O88898 (P63_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tumor protein 63
Short name=p63

Alternative name(s):
Transformation-related protein 63
Short name=TP63
Tumor protein p73-like
Short name=p73L

Gene names

Name:	Tp63
Synonyms:	P63, P73l, Tp73l, Trp63

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	680 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 specificactivity. 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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.10
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Binds DNA as a homotetramer. Isoform compositionof 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. Ref.9
Subcellular location	Nucleus Ref.8.
Tissue specificity	Widely expressed, notably in thymus, prostate, placenta and skeletal muscle, although the precise isoform variesaccording to tissue type. Progenitor cell layers of skin, breast and prostate express high levels of DeltaN-type isoforms. Ref.1
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. Ref.8
Induction	Induced by DNA damaging agents. Ref.7
Domain	The transactivation inhibitory domain (TID) can interact with, and inhibit the activity of the N-terminal transcriptional activation domain of TA*-type isoforms By similarity.
Post-translational modification	May be sumoylated By similarity. Ubiquitinated. Polyubiquitination involves WWP1 and leads to proteasomal degradation of this protein. Ref.9
Sequence similarities	Belongs to the p53 family. Contains 1 SAM (sterile alpha motif) domain.
Sequence caution	The sequence BAC33397.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
Biological process	Apoptosis Notch signaling pathway Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative promoter usage Alternative splicing
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Developmental protein
PTM	Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Inferred from Biological aspect of Ancestor. Source: RefGenome Notch signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cell aging Inferred from mutant phenotype PubMed 16107615. Source: MGI cellular response to UV Inferred from Biological aspect of Ancestor. Source: RefGenome chromatin remodeling Inferred from mutant phenotype PubMed 21930775. Source: MGI cloacal septation Inferred from mutant phenotype PubMed 12368184. Source: MGI ectoderm and mesoderm interaction Inferred from mutant phenotype Ref.5Ref.6. Source: MGI embryonic limb morphogenesis Inferred from mutant phenotype Ref.5. Source: MGI epidermal cell division Inferred from mutant phenotype PubMed 21127502. Source: MGI epithelial cell development Inferred from direct assay PubMed 16601749. Source: MGI establishment of planar polarity Inferred from direct assay Ref.8. Source: MGI female genitalia morphogenesis Inferred from mutant phenotype PubMed 12368184. Source: MGI hair follicle development Inferred from mutant phenotype PubMed 16410075. Source: MGI hair follicle morphogenesis Inferred from mutant phenotype PubMed 16524929. Source: MGI intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Inferred from mutant phenotype PubMed 17122775. Source: MGI keratinocyte differentiation Inferred from direct assay Ref.8. Source: MGI keratinocyte proliferation Inferred from direct assay PubMed 16601749. Source: MGI mitotic G1 DNA damage checkpoint Inferred from Biological aspect of Ancestor. Source: RefGenome multicellular organismal aging Inferred from mutant phenotype PubMed 16107615. Source: MGI negative regulation of apoptotic process Inferred from mutant phenotype PubMed 17079275. Source: MGI negative regulation of keratinocyte differentiation Inferred from mutant phenotype PubMed 22274697. Source: MGI negative regulation of mesoderm development Inferred from mutant phenotype PubMed 21127502. Source: MGI negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 23906066. Source: MGI neuron apoptotic process Inferred from mutant phenotype PubMed 16337913. Source: MGI odontogenesis of dentin-containing tooth Inferred from mutant phenotype PubMed 16410075PubMed 16524929. Source: MGI polarized epithelial cell differentiation Inferred from mutant phenotype PubMed 15189821. Source: MGI positive regulation of Notch signaling pathway Inferred from electronic annotation. Source: Ensembl positive regulation of apoptotic signaling pathway Inferred from direct assay Ref.1. Source: MGI positive regulation of fibroblast apoptotic process Inferred from electronic annotation. Source: Ensembl positive regulation of mesenchymal cell proliferation Inferred from mutant phenotype PubMed 17079275. Source: MGI positive regulation of osteoblast differentiation Inferred from electronic annotation. Source: Ensembl positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 12789272PubMed 16601749PubMed 17093266PubMed 21285247PubMed 21930775PubMed 23906066Ref.1. Source: MGI post-anal tail morphogenesis Inferred from mutant phenotype PubMed 12368184. Source: MGI prostatic bud formation Inferred from mutant phenotype PubMed 11106548. Source: MGI protein homotetramerization Inferred from electronic annotation. Source: Ensembl proximal/distal pattern formation Inferred from mutant phenotype Ref.5. Source: MGI regulation of neuron apoptotic process Inferred from Biological aspect of Ancestor. Source: RefGenome response to X-ray Inferred from Biological aspect of Ancestor. Source: RefGenome response to gamma radiation Inferred from Biological aspect of Ancestor. Source: RefGenome skeletal system development Inferred from mutant phenotype Ref.6. Source: MGI smooth muscle tissue development Inferred from mutant phenotype PubMed 17079275. Source: MGI squamous basal epithelial stem cell differentiation involved in prostate gland acinus development Inferred from mutant phenotype PubMed 15371309. Source: MGI sympathetic nervous system development Inferred from mutant phenotype PubMed 16337913. Source: MGI urinary bladder development Inferred from mutant phenotype PubMed 17079275. Source: MGI
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Ensembl chromatin Inferred from Biological aspect of Ancestor. Source: RefGenome cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome dendrite Inferred from Biological aspect of Ancestor. Source: RefGenome nuclear chromatin Inferred from electronic annotation. Source: Ensembl nucleoplasm Inferred from electronic annotation. Source: Ensembl nucleus Inferred from direct assay PubMed 11106548PubMed 11522642PubMed 12368184Ref.8PubMed 15361520PubMed 15585950PubMed 16080917PubMed 16466397PubMed 16601749PubMed 17383628PubMed 17522155PubMed 21285247PubMed 23608756. Source: MGI transcription factor complex Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Inferred from direct assay PubMed 21930775. Source: MGI chromatin binding Inferred from direct assay PubMed 16524929PubMed 16601749. Source: MGI damaged DNA binding Inferred from direct assay PubMed 17122775. Source: MGI double-stranded DNA binding Inferred from Biological aspect of Ancestor. Source: RefGenome metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW p53 binding Inferred from Biological aspect of Ancestor. Source: RefGenome sequence-specific DNA binding Inferred from direct assay PubMed 16618808PubMed 18256694. Source: MGI sequence-specific DNA binding transcription factor activity Inferred from Biological aspect of Ancestor. Source: RefGenome transcription factor binding transcription factor activity Inferred from physical interaction PubMed 23906066. Source: MGI transcription regulatory region DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-2338025,EBI-2338025
Cables1	Q9ESJ1	2	EBI-2338025,EBI-604411
KAT2B	Q92831	3	EBI-2338228,EBI-477430	From a different organism.
NQO1	P15559	2	EBI-2338244,EBI-3989435	From a different organism.
TP53	P04637	2	EBI-2338025,EBI-366083	From a different organism.

