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Tumor protein 63 (p63) (Transformation-related protein 63) (TP63) (Tumor protein p73-like) (p73L)

 P63_MOUSE               Reviewed;         680 AA.
O88898; O88897; O88899; O89097; Q8C826; Q9QWY9; Q9QWZ0;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
22-NOV-2017, entry version 164.
RecName: Full=Tumor protein 63;
Short=p63;
AltName: Full=Transformation-related protein 63;
Short=TP63;
AltName: Full=Tumor protein p73-like;
Short=p73L;
Name=Tp63; Synonyms=P63, P73l, Tp73l, Trp63;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), 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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Thymus;
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Kui J.S., Wang J.H., Zhang M.Q., Mills A.A.;
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-376 (ISOFORMS 2 AND 4).
STRAIN=C57BL/6J; TISSUE=Head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
FUNCTION IN EPITHELIAL MORPHOGENESIS.
PubMed=10227293; DOI=10.1038/19531;
Mills A.A., Zheng B., Wang X.-J., Vogel H., Roop D.R., Bradley A.;
"p63 is a p53 homologue required for limb and epidermal
morphogenesis.";
Nature 398:708-713(1999).
[6]
FUNCTION IN EPITHELIAL MORPHOGENESIS.
PubMed=10227294; DOI=10.1038/19539;
Yang A., Schweitzer R., Sun D., Kaghad M., Walker N., Bronson R.T.,
Tabin C., Sharpe A., Caput D., Crum C., McKeon F.;
"p63 is essential for regenerative proliferation in limb, craniofacial
and epithelial development.";
Nature 398:714-718(1999).
[7]
FUNCTION IN TP53 DEPENDENT APOPTOSIS, AND INDUCTION.
PubMed=11932750; DOI=10.1038/416560a;
Flores E.R., Tsai K.Y., Crowley D., Sengupta S., Yang A., McKeon F.,
Jacks T.;
"p63 and p73 are required for p53-dependent apoptosis in response to
DNA damage.";
Nature 416:560-564(2002).
[8]
FUNCTION IN EPITHELIAL MORPHOGENESIS, SUBCELLULAR LOCATION, AND
DEVELOPMENTAL STAGE.
PubMed=14729569; DOI=10.1101/gad.1165104;
Koster M.I., Kim S., Mills A.A., DeMayo F.J., Roop D.R.;
"p63 is the molecular switch for initiation of an epithelial
stratification program.";
Genes Dev. 18:126-131(2004).
[9]
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).
[10]
FUNCTION IN RIPK4 TRANSACTIVATION.
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).
-!- 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. 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. Activates transcription of the p21
promoter (By similarity). Activates RIPK4 transcription. 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. {ECO:0000250, ECO:0000269|PubMed:10227293,
ECO:0000269|PubMed:10227294, ECO:0000269|PubMed:11932750,
ECO:0000269|PubMed:14729569, ECO:0000269|PubMed:22197488}.
-!- 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. Interacts with
HIPK2. Interacts with SSRP1, leading to stimulate coactivator
activity. Interacts with PDS5A. Interacts (via activation domain)
with NOC2L (By similarity). Interacts with WWP1. {ECO:0000250,
ECO:0000269|PubMed:18806757}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-2338025, EBI-2338025;
Q9ESJ1:Cables1; NbExp=2; IntAct=EBI-2338025, EBI-604411;
Q92831:KAT2B (xeno); NbExp=3; IntAct=EBI-2338228, EBI-477430;
P15559:NQO1 (xeno); NbExp=2; IntAct=EBI-2338228, EBI-3989435;
P04637:TP53 (xeno); NbExp=2; IntAct=EBI-2338025, EBI-366083;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14729569}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=6;
Name=1; Synonyms=TA*-alpha, TA*p63alpha;
IsoId=O88898-1; Sequence=Displayed;
Note=Produced by alternative promoter usage.;
Name=2; Synonyms=DeltaN-alpha;
IsoId=O88898-2; Sequence=VSP_012471;
Note=Produced by alternative promoter usage.;
Name=3; Synonyms=TA*-beta, TA*p63beta;
IsoId=O88898-3; Sequence=VSP_012474;
Note=Produced by alternative splicing of isoform 1.;
Name=4; Synonyms=DeltaN-beta;
IsoId=O88898-4; Sequence=VSP_012471, VSP_012474;
Note=Produced by alternative splicing of isoform 2.;
Name=5; Synonyms=TA*-gamma, TA*p63gamma;
IsoId=O88898-5; Sequence=VSP_012472, VSP_012473;
Note=Produced by alternative splicing of isoform 1.;
Name=6; Synonyms=DeltaN-gamma;
IsoId=O88898-6; Sequence=VSP_012471, VSP_012472, VSP_012473;
Note=Produced by alternative splicing of isoform 2.;
-!- TISSUE SPECIFICITY: Widely expressed, notably in thymus, prostate,
placenta and skeletal muscle, although the precise isoform varies
according to tissue type. Progenitor cell layers of skin, breast
and prostate express high levels of DeltaN-type isoforms.
