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O88898

- P63_MOUSE

UniProt

O88898 - P63_MOUSE

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Protein

Tumor protein 63

Gene

Tp63

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity5 Publications

Cofactori

Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi244 – 2441ZincBy similarity
Metal bindingi247 – 2471ZincBy similarity
Metal bindingi308 – 3081ZincBy similarity
Metal bindingi312 – 3121ZincBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi170 – 362193By similarityAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: MGI
  2. damaged DNA binding Source: MGI
  3. DNA binding Source: MGI
  4. double-stranded DNA binding Source: RefGenome
  5. identical protein binding Source: IntAct
  6. metal ion binding Source: UniProtKB-KW
  7. p53 binding Source: RefGenome
  8. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
  9. sequence-specific DNA binding Source: MGI
  10. sequence-specific DNA binding transcription factor activity Source: RefGenome
  11. transcription factor binding transcription factor activity Source: MGI
  12. transcription regulatory region DNA binding Source: InterPro

GO - Biological processi

  1. anatomical structure formation involved in morphogenesis Source: MGI
  2. apoptotic process Source: MGI
  3. cell aging Source: MGI
  4. cell differentiation Source: MGI
  5. cellular response to UV Source: RefGenome
  6. chromatin remodeling Source: MGI
  7. cloacal septation Source: MGI
  8. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: RefGenome
  9. ectoderm and mesoderm interaction Source: MGI
  10. embryonic limb morphogenesis Source: MGI
  11. epidermal cell division Source: MGI
  12. epidermis development Source: MGI
  13. epithelial cell development Source: MGI
  14. epithelial cell differentiation Source: MGI
  15. establishment of planar polarity Source: MGI
  16. establishment of skin barrier Source: UniProtKB
  17. female genitalia morphogenesis Source: MGI
  18. hair follicle development Source: MGI
  19. hair follicle morphogenesis Source: MGI
  20. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: MGI
  21. keratinocyte differentiation Source: MGI
  22. keratinocyte proliferation Source: MGI
  23. mitotic G1 DNA damage checkpoint Source: RefGenome
  24. morphogenesis of a polarized epithelium Source: MGI
  25. multicellular organismal aging Source: MGI
  26. multicellular organismal development Source: MGI
  27. negative regulation of apoptotic process Source: MGI
  28. negative regulation of cellular senescence Source: Ensembl
  29. negative regulation of keratinocyte differentiation Source: MGI
  30. negative regulation of mesoderm development Source: MGI
  31. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  32. neuron apoptotic process Source: MGI
  33. Notch signaling pathway Source: UniProtKB-KW
  34. odontogenesis of dentin-containing tooth Source: MGI
  35. organ morphogenesis Source: MGI
  36. pattern specification process Source: MGI
  37. polarized epithelial cell differentiation Source: MGI
  38. positive regulation of apoptotic signaling pathway Source: MGI
  39. positive regulation of cell cycle G1/S phase transition Source: Ensembl
  40. positive regulation of fibroblast apoptotic process Source: Ensembl
  41. positive regulation of keratinocyte proliferation Source: MGI
  42. positive regulation of mesenchymal cell proliferation Source: MGI
  43. positive regulation of Notch signaling pathway Source: MGI
  44. positive regulation of osteoblast differentiation Source: Ensembl
  45. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  46. post-anal tail morphogenesis Source: MGI
  47. prostate gland development Source: MGI
  48. prostatic bud formation Source: MGI
  49. protein homotetramerization Source: Ensembl
  50. proximal/distal pattern formation Source: MGI
  51. regulation of epidermal cell division Source: UniProtKB
  52. regulation of neuron apoptotic process Source: RefGenome
  53. response to gamma radiation Source: RefGenome
  54. response to X-ray Source: RefGenome
  55. skeletal system development Source: MGI
  56. skin morphogenesis Source: MGI
  57. smooth muscle tissue development Source: MGI
  58. squamous basal epithelial stem cell differentiation involved in prostate gland acinus development Source: MGI
  59. sympathetic nervous system development Source: MGI
  60. urinary bladder development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Apoptosis, Notch signaling pathway, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
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 namesi
Name:Tp63
Synonyms:P63, P73l, Tp73l, Trp63
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:1330810. Trp63.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. chromatin Source: RefGenome
  2. cytosol Source: RefGenome
  3. dendrite Source: RefGenome
  4. nuclear chromatin Source: Ensembl
  5. nucleoplasm Source: Ensembl
  6. nucleus Source: MGI
  7. transcription factor complex Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi543 – 5431Y → F: Abolishes interaction with WWP1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 680680Tumor protein 63PRO_0000185730Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki676 – 676Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Post-translational modificationi

May be sumoylated.By similarity
Ubiquitinated. Polyubiquitination involves WWP1 and leads to proteasomal degradation of this protein.1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiO88898.
PRIDEiO88898.