Alternative products

This entry describes 6 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]

Isoform 1 (identifier: O88898-1)

Also known as: TA*-alpha; TA*p63alpha;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: Produced by alternative promoter usage.

Isoform 2 (identifier: O88898-2)

Also known as: DeltaN-alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     1-108: MNFETSRCAT...QDSDLSDPMW → MLYLENNAQTQFSE

Note: Produced by alternative promoter usage.

Isoform 3 (identifier: O88898-3)

Also known as: TA*-beta; TA*p63beta;

The sequence of this isoform differs from the canonical sequence as follows:
     551-680: SFLARLGCSS...KQQRIKEEGE → RIWQV

Note: Produced by alternative splicing of isoform 1.

Isoform 4 (identifier: O88898-4)

Also known as: DeltaN-beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-108: MNFETSRCAT...QDSDLSDPMW → MLYLENNAQTQFSE
     551-680: SFLARLGCSS...KQQRIKEEGE → RIWQV

Note: Produced by alternative splicing of isoform 2.

Isoform 5 (identifier: O88898-5)

Also known as: TA*-gamma; TA*p63gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     373-377: GTKRP → A
     450-680: QTSMQSQSSY...KQQRIKEEGE → HLLSACFRNE...SNPPNHSVYP

Note: Produced by alternative splicing of isoform 1.