{ECO:0000269|PubMed:9774969}.
-!- DEVELOPMENTAL STAGE: TA*-type isoforms are expressed from E7.5,
prior to the onset of epithelial stratification, while DeltaN-type
isoforms are expressed from E9.5. {ECO:0000269|PubMed:14729569}.
-!- INDUCTION: Induced by DNA damaging agents.
{ECO:0000269|PubMed:11932750}.
-!- 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:0000250}.
-!- PTM: May be sumoylated. {ECO:0000250}.
-!- PTM: Ubiquitinated. Polyubiquitination involves WWP1 and leads to
proteasomal degradation of this protein.
{ECO:0000269|PubMed:18806757}.
-!- SIMILARITY: Belongs to the p53 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC33397.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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EMBL; AF075434; AAC62639.1; -; mRNA.
EMBL; AF075435; AAC62640.1; -; mRNA.
EMBL; AF075436; AAC62641.1; -; mRNA.
EMBL; AF075437; AAC62642.1; -; mRNA.
EMBL; AF075438; AAC62643.1; -; mRNA.
EMBL; AF075439; AAC62644.1; -; mRNA.
EMBL; AB010152; BAA32432.1; -; mRNA.
EMBL; AF533892; AAP87982.1; -; Genomic_DNA.
EMBL; AF533892; AAP87985.1; -; Genomic_DNA.
EMBL; AF533892; AAP87983.1; -; Genomic_DNA.
EMBL; AF533892; AAP87984.1; -; Genomic_DNA.
EMBL; AF533892; AAP87986.1; -; Genomic_DNA.
EMBL; AF533892; AAP87987.1; -; Genomic_DNA.
EMBL; AK048623; BAC33397.1; ALT_SEQ; mRNA.
CCDS; CCDS28085.1; -. [O88898-2]
CCDS; CCDS49808.1; -. [O88898-5]
CCDS; CCDS49809.1; -. [O88898-1]
CCDS; CCDS49810.1; -. [O88898-3]
RefSeq; NP_001120731.1; NM_001127259.1. [O88898-1]
RefSeq; NP_001120732.1; NM_001127260.1. [O88898-3]
RefSeq; NP_001120733.1; NM_001127261.1. [O88898-5]
RefSeq; NP_001120734.1; NM_001127262.1. [O88898-4]
RefSeq; NP_001120736.1; NM_001127264.1.
RefSeq; NP_001120737.1; NM_001127265.1. [O88898-6]
RefSeq; NP_035771.1; NM_011641.2. [O88898-2]
UniGene; Mm.20894; -.
ProteinModelPortal; O88898; -.
SMR; O88898; -.
BioGrid; 204325; 3.
ELM; O88898; -.
IntAct; O88898; 7.
MINT; MINT-4585054; -.
STRING; 10090.ENSMUSP00000110965; -.
iPTMnet; O88898; -.
PhosphoSitePlus; O88898; -.
PaxDb; O88898; -.
PRIDE; O88898; -.
Ensembl; ENSMUST00000040231; ENSMUSP00000038117; ENSMUSG00000022510. [O88898-2]
Ensembl; ENSMUST00000065523; ENSMUSP00000067005; ENSMUSG00000022510. [O88898-3]
Ensembl; ENSMUST00000115308; ENSMUSP00000110963; ENSMUSG00000022510. [O88898-5]
Ensembl; ENSMUST00000115310; ENSMUSP00000110965; ENSMUSG00000022510. [O88898-1]
GeneID; 22061; -.
KEGG; mmu:22061; -.
UCSC; uc007yuo.2; mouse. [O88898-5]
UCSC; uc007yup.2; mouse. [O88898-1]
UCSC; uc007yuq.2; mouse. [O88898-3]
UCSC; uc007yut.2; mouse. [O88898-6]
UCSC; uc007yuu.2; mouse. [O88898-2]
UCSC; uc007yuv.2; mouse. [O88898-4]
CTD; 22061; -.
