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Q9H3D4

- P63_HUMAN

UniProt

Q9H3D4 - P63_HUMAN

Protein

Tumor protein 63

Gene

TP63

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      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. Isoform 2 activates RIPK4 transcription. 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. Plays a role in the regulation of epithelial morphogenesis. The ratio of DeltaN-type and TA*-type isoforms may govern the maintenance of epithelial stem cell compartments and regulate the initiation of epithelial stratification from the undifferentiated embryonal ectoderm. Required for limb formation from the apical ectodermal ridge. Activates transcription of the p21 promoter.7 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 – 362193Add
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: RefGenome
    2. damaged DNA binding Source: RefGenome
    3. DNA binding Source: UniProtKB
    4. double-stranded DNA binding Source: RefGenome
    5. identical protein binding Source: UniProtKB
    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: Ensembl
    10. sequence-specific DNA binding Source: RefGenome
    11. sequence-specific DNA binding transcription factor activity Source: RefGenome
    12. transcription regulatory region DNA binding Source: InterPro
    13. WW domain binding Source: UniProt

    GO - Biological processi

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

    Keywords - Molecular functioni

    Activator, Developmental protein

    Keywords - Biological processi

    Apoptosis, Notch signaling pathway, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ9H3D4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tumor protein 63
    Short name:
    p63
    Alternative name(s):
    Chronic ulcerative stomatitis protein
    Short name:
    CUSP
    Keratinocyte transcription factor KET
    Transformation-related protein 63
    Short name:
    TP63
    Tumor protein p73-like
    Short name:
    p73L
    p40
    p51
    Gene namesi
    Name:TP63
    Synonyms:KET, P63, P73H, P73L, TP73L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:15979. TP63.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. chromatin Source: RefGenome
    2. cytoplasm Source: MGI
    3. cytosol Source: RefGenome
    4. dendrite Source: RefGenome
    5. nuclear chromatin Source: BHF-UCL
    6. nucleoplasm Source: UniProtKB
    7. nucleus Source: UniProtKB
    8. transcription factor complex Source: RefGenome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Acro-dermato-ungual-lacrimal-tooth syndrome (ADULT syndrome) [MIM:103285]: A form of ectodermal dysplasia. Ectodermal dysplasia defines a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. ADULT syndrome involves ectrodactyly, syndactyly, finger- and toenail dysplasia, hypoplastic breasts and nipples, intensive freckling, lacrimal duct atresia, frontal alopecia, primary hypodontia and loss of permanent teeth. ADULT syndrome differs significantly from EEC3 syndrome by the absence of facial clefting.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti337 – 3371R → Q in ADULT syndrome; confers novel transcription activation capacity on isoform 6. 1 Publication
    VAR_020875
    Isoform 2 (identifier: Q9H3D4-2)
    Natural varianti6 – 61N → H in ADULT syndrome.
    Isoform 4 (identifier: Q9H3D4-4)
    Natural varianti6 – 61N → H in ADULT syndrome.
    Isoform 6 (identifier: Q9H3D4-6)
    Natural varianti6 – 61N → H in ADULT syndrome.
    Isoform 8 (identifier: Q9H3D4-8)
    Natural varianti6 – 61N → H in ADULT syndrome.
    Isoform 10 (identifier: Q9H3D4-10)
    Natural varianti6 – 61N → H in ADULT syndrome.
    Isoform 12 (identifier: Q9H3D4-12)
    Natural varianti6 – 61N → H in ADULT syndrome.
    Ankyloblepharon-ectodermal defects-cleft lip/palate (AEC) [MIM:106260]: An autosomal dominant condition characterized by congenital ectodermal dysplasia with coarse, wiry, sparse hair, dystrophic nails, slight hypohidrosis, scalp infections, ankyloblepharon filiform adnatum, maxillary hypoplasia, hypodontia and cleft lip/palate.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti553 – 5531L → F in AEC. 1 Publication
    VAR_020879
    Natural varianti561 – 5611C → G in AEC. 1 Publication
    VAR_020881
    Ectrodactyly, ectodermal dysplasia, and cleft lip/palate syndrome 3 (EEC3) [MIM:604292]: A form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. It is an autosomal dominant syndrome characterized by ectrodactyly of hands and feet, ectodermal dysplasia and facial clefting.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti243 – 2431R → Q in EEC3. 2 Publications
    VAR_020870
    Natural varianti243 – 2431R → W in EEC3. 2 Publications
    VAR_020871
    Natural varianti266 – 2661R → Q in EEC3. 1 Publication
    VAR_032738
    Natural varianti308 – 3081C → Y in EEC3. 1 Publication
    VAR_032739
    Natural varianti311 – 3111S → N in EEC3. 1 Publication
    VAR_032740
    Natural varianti318 – 3181R → C in EEC3. 1 Publication
    VAR_032741
    Natural varianti318 – 3181R → H in EEC3 and EDRH; does not decrease the transcriptional activity of the isoform 5 on a TP53 reporter system but disrupts the dominant-negative activity of isoform 2 and isoform 5 on the transcriptional activity of TP53. 3 Publications
    VAR_020873
    Natural varianti318 – 3181R → Q in EEC3. 1 Publication
    VAR_032742
    Natural varianti319 – 3191R → C in EEC3. 2 Publications
    VAR_020874
    Natural varianti319 – 3191R → H in EEC3 and SHFM4. 1 Publication
    VAR_032743
    Natural varianti319 – 3191R → S in EEC3. 1 Publication
    VAR_032744
    Natural varianti343 – 3431R → Q in EEC3. 2 Publications
    VAR_020876
    Natural varianti343 – 3431R → W in EEC3. 1 Publication
    VAR_032745
    Natural varianti345 – 3451C → R in EEC3; abolishes transcription activation. 2 Publications
    VAR_020877
    Natural varianti347 – 3471C → S in EEC3. 1 Publication
    VAR_032746
    Natural varianti348 – 3481P → S in EEC3. 1 Publication
    VAR_032747
    Natural varianti351 – 3511D → G in EEC3. 1 Publication
    VAR_020878
    Natural varianti351 – 3511D → H in EEC3. 1 Publication
    VAR_032748
    Split-hand/foot malformation 4 (SHFM4) [MIM:605289]: A limb malformation involving the central rays of the autopod and presenting with syndactyly, median clefts of the hands and feet, and aplasia and/or hypoplasia of the phalanges, metacarpals, and metatarsals. Some patients have been found to have mental retardation, ectodermal and craniofacial findings, and orofacial clefting.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti193 – 1931T → TP in SHFM4. 1 Publication
    VAR_032736
    Natural varianti232 – 2321K → E in SHFM4. 1 Publication
    VAR_032737
    Natural varianti233 – 2331K → E in SHFM4. 1 Publication
    VAR_020869
    Natural varianti319 – 3191R → H in EEC3 and SHFM4. 1 Publication
    VAR_032743
    Limb-mammary syndrome (LMS) [MIM:603543]: Characterized by ectrodactyly, cleft palate and mammary-gland abnormalities.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Defects in TP63 are a cause of cervical, colon, head and neck, lung and ovarian cancers.
    Ectodermal dysplasia, Rapp-Hodgkin type (EDRH) [MIM:129400]: A form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Characterized by the combination of anhidrotic ectodermal dysplasia, cleft lip, and cleft palate. The clinical syndrome is comprised of a characteristic facies (narrow nose and small mouth), wiry, slow-growing, and uncombable hair, sparse eyelashes and eyebrows, obstructed lacrimal puncta/epiphora, bilateral stenosis of external auditory canals, microsomia, hypodontia, cone-shaped incisors, enamel hypoplasia, dystrophic nails, and cleft lip/cleft palate.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti318 – 3181R → H in EEC3 and EDRH; does not decrease the transcriptional activity of the isoform 5 on a TP53 reporter system but disrupts the dominant-negative activity of isoform 2 and isoform 5 on the transcriptional activity of TP53. 3 Publications
    VAR_020873
    Natural varianti352 – 3521R → G in EDRH and OFC8. 1 Publication
    VAR_035127
    Natural varianti549 – 5491I → T in EDRH. 1 Publication
    VAR_035128
    Natural varianti580 – 5801S → P in EDRH. 1 Publication
    VAR_035129
    Non-syndromic orofacial cleft 8 (OFC8) [MIM:129400]: A birth defect consisting of cleft lips with or without cleft palate. Cleft lips are associated with cleft palate in two-third of cases. A cleft lip can occur on one or both sides and range in severity from a simple notch in the upper lip to a complete opening in the lip extending into the floor of the nostril and involving the upper gum.
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti352 – 3521R → G in EDRH and OFC8. 1 Publication
    VAR_035127

