ID P63_HUMAN Reviewed; 680 AA. AC Q9H3D4; O75080; O75195; O75922; O76078; Q6VEG2; Q6VEG3; Q6VEG4; Q6VFJ1; AC Q6VFJ2; Q6VFJ3; Q6VH20; Q7LDI3; Q7LDI4; Q7LDI5; Q96KR0; Q9H3D2; Q9H3D3; AC Q9H3P8; Q9NPH7; Q9P1B4; Q9P1B5; Q9P1B6; Q9P1B7; Q9UBV9; Q9UE10; Q9UP26; AC Q9UP27; Q9UP28; Q9UP74; DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 220. DE RecName: Full=Tumor protein 63; DE Short=p63; DE AltName: Full=Chronic ulcerative stomatitis protein; DE Short=CUSP; DE AltName: Full=Keratinocyte transcription factor KET; DE AltName: Full=Transformation-related protein 63; DE Short=TP63; DE AltName: Full=Tumor protein p73-like; DE Short=p73L; DE AltName: Full=p40; DE AltName: Full=p51; GN Name=TP63; Synonyms=KET, P63, P73H, P73L, TP73L; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=9703973; DOI=10.1006/bbrc.1998.9013; RA Senoo M., Seki N., Ohira M., Sugano S., Watanabe M., Tachibana M., RA Tanaka T., Shinkai Y., Kato H.; RT "A second p53-related protein, p73L, with high homology to p73."; RL Biochem. Biophys. Res. Commun. 248:603-607(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Keratinocyte, and Skeletal muscle; RX PubMed=9799841; DOI=10.1007/s003359900891; RA Augustin M., Bamberger C., Paul D., Schmale H.; RT "Cloning and chromosomal mapping of the human p53-related KET gene to RT chromosome 3q27 and its murine homolog Ket to mouse chromosome 16."; RL Mamm. Genome 9:899-902(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4 AND 6), NUCLEOTIDE SEQUENCE RP [GENOMIC DNA] OF 32-680 (ISOFORMS 1; 3 AND 5), FUNCTION, AND TISSUE RP SPECIFICITY. RX PubMed=9774969; DOI=10.1016/s1097-2765(00)80275-0; RA Yang A., Kaghad M., Wang Y., Gillett E., Fleming M.D., Doetsch V., RA Andrews N.C., Caput D., McKeon F.; RT "p63, a p53 homolog at 3q27-29, encodes multiple products with RT transactivating, death-inducing, and dominant-negative activities."; RL Mol. Cell 2:305-316(1998). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5), VARIANT HEAD/NECK CANCER RP LEU-184, VARIANT LUNG CARCINOMA PRO-187, AND VARIANT CERVICAL CANCER RP LEU-204. RC TISSUE=Skeletal muscle; RX PubMed=9662378; DOI=10.1038/nm0798-839; RA Osada M., Ohba M., Kawahara C., Ishioka C., Kanamaru R., Katoh I., RA Ikawa Y., Nimura Y., Nakagawara A., Obinata M., Ikawa S.; RT "Cloning and functional analysis of human p51, which structurally and RT functionally resembles p53."; RL Nat. Med. 4:839-843(1998). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT COLON CANCER HIS-279, AND RP VARIANT OVARIAN CANCER ALA-560. RX PubMed=10485447; RA Hagiwara K., McMenamin M.G., Miura K., Harris C.C.; RT "Mutational analysis of the p63/p73L/p51/p40/CUSP/KET gene in human cancer RT cell lines using intronic primers."; RL Cancer Res. 59:4165-4169(1999). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=10469295; DOI=10.1046/j.1523-1747.1999.00651.x; RA Lee L.A., Walsh P., Prater C.A., Su L.-J., Marchbank A., Egbert T.B., RA Dellavalle R.P., Targoff I.N., Kaufman K.M., Chorzelski T.P., Jablonska S.; RT "Characterization of an autoantigen associated with chronic ulcerative RT stomatitis: the CUSP autoantigen is a member of the p53 family."; RL J. Invest. Dermatol. 113:146-151(1999). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 7), AND ALTERNATIVE RP SPLICING (ISOFORM 8). RX PubMed=10935472; DOI=10.1038/sj.neo.7900008; RA Tani M., Shimizu K., Kawahara C., Kohno T., Ishimoto O., Ikawa S., RA Yokota J.; RT "Mutation and expression of the p51 gene in human lung cancer."; RL Neoplasia 1:71-79(1999). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10), AND TISSUE SPECIFICITY (ISOFORM RP 10). RX PubMed=11336476; DOI=10.1054/bjoc.2000.1735; RA Senoo M., Tsuchiya I., Matsumura Y., Mori T., Saito Y., Kato H., RA Okamoto T., Habu S.; RT "Transcriptional dysregulation of the p73L/p63/p51/p40/KET gene in human RT squamous cell carcinomas: expression of Delta Np73L, a novel dominant- RT negative isoform, and loss of expression of the potential tumour suppressor RT p51."; RL Br. J. Cancer 84:1235-1241(2001). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lymph; 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 [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-450 (ISOFORMS 2/4/8), SUBUNIT, RP ZINC-BINDING, AND DNA-BINDING. RC TISSUE=Prostate; RX PubMed=9662346; DOI=10.1038/nm0798-747; RA Trink B., Okami K., Wu L., Sriuranpong V., Jen J., Sidransky D.; RT "A new human p53 homologue."; RL Nat. Med. 4:747-748(1998). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21; 95-255; 295-330; 378-502 AND RP 583-680. RA Vieira A.R., Murray J.C.; RT "Sequencing of candidate genes for non-syndromic cleft lip and palate."; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 153-388 (ISOFORM 11). RC TISSUE=Placenta; RX PubMed=11477076; DOI=10.1074/jbc.m103801200; RA Klein C., Georges G., Kunkele K.P., Huber R., Engh R.A., Hansen S.; RT "High thermostability and lack of cooperative DNA binding distinguish the RT p63 core domain from the homologous tumor suppressor p53."; RL J. Biol. Chem. 276:37390-37401(2001). RN [13] RP SUBUNIT. RX PubMed=10373484; DOI=10.1074/jbc.274.26.18709; RA Davison T.S., Vagner C., Kaghad M., Ayed A., Caput D., Arrowsmith C.H.; RT "p73 and p63 are homotetramers capable of weak heterotypic interactions RT with each other but not with p53."; RL J. Biol. Chem. 274:18709-18714(1999). RN [14] RP TISSUE SPECIFICITY. RX PubMed=11248048; DOI=10.1073/pnas.061032098; RA Pellegrini G., Dellambra E., Golisano O., Martinelli E., Fantozzi I., RA Bondanza S., Ponzin D., McKeon F., De Luca M.; RT "p63 identifies keratinocyte stem cells."; RL Proc. Natl. Acad. Sci. U.S.A. 98:3156-3161(2001). RN [15] RP FUNCTION IN NOTCH SIGNALING. RX PubMed=11641404; DOI=10.1074/jbc.m108080200; RA Sasaki Y., Ishida S., Morimoto I., Yamashita T., Kojima T., Kihara C., RA Tanaka T., Imai K., Nakamura Y., Tokino T.; RT "The p53 family member genes are involved in the Notch signal pathway."; RL J. Biol. Chem. 277:719-724(2002). RN [16] RP INTERACTION WITH HIPK2. RX 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 RT modulating functions of the p53 family in vivo."; RL J. Biol. Chem. 277:32020-32028(2002). RN [17] RP FUNCTION, DOMAIN, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-55; TRP-59 RP AND LEU-62. RX PubMed=12446779; DOI=10.1128/mcb.22.24.8601-8611.2002; RA Serber Z., Lai H.C., Yang A., Ou H.D., Sigal M.S., Kelly A.E., RA Darimont B.D., Duijf P.H.G., Van Bokhoven H., McKeon F., Doetsch V.; RT "A C-terminal inhibitory domain controls the activity of p63 by an RT intramolecular mechanism."; RL Mol. Cell. Biol. 22:8601-8611(2002). RN [18] RP FUNCTION, AND DOMAIN. RX PubMed=12446784; DOI=10.1128/mcb.22.24.8659-8668.2002; RA Ghioni P., Bolognese F., Duijf P.H.G., Van Bokhoven H., Mantovani R., RA Guerrini L.; RT "Complex transcriptional effects of p63 isoforms: identification of novel RT activation and repression domains."; RL Mol. Cell. Biol. 22:8659-8668(2002). RN [19] RP FUNCTION, AND INTERACTION WITH SSRP1. RX PubMed=12374749; DOI=10.1093/emboj/cdf540; RA Zeng S.X., Dai M.-S., Keller D.M., Lu H.; RT "SSRP1 functions as a co-activator of the transcriptional activator p63."; RL EMBO J. 21:5487-5497(2002). RN [20] RP ERRATUM OF PUBMED:12374749. RA Zeng S.X., Dai M.-S., Keller D.M., Lu H.; RL EMBO J. 23:1679-1679(2004). RN [21] RP UBIQUITINATION, INTERACTION WITH WWP1, AND MUTAGENESIS OF TYR-543. RX PubMed=18806757; DOI=10.1038/cdd.2008.134; RA Li Y., Zhou Z., Chen C.; RT "WW domain-containing E3 ubiquitin protein ligase 1 targets p63 RT transcription factor for ubiquitin-mediated proteasomal degradation and RT regulates apoptosis."; RL Cell Death Differ. 15:1941-1951(2008). RN [22] RP INTERACTION WITH PDS5A. RX PubMed=17846787; DOI=10.1007/s00432-007-0306-x; RA Zheng M.Z., Zheng L.M., Zeng Y.X.; RT "SCC-112 gene is involved in tumor progression and promotes the cell RT proliferation in G2/M phase."; RL J. Cancer Res. Clin. Oncol. 