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Tumor protein 63 (p63) (Chronic ulcerative stomatitis protein) (CUSP) (Keratinocyte transcription factor KET) (Transformation-related protein 63) (TP63) (Tumor protein p73-like) (p73L) (p40) (p51)

 P63_HUMAN               Reviewed;         680 AA.
Q9H3D4; O75080; O75195; O75922; O76078; Q6VEG2; Q6VEG3; Q6VEG4;
Q6VFJ1; Q6VFJ2; Q6VFJ3; Q6VH20; Q7LDI3; Q7LDI4; Q7LDI5; Q96KR0;
Q9H3D2; Q9H3D3; Q9H3P8; Q9NPH7; Q9P1B4; Q9P1B5; Q9P1B6; Q9P1B7;
Q9UBV9; Q9UE10; Q9UP26; Q9UP27; Q9UP28; Q9UP74;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
27-SEP-2017, entry version 174.
RecName: Full=Tumor protein 63;
Short=p63;
AltName: Full=Chronic ulcerative stomatitis protein;
Short=CUSP;
AltName: Full=Keratinocyte transcription factor KET;
AltName: Full=Transformation-related protein 63;
Short=TP63;
AltName: Full=Tumor protein p73-like;
Short=p73L;
AltName: Full=p40;
AltName: Full=p51;
Name=TP63; Synonyms=KET, P63, P73H, P73L, TP73L;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=9703973; DOI=10.1006/bbrc.1998.9013;
Senoo M., Seki N., Ohira M., Sugano S., Watanabe M., Tachibana M.,
Tanaka T., Shinkai Y., Kato H.;
"A second p53-related protein, p73L, with high homology to p73.";
Biochem. Biophys. Res. Commun. 248:603-607(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Keratinocyte, and Skeletal muscle;
PubMed=9799841; DOI=10.1007/s003359900891;
Augustin M., Bamberger C., Paul D., Schmale H.;
"Cloning and chromosomal mapping of the human p53-related KET gene to
chromosome 3q27 and its murine homolog Ket to mouse chromosome 16.";
Mamm. Genome 9:899-902(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4 AND 6), NUCLEOTIDE SEQUENCE
[GENOMIC DNA] OF 32-680 (ISOFORMS 1; 3 AND 5), FUNCTION, AND TISSUE
SPECIFICITY.
PubMed=9774969; DOI=10.1016/S1097-2765(00)80275-0;
Yang A., Kaghad M., Wang Y., Gillett E., Fleming M.D., Doetsch V.,
Andrews N.C., Caput D., McKeon F.;
"p63, a p53 homolog at 3q27-29, encodes multiple products with
transactivating, death-inducing, and dominant-negative activities.";
Mol. Cell 2:305-316(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5), VARIANT HEAD AND NECK
CANCER LEU-184, VARIANT LUNG CARCINOMA PRO-187, AND VARIANT CERVICAL
CANCER LEU-204.
TISSUE=Skeletal muscle;
PubMed=9662378; DOI=10.1038/nm0798-839;
Osada M., Ohba M., Kawahara C., Ishioka C., Kanamaru R., Katoh I.,
Ikawa Y., Nimura Y., Nakagawara A., Obinata M., Ikawa S.;
"Cloning and functional analysis of human p51, which structurally and
functionally resembles p53.";
Nat. Med. 4:839-843(1998).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT COLON CANCER HIS-279, AND
VARIANT OVARIAN CANCER ALA-560.
PubMed=10485447;
Hagiwara K., McMenamin M.G., Miura K., Harris C.C.;
"Mutational analysis of the p63/p73L/p51/p40/CUSP/KET gene in human
cancer cell lines using intronic primers.";
Cancer Res. 59:4165-4169(1999).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=10469295; DOI=10.1046/j.1523-1747.1999.00651.x;
Lee L.A., Walsh P., Prater C.A., Su L.-J., Marchbank A., Egbert T.B.,
Dellavalle R.P., Targoff I.N., Kaufman K.M., Chorzelski T.P.,
Jablonska S.;
"Characterization of an autoantigen associated with chronic ulcerative
stomatitis: the CUSP autoantigen is a member of the p53 family.";
J. Invest. Dermatol. 113:146-151(1999).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 7), AND ALTERNATIVE
SPLICING (ISOFORM 8).
PubMed=10935472; DOI=10.1038/sj.neo.7900008;
Tani M., Shimizu K., Kawahara C., Kohno T., Ishimoto O., Ikawa S.,
Yokota J.;
"Mutation and expression of the p51 gene in human lung cancer.";
Neoplasia 1:71-79(1999).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10), AND TISSUE SPECIFICITY
(ISOFORM 10).
PubMed=11336476; DOI=10.1054/bjoc.2000.1735;
Senoo M., Tsuchiya I., Matsumura Y., Mori T., Saito Y., Kato H.,
Okamoto T., Habu S.;
"Transcriptional dysregulation of the p73L/p63/p51/p40/KET gene in
human squamous cell carcinomas: expression of Delta Np73L, a novel
dominant-negative isoform, and loss of expression of the potential
tumour suppressor p51.";
Br. J. Cancer 84:1235-1241(2001).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-450 (ISOFORMS 2/4/8), SUBUNIT,
ZINC-BINDING, AND DNA-BINDING.
TISSUE=Prostate;
PubMed=9662346; DOI=10.1038/nm0798-747;
Trink B., Okami K., Wu L., Sriuranpong V., Jen J., Sidransky D.;
"A new human p53 homologue.";
Nat. Med. 4:747-748(1998).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21; 95-255; 295-330; 378-502
AND 583-680.
Vieira A.R., Murray J.C.;
"Sequencing of candidate genes for non-syndromic cleft lip and
palate.";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 153-388 (ISOFORM 11).
TISSUE=Placenta;
PubMed=11477076; DOI=10.1074/jbc.M103801200;
Klein C., Georges G., Kunkele K.P., Huber R., Engh R.A., Hansen S.;
"High thermostability and lack of cooperative DNA binding distinguish
the p63 core domain from the homologous tumor suppressor p53.";
J. Biol. Chem. 276:37390-37401(2001).
[13]
SUBUNIT.
PubMed=10373484; DOI=10.1074/jbc.274.26.18709;
Davison T.S., Vagner C., Kaghad M., Ayed A., Caput D.,
Arrowsmith C.H.;
"p73 and p63 are homotetramers capable of weak heterotypic
interactions with each other but not with p53.";
J. Biol. Chem. 274:18709-18714(1999).
[14]
TISSUE SPECIFICITY.
PubMed=11248048; DOI=10.1073/pnas.061032098;
Pellegrini G., Dellambra E., Golisano O., Martinelli E., Fantozzi I.,
Bondanza S., Ponzin D., McKeon F., De Luca M.;
"p63 identifies keratinocyte stem cells.";
Proc. Natl. Acad. Sci. U.S.A. 98:3156-3161(2001).
[15]
FUNCTION IN NOTCH SIGNALING.
PubMed=11641404; DOI=10.1074/jbc.M108080200;
Sasaki Y., Ishida S., Morimoto I., Yamashita T., Kojima T., Kihara C.,
Tanaka T., Imai K., Nakamura Y., Tokino T.;
"The p53 family member genes are involved in the Notch signal
pathway.";
J. Biol. Chem. 277:719-724(2002).
[16]
INTERACTION WITH HIPK2.
PubMed=11925430; DOI=10.1074/jbc.M200153200;
Kim E.-J., Park J.-S., Um S.-J.;
"Identification and characterization of HIPK2 interacting with p73 and
modulating functions of the p53 family in vivo.";
J. Biol. Chem. 277:32020-32028(2002).
[17]
FUNCTION, DOMAIN, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-55;
TRP-59 AND LEU-62.
PubMed=12446779; DOI=10.1128/MCB.22.24.8601-8611.2002;
Serber Z., Lai H.C., Yang A., Ou H.D., Sigal M.S., Kelly A.E.,
Darimont B.D., Duijf P.H.G., Van Bokhoven H., McKeon F., Doetsch V.;
"A C-terminal inhibitory domain controls the activity of p63 by an
intramolecular mechanism.";
Mol. Cell. Biol. 22:8601-8611(2002).
[18]
FUNCTION, AND DOMAIN.
PubMed=12446784; DOI=10.1128/MCB.22.24.8659-8668.2002;
Ghioni P., Bolognese F., Duijf P.H.G., Van Bokhoven H., Mantovani R.,
Guerrini L.;
"Complex transcriptional effects of p63 isoforms: identification of
novel activation and repression domains.";
Mol. Cell. Biol. 22:8659-8668(2002).