MGI; MGI:1330810; Trp63.
eggNOG; ENOG410IGE4; Eukaryota.
eggNOG; ENOG410XV9W; LUCA.
GeneTree; ENSGT00390000015092; -.
HOVERGEN; HBG005201; -.
InParanoid; O88898; -.
KO; K10149; -.
OMA; YQIENYN; -.
OrthoDB; EOG091G0XY5; -.
PhylomeDB; O88898; -.
TreeFam; TF106101; -.
Reactome; R-MMU-6804759; Regulation of TP53 Activity through Association with Co-factors.
PRO; PR:O88898; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000022510; -.
CleanEx; MM_TRP63; -.
ExpressionAtlas; O88898; baseline and differential.
Genevisible; O88898; MM.
GO; GO:0000785; C:chromatin; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030425; C:dendrite; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
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:MGI.
GO; GO:0003684; F:damaged DNA binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0097371; F:MDM2/MDM4 family protein binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0002039; F:p53 binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISO:MGI.
GO; GO:0000989; F:transcription factor activity, transcription factor binding; IPI:MGI.
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; IDA:MGI.
GO; GO:0050699; F:WW domain binding; ISO:MGI.
GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; IMP:MGI.
GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
GO; GO:0006915; P:apoptotic process; TAS:MGI.
GO; GO:0007569; P:cell aging; IMP:MGI.
GO; GO:0030154; P:cell differentiation; IMP:MGI.
GO; GO:0008283; P:cell proliferation; IMP:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
GO; GO:0034644; P:cellular response to UV; IBA:GO_Central.
GO; GO:0006338; P:chromatin remodeling; IMP:MGI.
GO; GO:0060197; P:cloacal septation; IMP:MGI.
GO; GO:1904888; P:cranial skeletal system development; IMP:MGI.
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; IMP:MGI.
GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:MGI.
GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
GO; GO:0009913; P:epidermal cell differentiation; IMP:MGI.
GO; GO:0010481; P:epidermal cell division; IMP:MGI.
GO; GO:0008544; P:epidermis development; IMP:MGI.
GO; GO:0002064; P:epithelial cell development; IDA:MGI.
GO; GO:0030855; P:epithelial cell differentiation; IMP:MGI.
GO; GO:0001736; P:establishment of planar polarity; IDA:MGI.
GO; GO:0061436; P:establishment of skin barrier; IMP:UniProtKB.
GO; GO:0048807; P:female genitalia morphogenesis; IMP:MGI.
GO; GO:0001942; P:hair follicle development; IMP:MGI.
GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:MGI.
GO; GO:0030216; P:keratinocyte differentiation; IDA:MGI.
GO; GO:0043616; P:keratinocyte proliferation; IDA:MGI.
GO; GO:0031571; P:mitotic G1 DNA damage checkpoint; IBA:GO_Central.
GO; GO:0001738; P:morphogenesis of a polarized epithelium; IMP:MGI.
GO; GO:0010259; P:multicellular organism aging; IMP:MGI.
GO; GO:0007275; P:multicellular organism development; TAS:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:2000773; P:negative regulation of cellular senescence; ISO:MGI.
GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; IMP:CAFA.
GO; GO:0045617; P:negative regulation of keratinocyte differentiation; IMP:MGI.
GO; GO:2000381; P:negative regulation of mesoderm development; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
GO; GO:0007389; P:pattern specification process; IMP:MGI.
GO; GO:0030859; P:polarized epithelial cell differentiation; IMP:MGI.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IDA:MGI.
GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; ISO:MGI.
GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; ISO:MGI.
GO; GO:0010838; P:positive regulation of keratinocyte proliferation; IGI:MGI.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:MGI.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:MGI.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:MGI.
GO; GO:1904674; P:positive regulation of somatic stem cell population maintenance; IMP:CAFA.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0036342; P:post-anal tail morphogenesis; IMP:MGI.
GO; GO:0030850; P:prostate gland development; IMP:MGI.
GO; GO:0060513; P:prostatic bud formation; IMP:MGI.
GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
GO; GO:0009954; P:proximal/distal pattern formation; IMP:MGI.
GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:MGI.
GO; GO:0010482; P:regulation of epidermal cell division; IMP:UniProtKB.
GO; GO:0043523; P:regulation of neuron apoptotic process; IBA:GO_Central.
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; IMP:MGI.
GO; GO:0098773; P:skin epidermis development; IMP:MGI.
GO; GO:0043589; P:skin morphogenesis; IMP:MGI.
GO; GO:0048745; P:smooth muscle tissue development; IMP:MGI.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0060529; P:squamous basal epithelial stem cell differentiation involved in prostate gland acinus development; IMP:MGI.
GO; GO:0048485; P:sympathetic nervous system development; IMP:MGI.
GO; GO:0060157; P:urinary bladder development; IMP:MGI.
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_sf.
InterPro; IPR011615; p53_DNA-bd.
InterPro; IPR036674; p53_tetramer_sf.
InterPro; IPR010991; p53_tetrameristn.
InterPro; IPR002117; p53_tumour_suppressor.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR032645; Tp63.
PANTHER; PTHR11447; PTHR11447; 1.
PANTHER; PTHR11447:SF8; PTHR11447:SF8; 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;
Activator; Alternative promoter usage; Alternative splicing;
Apoptosis; Complete proteome; Developmental protein; DNA-binding;
Isopeptide bond; Metal-binding; Notch signaling pathway; Nucleus;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation; Zinc.
CHAIN 1 680 Tumor protein 63.
/FTId=PRO_0000185730.
DOMAIN 541 607 SAM.
DNA_BIND 170 362 {ECO:0000250}.
REGION 1 107 Transcription activation. {ECO:0000250}.
REGION 352 388 Interaction with HIPK2. {ECO:0000250}.
REGION 394 443 Oligomerization. {ECO:0000250}.
REGION 610 680 Transactivation inhibition.
{ECO:0000250}.
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 MNFETSRCATLQYCPDPYIQRFIETPAHFSWKESYYRSAMS
QSTQTSEFLSPEVFQHIWDFLEQPICSVQPIELNFVDEPSE
NGATNKIEISMDCIRMQDSDLSDPMW -> MLYLENNAQTQ
FSE (in isoform 2, isoform 4 and isoform
6). {ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:9703973,
ECO:0000303|PubMed:9774969}.
/FTId=VSP_012471.
VAR_SEQ 373 377 GTKRP -> A (in isoform 5 and isoform 6).
{ECO:0000303|PubMed:9774969}.
/FTId=VSP_012472.
VAR_SEQ 450 680 QTSMQSQSSYGNSSPPLNKMNSMNKLPSVSQLINPQQRNAL
TPTTMPEGMGANIPMMGTHMPMAGDMNGLSPTQALPPPLSM
PSTSHCTPPPPYPTDCSIVSFLARLGCSSCLDYFTTQGLTT
IYQIEHYSMDDLASLKIPEQFRHAIWKGILDHRQLHDFSSP
PHLLRTPSGASTVSVGSSETRGERVIDAVRFTLRQTISFPP
RDEWNDFNFDMDSRRNKQQRIKEEGE -> HLLSACFRNEL
VEPRGEAPTQSDVFFRHSNPPNHSVYP (in isoform 5
and isoform 6).
{ECO:0000303|PubMed:9774969}.
/FTId=VSP_012473.
VAR_SEQ 551 680 SFLARLGCSSCLDYFTTQGLTTIYQIEHYSMDDLASLKIPE
QFRHAIWKGILDHRQLHDFSSPPHLLRTPSGASTVSVGSSE
TRGERVIDAVRFTLRQTISFPPRDEWNDFNFDMDSRRNKQQ
RIKEEGE -> RIWQV (in isoform 3 and
isoform 4). {ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:9774969}.
/FTId=VSP_012474.
MUTAGEN 543 543 Y->F: Abolishes interaction with WWP1.
{ECO:0000269|PubMed:18806757}.
SEQUENCE 680 AA; 76789 MW; 8DFF0284F247C68A CRC64;
MNFETSRCAT LQYCPDPYIQ RFIETPAHFS WKESYYRSAM SQSTQTSEFL SPEVFQHIWD
FLEQPICSVQ PIELNFVDEP SENGATNKIE 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
KQQVSDSAKN GDGTKRPFRQ NTHGIQMTSI KKRRSPDDEL LYLPVRGRET YEMLLKIKES
LELMQYLPQH TIETYRQQQQ QQHQHLLQKQ TSMQSQSSYG NSSPPLNKMN SMNKLPSVSQ
LINPQQRNAL TPTTMPEGMG ANIPMMGTHM PMAGDMNGLS PTQALPPPLS MPSTSHCTPP
PPYPTDCSIV SFLARLGCSS CLDYFTTQGL TTIYQIEHYS MDDLASLKIP EQFRHAIWKG
ILDHRQLHDF SSPPHLLRTP SGASTVSVGS SETRGERVID AVRFTLRQTI SFPPRDEWND
FNFDMDSRRN KQQRIKEEGE


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