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi55 – 551F → A: Abrogates transcriptional activity and interaction with transactivation inhibition domain; when associated with A-59 and A-62. 1 Publication
    Mutagenesisi59 – 591W → A: Abrogates transcriptional activity and interaction with transactivation inhibition domain; when associated with A-55 and A-62. 1 Publication
    Mutagenesisi62 – 621L → A: Abrogates transcriptional activity and interaction with transactivation inhibition domain; when associated with A-55 and A-59. 1 Publication
    Mutagenesisi543 – 5431Y → F: Abolishes ubiquitination. 1 Publication

    Keywords - Diseasei

    Disease mutation, Ectodermal dysplasia

    Organism-specific databases

    MIMi103285. phenotype.
    106260. phenotype.
    129400. phenotype.
    603543. phenotype.
    604292. phenotype.
    605289. phenotype.
    Orphaneti978. ADULT syndrome.
    1071. Ankyloblepharon - ectodermal defects - cleft lip/palate.
    93930. Bladder exstrophy.
    1991. Cleft lip with or without cleft palate.
    1896. EEC syndrome.
    69085. Limb-mammary syndrome.
    3022. Rapp-Hodgkin syndrome.
    2440. Split hand-split foot malformation.
    PharmGKBiPA162406776.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 680680Tumor protein 63PRO_0000185729Add
    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

    MaxQBiQ9H3D4.
    PaxDbiQ9H3D4.
    PRIDEiQ9H3D4.

    PTM databases

    PhosphoSiteiQ9H3D4.

    Expressioni

    Tissue specificityi

    Widely expressed, notably in heart, kidney, placenta, prostate, skeletal muscle, testis and thymus, although the precise isoform varies according to tissue type. Progenitor cell layers of skin, breast, eye and prostate express high levels of DeltaN-type isoforms. Isoform 10 is predominantly expressed in skin squamous cell carcinomas, but not in normal skin tissues.2 Publications

    Gene expression databases

    ArrayExpressiQ9H3D4.
    BgeeiQ9H3D4.
    GenevestigatoriQ9H3D4.

    Organism-specific databases

    HPAiCAB000083.
    HPA006288.
    HPA007010.

    Interactioni

    Subunit structurei

    Binds DNA as a homotetramer. Isoform composition of the tetramer may determine transactivation activity. Isoforms Alpha and Gamma interact with HIPK2. Interacts with SSRP1, leading to stimulate coactivator activity. Isoform 1 and isoform 2 interact with WWP1. Interacts with PDS5A. Isoform 5 (via activation domain) interacts with NOC2L.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CABLES1Q8TDN47EBI-2400586,EBI-604615
    FUSP356372EBI-2337775,EBI-400434
    HNRNPKP619782EBI-2337775,EBI-304185
    NIPSNAP3AQ9UFN02EBI-2337775,EBI-716291
    SATB2Q9UPW65EBI-6481107,EBI-8298169
    SMAD2Q157963EBI-2337775,EBI-1040141
    TP53P046375EBI-2337775,EBI-366083

    Protein-protein interaction databases

    BioGridi114181. 117 interactions.
    DIPiDIP-29588N.
    IntActiQ9H3D4. 64 interactions.
    MINTiMINT-190238.

    Structurei

    Secondary structure

    1
    680
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi156 – 1616
    Helixi173 – 1753
    Beta strandi178 – 1803
    Beta strandi187 – 1893
    Beta strandi191 – 1955
    Turni196 – 1994
    Beta strandi200 – 2034
    Beta strandi209 – 2146
    Beta strandi224 – 23310
    Turni234 – 2385
    Helixi245 – 2495
    Turni252 – 2565
    Beta strandi263 – 2697
    Beta strandi274 – 2774
    Turni279 – 2813
    Beta strandi284 – 2896
    Beta strandi300 – 3067
    Turni313 – 3186
    Beta strandi321 – 3288
    Beta strandi330 – 3323
    Beta strandi334 – 34310
    Helixi348 – 3558
    Beta strandi369 – 3724
    Beta strandi401 – 4077
    Helixi408 – 42619
    Helixi429 – 4368
    Beta strandi546 – 5483
    Helixi549 – 5546
    Turni555 – 5573
    Helixi559 – 5613
    Helixi562 – 5665
    Turni567 – 5693
    Helixi573 – 5764
    Helixi581 – 5866
    Helixi591 – 60919
    Beta strandi613 – 6153

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RG6NMR-A540-614[»]
    2RMNNMR-A153-388[»]
    2Y9TNMR-A543-622[»]
    2Y9UX-ray1.60A545-611[»]
    3QYMX-ray3.20A/B/C/D/E/F/G/H166-362[»]
    3QYNX-ray2.50A/B/C/D166-362[»]
    3US0X-ray2.50A/B/C/D166-362[»]
    3US1X-ray2.80A/D166-362[»]
    3US2X-ray4.20A/B/C/D/G/H/I/J166-362[»]
    3ZY0X-ray1.90A/B/C/D398-427[»]
    3ZY1X-ray2.15A398-441[»]
    4A9ZX-ray2.29A/B/C/D397-455[»]
    ProteinModelPortaliQ9H3D4.
    SMRiQ9H3D4. Positions 153-437, 543-622.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H3D4.