[19]
FUNCTION, AND INTERACTION WITH SSRP1.
PubMed=12374749; DOI=10.1093/emboj/cdf540;
Zeng S.X., Dai M.-S., Keller D.M., Lu H.;
"SSRP1 functions as a co-activator of the transcriptional activator
p63.";
EMBO J. 21:5487-5497(2002).
[20]
ERRATUM.
Zeng S.X., Dai M.-S., Keller D.M., Lu H.;
EMBO J. 23:1679-1679(2004).
[21]
UBIQUITINATION, INTERACTION WITH WWP1, AND MUTAGENESIS OF TYR-543.
PubMed=18806757; DOI=10.1038/cdd.2008.134;
Li Y., Zhou Z., Chen C.;
"WW domain-containing E3 ubiquitin protein ligase 1 targets p63
transcription factor for ubiquitin-mediated proteasomal degradation
and regulates apoptosis.";
Cell Death Differ. 15:1941-1951(2008).
[22]
INTERACTION WITH PDS5A.
PubMed=17846787; DOI=10.1007/s00432-007-0306-x;
Zheng M.Z., Zheng L.M., Zeng Y.X.;
"SCC-112 gene is involved in tumor progression and promotes the cell
proliferation in G2/M phase.";
J. Cancer Res. Clin. Oncol. 134:453-462(2008).
[23]
FUNCTION, INTERACTION WITH NOC2L, AND SUBCELLULAR LOCATION.
PubMed=20123734; DOI=10.1093/nar/gkq016;
Heyne K., Willnecker V., Schneider J., Conrad M., Raulf N., Schule R.,
Roemer K.;
"NIR, an inhibitor of histone acetyltransferases, regulates
transcription factor TAp63 and is controlled by the cell cycle.";
Nucleic Acids Res. 38:3159-3171(2010).
[24]
FUNCTION.
PubMed=22197488; DOI=10.1016/j.ajhg.2011.11.013;
Mitchell K., O'Sullivan J., Missero C., Blair E., Richardson R.,
Anderson B., Antonini D., Murray J.C., Shanske A.L., Schutte B.C.,
Romano R.A., Sinha S., Bhaskar S.S., Black G.C., Dixon J., Dixon M.J.;
"Exome sequence identifies RIPK4 as the Bartsocas-Papas syndrome
locus.";
Am. J. Hum. Genet. 90:69-75(2012).
[25]
STRUCTURE BY NMR OF 540-610.
Cadot B., Candi E., Cicero D.O., Desideri A., Mele S., Melino G.,
Paci M.;
"Solution structure of the C-terminal domain of p63.";
Submitted (NOV-2004) to the PDB data bank.
[26]
VARIANTS EEC3 TRP-243; GLN-243 AND ARG-345.
PubMed=10535733; DOI=10.1016/S0092-8674(00)81646-3;
Celli J., Duijf P.H.G., Hamel B.C.J., Bamshad M., Kramer B.,
Smits A.P.T., Newbury-Ecob R., Hennekam R.C.M., Van Buggenhout G.,
van Haeringen A., Woods C.G., van Essen A.J., de Waal R., Vriend G.,
Haber D.A., Yang A., McKeon F., Brunner H.G., van Bokhoven H.;
"Heterozygous germline mutations in the p53 homolog p63 are the cause
of EEC syndrome.";
Cell 99:143-153(1999).
[27]
VARIANTS SHFM4 GLU-233 AND CYS-319, AND VARIANTS EEC3 HIS-318 AND
GLN-343.
PubMed=10839977; DOI=10.1086/302972;
Ianakiev P., Kilpatrick M.W., Toudjarska I., Basel D., Beighton P.,
Tsipouras P.;
"Split-hand/split-foot malformation is caused by mutations in the p63
gene on 3q27.";
Am. J. Hum. Genet. 67:59-66(2000).
[28]
VARIANT ADULT IN NDELTA-TYPE ISOFORMS.
PubMed=11528512; DOI=10.1038/sj.ejhg.5200676;
Amiel J., Bougeard G., Francannet C., Raclin V., Munnich A.,
Lyonnet S., Frebourg T.;
"TP63 gene mutation in ADULT syndrome.";
Eur. J. Hum. Genet. 9:642-645(2001).
[29]
VARIANTS AEC PHE-553 AND GLY-561.
PubMed=11159940; DOI=10.1093/hmg/10.3.221;
McGrath J.A., Duijf P.H.G., Doetsch V., Irvine A.D., de Waal R.,
Vanmolkot K.R., Wessagowit V., Kelly A., Atherton D.J.,
Griffiths W.A., Orlow S.J., van Haeringen A., Ausems M.G., Yang A.,
McKeon F., Bamshad M.A., Brunner H.G., Hamel B.C.J., van Bokhoven H.;
"Hay-Wells syndrome is caused by heterozygous missense mutations in
the SAM domain of p63.";
Hum. Mol. Genet. 10:221-229(2001).
[30]
VARIANTS EEC3 GLN-243; TRP-243; GLN-266; TYR-308; ASN-311; CYS-318;
HIS-318; GLN-318; CYS-319; HIS-319; SER-319; TRP-343; GLN-343;
ARG-345; SER-347; SER-348 AND HIS-351, VARIANTS SHFM4 PRO-193 INS;
GLU-232 AND HIS-319, AND INVOLVEMENT IN LMS.
PubMed=11462173; DOI=10.1086/323123;
van Bokhoven H., Hamel B.C.J., Bamshad M., Sangiorgi E., Gurrieri F.,
Duijf P.H.G., Vanmolkot K.R.J., van Beusekom E., van Beersum S.E.C.,
Celli J., Merkx G.F.M., Tenconi R., Fryns J.-P., Verloes A.,
Newbury-Ecob R.A., Raas-Rotschild A., Majewski F., Beemer F.A.,
Janecke A., Chitayat D., Crisponi G., Kayserili H., Yates J.R.W.,
Neri G., Brunner H.G.;
"p63 gene mutations in EEC syndrome, limb-mammary syndrome, and
isolated split hand-split foot malformation suggest a genotype-
phenotype correlation.";
Am. J. Hum. Genet. 69:481-492(2001).
[31]
VARIANT ADULT SYNDROME GLN-337.
PubMed=11929852; DOI=10.1093/hmg/11.7.799;
Duijf P.H.G., Vanmolkot K.R., Propping P., Friedl W., Krieger E.,
McKeon F., Doetsch V., Brunner H.G., van Bokhoven H.;
"Gain-of-function mutation in ADULT syndrome reveals the presence of a
second transactivation domain in p63.";
Hum. Mol. Genet. 11:799-804(2002).
[32]
VARIANT EEC3 GLY-351.
PubMed=12838557; DOI=10.1002/ajmg.a.20064;
Akahoshi K., Sakazume S., Kosaki K., Ohashi H., Fukushima Y.;
"EEC syndrome type 3 with a heterozygous germline mutation in the P63
gene and B cell lymphoma.";
Am. J. Med. Genet. A 120:370-373(2003).
[33]
VARIANT EDRH HIS-318, AND CHARACTERIZATION OF VARIANT EDRH HIS-318.
PubMed=12939657; DOI=10.1038/sj.ejhg.5201004;
Bougeard G., Hadj-Rabia S., Faivre L., Sarafan-Vasseur N.,
Frebourg T.;
"The Rapp-Hodgkin syndrome results from mutations of the TP63 gene.";
Eur. J. Hum. Genet. 11:700-704(2003).
[34]
VARIANT EDRH PRO-580.
PubMed=12766194; DOI=10.1177/154405910308200606;
Kantaputra P.N., Hamada T., Kumchai T., McGrath J.A.;
"Heterozygous mutation in the SAM domain of p63 underlies Rapp-Hodgkin
ectodermal dysplasia.";
J. Dent. Res. 82:433-437(2003).
[35]
VARIANT EDRH THR-549.
PubMed=15200513; DOI=10.1111/j.0009-9163.2004.00278.x;
Bertola D.R., Kim C.A., Albano L.M.J., Scheffer H., Meijer R.,
van Bokhoven H.;
"Molecular evidence that AEC syndrome and Rapp-Hodgkin syndrome are
variable expression of a single genetic disorder.";
Clin. Genet. 66:79-80(2004).
[36]
VARIANT EDRH/OFC8 GLY-352, AND VARIANTS LEU-129 AND HIS-603.