134:453-462(2008). RN [23] RP FUNCTION, INTERACTION WITH NOC2L, AND SUBCELLULAR LOCATION. RX PubMed=20123734; DOI=10.1093/nar/gkq016; RA Heyne K., Willnecker V., Schneider J., Conrad M., Raulf N., Schule R., RA Roemer K.; RT "NIR, an inhibitor of histone acetyltransferases, regulates transcription RT factor TAp63 and is controlled by the cell cycle."; RL Nucleic Acids Res. 38:3159-3171(2010). RN [24] RP FUNCTION. RX PubMed=22197488; DOI=10.1016/j.ajhg.2011.11.013; RA Mitchell K., O'Sullivan J., Missero C., Blair E., Richardson R., RA Anderson B., Antonini D., Murray J.C., Shanske A.L., Schutte B.C., RA Romano R.A., Sinha S., Bhaskar S.S., Black G.C., Dixon J., Dixon M.J.; RT "Exome sequence identifies RIPK4 as the Bartsocas-Papas syndrome locus."; RL Am. J. Hum. Genet. 90:69-75(2012). RN [25] RP STRUCTURE BY NMR OF 540-610. RA Cadot B., Candi E., Cicero D.O., Desideri A., Mele S., Melino G., Paci M.; RT "Solution structure of the C-terminal domain of p63."; RL Submitted (NOV-2004) to the PDB data bank. RN [26] RP VARIANTS EEC3 TRP-243; GLN-243 AND ARG-345. RX PubMed=10535733; DOI=10.1016/s0092-8674(00)81646-3; RA Celli J., Duijf P.H.G., Hamel B.C.J., Bamshad M., Kramer B., Smits A.P.T., RA Newbury-Ecob R., Hennekam R.C.M., Van Buggenhout G., van Haeringen A., RA Woods C.G., van Essen A.J., de Waal R., Vriend G., Haber D.A., Yang A., RA McKeon F., Brunner H.G., van Bokhoven H.; RT "Heterozygous germline mutations in the p53 homolog p63 are the cause of RT EEC syndrome."; RL Cell 99:143-153(1999). RN [27] RP VARIANTS SHFM4 GLU-233 AND CYS-319, AND VARIANTS EEC3 HIS-318 AND GLN-343. RX PubMed=10839977; DOI=10.1086/302972; RA Ianakiev P., Kilpatrick M.W., Toudjarska I., Basel D., Beighton P., RA Tsipouras P.; RT "Split-hand/split-foot malformation is caused by mutations in the p63 gene RT on 3q27."; RL Am. J. Hum. Genet. 67:59-66(2000). RN [28] RP VARIANT ADULT SYNDROME HIS-6 (ISOFORMS 2; 4; 6; 8; 10 AND 12). RX PubMed=11528512; DOI=10.1038/sj.ejhg.5200676; RA Amiel J., Bougeard G., Francannet C., Raclin V., Munnich A., Lyonnet S., RA Frebourg T.; RT "TP63 gene mutation in ADULT syndrome."; RL Eur. J. Hum. Genet. 9:642-645(2001). RN [29] RP VARIANTS AEC PHE-553 AND GLY-561. RX PubMed=11159940; DOI=10.1093/hmg/10.3.221; RA McGrath J.A., Duijf P.H.G., Doetsch V., Irvine A.D., de Waal R., RA Vanmolkot K.R., Wessagowit V., Kelly A., Atherton D.J., Griffiths W.A., RA Orlow S.J., van Haeringen A., Ausems M.G., Yang A., McKeon F., RA Bamshad M.A., Brunner H.G., Hamel B.C.J., van Bokhoven H.; RT "Hay-Wells syndrome is caused by heterozygous missense mutations in the SAM RT domain of p63."; RL Hum. Mol. Genet. 10:221-229(2001). RN [30] RP VARIANTS EEC3 GLN-243; TRP-243; GLN-266; TYR-308; ASN-311; CYS-318; RP HIS-318; GLN-318; CYS-319; HIS-319; SER-319; TRP-343; GLN-343; ARG-345; RP SER-347; SER-348 AND HIS-351, VARIANTS SHFM4 PRO-193 INS; GLU-232 AND RP HIS-319, AND INVOLVEMENT IN LMS. RX PubMed=11462173; DOI=10.1086/323123; RA van Bokhoven H., Hamel B.C.J., Bamshad M., Sangiorgi E., Gurrieri F., RA Duijf P.H.G., Vanmolkot K.R.J., van Beusekom E., van Beersum S.E.C., RA Celli J., Merkx G.F.M., Tenconi R., Fryns J.-P., Verloes A., RA Newbury-Ecob R.A., Raas-Rotschild A., Majewski F., Beemer F.A., Janecke A., RA Chitayat D., Crisponi G., Kayserili H., Yates J.R.W., Neri G., RA Brunner H.G.; RT "p63 gene mutations in EEC syndrome, limb-mammary syndrome, and isolated RT split hand-split foot malformation suggest a genotype-phenotype RT correlation."; RL Am. J. Hum. Genet. 69:481-492(2001). RN [31] RP VARIANT ADULT SYNDROME GLN-337. RX PubMed=11929852; DOI=10.1093/hmg/11.7.799; RA Duijf P.H.G., Vanmolkot K.R., Propping P., Friedl W., Krieger E., RA McKeon F., Doetsch V., Brunner H.G., van Bokhoven H.; RT "Gain-of-function mutation in ADULT syndrome reveals the presence of a RT second transactivation domain in p63."; RL Hum. Mol. Genet. 11:799-804(2002). RN [32] RP VARIANT EEC3 GLY-351. RX PubMed=12838557; DOI=10.1002/ajmg.a.20064; RA Akahoshi K., Sakazume S., Kosaki K., Ohashi H., Fukushima Y.; RT "EEC syndrome type 3 with a heterozygous germline mutation in the P63 gene RT and B cell lymphoma."; RL Am. J. Med. Genet. A 120:370-373(2003). RN [33] RP VARIANT RHS HIS-318, AND CHARACTERIZATION OF VARIANT RHS HIS-318. RX PubMed=12939657; DOI=10.1038/sj.ejhg.5201004; RA Bougeard G., Hadj-Rabia S., Faivre L., Sarafan-Vasseur N., Frebourg T.; RT "The Rapp-Hodgkin syndrome results from mutations of the TP63 gene."; RL Eur. J. Hum. Genet. 11:700-704(2003). RN [34] RP VARIANT RHS PRO-580. RX PubMed=12766194; DOI=10.1177/154405910308200606; RA Kantaputra P.N., Hamada T., Kumchai T., McGrath J.A.; RT "Heterozygous mutation in the SAM domain of p63 underlies Rapp-Hodgkin RT ectodermal dysplasia."; RL J. Dent. Res. 82:433-437(2003). RN [35] RP VARIANT RHS THR-549. RX PubMed=15200513; DOI=10.1111/j.0009-9163.2004.00278.x; RA Bertola D.R., Kim C.A., Albano L.M.J., Scheffer H., Meijer R., RA van Bokhoven H.; RT "Molecular evidence that AEC syndrome and Rapp-Hodgkin syndrome are RT variable expression of a single genetic disorder."; RL Clin. Genet. 66:79-80(2004). RN [36] RP INVOLVEMENT IN OFC8, VARIANT OFC8 GLY-352, AND VARIANTS LEU-129 AND RP HIS-603. RX PubMed=16740912; DOI=10.1136/jmg.2005.036442; RA Leoyklang P., Siriwan P., Shotelersuk V.; RT "A mutation of the p63 gene in non-syndromic cleft lip."; RL J. Med. Genet. 43:E28-E28(2006). RN [37] RP VARIANTS POF21 594-ARG--GLU-680 DEL AND 598-TRP--GLU-680 DEL, AND RP INVOLVEMENT IN POF21. RX PubMed=30924587; DOI=10.1002/humu.23744; RA Tucker E.J., Jaillard S., Grover S.R., van den Bergen J., Robevska G., RA Bell K.M., Sadedin S., Hanna C., Dulon J., Touraine P., Sinclair A.H.; RT "TP63-truncating variants cause isolated premature ovarian insufficiency."; RL Hum. Mutat. 40:886-892(2019). RN [38] RP VARIANT LMS 643-ARG--GLU-680 DEL. RX PubMed=32067224; DOI=10.1111/cge.13725; RA Mathorne S.W., Ravn P., Hansen D., Beck-Nielsen S.S., Gjoerup H., RA Soerensen K.P., Fagerberg C.R.; RT "Novel phenotype of syndromic premature ovarian insufficiency associated RT with TP63 molecular defect."; RL Clin. Genet. 97:779-784(2020). RN [39] RP VARIANTS POF21 CYS-18; PRO-97 AND CYS-647, INVOLVEMENT IN POF21, RP CHARACTERIZATION OF VARIANTS POF21 CYS-18; PRO-97 AND CYS-647, AND RP MUTAGENESIS OF TYR-18; ARG-97; ARG-643 AND ARG-647. RX PubMed=35801529; DOI=10.1002/humu.24432; RA Tucker E.J., Gutfreund N., Belaud-Rotureau M.A., Gilot D., Brun T., RA Kline B.L., Bell K.M., Domin-Bernhard M., Theard C., Touraine P., RA Robevska G., van van den Bergen J., Ayers K.L., Sinclair A.H., Doetsch V., RA Jaillard S.; RT "Dominant TP63 missense variants lead to constitutive activation and RT premature ovarian insufficiency."; RL Hum. Mutat. 43:1443-1453(2022). RN [40] RP VARIANTS POF21 ASN-285; ALA-538; ILE-567; 594-ARG--GLU-680 DEL; GLN-643; RP PRO-646; CYS-647 AND GLN-655, INVOLVEMENT IN POF21, AND CHARACTERIZATION OF RP VARIANTS POF21 ASN-285; ALA-538; ILE-567; 594-ARG--GLU-680 DEL; GLN-643; RP PRO-646; CYS-647 AND GLN-655. RX PubMed=36856110; DOI=10.1172/jci162315; RA Huang C., Zhao S., Yang Y., Guo T., Ke H., Mi X., Qin Y., Chen Z.J., RA Zhao S.; RT "TP63 gain-of-function mutations cause premature ovarian insufficiency by RT inducing oocyte apoptosis."; RL J. Clin. Invest. 133:0-0(2023). CC -!