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Tumor protein 63 (p63) (Keratinocyte transcription factor KET) (Transformation-related protein 63) (TP63) (Tumor protein p73-like) (p73L)

 P63_RAT                 Reviewed;         680 AA.
Q9JJP6; Q99JD6; Q99JD7; Q99JD8; Q99JD9; Q99JE0; Q99JE1; Q99JE2;
Q99JE3;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
20-JUN-2018, entry version 146.
RecName: Full=Tumor protein 63;
Short=p63;
AltName: Full=Keratinocyte transcription factor KET;
AltName: Full=Transformation-related protein 63;
Short=TP63;
AltName: Full=Tumor protein p73-like;
Short=p73L;
Name=Tp63; Synonyms=Ket, P63, Tp73l, Trp63;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Tongue epithelium;
PubMed=9315105; DOI=10.1038/sj.onc.1201500;
Schmale H., Bamberger C.;
"A novel protein with strong homology to the tumor suppressor p53.";
Oncogene 15:1363-1367(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6; 7; 8 AND 9),
FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=Wistar; TISSUE=Tongue;
PubMed=11470269; DOI=10.1016/S0014-5793(01)02643-6;
Bamberger C., Schmale H.;
"Identification and tissue distribution of novel KET/p63 splice
variants.";
FEBS Lett. 501:121-126(2001).
-!- 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 RIPK4 transcription (By
similarity). 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 (By similarity). {ECO:0000250,
ECO:0000269|PubMed:11470269}.
-!- 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 WWP1. Interacts with PDS5A. Interacts
(via activation domain) with NOC2L (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=9;
Name=1; Synonyms=TA2-alpha;
IsoId=Q9JJP6-1; Sequence=Displayed;
Note=Produced by alternative promoter usage.;
Name=2; Synonyms=DeltaN-alpha;
IsoId=Q9JJP6-2; Sequence=VSP_012475;
Note=Produced by alternative promoter usage.;
Name=3; Synonyms=TA2-beta;
IsoId=Q9JJP6-3; Sequence=VSP_012478;
Note=Produced by alternative splicing of isoform 1.;
Name=4; Synonyms=DeltaN-beta;
IsoId=Q9JJP6-4; Sequence=VSP_012475, VSP_012478;
Note=Produced by alternative splicing of isoform 2.;
Name=5; Synonyms=TA2-gamma;
IsoId=Q9JJP6-5; Sequence=VSP_012477;
Note=Produced by alternative splicing of isoform 1.;
Name=6; Synonyms=DeltaN-gamma;
IsoId=Q9JJP6-6; Sequence=VSP_012475, VSP_012477;
Note=Produced by alternative splicing of isoform 2.;
Name=7; Synonyms=TA1-alpha;
IsoId=Q9JJP6-7; Sequence=VSP_012476;
Note=Produced by alternative promoter usage.;
Name=8; Synonyms=TA1-beta;
IsoId=Q9JJP6-8; Sequence=VSP_012476, VSP_012478;
Note=Produced by alternative splicing of isoform 7.;
Name=9; Synonyms=TA1-gamma;
IsoId=Q9JJP6-9; Sequence=VSP_012476, VSP_012477;
Note=Produced by alternative splicing of isoform 7.;
-!- 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:11470269, ECO:0000269|PubMed:9315105}.
-!- 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 (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the p53 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y10258; CAB88216.1; -; mRNA.
EMBL; AJ277446; CAC37098.1; -; mRNA.
EMBL; AJ277447; CAC37099.1; -; mRNA.
EMBL; AJ277448; CAC37100.1; -; mRNA.
EMBL; AJ277449; CAC37101.1; -; mRNA.
EMBL; AJ277450; CAC37102.1; -; mRNA.
EMBL; AJ277451; CAC37103.1; -; mRNA.
EMBL; AJ277452; CAC37104.1; -; mRNA.
EMBL; AJ277453; CAC37105.1; -; mRNA.
RefSeq; NP_001120811.1; NM_001127339.1. [Q9JJP6-3]
RefSeq; NP_001120813.1; NM_001127341.1. [Q9JJP6-5]
RefSeq; NP_001120814.1; NM_001127342.1. [Q9JJP6-2]
RefSeq; NP_001120815.1; NM_001127343.1. [Q9JJP6-4]
RefSeq; NP_001120816.1; NM_001127344.1. [Q9JJP6-6]
RefSeq; NP_062094.1; NM_019221.3. [Q9JJP6-1]
RefSeq; XP_008767013.1; XM_008768791.2. [Q9JJP6-1]
UniGene; Rn.42907; -.
ProteinModelPortal; Q9JJP6; -.
SMR; Q9JJP6; -.
STRING; 10116.ENSRNOP00000033463; -.
PhosphoSitePlus; Q9JJP6; -.
PaxDb; Q9JJP6; -.