PTM databases

PhosphoSiteiO88898.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

TA*-type isoforms are expressed from E7.5, prior to the onset of epithelial stratification, while DeltaN-type isoforms are expressed from E9.5.1 Publication

Inductioni

Induced by DNA damaging agents.1 Publication

Gene expression databases

BgeeiO88898.
CleanExiMM_TRP63.
ExpressionAtlasiO88898. baseline and differential.
GenevestigatoriO88898.

Interactioni

Subunit structurei

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.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-2338025,EBI-2338025
Cables1Q9ESJ12EBI-2338025,EBI-604411
KAT2BQ928313EBI-2338228,EBI-477430From a different organism.
NQO1P155592EBI-2338228,EBI-3989435From a different organism.
TP53P046372EBI-2338025,EBI-366083From a different organism.

Protein-protein interaction databases

BioGridi204325. 5 interactions.
IntActiO88898. 7 interactions.
MINTiMINT-4585054.

Structurei

3D structure databases

ProteinModelPortaliO88898.
SMRiO88898. Positions 153-437, 545-611.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini541 – 60767SAMAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 107107Transcription activationBy similarityAdd
BLAST
Regioni352 – 38837Interaction with HIPK2By similarityAdd
BLAST
Regioni394 – 44350OligomerizationBy similarityAdd
BLAST
Regioni610 – 68071Transactivation inhibitionBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi437 – 4448Poly-Gln

Domaini

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

Sequence similaritiesi

Belongs to the p53 family.Curated

Phylogenomic databases

eggNOGiNOG80479.
GeneTreeiENSGT00390000015092.
HOVERGENiHBG005201.
InParanoidiO88898.
KOiK10149.
OMAiQRNTLTP.
OrthoDBiEOG7JQBNW.
PhylomeDBiO88898.
TreeFamiTF106101.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
2.60.40.720. 1 hit.
4.10.170.10. 1 hit.
InterProiIPR008967. 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]
PANTHERiPTHR11447. PTHR11447. 1 hit.
PfamiPF00870. P53. 1 hit.
PF07710. P53_tetramer. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
PRINTSiPR00386. P53SUPPRESSR.
SMARTiSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47719. SSF47719. 1 hit.
SSF47769. SSF47769. 1 hit.
SSF49417. SSF49417. 1 hit.
PROSITEiPS00348. P53. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative promoter usage and alternative splicing. Align

Isoform 1 (identifier: O88898-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MNFETSRCAT LQYCPDPYIQ RFIETPAHFS WKESYYRSAM SQSTQTSEFL
60 70 80 90 100
SPEVFQHIWD FLEQPICSVQ PIELNFVDEP SENGATNKIE ISMDCIRMQD
110 120 130 140 150
SDLSDPMWPQ YTNLGLLNSM DQQIQNGSSS TSPYNTDHAQ NSVTAPSPYA
160 170 180 190 200
QPSSTFDALS PSPAIPSNTD YPGPHSFDVS FQQSSTAKSA TWTYSTELKK
210 220 230 240 250
LYCQIAKTCP IQIKVMTPPP QGAVIRAMPV YKKAEHVTEV VKRCPNHELS
260 270 280 290 300
REFNEGQIAP PSHLIRVEGN SHAQYVEDPI TGRQSVLVPY EPPQVGTEFT
310 320 330 340 350
TVLYNFMCNS SCVGGMNRRP ILIIVTLETR DGQVLGRRCF EARICACPGR
360 370 380 390 400
DRKADEDSIR KQQVSDSAKN GDGTKRPFRQ NTHGIQMTSI KKRRSPDDEL
410 420 430 440 450
LYLPVRGRET YEMLLKIKES LELMQYLPQH TIETYRQQQQ QQHQHLLQKQ
460 470 480 490 500
TSMQSQSSYG NSSPPLNKMN SMNKLPSVSQ LINPQQRNAL TPTTMPEGMG
510 520 530 540 550
ANIPMMGTHM PMAGDMNGLS PTQALPPPLS MPSTSHCTPP PPYPTDCSIV
560 570 580 590 600
SFLARLGCSS CLDYFTTQGL TTIYQIEHYS MDDLASLKIP EQFRHAIWKG
610 620 630 640 650
ILDHRQLHDF SSPPHLLRTP SGASTVSVGS SETRGERVID AVRFTLRQTI
660 670 680
SFPPRDEWND FNFDMDSRRN KQQRIKEEGE

Note: Produced by alternative promoter usage.

Length:680
Mass (Da):76,789
Last modified:November 1, 1998 - v1
Checksum:i8DFF0284F247C68A
GO
Isoform 2 (identifier: O88898-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:586
Mass (Da):65,789
Checksum:i622E24085B8BDCB7
GO
Isoform 3 (identifier: O88898-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:555
Mass (Da):62,455
Checksum:i059E034046EB8987
GO
Isoform 4 (identifier: O88898-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:461
Mass (Da):51,455
Checksum:i7613296F2F85DBC8
GO
Isoform 5 (identifier: O88898-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:483
Mass (Da):54,970
Checksum:iA90ED0C110C50EAD
GO
Isoform 6 (identifier: O88898-6) [UniParc]FASTAAdd to Basket

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.