Isoform 6 (identifier: O88898-6)

Also known as: DeltaN-gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     1-108: MNFETSRCAT...QDSDLSDPMW → MLYLENNAQTQFSE
     373-377: GTKRP → A
     450-680: QTSMQSQSSY...KQQRIKEEGE → HLLSACFRNE...SNPPNHSVYP

Note: Produced by alternative splicing of isoform 2.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 680	680	Tumor protein 63		PRO_0000185730
Regions
	Domain	541 – 607	67	SAM
	DNA binding	170 – 362	193	By similarity
	Region	1 – 107	107	Transcription activation By similarity
	Region	352 – 388	37	Interaction with HIPK2 By similarity
	Region	394 – 443	50	Oligomerization By similarity
	Region	610 – 680	71	Transactivation inhibition By similarity
	Compositional bias	437 – 444	8	Poly-Gln
Sites
	Metal binding	244	1	Zinc By similarity
	Metal binding	247	1	Zinc By similarity
	Metal binding	308	1	Zinc By similarity
	Metal binding	312	1	Zinc By similarity
Amino acid modifications
	Cross-link	676		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Natural variations
	Alternative sequence	1 – 108	108	MNFET…SDPMW → MLYLENNAQTQFSE in isoform 2, isoform 4 and isoform 6.		VSP_012471
	Alternative sequence	373 – 377	5	GTKRP → A in isoform 5 and isoform 6.		VSP_012472
	Alternative sequence	450 – 680	231	QTSMQ…KEEGE → HLLSACFRNELVEPRGEAPT QSDVFFRHSNPPNHSVYP in isoform 5 and isoform 6.		VSP_012473
	Alternative sequence	551 – 680	130	SFLAR…KEEGE → RIWQV in isoform 3 and isoform 4.		VSP_012474
Experimental info
	Mutagenesis	543	1	Y → F: Abolishes interaction with WWP1. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (TA*-alpha) (TA*p63alpha) [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 8DFF0284F247C68A	FASTA	680	76,789
	10 20 30 40 50 60 MNFETSRCAT LQYCPDPYIQ RFIETPAHFS WKESYYRSAM SQSTQTSEFL SPEVFQHIWD 70 80 90 100 110 120 FLEQPICSVQ PIELNFVDEP SENGATNKIE ISMDCIRMQD SDLSDPMWPQ YTNLGLLNSM 130 140 150 160 170 180 DQQIQNGSSS TSPYNTDHAQ NSVTAPSPYA QPSSTFDALS PSPAIPSNTD YPGPHSFDVS 190 200 210 220 230 240 FQQSSTAKSA TWTYSTELKK LYCQIAKTCP IQIKVMTPPP QGAVIRAMPV YKKAEHVTEV 250 260 270 280 290 300 VKRCPNHELS REFNEGQIAP PSHLIRVEGN SHAQYVEDPI TGRQSVLVPY EPPQVGTEFT 310 320 330 340 350 360 TVLYNFMCNS SCVGGMNRRP ILIIVTLETR DGQVLGRRCF EARICACPGR DRKADEDSIR 370 380 390 400 410 420 KQQVSDSAKN GDGTKRPFRQ NTHGIQMTSI KKRRSPDDEL LYLPVRGRET YEMLLKIKES 430 440 450 460 470 480 LELMQYLPQH TIETYRQQQQ QQHQHLLQKQ TSMQSQSSYG NSSPPLNKMN SMNKLPSVSQ 490 500 510 520 530 540 LINPQQRNAL TPTTMPEGMG ANIPMMGTHM PMAGDMNGLS PTQALPPPLS MPSTSHCTPP 550 560 570 580 590 600 PPYPTDCSIV SFLARLGCSS CLDYFTTQGL TTIYQIEHYS MDDLASLKIP EQFRHAIWKG 610 620 630 640 650 660 ILDHRQLHDF SSPPHLLRTP SGASTVSVGS SETRGERVID AVRFTLRQTI SFPPRDEWND 670 680 FNFDMDSRRN KQQRIKEEGE
	Isoform 2 (DeltaN-alpha) [UniParc]. Checksum: 622E24085B8BDCB7	FASTA	586	65,789