- FUNCTION: Acts as a sequence specific DNA binding transcriptional CC activator or repressor. The isoforms contain a varying set of CC transactivation and auto-regulating transactivation inhibiting domains CC thus showing an isoform specific activity. Isoform 2 activates RIPK4 CC transcription. May be required in conjunction with TP73/p73 for CC initiation of p53/TP53 dependent apoptosis in response to genotoxic CC insults and the presence of activated oncogenes. Involved in Notch CC signaling by probably inducing JAG1 and JAG2. Plays a role in the CC regulation of epithelial morphogenesis. The ratio of DeltaN-type and CC TA*-type isoforms may govern the maintenance of epithelial stem cell CC compartments and regulate the initiation of epithelial stratification CC from the undifferentiated embryonal ectoderm. Required for limb CC formation from the apical ectodermal ridge. Activates transcription of CC the p21 promoter. {ECO:0000269|PubMed:11641404, CC ECO:0000269|PubMed:12374749, ECO:0000269|PubMed:12446779, CC ECO:0000269|PubMed:12446784, ECO:0000269|PubMed:20123734, CC ECO:0000269|PubMed:22197488, ECO:0000269|PubMed:9774969}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Binds DNA as a homotetramer. Isoform composition of the CC tetramer may determine transactivation activity. Isoforms Alpha and CC Gamma interact with HIPK2. Interacts with SSRP1, leading to stimulate CC coactivator activity. Isoform 1 and isoform 2 interact with WWP1. CC Interacts with PDS5A. Isoform 5 (via activation domain) interacts with CC NOC2L. {ECO:0000269|PubMed:10373484, ECO:0000269|PubMed:11925430, CC ECO:0000269|PubMed:12374749, ECO:0000269|PubMed:17846787, CC ECO:0000269|PubMed:18806757, ECO:0000269|PubMed:20123734, CC ECO:0000269|PubMed:9662346}. CC -!- INTERACTION: CC Q9H3D4; P35637: FUS; NbExp=2; IntAct=EBI-2337775, EBI-400434; CC Q9H3D4; Q9H2X6: HIPK2; NbExp=2; IntAct=EBI-2337775, EBI-348345; CC Q9H3D4; Q99729: HNRNPAB; NbExp=3; IntAct=EBI-2337775, EBI-1044873; CC Q9H3D4; P61978: HNRNPK; NbExp=2; IntAct=EBI-2337775, EBI-304185; CC Q9H3D4; Q96J02: ITCH; NbExp=2; IntAct=EBI-2337775, EBI-1564678; CC Q9H3D4; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-2337775, EBI-348259; CC Q9H3D4; Q9UFN0: NIPSNAP3A; NbExp=2; IntAct=EBI-2337775, EBI-716291; CC Q9H3D4; Q96FA3: PELI1; NbExp=3; IntAct=EBI-2337775, EBI-448369; CC Q9H3D4; Q9HAT8: PELI2; NbExp=3; IntAct=EBI-2337775, EBI-448407; CC Q9H3D4; Q13526: PIN1; NbExp=3; IntAct=EBI-2337775, EBI-714158; CC Q9H3D4; Q05655: PRKCD; NbExp=2; IntAct=EBI-2337775, EBI-704279; CC Q9H3D4; Q15796: SMAD2; NbExp=3; IntAct=EBI-2337775, EBI-1040141; CC Q9H3D4; P04637: TP53; NbExp=5; IntAct=EBI-2337775, EBI-366083; CC Q9H3D4; Q13625: TP53BP2; NbExp=2; IntAct=EBI-2337775, EBI-77642; CC Q9H3D4; Q9H3D4: TP63; NbExp=4; IntAct=EBI-2337775, EBI-2337775; CC Q9H3D4; O15350: TP73; NbExp=3; IntAct=EBI-2337775, EBI-389606; CC Q9H3D4; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-2337775, EBI-7353612; CC Q9H3D4; P46937: YAP1; NbExp=2; IntAct=EBI-2337775, EBI-1044059; CC Q9H3D4-1; Q8TDN4: CABLES1; NbExp=7; IntAct=EBI-2400586, EBI-604615; CC Q9H3D4-1; Q99729: HNRNPAB; NbExp=2; IntAct=EBI-2400586, EBI-1044873; CC Q9H3D4-2; Q99729: HNRNPAB; NbExp=2; IntAct=EBI-6481107, EBI-1044873; CC Q9H3D4-2; Q9UPW6: SATB2; NbExp=5; IntAct=EBI-6481107, EBI-8298169; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12446779, CC ECO:0000269|PubMed:20123734}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=12; CC Name=1; Synonyms=TA*-alpha, TAp63alpha, P51B; CC IsoId=Q9H3D4-1; Sequence=Displayed; CC Name=2; Synonyms=DeltaN-alpha, DeltaNp63 alpha, P51delNalpha; CC IsoId=Q9H3D4-2; Sequence=VSP_012465; CC Name=3; Synonyms=TA*-beta, TAp63beta; CC IsoId=Q9H3D4-3; Sequence=VSP_012470; CC Name=4; Synonyms=DeltaN-beta, DeltaNp63 beta, P51delNbeta; CC IsoId=Q9H3D4-4; Sequence=VSP_012465, VSP_012470; CC Name=5; Synonyms=TA*-gamma, TAp63gamma, P51A; CC IsoId=Q9H3D4-5; Sequence=VSP_012468; CC Name=6; Synonyms=DeltaN-gamma, DeltaNp63gamma, P51delNgamma; CC IsoId=Q9H3D4-6; Sequence=VSP_012465, VSP_012468; CC Name=7; Synonyms=TA*-delta, TAp63delta, P51delta; CC IsoId=Q9H3D4-7; Sequence=VSP_012469; CC Name=8; Synonyms=DeltaN-delta; CC IsoId=Q9H3D4-8; Sequence=VSP_012465, VSP_012469; CC Name=9; Synonyms=TA*-epsilon; CC IsoId=Q9H3D4-9; Sequence=VSP_012466; CC Name=10; Synonyms=DeltaN-epsilon, DeltaNp73L; CC IsoId=Q9H3D4-10; Sequence=VSP_012465, VSP_012466; CC Name=11; Synonyms=P63 delta; CC IsoId=Q9H3D4-11; Sequence=VSP_012467; CC Name=12; CC IsoId=Q9H3D4-12; Sequence=VSP_012465, VSP_012467; CC -!- TISSUE SPECIFICITY: Widely expressed, notably in heart, kidney, CC placenta, prostate, skeletal muscle, testis and thymus, although the CC precise isoform varies according to tissue type. Progenitor cell layers CC of skin, breast, eye and prostate express high levels of DeltaN-type CC isoforms. Isoform 10 is predominantly expressed in skin squamous cell CC carcinomas, but not in normal skin tissues. CC {ECO:0000269|PubMed:11248048, ECO:0000269|PubMed:9774969}. CC -!- DOMAIN: The transactivation inhibitory domain (TID) can interact with, CC and inhibit the activity of the N-terminal transcriptional activation CC domain of TA*-type isoforms. {ECO:0000269|PubMed:12446779, CC ECO:0000269|PubMed:12446784}. CC -!- PTM: May be sumoylated. {ECO:0000250}. CC -!- PTM: Ubiquitinated. Polyubiquitination involves WWP1 and leads to CC proteasomal degradation of this protein. {ECO:0000269|PubMed:18806757}. CC -!- DISEASE: Acro-dermato-ungual-lacrimal-tooth syndrome (ADULT syndrome) CC [MIM:103285]: A form of ectodermal dysplasia. Ectodermal dysplasia CC defines a heterogeneous group of disorders due to abnormal development CC of two or more ectodermal structures. ADULT syndrome involves CC ectrodactyly, syndactyly, finger- and toenail dysplasia, hypoplastic CC breasts and nipples, intensive freckling, lacrimal duct atresia, CC frontal alopecia, primary hypodontia and loss of permanent teeth. ADULT CC syndrome differs significantly from EEC3 syndrome by the absence of CC facial clefting. Inheritance is autosomal dominant. CC {ECO:0000269|PubMed:11929852}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Ankyloblepharon-ectodermal defects-cleft lip/palate (AEC) CC [MIM:106260]: An autosomal dominant condition characterized by CC congenital ectodermal dysplasia with coarse, wiry, sparse hair, CC dystrophic nails, slight hypohidrosis, scalp infections, CC ankyloblepharon filiform adnatum, maxillary hypoplasia, hypodontia and CC cleft lip/palate. {ECO:0000269|PubMed:11159940}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Ectrodactyly, ectodermal dysplasia, and cleft lip/palate CC syndrome 3 (EEC3) [MIM:604292]: A form of ectodermal dysplasia, a CC heterogeneous group of disorders due to abnormal development of two or CC more ectodermal structures. It is an autosomal dominant syndrome CC characterized by ectrodactyly of hands and feet, ectodermal dysplasia CC and facial clefting. {ECO:0000269|PubMed:10535733, CC ECO:0000269|PubMed:10839977, ECO:0000269|PubMed:11462173, CC ECO:0000269|PubMed:12838557}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Split-hand/foot malformation 4 (SHFM4) [MIM:605289]: A limb CC malformation involving the central rays of the autopod and presenting CC with syndactyly, median clefts of the hands and feet, and aplasia CC and/or hypoplasia of the phalanges, metacarpals, and metatarsals. Some CC patients have been found to have intellectual disability, ectodermal CC and craniofacial findings, and orofacial clefting. CC {ECO:0000269|PubMed:10839977, ECO:0000269|PubMed:11462173}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Limb-mammary syndrome (LMS) [MIM:603543]: Characterized by CC ectrodactyly, cleft palate and mammary-gland abnormalities. CC {ECO:0000269|PubMed:11462173, ECO:0000269|PubMed:32067224}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Rapp-Hodgkin syndrome (RHS) [MIM:129400]: A form of ectodermal CC dysplasia, a heterogeneous group of disorders due to abnormal CC development of two or more ectodermal structures. Characterized by the CC combination of anhidrotic ectodermal dysplasia, cleft lip, and cleft CC