PubMed=16740912; DOI=10.1136/jmg.2005.036442;
Leoyklang P., Siriwan P., Shotelersuk V.;
"A mutation of the p63 gene in non-syndromic cleft lip.";
J. Med. Genet. 43:E28-E28(2006).
-!- FUNCTION: Acts as a sequence specific DNA binding transcriptional
activator or repressor. The isoforms contain a varying set of
transactivation and auto-regulating transactivation inhibiting
domains thus showing an isoform specific activity. Isoform 2
activates RIPK4 transcription. May be required in conjunction with
TP73/p73 for initiation of p53/TP53 dependent apoptosis in
response to genotoxic insults and the presence of activated
oncogenes. Involved in Notch signaling by probably inducing JAG1
and JAG2. Plays a role in the regulation of epithelial
morphogenesis. The ratio of DeltaN-type and TA*-type isoforms may
govern the maintenance of epithelial stem cell compartments and
regulate the initiation of epithelial stratification from the
undifferentiated embryonal ectoderm. Required for limb formation
from the apical ectodermal ridge. Activates transcription of the
p21 promoter. {ECO:0000269|PubMed:11641404,
ECO:0000269|PubMed:12374749, ECO:0000269|PubMed:12446779,
ECO:0000269|PubMed:12446784, ECO:0000269|PubMed:20123734,
ECO:0000269|PubMed:22197488, ECO:0000269|PubMed:9774969}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: Binds DNA as a homotetramer. Isoform composition of the
tetramer may determine transactivation activity. Isoforms Alpha
and Gamma interact with HIPK2. Interacts with SSRP1, leading to
stimulate coactivator activity. Isoform 1 and isoform 2 interact
with WWP1. Interacts with PDS5A. Isoform 5 (via activation domain)
interacts with NOC2L. {ECO:0000269|PubMed:10373484,
ECO:0000269|PubMed:11925430, ECO:0000269|PubMed:12374749,
ECO:0000269|PubMed:17846787, ECO:0000269|PubMed:18806757,
ECO:0000269|PubMed:20123734, ECO:0000269|PubMed:9662346}.
-!- INTERACTION:
Q8TDN4:CABLES1; NbExp=7; IntAct=EBI-2400586, EBI-604615;
P35637:FUS; NbExp=2; IntAct=EBI-2337775, EBI-400434;
P61978:HNRNPK; NbExp=2; IntAct=EBI-2337775, EBI-304185;
Q9UFN0:NIPSNAP3A; NbExp=2; IntAct=EBI-2337775, EBI-716291;
Q13526:PIN1; NbExp=4; IntAct=EBI-2337775, EBI-714158;
Q96KQ4:PPP1R13B; NbExp=2; IntAct=EBI-2337775, EBI-1105153;
Q05655:PRKCD; NbExp=2; IntAct=EBI-2337775, EBI-704279;
Q9UPW6:SATB2; NbExp=5; IntAct=EBI-6481107, EBI-8298169;
Q15796:SMAD2; NbExp=3; IntAct=EBI-2337775, EBI-1040141;
P04637:TP53; NbExp=5; IntAct=EBI-2337775, EBI-366083;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12446779,
ECO:0000269|PubMed:20123734}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=12;
Name=1; Synonyms=TA*-alpha, TAp63alpha, P51B;
IsoId=Q9H3D4-1; Sequence=Displayed;
Note=Produced by alternative promoter usage.;
Name=2; Synonyms=DeltaN-alpha, DeltaNp63 alpha, P51delNalpha;
IsoId=Q9H3D4-2; Sequence=VSP_012465;
Note=Produced by alternative promoter usage. Variant in
position: 6:N->H (in ADULT syndrome).;
Name=3; Synonyms=TA*-beta, TAp63beta;
IsoId=Q9H3D4-3; Sequence=VSP_012470;
Note=Produced by alternative splicing of isoform 1.;
Name=4; Synonyms=DeltaN-beta, DeltaNp63 beta, P51delNbeta;
IsoId=Q9H3D4-4; Sequence=VSP_012465, VSP_012470;
Note=Produced by alternative splicing of isoform 2. Variant in
position: 6:N->H (in ADULT syndrome).;
Name=5; Synonyms=TA*-gamma, TAp63gamma, P51A;
IsoId=Q9H3D4-5; Sequence=VSP_012468;
Note=Produced by alternative splicing of isoform 1.;
Name=6; Synonyms=DeltaN-gamma, DeltaNp63gamma, P51delNgamma;
IsoId=Q9H3D4-6; Sequence=VSP_012465, VSP_012468;
Note=Produced by alternative splicing of isoform 2. Variant in
position: 6:N->H (in ADULT syndrome).;
Name=7; Synonyms=TA*-delta, TAp63delta, P51delta;
IsoId=Q9H3D4-7; Sequence=VSP_012469;
Note=Produced by alternative splicing of isoform 1.;
Name=8; Synonyms=DeltaN-delta;
IsoId=Q9H3D4-8; Sequence=VSP_012465, VSP_012469;
Note=Produced by alternative splicing of isoform 2. No
experimental confirmation available. Variant in position: 6:N->H
(in ADULT syndrome).;
Name=9; Synonyms=TA*-epsilon;
IsoId=Q9H3D4-9; Sequence=VSP_012466;
Note=Produced by alternative splicing of isoform 1. No
experimental confirmation available.;
Name=10; Synonyms=DeltaN-epsilon, DeltaNp73L;
IsoId=Q9H3D4-10; Sequence=VSP_012465, VSP_012466;
Note=Produced by alternative splicing of isoform 2. Variant in
position: 6:N->H (in ADULT syndrome).;
Name=11; Synonyms=P63 delta;
IsoId=Q9H3D4-11; Sequence=VSP_012467;
Note=Produced by alternative splicing of isoform 1.;
Name=12;
IsoId=Q9H3D4-12; Sequence=VSP_012465, VSP_012467;
Note=Produced by alternative splicing of isoform 2. No
experimental confirmation available. Variant in position: 6:N->H
(in ADULT syndrome).;
-!- TISSUE SPECIFICITY: Widely expressed, notably in heart, kidney,
placenta, prostate, skeletal muscle, testis and thymus, although
the precise isoform varies according to tissue type. Progenitor
cell layers of skin, breast, eye and prostate express high levels
of DeltaN-type isoforms. Isoform 10 is predominantly expressed in
skin squamous cell carcinomas, but not in normal skin tissues.
{ECO:0000269|PubMed:11248048, ECO:0000269|PubMed:9774969}.
-!- DOMAIN: The transactivation inhibitory domain (TID) can interact
with, and inhibit the activity of the N-terminal transcriptional
activation domain of TA*-type isoforms.
{ECO:0000269|PubMed:12446779, ECO:0000269|PubMed:12446784}.
-!- PTM: May be sumoylated. {ECO:0000250}.
-!- PTM: Ubiquitinated. Polyubiquitination involves WWP1 and leads to
proteasomal degradation of this protein.
{ECO:0000269|PubMed:18806757}.
-!- DISEASE: Acro-dermato-ungual-lacrimal-tooth syndrome (ADULT
syndrome) [MIM:103285]: A form of ectodermal dysplasia. Ectodermal
dysplasia defines a heterogeneous group of disorders due to
abnormal development of two or more ectodermal structures. ADULT
syndrome involves ectrodactyly, syndactyly, finger- and toenail
dysplasia, hypoplastic breasts and nipples, intensive freckling,
lacrimal duct atresia, frontal alopecia, primary hypodontia and
loss of permanent teeth. ADULT syndrome differs significantly from
EEC3 syndrome by the absence of facial clefting.
{ECO:0000269|PubMed:11929852}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Ankyloblepharon-ectodermal defects-cleft lip/palate (AEC)
[MIM:106260]: An autosomal dominant condition characterized by
congenital ectodermal dysplasia with coarse, wiry, sparse hair,
dystrophic nails, slight hypohidrosis, scalp infections,
ankyloblepharon filiform adnatum, maxillary hypoplasia, hypodontia
and cleft lip/palate. {ECO:0000269|PubMed:11159940}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Ectrodactyly, ectodermal dysplasia, and cleft lip/palate
syndrome 3 (EEC3) [MIM:604292]: A form of ectodermal dysplasia, a
heterogeneous group of disorders due to abnormal development of
two or more ectodermal structures. It is an autosomal dominant
syndrome characterized by ectrodactyly of hands and feet,
ectodermal dysplasia and facial clefting.
