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Q9H3D4 (P63_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:TP63
Synonyms:KET, P63, P73H, P73L, TP73L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length680 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a sequence specific DNA binding transcriptional activator or repressor. The isoforms contain a varying set of transactivation and auto-regulating transactivation inhibiting domains thus showing an isoform specificactivity. 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. Ref.3 Ref.15 Ref.17 Ref.18 Ref.19 Ref.23 Ref.24

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Binds DNA as a homotetramer. Isoform compositionof 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. Ref.10 Ref.13 Ref.16 Ref.19 Ref.21 Ref.22 Ref.23

Subcellular location

Nucleus Ref.17 Ref.23.

Tissue specificity

Widely expressed, notably in heart, kidney, placenta, prostate, skeletal muscle, testis and thymus, although the precise isoform variesaccording 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. Ref.3 Ref.8 Ref.14

Domain

The transactivation inhibitory domain (TID) can interact with, and inhibit the activity of the N-terminal transcriptional activation domain of TA*-type isoforms. Ref.17 Ref.18

Post-translational modification

May be sumoylated By similarity.

Ubiquitinated. Polyubiquitination involves WWP1 and leads to proteasomal degradation of this protein. Ref.21

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.29

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.26 Ref.27 Ref.30 Ref.32

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.27 Ref.30

Limb-mammary syndrome (LMS) [MIM:603543]: Characterized by ectrodactyly, cleft palate and mammary-gland abnormalities.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.30

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.33 Ref.34 Ref.35 Ref.36

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.

Sequence similarities

Belongs to the p53 family.

Contains 1 SAM (sterile alpha motif) domain.

Sequence caution

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.

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.

Ontologies

Keywords
   Biological processApoptosis
Notch signaling pathway
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative promoter usage
Alternative splicing
   DiseaseDisease mutation
Ectodermal dysplasia
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Developmental protein
   PTMIsopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator

Inferred from Biological aspect of Ancestor. Source: RefGenome

Notch signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

apoptotic process

Traceable author statement Ref.4. Source: ProtInc

cell aging

Inferred from electronic annotation. Source: Ensembl

cellular response to UV

Inferred from Biological aspect of Ancestor. Source: RefGenome

chromatin remodeling

Inferred from electronic annotation. Source: Ensembl

cloacal septation

Inferred from electronic annotation. Source: Ensembl

ectoderm and mesoderm interaction

Inferred from electronic annotation. Source: Ensembl

embryonic limb morphogenesis

Inferred from electronic annotation. Source: Ensembl

epidermal cell division

Inferred from electronic annotation. Source: Ensembl

epithelial cell development

Inferred from electronic annotation. Source: Ensembl

establishment of planar polarity

Inferred from electronic annotation. Source: Ensembl

female genitalia morphogenesis

Inferred from electronic annotation. Source: Ensembl

hair follicle morphogenesis

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from Biological aspect of Ancestor. Source: RefGenome

keratinocyte differentiation

Inferred from electronic annotation. Source: Ensembl

keratinocyte proliferation

Inferred from electronic annotation. Source: Ensembl

mitotic G1 DNA damage checkpoint

Inferred from Biological aspect of Ancestor. Source: RefGenome

multicellular organismal aging

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of keratinocyte differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of mesoderm development

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.18. Source: UniProtKB

neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

odontogenesis of dentin-containing tooth

Inferred from electronic annotation. Source: Ensembl

polarized epithelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of Notch signaling pathway

Inferred from direct assay Ref.15. Source: UniProtKB

positive regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of fibroblast apoptotic process

Inferred from direct assay Ref.3. Source: UniProtKB

positive regulation of mesenchymal cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoblast differentiation

Inferred from mutant phenotype PubMed 22521434. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 22521434. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.18PubMed 16343436. Source: UniProtKB

post-anal tail morphogenesis

Inferred from electronic annotation. Source: Ensembl

prostatic bud formation

Inferred from electronic annotation. Source: Ensembl

protein homotetramerization

Inferred from physical interaction Ref.13. Source: UniProtKB

proximal/distal pattern formation

Inferred from electronic annotation. Source: Ensembl

regulation of neuron apoptotic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to X-ray

