FT TURN 105 108 FT STRAND 110 112 FT STRAND 123 127 FT TURN 128 131 FT STRAND 132 135 FT STRAND 141 146 FT STRAND 156 165 FT HELIX 166 168 FT HELIX 177 180 FT STRAND 187 189 FT STRAND 194 199 FT STRAND 204 207 FT TURN 209 211 FT STRAND 214 219 FT STRAND 228 236 FT TURN 243 248 FT STRAND 251 258 FT STRAND 264 274 FT HELIX 278 287 FT STRAND 327 334 FT HELIX 335 354 SQ SEQUENCE 393 AA; 43653 MW; AD5C149FD8106131 CRC64; MEEPQSDPSV EPPLSQETFS DLWKLLPENN VLSPLPSQAM DDLMLSPDDI EQWFTEDPGP DEAPRMPEAA PPVAPAPAAP TPAAPAPAPS WPLSSSVPSQ KTYQGSYGFR LGFLHSGTAK SVTCTYSPAL NKMFCQLAKT CPVQLWVDST PPPGTRVRAM AIYKQSQHMT EVVRRCPHHE RCSDSDGLAP PQHLIRVEGN LRVEYLDDRN TFRHSVVVPY EPPEVGSDCT TIHYNYMCNS SCMGGMNRRP ILTIITLEDS SGNLLGRNSF EVRVCACPGR DRRTEEENLR KKGEPHHELP PGSTKRALPN NTSSSPQPKK KPLDGEYFTL QIRGRERFEM FRELNEALEL KDAQAGKEPG GSRAHSSHLK SKKGQSTSRH KKLMFKTEGP DSD //