{ECO:0000269|PubMed:10535733, ECO:0000269|PubMed:10839977,
ECO:0000269|PubMed:11462173, ECO:0000269|PubMed:12838557}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Split-hand/foot malformation 4 (SHFM4) [MIM:605289]: A
limb malformation involving the central rays of the autopod and
presenting with syndactyly, median clefts of the hands and feet,
and aplasia and/or hypoplasia of the phalanges, metacarpals, and
metatarsals. Some patients have been found to have mental
retardation, ectodermal and craniofacial findings, and orofacial
clefting. {ECO:0000269|PubMed:10839977,
ECO:0000269|PubMed:11462173}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Limb-mammary syndrome (LMS) [MIM:603543]: Characterized
by ectrodactyly, cleft palate and mammary-gland abnormalities.
{ECO:0000269|PubMed:11462173}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=Defects in TP63 are a cause of cervical, colon, head
and neck, lung and ovarian cancers.
-!- DISEASE: Ectodermal dysplasia, Rapp-Hodgkin type (EDRH)
[MIM:129400]: A form of ectodermal dysplasia, a heterogeneous
group of disorders due to abnormal development of two or more
ectodermal structures. Characterized by the combination of
anhidrotic ectodermal dysplasia, cleft lip, and cleft palate. The
clinical syndrome is comprised of a characteristic facies (narrow
nose and small mouth), wiry, slow-growing, and uncombable hair,
sparse eyelashes and eyebrows, obstructed lacrimal
puncta/epiphora, bilateral stenosis of external auditory canals,
microsomia, hypodontia, cone-shaped incisors, enamel hypoplasia,
dystrophic nails, and cleft lip/cleft palate.
{ECO:0000269|PubMed:12766194, ECO:0000269|PubMed:12939657,
ECO:0000269|PubMed:15200513, ECO:0000269|PubMed:16740912}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Non-syndromic orofacial cleft 8 (OFC8) [MIM:129400]: A
birth defect consisting of cleft lips with or without cleft
palate. Cleft lips are associated with cleft palate in two-third
of cases. A cleft lip can occur on one or both sides and range in
severity from a simple notch in the upper lip to a complete
opening in the lip extending into the floor of the nostril and
involving the upper gum. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the p53 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF43486.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAF43487.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAF43488.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAF43489.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAF61624.1; Type=Frameshift; Positions=26; Evidence={ECO:0000305};
Sequence=BAA32592.1; Type=Frameshift; Positions=26; Evidence={ECO:0000305};
Sequence=BAA32593.1; Type=Frameshift; Positions=26; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TP63ID365ch3q27.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB010153; BAA32433.1; -; mRNA.
EMBL; Y16961; CAA76562.1; -; mRNA.
EMBL; AF075428; AAC62633.1; -; mRNA.
EMBL; AF075429; AAC62634.1; -; mRNA.
EMBL; AF075430; AAC62635.1; -; mRNA.
EMBL; AF075431; AAC62636.1; -; mRNA.
EMBL; AF075432; AAC62637.1; -; mRNA.
EMBL; AF075433; AAC62638.1; -; mRNA.
EMBL; AF124539; AAG45607.1; -; Genomic_DNA.
EMBL; AF124528; AAG45607.1; JOINED; Genomic_DNA.
EMBL; AF124529; AAG45607.1; JOINED; Genomic_DNA.
EMBL; AF124531; AAG45607.1; JOINED; Genomic_DNA.
EMBL; AF124532; AAG45607.1; JOINED; Genomic_DNA.
EMBL; AF124533; AAG45607.1; JOINED; Genomic_DNA.
EMBL; AF124534; AAG45607.1; JOINED; Genomic_DNA.
EMBL; AF124535; AAG45607.1; JOINED; Genomic_DNA.
EMBL; AF124536; AAG45607.1; JOINED; Genomic_DNA.
EMBL; AF124537; AAG45607.1; JOINED; Genomic_DNA.
EMBL; AF124538; AAG45607.1; JOINED; Genomic_DNA.
EMBL; AF124539; AAG45608.1; -; Genomic_DNA.
EMBL; AF124528; AAG45608.1; JOINED; Genomic_DNA.
EMBL; AF124529; AAG45608.1; JOINED; Genomic_DNA.
EMBL; AF124531; AAG45608.1; JOINED; Genomic_DNA.
EMBL; AF124532; AAG45608.1; JOINED; Genomic_DNA.
EMBL; AF124533; AAG45608.1; JOINED; Genomic_DNA.
EMBL; AF124534; AAG45608.1; JOINED; Genomic_DNA.
EMBL; AF124535; AAG45608.1; JOINED; Genomic_DNA.
EMBL; AF124536; AAG45608.1; JOINED; Genomic_DNA.
EMBL; AF124537; AAG45608.1; JOINED; Genomic_DNA.
EMBL; AF124540; AAG45609.1; -; Genomic_DNA.
EMBL; AF124528; AAG45609.1; JOINED; Genomic_DNA.
EMBL; AF124529; AAG45609.1; JOINED; Genomic_DNA.
EMBL; AF124531; AAG45609.1; JOINED; Genomic_DNA.
EMBL; AF124532; AAG45609.1; JOINED; Genomic_DNA.
EMBL; AF124533; AAG45609.1; JOINED; Genomic_DNA.
EMBL; AF124534; AAG45609.1; JOINED; Genomic_DNA.
EMBL; AF124535; AAG45609.1; JOINED; Genomic_DNA.
EMBL; AF124539; AAG45610.1; -; Genomic_DNA.
EMBL; AF124530; AAG45610.1; JOINED; Genomic_DNA.
EMBL; AF124531; AAG45610.1; JOINED; Genomic_DNA.
EMBL; AF124532; AAG45610.1; JOINED; Genomic_DNA.
EMBL; AF124533; AAG45610.1; JOINED; Genomic_DNA.
EMBL; AF124534; AAG45610.1; JOINED; Genomic_DNA.
EMBL; AF124535; AAG45610.1; JOINED; Genomic_DNA.
EMBL; AF124536; AAG45610.1; JOINED; Genomic_DNA.
EMBL; AF124537; AAG45610.1; JOINED; Genomic_DNA.
EMBL; AF124538; AAG45610.1; JOINED; Genomic_DNA.
EMBL; AF124539; AAG45611.1; -; Genomic_DNA.
EMBL; AF124530; AAG45611.1; JOINED; Genomic_DNA.
EMBL; AF124531; AAG45611.1; JOINED; Genomic_DNA.
EMBL; AF124532; AAG45611.1; JOINED; Genomic_DNA.
EMBL; AF124533; AAG45611.1; JOINED; Genomic_DNA.
EMBL; AF124534; AAG45611.1; JOINED; Genomic_DNA.
EMBL; AF124535; AAG45611.1; JOINED; Genomic_DNA.
EMBL; AF124536; AAG45611.1; JOINED; Genomic_DNA.
EMBL; AF124537; AAG45611.1; JOINED; Genomic_DNA.
EMBL; AF124540; AAG45612.1; -; Genomic_DNA.
EMBL; AF124531; AAG45612.1; JOINED; Genomic_DNA.
EMBL; AF124533; AAG45612.1; JOINED; Genomic_DNA.
EMBL; AF124535; AAG45612.1; JOINED; Genomic_DNA.
EMBL; AF124534; AAG45612.1; JOINED; Genomic_DNA.
EMBL; AF124532; AAG45612.1; JOINED; Genomic_DNA.
EMBL; AF124530; AAG45612.1; JOINED; Genomic_DNA.
EMBL; AB016072; BAA32592.1; ALT_FRAME; mRNA.
EMBL; AB016073; BAA32593.1; ALT_FRAME; mRNA.
EMBL; AF091627; AAC43038.1; -; mRNA.
EMBL; AF116770; AAF43486.1; ALT_INIT; Genomic_DNA.
EMBL; AF116756; AAF43486.1; JOINED; Genomic_DNA.
EMBL; AF116757; AAF43486.1; JOINED; Genomic_DNA.
EMBL; AF116759; AAF43486.1; JOINED; Genomic_DNA.
EMBL; AF116760; AAF43486.1; JOINED; Genomic_DNA.
EMBL; AF116761; AAF43486.1; JOINED; Genomic_DNA.
EMBL; AF116762; AAF43486.1; JOINED; Genomic_DNA.
EMBL; AF116763; AAF43486.1; JOINED; Genomic_DNA.
EMBL; AF116764; AAF43486.1; JOINED; Genomic_DNA.
EMBL; AF116765; AAF43486.1; JOINED; Genomic_DNA.
EMBL; AF116769; AAF43487.1; ALT_INIT; Genomic_DNA.
