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O88898

- P63_MOUSE

UniProt

O88898 - P63_MOUSE

Protein

Tumor protein 63

Gene

Tp63

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    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. protein binding Source: IntAct
    9. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
    10. sequence-specific DNA binding Source: MGI
    11. sequence-specific DNA binding transcription factor activity Source: RefGenome
    12. transcription factor binding transcription factor activity Source: MGI
    13. 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 keratinocyte differentiation Source: MGI
    29. negative regulation of mesoderm development Source: MGI
    30. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    31. neuron apoptotic process Source: MGI
    32. Notch signaling pathway Source: UniProtKB-KW
    33. odontogenesis of dentin-containing tooth Source: MGI
    34. organ morphogenesis Source: MGI
    35. pattern specification process Source: MGI
    36. polarized epithelial cell differentiation Source: MGI
    37. positive regulation of apoptotic signaling pathway Source: MGI
    38. positive regulation of fibroblast apoptotic process Source: Ensembl
    39. positive regulation of keratinocyte proliferation Source: MGI
    40. positive regulation of mesenchymal cell proliferation Source: MGI
    41. positive regulation of Notch signaling pathway Source: MGI
    42. positive regulation of osteoblast differentiation Source: Ensembl
    43. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    44. post-anal tail morphogenesis Source: MGI
    45. prostate gland development Source: MGI
    46. prostatic bud formation Source: MGI
    47. protein homotetramerization Source: Ensembl
    48. proximal/distal pattern formation Source: MGI
    49. regulation of epidermal cell division Source: UniProtKB
    50. regulation of neuron apoptotic process Source: RefGenome
    51. response to gamma radiation Source: RefGenome
    52. response to X-ray Source: RefGenome
    53. skeletal system development Source: MGI
    54. skin morphogenesis Source: MGI
    55. smooth muscle tissue development Source: MGI
    56. squamous basal epithelial stem cell differentiation involved in prostate gland acinus development Source: MGI
    57. sympathetic nervous system development Source: MGI
    58. urinary bladder development Source: MGI

    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. Golgi apparatus Source: Ensembl
    5. nuclear chromatin Source: Ensembl
    6. nucleoplasm Source: Ensembl
    7. nucleus Source: MGI
    8. transcription factor complex Source: RefGenome

    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

    ArrayExpressiO88898.
    BgeeiO88898.
    CleanExiMM_TRP63.
    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-2338244,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

    MNFETSRCAT LQYCPDPYIQ RFIETPAHFS WKESYYRSAM SQSTQTSEFL    50
    SPEVFQHIWD FLEQPICSVQ PIELNFVDEP SENGATNKIE ISMDCIRMQD 100
    SDLSDPMWPQ YTNLGLLNSM DQQIQNGSSS TSPYNTDHAQ NSVTAPSPYA 150
    QPSSTFDALS PSPAIPSNTD YPGPHSFDVS FQQSSTAKSA TWTYSTELKK 200
    LYCQIAKTCP IQIKVMTPPP QGAVIRAMPV YKKAEHVTEV VKRCPNHELS 250
    REFNEGQIAP PSHLIRVEGN SHAQYVEDPI TGRQSVLVPY EPPQVGTEFT 300
    TVLYNFMCNS SCVGGMNRRP ILIIVTLETR DGQVLGRRCF EARICACPGR 350
    DRKADEDSIR KQQVSDSAKN GDGTKRPFRQ NTHGIQMTSI KKRRSPDDEL 400
    LYLPVRGRET YEMLLKIKES LELMQYLPQH TIETYRQQQQ QQHQHLLQKQ 450
    TSMQSQSSYG NSSPPLNKMN SMNKLPSVSQ LINPQQRNAL TPTTMPEGMG 500
    ANIPMMGTHM PMAGDMNGLS PTQALPPPLS MPSTSHCTPP PPYPTDCSIV 550
    SFLARLGCSS CLDYFTTQGL TTIYQIEHYS MDDLASLKIP EQFRHAIWKG 600
    ILDHRQLHDF SSPPHLLRTP SGASTVSVGS SETRGERVID AVRFTLRQTI 650
    SFPPRDEWND FNFDMDSRRN KQQRIKEEGE 680

    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

    ArrayExpressi O88898.
    Bgeei O88898.
    CleanExi MM_TRP63.
    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

    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 1, 2014
    This is version 136 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