P63_HUMAN
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 03-AUG-2022, entry version 211.
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 AND 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 IN NDELTA-TYPE ISOFORMS.
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).
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=2; 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}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=Defects in TP63 are a cause of cervical, colon, head and
CC neck, lung and ovarian cancers.
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 -!- 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="http://atlasgeneticsoncology.org/Genes/TP63ID365ch3q27.html";
CC ---------------------------------------------------------------------------
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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 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 AlphaFoldDB; Q9H3D4; -.
DR BMRB; Q9H3D4; -.
DR SMR; Q9H3D4; -.
DR BioGRID; 114181; 295.
DR DIP; DIP-29588N; -.
DR ELM; Q9H3D4; -.
DR IntAct; Q9H3D4; 93.
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; Q9H3D4; -.
DR PeptideAtlas; Q9H3D4; -.
DR PRIDE; 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; 1024 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 CTD; 8626; -.
DR DisGeNET; 8626; -.
DR GeneCards; TP63; -.
DR GeneReviews; TP63; -.
DR HGNC; HGNC:15979; TP63.
DR HPA; ENSG00000073282; Tissue enhanced (esophagus, skin, vagina).
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 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 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 1101 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 149 other tissues.
DR ExpressionAtlas; Q9H3D4; baseline and differential.
DR Genevisible; Q9H3D4; HS.
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:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl.
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:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
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: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:0010259; P:multicellular organism aging; IEA:Ensembl.
DR GO; GO:2000773; P:negative regulation of cellular senescence; IMP: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:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
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: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:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
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:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; 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; 1.10.150.50; -; 1.
DR Gene3D; 2.60.40.720; -; 1.
DR Gene3D; 4.10.170.10; -; 1.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
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; IPR032645; Tp63.
DR InterPro; IPR037611; Tumor-p63_SAM.
DR PANTHER; PTHR11447; PTHR11447; 1.
DR PANTHER; PTHR11447:SF8; PTHR11447:SF8; 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; SSF47719; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR PROSITE; PS00348; P53; 1.
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; Reference proteome; Transcription;
KW Transcription regulation; 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 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 and 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 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 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 580
FT /note="S -> P (in RHS; dbSNP:rs121908846)"
FT /evidence="ECO:0000269|PubMed:12766194"
FT /id="VAR_035129"
FT VARIANT 603
FT /note="D -> H (in dbSNP:rs767906723)"
FT /evidence="ECO:0000269|PubMed:16740912"
FT /id="VAR_035130"
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 543
FT /note="Y->F: Abolishes ubiquitination."
FT /evidence="ECO:0000269|PubMed:18806757"
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; AAF43487/
FT 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:3QYN"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:3QYN"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:3QYN"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:3QYN"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:3QYN"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:3QYN"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:3QYN"
FT STRAND 224..233
FT /evidence="ECO:0007829|PDB:3QYN"
FT TURN 234..238
FT /evidence="ECO:0007829|PDB:3QYN"
FT HELIX 245..249
FT /evidence="ECO:0007829|PDB:3QYN"
FT TURN 252..256
FT /evidence="ECO:0007829|PDB:3QYN"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:3QYN"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:3QYN"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:3QYN"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:3QYN"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:3QYN"
FT TURN 313..318
FT /evidence="ECO:0007829|PDB:3QYN"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:3QYN"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:3QYM"
FT STRAND 334..343
FT /evidence="ECO:0007829|PDB:3QYN"
FT HELIX 348..355
FT /evidence="ECO:0007829|PDB:3QYN"
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