EMBL; AF116756; AAF43487.1; JOINED; Genomic_DNA.
EMBL; AF116757; AAF43487.1; JOINED; Genomic_DNA.
EMBL; AF116759; AAF43487.1; JOINED; Genomic_DNA.
EMBL; AF116760; AAF43487.1; JOINED; Genomic_DNA.
EMBL; AF116761; AAF43487.1; JOINED; Genomic_DNA.
EMBL; AF116762; AAF43487.1; JOINED; Genomic_DNA.
EMBL; AF116763; AAF43487.1; JOINED; Genomic_DNA.
EMBL; AF116764; AAF43487.1; JOINED; Genomic_DNA.
EMBL; AF116765; AAF43487.1; JOINED; Genomic_DNA.
EMBL; AF116766; AAF43487.1; JOINED; Genomic_DNA.
EMBL; AF116767; AAF43487.1; JOINED; Genomic_DNA.
EMBL; AF116768; AAF43487.1; JOINED; Genomic_DNA.
EMBL; AF116769; AAF43488.1; ALT_INIT; Genomic_DNA.
EMBL; AF116756; AAF43488.1; JOINED; Genomic_DNA.
EMBL; AF116759; AAF43488.1; JOINED; Genomic_DNA.
EMBL; AF116757; AAF43488.1; JOINED; Genomic_DNA.
EMBL; AF116762; AAF43488.1; JOINED; Genomic_DNA.
EMBL; AF116764; AAF43488.1; JOINED; Genomic_DNA.
EMBL; AF116766; AAF43488.1; JOINED; Genomic_DNA.
EMBL; AF116767; AAF43488.1; JOINED; Genomic_DNA.
EMBL; AF116765; AAF43488.1; JOINED; Genomic_DNA.
EMBL; AF116763; AAF43488.1; JOINED; Genomic_DNA.
EMBL; AF116761; AAF43488.1; JOINED; Genomic_DNA.
EMBL; AF116760; AAF43488.1; JOINED; Genomic_DNA.
EMBL; AF116769; AAF43489.1; ALT_INIT; Genomic_DNA.
EMBL; AF116756; AAF43489.1; JOINED; Genomic_DNA.
EMBL; AF116757; AAF43489.1; JOINED; Genomic_DNA.
EMBL; AF116759; AAF43489.1; JOINED; Genomic_DNA.
EMBL; AF116760; AAF43489.1; JOINED; Genomic_DNA.
EMBL; AF116761; AAF43489.1; JOINED; Genomic_DNA.
EMBL; AF116762; AAF43489.1; JOINED; Genomic_DNA.
EMBL; AF116763; AAF43489.1; JOINED; Genomic_DNA.
EMBL; AF116764; AAF43489.1; JOINED; Genomic_DNA.
EMBL; AF116765; AAF43489.1; JOINED; Genomic_DNA.
EMBL; AF116766; AAF43489.1; JOINED; Genomic_DNA.
EMBL; AF116770; AAF43490.1; -; Genomic_DNA.
EMBL; AF116758; AAF43490.1; JOINED; Genomic_DNA.
EMBL; AF116760; AAF43490.1; JOINED; Genomic_DNA.
EMBL; AF116762; AAF43490.1; JOINED; Genomic_DNA.
EMBL; AF116764; AAF43490.1; JOINED; Genomic_DNA.
EMBL; AF116765; AAF43490.1; JOINED; Genomic_DNA.
EMBL; AF116763; AAF43490.1; JOINED; Genomic_DNA.
EMBL; AF116761; AAF43490.1; JOINED; Genomic_DNA.
EMBL; AF116759; AAF43490.1; JOINED; Genomic_DNA.
EMBL; AF116769; AAF43491.1; -; Genomic_DNA.
EMBL; AF116758; AAF43491.1; JOINED; Genomic_DNA.
EMBL; AF116759; AAF43491.1; JOINED; Genomic_DNA.
EMBL; AF116760; AAF43491.1; JOINED; Genomic_DNA.
EMBL; AF116764; AAF43491.1; JOINED; Genomic_DNA.
EMBL; AF116766; AAF43491.1; JOINED; Genomic_DNA.
EMBL; AF116768; AAF43491.1; JOINED; Genomic_DNA.
EMBL; AF116767; AAF43491.1; JOINED; Genomic_DNA.
EMBL; AF116765; AAF43491.1; JOINED; Genomic_DNA.
EMBL; AF116763; AAF43491.1; JOINED; Genomic_DNA.
EMBL; AF116762; AAF43491.1; JOINED; Genomic_DNA.
EMBL; AF116761; AAF43491.1; JOINED; Genomic_DNA.
EMBL; AF116769; AAF43492.1; -; Genomic_DNA.
EMBL; AF116758; AAF43492.1; JOINED; Genomic_DNA.
EMBL; AF116760; AAF43492.1; JOINED; Genomic_DNA.
EMBL; AF116759; AAF43492.1; JOINED; Genomic_DNA.
EMBL; AF116761; AAF43492.1; JOINED; Genomic_DNA.
EMBL; AF116763; AAF43492.1; JOINED; Genomic_DNA.
EMBL; AF116765; AAF43492.1; JOINED; Genomic_DNA.
EMBL; AF116767; AAF43492.1; JOINED; Genomic_DNA.
EMBL; AF116766; AAF43492.1; JOINED; Genomic_DNA.
EMBL; AF116764; AAF43492.1; JOINED; Genomic_DNA.
EMBL; AF116762; AAF43492.1; JOINED; Genomic_DNA.
EMBL; AF116769; AAF43493.1; -; Genomic_DNA.
EMBL; AF116758; AAF43493.1; JOINED; Genomic_DNA.
EMBL; AF116760; AAF43493.1; JOINED; Genomic_DNA.
EMBL; AF116759; AAF43493.1; JOINED; Genomic_DNA.
EMBL; AF116761; AAF43493.1; JOINED; Genomic_DNA.
EMBL; AF116763; AAF43493.1; JOINED; Genomic_DNA.
EMBL; AF116765; AAF43493.1; JOINED; Genomic_DNA.
EMBL; AF116766; AAF43493.1; JOINED; Genomic_DNA.
EMBL; AF116764; AAF43493.1; JOINED; Genomic_DNA.
EMBL; AF116762; AAF43493.1; JOINED; Genomic_DNA.
EMBL; AF116771; AAF61624.1; ALT_FRAME; mRNA.
EMBL; AB042841; BAB20591.1; -; mRNA.
EMBL; BC039815; AAH39815.1; -; mRNA.
EMBL; AF061512; AAC24830.1; -; mRNA.
EMBL; AY342152; AAQ63448.1; -; Genomic_DNA.
EMBL; AY341145; AAQ63448.1; JOINED; Genomic_DNA.
EMBL; AY339663; AAQ63449.1; -; Genomic_DNA.
EMBL; AY341143; AAQ63450.1; -; Genomic_DNA.
EMBL; AY339664; AAQ63450.1; JOINED; Genomic_DNA.
EMBL; AY341142; AAQ63450.1; JOINED; Genomic_DNA.
EMBL; AY341143; AAQ63451.1; -; Genomic_DNA.
EMBL; AY341142; AAQ63451.1; JOINED; Genomic_DNA.
EMBL; AY341144; AAQ63452.1; -; Genomic_DNA.
EMBL; AY342153; AAQ63453.1; -; Genomic_DNA.
EMBL; AY342154; AAQ63454.1; -; Genomic_DNA.
EMBL; AJ315499; CAC48053.1; -; mRNA.
CCDS; CCDS3293.1; -. [Q9H3D4-1]
CCDS; CCDS46976.1; -. [Q9H3D4-3]
CCDS; CCDS46977.1; -. [Q9H3D4-5]
CCDS; CCDS46978.1; -. [Q9H3D4-2]
CCDS; CCDS46979.1; -. [Q9H3D4-4]
CCDS; CCDS46980.1; -. [Q9H3D4-6]
CCDS; CCDS82887.1; -. [Q9H3D4-11]
RefSeq; NP_001108450.1; NM_001114978.1. [Q9H3D4-3]
RefSeq; NP_001108451.1; NM_001114979.1. [Q9H3D4-5]
RefSeq; NP_001108452.1; NM_001114980.1. [Q9H3D4-2]
RefSeq; NP_001108453.1; NM_001114981.1. [Q9H3D4-4]
RefSeq; NP_001108454.1; NM_001114982.1. [Q9H3D4-6]
RefSeq; NP_001316073.1; NM_001329144.1. [Q9H3D4-7]
RefSeq; NP_001316074.1; NM_001329145.1. [Q9H3D4-8]
RefSeq; NP_001316075.1; NM_001329146.1. [Q9H3D4-10]
RefSeq; NP_001316077.1; NM_001329148.1. [Q9H3D4-11]
RefSeq; NP_003713.3; NM_003722.4. [Q9H3D4-1]
RefSeq; XP_016862876.1; XM_017007387.1. [Q9H3D4-12]
UniGene; Hs.137569; -.