palate. The clinical syndrome is comprised of a characteristic facies CC (narrow nose and small mouth), wiry, slow-growing, and uncombable hair, CC sparse eyelashes and eyebrows, obstructed lacrimal puncta/epiphora, CC bilateral stenosis of external auditory canals, microsomia, hypodontia, CC cone-shaped incisors, enamel hypoplasia, dystrophic nails, and cleft CC lip/cleft palate. RHS inheritance is autosomal dominant. CC {ECO:0000269|PubMed:12766194, ECO:0000269|PubMed:12939657, CC ECO:0000269|PubMed:15200513}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Orofacial cleft 8 (OFC8) [MIM:618149]: A birth defect CC consisting of cleft lips with or without cleft palate. Cleft lips are CC associated with cleft palate in two-third of cases. A cleft lip can CC occur on one or both sides and range in severity from a simple notch in CC the upper lip to a complete opening in the lip extending into the floor CC of the nostril and involving the upper gum. CC {ECO:0000269|PubMed:16740912}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Premature ovarian failure 21 (POF21) [MIM:620311]: A form of CC premature ovarian failure, an ovarian disorder defined as the cessation CC of ovarian function under the age of 40 years. It is characterized by CC oligomenorrhea or amenorrhea, in the presence of elevated levels of CC serum gonadotropins and low estradiol. POF21 inheritance is autosomal CC dominant. {ECO:0000269|PubMed:30924587, ECO:0000269|PubMed:35801529, CC ECO:0000269|PubMed:36856110}. Note=The disease is caused by variants CC affecting the gene represented in this entry. Gain-of-function variants CC located in the transactivation inhibition domain are responsible for CC premature ovarian failure by inducing accelerated oocyte loss, as shown CC in mutant mice carrying the pathogenic variant p.Arg647Cys. CC {ECO:0000269|PubMed:36856110}. CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage. CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing of isoform CC 1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing of isoform CC 2. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative splicing of isoform CC 1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 6]: Produced by alternative splicing of isoform CC 2. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 7]: Produced by alternative splicing of isoform CC 1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 8]: Produced by alternative splicing of isoform CC 2. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 9]: Produced by alternative splicing of isoform CC 1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 10]: Produced by alternative splicing of CC isoform 2. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 11]: Produced by alternative splicing of CC isoform 1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 12]: Produced by alternative splicing of CC isoform 2. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the p53 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF43486.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAF43487.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAF43488.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAF43489.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAF61624.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAA32592.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAA32593.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/365/TP63"; 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; AB010153; BAA32433.1; -; mRNA. DR EMBL; Y16961; CAA76562.1; -; mRNA. DR EMBL; AF075428; AAC62633.1; -; mRNA. DR EMBL; AF075429; AAC62634.1; -; mRNA. DR EMBL; AF075430; AAC62635.1; -; mRNA. DR EMBL; AF075431; AAC62636.1; -; mRNA. DR EMBL; AF075432; AAC62637.1; -; mRNA. DR EMBL; AF075433; AAC62638.1; -; mRNA. DR EMBL; AF124539; AAG45607.1; -; Genomic_DNA. DR EMBL; AF124528; AAG45607.1; JOINED; Genomic_DNA. DR EMBL; AF124529; AAG45607.1; JOINED; Genomic_DNA. DR EMBL; AF124531; AAG45607.1; JOINED; Genomic_DNA. DR EMBL; AF124532; AAG45607.1; JOINED; Genomic_DNA. DR EMBL; AF124533; AAG45607.1; JOINED; Genomic_DNA. DR EMBL; AF124534; AAG45607.1; JOINED; Genomic_DNA. DR EMBL; AF124535; AAG45607.1; JOINED; Genomic_DNA. DR EMBL; AF124536; AAG45607.1; JOINED; Genomic_DNA. DR EMBL; AF124537; AAG45607.1; JOINED; Genomic_DNA. DR EMBL; AF124538; AAG45607.1; JOINED; Genomic_DNA. DR EMBL; AF124539; AAG45608.1; -; Genomic_DNA. DR EMBL; AF124528; AAG45608.1; JOINED; Genomic_DNA. DR EMBL; AF124529; AAG45608.1; JOINED; Genomic_DNA. DR EMBL; AF124531; AAG45608.1; JOINED; Genomic_DNA. DR EMBL; AF124532; AAG45608.1; JOINED; Genomic_DNA. DR EMBL; AF124533; AAG45608.1; JOINED; Genomic_DNA. DR EMBL; AF124534; AAG45608.1; JOINED; Genomic_DNA. DR EMBL; AF124535; AAG45608.1; JOINED; Genomic_DNA. DR EMBL; AF124536; AAG45608.1; JOINED; Genomic_DNA. DR EMBL; AF124537; AAG45608.1; JOINED; Genomic_DNA. DR EMBL; AF124540; AAG45609.1; -; Genomic_DNA. DR EMBL; AF124528; AAG45609.1; JOINED; Genomic_DNA. DR EMBL; AF124529; AAG45609.1; JOINED; Genomic_DNA. DR EMBL; AF124531; AAG45609.1; JOINED; Genomic_DNA. DR EMBL; AF124532; AAG45609.1; JOINED; Genomic_DNA. DR EMBL; AF124533; AAG45609.1; JOINED; Genomic_DNA. DR EMBL; AF124534; AAG45609.1; JOINED; Genomic_DNA. DR EMBL; AF124535; AAG45609.1; JOINED; Genomic_DNA. DR EMBL; AF124539; AAG45610.1; -; Genomic_DNA. DR EMBL; AF124530; AAG45610.1; JOINED; Genomic_DNA. DR EMBL; AF124531; AAG45610.1; JOINED; Genomic_DNA. DR EMBL; AF124532; AAG45610.1; JOINED; Genomic_DNA. DR EMBL; AF124533; AAG45610.1; JOINED; Genomic_DNA. DR EMBL; AF124534; AAG45610.1; JOINED; Genomic_DNA. DR EMBL; AF124535; AAG45610.1; JOINED; Genomic_DNA. DR EMBL; AF124536; AAG45610.1; JOINED; Genomic_DNA. DR EMBL; AF124537; AAG45610.1; JOINED; Genomic_DNA. DR EMBL; AF124538; AAG45610.1; JOINED; Genomic_DNA. DR EMBL; AF124539; AAG45611.1; -; Genomic_DNA. DR EMBL; AF124530; AAG45611.1; JOINED; Genomic_DNA. DR EMBL; AF124531; AAG45611.1; JOINED; Genomic_DNA. DR EMBL; AF124532; AAG45611.1; JOINED; Genomic_DNA. DR EMBL; AF124533; AAG45611.1; JOINED; Genomic_DNA. DR EMBL; AF124534; AAG45611.1; JOINED; Genomic_DNA. DR EMBL; AF124535; AAG45611.1; JOINED; Genomic_DNA. DR EMBL; AF124536; AAG45611.1; JOINED; Genomic_DNA. DR EMBL; AF124537; AAG45611.1; JOINED; Genomic_DNA. DR EMBL; AF124540; AAG45612.1; -; Genomic_DNA. DR EMBL; AF124531; AAG45612.1; JOINED; Genomic_DNA. DR EMBL; AF124533; AAG45612.1; JOINED; Genomic_DNA. DR EMBL; AF124535; AAG45612.1; JOINED; Genomic_DNA. DR EMBL; AF124534; AAG45612.1; JOINED; Genomic_DNA. DR EMBL; AF124532; AAG45612.1; JOINED; Genomic_DNA. DR EMBL; AF124530; AAG45612.1; JOINED; Genomic_DNA. DR EMBL; AB016072; BAA32592.1; ALT_FRAME; mRNA. DR EMBL; AB016073; BAA32593.1; ALT_FRAME; mRNA. DR EMBL; AF091627; AAC43038.1; -; mRNA. DR EMBL; AF116770; AAF43486.1; ALT_INIT; Genomic_DNA. DR EMBL; AF116756; AAF43486.1; JOINED; Genomic_DNA. DR EMBL; AF116757; AAF43486.1; JOINED; Genomic_DNA. DR EMBL; AF116759; AAF43486.1; JOINED; Genomic_DNA. DR EMBL; AF116760; AAF43486.1; JOINED; Genomic_DNA. DR EMBL; AF116761; AAF43486.1; JOINED; Genomic_DNA. DR EMBL; AF116762; AAF43486.1; JOINED; Genomic_DNA. DR EMBL; AF116763; AAF43486.1; JOINED; Genomic_DNA. DR EMBL; AF116764; AAF43486.1; JOINED; Genomic_DNA. DR EMBL; AF116765; AAF43486.1; JOINED; Genomic_DNA. DR EMBL; AF116769; AAF43487.1; ALT_INIT; Genomic_DNA. DR EMBL; AF116756; AAF43487.1; JOINED; Genomic_DNA. DR EMBL; AF116757; AAF43487.1; JOINED; Genomic_DNA. DR EMBL; AF116759; AAF43487.1; JOINED; Genomic_DNA. DR EMBL; AF116760; AAF43487.1; JOINED; Genomic_DNA. DR EMBL; AF116761; AAF43487.1; JOINED; Genomic_DNA. DR EMBL; AF116762; AAF43487.1; JOINED; Genomic_DNA. DR EMBL; AF116763; AAF43487.1; JOINED; Genomic_DNA. DR EMBL; AF116764; AAF43487.1; JOINED; Genomic_DNA. DR EMBL; AF116765; AAF43487.1; JOINED; Genomic_DNA. DR