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to gamma radiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

skeletal system development

Inferred from electronic annotation. Source: Ensembl

smooth muscle tissue development

Inferred from electronic annotation. Source: Ensembl

squamous basal epithelial stem cell differentiation involved in prostate gland acinus development

Inferred from electronic annotation. Source: Ensembl

sympathetic nervous system development

Inferred from electronic annotation. Source: Ensembl

urinary bladder development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentchromatin

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoplasm

Inferred from direct assay PubMed 10657951. Source: MGI

cytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

dendrite

Inferred from Biological aspect of Ancestor. Source: RefGenome

nuclear chromatin

Inferred from direct assay PubMed 22521434. Source: BHF-UCL

nucleoplasm

Inferred from direct assay Ref.23. Source: UniProtKB

nucleus

Inferred from direct assay Ref.17. Source: UniProtKB

transcription factor complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionDNA binding

Non-traceable author statement Ref.10. Source: UniProtKB

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

damaged DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

double-stranded DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

identical protein binding

Inferred from physical interaction Ref.17. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

p53 binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

sequence-specific DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

sequence-specific DNA binding transcription factor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription regulatory region DNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 12 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H3D4-1)

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.
Note: Produced by alternative promoter usage.
Isoform 2 (identifier: Q9H3D4-2)

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.
Isoform 3 (identifier: Q9H3D4-3)

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.
Isoform 4 (identifier: Q9H3D4-4)

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.
Isoform 5 (identifier: Q9H3D4-5)

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.
Isoform 6 (identifier: Q9H3D4-6)

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.
Isoform 7 (identifier: Q9H3D4-7)

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.
Isoform 8 (identifier: Q9H3D4-8)

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.
Isoform 9 (identifier: Q9H3D4-9)

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.
Isoform 10 (identifier: Q9H3D4-10)

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.
Isoform 11 (identifier: Q9H3D4-11)

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.
Isoform 12 (identifier: Q9H3D4-12)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 680680Tumor protein 63
PRO_0000185729

Regions

Domain541 – 60767SAM
DNA binding170 – 362193 Ref.10
Region1 – 107107Transcription activation
Region352 – 38837Interaction with HIPK2
Region394 – 44350Oligomerization
Region610 – 68071Transactivation inhibition
Compositional bias437 – 4448Poly-Gln