PDB; 1RG6; NMR; -; A=540-614.
PDB; 2NB1; NMR; -; A/C=397-455.
PDB; 2RMN; NMR; -; A=153-388.
PDB; 2Y9T; NMR; -; A=543-622.
PDB; 2Y9U; X-ray; 1.60 A; A=545-611.
PDB; 3QYM; X-ray; 3.20 A; A/B/C/D/E/F/G/H=166-362.
PDB; 3QYN; X-ray; 2.50 A; A/B/C/D=166-362.
PDB; 3US0; X-ray; 2.50 A; A/B/C/D=166-362.
PDB; 3US1; X-ray; 2.80 A; A/D=166-362.
PDB; 3US2; X-ray; 4.20 A; A/B/C/D/G/H/I/J=166-362.
PDB; 3ZY0; X-ray; 1.90 A; A/B/C/D=398-427.
PDB; 3ZY1; X-ray; 2.15 A; A=398-441.
PDB; 4A9Z; X-ray; 2.29 A; A/B/C/D=397-455.
PDBsum; 1RG6; -.
PDBsum; 2NB1; -.
PDBsum; 2RMN; -.
PDBsum; 2Y9T; -.
PDBsum; 2Y9U; -.
PDBsum; 3QYM; -.
PDBsum; 3QYN; -.
PDBsum; 3US0; -.
PDBsum; 3US1; -.
PDBsum; 3US2; -.
PDBsum; 3ZY0; -.
PDBsum; 3ZY1; -.
PDBsum; 4A9Z; -.
ProteinModelPortal; Q9H3D4; -.
SMR; Q9H3D4; -.
BioGrid; 114181; 127.
DIP; DIP-29588N; -.
ELM; Q9H3D4; -.
IntAct; Q9H3D4; 71.
MINT; MINT-190238; -.
STRING; 9606.ENSP00000264731; -.
iPTMnet; Q9H3D4; -.
PhosphoSitePlus; Q9H3D4; -.
BioMuta; TP63; -.
DMDM; 57013009; -.
MaxQB; Q9H3D4; -.
PaxDb; Q9H3D4; -.
PeptideAtlas; Q9H3D4; -.
PRIDE; Q9H3D4; -.
DNASU; 8626; -.
Ensembl; ENST00000264731; ENSP00000264731; ENSG00000073282. [Q9H3D4-1]
Ensembl; ENST00000320472; ENSP00000317510; ENSG00000073282. [Q9H3D4-7]
Ensembl; ENST00000354600; ENSP00000346614; ENSG00000073282. [Q9H3D4-2]
Ensembl; ENST00000392460; ENSP00000376253; ENSG00000073282. [Q9H3D4-3]
Ensembl; ENST00000392461; ENSP00000376254; ENSG00000073282. [Q9H3D4-8]
Ensembl; ENST00000392463; ENSP00000376256; ENSG00000073282. [Q9H3D4-4]
Ensembl; ENST00000418709; ENSP00000407144; ENSG00000073282. [Q9H3D4-5]
Ensembl; ENST00000437221; ENSP00000392488; ENSG00000073282. [Q9H3D4-6]
Ensembl; ENST00000440651; ENSP00000394337; ENSG00000073282. [Q9H3D4-11]
Ensembl; ENST00000449992; ENSP00000387839; ENSG00000073282. [Q9H3D4-10]
Ensembl; ENST00000456148; ENSP00000389485; ENSG00000073282. [Q9H3D4-12]
GeneID; 8626; -.
KEGG; hsa:8626; -.
UCSC; uc003frx.3; human. [Q9H3D4-1]
CTD; 8626; -.
DisGeNET; 8626; -.
EuPathDB; HostDB:ENSG00000073282.12; -.
GeneCards; TP63; -.
GeneReviews; TP63; -.
HGNC; HGNC:15979; TP63.
HPA; CAB000083; -.
HPA; HPA006288; -.
HPA; HPA007010; -.
MalaCards; TP63; -.
MIM; 103285; phenotype.
MIM; 106260; phenotype.
MIM; 129400; phenotype.
MIM; 603273; gene.
MIM; 603543; phenotype.
MIM; 604292; phenotype.
MIM; 605289; phenotype.
neXtProt; NX_Q9H3D4; -.
OpenTargets; ENSG00000073282; -.
Orphanet; 978; ADULT syndrome.
Orphanet; 1071; Ankyloblepharon - ectodermal defects - cleft lip/palate.
Orphanet; 93930; Bladder exstrophy.
Orphanet; 1991; Cleft lip with or without cleft palate.
Orphanet; 1896; EEC syndrome.
Orphanet; 69085; Limb-mammary syndrome.
Orphanet; 2440; Split hand-split foot malformation.
PharmGKB; PA162406776; -.
eggNOG; ENOG410IGE4; Eukaryota.
eggNOG; ENOG410XV9W; LUCA.
GeneTree; ENSGT00390000015092; -.
HOVERGEN; HBG005201; -.
InParanoid; Q9H3D4; -.
KO; K10149; -.
OMA; YQIENYN; -.
OrthoDB; EOG091G0XY5; -.
PhylomeDB; Q9H3D4; -.
TreeFam; TF106101; -.
Reactome; R-HSA-139915; Activation of PUMA and translocation to mitochondria.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
Reactome; R-HSA-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
Reactome; R-HSA-6803207; TP53 Regulates Transcription of Caspase Activators and Caspases.
Reactome; R-HSA-6803211; TP53 Regulates Transcription of Death Receptors and Ligands.
Reactome; R-HSA-6804759; Regulation of TP53 Activity through Association with Co-factors.
SignaLink; Q9H3D4; -.
SIGNOR; Q9H3D4; -.
ChiTaRS; TP63; human.
EvolutionaryTrace; Q9H3D4; -.
GeneWiki; TP63; -.
GenomeRNAi; 8626; -.
PRO; PR:Q9H3D4; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000073282; -.
ExpressionAtlas; Q9H3D4; baseline and differential.
Genevisible; Q9H3D4; HS.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl.
GO; GO:0005667; C:transcription factor complex; IBA:GO_Central.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
GO; GO:0097371; F:MDM2/MDM4 family protein binding; IPI:CAFA.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0002039; F:p53 binding; IPI:CAFA.
GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IMP:CAFA.
GO; GO:0000989; F:transcription factor activity, transcription factor binding; IEA:Ensembl.
GO; GO:0044212; F:transcription regulatory region DNA binding; IEA:InterPro.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl.
GO; GO:0050699; F:WW domain binding; IPI:UniProtKB.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0034644; P:cellular response to UV; IBA:GO_Central.
GO; GO:0006338; P:chromatin remodeling; IEA:Ensembl.
GO; GO:0060197; P:cloacal septation; IEA:Ensembl.
GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IBA:GO_Central.
GO; GO:0007499; P:ectoderm and mesoderm interaction; IEA:Ensembl.
GO; GO:0030326; P:embryonic limb morphogenesis; IEA:Ensembl.
GO; GO:0010481; P:epidermal cell division; IEA:Ensembl.
GO; GO:0002064; P:epithelial cell development; IEA:Ensembl.
GO; GO:0001736; P:establishment of planar polarity; IEA:Ensembl.
GO; GO:0061436; P:establishment of skin barrier; ISS:UniProtKB.
GO; GO:0048807; P:female genitalia morphogenesis; IEA:Ensembl.
GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IBA:GO_Central.
GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
GO; GO:0043616; P:keratinocyte proliferation; IEA:Ensembl.
GO; GO:0031571; P:mitotic G1 DNA damage checkpoint; IBA:GO_Central.
GO; GO:0010259; P:multicellular organism aging; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
GO; GO:2000773; P:negative regulation of cellular senescence; IMP:UniProtKB.
GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; IEA:Ensembl.
GO; GO:0045617; P:negative regulation of keratinocyte differentiation; IEA:Ensembl.
GO; GO:2000381; P:negative regulation of mesoderm development; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0030859; P:polarized epithelial cell differentiation; IEA:Ensembl.
GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; IMP:UniProtKB.
GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; IDA:UniProtKB.