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 107107Transcription activationAdd
    BLAST
    Regioni352 – 38837Interaction with HIPK2Add
    BLAST
    Regioni394 – 44350OligomerizationAdd
    BLAST
    Regioni610 – 68071Transactivation inhibitionAdd
    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.2 Publications

    Sequence similaritiesi

    Belongs to the p53 family.Curated

    Phylogenomic databases

    eggNOGiNOG80479.
    HOVERGENiHBG005201.
    InParanoidiQ9H3D4.
    KOiK10149.
    OMAiQRNTLTP.
    OrthoDBiEOG7JQBNW.
    PhylomeDBiQ9H3D4.
    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 (12)i

    Sequence statusi: Complete.

    This entry describes 12 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform 1 (identifier: Q9H3D4-1) [UniParc]FASTAAdd to Basket

    Also known as: TA*-alpha, TAp63alpha, P51B

    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 RFVETPAHFS WKESYYRSTM SQSTQTNEFL    50
    SPEVFQHIWD FLEQPICSVQ PIDLNFVDEP SEDGATNKIE 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 KQQVSDSTKN GDGTKRPFRQ NTHGIQMTSI KKRRSPDDEL 400
    LYLPVRGRET YEMLLKIKES LELMQYLPQH TIETYRQQQQ QQHQHLLQKQ 450
    TSIQSPSSYG NSSPPLNKMN SMNKLPSVSQ LINPQQRNAL TPTTIPDGMG 500
    ANIPMMGTHM PMAGDMNGLS PTQALPPPLS MPSTSHCTPP PPYPTDCSIV 550
    SFLARLGCSS CLDYFTTQGL TTIYQIEHYS MDDLASLKIP EQFRHAIWKG 600
    ILDHRQLHEF SSPSHLLRTP SSASTVSVGS SETRGERVID AVRFTLRQTI 650
    SFPPRDEWND FNFDMDARRN KQQRIKEEGE 680

    Note: Produced by alternative promoter usage.

    Length:680
    Mass (Da):76,785
    Last modified:March 1, 2001 - v1
    Checksum:iF66ECD45E87D9799
    GO
    Isoform 2 (identifier: Q9H3D4-2) [UniParc]FASTAAdd to Basket

    Also known as: DeltaN-alpha, DeltaNp63 alpha, P51delNalpha

    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):65,756
    Checksum:i2E2F92ABF1AF8629
    GO
    Isoform 3 (identifier: Q9H3D4-3) [UniParc]FASTAAdd to Basket

    Also known as: TA*-beta, TAp63beta

    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):62,433
    Checksum:iE22874BE7DBABCBE
    GO
    Isoform 4 (identifier: Q9H3D4-4) [UniParc]FASTAAdd to Basket

    Also known as: DeltaN-beta, DeltaNp63 beta, P51delNbeta

    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):51,404
    Checksum:i68B63547A46C1B05
    GO
    Isoform 5 (identifier: Q9H3D4-5) [UniParc]FASTAAdd to Basket

    Also known as: TA*-gamma, TAp63gamma, P51A

    The sequence of this isoform differs from the canonical sequence as follows:
         450-680: QTSIQSPSSY...KQQRIKEEGE → HLLSACFRNE...SKPPNRSVYP

    Note: Produced by alternative splicing of isoform 1.

    Show »
    Length:487
    Mass (Da):55,688
    Checksum:i86CC865BDF2643DD
    GO
    Isoform 6 (identifier: Q9H3D4-6) [UniParc]FASTAAdd to Basket

    Also known as: DeltaN-gamma, DeltaNp63gamma, P51delNgamma

    The sequence of this isoform differs from the canonical sequence as follows:
         1-108: MNFETSRCAT...QDSDLSDPMW → MLYLENNAQTQFSE
         450-680: QTSIQSPSSY...KQQRIKEEGE → HLLSACFRNE...SKPPNRSVYP

    Note: Produced by alternative splicing of isoform 2.

    Show »
    Length:393
    Mass (Da):44,658
    Checksum:iC6689B83FD701610
    GO
    Isoform 7 (identifier: Q9H3D4-7) [UniParc]FASTAAdd to Basket

    Also known as: TA*-delta, TAp63delta, P51delta

    The sequence of this isoform differs from the canonical sequence as follows:
         503-680: IPMMGTHMPM...KQQRIKEEGE → RSGKSENP

    Note: Produced by alternative splicing of isoform 1.

    Show »
    Length:510
    Mass (Da):57,619
    Checksum:i3539D81485635FF0
    GO
    Isoform 8 (identifier: Q9H3D4-8) [UniParc]FASTAAdd to Basket

    Also known as: DeltaN-delta

    The sequence of this isoform differs from the canonical sequence as follows:
         1-108: MNFETSRCAT...QDSDLSDPMW → MLYLENNAQTQFSE
         503-680: IPMMGTHMPM...KQQRIKEEGE → RSGKSENP

    Note: Produced by alternative splicing of isoform 2. No experimental confirmation available.

    Show »
    Length:416
    Mass (Da):46,589
    Checksum:iA5974A14B25E3118
    GO
    Isoform 9 (identifier: Q9H3D4-9) [UniParc]FASTAAdd to Basket

    Also known as: TA*-epsilon

    The sequence of this isoform differs from the canonical sequence as follows:
         109-193: Missing.

    Note: Produced by alternative splicing of isoform 1. No experimental confirmation available.

    Show »
    Length:595
    Mass (Da):67,779
    Checksum:iF07014CB9FEF1FF2
    GO
    Isoform 10 (identifier: Q9H3D4-10) [UniParc]FASTAAdd to Basket

    Also known as: DeltaN-epsilon, DeltaNp73L

    The sequence of this isoform differs from the canonical sequence as follows:
         1-108: MNFETSRCAT...QDSDLSDPMW → MLYLENNAQTQFSE
         109-193: Missing.

    Note: Produced by alternative splicing of isoform 2.

    Show »
    Length:501
    Mass (Da):56,750
    Checksum:i31E1BEA3CA305B88
    GO
    Isoform 11 (identifier: Q9H3D4-11) [UniParc]FASTAAdd to Basket

    Also known as: P63 delta

    The sequence of this isoform differs from the canonical sequence as follows:
         373-377: GTKRP → A

    Note: Produced by alternative splicing of isoform 1.