	10 20 30 40 50 60 MLYLENNAQT QFSEPQYTNL GLLNSMDQQI QNGSSSTSPY NTDHAQNSVT APSPYAQPSS 70 80 90 100 110 120 TFDALSPSPA IPSNTDYPGP HSFDVSFQQS STAKSATWTY STELKKLYCQ IAKTCPIQIK 130 140 150 160 170 180 VMTPPPQGAV IRAMPVYKKA EHVTEVVKRC PNHELSREFN EGQIAPPSHL IRVEGNSHAQ 190 200 210 220 230 240 YVEDPITGRQ SVLVPYEPPQ VGTEFTTVLY NFMCNSSCVG GMNRRPILII VTLETRDGQV 250 260 270 280 290 300 LGRRCFEARI CACPGRDRKA DEDSIRKQQV SDSAKNGDGT KRPFRQNTHG IQMTSIKKRR 310 320 330 340 350 360 SPDDELLYLP VRGRETYEML LKIKESLELM QYLPQHTIET YRQQQQQQHQ HLLQKQTSMQ 370 380 390 400 410 420 SQSSYGNSSP PLNKMNSMNK LPSVSQLINP QQRNALTPTT MPEGMGANIP MMGTHMPMAG 430 440 450 460 470 480 DMNGLSPTQA LPPPLSMPST SHCTPPPPYP TDCSIVSFLA RLGCSSCLDY FTTQGLTTIY 490 500 510 520 530 540 QIEHYSMDDL ASLKIPEQFR HAIWKGILDH RQLHDFSSPP HLLRTPSGAS TVSVGSSETR 550 560 570 580 GERVIDAVRF TLRQTISFPP RDEWNDFNFD MDSRRNKQQR IKEEGE
	Isoform 3 (TA*-beta) (TA*p63beta) [UniParc]. Checksum: 059E034046EB8987	FASTA	555	62,455
	10 20 30 40 50 60 MNFETSRCAT LQYCPDPYIQ RFIETPAHFS WKESYYRSAM SQSTQTSEFL SPEVFQHIWD 70 80 90 100 110 120 FLEQPICSVQ PIELNFVDEP SENGATNKIE ISMDCIRMQD SDLSDPMWPQ YTNLGLLNSM 130 140 150 160 170 180 DQQIQNGSSS TSPYNTDHAQ NSVTAPSPYA QPSSTFDALS PSPAIPSNTD YPGPHSFDVS 190 200 210 220 230 240 FQQSSTAKSA TWTYSTELKK LYCQIAKTCP IQIKVMTPPP QGAVIRAMPV YKKAEHVTEV 250 260 270 280 290 300 VKRCPNHELS REFNEGQIAP PSHLIRVEGN SHAQYVEDPI TGRQSVLVPY EPPQVGTEFT 310 320 330 340 350 360 TVLYNFMCNS SCVGGMNRRP ILIIVTLETR DGQVLGRRCF EARICACPGR DRKADEDSIR 370 380 390 400 410 420 KQQVSDSAKN GDGTKRPFRQ NTHGIQMTSI KKRRSPDDEL LYLPVRGRET YEMLLKIKES 430 440 450 460 470 480 LELMQYLPQH TIETYRQQQQ QQHQHLLQKQ TSMQSQSSYG NSSPPLNKMN SMNKLPSVSQ 490 500 510 520 530 540 LINPQQRNAL TPTTMPEGMG ANIPMMGTHM PMAGDMNGLS PTQALPPPLS MPSTSHCTPP 550 PPYPTDCSIV RIWQV
	Isoform 4 (DeltaN-beta) [UniParc]. Checksum: 7613296F2F85DBC8	FASTA	461	51,455
	10 20 30 40 50 60 MLYLENNAQT QFSEPQYTNL GLLNSMDQQI QNGSSSTSPY NTDHAQNSVT APSPYAQPSS 70 80 90 100 110 120 TFDALSPSPA IPSNTDYPGP HSFDVSFQQS STAKSATWTY STELKKLYCQ IAKTCPIQIK 130 140 150 160 170 180 VMTPPPQGAV IRAMPVYKKA EHVTEVVKRC PNHELSREFN EGQIAPPSHL IRVEGNSHAQ 190 200 210 220 230 240 YVEDPITGRQ SVLVPYEPPQ VGTEFTTVLY NFMCNSSCVG GMNRRPILII VTLETRDGQV 250 260 270 280 290 300 LGRRCFEARI CACPGRDRKA DEDSIRKQQV SDSAKNGDGT KRPFRQNTHG IQMTSIKKRR 310 320 330 340 350 360 SPDDELLYLP VRGRETYEML LKIKESLELM QYLPQHTIET YRQQQQQQHQ HLLQKQTSMQ 370 380 390 400 410 420 SQSSYGNSSP PLNKMNSMNK LPSVSQLINP QQRNALTPTT MPEGMGANIP MMGTHMPMAG 430 440 450 460 DMNGLSPTQA LPPPLSMPST SHCTPPPPYP TDCSIVRIWQ V
	Isoform 5 (TA*-gamma) (TA*p63gamma) [UniParc]. Checksum: A90ED0C110C50EAD	FASTA	483	54,970
	10 20 30 40 50 60 MNFETSRCAT LQYCPDPYIQ RFIETPAHFS WKESYYRSAM SQSTQTSEFL SPEVFQHIWD 70 80 90 100 110 120 FLEQPICSVQ PIELNFVDEP SENGATNKIE ISMDCIRMQD SDLSDPMWPQ YTNLGLLNSM 130 140 150 160 170 180 DQQIQNGSSS TSPYNTDHAQ NSVTAPSPYA QPSSTFDALS PSPAIPSNTD YPGPHSFDVS 190 200 210 220 230 240 FQQSSTAKSA TWTYSTELKK LYCQIAKTCP IQIKVMTPPP QGAVIRAMPV YKKAEHVTEV 250 260 270 280 290 300 VKRCPNHELS REFNEGQIAP PSHLIRVEGN SHAQYVEDPI TGRQSVLVPY EPPQVGTEFT 310 320 330 340 350 360 TVLYNFMCNS SCVGGMNRRP ILIIVTLETR DGQVLGRRCF EARICACPGR DRKADEDSIR 370 380 390 400 410 420 KQQVSDSAKN GDAFRQNTHG IQMTSIKKRR SPDDELLYLP VRGRETYEML LKIKESLELM 430 440 450 460 470 480 QYLPQHTIET YRQQQQQQHQ HLLQKHLLSA CFRNELVEPR GEAPTQSDVF FRHSNPPNHS VYP