EMBL; AF116766; AAF43487.1; JOINED; Genomic_DNA. DR EMBL; AF116767; AAF43487.1; JOINED; Genomic_DNA. DR EMBL; AF116768; AAF43487.1; JOINED; Genomic_DNA. DR EMBL; AF116769; AAF43488.1; ALT_INIT; Genomic_DNA. DR EMBL; AF116756; AAF43488.1; JOINED; Genomic_DNA. DR EMBL; AF116759; AAF43488.1; JOINED; Genomic_DNA. DR EMBL; AF116757; AAF43488.1; JOINED; Genomic_DNA. DR EMBL; AF116762; AAF43488.1; JOINED; Genomic_DNA. DR EMBL; AF116764; AAF43488.1; JOINED; Genomic_DNA. DR EMBL; AF116766; AAF43488.1; JOINED; Genomic_DNA. DR EMBL; AF116767; AAF43488.1; JOINED; Genomic_DNA. DR EMBL; AF116765; AAF43488.1; JOINED; Genomic_DNA. DR EMBL; AF116763; AAF43488.1; JOINED; Genomic_DNA. DR EMBL; AF116761; AAF43488.1; JOINED; Genomic_DNA. DR EMBL; AF116760; AAF43488.1; JOINED; Genomic_DNA. DR EMBL; AF116769; AAF43489.1; ALT_INIT; Genomic_DNA. DR EMBL; AF116756; AAF43489.1; JOINED; Genomic_DNA. DR EMBL; AF116757; AAF43489.1; JOINED; Genomic_DNA. DR EMBL; AF116759; AAF43489.1; JOINED; Genomic_DNA. DR EMBL; AF116760; AAF43489.1; JOINED; Genomic_DNA. DR EMBL; AF116761; AAF43489.1; JOINED; Genomic_DNA. DR EMBL; AF116762; AAF43489.1; JOINED; Genomic_DNA. DR EMBL; AF116763; AAF43489.1; JOINED; Genomic_DNA. DR EMBL; AF116764; AAF43489.1; JOINED; Genomic_DNA. DR EMBL; AF116765; AAF43489.1; JOINED; Genomic_DNA. DR EMBL; AF116766; AAF43489.1; JOINED; Genomic_DNA. DR EMBL; AF116770; AAF43490.1; -; Genomic_DNA. DR EMBL; AF116758; AAF43490.1; JOINED; Genomic_DNA. DR EMBL; AF116760; AAF43490.1; JOINED; Genomic_DNA. DR EMBL; AF116762; AAF43490.1; JOINED; Genomic_DNA. DR EMBL; AF116764; AAF43490.1; JOINED; Genomic_DNA. DR EMBL; AF116765; AAF43490.1; JOINED; Genomic_DNA. DR EMBL; AF116763; AAF43490.1; JOINED; Genomic_DNA. DR EMBL; AF116761; AAF43490.1; JOINED; Genomic_DNA. DR EMBL; AF116759; AAF43490.1; JOINED; Genomic_DNA. DR EMBL; AF116769; AAF43491.1; -; Genomic_DNA. DR EMBL; AF116758; AAF43491.1; JOINED; Genomic_DNA. DR EMBL; AF116759; AAF43491.1; JOINED; Genomic_DNA. DR EMBL; AF116760; AAF43491.1; JOINED; Genomic_DNA. DR EMBL; AF116764; AAF43491.1; JOINED; Genomic_DNA. DR EMBL; AF116766; AAF43491.1; JOINED; Genomic_DNA. DR EMBL; AF116768; AAF43491.1; JOINED; Genomic_DNA. DR EMBL; AF116767; AAF43491.1; JOINED; Genomic_DNA. DR EMBL; AF116765; AAF43491.1; JOINED; Genomic_DNA. DR EMBL; AF116763; AAF43491.1; JOINED; Genomic_DNA. DR EMBL; AF116762; AAF43491.1; JOINED; Genomic_DNA. DR EMBL; AF116761; AAF43491.1; JOINED; Genomic_DNA. DR EMBL; AF116769; AAF43492.1; -; Genomic_DNA. DR EMBL; AF116758; AAF43492.1; JOINED; Genomic_DNA. DR EMBL; AF116760; AAF43492.1; JOINED; Genomic_DNA. DR EMBL; AF116759; AAF43492.1; JOINED; Genomic_DNA. DR EMBL; AF116761; AAF43492.1; JOINED; Genomic_DNA. DR EMBL; AF116763; AAF43492.1; JOINED; Genomic_DNA. DR EMBL; AF116765; AAF43492.1; JOINED; Genomic_DNA. DR EMBL; AF116767; AAF43492.1; JOINED; Genomic_DNA. DR EMBL; AF116766; AAF43492.1; JOINED; Genomic_DNA. DR EMBL; AF116764; AAF43492.1; JOINED; Genomic_DNA. DR EMBL; AF116762; AAF43492.1; JOINED; Genomic_DNA. DR EMBL; AF116769; AAF43493.1; -; Genomic_DNA. DR EMBL; AF116758; AAF43493.1; JOINED; Genomic_DNA. DR EMBL; AF116760; AAF43493.1; JOINED; Genomic_DNA. DR EMBL; AF116759; AAF43493.1; JOINED; Genomic_DNA. DR EMBL; AF116761; AAF43493.1; JOINED; Genomic_DNA. DR EMBL; AF116763; AAF43493.1; JOINED; Genomic_DNA. DR EMBL; AF116765; AAF43493.1; JOINED; Genomic_DNA. DR EMBL; AF116766; AAF43493.1; JOINED; Genomic_DNA. DR EMBL; AF116764; AAF43493.1; JOINED; Genomic_DNA. DR EMBL; AF116762; AAF43493.1; JOINED; Genomic_DNA. DR EMBL; AF116771; AAF61624.1; ALT_FRAME; mRNA. DR EMBL; AB042841; BAB20591.1; -; mRNA. DR EMBL; BC039815; AAH39815.1; -; mRNA. DR EMBL; AF061512; AAC24830.1; -; mRNA. DR EMBL; AY342152; AAQ63448.1; -; Genomic_DNA. DR EMBL; AY341145; AAQ63448.1; JOINED; Genomic_DNA. DR EMBL; AY339663; AAQ63449.1; -; Genomic_DNA. DR EMBL; AY341143; AAQ63450.1; -; Genomic_DNA. DR EMBL; AY339664; AAQ63450.1; JOINED; Genomic_DNA. DR EMBL; AY341142; AAQ63450.1; JOINED; Genomic_DNA. DR EMBL; AY341143; AAQ63451.1; -; Genomic_DNA. DR EMBL; AY341142; AAQ63451.1; JOINED; Genomic_DNA. DR EMBL; AY341144; AAQ63452.1; -; Genomic_DNA. DR EMBL; AY342153; AAQ63453.1; -; Genomic_DNA. DR EMBL; AY342154; AAQ63454.1; -; Genomic_DNA. DR EMBL; AJ315499; CAC48053.1; -; mRNA. DR CCDS; CCDS3293.1; -. [Q9H3D4-1] DR CCDS; CCDS46976.1; -. [Q9H3D4-3] DR CCDS; CCDS46977.1; -. [Q9H3D4-5] DR CCDS; CCDS46978.1; -. [Q9H3D4-2] DR CCDS; CCDS46979.1; -. [Q9H3D4-4] DR CCDS; CCDS46980.1; -. [Q9H3D4-6] DR CCDS; CCDS82887.1; -. [Q9H3D4-11] DR CCDS; CCDS87179.1; -. [Q9H3D4-7] DR CCDS; CCDS87180.1; -. [Q9H3D4-8] DR CCDS; CCDS87181.1; -. [Q9H3D4-10] DR RefSeq; NP_001108450.1; NM_001114978.1. [Q9H3D4-3] DR RefSeq; NP_001108451.1; NM_001114979.1. [Q9H3D4-5] DR RefSeq; NP_001108452.1; NM_001114980.1. [Q9H3D4-2] DR RefSeq; NP_001108453.1; NM_001114981.1. [Q9H3D4-4] DR RefSeq; NP_001108454.1; NM_001114982.1. [Q9H3D4-6] DR RefSeq; NP_001316073.1; NM_001329144.1. [Q9H3D4-7] DR RefSeq; NP_001316074.1; NM_001329145.1. [Q9H3D4-8] DR RefSeq; NP_001316075.1; NM_001329146.1. [Q9H3D4-10] DR RefSeq; NP_001316077.1; NM_001329148.1. [Q9H3D4-11] DR RefSeq; NP_003713.3; NM_003722.4. [Q9H3D4-1] DR RefSeq; XP_016862876.1; XM_017007387.1. DR PDB; 1RG6; NMR; -; A=540-614. DR PDB; 2NB1; NMR; -; A/C=397-455. DR PDB; 2RMN; NMR; -; A=153-388. DR PDB; 2Y9T; NMR; -; A=543-622. DR PDB; 2Y9U; X-ray; 1.60 A; A=545-611. DR PDB; 3QYM; X-ray; 3.20 A; A/B/C/D/E/F/G/H=166-362. DR PDB; 3QYN; X-ray; 2.50 A; A/B/C/D=166-362. DR PDB; 3US0; X-ray; 2.50 A; A/B/C/D=166-362. DR PDB; 3US1; X-ray; 2.80 A; A/D=166-362. DR PDB; 3US2; X-ray; 4.20 A; A/B/C/D/G/H/I/J=166-362. DR PDB; 3ZY0; X-ray; 1.90 A; A/B/C/D=398-427. DR PDB; 3ZY1; X-ray; 2.15 A; A=398-441. DR PDB; 4A9Z; X-ray; 2.29 A; A/B/C/D=397-455. DR PDB; 6FGN; NMR; -; A=47-73. DR PDB; 6RU6; X-ray; 2.05 A; C=618-630. DR PDB; 6RU7; X-ray; 2.08 A; C/D=618-633. DR PDB; 6RU8; X-ray; 1.92 A; E/F/G/H=621-632. DR PDB; 7Z71; X-ray; 1.85 A; A/C=162-363. DR PDB; 7Z72; X-ray; 1.80 A; A=545-611. DR PDB; 7Z73; X-ray; 2.27 A; A/B/C/D=397-455. DR PDB; 7Z7E; X-ray; 1.80 A; A=162-363. DR PDB; 8P9C; X-ray; 1.76 A; A=397-455. DR PDB; 8P9D; X-ray; 2.70 A; A/C=397-455. DR PDB; 8P9E; X-ray; 2.25 A; A=397-455. DR PDBsum; 1RG6; -. DR PDBsum; 2NB1; -. DR PDBsum; 2RMN; -. DR PDBsum; 2Y9T; -. DR PDBsum; 2Y9U; -. DR PDBsum; 3QYM; -. DR PDBsum; 3QYN; -. DR PDBsum; 3US0; -. DR PDBsum; 3US1; -. DR PDBsum; 3US2; -. DR PDBsum; 3ZY0; -. DR PDBsum; 3ZY1; -. DR PDBsum; 4A9Z; -. DR PDBsum; 6FGN; -. DR PDBsum; 6RU6; -. DR PDBsum; 6RU7; -. DR PDBsum; 6RU8; -. DR PDBsum; 7Z71; -. DR PDBsum; 7Z72; -. DR PDBsum; 7Z73; -. DR PDBsum; 7Z7E; -. DR PDBsum; 8P9C; -. DR PDBsum; 8P9D; -. DR PDBsum; 8P9E; -. DR AlphaFoldDB; Q9H3D4; -. DR BMRB; Q9H3D4; -. DR SMR; Q9H3D4; -. DR BioGRID; 114181; 298. DR DIP; DIP-29588N; -. DR ELM; Q9H3D4; -. DR IntAct; Q9H3D4; 92. DR MINT; Q9H3D4; -. DR STRING; 9606.ENSP00000264731; -. DR iPTMnet; Q9H3D4; -. DR PhosphoSitePlus; Q9H3D4; -. DR BioMuta; TP63; -. DR DMDM; 57013009; -. DR EPD; Q9H3D4; -. DR MassIVE; Q9H3D4; -. DR MaxQB; Q9H3D4; -. DR PaxDb; 9606-ENSP00000264731; -. DR PeptideAtlas; Q9H3D4; -. DR ProteomicsDB; 80692; -. [Q9H3D4-1] DR ProteomicsDB; 80693; -. [Q9H3D4-10] DR ProteomicsDB; 80694; -. [Q9H3D4-11] DR ProteomicsDB; 80695; -. [Q9H3D4-12] DR ProteomicsDB; 80696; -. [Q9H3D4-2] DR ProteomicsDB; 80697; -. [Q9H3D4-3] DR ProteomicsDB; 80698; -. [Q9H3D4-4] DR ProteomicsDB; 80699; -. [Q9H3D4-5] DR ProteomicsDB; 80700; -. [Q9H3D4-6] DR ProteomicsDB; 80701; -. [Q9H3D4-7] DR ProteomicsDB; 80702; -. [Q9H3D4-8] DR ProteomicsDB; 80703; -. [Q9H3D4-9] DR Antibodypedia; 1750; 1268 antibodies from 50 providers. DR DNASU; 8626; -. DR Ensembl; ENST00000264731.8; ENSP00000264731.3; ENSG00000073282.14. [Q9H3D4-1] DR Ensembl; ENST00000320472.9; ENSP00000317510.5; ENSG00000073282.14. [Q9H3D4-7] DR