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O88898 (P63_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length680 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processApoptosis
Notch signaling pathway
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative promoter usage
Alternative splicing
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Developmental protein
   PTMIsopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA 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

anatomical structure formation involved in morphogenesis

Inferred from mutant phenotype PubMed 17878916. Source: MGI

apoptotic process

Traceable author statement PubMed 14555234. Source: MGI

cell aging

Inferred from mutant phenotype PubMed 16107615. Source: MGI

cell differentiation

Inferred from mutant phenotype PubMed 15371309. 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

epidermis development

Inferred from mutant phenotype Ref.5PubMed 16601749PubMed 22274697. Source: MGI

epithelial cell development

Inferred from direct assay PubMed 16601749. Source: MGI

epithelial cell differentiation

Inferred from mutant phenotype PubMed 12368184PubMed 17878916. Source: MGI

establishment of planar polarity

Inferred from direct assay Ref.8. Source: MGI

establishment of skin barrier

Inferred from mutant phenotype PubMed 24075906. Source: UniProtKB

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

morphogenesis of a polarized epithelium

Inferred from mutant phenotype PubMed 15189821. Source: MGI

multicellular organismal aging

Inferred from mutant phenotype PubMed 16107615. Source: MGI

multicellular organismal development

Traceable author statement PubMed 14555234. 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

organ morphogenesis

Inferred from mutant phenotype Ref.6. Source: MGI

pattern specification process

Inferred from mutant phenotype Ref.6. Source: MGI

polarized epithelial cell differentiation

Inferred from mutant phenotype PubMed 15189821. Source: MGI

positive regulation of Notch signaling pathway

Inferred from mutant phenotype PubMed 22274697. Source: MGI

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 keratinocyte proliferation

Inferred from genetic interaction PubMed 24075906. Source: MGI

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 18326838PubMed 21285247PubMed 21930775PubMed 23906066Ref.1. Source: MGI

post-anal tail morphogenesis

Inferred from mutant phenotype PubMed 12368184. Source: MGI

prostate gland development

Inferred from mutant phenotype PubMed 11106548. 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 epidermal cell division

Inferred from mutant phenotype PubMed 24075906. Source: UniProtKB

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

skin morphogenesis

Inferred from mutant phenotype PubMed 17041603. 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_componentGolgi 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 18326838PubMed 21285247PubMed 23608756. Source: MGI

transcription factor complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionDNA binding

Inferred from direct assay PubMed 16363065. Source: MGI

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

identical protein binding

Inferred from physical interaction PubMed 21335238PubMed 21335238PubMed 21335238PubMed 22575646PubMed 21335238. Source: IntAct

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

p53 binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction PubMed 19345189PubMed 20559324PubMed 21042282PubMed 22575646PubMed 21042282. Source: IntAct

sequence-specific DNA binding

Inferred from direct assay PubMed 16618808PubMed 18256694PubMed 18326838. 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

itself2EBI-2338025,EBI-2338025
Cables1Q9ESJ12EBI-2338025,EBI-604411
KAT2BQ928313EBI-2338228,EBI-477430From a different organism.
NQO1P155592EBI-2338244,EBI-3989435From a different organism.
TP53P046372EBI-2338025,EBI-366083From 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 680680Tumor protein 63
PRO_0000185730

Regions

Domain541 – 60767SAM
DNA binding170 – 362193 By similarity
Region1 – 107107Transcription activation By similarity
Region352 – 38837Interaction with HIPK2 By similarity
Region394 – 44350Oligomerization By similarity
Region610 – 68071Transactivation inhibition By similarity
Compositional bias437 – 4448Poly-Gln

Sites

Metal binding2441Zinc By similarity
Metal binding2471Zinc By similarity
Metal binding3081Zinc By similarity
Metal binding3121Zinc By similarity

Amino acid modifications

Cross-link676Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence1 – 108108MNFET…SDPMW → MLYLENNAQTQFSE in isoform 2, isoform 4 and isoform 6.
VSP_012471
Alternative sequence373 – 3775GTKRP → A in isoform 5 and isoform 6.
VSP_012472
Alternative sequence450 – 680231QTSMQ…KEEGE → HLLSACFRNELVEPRGEAPT QSDVFFRHSNPPNHSVYP in isoform 5 and isoform 6.
VSP_012473
Alternative sequence551 – 680130SFLAR…KEEGE → RIWQV in isoform 3 and isoform 4.
VSP_012474

Experimental info

Mutagenesis5431Y → F: Abolishes interaction with WWP1. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (TA*-alpha) (TA*p63alpha) [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 8DFF0284F247C68A

FASTA68076,789
        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 

« Hide

Isoform 2 (DeltaN-alpha) [UniParc].