    Show »
    Length:676
    Mass (Da):76,317
    Checksum:iEB0E2C9E93C6D34A
    GO
    Isoform 12 (identifier: Q9H3D4-12) [UniParc]FASTAAdd to Basket

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

    Note: Produced by alternative splicing of isoform 2. No experimental confirmation available.

    Show »
    Length:582
    Mass (Da):65,288
    Checksum:iA2DC3D2E13B6B531
    GO

    Sequence cautioni

    The sequence AAF61624.1 differs from that shown. Reason: Frameshift at position 26.
    The sequence BAA32592.1 differs from that shown. Reason: Frameshift at position 26.
    The sequence BAA32593.1 differs from that shown. Reason: Frameshift at position 26.
    The sequence AAF43486.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAF43487.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAF43488.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAF43489.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti125 – 1251Q → R in BAA32433. (PubMed:9703973)Curated
    Sequence conflicti154 – 1541S → P in BAA32433. (PubMed:9703973)Curated
    Sequence conflicti177 – 1771F → S in BAA32433. (PubMed:9703973)Curated
    Sequence conflicti378 – 3781F → S in AAC24830. (PubMed:9662346)Curated
    Sequence conflicti536 – 5361H → Q in CAA76562. (PubMed:9799841)Curated
    Sequence conflicti551 – 5511S → G in BAA32593. (PubMed:9662378)Curated
    Sequence conflicti551 – 5511S → G in AAF43487. (PubMed:10935472)Curated
    Sequence conflicti551 – 5511S → G in AAF43491. (PubMed:10935472)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti129 – 1291S → L.1 Publication
    Corresponds to variant rs193287780 [ dbSNP | Ensembl ].
    VAR_035126
    Natural varianti184 – 1841S → L in head and neck cancer. 1 Publication
    VAR_020866
    Natural varianti187 – 1871A → P in lung carcinoma; somatic mutation. 1 Publication
    VAR_020867
    Natural varianti193 – 1931T → TP in SHFM4. 1 Publication
    VAR_032736
    Natural varianti204 – 2041Q → L in cervical cancer. 1 Publication
    VAR_020868
    Natural varianti232 – 2321K → E in SHFM4. 1 Publication
    VAR_032737
    Natural varianti233 – 2331K → E in SHFM4. 1 Publication
    VAR_020869
    Natural varianti243 – 2431R → Q in EEC3. 2 Publications
    VAR_020870
    Natural varianti243 – 2431R → W in EEC3. 2 Publications
    VAR_020871
    Natural varianti266 – 2661R → Q in EEC3. 1 Publication
    VAR_032738
    Natural varianti279 – 2791P → H in colon cancer. 1 Publication
    VAR_020872
    Natural varianti308 – 3081C → Y in EEC3. 1 Publication
    VAR_032739
    Natural varianti311 – 3111S → N in EEC3. 1 Publication
    VAR_032740
    Natural varianti318 – 3181R → C in EEC3. 1 Publication
    VAR_032741
    Natural varianti318 – 3181R → H in EEC3 and EDRH; does not decrease the transcriptional activity of the isoform 5 on a TP53 reporter system but disrupts the dominant-negative activity of isoform 2 and isoform 5 on the transcriptional activity of TP53. 3 Publications
    VAR_020873
    Natural varianti318 – 3181R → Q in EEC3. 1 Publication
    VAR_032742
    Natural varianti319 – 3191R → C in EEC3. 2 Publications
    VAR_020874
    Natural varianti319 – 3191R → H in EEC3 and SHFM4. 1 Publication
    VAR_032743
    Natural varianti319 – 3191R → S in EEC3. 1 Publication
    VAR_032744
    Natural varianti337 – 3371R → Q in ADULT syndrome; confers novel transcription activation capacity on isoform 6. 1 Publication
    VAR_020875
    Natural varianti343 – 3431R → Q in EEC3. 2 Publications
    VAR_020876
    Natural varianti343 – 3431R → W in EEC3. 1 Publication
    VAR_032745
    Natural varianti345 – 3451C → R in EEC3; abolishes transcription activation. 2 Publications
    VAR_020877
    Natural varianti347 – 3471C → S in EEC3. 1 Publication
    VAR_032746
    Natural varianti348 – 3481P → S in EEC3. 1 Publication
    VAR_032747
    Natural varianti351 – 3511D → G in EEC3. 1 Publication
    VAR_020878
    Natural varianti351 – 3511D → H in EEC3. 1 Publication
    VAR_032748
    Natural varianti352 – 3521R → G in EDRH and OFC8. 1 Publication
    VAR_035127
    Natural varianti549 – 5491I → T in EDRH. 1 Publication
    VAR_035128
    Natural varianti553 – 5531L → F in AEC. 1 Publication
    VAR_020879
    Natural varianti560 – 5601S → A in ovarian cancer. 1 Publication
    VAR_020880
    Natural varianti561 – 5611C → G in AEC. 1 Publication
    VAR_020881
    Natural varianti580 – 5801S → P in EDRH. 1 Publication
    VAR_035129
    Natural varianti603 – 6031D → H.1 Publication
    VAR_035130
    Isoform 2 (identifier: Q9H3D4-2)
    Natural varianti6 – 61N → H in ADULT syndrome.
    Isoform 4 (identifier: Q9H3D4-4)
    Natural varianti6 – 61N → H in ADULT syndrome.
    Isoform 6 (identifier: Q9H3D4-6)
    Natural varianti6 – 61N → H in ADULT syndrome.
    Isoform 8 (identifier: Q9H3D4-8)
    Natural varianti6 – 61N → H in ADULT syndrome.
    Isoform 10 (identifier: Q9H3D4-10)
    Natural varianti6 – 61N → H in ADULT syndrome.
    Isoform 12 (identifier: Q9H3D4-12)
    Natural varianti6 – 61N → H in ADULT syndrome.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 108108MNFET…SDPMW → MLYLENNAQTQFSE in isoform 2, isoform 4, isoform 6, isoform 8, isoform 10 and isoform 12. 4 PublicationsVSP_012465Add
    BLAST
    Alternative sequencei109 – 19385Missing in isoform 9 and isoform 10. 1 PublicationVSP_012466Add
    BLAST
    Alternative sequencei373 – 3775GTKRP → A in isoform 11 and isoform 12. 1 PublicationVSP_012467
    Alternative sequencei450 – 680231QTSIQ…KEEGE → HLLSACFRNELVEPRRETPK QSDVFFRHSKPPNRSVYP in isoform 5 and isoform 6. 2 PublicationsVSP_012468Add
    BLAST
    Alternative sequencei503 – 680178IPMMG…KEEGE → RSGKSENP in isoform 7 and isoform 8. 1 PublicationVSP_012469Add
    BLAST
    Alternative sequencei551 – 680130SFLAR…KEEGE → RIWQV in isoform 3 and isoform 4. 1 PublicationVSP_012470Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB010153 mRNA. Translation: BAA32433.1.
    Y16961 mRNA. Translation: CAA76562.1.
    AF075428 mRNA. Translation: AAC62633.1.
    AF075429 mRNA. Translation: AAC62634.1.
    AF075430 mRNA. Translation: AAC62635.1.
    AF075431 mRNA. Translation: AAC62636.1.
    AF075432 mRNA. Translation: AAC62637.1.
    AF075433 mRNA. Translation: AAC62638.1.
    AF124539
    , AF124528, AF124529, AF124531, AF124532, AF124533, AF124534, AF124535, AF124536, AF124537, AF124538 Genomic DNA. Translation: AAG45607.1.
    AF124539
    , AF124528, AF124529, AF124531, AF124532, AF124533, AF124534, AF124535, AF124536, AF124537 Genomic DNA. Translation: AAG45608.1.
    AF124540
    , AF124528, AF124529, AF124531, AF124532, AF124533, AF124534, AF124535 Genomic DNA. Translation: AAG45609.1.
    AF124539
    , AF124530, AF124531, AF124532, AF124533, AF124534, AF124535, AF124536, AF124537, AF124538 Genomic DNA. Translation: AAG45610.1.
    AF124539
    , AF124530, AF124531, AF124532, AF124533, AF124534, AF124535, AF124536, AF124537 Genomic DNA. Translation: AAG45611.1.
    AF124540
    , AF124531, AF124533, AF124535, AF124534, AF124532, AF124530 Genomic DNA. Translation: AAG45612.1.
    AB016072 mRNA. Translation: BAA32592.1. Frameshift.
    AB016073 mRNA. Translation: BAA32593.1. Frameshift.
    AF091627 mRNA. Translation: AAC43038.1.
    AF116770
    , AF116756, AF116757, AF116759, AF116760, AF116761, AF116762, AF116763, AF116764, AF116765 Genomic DNA. Translation: AAF43486.1. Different initiation.
    AF116769
    , AF116756, AF116757, AF116759, AF116760, AF116761, AF116762, AF116763, AF116764, AF116765, AF116766, AF116767, AF116768 Genomic DNA. Translation: AAF43487.1. Different initiation.
    AF116769
    , AF116756, AF116759, AF116757, AF116762, AF116764, AF116766, AF116767, AF116765, AF116763, AF116761, AF116760 Genomic DNA. Translation: AAF43488.1. Different initiation.
    AF116769
    , AF116756, AF116757, AF116759, AF116760, AF116761, AF116762, AF116763, AF116764, AF116765, AF116766 Genomic DNA. Translation: AAF43489.1. Different initiation.
    AF116770
    , AF116758, AF116760, AF116762, AF116764, AF116765, AF116763, AF116761, AF116759 Genomic DNA. Translation: AAF43490.1.
    AF116769
    , AF116758, AF116759, AF116760, AF116764, AF116766, AF116768, AF116767, AF116765, AF116763, AF116762, AF116761 Genomic DNA. Translation: AAF43491.1.
    AF116769
    , AF116758, AF116760, AF116759, AF116761, AF116763, AF116765, AF116767, AF116766, AF116764, AF116762 Genomic DNA. Translation: AAF43492.1.
    AF116769
    , AF116758, AF116760, AF116759, AF116761, AF116763, AF116765, AF116766, AF116764, AF116762 Genomic DNA. Translation: AAF43493.1.
    AF116771 mRNA. Translation: AAF61624.1. Frameshift.
    AB042841 mRNA. Translation: BAB20591.1.
    BC039815 mRNA. Translation: AAH39815.1.
    AF061512 mRNA. Translation: AAC24830.1.
    AY342152, AY341145 Genomic DNA. Translation: AAQ63448.1.
    AY339663 Genomic DNA. Translation: AAQ63449.1.
    AY341143, AY339664, AY341142 Genomic DNA. Translation: AAQ63450.1.
    AY341143, AY341142 Genomic DNA. Translation: AAQ63451.1.
    AY341144 Genomic DNA. Translation: AAQ63452.1.
    AY342153 Genomic DNA. Translation: AAQ63453.1.
    AY342154 Genomic DNA. Translation: AAQ63454.1.
    AJ315499 mRNA. Translation: CAC48053.1.
    CCDSiCCDS3293.1. [Q9H3D4-1]
    CCDS46976.1. [Q9H3D4-3]
    CCDS46977.1. [Q9H3D4-5]
    CCDS46978.1. [Q9H3D4-2]
    CCDS46979.1. [Q9H3D4-4]
    CCDS46980.1. [Q9H3D4-6]
    RefSeqiNP_001108450.1. NM_001114978.1. [Q9H3D4-3]
    NP_001108451.1. NM_001114979.1. [Q9H3D4-5]
    NP_001108452.1. NM_001114980.1. [Q9H3D4-2]
    NP_001108453.1. NM_001114981.1. [Q9H3D4-4]
    NP_001108454.1. NM_001114982.1. [Q9H3D4-6]
    NP_003713.3. NM_003722.4. [Q9H3D4-1]
    XP_005247900.1. XM_005247843.1. [Q9H3D4-11]
    UniGeneiHs.137569.