Ensembl; ENST00000354600.10; ENSP00000346614.5; ENSG00000073282.14. [Q9H3D4-2] DR Ensembl; ENST00000392460.7; ENSP00000376253.3; ENSG00000073282.14. [Q9H3D4-3] DR Ensembl; ENST00000392461.7; ENSP00000376254.3; ENSG00000073282.14. [Q9H3D4-8] DR Ensembl; ENST00000392463.6; ENSP00000376256.2; ENSG00000073282.14. [Q9H3D4-4] DR Ensembl; ENST00000418709.6; ENSP00000407144.2; ENSG00000073282.14. [Q9H3D4-5] DR Ensembl; ENST00000437221.5; ENSP00000392488.1; ENSG00000073282.14. [Q9H3D4-6] DR Ensembl; ENST00000440651.6; ENSP00000394337.2; ENSG00000073282.14. [Q9H3D4-11] DR Ensembl; ENST00000449992.5; ENSP00000387839.1; ENSG00000073282.14. [Q9H3D4-10] DR Ensembl; ENST00000456148.1; ENSP00000389485.1; ENSG00000073282.14. [Q9H3D4-12] DR GeneID; 8626; -. DR KEGG; hsa:8626; -. DR MANE-Select; ENST00000264731.8; ENSP00000264731.3; NM_003722.5; NP_003713.3. DR UCSC; uc003frx.3; human. [Q9H3D4-1] DR AGR; HGNC:15979; -. DR CTD; 8626; -. DR DisGeNET; 8626; -. DR GeneCards; TP63; -. DR GeneReviews; TP63; -. DR HGNC; HGNC:15979; TP63. DR HPA; ENSG00000073282; Tissue enhanced (esophagus, skin). DR MalaCards; TP63; -. DR MIM; 103285; phenotype. DR MIM; 106260; phenotype. DR MIM; 129400; phenotype. DR MIM; 603273; gene. DR MIM; 603543; phenotype. DR MIM; 604292; phenotype. DR MIM; 605289; phenotype. DR MIM; 618149; phenotype. DR MIM; 620311; phenotype. DR neXtProt; NX_Q9H3D4; -. DR OpenTargets; ENSG00000073282; -. DR Orphanet; 978; ADULT syndrome. DR Orphanet; 1072; Ankyloblepharon filiforme adnatum-cleft palate syndrome. DR Orphanet; 93930; Bladder exstrophy. DR Orphanet; 141291; Cleft lip and alveolus. DR Orphanet; 199306; Cleft lip/palate. DR Orphanet; 1896; EEC syndrome. DR Orphanet; 199302; Isolated cleft lip. DR Orphanet; 2440; Isolated split hand-split foot malformation. DR Orphanet; 69085; Limb-mammary syndrome. DR PharmGKB; PA162406776; -. DR VEuPathDB; HostDB:ENSG00000073282; -. DR eggNOG; ENOG502QQ48; Eukaryota. DR GeneTree; ENSGT00950000183153; -. DR HOGENOM; CLU_019621_1_0_1; -. DR InParanoid; Q9H3D4; -. DR OMA; IRMQDSE; -. DR OrthoDB; 2902631at2759; -. DR PhylomeDB; Q9H3D4; -. DR TreeFam; TF106101; -. DR PathwayCommons; Q9H3D4; -. DR Reactome; R-HSA-139915; Activation of PUMA and translocation to mitochondria. DR Reactome; R-HSA-5620971; Pyroptosis. DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes. DR Reactome; R-HSA-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release. DR Reactome; R-HSA-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain. DR Reactome; R-HSA-6803207; TP53 Regulates Transcription of Caspase Activators and Caspases. DR Reactome; R-HSA-6803211; TP53 Regulates Transcription of Death Receptors and Ligands. DR Reactome; R-HSA-6804759; Regulation of TP53 Activity through Association with Co-factors. DR SignaLink; Q9H3D4; -. DR SIGNOR; Q9H3D4; -. DR BioGRID-ORCS; 8626; 53 hits in 1184 CRISPR screens. DR ChiTaRS; TP63; human. DR EvolutionaryTrace; Q9H3D4; -. DR GeneWiki; TP63; -. DR GenomeRNAi; 8626; -. DR Pharos; Q9H3D4; Tbio. DR PRO; PR:Q9H3D4; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9H3D4; Protein. DR Bgee; ENSG00000073282; Expressed in upper leg skin and 151 other cell types or tissues. DR ExpressionAtlas; Q9H3D4; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB. DR GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl. DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:CAFA. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB. DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; IPI:CAFA. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0002039; F:p53 binding; IPI:CAFA. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:GO_Central. DR GO; GO:0050699; F:WW domain binding; IPI:UniProtKB. DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc. DR GO; GO:0090398; P:cellular senescence; IEA:Ensembl. DR GO; GO:0006338; P:chromatin remodeling; IEA:Ensembl. DR GO; GO:0060197; P:cloacal septation; IEA:Ensembl. DR GO; GO:1904888; P:cranial skeletal system development; IEA:Ensembl. DR GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl. DR GO; GO:0006974; P:DNA damage response; IDA:UniProtKB. DR GO; GO:0007499; P:ectoderm and mesoderm interaction; IEA:Ensembl. DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl. DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl. DR GO; GO:0010481; P:epidermal cell division; IEA:Ensembl. DR GO; GO:0002064; P:epithelial cell development; IEA:Ensembl. DR GO; GO:0001736; P:establishment of planar polarity; IEA:Ensembl. DR GO; GO:0061436; P:establishment of skin barrier; ISS:UniProtKB. DR GO; GO:0048807; P:female genitalia morphogenesis; IEA:Ensembl. DR GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl. DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl. DR GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl. DR GO; GO:0043616; P:keratinocyte proliferation; IEA:Ensembl. DR GO; GO:2000773; P:negative regulation of cellular senescence; IMP:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; IEA:Ensembl. DR GO; GO:0045617; P:negative regulation of keratinocyte differentiation; IEA:Ensembl. DR GO; GO:2000381; P:negative regulation of mesoderm development; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl. DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl. DR GO; GO:0030859; P:polarized epithelial cell differentiation; IEA:Ensembl. DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; IMP:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; IDA:UniProtKB. DR GO; GO:0010838; P:positive regulation of keratinocyte proliferation; IEA:Ensembl. DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:UniProtKB. DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL. DR GO; GO:1904674; P:positive regulation of somatic stem cell population maintenance; IEA:Ensembl. DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0036342; P:post-anal tail morphogenesis; IEA:Ensembl. DR GO; GO:0060513; P:prostatic bud formation; IEA:Ensembl. DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro. DR GO; GO:0009954; P:proximal/distal pattern formation; IEA:Ensembl. DR GO; GO:0010482; P:regulation of epidermal cell division; ISS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl. DR GO; GO:0043589; P:skin morphogenesis; IEA:Ensembl. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR GO; GO:0060529; P:squamous basal epithelial stem cell differentiation involved in prostate gland acinus development; IEA:Ensembl. DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl. DR GO; GO:0048485; P:sympathetic nervous system development; IEA:Ensembl. DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl. DR CDD; cd08367; P53; 1. DR CDD; cd09572; SAM_tumor-p63; 1. DR Gene3D; 2.60.40.720; -; 1. DR Gene3D; 4.10.170.10; p53-like tetramerisation domain; 1. DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 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; IPR002117; p53_tumour_suppressor. DR InterPro; IPR001660; SAM. DR InterPro; IPR013761; SAM/pointed_sf. DR InterPro; IPR037611; Tumor-p63_SAM. DR PANTHER; PTHR11447; CELLULAR TUMOR ANTIGEN P53; 1. DR PANTHER; PTHR11447:SF8; TUMOR PROTEIN 63; 1. DR Pfam; PF00870; P53; 1. DR Pfam; PF07710; P53_tetramer; 1. DR Pfam; PF07647; SAM_2; 1. DR PRINTS; PR00386; P53SUPPRESSR. DR SMART; SM00454; SAM; 1. DR SUPFAM; SSF47719; p53 tetramerization domain; 1. DR SUPFAM; SSF49417; p53-like transcription factors; 1. DR SUPFAM; SSF47769; SAM/Pointed domain; 1. DR PROSITE; PS00348; P53; 1. DR Genevisible; Q9H3D4; HS. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative promoter usage; Alternative splicing; KW Apoptosis; Developmental protein; Disease variant; DNA-binding; KW Ectodermal dysplasia; Isopeptide bond; Metal-binding; KW Notch signaling pathway; Nucleus; Premature ovarian failure; KW Reference proteome; Transcription; Transcription regulation; KW Ubl conjugation; Zinc. FT CHAIN 1..680 FT /note="Tumor protein 63" FT /id="PRO_0000185729" FT DOMAIN 541..607 FT /note="SAM" FT DNA_BIND 170..362 FT REGION 1..107 FT /note="Transcription activation" FT REGION 123..171 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 351..393 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 352..388 FT /note="Interaction with HIPK2" FT /evidence="ECO:0000269|PubMed:11925430" FT REGION 394..443 FT /note="Oligomerization" FT REGION 435..472 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 610..680 FT /note="Transactivation inhibition" FT COMPBIAS 123..166 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 364..389 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 244 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 247 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 308 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 312 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT CROSSLNK 676 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000250" FT VAR_SEQ 1..108 FT /note="MNFETSRCATLQYCPDPYIQRFVETPAHFSWKESYYRSTMSQSTQTNEFLSP FT EVFQHIWDFLEQPICSVQPIDLNFVDEPSEDGATNKIEISMDCIRMQDSDLSDPMW -> FT MLYLENNAQTQFSE (in isoform 2, isoform 4, isoform 6, isoform FT 8, isoform 10 and isoform 12)" FT /evidence="ECO:0000303|PubMed:10469295, FT ECO:0000303|PubMed:11336476, ECO:0000303|PubMed:9703973, FT ECO:0000303|PubMed:9774969" FT /id="VSP_012465" FT VAR_SEQ 109..193 FT /note="Missing (in isoform 9 and isoform 10)" FT /evidence="ECO:0000303|PubMed:11336476" FT /id="VSP_012466" FT VAR_SEQ 373..377 FT /note="GTKRP -> A (in isoform 11 and isoform 12)" FT /evidence="ECO:0000303|PubMed:11477076" FT /id="VSP_012467" FT VAR_SEQ 450..680 FT /note="QTSIQSPSSYGNSSPPLNKMNSMNKLPSVSQLINPQQRNALTPTTIPDGMGA FT NIPMMGTHMPMAGDMNGLSPTQALPPPLSMPSTSHCTPPPPYPTDCSIVSFLARLGCSS FT CLDYFTTQGLTTIYQIEHYSMDDLASLKIPEQFRHAIWKGILDHRQLHEFSSPSHLLRT FT PSSASTVSVGSSETRGERVIDAVRFTLRQTISFPPRDEWNDFNFDMDARRNKQQRIKEE FT GE -> HLLSACFRNELVEPRRETPKQSDVFFRHSKPPNRSVYP (in isoform 5 FT and isoform 6)" FT /evidence="ECO:0000303|PubMed:9662378, FT ECO:0000303|PubMed:9774969" FT /id="VSP_012468" FT VAR_SEQ 503..680 FT /note="IPMMGTHMPMAGDMNGLSPTQALPPPLSMPSTSHCTPPPPYPTDCSIVSFLA FT RLGCSSCLDYFTTQGLTTIYQIEHYSMDDLASLKIPEQFRHAIWKGILDHRQLHEFSSP FT SHLLRTPSSASTVSVGSSETRGERVIDAVRFTLRQTISFPPRDEWNDFNFDMDARRNKQ FT QRIKEEGE -> RSGKSENP (in isoform 7 and isoform 8)" FT /evidence="ECO:0000303|PubMed:10935472" FT /id="VSP_012469" FT VAR_SEQ 551..680 FT /note="SFLARLGCSSCLDYFTTQGLTTIYQIEHYSMDDLASLKIPEQFRHAIWKGIL FT DHRQLHEFSSPSHLLRTPSSASTVSVGSSETRGERVIDAVRFTLRQTISFPPRDEWNDF FT NFDMDARRNKQQRIKEEGE -> RIWQV (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:9774969" FT /id="VSP_012470" FT VARIANT 18 FT /note="Y -> C (in POF21; uncertain significance; no effect FT on transcriptional activation in a luciferase reporter FT assay; does not affect oligomerization)" FT /evidence="ECO:0000269|PubMed:35801529" FT /id="VAR_088375" FT VARIANT 97 FT /note="R -> P (in POF21; uncertain significance; results in FT increased transcriptional activation in a luciferase FT reporter assay; affects oligomerization)" FT /evidence="ECO:0000269|PubMed:35801529" FT /id="VAR_088376" FT VARIANT 129 FT /note="S -> L (in dbSNP:rs193287780)" FT /evidence="ECO:0000269|PubMed:16740912" FT /id="VAR_035126" FT VARIANT 184 FT /note="S -> L (in head/neck cancer)" FT /evidence="ECO:0000269|PubMed:9662378" FT /id="VAR_020866" FT VARIANT 187 FT /note="A -> P (in lung carcinoma; somatic mutation)" FT /evidence="ECO:0000269|PubMed:9662378" FT /id="VAR_020867" FT VARIANT 193 FT /note="T -> TP (in SHFM4)" FT /evidence="ECO:0000269|PubMed:11462173" FT /id="VAR_032736" FT VARIANT 204 FT /note="Q -> L (in cervical cancer)" FT /evidence="ECO:0000269|PubMed:9662378" FT /id="VAR_020868" FT VARIANT 232 FT /note="K -> E (in SHFM4; dbSNP:rs1560274243)" FT /evidence="ECO:0000269|PubMed:11462173" FT /id="VAR_032737" FT VARIANT 233 FT /note="K -> E (in SHFM4; dbSNP:rs121908838)" FT /evidence="ECO:0000269|PubMed:10839977" FT /id="VAR_020869" FT VARIANT 243 FT /note="R -> Q (in EEC3; dbSNP:rs121908836)" FT /evidence="ECO:0000269|PubMed:10535733, FT ECO:0000269|PubMed:11462173" FT /id="VAR_020870" FT VARIANT 243 FT /note="R -> W (in EEC3; dbSNP:rs121908835)" FT /evidence="ECO:0000269|PubMed:10535733, FT ECO:0000269|PubMed:11462173" FT /id="VAR_020871" FT VARIANT 266 FT /note="R -> Q (in EEC3; dbSNP:rs121908849)" FT /evidence="ECO:0000269|PubMed:11462173" FT /id="VAR_032738" FT VARIANT 279 FT /note="P -> H (in colon cancer)" FT /evidence="ECO:0000269|PubMed:10485447" FT /id="VAR_020872" FT VARIANT 285 FT /note="S -> N (in POF21; uncertain significance; no effect FT on transcriptional activation in a luciferase reporter FT assay; does not affect oligomerization)" FT /evidence="ECO:0000269|PubMed:36856110" FT /id="VAR_088377" FT VARIANT 308 FT /note="C -> Y (in EEC3)" FT /evidence="ECO:0000269|PubMed:11462173" FT /id="VAR_032739" FT VARIANT 311 FT /note="S -> N (in EEC3)" FT /evidence="ECO:0000269|PubMed:11462173" FT /id="VAR_032740" FT VARIANT 318 FT /note="R -> C (in EEC3; dbSNP:rs1205536026)" FT /evidence="ECO:0000269|PubMed:11462173" FT /id="VAR_032741" FT VARIANT 318 FT /note="R -> H (in EEC3 and RHS; does not decrease the FT transcriptional activity of the isoform 5 on a TP53 FT reporter system but disrupts the dominant-negative activity FT of isoform 2 and isoform 5 on the transcriptional activity FT of TP53; dbSNP:rs121908840)" FT /evidence="ECO:0000269|PubMed:10839977, FT ECO:0000269|PubMed:11462173, ECO:0000269|PubMed:12939657" FT /id="VAR_020873" FT VARIANT 318 FT /note="R -> Q (in EEC3)" FT /evidence="ECO:0000269|PubMed:11462173" FT /id="VAR_032742" FT VARIANT 319 FT /note="R -> C (in EEC3; dbSNP:rs121908839)" FT /evidence="ECO:0000269|PubMed:10839977, FT ECO:0000269|PubMed:11462173" FT /id="VAR_020874" FT VARIANT 319 FT /note="R -> H (in EEC3 and SHFM4; dbSNP:rs886039442)" FT /evidence="ECO:0000269|PubMed:11462173" FT /id="VAR_032743" FT VARIANT 319 FT /note="R -> S (in EEC3)" FT /evidence="ECO:0000269|PubMed:11462173" FT /id="VAR_032744" FT VARIANT 337 FT /note="R -> Q (in ADULT syndrome; confers novel FT transcription activation capacity on isoform 6; FT dbSNP:rs113993967)" FT /evidence="ECO:0000269|PubMed:11929852" FT /id="VAR_020875" FT VARIANT 343 FT /note="R -> Q (in EEC3; dbSNP:rs121908841)" FT /evidence="ECO:0000269|PubMed:10839977, FT ECO:0000269|PubMed:11462173" FT /id="VAR_020876" FT VARIANT 343 FT /note="R -> W (in EEC3; dbSNP:rs886041251)" FT /evidence="ECO:0000269|PubMed:11462173" FT /id="VAR_032745" FT VARIANT 345 FT /note="C -> R (in EEC3; abolishes transcription activation; FT dbSNP:rs121908837)" FT /evidence="ECO:0000269|PubMed:10535733, FT ECO:0000269|PubMed:11462173" FT /id="VAR_020877" FT VARIANT 347 FT /note="C -> S (in EEC3)" FT /evidence="ECO:0000269|PubMed:11462173" FT /id="VAR_032746" FT VARIANT 348 FT /note="P -> S (in EEC3)" FT /evidence="ECO:0000269|PubMed:11462173" FT /id="VAR_032747" FT VARIANT 351 FT /note="D -> G (in EEC3; dbSNP:rs121908844)" FT /evidence="ECO:0000269|PubMed:12838557" FT /id="VAR_020878" FT VARIANT 351 FT /note="D -> H (in EEC3)" FT /evidence="ECO:0000269|PubMed:11462173" FT /id="VAR_032748" FT VARIANT 352 FT /note="R -> G (in OFC8; dbSNP:rs121908847)" FT /evidence="ECO:0000269|PubMed:16740912" FT /id="VAR_035127" FT VARIANT 538 FT /note="T -> A (in POF21; uncertain significance; no effect FT on transcriptional activation in a luciferase reporter FT assay; does not affect oligomerization)" FT /evidence="ECO:0000269|PubMed:36856110" FT /id="VAR_088378" FT VARIANT 549 FT /note="I -> T (in RHS; dbSNP:rs121908845)" FT /evidence="ECO:0000269|PubMed:15200513" FT /id="VAR_035128" FT VARIANT 553 FT /note="L -> F (in