Sites

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

Amino acid modifications

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

Natural variations

Alternative sequence1 – 108108MNFET…SDPMW → MLYLENNAQTQFSE in isoform 2, isoform 4, isoform 6, isoform 8, isoform 10 and isoform 12.
VSP_012465
Alternative sequence109 – 19385Missing in isoform 9 and isoform 10.
VSP_012466
Alternative sequence373 – 3775GTKRP → A in isoform 11 and isoform 12.
VSP_012467
Alternative sequence450 – 680231QTSIQ…KEEGE → HLLSACFRNELVEPRRETPK QSDVFFRHSKPPNRSVYP in isoform 5 and isoform 6.
VSP_012468
Alternative sequence503 – 680178IPMMG…KEEGE → RSGKSENP in isoform 7 and isoform 8.
VSP_012469
Alternative sequence551 – 680130SFLAR…KEEGE → RIWQV in isoform 3 and isoform 4.
VSP_012470
Natural variant1291S → L. Ref.36
Corresponds to variant rs193287780 [ dbSNP | Ensembl ].
VAR_035126
Natural variant1841S → L in head and neck cancer. Ref.4
VAR_020866
Natural variant1871A → P in lung carcinoma; somatic mutation. Ref.4
VAR_020867
Natural variant1931T → TP in SHFM4. Ref.30
VAR_032736
Natural variant2041Q → L in cervical cancer. Ref.4
VAR_020868
Natural variant2321K → E in SHFM4. Ref.30
VAR_032737
Natural variant2331K → E in SHFM4. Ref.27
VAR_020869
Natural variant2431R → Q in EEC3. Ref.26 Ref.30
VAR_020870
Natural variant2431R → W in EEC3. Ref.26 Ref.30
VAR_020871
Natural variant2661R → Q in EEC3. Ref.30
VAR_032738
Natural variant2791P → H in colon cancer. Ref.5
VAR_020872
Natural variant3081C → Y in EEC3. Ref.30
VAR_032739
Natural variant3111S → N in EEC3. Ref.30
VAR_032740
Natural variant3181R → C in EEC3. Ref.30
VAR_032741
Natural variant3181R → 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. Ref.27 Ref.30 Ref.33
VAR_020873
Natural variant3181R → Q in EEC3. Ref.30
VAR_032742
Natural variant3191R → C in EEC3. Ref.27 Ref.30
VAR_020874
Natural variant3191R → H in EEC3 and SHFM4. Ref.30
VAR_032743
Natural variant3191R → S in EEC3. Ref.30
VAR_032744
Natural variant3371R → Q in ADULT syndrome; confers novel transcription activation capacity on isoform 6. Ref.31
VAR_020875
Natural variant3431R → Q in EEC3. Ref.27 Ref.30
VAR_020876
Natural variant3431R → W in EEC3. Ref.30
VAR_032745
Natural variant3451C → R in EEC3; abolishes transcription activation. Ref.26 Ref.30
VAR_020877
Natural variant3471C → S in EEC3. Ref.30
VAR_032746
Natural variant3481P → S in EEC3. Ref.30
VAR_032747
Natural variant3511D → G in EEC3. Ref.32
VAR_020878
Natural variant3511D → H in EEC3. Ref.30
VAR_032748
Natural variant3521R → G in EDRH and OFC8. Ref.36
VAR_035127
Natural variant5491I → T in EDRH. Ref.35
VAR_035128
Natural variant5531L → F in AEC. Ref.29
VAR_020879
Natural variant5601S → A in ovarian cancer. Ref.5
VAR_020880
Natural variant5611C → G in AEC. Ref.29
VAR_020881
Natural variant5801S → P in EDRH. Ref.34
VAR_035129
Natural variant6031D → H. Ref.36
VAR_035130
Isoform 2:
Natural variant61N → H in ADULT syndrome.
Isoform 4:
Natural variant61N → H in ADULT syndrome.
Isoform 6:
Natural variant61N → H in ADULT syndrome.
Isoform 8:
Natural variant61N → H in ADULT syndrome.
Isoform 10:
Natural variant61N → H in ADULT syndrome.
Isoform 12:
Natural variant61N → H in ADULT syndrome.

Experimental info

Mutagenesis551F → A: Abrogates transcriptional activity and interaction with transactivation inhibition domain; when associated with A-59 and A-62. Ref.17
Mutagenesis591W → A: Abrogates transcriptional activity and interaction with transactivation inhibition domain; when associated with A-55 and A-62. Ref.17
Mutagenesis621L → A: Abrogates transcriptional activity and interaction with transactivation inhibition domain; when associated with A-55 and A-59. Ref.17
Mutagenesis5431Y → F: Abolishes ubiquitination. Ref.21
Sequence conflict1251Q → R in BAA32433. Ref.1
Sequence conflict1541S → P in BAA32433. Ref.1
Sequence conflict1771F → S in BAA32433. Ref.1
Sequence conflict3781F → S in AAC24830. Ref.10
Sequence conflict5361H → Q in CAA76562. Ref.2
Sequence conflict5511S → G in BAA32593. Ref.4
Sequence conflict5511S → G in AAF43487. Ref.7
Sequence conflict5511S → G in AAF43491. Ref.7

Secondary structure

................................................................. 680
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (TA*-alpha) (TAp63alpha) (P51B) [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: F66ECD45E87D9799

FASTA68076,785
        10         20         30         40         50         60 
MNFETSRCAT LQYCPDPYIQ RFVETPAHFS WKESYYRSTM SQSTQTNEFL SPEVFQHIWD 

        70         80         90        100        110        120 
FLEQPICSVQ PIDLNFVDEP SEDGATNKIE ISMDCIRMQD SDLSDPMWPQ YTNLGLLNSM 

       130        140        150        160        170        180 
DQQIQNGSSS TSPYNTDHAQ NSVTAPSPYA QPSSTFDALS PSPAIPSNTD YPGPHSFDVS 

       190        200        210        220        230        240 
FQQSSTAKSA TWTYSTELKK LYCQIAKTCP IQIKVMTPPP QGAVIRAMPV YKKAEHVTEV 

       250        260        270        280        290        300 
VKRCPNHELS REFNEGQIAP PSHLIRVEGN SHAQYVEDPI TGRQSVLVPY EPPQVGTEFT 