    Genome annotation databases

    EnsembliENST00000264731; ENSP00000264731; ENSG00000073282. [Q9H3D4-1]
    ENST00000320472; ENSP00000317510; ENSG00000073282. [Q9H3D4-7]
    ENST00000354600; ENSP00000346614; ENSG00000073282. [Q9H3D4-2]
    ENST00000392460; ENSP00000376253; ENSG00000073282. [Q9H3D4-3]
    ENST00000392461; ENSP00000376254; ENSG00000073282. [Q9H3D4-8]
    ENST00000392463; ENSP00000376256; ENSG00000073282. [Q9H3D4-4]
    ENST00000418709; ENSP00000407144; ENSG00000073282. [Q9H3D4-5]
    ENST00000437221; ENSP00000392488; ENSG00000073282. [Q9H3D4-6]
    ENST00000440651; ENSP00000394337; ENSG00000073282. [Q9H3D4-11]
    ENST00000449992; ENSP00000387839; ENSG00000073282. [Q9H3D4-10]
    ENST00000456148; ENSP00000389485; ENSG00000073282. [Q9H3D4-12]
    GeneIDi8626.
    KEGGihsa:8626.
    UCSCiuc003frx.2. human. [Q9H3D4-5]
    uc003fry.2. human. [Q9H3D4-1]
    uc003frz.2. human. [Q9H3D4-3]
    uc003fsb.2. human. [Q9H3D4-6]
    uc003fsc.2. human. [Q9H3D4-2]
    uc003fsd.2. human. [Q9H3D4-4]
    uc010hzc.1. human. [Q9H3D4-7]
    uc010hzd.1. human. [Q9H3D4-10]