GO; GO:0010838; P:positive regulation of keratinocyte proliferation; IEA:Ensembl.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:UniProtKB.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL.
GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:1904674; P:positive regulation of somatic stem cell population maintenance; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0036342; P:post-anal tail morphogenesis; IEA:Ensembl.
GO; GO:0060513; P:prostatic bud formation; IEA:Ensembl.
GO; GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
GO; GO:0009954; P:proximal/distal pattern formation; IEA:Ensembl.
GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0010482; P:regulation of epidermal cell division; ISS:UniProtKB.
GO; GO:0043523; P:regulation of neuron apoptotic process; IBA:GO_Central.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0001302; P:replicative cell aging; IEA:Ensembl.
GO; GO:0010332; P:response to gamma radiation; IBA:GO_Central.
GO; GO:0010165; P:response to X-ray; IBA:GO_Central.
GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
GO; GO:0043589; P:skin morphogenesis; IEA:Ensembl.
GO; GO:0048745; P:smooth muscle tissue development; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0060529; P:squamous basal epithelial stem cell differentiation involved in prostate gland acinus development; IEA:Ensembl.
GO; GO:0048485; P:sympathetic nervous system development; IEA:Ensembl.
GO; GO:0060157; P:urinary bladder development; IEA:Ensembl.
CDD; cd08367; P53; 1.
Gene3D; 2.60.40.720; -; 1.
Gene3D; 4.10.170.10; -; 1.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd.
InterPro; IPR011615; p53_DNA-bd.
InterPro; IPR010991; p53_tetrameristn.
InterPro; IPR002117; p53_tumour_suppressor.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed.
InterPro; IPR032645; Tp63.
PANTHER; PTHR11447; PTHR11447; 1.
PANTHER; PTHR11447:SF24; PTHR11447:SF24; 1.
Pfam; PF00870; P53; 1.
Pfam; PF07710; P53_tetramer; 1.
Pfam; PF07647; SAM_2; 1.
PRINTS; PR00386; P53SUPPRESSR.
SMART; SM00454; SAM; 1.
SUPFAM; SSF47719; SSF47719; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF49417; SSF49417; 1.
PROSITE; PS00348; P53; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative promoter usage;
Alternative splicing; Apoptosis; Complete proteome;
Developmental protein; Disease mutation; DNA-binding;
Ectodermal dysplasia; Isopeptide bond; Metal-binding;
Notch signaling pathway; Nucleus; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Zinc.
CHAIN 1 680 Tumor protein 63.
/FTId=PRO_0000185729.
DOMAIN 541 607 SAM.
DNA_BIND 170 362
REGION 1 107 Transcription activation.
REGION 352 388 Interaction with HIPK2.
{ECO:0000269|PubMed:11925430}.
REGION 394 443 Oligomerization.
REGION 610 680 Transactivation inhibition.
COMPBIAS 437 444 Poly-Gln.
METAL 244 244 Zinc. {ECO:0000250}.
METAL 247 247 Zinc. {ECO:0000250}.
METAL 308 308 Zinc. {ECO:0000250}.
METAL 312 312 Zinc. {ECO:0000250}.
CROSSLNK 676 676 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
VAR_SEQ 1 108 MNFETSRCATLQYCPDPYIQRFVETPAHFSWKESYYRSTMS
QSTQTNEFLSPEVFQHIWDFLEQPICSVQPIDLNFVDEPSE
DGATNKIEISMDCIRMQDSDLSDPMW -> MLYLENNAQTQ
FSE (in isoform 2, isoform 4, isoform 6,
isoform 8, isoform 10 and isoform 12).
{ECO:0000303|PubMed:10469295,
ECO:0000303|PubMed:11336476,
ECO:0000303|PubMed:9703973,
ECO:0000303|PubMed:9774969}.
/FTId=VSP_012465.
VAR_SEQ 109 193 Missing (in isoform 9 and isoform 10).
{ECO:0000303|PubMed:11336476}.
/FTId=VSP_012466.
VAR_SEQ 373 377 GTKRP -> A (in isoform 11 and isoform
12). {ECO:0000303|PubMed:11477076}.
/FTId=VSP_012467.
VAR_SEQ 450 680 QTSIQSPSSYGNSSPPLNKMNSMNKLPSVSQLINPQQRNAL
TPTTIPDGMGANIPMMGTHMPMAGDMNGLSPTQALPPPLSM
PSTSHCTPPPPYPTDCSIVSFLARLGCSSCLDYFTTQGLTT
IYQIEHYSMDDLASLKIPEQFRHAIWKGILDHRQLHEFSSP
SHLLRTPSSASTVSVGSSETRGERVIDAVRFTLRQTISFPP
RDEWNDFNFDMDARRNKQQRIKEEGE -> HLLSACFRNEL
VEPRRETPKQSDVFFRHSKPPNRSVYP (in isoform 5
and isoform 6).
{ECO:0000303|PubMed:9662378,
ECO:0000303|PubMed:9774969}.
/FTId=VSP_012468.
VAR_SEQ 503 680 IPMMGTHMPMAGDMNGLSPTQALPPPLSMPSTSHCTPPPPY
PTDCSIVSFLARLGCSSCLDYFTTQGLTTIYQIEHYSMDDL
ASLKIPEQFRHAIWKGILDHRQLHEFSSPSHLLRTPSSAST
VSVGSSETRGERVIDAVRFTLRQTISFPPRDEWNDFNFDMD
ARRNKQQRIKEEGE -> RSGKSENP (in isoform 7
and isoform 8).
{ECO:0000303|PubMed:10935472}.
/FTId=VSP_012469.
VAR_SEQ 551 680 SFLARLGCSSCLDYFTTQGLTTIYQIEHYSMDDLASLKIPE
QFRHAIWKGILDHRQLHEFSSPSHLLRTPSSASTVSVGSSE
TRGERVIDAVRFTLRQTISFPPRDEWNDFNFDMDARRNKQQ
RIKEEGE -> RIWQV (in isoform 3 and
isoform 4). {ECO:0000303|PubMed:9774969}.
/FTId=VSP_012470.
VARIANT 129 129 S -> L (in dbSNP:rs193287780).
{ECO:0000269|PubMed:16740912}.
/FTId=VAR_035126.
VARIANT 184 184 S -> L (in head and neck cancer).
{ECO:0000269|PubMed:9662378}.
/FTId=VAR_020866.
VARIANT 187 187 A -> P (in lung carcinoma; somatic
mutation). {ECO:0000269|PubMed:9662378}.
/FTId=VAR_020867.
VARIANT 193 193 T -> TP (in SHFM4).
{ECO:0000269|PubMed:11462173}.
/FTId=VAR_032736.
VARIANT 204 204 Q -> L (in cervical cancer).
{ECO:0000269|PubMed:9662378}.
/FTId=VAR_020868.
VARIANT 232 232 K -> E (in SHFM4).
{ECO:0000269|PubMed:11462173}.
/FTId=VAR_032737.
VARIANT 233 233 K -> E (in SHFM4; dbSNP:rs121908838).
{ECO:0000269|PubMed:10839977}.
/FTId=VAR_020869.
VARIANT 243 243 R -> Q (in EEC3; dbSNP:rs121908836).
{ECO:0000269|PubMed:10535733,
ECO:0000269|PubMed:11462173}.
/FTId=VAR_020870.
VARIANT 243 243 R -> W (in EEC3; dbSNP:rs121908835).
{ECO:0000269|PubMed:10535733,
ECO:0000269|PubMed:11462173}.
/FTId=VAR_020871.
VARIANT 266 266 R -> Q (in EEC3; dbSNP:rs121908849).
{ECO:0000269|PubMed:11462173}.
/FTId=VAR_032738.
VARIANT 279 279 P -> H (in colon cancer).
{ECO:0000269|PubMed:10485447}.
/FTId=VAR_020872.
VARIANT 308 308 C -> Y (in EEC3).
{ECO:0000269|PubMed:11462173}.
/FTId=VAR_032739.
VARIANT 311 311 S -> N (in EEC3).
{ECO:0000269|PubMed:11462173}.
/FTId=VAR_032740.
VARIANT 318 318 R -> C (in EEC3).
{ECO:0000269|PubMed:11462173}.
/FTId=VAR_032741.
VARIANT 318 318 R -> H (in EEC3 and EDRH; does not
decrease the transcriptional activity of
the isoform 5 on a TP53 reporter system
but disrupts the dominant-negative
activity of isoform 2 and isoform 5 on
the transcriptional activity of TP53;
dbSNP:rs121908840).