       310        320        330        340        350        360 
TVLYNFMCNS SCVGGMNRRP ILIIVTLETR DGQVLGRRCF EARICACPGR DRKADEDSIR 

       370        380        390        400        410        420 
KQQVSDSTKN GDGTKRPFRQ NTHGIQMTSI KKRRSPDDEL LYLPVRGRET YEMLLKIKES 

       430        440        450        460        470        480 
LELMQYLPQH TIETYRQQQQ QQHQHLLQKQ TSIQSPSSYG NSSPPLNKMN SMNKLPSVSQ 

       490        500        510        520        530        540 
LINPQQRNAL TPTTIPDGMG ANIPMMGTHM PMAGDMNGLS PTQALPPPLS MPSTSHCTPP 

       550        560        570        580        590        600 
PPYPTDCSIV SFLARLGCSS CLDYFTTQGL TTIYQIEHYS MDDLASLKIP EQFRHAIWKG 

       610        620        630        640        650        660 
ILDHRQLHEF SSPSHLLRTP SSASTVSVGS SETRGERVID AVRFTLRQTI SFPPRDEWND 

       670        680 
FNFDMDARRN KQQRIKEEGE 

« Hide

Isoform 2 (DeltaN-alpha) (DeltaNp63 alpha) (P51delNalpha) [UniParc].

Checksum: 2E2F92ABF1AF8629
Show »

FASTA58665,756
Isoform 3 (TA*-beta) (TAp63beta) [UniParc].

Checksum: E22874BE7DBABCBE
Show »

FASTA55562,433
Isoform 4 (DeltaN-beta) (DeltaNp63 beta) (P51delNbeta) [UniParc].

Checksum: 68B63547A46C1B05
Show »

FASTA46151,404
Isoform 5 (TA*-gamma) (TAp63gamma) (P51A) [UniParc].

Checksum: 86CC865BDF2643DD
Show »

FASTA48755,688
Isoform 6 (DeltaN-gamma) (DeltaNp63gamma) (P51delNgamma) [UniParc].

Checksum: C6689B83FD701610
Show »

FASTA39344,658
Isoform 7 (TA*-delta) (TAp63delta) (P51delta) [UniParc].

Checksum: 3539D81485635FF0
Show »

FASTA51057,619
Isoform 8 (DeltaN-delta) [UniParc].

Checksum: A5974A14B25E3118
Show »

FASTA41646,589
Isoform 9 (TA*-epsilon) [UniParc].

Checksum: F07014CB9FEF1FF2
Show »

FASTA59567,779
Isoform 10 (DeltaN-epsilon) (DeltaNp73L) [UniParc].

Checksum: 31E1BEA3CA305B88
Show »

FASTA50156,750
Isoform 11 (P63 delta) [UniParc].

Checksum: EB0E2C9E93C6D34A
Show »

FASTA67676,317
Isoform 12 [UniParc].

Checksum: A2DC3D2E13B6B531
Show »