    Polymorphism databases

    DMDMi57013009.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB010153 mRNA. Translation: BAA32433.1 .
    Y16961 mRNA. Translation: CAA76562.1 .
    AF075428 mRNA. Translation: AAC62633.1 .
    AF075429 mRNA. Translation: AAC62634.1 .
    AF075430 mRNA. Translation: AAC62635.1 .
    AF075431 mRNA. Translation: AAC62636.1 .
    AF075432 mRNA. Translation: AAC62637.1 .
    AF075433 mRNA. Translation: AAC62638.1 .
    AF124539
    , AF124528 , AF124529 , AF124531 , AF124532 , AF124533 , AF124534 , AF124535 , AF124536 , AF124537 , AF124538 Genomic DNA. Translation: AAG45607.1 .
    AF124539
    , AF124528 , AF124529 , AF124531 , AF124532 , AF124533 , AF124534 , AF124535 , AF124536 , AF124537 Genomic DNA. Translation: AAG45608.1 .
    AF124540
    , AF124528 , AF124529 , AF124531 , AF124532 , AF124533 , AF124534 , AF124535 Genomic DNA. Translation: AAG45609.1 .
    AF124539
    , AF124530 , AF124531 , AF124532 , AF124533 , AF124534 , AF124535 , AF124536 , AF124537 , AF124538 Genomic DNA. Translation: AAG45610.1 .
    AF124539
    , AF124530 , AF124531 , AF124532 , AF124533 , AF124534 , AF124535 , AF124536 , AF124537 Genomic DNA. Translation: AAG45611.1 .
    AF124540
    , AF124531 , AF124533 , AF124535 , AF124534 , AF124532 , AF124530 Genomic DNA. Translation: AAG45612.1 .
    AB016072 mRNA. Translation: BAA32592.1 . Frameshift.
    AB016073 mRNA. Translation: BAA32593.1 . Frameshift.
    AF091627 mRNA. Translation: AAC43038.1 .
    AF116770
    , AF116756 , AF116757 , AF116759 , AF116760 , AF116761 , AF116762 , AF116763 , AF116764 , AF116765 Genomic DNA. Translation: AAF43486.1 . Different initiation.
    AF116769
    , AF116756 , AF116757 , AF116759 , AF116760 , AF116761 , AF116762 , AF116763 , AF116764 , AF116765 , AF116766 , AF116767 , AF116768 Genomic DNA. Translation: AAF43487.1 . Different initiation.
    AF116769
    , AF116756 , AF116759 , AF116757 , AF116762 , AF116764 , AF116766 , AF116767 , AF116765 , AF116763 , AF116761 , AF116760 Genomic DNA. Translation: AAF43488.1 . Different initiation.
    AF116769
    , AF116756 , AF116757 , AF116759 , AF116760 , AF116761 , AF116762 , AF116763 , AF116764 , AF116765 , AF116766 Genomic DNA. Translation: AAF43489.1 . Different initiation.
    AF116770
    , AF116758 , AF116760 , AF116762 , AF116764 , AF116765 , AF116763 , AF116761 , AF116759 Genomic DNA. Translation: AAF43490.1 .
    AF116769
    , AF116758 , AF116759 , AF116760 , AF116764 , AF116766 , AF116768 , AF116767 , AF116765 , AF116763 , AF116762 , AF116761 Genomic DNA. Translation: AAF43491.1 .
    AF116769
    , AF116758 , AF116760 , AF116759 , AF116761 , AF116763 , AF116765 , AF116767 , AF116766 , AF116764 , AF116762 Genomic DNA. Translation: AAF43492.1 .
    AF116769
    , AF116758 , AF116760 , AF116759 , AF116761 , AF116763 , AF116765 , AF116766 , AF116764 , AF116762 Genomic DNA. Translation: AAF43493.1 .
    AF116771 mRNA. Translation: AAF61624.1 . Frameshift.
    AB042841 mRNA. Translation: BAB20591.1 .
    BC039815 mRNA. Translation: AAH39815.1 .
    AF061512 mRNA. Translation: AAC24830.1 .
    AY342152 , AY341145 Genomic DNA. Translation: AAQ63448.1 .
    AY339663 Genomic DNA. Translation: AAQ63449.1 .
    AY341143 , AY339664 , AY341142 Genomic DNA. Translation: AAQ63450.1 .
    AY341143 , AY341142 Genomic DNA. Translation: AAQ63451.1 .
    AY341144 Genomic DNA. Translation: AAQ63452.1 .
    AY342153 Genomic DNA. Translation: AAQ63453.1 .
    AY342154 Genomic DNA. Translation: AAQ63454.1 .
    AJ315499 mRNA. Translation: CAC48053.1 .
    CCDSi CCDS3293.1. [Q9H3D4-1 ]
    CCDS46976.1. [Q9H3D4-3 ]
    CCDS46977.1. [Q9H3D4-5 ]
    CCDS46978.1. [Q9H3D4-2 ]
    CCDS46979.1. [Q9H3D4-4 ]
    CCDS46980.1. [Q9H3D4-6 ]
    RefSeqi NP_001108450.1. NM_001114978.1. [Q9H3D4-3 ]
    NP_001108451.1. NM_001114979.1. [Q9H3D4-5 ]
    NP_001108452.1. NM_001114980.1. [Q9H3D4-2 ]
    NP_001108453.1. NM_001114981.1. [Q9H3D4-4 ]
    NP_001108454.1. NM_001114982.1. [Q9H3D4-6 ]
    NP_003713.3. NM_003722.4. [Q9H3D4-1 ]
    XP_005247900.1. XM_005247843.1. [Q9H3D4-11 ]
    UniGenei Hs.137569.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RG6 NMR - A 540-614 [» ]
    2RMN NMR - A 153-388 [» ]
    2Y9T NMR - A 543-622 [» ]
    2Y9U X-ray 1.60 A 545-611 [» ]
    3QYM X-ray 3.20 A/B/C/D/E/F/G/H 166-362 [» ]
    3QYN X-ray 2.50 A/B/C/D 166-362 [» ]
    3US0 X-ray 2.50 A/B/C/D 166-362 [» ]
    3US1 X-ray 2.80 A/D 166-362 [» ]
    3US2 X-ray 4.20 A/B/C/D/G/H/I/J 166-362 [» ]
    3ZY0 X-ray 1.90 A/B/C/D 398-427 [» ]
    3ZY1 X-ray 2.15 A 398-441 [» ]
    4A9Z X-ray 2.29 A/B/C/D 397-455 [» ]
    ProteinModelPortali Q9H3D4.
    SMRi Q9H3D4. Positions 153-437, 543-622.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114181. 117 interactions.
    DIPi DIP-29588N.
    IntActi Q9H3D4. 64 interactions.
    MINTi MINT-190238.