Show »
Length:389
Mass (Da):43,970
Checksum:iFE6B4A859C5F00BB
GO

Sequence cautioni

The sequence BAC33397.1 differs from that shown. Reason: Intron retention.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 108108MNFET…SDPMW → MLYLENNAQTQFSE in isoform 2, isoform 4 and isoform 6. 3 PublicationsVSP_012471Add
BLAST
Alternative sequencei373 – 3775GTKRP → A in isoform 5 and isoform 6. 1 PublicationVSP_012472
Alternative sequencei450 – 680231QTSMQ…KEEGE → HLLSACFRNELVEPRGEAPT QSDVFFRHSNPPNHSVYP in isoform 5 and isoform 6. 1 PublicationVSP_012473Add
BLAST
Alternative sequencei551 – 680130SFLAR…KEEGE → RIWQV in isoform 3 and isoform 4. 2 PublicationsVSP_012474Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS28085.1. [O88898-2]
CCDS49808.1. [O88898-5]
CCDS49809.1. [O88898-1]
CCDS49810.1. [O88898-3]
RefSeqiNP_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]
UniGeneiMm.20894.

Genome annotation databases

EnsembliENSMUST00000040231; ENSMUSP00000038117; ENSMUSG00000022510. [O88898-2]
ENSMUST00000065523; ENSMUSP00000067005; ENSMUSG00000022510. [O88898-3]
ENSMUST00000115304; ENSMUSP00000110959; ENSMUSG00000022510.
ENSMUST00000115308; ENSMUSP00000110963; ENSMUSG00000022510. [O88898-5]
ENSMUST00000115310; ENSMUSP00000110965; ENSMUSG00000022510. [O88898-1]
GeneIDi22061.
KEGGimmu:22061.
UCSCiuc007yuo.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]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS28085.1. [O88898-2 ]
CCDS49808.1. [O88898-5 ]
CCDS49809.1. [O88898-1 ]
CCDS49810.1. [O88898-3 ]
RefSeqi NP_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 ]
UniGenei Mm.20894.

3D structure databases

ProteinModelPortali O88898.
SMRi O88898. Positions 153-437, 545-611.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204325. 5 interactions.
IntActi O88898. 7 interactions.
MINTi MINT-4585054.

PTM databases

PhosphoSitei O88898.

Proteomic databases

PaxDbi O88898.
PRIDEi O88898.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000040231 ; ENSMUSP00000038117 ; ENSMUSG00000022510 . [O88898-2 ]
ENSMUST00000065523 ; ENSMUSP00000067005 ; ENSMUSG00000022510 . [O88898-3 ]
ENSMUST00000115304 ; ENSMUSP00000110959 ; ENSMUSG00000022510 .
ENSMUST00000115308 ; ENSMUSP00000110963 ; ENSMUSG00000022510 . [O88898-5 ]
ENSMUST00000115310 ; ENSMUSP00000110965 ; ENSMUSG00000022510 . [O88898-1 ]
GeneIDi 22061.
KEGGi mmu:22061.
UCSCi uc007yuo.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

CTDi 22061.
MGIi MGI:1330810. Trp63.

Phylogenomic databases

eggNOGi NOG80479.
GeneTreei ENSGT00390000015092.
HOVERGENi HBG005201.
InParanoidi O88898.
KOi K10149.
OMAi QRNTLTP.
OrthoDBi EOG7JQBNW.
PhylomeDBi O88898.
TreeFami TF106101.

Miscellaneous databases

NextBioi 301864.
PROi O88898.
SOURCEi Search...

Gene expression databases

Bgeei O88898.
CleanExi MM_TRP63.
ExpressionAtlasi O88898. baseline and differential.
Genevestigatori O88898.

Family and domain databases

Gene3Di 1.10.150.50. 1 hit.
2.60.40.720. 1 hit.
4.10.170.10. 1 hit.
InterProi 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 ]
PANTHERi PTHR11447. PTHR11447. 1 hit.
Pfami PF00870. P53. 1 hit.
PF07710. P53_tetramer. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view ]
PRINTSi PR00386. P53SUPPRESSR.
SMARTi SM00454. SAM. 1 hit.
[Graphical view ]
SUPFAMi SSF47719. SSF47719. 1 hit.
SSF47769. SSF47769. 1 hit.
SSF49417. SSF49417. 1 hit.
PROSITEi PS00348. P53. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: FUNCTION IN RIPK4 TRANSACTIVATION.

Entry informationi

Entry nameiP63_MOUSE
AccessioniPrimary (citable) accession number: O88898
Secondary accession number(s): O88897
, O88899, O89097, Q8C826, Q9QWY9, Q9QWZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: November 1, 1998
Last modified: October 29, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3