FASTA58265,288

References

« Hide 'large scale' references
[1]"A second p53-related protein, p73L, with high homology to p73."
Senoo M., Seki N., Ohira M., Sugano S., Watanabe M., Tachibana M., Tanaka T., Shinkai Y., Kato H.
Biochem. Biophys. Res. Commun. 248:603-607(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[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]"A new human p53 homologue."
Trink B., Okami K., Wu L., Sriuranpong V., Jen J., Sidransky D.
Nat. Med. 4:747-748(1998) [PubMed] [Europe PMC] [Abstract]
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]"p63 identifies keratinocyte stem cells."
Pellegrini G., Dellambra E., Golisano O., Martinelli E., Fantozzi I., Bondanza S., Ponzin D., McKeon F., De Luca M.
Proc. Natl. Acad. Sci. U.S.A. 98:3156-3161(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[15]"The p53 family member genes are involved in the Notch signal pathway."
Sasaki Y., Ishida S., Morimoto I., Yamashita T., Kojima T., Kihara C., Tanaka T., Imai K., Nakamura Y., Tokino T.
J. Biol. Chem. 277:719-724(2002) [PubMed] [Europe PMC] [Abstract]
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]"Exome sequence identifies RIPK4 as the Bartsocas-Papas syndrome locus."
Mitchell K., O'Sullivan J., Missero C., Blair E., Richardson R., Anderson B., Antonini D., Murray J.C., Shanske A.L., Schutte B.C., Romano R.A., Sinha S., Bhaskar S.S., Black G.C., Dixon J., Dixon M.J.
Am. J. Hum. Genet. 90:69-75(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[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]"Heterozygous germline mutations in the p53 homolog p63 are the cause of EEC syndrome."
Celli J., Duijf P.H.G., Hamel B.C.J., Bamshad M., Kramer B., Smits A.P.T., Newbury-Ecob R., Hennekam R.C.M., Van Buggenhout G., van Haeringen A., Woods C.G., van Essen A.J., de Waal R., Vriend G., Haber D.A., Yang A., McKeon F., Brunner H.G., van Bokhoven H.
Cell 99:143-153(1999) [PubMed] [Europe PMC] [Abstract]
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]"TP63 gene mutation in ADULT syndrome."
Amiel J., Bougeard G., Francannet C., Raclin V., Munnich A., Lyonnet S., Frebourg T.
Eur. J. Hum. Genet. 9:642-645(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ADULT IN NDELTA-TYPE ISOFORMS.
[29]"Hay-Wells syndrome is caused by heterozygous missense mutations in the SAM domain of p63."
McGrath J.A., Duijf P.H.G., Doetsch V., Irvine A.D., de Waal R., Vanmolkot K.R., Wessagowit V., Kelly A., Atherton D.J., Griffiths W.A., Orlow S.J., van Haeringen A., Ausems M.G., Yang A., McKeon F., Bamshad M.A., Brunner H.G., Hamel B.C.J., van Bokhoven H.
Hum. Mol. Genet. 10:221-229(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AEC PHE-553 AND GLY-561.
[30]"p63 gene mutations in EEC syndrome, limb-mammary syndrome, and isolated split hand-split foot malformation suggest a genotype-phenotype correlation."
van Bokhoven H., Hamel B.C.J., Bamshad M., Sangiorgi E., Gurrieri F., Duijf P.H.G., Vanmolkot K.R.J., van Beusekom E., van Beersum S.E.C., Celli J., Merkx G.F.M., Tenconi R., Fryns J.-P., Verloes A., Newbury-Ecob R.A., Raas-Rotschild A., Majewski F., Beemer F.A. expand/collapse author list , Janecke A., Chitayat D., Crisponi G., Kayserili H., Yates J.R.W., Neri G., Brunner H.G.
Am. J. Hum. Genet. 69:481-492(2001) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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 expand/collapse EMBL AC list , AF124528, AF124529, AF124531, AF124532, AF124533, AF124534, AF124535, AF124536, AF124537, AF124538 Genomic DNA. Translation: AAG45607.1.
AF124539 expand/collapse EMBL AC list , AF124528, AF124529, AF124531, AF124532, AF124533, AF124534, AF124535, AF124536, AF124537 Genomic DNA. Translation: AAG45608.1.
AF124540 expand/collapse EMBL AC list , AF124528, AF124529, AF124531, AF124532, AF124533, AF124534, AF124535 Genomic DNA. Translation: AAG45609.1.
AF124539 expand/collapse EMBL AC list , AF124530, AF124531, AF124532, AF124533, AF124534, AF124535, AF124536, AF124537, AF124538 Genomic DNA. Translation: AAG45610.1.
AF124539 expand/collapse EMBL AC list , AF124530, AF124531, AF124532, AF124533, AF124534, AF124535, AF124536, AF124537 Genomic DNA. Translation: AAG45611.1.
AF124540 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , AF116756, AF116757, AF116759, AF116760, AF116761, AF116762, AF116763, AF116764, AF116765 Genomic DNA. Translation: AAF43486.1. Different initiation.
AF116769 expand/collapse EMBL AC list , AF116756, AF116757, AF116759, AF116760, AF116761, AF116762, AF116763, AF116764, AF116765, AF116766, AF116767, AF116768 Genomic DNA. Translation: AAF43487.1. Different initiation.
AF116769 expand/collapse EMBL AC list , AF116756, AF116759, AF116757, AF116762, AF116764, AF116766, AF116767, AF116765, AF116763, AF116761, AF116760 Genomic DNA. Translation: AAF43488.1. Different initiation.
AF116769 expand/collapse EMBL AC list , AF116756, AF116757, AF116759, AF116760, AF116761, AF116762, AF116763, AF116764, AF116765, AF116766 Genomic DNA. Translation: AAF43489.1. Different initiation.
AF116770 expand/collapse EMBL AC list , AF116758, AF116760, AF116762, AF116764, AF116765, AF116763, AF116761, AF116759 Genomic DNA. Translation: AAF43490.1.
AF116769 expand/collapse EMBL AC list , AF116758, AF116759, AF116760, AF116764, AF116766, AF116768, AF116767, AF116765, AF116763, AF116762, AF116761 Genomic DNA. Translation: AAF43491.1.
AF116769 expand/collapse EMBL AC list , AF116758, AF116760, AF116759, AF116761, AF116763, AF116765, AF116767, AF116766, AF116764, AF116762 Genomic DNA. Translation: AAF43492.1.
AF116769 expand/collapse EMBL AC list , 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.
RefSeqNP_001108450.1. NM_001114978.1.
NP_001108451.1. NM_001114979.1.
NP_001108452.1. NM_001114980.1.
NP_001108453.1. NM_001114981.1.
NP_001108454.1. NM_001114982.1.
NP_003713.3. NM_003722.4.
XP_005247900.1. XM_005247843.1.
UniGeneHs.137569.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RG6NMR-A540-610[»]
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[»]
ProteinModelPortalQ9H3D4.
SMRQ9H3D4. Positions 153-437, 543-622.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114181. 117 interactions.
DIPDIP-29588N.
IntActQ9H3D4. 64 interactions.
MINTMINT-190238.