Ensembl; ENSRNOT00000002636; ENSRNOP00000002636; ENSRNOG00000001924. [Q9JJP6-2]
Ensembl; ENSRNOT00000036179; ENSRNOP00000032308; ENSRNOG00000001924. [Q9JJP6-5]
Ensembl; ENSRNOT00000036193; ENSRNOP00000033463; ENSRNOG00000001924. [Q9JJP6-1]
Ensembl; ENSRNOT00000067251; ENSRNOP00000059178; ENSRNOG00000001924. [Q9JJP6-3]
Ensembl; ENSRNOT00000068116; ENSRNOP00000061884; ENSRNOG00000001924. [Q9JJP6-4]
GeneID; 246334; -.
KEGG; rno:246334; -.
CTD; 8626; -.
RGD; 620863; Tp63.
eggNOG; ENOG410IGE4; Eukaryota.
eggNOG; ENOG410XV9W; LUCA.
GeneTree; ENSGT00390000015092; -.
HOVERGEN; HBG005201; -.
InParanoid; Q9JJP6; -.
KO; K10149; -.
OMA; GIMEHRQ; -.
OrthoDB; EOG091G0XY5; -.
PhylomeDB; Q9JJP6; -.
TreeFam; TF106101; -.
Reactome; R-RNO-6804759; Regulation of TP53 Activity through Association with Co-factors.
PRO; PR:Q9JJP6; -.
Proteomes; UP000002494; Chromosome 11.
Bgee; ENSRNOG00000001924; -.
Genevisible; Q9JJP6; RN.
GO; GO:0000785; C:chromatin; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
GO; GO:0005667; C:transcription factor complex; IBA:GO_Central.
GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
GO; GO:0003700; F:DNA binding transcription factor activity; IDA:RGD.
GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0097371; F:MDM2/MDM4 family protein binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0002039; F:p53 binding; IBA:GO_Central.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
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 proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0050699; F:WW domain binding; IEA:Ensembl.
GO; GO:0007568; P:aging; IEP:RGD.
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:1904888; P:cranial skeletal system development; 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:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl.
GO; GO:0035116; P:embryonic hindlimb 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: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 by RNA polymerase II; IBA:GO_Central.
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:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:1904674; P:positive regulation of somatic stem cell population maintenance; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; IEA:Ensembl.
GO; GO:0009954; P:proximal/distal pattern formation; IEA:Ensembl.
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:0001302; P:replicative cell aging; IMP:RGD.
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; IEP:RGD.
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.
CDD; cd09572; SAM_tumor-p63; 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.
InterPro; IPR037611; Tumor-p63_SAM.
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.
2: Evidence at transcript 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_0000185731.
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 MNFETSRCATLQYCPDPYIQRFIETPSHFSWKESYYRSAMS
QSTQTSEFLSPEVFQHIWDFLEQPICSVQPIDLNFVDEPSE
NGATNKIEISMDCIRMQDSDLSDPMW -> MLYLESNAQTQ
FSE (in isoform 2, isoform 4 and isoform
6). {ECO:0000303|PubMed:11470269}.
/FTId=VSP_012475.
VAR_SEQ 1 21 MNFETSRCATLQYCPDPYIQR -> MPSC (in isoform
7, isoform 8 and isoform 9).
{ECO:0000303|PubMed:11470269}.
/FTId=VSP_012476.
VAR_SEQ 450 680 QTSMQSQSSYGNSSPPLNKMNSMNKLPSVSQLINPQQRNAL
TPTTMPEGMGANIPMMGTHMPMAGDMNGLSPTQALPPPLSM
PSTSHCTPPPPYPTDCSIVSFLARLGCSSCLDYFTTQGLTT
IYQIEHYSMDDLASLKIPEQFRHAIWKGILDHRQLHDFSSP
PHLLRTPSGASTVSVGSSETRGERVIDAVRFTLRQTISFPP
RDEWNDFNFDMDSRRNKQQRIKEEGE -> HLLSACFRNEL
VESRREAPTQSDVFFRHSNPPNHSVYP (in isoform
5, isoform 6 and isoform 9).
{ECO:0000303|PubMed:11470269}.
/FTId=VSP_012477.
VAR_SEQ 551 680 SFLARLGCSSCLDYFTTQGLTTIYQIEHYSMDDLASLKIPE
QFRHAIWKGILDHRQLHDFSSPPHLLRTPSGASTVSVGSSE
TRGERVIDAVRFTLRQTISFPPRDEWNDFNFDMDSRRNKQQ
RIKEEGE -> RIWQV (in isoform 3, isoform 4
and isoform 8).
{ECO:0000303|PubMed:11470269}.
/FTId=VSP_012478.
SEQUENCE 680 AA; 76760 MW; AC45DABB88F61400 CRC64;
MNFETSRCAT LQYCPDPYIQ RFIETPSHFS WKESYYRSAM SQSTQTSEFL SPEVFQHIWD
FLEQPICSVQ PIDLNFVDEP SENGATNKIE ISMDCIRMQD SDLSDPMWPQ YTNLGLLNGM
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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