    PTM databases

    PhosphoSitei Q9H3D4.

    Polymorphism databases

    DMDMi 57013009.

    Proteomic databases

    MaxQBi Q9H3D4.
    PaxDbi Q9H3D4.
    PRIDEi Q9H3D4.

    Protocols and materials databases

    DNASUi 8626.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264731 ; ENSP00000264731 ; ENSG00000073282 . [Q9H3D4-1 ]
    ENST00000320472 ; ENSP00000317510 ; ENSG00000073282 . [Q9H3D4-7 ]
    ENST00000354600 ; ENSP00000346614 ; ENSG00000073282 . [Q9H3D4-2 ]
    ENST00000392460 ; ENSP00000376253 ; ENSG00000073282 . [Q9H3D4-3 ]
    ENST00000392461 ; ENSP00000376254 ; ENSG00000073282 . [Q9H3D4-8 ]
    ENST00000392463 ; ENSP00000376256 ; ENSG00000073282 . [Q9H3D4-4 ]
    ENST00000418709 ; ENSP00000407144 ; ENSG00000073282 . [Q9H3D4-5 ]
    ENST00000437221 ; ENSP00000392488 ; ENSG00000073282 . [Q9H3D4-6 ]
    ENST00000440651 ; ENSP00000394337 ; ENSG00000073282 . [Q9H3D4-11 ]
    ENST00000449992 ; ENSP00000387839 ; ENSG00000073282 . [Q9H3D4-10 ]
    ENST00000456148 ; ENSP00000389485 ; ENSG00000073282 . [Q9H3D4-12 ]
    GeneIDi 8626.
    KEGGi hsa:8626.
    UCSCi uc003frx.2. human. [Q9H3D4-5 ]
    uc003fry.2. human. [Q9H3D4-1 ]
    uc003frz.2. human. [Q9H3D4-3 ]
    uc003fsb.2. human. [Q9H3D4-6 ]
    uc003fsc.2. human. [Q9H3D4-2 ]
    uc003fsd.2. human. [Q9H3D4-4 ]
    uc010hzc.1. human. [Q9H3D4-7 ]
    uc010hzd.1. human. [Q9H3D4-10 ]

    Organism-specific databases

    CTDi 8626.
    GeneCardsi GC03P189349.
    GeneReviewsi TP63.
    HGNCi HGNC:15979. TP63.
    HPAi CAB000083.
    HPA006288.
    HPA007010.
    MIMi 103285. phenotype.
    106260. phenotype.
    129400. phenotype.
    603273. gene.
    603543. phenotype.
    604292. phenotype.
    605289. phenotype.
    neXtProti NX_Q9H3D4.
    Orphaneti 978. ADULT syndrome.
    1071. Ankyloblepharon - ectodermal defects - cleft lip/palate.
    93930. Bladder exstrophy.
    1991. Cleft lip with or without cleft palate.
    1896. EEC syndrome.
    69085. Limb-mammary syndrome.
    3022. Rapp-Hodgkin syndrome.
    2440. Split hand-split foot malformation.
    PharmGKBi PA162406776.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG80479.
    HOVERGENi HBG005201.
    InParanoidi Q9H3D4.
    KOi K10149.
    OMAi QRNTLTP.
    OrthoDBi EOG7JQBNW.
    PhylomeDBi Q9H3D4.
    TreeFami TF106101.

    Enzyme and pathway databases

    SignaLinki Q9H3D4.