{ECO:0000269|PubMed:10839977,
ECO:0000269|PubMed:11462173,
ECO:0000269|PubMed:12939657}.
/FTId=VAR_020873.
VARIANT 318 318 R -> Q (in EEC3).
{ECO:0000269|PubMed:11462173}.
/FTId=VAR_032742.
VARIANT 319 319 R -> C (in EEC3; dbSNP:rs121908839).
{ECO:0000269|PubMed:10839977,
ECO:0000269|PubMed:11462173}.
/FTId=VAR_020874.
VARIANT 319 319 R -> H (in EEC3 and SHFM4).
{ECO:0000269|PubMed:11462173}.
/FTId=VAR_032743.
VARIANT 319 319 R -> S (in EEC3).
{ECO:0000269|PubMed:11462173}.
/FTId=VAR_032744.
VARIANT 337 337 R -> Q (in ADULT syndrome; confers novel
transcription activation capacity on
isoform 6; dbSNP:rs113993967).
{ECO:0000269|PubMed:11929852}.
/FTId=VAR_020875.
VARIANT 343 343 R -> Q (in EEC3; dbSNP:rs121908841).
{ECO:0000269|PubMed:10839977,
ECO:0000269|PubMed:11462173}.
/FTId=VAR_020876.
VARIANT 343 343 R -> W (in EEC3).
{ECO:0000269|PubMed:11462173}.
/FTId=VAR_032745.
VARIANT 345 345 C -> R (in EEC3; abolishes transcription
activation; dbSNP:rs121908837).
{ECO:0000269|PubMed:10535733,
ECO:0000269|PubMed:11462173}.
/FTId=VAR_020877.
VARIANT 347 347 C -> S (in EEC3).
{ECO:0000269|PubMed:11462173}.
/FTId=VAR_032746.
VARIANT 348 348 P -> S (in EEC3).
{ECO:0000269|PubMed:11462173}.
/FTId=VAR_032747.
VARIANT 351 351 D -> G (in EEC3; dbSNP:rs121908844).
{ECO:0000269|PubMed:12838557}.
/FTId=VAR_020878.
VARIANT 351 351 D -> H (in EEC3).
{ECO:0000269|PubMed:11462173}.
/FTId=VAR_032748.
VARIANT 352 352 R -> G (in EDRH and OFC8;
dbSNP:rs121908847).
{ECO:0000269|PubMed:16740912}.
/FTId=VAR_035127.
VARIANT 549 549 I -> T (in EDRH; dbSNP:rs121908845).
{ECO:0000269|PubMed:15200513}.
/FTId=VAR_035128.
VARIANT 553 553 L -> F (in AEC; dbSNP:rs121908842).
{ECO:0000269|PubMed:11159940}.
/FTId=VAR_020879.
VARIANT 560 560 S -> A (in ovarian cancer).
{ECO:0000269|PubMed:10485447}.
/FTId=VAR_020880.
VARIANT 561 561 C -> G (in AEC; dbSNP:rs121908843).
{ECO:0000269|PubMed:11159940}.
/FTId=VAR_020881.
VARIANT 580 580 S -> P (in EDRH; dbSNP:rs121908846).
{ECO:0000269|PubMed:12766194}.
/FTId=VAR_035129.
VARIANT 603 603 D -> H (in dbSNP:rs767906723).
{ECO:0000269|PubMed:16740912}.
/FTId=VAR_035130.
MUTAGEN 55 55 F->A: Abrogates transcriptional activity
and interaction with transactivation
inhibition domain; when associated with
A-59 and A-62.
{ECO:0000269|PubMed:12446779}.
MUTAGEN 59 59 W->A: Abrogates transcriptional activity
and interaction with transactivation
inhibition domain; when associated with
A-55 and A-62.
{ECO:0000269|PubMed:12446779}.
MUTAGEN 62 62 L->A: Abrogates transcriptional activity
and interaction with transactivation
inhibition domain; when associated with
A-55 and A-59.
{ECO:0000269|PubMed:12446779}.
MUTAGEN 543 543 Y->F: Abolishes ubiquitination.
{ECO:0000269|PubMed:18806757}.
CONFLICT 125 125 Q -> R (in Ref. 1; BAA32433).
{ECO:0000305}.
CONFLICT 154 154 S -> P (in Ref. 1; BAA32433).
{ECO:0000305}.
CONFLICT 177 177 F -> S (in Ref. 1; BAA32433).
{ECO:0000305}.
CONFLICT 378 378 F -> S (in Ref. 10; AAC24830).
{ECO:0000305}.
CONFLICT 536 536 H -> Q (in Ref. 2; CAA76562).
{ECO:0000305}.
CONFLICT 551 551 S -> G (in Ref. 4; BAA32593 and 7;
AAF43487/AAF43491). {ECO:0000305}.
STRAND 156 161 {ECO:0000244|PDB:2RMN}.
HELIX 173 175 {ECO:0000244|PDB:3QYN}.
STRAND 178 180 {ECO:0000244|PDB:3QYN}.
STRAND 187 189 {ECO:0000244|PDB:3QYN}.
STRAND 191 195 {ECO:0000244|PDB:3QYN}.
TURN 196 199 {ECO:0000244|PDB:3QYN}.
STRAND 200 203 {ECO:0000244|PDB:3QYN}.
STRAND 209 214 {ECO:0000244|PDB:3QYN}.
STRAND 224 233 {ECO:0000244|PDB:3QYN}.
TURN 234 238 {ECO:0000244|PDB:3QYN}.
HELIX 245 249 {ECO:0000244|PDB:3QYN}.
TURN 252 256 {ECO:0000244|PDB:3QYN}.
STRAND 263 269 {ECO:0000244|PDB:3QYN}.
STRAND 274 277 {ECO:0000244|PDB:3QYN}.
TURN 279 281 {ECO:0000244|PDB:3QYN}.
STRAND 284 289 {ECO:0000244|PDB:3QYN}.
STRAND 300 306 {ECO:0000244|PDB:3QYN}.
TURN 313 318 {ECO:0000244|PDB:3QYN}.
STRAND 321 328 {ECO:0000244|PDB:3QYN}.
STRAND 330 332 {ECO:0000244|PDB:3QYM}.
STRAND 334 343 {ECO:0000244|PDB:3QYN}.
HELIX 348 355 {ECO:0000244|PDB:3QYN}.
STRAND 369 372 {ECO:0000244|PDB:2RMN}.
STRAND 401 407 {ECO:0000244|PDB:3ZY0}.
HELIX 408 426 {ECO:0000244|PDB:3ZY0}.
HELIX 429 436 {ECO:0000244|PDB:3ZY1}.
HELIX 444 449 {ECO:0000244|PDB:4A9Z}.
STRAND 546 548 {ECO:0000244|PDB:2Y9T}.
HELIX 549 554 {ECO:0000244|PDB:2Y9U}.
TURN 555 557 {ECO:0000244|PDB:2Y9U}.
HELIX 559 561 {ECO:0000244|PDB:2Y9U}.
HELIX 562 566 {ECO:0000244|PDB:2Y9U}.
TURN 567 569 {ECO:0000244|PDB:2Y9U}.
HELIX 573 576 {ECO:0000244|PDB:2Y9U}.
HELIX 581 586 {ECO:0000244|PDB:2Y9U}.
HELIX 591 609 {ECO:0000244|PDB:2Y9U}.
STRAND 613 615 {ECO:0000244|PDB:2Y9T}.
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


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U0651Rb CLIA Hyaluronate-binding protein PS4,Oryctolagus cuniculus,PS4,Rabbit,TNF alpha-induced protein 6,TNFAIP6,TNF-stimulated gene 6 protein,TSG6,TSG-6,Tumor necrosis factor alpha-induced protein 6,Tumor n 96T
E0651Rb ELISA Hyaluronate-binding protein PS4,Oryctolagus cuniculus,PS4,Rabbit,TNF alpha-induced protein 6,TNFAIP6,TNF-stimulated gene 6 protein,TSG6,TSG-6,Tumor necrosis factor alpha-induced protein 6,Tumor 96T
E0277m ELISA Mouse,Mus musculus,Pentaxin-related protein PTX3,Pentraxin-related protein PTX3,Ptx3,Tsg14,TSG-14,Tumor necrosis factor-inducible gene 14 protein 96T
E0277m ELISA kit Mouse,Mus musculus,Pentaxin-related protein PTX3,Pentraxin-related protein PTX3,Ptx3,Tsg14,TSG-14,Tumor necrosis factor-inducible gene 14 protein 96T


 

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