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Protein

Tumor protein 63

Gene

TP63

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a sequence specific DNA binding transcriptional activator or repressor. The isoforms contain a varying set of transactivation and auto-regulating transactivation inhibiting domains thus showing an isoform specific activity. 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

Zn2+By similarityNote: 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Apoptosis, Notch signaling pathway, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_355377. TP53 Regulates Metabolic Genes.
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 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:15979. TP63.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: GO_Central
  • dendrite Source: GO_Central
  • nuclear chromatin Source: BHF-UCL
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
  • rough endoplasmic reticulum Source: Ensembl
  • transcription factor complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Acro-dermato-ungual-lacrimal-tooth syndrome (ADULT syndrome)1 Publication

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

Disease descriptionA 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.

See also OMIM:103285
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)1 Publication

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

Disease descriptionAn 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.

See also OMIM:106260
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)4 Publications

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

Disease descriptionA 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.

See also OMIM:604292
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)2 Publications

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

Disease descriptionA 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.

See also OMIM:605289
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)1 Publication

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

Disease descriptionCharacterized by ectrodactyly, cleft palate and mammary-gland abnormalities.

See also OMIM:603543

Defects in TP63 are a cause of cervical, colon, head and neck, lung and ovarian cancers.

Ectodermal dysplasia, Rapp-Hodgkin type (EDRH)4 Publications

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

Disease descriptionA 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.

See also OMIM:129400
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)

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

Disease descriptionA 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.

See also OMIM:129400
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.
2440. Split hand-split foot malformation.
PharmGKBiPA162406776.

Polymorphism and mutation databases

BioMutaiTP63.
DMDMi57013009.

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
Modified residuei149 – 1491PhosphotyrosineBy similarity
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, Phosphoprotein, 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

BgeeiQ9H3D4.
ExpressionAtlasiQ9H3D4. baseline and differential.
GenevisibleiQ9H3D4. HS.

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. 127 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 – 1616Combined sources
Helixi173 – 1753Combined sources
Beta strandi178 – 1803Combined sources
Beta strandi187 – 1893Combined sources
Beta strandi191 – 1955Combined sources
Turni196 – 1994Combined sources
Beta strandi200 – 2034Combined sources
Beta strandi209 – 2146Combined sources
Beta strandi224 – 23310Combined sources
Turni234 – 2385Combined sources
Helixi245 – 2495Combined sources
Turni252 – 2565Combined sources
Beta strandi263 – 2697Combined sources
Beta strandi274 – 2774Combined sources
Turni279 – 2813Combined sources
Beta strandi284 – 2896Combined sources
Beta strandi300 – 3067Combined sources
Turni313 – 3186Combined sources
Beta strandi321 – 3288Combined sources
Beta strandi330 – 3323Combined sources
Beta strandi334 – 34310Combined sources
Helixi348 – 3558Combined sources
Beta strandi369 – 3724Combined sources
Beta strandi401 – 4077Combined sources
Helixi408 – 42619Combined sources
Helixi429 – 4368Combined sources
Helixi444 – 4496Combined sources
Beta strandi546 – 5483Combined sources
Helixi549 – 5546Combined sources
Turni555 – 5573Combined sources
Helixi559 – 5613Combined sources
Helixi562 – 5665Combined sources
Turni567 – 5693Combined sources
Helixi573 – 5764Combined sources
Helixi581 – 5866Combined sources
Helixi591 – 60919Combined sources
Beta strandi613 – 6153Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000015092.
HOVERGENiHBG005201.
InParanoidiQ9H3D4.
KOiK10149.
OMAiVPSSHCT.
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. AlignAdd to basket