PTM databases

PhosphoSiteQ9H3D4.

Polymorphism databases

DMDM57013009.

Proteomic databases

PaxDbQ9H3D4.
PRIDEQ9H3D4.

Protocols and materials databases

DNASU8626.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264731; ENSP00000264731; ENSG00000073282. [Q9H3D4-1]
ENST00000320472; ENSP00000317510; ENSG00000073282. [Q9H3D4-7]
ENST00000354600; ENSP00000346614; ENSG00000073282. [Q9H3D4-2]
ENST00000382063; ENSP00000371495; ENSG00000073282. [Q9H3D4-9]
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]
GeneID8626.
KEGGhsa:8626.
UCSCuc003frx.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

CTD8626.
GeneCardsGC03P189349.
HGNCHGNC:15979. TP63.
HPACAB000083.
HPA006288.
HPA007010.
MIM103285. phenotype.
106260. phenotype.
129400. phenotype.
603273. gene.
603543. phenotype.
604292. phenotype.
605289. phenotype.
neXtProtNX_Q9H3D4.
Orphanet978. 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.
PharmGKBPA162406776.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG80479.
HOVERGENHBG005201.
InParanoidQ9H3D4.
KOK10149.
OMAQRNTLTP.
OrthoDBEOG7JQBNW.
PhylomeDBQ9H3D4.
TreeFamTF106101.

Enzyme and pathway databases

SignaLinkQ9H3D4.

Gene expression databases

ArrayExpressQ9H3D4.
BgeeQ9H3D4.
GenevestigatorQ9H3D4.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
2.60.40.720. 1 hit.
4.10.170.10. 1 hit.
InterProIPR008967. p53-like_TF_DNA-bd.
IPR012346. p53/RUNT-type_TF_DNA-bd.
IPR011615. p53_DNA-bd.
IPR010991. p53_tetrameristn.
IPR002117. p53_tumour_suppressor.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
[Graphical view]
PANTHERPTHR11447. PTHR11447. 1 hit.
PfamPF00870. P53. 1 hit.
PF07710. P53_tetramer. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
PRINTSPR00386. P53SUPPRESSR.
SMARTSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMSSF47719. SSF47719. 1 hit.
SSF47769. SSF47769. 1 hit.
SSF49417. SSF49417. 1 hit.
PROSITEPS00348. P53. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTP63. human.
EvolutionaryTraceQ9H3D4.
GeneWikiTP63.
GenomeRNAi8626.
NextBio32339.
PROQ9H3D4.
SOURCESearch...

Entry information

Entry nameP63_HUMAN
AccessionPrimary (citable) accession number: Q9H3D4
Secondary accession number(s): O75080 expand/collapse secondary AC list , 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 history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

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