	Isoform 6 (DeltaN-gamma) [UniParc]. Checksum: FE6B4A859C5F00BB	FASTA	389	43,970
	10 20 30 40 50 60 MLYLENNAQT QFSEPQYTNL GLLNSMDQQI QNGSSSTSPY NTDHAQNSVT APSPYAQPSS 70 80 90 100 110 120 TFDALSPSPA IPSNTDYPGP HSFDVSFQQS STAKSATWTY STELKKLYCQ IAKTCPIQIK 130 140 150 160 170 180 VMTPPPQGAV IRAMPVYKKA EHVTEVVKRC PNHELSREFN EGQIAPPSHL IRVEGNSHAQ 190 200 210 220 230 240 YVEDPITGRQ SVLVPYEPPQ VGTEFTTVLY NFMCNSSCVG GMNRRPILII VTLETRDGQV 250 260 270 280 290 300 LGRRCFEARI CACPGRDRKA DEDSIRKQQV SDSAKNGDAF RQNTHGIQMT SIKKRRSPDD 310 320 330 340 350 360 ELLYLPVRGR ETYEMLLKIK ESLELMQYLP QHTIETYRQQ QQQQHQHLLQ KHLLSACFRN 370 380 ELVEPRGEAP TQSDVFFRHS NPPNHSVYP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"p63, a p53 homolog at 3q27-29, encodes multiple products with transactivating, death-inducing, and dominant-negative activities." Yang A., Kaghad M., Wang Y., Gillett E., Fleming M.D., Doetsch V., Andrews N.C., Caput D., McKeon F. Mol. Cell 2:305-316(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), TISSUE SPECIFICITY.
[2]	"A second p53-related protein, p73L, with high homology to p73." Senoo M., Seki N., Ohira M., Sugano S., Watanabe M., Tachibana M., Tanaka T., Shinkai Y., Kato H. Biochem. Biophys. Res. Commun. 248:603-607(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Thymus.
[3]	Kui J.S., Wang J.H., Zhang M.Q., Mills A.A. Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-376 (ISOFORMS 2 AND 4). Strain: C57BL/6J. Tissue: Head.
[5]	"p63 is a p53 homologue required for limb and epidermal morphogenesis." Mills A.A., Zheng B., Wang X.-J., Vogel H., Roop D.R., Bradley A. Nature 398:708-713(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN EPITHELIAL MORPHOGENESIS.
[6]	"p63 is essential for regenerative proliferation in limb, craniofacial and epithelial development." Yang A., Schweitzer R., Sun D., Kaghad M., Walker N., Bronson R.T., Tabin C., Sharpe A., Caput D., Crum C., McKeon F. Nature 398:714-718(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN EPITHELIAL MORPHOGENESIS.
[7]	"p63 and p73 are required for p53-dependent apoptosis in response to DNA damage." Flores E.R., Tsai K.Y., Crowley D., Sengupta S., Yang A., McKeon F., Jacks T. Nature 416:560-564(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN TP53 DEPENDENT APOPTOSIS, INDUCTION.
[8]	"p63 is the molecular switch for initiation of an epithelial stratification program." Koster M.I., Kim S., Mills A.A., DeMayo F.J., Roop D.R. Genes Dev. 18:126-131(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN EPITHELIAL MORPHOGENESIS, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[9]	"WW domain-containing E3 ubiquitin protein ligase 1 targets p63 transcription factor for ubiquitin-mediated proteasomal degradation and regulates apoptosis." Li Y., Zhou Z., Chen C. Cell Death Differ. 15:1941-1951(2008) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, INTERACTION WITH WWP1, MUTAGENESIS OF TYR-543.