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

        10         20         30         40         50
MNFETSRCAT LQYCPDPYIQ RFVETPAHFS WKESYYRSTM SQSTQTNEFL
60 70 80 90 100
SPEVFQHIWD FLEQPICSVQ PIDLNFVDEP SEDGATNKIE ISMDCIRMQD
110 120 130 140 150
SDLSDPMWPQ YTNLGLLNSM DQQIQNGSSS TSPYNTDHAQ NSVTAPSPYA
160 170 180 190 200
QPSSTFDALS PSPAIPSNTD YPGPHSFDVS FQQSSTAKSA TWTYSTELKK
210 220 230 240 250
LYCQIAKTCP IQIKVMTPPP QGAVIRAMPV YKKAEHVTEV VKRCPNHELS
260 270 280 290 300
REFNEGQIAP PSHLIRVEGN SHAQYVEDPI TGRQSVLVPY EPPQVGTEFT
310 320 330 340 350
TVLYNFMCNS SCVGGMNRRP ILIIVTLETR DGQVLGRRCF EARICACPGR
360 370 380 390 400
DRKADEDSIR KQQVSDSTKN GDGTKRPFRQ NTHGIQMTSI KKRRSPDDEL
410 420 430 440 450
LYLPVRGRET YEMLLKIKES LELMQYLPQH TIETYRQQQQ QQHQHLLQKQ
460 470 480 490 500
TSIQSPSSYG NSSPPLNKMN SMNKLPSVSQ LINPQQRNAL TPTTIPDGMG
510 520 530 540 550
ANIPMMGTHM PMAGDMNGLS PTQALPPPLS MPSTSHCTPP PPYPTDCSIV
560 570 580 590 600
SFLARLGCSS CLDYFTTQGL TTIYQIEHYS MDDLASLKIP EQFRHAIWKG
610 620 630 640 650
ILDHRQLHEF SSPSHLLRTP SSASTVSVGS SETRGERVID AVRFTLRQTI
660 670 680
SFPPRDEWND FNFDMDARRN KQQRIKEEGE
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 AAF43486.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAF43487.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAF43488.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAF43489.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAF61624.1 differs from that shown. Reason: Frameshift at position 26. Curated
The sequence BAA32592.1 differs from that shown. Reason: Frameshift at position 26. Curated
The sequence BAA32593.1 differs from that shown. Reason: Frameshift at position 26. Curated

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:
EMBLi
GenBanki
DDBJi
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_005247843.2. [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]

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:
EMBLi
GenBanki
DDBJi
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_005247843.2. [Q9H3D4-11]
UniGeneiHs.137569.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi114181. 127 interactions.
DIPiDIP-29588N.
IntActiQ9H3D4. 64 interactions.
MINTiMINT-190238.

PTM databases

PhosphoSiteiQ9H3D4.

Polymorphism and mutation databases

BioMutaiTP63.
DMDMi57013009.

Proteomic databases

MaxQBiQ9H3D4.
PaxDbiQ9H3D4.
PRIDEiQ9H3D4.

Protocols and materials databases

DNASUi8626.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi8626.
GeneCardsiGC03P189349.
GeneReviewsiTP63.
HGNCiHGNC:15979. TP63.
HPAiCAB000083.
HPA006288.
HPA007010.
MIMi103285. phenotype.
106260. phenotype.
129400. phenotype.
603273. gene.
603543. phenotype.
604292. phenotype.
605289. phenotype.
neXtProtiNX_Q9H3D4.
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.
2440. Split hand-split foot malformation.
PharmGKBiPA162406776.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG80479.
GeneTreeiENSGT00390000015092.
HOVERGENiHBG005201.
InParanoidiQ9H3D4.
KOiK10149.
OMAiVPSSHCT.
OrthoDBiEOG7JQBNW.
PhylomeDBiQ9H3D4.
TreeFamiTF106101.

Enzyme and pathway databases

ReactomeiREACT_355377. TP53 Regulates Metabolic Genes.
SignaLinkiQ9H3D4.

Miscellaneous databases

ChiTaRSiTP63. human.
EvolutionaryTraceiQ9H3D4.
GeneWikiiTP63.
GenomeRNAii8626.
NextBioi32339.
PROiQ9H3D4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H3D4.
ExpressionAtlasiQ9H3D4. baseline and differential.
GenevisibleiQ9H3D4. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 153 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.