    Miscellaneous databases

    ChiTaRSi TP63. human.
    EvolutionaryTracei Q9H3D4.
    GeneWikii TP63.
    GenomeRNAii 8626.
    NextBioi 32339.
    PROi Q9H3D4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H3D4.
    Bgeei Q9H3D4.
    Genevestigatori Q9H3D4.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. "Cloning and chromosomal mapping of the human p53-related KET gene to chromosome 3q27 and its murine homolog Ket to mouse chromosome 16."
      Augustin M., Bamberger C., Paul D., Schmale H.
      Mamm. Genome 9:899-902(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Keratinocyte and Skeletal muscle.
    3. "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 2; 4 AND 6), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-680 (ISOFORMS 1; 3 AND 5), FUNCTION, TISSUE SPECIFICITY.
    4. "Cloning and functional analysis of human p51, which structurally and functionally resembles p53."
      Osada M., Ohba M., Kawahara C., Ishioka C., Kanamaru R., Katoh I., Ikawa Y., Nimura Y., Nakagawara A., Obinata M., Ikawa S.
      Nat. Med. 4:839-843(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5), VARIANT HEAD AND NECK CANCER LEU-184, VARIANT LUNG CARCINOMA PRO-187, VARIANT CERVICAL CANCER LEU-204.
      Tissue: Skeletal muscle.
    5. "Mutational analysis of the p63/p73L/p51/p40/CUSP/KET gene in human cancer cell lines using intronic primers."
      Hagiwara K., McMenamin M.G., Miura K., Harris C.C.
      Cancer Res. 59:4165-4169(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT COLON CANCER HIS-279, VARIANT OVARIAN CANCER ALA-560.
    6. "Characterization of an autoantigen associated with chronic ulcerative stomatitis: the CUSP autoantigen is a member of the p53 family."
      Lee L.A., Walsh P., Prater C.A., Su L.-J., Marchbank A., Egbert T.B., Dellavalle R.P., Targoff I.N., Kaufman K.M., Chorzelski T.P., Jablonska S.
      J. Invest. Dermatol. 113:146-151(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    7. "Mutation and expression of the p51 gene in human lung cancer."
      Tani M., Shimizu K., Kawahara C., Kohno T., Ishimoto O., Ikawa S., Yokota J.
      Neoplasia 1:71-79(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 7), ALTERNATIVE SPLICING (ISOFORM 8).
    8. "Transcriptional dysregulation of the p73L/p63/p51/p40/KET gene in human squamous cell carcinomas: expression of Delta Np73L, a novel dominant-negative isoform, and loss of expression of the potential tumour suppressor p51."
      Senoo M., Tsuchiya I., Matsumura Y., Mori T., Saito Y., Kato H., Okamoto T., Habu S.
      Br. J. Cancer 84:1235-1241(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10), TISSUE SPECIFICITY (ISOFORM 10).
    9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Lymph.
    10. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-450 (ISOFORMS 2/4/8), SUBUNIT, ZINC-BINDING, DNA-BINDING.
      Tissue: Prostate.
    11. "Sequencing of candidate genes for non-syndromic cleft lip and palate."
      Vieira A.R., Murray J.C.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21; 95-255; 295-330; 378-502 AND 583-680.
    12. "High thermostability and lack of cooperative DNA binding distinguish the p63 core domain from the homologous tumor suppressor p53."
      Klein C., Georges G., Kunkele K.P., Huber R., Engh R.A., Hansen S.
      J. Biol. Chem. 276:37390-37401(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 153-388 (ISOFORM 11).
      Tissue: Placenta.
    13. "p73 and p63 are homotetramers capable of weak heterotypic interactions with each other but not with p53."
      Davison T.S., Vagner C., Kaghad M., Ayed A., Caput D., Arrowsmith C.H.
      J. Biol. Chem. 274:18709-18714(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    14. Cited for: TISSUE SPECIFICITY.
    15. Cited for: FUNCTION IN NOTCH SIGNALING.
    16. "Identification and characterization of HIPK2 interacting with p73 and modulating functions of the p53 family in vivo."
      Kim E.-J., Park J.-S., Um S.-J.
      J. Biol. Chem. 277:32020-32028(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIPK2.
    17. "A C-terminal inhibitory domain controls the activity of p63 by an intramolecular mechanism."
      Serber Z., Lai H.C., Yang A., Ou H.D., Sigal M.S., Kelly A.E., Darimont B.D., Duijf P.H.G., Van Bokhoven H., McKeon F., Doetsch V.
      Mol. Cell. Biol. 22:8601-8611(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-55; TRP-59 AND LEU-62.
    18. "Complex transcriptional effects of p63 isoforms: identification of novel activation and repression domains."
      Ghioni P., Bolognese F., Duijf P.H.G., Van Bokhoven H., Mantovani R., Guerrini L.
      Mol. Cell. Biol. 22:8659-8668(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN.
    19. "SSRP1 functions as a co-activator of the transcriptional activator p63."
      Zeng S.X., Dai M.-S., Keller D.M., Lu H.
      EMBO J. 21:5487-5497(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SSRP1.
    20. Erratum
      Zeng S.X., Dai M.-S., Keller D.M., Lu H.
      EMBO J. 23:1679-1679(2004)
    21. "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.
    22. "SCC-112 gene is involved in tumor progression and promotes the cell proliferation in G2/M phase."
      Zheng M.Z., Zheng L.M., Zeng Y.X.
      J. Cancer Res. Clin. Oncol. 134:453-462(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDS5A.
    23. "NIR, an inhibitor of histone acetyltransferases, regulates transcription factor TAp63 and is controlled by the cell cycle."
      Heyne K., Willnecker V., Schneider J., Conrad M., Raulf N., Schule R., Roemer K.
      Nucleic Acids Res. 38:3159-3171(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NOC2L, SUBCELLULAR LOCATION.
    24. Cited for: FUNCTION.
    25. "Solution structure of the C-terminal domain of p63."
      Cadot B., Candi E., Cicero D.O., Desideri A., Mele S., Melino G., Paci M.
      Submitted (NOV-2004) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 540-610.
    26. Cited for: VARIANTS EEC3 TRP-243; GLN-243 AND ARG-345.
    27. "Split-hand/split-foot malformation is caused by mutations in the p63 gene on 3q27."
      Ianakiev P., Kilpatrick M.W., Toudjarska I., Basel D., Beighton P., Tsipouras P.
      Am. J. Hum. Genet. 67:59-66(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SHFM4 GLU-233 AND CYS-319, VARIANTS EEC3 HIS-318 AND GLN-343.
    28. Cited for: VARIANT ADULT IN NDELTA-TYPE ISOFORMS.
    29. Cited for: VARIANTS AEC PHE-553 AND GLY-561.
    30. Cited for: VARIANTS EEC3 GLN-243; TRP-243; GLN-266; TYR-308; ASN-311; CYS-318; HIS-318; GLN-318; CYS-319; HIS-319; SER-319; TRP-343; GLN-343; ARG-345; SER-347; SER-348 AND HIS-351, VARIANTS SHFM4 PRO-193 INS; GLU-232 AND HIS-319, INVOLVEMENT IN LMS.
    31. "Gain-of-function mutation in ADULT syndrome reveals the presence of a second transactivation domain in p63."
      Duijf P.H.G., Vanmolkot K.R., Propping P., Friedl W., Krieger E., McKeon F., Doetsch V., Brunner H.G., van Bokhoven H.
      Hum. Mol. Genet. 11:799-804(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ADULT SYNDROME GLN-337.
    32. "EEC syndrome type 3 with a heterozygous germline mutation in the P63 gene and B cell lymphoma."
      Akahoshi K., Sakazume S., Kosaki K., Ohashi H., Fukushima Y.
      Am. J. Med. Genet. A 120:370-373(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EEC3 GLY-351.
    33. "The Rapp-Hodgkin syndrome results from mutations of the TP63 gene."
      Bougeard G., Hadj-Rabia S., Faivre L., Sarafan-Vasseur N., Frebourg T.
      Eur. J. Hum. Genet. 11:700-704(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDRH HIS-318, CHARACTERIZATION OF VARIANT EDRH HIS-318.
    34. "Heterozygous mutation in the SAM domain of p63 underlies Rapp-Hodgkin ectodermal dysplasia."
      Kantaputra P.N., Hamada T., Kumchai T., McGrath J.A.
      J. Dent. Res. 82:433-437(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDRH PRO-580.
    35. "Molecular evidence that AEC syndrome and Rapp-Hodgkin syndrome are variable expression of a single genetic disorder."
      Bertola D.R., Kim C.A., Albano L.M.J., Scheffer H., Meijer R., van Bokhoven H.
      Clin. Genet. 66:79-80(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDRH THR-549.
    36. "A mutation of the p63 gene in non-syndromic cleft lip."
      Leoyklang P., Siriwan P., Shotelersuk V.
      J. Med. Genet. 43:E28-E28(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDRH/OFC8 GLY-352, VARIANTS LEU-129 AND HIS-603.

    Entry informationi

    Entry nameiP63_HUMAN
    AccessioniPrimary (citable) accession number: Q9H3D4
    Secondary accession number(s): O75080
    , O75195, O75922, O76078, Q6VEG2, Q6VEG3, Q6VEG4, Q6VFJ1, Q6VFJ2, Q6VFJ3, Q6VH20, Q7LDI3, Q7LDI4, Q7LDI5, Q96KR0, Q9H3D2, Q9H3D3, Q9H3P8, Q9NPH7, Q9P1B4, Q9P1B5, Q9P1B6, Q9P1B7, Q9UBV9, Q9UE10, Q9UP26, Q9UP27, Q9UP28, Q9UP74
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 4, 2005
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 144 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3