AEC; dbSNP:rs121908842)" FT /evidence="ECO:0000269|PubMed:11159940" FT /id="VAR_020879" FT VARIANT 560 FT /note="S -> A (in ovarian cancer)" FT /evidence="ECO:0000269|PubMed:10485447" FT /id="VAR_020880" FT VARIANT 561 FT /note="C -> G (in AEC; dbSNP:rs121908843)" FT /evidence="ECO:0000269|PubMed:11159940" FT /id="VAR_020881" FT VARIANT 567 FT /note="T -> I (in POF21; uncertain significance; no effect FT on transcriptional activation in a luciferase reporter FT assay; does not affect oligomerization)" FT /evidence="ECO:0000269|PubMed:36856110" FT /id="VAR_088379" FT VARIANT 580 FT /note="S -> P (in RHS; dbSNP:rs121908846)" FT /evidence="ECO:0000269|PubMed:12766194" FT /id="VAR_035129" FT VARIANT 594..680 FT /note="Missing (in POF21; results in increased FT transcriptional activation in luciferase reporter assays; FT affects oligomerization)" FT /evidence="ECO:0000269|PubMed:30924587, FT ECO:0000269|PubMed:36856110" FT /id="VAR_088380" FT VARIANT 598..680 FT /note="Missing (in POF21)" FT /evidence="ECO:0000269|PubMed:30924587" FT /id="VAR_088381" FT VARIANT 603 FT /note="D -> H (in dbSNP:rs767906723)" FT /evidence="ECO:0000269|PubMed:16740912" FT /id="VAR_035130" FT VARIANT 643..680 FT /note="Missing (in LMS)" FT /evidence="ECO:0000269|PubMed:32067224" FT /id="VAR_088382" FT VARIANT 643 FT /note="R -> Q (in POF21; results in increased FT transcriptional activation in luciferase reporter assays; FT affects oligomerization)" FT /evidence="ECO:0000269|PubMed:36856110" FT /id="VAR_088383" FT VARIANT 646 FT /note="L -> P (in POF21; results in increased FT transcriptional activation in luciferase reporter assays; FT affects oligomerization)" FT /evidence="ECO:0000269|PubMed:36856110" FT /id="VAR_088384" FT VARIANT 647 FT /note="R -> C (in POF21; results in increased FT transcriptional activation in luciferase reporter assays; FT affects oligomerization; when expressed in mice, it results FT in accelerated oocyte loss via apoptosis)" FT /evidence="ECO:0000269|PubMed:35801529, FT ECO:0000269|PubMed:36856110" FT /id="VAR_088385" FT VARIANT 655 FT /note="R -> Q (in POF21; results in increased FT transcriptional activation in luciferase reporter assays)" FT /evidence="ECO:0000269|PubMed:36856110" FT /id="VAR_088386" FT MUTAGEN 18 FT /note="Y->A: No effect on transcriptional activation in a FT luciferase reporter assay." FT /evidence="ECO:0000269|PubMed:35801529" FT MUTAGEN 55 FT /note="F->A: Abrogates transcriptional activity and FT interaction with transactivation inhibition domain; when FT associated with A-59 and A-62." FT /evidence="ECO:0000269|PubMed:12446779" FT MUTAGEN 59 FT /note="W->A: Abrogates transcriptional activity and FT interaction with transactivation inhibition domain; when FT associated with A-55 and A-62." FT /evidence="ECO:0000269|PubMed:12446779" FT MUTAGEN 62 FT /note="L->A: Abrogates transcriptional activity and FT interaction with transactivation inhibition domain; when FT associated with A-55 and A-59." FT /evidence="ECO:0000269|PubMed:12446779" FT MUTAGEN 97 FT /note="R->C: No effect on transcriptional activation in a FT luciferase reporter assay." FT /evidence="ECO:0000269|PubMed:35801529" FT MUTAGEN 543 FT /note="Y->F: Abolishes ubiquitination." FT /evidence="ECO:0000269|PubMed:18806757" FT MUTAGEN 643 FT /note="R->A: Increased transcriptional activation in a FT luciferase reporter assay." FT /evidence="ECO:0000269|PubMed:35801529" FT MUTAGEN 647 FT /note="R->A: Increased transcriptional activation in a FT luciferase reporter assay." FT /evidence="ECO:0000269|PubMed:35801529" FT CONFLICT 125 FT /note="Q -> R (in Ref. 1; BAA32433)" FT /evidence="ECO:0000305" FT CONFLICT 154 FT /note="S -> P (in Ref. 1; BAA32433)" FT /evidence="ECO:0000305" FT CONFLICT 177 FT /note="F -> S (in Ref. 1; BAA32433)" FT /evidence="ECO:0000305" FT CONFLICT 378 FT /note="F -> S (in Ref. 10; AAC24830)" FT /evidence="ECO:0000305" FT CONFLICT 536 FT /note="H -> Q (in Ref. 2; CAA76562)" FT /evidence="ECO:0000305" FT CONFLICT 551 FT /note="S -> G (in Ref. 4; BAA32593 and 7; FT AAF43487/AAF43491)" FT /evidence="ECO:0000305" FT HELIX 54..63 FT /evidence="ECO:0007829|PDB:6FGN" FT STRAND 156..161 FT /evidence="ECO:0007829|PDB:2RMN" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:7Z7E" FT STRAND 178..180 FT /evidence="ECO:0007829|PDB:7Z7E" FT STRAND 186..189 FT /evidence="ECO:0007829|PDB:7Z71" FT STRAND 193..195 FT /evidence="ECO:0007829|PDB:7Z7E" FT TURN 196..199 FT /evidence="ECO:0007829|PDB:7Z7E" FT STRAND 200..203 FT /evidence="ECO:0007829|PDB:7Z7E" FT STRAND 209..214 FT /evidence="ECO:0007829|PDB:7Z7E" FT STRAND 224..233 FT /evidence="ECO:0007829|PDB:7Z7E" FT HELIX 234..236 FT /evidence="ECO:0007829|PDB:7Z7E" FT HELIX 245..249 FT /evidence="ECO:0007829|PDB:7Z7E" FT TURN 252..256 FT /evidence="ECO:0007829|PDB:7Z7E" FT STRAND 264..269 FT /evidence="ECO:0007829|PDB:7Z7E" FT STRAND 274..277 FT /evidence="ECO:0007829|PDB:7Z7E" FT TURN 279..281 FT /evidence="ECO:0007829|PDB:7Z7E" FT STRAND 284..289 FT /evidence="ECO:0007829|PDB:7Z7E" FT STRAND 294..296 FT /evidence="ECO:0007829|PDB:7Z7E" FT STRAND 300..306 FT /evidence="ECO:0007829|PDB:7Z7E" FT TURN 313..318 FT /evidence="ECO:0007829|PDB:7Z7E" FT STRAND 321..328 FT /evidence="ECO:0007829|PDB:7Z7E" FT STRAND 330..332 FT /evidence="ECO:0007829|PDB:3QYM" FT STRAND 334..344 FT /evidence="ECO:0007829|PDB:7Z7E" FT HELIX 348..357 FT /evidence="ECO:0007829|PDB:7Z7E" FT STRAND 369..372 FT /evidence="ECO:0007829|PDB:2RMN" FT STRAND 401..407 FT /evidence="ECO:0007829|PDB:3ZY0" FT HELIX 408..426 FT /evidence="ECO:0007829|PDB:3ZY0" FT HELIX 429..436 FT /evidence="ECO:0007829|PDB:3ZY1" FT HELIX 444..449 FT /evidence="ECO:0007829|PDB:4A9Z" FT STRAND 546..548 FT /evidence="ECO:0007829|PDB:2Y9T" FT HELIX 549..554 FT /evidence="ECO:0007829|PDB:2Y9U" FT TURN 555..557 FT /evidence="ECO:0007829|PDB:2Y9U" FT HELIX 559..561 FT /evidence="ECO:0007829|PDB:2Y9U" FT HELIX 562..566 FT /evidence="ECO:0007829|PDB:2Y9U" FT TURN 567..569 FT /evidence="ECO:0007829|PDB:2Y9U" FT HELIX 573..576 FT /evidence="ECO:0007829|PDB:2Y9U" FT HELIX 581..586 FT /evidence="ECO:0007829|PDB:2Y9U" FT HELIX 591..609 FT /evidence="ECO:0007829|PDB:2Y9U" FT STRAND 613..615 FT /evidence="ECO:0007829|PDB:2Y9T" FT HELIX 622..625 FT /evidence="ECO:0007829|PDB:6RU8" FT VARIANT Q9H3D4-2:6 FT /note="N -> H (in ADULT syndrome; dbSNP:rs113993963)" FT /evidence="ECO:0000305" FT /id="VAR_082924" FT VARIANT Q9H3D4-4:6 FT /note="N -> H (in ADULT syndrome; dbSNP:rs113993963)" FT /evidence="ECO:0000305" FT /id="VAR_082925" FT VARIANT Q9H3D4-6:6 FT /note="N -> H (in ADULT syndrome; dbSNP:rs113993963)" FT /evidence="ECO:0000305" FT /id="VAR_082926" FT VARIANT Q9H3D4-8:6 FT /note="N -> H (in ADULT syndrome; dbSNP:rs113993963)" FT /evidence="ECO:0000305" FT /id="VAR_082927" FT VARIANT Q9H3D4-10:6 FT /note="N -> H (in ADULT syndrome; dbSNP:rs113993963)" FT /evidence="ECO:0000305" FT /id="VAR_082928" FT VARIANT Q9H3D4-12:6 FT /note="N -> H (in ADULT syndrome; dbSNP:rs113993963)" FT /evidence="ECO:0000305" FT /id="VAR_082929" SQ SEQUENCE 680 AA; 76785 MW; F66ECD45E87D9799 CRC64; MNFETSRCAT LQYCPDPYIQ RFVETPAHFS WKESYYRSTM SQSTQTNEFL SPEVFQHIWD FLEQPICSVQ PIDLNFVDEP SEDGATNKIE ISMDCIRMQD SDLSDPMWPQ YTNLGLLNSM DQQIQNGSSS TSPYNTDHAQ NSVTAPSPYA QPSSTFDALS PSPAIPSNTD YPGPHSFDVS FQQSSTAKSA TWTYSTELKK LYCQIAKTCP IQIKVMTPPP QGAVIRAMPV YKKAEHVTEV VKRCPNHELS REFNEGQIAP PSHLIRVEGN SHAQYVEDPI TGRQSVLVPY EPPQVGTEFT TVLYNFMCNS SCVGGMNRRP ILIIVTLETR DGQVLGRRCF EARICACPGR DRKADEDSIR KQQVSDSTKN GDGTKRPFRQ NTHGIQMTSI KKRRSPDDEL LYLPVRGRET YEMLLKIKES LELMQYLPQH TIETYRQQQQ QQHQHLLQKQ TSIQSPSSYG NSSPPLNKMN SMNKLPSVSQ LINPQQRNAL TPTTIPDGMG ANIPMMGTHM PMAGDMNGLS PTQALPPPLS MPSTSHCTPP PPYPTDCSIV SFLARLGCSS CLDYFTTQGL TTIYQIEHYS MDDLASLKIP EQFRHAIWKG ILDHRQLHEF SSPSHLLRTP SSASTVSVGS SETRGERVID AVRFTLRQTI SFPPRDEWND FNFDMDARRN KQQRIKEEGE //