[10]	"Exome sequence identifies RIPK4 as the Bartsocas-Papas syndrome locus." 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. Am. J. Hum. Genet. 90:69-75(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN RIPK4 TRANSACTIVATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF075434 mRNA. Translation: AAC62639.1. AF075435 mRNA. Translation: AAC62640.1. AF075436 mRNA. Translation: AAC62641.1. AF075437 mRNA. Translation: AAC62642.1. AF075438 mRNA. Translation: AAC62643.1. AF075439 mRNA. Translation: AAC62644.1. AB010152 mRNA. Translation: BAA32432.1. AF533892 Genomic DNA. Translation: AAP87982.1. AF533892 Genomic DNA. Translation: AAP87985.1. AF533892 Genomic DNA. Translation: AAP87983.1. AF533892 Genomic DNA. Translation: AAP87984.1. AF533892 Genomic DNA. Translation: AAP87986.1. AF533892 Genomic DNA. Translation: AAP87987.1. AK048623 mRNA. Translation: BAC33397.1. Sequence problems.
RefSeq	NP_001120731.1. NM_001127259.1. NP_001120732.1. NM_001127260.1. NP_001120733.1. NM_001127261.1. NP_001120734.1. NM_001127262.1. NP_001120736.1. NM_001127264.1. NP_001120737.1. NM_001127265.1. NP_035771.1. NM_011641.2.
UniGene	Mm.20894.
3D structure databases
ProteinModelPortal	O88898.
SMR	O88898. Positions 153-437, 545-611.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	204325. 5 interactions.
IntAct	O88898. 7 interactions.
MINT	MINT-4585054.
PTM databases
PhosphoSite	O88898.
Proteomic databases
PaxDb	O88898.
PRIDE	O88898.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000040231; ENSMUSP00000038117; ENSMUSG00000022510. ENSMUST00000065523; ENSMUSP00000067005; ENSMUSG00000022510. ENSMUST00000115304; ENSMUSP00000110959; ENSMUSG00000022510. ENSMUST00000115308; ENSMUSP00000110963; ENSMUSG00000022510. ENSMUST00000115310; ENSMUSP00000110965; ENSMUSG00000022510.
GeneID	22061.
KEGG	mmu:22061.
UCSC	uc007yup.2. mouse.
Organism-specific databases
CTD	22061.
MGI	MGI:1330810. Trp63.
Phylogenomic databases
eggNOG	NOG80479.
GeneTree	ENSGT00390000015092.
HOVERGEN	HBG005201.
InParanoid	O88898.
KO	K10149.
OMA	QRNTLTP.
OrthoDB	EOG7JQBNW.
TreeFam	TF106101.
Gene expression databases
ArrayExpress	O88898.
Bgee	O88898.
CleanEx	MM_TRP63.
Genevestigator	O88898.
Family and domain databases
Gene3D	1.10.150.50. 1 hit. 2.60.40.720. 1 hit. 4.10.170.10. 1 hit.
InterPro	IPR008967. p53-like_TF_DNA-bd. IPR012346. p53/RUNT-type_TF_DNA-bd. IPR011615. p53_DNA-bd. IPR010991. p53_tetrameristn. IPR002117. p53_tumour_suppressor. IPR001660. SAM. IPR013761. SAM/pointed. IPR011510. SAM_2. [Graphical view]
PANTHER	PTHR11447. PTHR11447. 1 hit.
Pfam	PF00870. P53. 1 hit. PF07710. P53_tetramer. 1 hit. PF07647. SAM_2. 1 hit. [Graphical view]
PRINTS	PR00386. P53SUPPRESSR.
SMART	SM00454. SAM. 1 hit. [Graphical view]
SUPFAM	SSF47719. SSF47719. 1 hit. SSF47769. SSF47769. 1 hit. SSF49417. SSF49417. 1 hit.
PROSITE	PS00348. P53. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	301864.
PRO	O88898.
SOURCE	Search...

Entry information

Entry name

P63_MOUSE

Accession

Primary (citable) accession number: O88898
Secondary accession number(s): O88897 , O88899, O89097, Q8C826, Q9QWY9, Q9QWZ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	November 1, 1998
Last modified:	February 19, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program