Checksum: 622E24085B8BDCB7
Show »

FASTA58665,789
Isoform 3 (TA*-beta) (TA*p63beta) [UniParc].

Checksum: 059E034046EB8987
Show »

FASTA55562,455
Isoform 4 (DeltaN-beta) [UniParc].

Checksum: 7613296F2F85DBC8
Show »

FASTA46151,455
Isoform 5 (TA*-gamma) (TA*p63gamma) [UniParc].

Checksum: A90ED0C110C50EAD
Show »

FASTA48354,970
Isoform 6 (DeltaN-gamma) [UniParc].

Checksum: FE6B4A859C5F00BB
Show »

FASTA38943,970

References

« Hide '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. expand/collapse author list , 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.
CCDSCCDS28085.1. [O88898-2]
CCDS49808.1. [O88898-5]
CCDS49809.1. [O88898-1]
CCDS49810.1. [O88898-3]
RefSeqNP_001120731.1. NM_001127259.1. [O88898-1]
NP_001120732.1. NM_001127260.1. [O88898-3]
NP_001120733.1. NM_001127261.1. [O88898-5]
NP_001120734.1. NM_001127262.1. [O88898-4]
NP_001120736.1. NM_001127264.1.
NP_001120737.1. NM_001127265.1. [O88898-6]
NP_035771.1. NM_011641.2. [O88898-2]
UniGeneMm.20894.

3D structure databases

ProteinModelPortalO88898.
SMRO88898. Positions 153-437, 545-611.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204325. 5 interactions.
IntActO88898. 7 interactions.
MINTMINT-4585054.

PTM databases

PhosphoSiteO88898.

Proteomic databases

PaxDbO88898.
PRIDEO88898.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000040231; ENSMUSP00000038117; ENSMUSG00000022510. [O88898-2]
ENSMUST00000065523; ENSMUSP00000067005; ENSMUSG00000022510. [O88898-3]
ENSMUST00000115304; ENSMUSP00000110959; ENSMUSG00000022510.
ENSMUST00000115308; ENSMUSP00000110963; ENSMUSG00000022510. [O88898-5]
ENSMUST00000115310; ENSMUSP00000110965; ENSMUSG00000022510. [O88898-1]
GeneID22061.
KEGGmmu:22061.
UCSCuc007yuo.2. mouse. [O88898-5]
uc007yup.2. mouse. [O88898-1]
uc007yuq.2. mouse. [O88898-3]
uc007yut.2. mouse. [O88898-6]
uc007yuu.2. mouse. [O88898-2]
uc007yuv.2. mouse. [O88898-4]

Organism-specific databases

CTD22061.
MGIMGI:1330810. Trp63.

Phylogenomic databases

eggNOGNOG80479.
GeneTreeENSGT00390000015092.
HOVERGENHBG005201.
InParanoidO88898.
KOK10149.
OMAQRNTLTP.
OrthoDBEOG7JQBNW.
PhylomeDBO88898.
TreeFamTF106101.

Gene expression databases

ArrayExpressO88898.
BgeeO88898.
CleanExMM_TRP63.
GenevestigatorO88898.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
2.60.40.720. 1 hit.
4.10.170.10. 1 hit.
InterProIPR008967. 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]
PANTHERPTHR11447. PTHR11447. 1 hit.
PfamPF00870. P53. 1 hit.
PF07710. P53_tetramer. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
PRINTSPR00386. P53SUPPRESSR.
SMARTSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMSSF47719. SSF47719. 1 hit.
SSF47769. SSF47769. 1 hit.
SSF49417. SSF49417. 1 hit.
PROSITEPS00348. P53. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio301864.
PROO88898.
SOURCESearch...

Entry information

Entry nameP63_MOUSE
AccessionPrimary (citable) accession number: O88898
Secondary accession number(s): O88897 expand/collapse secondary AC list , O88899, O89097, Q8C826, Q9QWY9, Q9QWZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot