Q9H3D4 (P63_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	TP63
Synonyms:	KET, P63, P73H, P73L, TP73L

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	680 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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. 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 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. 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 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. 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 hypodontiaand 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 process	Apoptosis Notch signaling pathway Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative promoter usage Alternative splicing
Disease	Disease mutation Ectodermal dysplasia
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Developmental protein
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA 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 cell aging Inferred from electronic annotation. Source: Compara cellular response to UV Inferred from Biological aspect of Ancestor. Source: RefGenome chromatin remodeling Inferred from electronic annotation. Source: Compara cloacal septation Inferred from electronic annotation. Source: Compara ectoderm and mesoderm interaction Inferred from electronic annotation. Source: Compara embryonic limb morphogenesis Inferred from electronic annotation. Source: Compara epithelial cell development Inferred from electronic annotation. Source: Compara establishment of planar polarity Inferred from electronic annotation. Source: Compara female genitalia morphogenesis Inferred from electronic annotation. Source: Compara hair follicle morphogenesis Inferred from electronic annotation. Source: Compara induction of apoptosis Traceable author statement Ref.4. Source: ProtInc 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: Compara keratinocyte proliferation Inferred from electronic annotation. Source: Compara mitotic G1 DNA damage checkpoint Inferred from Biological aspect of Ancestor. Source: RefGenome multicellular organismal aging Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of keratinocyte differentiation Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from Biological aspect of Ancestor. Source: RefGenome neuron apoptotic process Inferred from electronic annotation. Source: Compara odontogenesis of dentin-containing tooth Inferred from electronic annotation. Source: Compara polarized epithelial cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of Notch signaling pathway Inferred from direct assay Ref.15. Source: UniProtKB positive regulation of mesenchymal cell proliferation Inferred from electronic annotation. Source: Compara 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 post-anal tail morphogenesis Inferred from electronic annotation. Source: Compara prostatic bud formation Inferred from electronic annotation. Source: Compara protein homotetramerization Inferred from physical interaction Ref.13. Source: UniProtKB proximal/distal pattern formation Inferred from electronic annotation. Source: Compara 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: Compara skin morphogenesis Inferred from electronic annotation. Source: Compara smooth muscle tissue development Inferred from electronic annotation. Source: Compara squamous basal epithelial stem cell differentiation involved in prostate gland acinus development Inferred from electronic annotation. Source: Compara sympathetic nervous system development Inferred from electronic annotation. Source: Compara urinary bladder development Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from direct assay. Source: HPA 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 transcription factor complex Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	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: Compara 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 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FUS	P35637	2	EBI-2337775,EBI-400434
HNRNPK	P61978	2	EBI-2337775,EBI-304185
NIPSNAP3A	Q9UFN0	2	EBI-2337775,EBI-716291
SMAD2	Q15796	3	EBI-2337775,EBI-1040141
TP53	P04637	5	EBI-2337775,EBI-366083

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 680

680

Tumor protein 63

PRO_0000185729

Regions

Domain

541 – 607

67

SAM

DNA binding

170 – 362

193

Ref.10

Region

1 – 107

107

Transcription activation

Region

352 – 388

37

Interaction with HIPK2

Region

394 – 443

50

Oligomerization

Region

610 – 680

71

Transactivation inhibition

Compositional bias

437 – 444

8

Poly-Gln

Sites

Metal binding

244

1

Zinc By similarity

Metal binding

247

1

Zinc By similarity

Metal binding

308

1

Zinc By similarity

Metal binding

312

1

Zinc By similarity

Amino acid modifications

Cross-link

676

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

Natural variations

Alternative sequence

1 – 108

108

MNFET…SDPMW → MLYLENNAQTQFSE in isoform 2, isoform 4, isoform 6, isoform 8, isoform 10 and isoform 12.

VSP_012465

Alternative sequence

109 – 193

85

Missing in isoform 9 and isoform 10.

VSP_012466

Alternative sequence

373 – 377

5

GTKRP → A in isoform 11 and isoform 12.

VSP_012467

Alternative sequence

450 – 680

231

QTSIQ…KEEGE → HLLSACFRNELVEPRRETPK QSDVFFRHSKPPNRSVYP in isoform 5 and isoform 6.

VSP_012468

Alternative sequence

503 – 680

178

IPMMG…KEEGE → RSGKSENP in isoform 7 and isoform 8.

VSP_012469

Alternative sequence

551 – 680

130

SFLAR…KEEGE → RIWQV in isoform 3 and isoform 4.

VSP_012470

Natural variant

129

1

S → L. Ref.36

VAR_035126

Natural variant

184

1

S → L in head and neck cancer. Ref.4

VAR_020866

Natural variant

187

1

A → P in lung carcinoma; somatic mutation. Ref.4

VAR_020867

Natural variant

193

1

T → TP in SHFM4. Ref.30

VAR_032736

Natural variant

204

1

Q → L in cervical cancer. Ref.4

VAR_020868

Natural variant

232

1

K → E in SHFM4. Ref.30

VAR_032737

Natural variant

233

1

K → E in SHFM4. Ref.27

VAR_020869

Natural variant

243

1

R → Q in EEC3. Ref.26 Ref.30

VAR_020870

Natural variant

243

1

R → W in EEC3. Ref.26 Ref.30

VAR_020871

Natural variant

266

1

R → Q in EEC3. Ref.30

VAR_032738

Natural variant

279

1

P → H in colon cancer. Ref.5

VAR_020872

Natural variant

308

1

C → Y in EEC3. Ref.30

VAR_032739

Natural variant

311

1

S → N in EEC3. Ref.30

VAR_032740

Natural variant

318

1

R → C in EEC3. Ref.30

VAR_032741

Natural variant

318

1

R → 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 variant

318

1

R → Q in EEC3. Ref.30

VAR_032742

Natural variant

319

1

R → C in EEC3. Ref.27 Ref.30

VAR_020874

Natural variant

319

1

R → H in EEC3 and SHFM4. Ref.30

VAR_032743

Natural variant

319

1

R → S in EEC3. Ref.30

VAR_032744

Natural variant

337

1

R → Q in ADULT syndrome; confers novel transcription activation capacity on isoform 6. Ref.31

VAR_020875

Natural variant

343

1

R → Q in EEC3. Ref.27 Ref.30

VAR_020876

Natural variant

343

1

R → W in EEC3. Ref.30

VAR_032745

Natural variant

345

1

C → R in EEC3; abolishes transcription activation. Ref.26 Ref.30

VAR_020877

Natural variant

347

1

C → S in EEC3. Ref.30

VAR_032746

Natural variant

348

1

P → S in EEC3. Ref.30

VAR_032747

Natural variant

351

1

D → G in EEC3. Ref.32

VAR_020878

Natural variant

351

1

D → H in EEC3. Ref.30

VAR_032748

Natural variant

352

1

R → G in EDRH and OFC8. Ref.36

VAR_035127

Natural variant

549

1

I → T in EDRH. Ref.35

VAR_035128

Natural variant

553

1

L → F in AEC. Ref.29

VAR_020879

Natural variant

560

1

S → A in ovarian cancer. Ref.5

VAR_020880

Natural variant

561

1

C → G in AEC. Ref.29

VAR_020881

Natural variant

580

1

S → P in EDRH. Ref.34

VAR_035129

Natural variant

603

1

D → H. Ref.36

VAR_035130

Isoform 2:

Natural variant

6

1

N → H in ADULT syndrome.

Isoform 4:

Natural variant

6

1

N → H in ADULT syndrome.

Isoform 6:

Natural variant

6

1

N → H in ADULT syndrome.

Isoform 8:

Natural variant

6

1

N → H in ADULT syndrome.

Isoform 10:

Natural variant

6

1

N → H in ADULT syndrome.

Isoform 12:

Natural variant

6

1

N → H in ADULT syndrome.

Experimental info

Mutagenesis

55

1

F → A: Abrogates transcriptional activity and interaction with transactivation inhibition domain; when associated with A-59 and A-62. Ref.17

Mutagenesis

59

1

W → A: Abrogates transcriptional activity and interaction with transactivation inhibition domain; when associated with A-55 and A-62. Ref.17

Mutagenesis

62

1

L → A: Abrogates transcriptional activity and interaction with transactivation inhibition domain; when associated with A-55 and A-59. Ref.17

Mutagenesis

543

1

Y → F: Abolishes ubiquitination. Ref.21

Sequence conflict

125

1

Q → R in BAA32433. Ref.1

Sequence conflict

154

1

S → P in BAA32433. Ref.1

Sequence conflict

177

1

F → S in BAA32433. Ref.1

Sequence conflict

378

1

F → S in AAC24830. Ref.10

Sequence conflict

536

1

H → Q in CAA76562. Ref.2

Sequence conflict

551

1

S → G in BAA32593. Ref.4

Sequence conflict

551

1

S → G in AAF43487. Ref.7

Sequence conflict

551

1

S → G in AAF43491. Ref.7

Secondary structure

1

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680

Helix Strand Turn

Details...

Beta strand

156 – 161

6

Helix

173 – 175

3

Beta strand

178 – 180

3

Beta strand

187 – 189

3

Beta strand

191 – 195

5

Turn

196 – 199

4

Beta strand

200 – 203

4

Beta strand

209 – 214

6

Beta strand

224 – 233

10

Turn

234 – 238

5

Helix

245 – 249

5

Turn

252 – 256

5

Beta strand

263 – 269

7

Beta strand

274 – 277

4

Turn

279 – 281

3

Beta strand

284 – 289

6

Beta strand

300 – 306

7

Turn

313 – 318

6

Beta strand

321 – 328

8

Beta strand

330 – 332

3

Beta strand

334 – 343

10

Helix

348 – 355

8

Beta strand

369 – 372

4

Beta strand

401 – 407

7

Helix

408 – 426

19

Helix

429 – 436

8

Beta strand

546 – 548

3

Helix

549 – 554

6

Turn

555 – 557

3

Helix

559 – 561

3

Helix

562 – 566

5

Turn

567 – 569

3

Helix

573 – 576

4

Helix

581 – 586

6

Helix

591 – 609

19

Beta strand

613 – 615

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (TA*-alpha) (TAp63alpha) (P51B) [UniParc]. Last modified March 1, 2001. Version 1. Checksum: F66ECD45E87D9799	FASTA	680	76,785
	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
	Isoform 2 (DeltaN-alpha) (DeltaNp63 alpha) (P51delNalpha) [UniParc]. Checksum: 2E2F92ABF1AF8629	FASTA	586	65,756
	10 20 30 40 50 60 MLYLENNAQT QFSEPQYTNL GLLNSMDQQI QNGSSSTSPY NTDHAQNSVT APSPYAQPSS 70 80 90 100 110 120 TFDALSPSPA IPSNTDYPGP HSFDVSFQQS STAKSATWTY STELKKLYCQ IAKTCPIQIK 130 140 150 160 170 180 VMTPPPQGAV IRAMPVYKKA EHVTEVVKRC PNHELSREFN EGQIAPPSHL IRVEGNSHAQ 190 200 210 220 230 240 YVEDPITGRQ SVLVPYEPPQ VGTEFTTVLY NFMCNSSCVG GMNRRPILII VTLETRDGQV 250 260 270 280 290 300 LGRRCFEARI CACPGRDRKA DEDSIRKQQV SDSTKNGDGT KRPFRQNTHG IQMTSIKKRR 310 320 330 340 350 360 SPDDELLYLP VRGRETYEML LKIKESLELM QYLPQHTIET YRQQQQQQHQ HLLQKQTSIQ 370 380 390 400 410 420 SPSSYGNSSP PLNKMNSMNK LPSVSQLINP QQRNALTPTT IPDGMGANIP MMGTHMPMAG 430 440 450 460 470 480 DMNGLSPTQA LPPPLSMPST SHCTPPPPYP TDCSIVSFLA RLGCSSCLDY FTTQGLTTIY 490 500 510 520 530 540 QIEHYSMDDL ASLKIPEQFR HAIWKGILDH RQLHEFSSPS HLLRTPSSAS TVSVGSSETR 550 560 570 580 GERVIDAVRF TLRQTISFPP RDEWNDFNFD MDARRNKQQR IKEEGE
	Isoform 3 (TA*-beta) (TAp63beta) [UniParc]. Checksum: E22874BE7DBABCBE	FASTA	555	62,433
	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 PPYPTDCSIV RIWQV
	Isoform 4 (DeltaN-beta) (DeltaNp63 beta) (P51delNbeta) [UniParc]. Checksum: 68B63547A46C1B05	FASTA	461	51,404
	10 20 30 40 50 60 MLYLENNAQT QFSEPQYTNL GLLNSMDQQI QNGSSSTSPY NTDHAQNSVT APSPYAQPSS 70 80 90 100 110 120 TFDALSPSPA IPSNTDYPGP HSFDVSFQQS STAKSATWTY STELKKLYCQ IAKTCPIQIK 130 140 150 160 170 180 VMTPPPQGAV IRAMPVYKKA EHVTEVVKRC PNHELSREFN EGQIAPPSHL IRVEGNSHAQ 190 200 210 220 230 240 YVEDPITGRQ SVLVPYEPPQ VGTEFTTVLY NFMCNSSCVG GMNRRPILII VTLETRDGQV 250 260 270 280 290 300 LGRRCFEARI CACPGRDRKA DEDSIRKQQV SDSTKNGDGT KRPFRQNTHG IQMTSIKKRR 310 320 330 340 350 360 SPDDELLYLP VRGRETYEML LKIKESLELM QYLPQHTIET YRQQQQQQHQ HLLQKQTSIQ 370 380 390 400 410 420 SPSSYGNSSP PLNKMNSMNK LPSVSQLINP QQRNALTPTT IPDGMGANIP MMGTHMPMAG 430 440 450 460 DMNGLSPTQA LPPPLSMPST SHCTPPPPYP TDCSIVRIWQ V
	Isoform 5 (TA*-gamma) (TAp63gamma) (P51A) [UniParc]. Checksum: 86CC865BDF2643DD	FASTA	487	55,688
	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 QQHQHLLQKH LLSACFRNEL VEPRRETPKQ SDVFFRHSKP PNRSVYP
	Isoform 6 (DeltaN-gamma) (DeltaNp63gamma) (P51delNgamma) [UniParc]. Checksum: C6689B83FD701610	FASTA	393	44,658
	10 20 30 40 50 60 MLYLENNAQT QFSEPQYTNL GLLNSMDQQI QNGSSSTSPY NTDHAQNSVT APSPYAQPSS 70 80 90 100 110 120 TFDALSPSPA IPSNTDYPGP HSFDVSFQQS STAKSATWTY STELKKLYCQ IAKTCPIQIK 130 140 150 160 170 180 VMTPPPQGAV IRAMPVYKKA EHVTEVVKRC PNHELSREFN EGQIAPPSHL IRVEGNSHAQ 190 200 210 220 230 240 YVEDPITGRQ SVLVPYEPPQ VGTEFTTVLY NFMCNSSCVG GMNRRPILII VTLETRDGQV 250 260 270 280 290 300 LGRRCFEARI CACPGRDRKA DEDSIRKQQV SDSTKNGDGT KRPFRQNTHG IQMTSIKKRR 310 320 330 340 350 360 SPDDELLYLP VRGRETYEML LKIKESLELM QYLPQHTIET YRQQQQQQHQ HLLQKHLLSA 370 380 390 CFRNELVEPR RETPKQSDVF FRHSKPPNRS VYP
	Isoform 7 (TA*-delta) (TAp63delta) (P51delta) [UniParc]. Checksum: 3539D81485635FF0	FASTA	510	57,619
	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 LINPQQRNAL TPTTIPDGMG ANRSGKSENP
	Isoform 8 (DeltaN-delta) [UniParc]. Checksum: A5974A14B25E3118	FASTA	416	46,589
	10 20 30 40 50 60 MLYLENNAQT QFSEPQYTNL GLLNSMDQQI QNGSSSTSPY NTDHAQNSVT APSPYAQPSS 70 80 90 100 110 120 TFDALSPSPA IPSNTDYPGP HSFDVSFQQS STAKSATWTY STELKKLYCQ IAKTCPIQIK 130 140 150 160 170 180 VMTPPPQGAV IRAMPVYKKA EHVTEVVKRC PNHELSREFN EGQIAPPSHL IRVEGNSHAQ 190 200 210 220 230 240 YVEDPITGRQ SVLVPYEPPQ VGTEFTTVLY NFMCNSSCVG GMNRRPILII VTLETRDGQV 250 260 270 280 290 300 LGRRCFEARI CACPGRDRKA DEDSIRKQQV SDSTKNGDGT KRPFRQNTHG IQMTSIKKRR 310 320 330 340 350 360 SPDDELLYLP VRGRETYEML LKIKESLELM QYLPQHTIET YRQQQQQQHQ HLLQKQTSIQ 370 380 390 400 410 SPSSYGNSSP PLNKMNSMNK LPSVSQLINP QQRNALTPTT IPDGMGANRS GKSENP
	Isoform 9 (TA*-epsilon) [UniParc]. Checksum: F07014CB9FEF1FF2	FASTA	595	67,779
	10 20 30 40 50 60 MNFETSRCAT LQYCPDPYIQ RFVETPAHFS WKESYYRSTM SQSTQTNEFL SPEVFQHIWD 70 80 90 100 110 120 FLEQPICSVQ PIDLNFVDEP SEDGATNKIE ISMDCIRMQD SDLSDPMWYS TELKKLYCQI 130 140 150 160 170 180 AKTCPIQIKV MTPPPQGAVI RAMPVYKKAE HVTEVVKRCP NHELSREFNE GQIAPPSHLI 190 200 210 220 230 240 RVEGNSHAQY VEDPITGRQS VLVPYEPPQV GTEFTTVLYN FMCNSSCVGG MNRRPILIIV 250 260 270 280 290 300 TLETRDGQVL GRRCFEARIC ACPGRDRKAD EDSIRKQQVS DSTKNGDGTK RPFRQNTHGI 310 320 330 340 350 360 QMTSIKKRRS PDDELLYLPV RGRETYEMLL KIKESLELMQ YLPQHTIETY RQQQQQQHQH 370 380 390 400 410 420 LLQKQTSIQS PSSYGNSSPP LNKMNSMNKL PSVSQLINPQ QRNALTPTTI PDGMGANIPM 430 440 450 460 470 480 MGTHMPMAGD MNGLSPTQAL PPPLSMPSTS HCTPPPPYPT DCSIVSFLAR LGCSSCLDYF 490 500 510 520 530 540 TTQGLTTIYQ IEHYSMDDLA SLKIPEQFRH AIWKGILDHR QLHEFSSPSH LLRTPSSAST 550 560 570 580 590 VSVGSSETRG ERVIDAVRFT LRQTISFPPR DEWNDFNFDM DARRNKQQRI KEEGE
	Isoform 10 (DeltaN-epsilon) (DeltaNp73L) [UniParc]. Checksum: 31E1BEA3CA305B88	FASTA	501	56,750
	10 20 30 40 50 60 MLYLENNAQT QFSEYSTELK KLYCQIAKTC PIQIKVMTPP PQGAVIRAMP VYKKAEHVTE 70 80 90 100 110 120 VVKRCPNHEL SREFNEGQIA PPSHLIRVEG NSHAQYVEDP ITGRQSVLVP YEPPQVGTEF 130 140 150 160 170 180 TTVLYNFMCN SSCVGGMNRR PILIIVTLET RDGQVLGRRC FEARICACPG RDRKADEDSI 190 200 210 220 230 240 RKQQVSDSTK NGDGTKRPFR QNTHGIQMTS IKKRRSPDDE LLYLPVRGRE TYEMLLKIKE 250 260 270 280 290 300 SLELMQYLPQ HTIETYRQQQ QQQHQHLLQK QTSIQSPSSY GNSSPPLNKM NSMNKLPSVS 310 320 330 340 350 360 QLINPQQRNA LTPTTIPDGM GANIPMMGTH MPMAGDMNGL SPTQALPPPL SMPSTSHCTP 370 380 390 400 410 420 PPPYPTDCSI VSFLARLGCS SCLDYFTTQG LTTIYQIEHY SMDDLASLKI PEQFRHAIWK 430 440 450 460 470 480 GILDHRQLHE FSSPSHLLRT PSSASTVSVG SSETRGERVI DAVRFTLRQT ISFPPRDEWN 490 500 DFNFDMDARR NKQQRIKEEG E
	Isoform 11 (P63 delta) [UniParc]. Checksum: EB0E2C9E93C6D34A	FASTA	676	76,317
	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 GDAFRQNTHG IQMTSIKKRR SPDDELLYLP VRGRETYEML LKIKESLELM 430 440 450 460 470 480 QYLPQHTIET YRQQQQQQHQ HLLQKQTSIQ SPSSYGNSSP PLNKMNSMNK LPSVSQLINP 490 500 510 520 530 540 QQRNALTPTT IPDGMGANIP MMGTHMPMAG DMNGLSPTQA LPPPLSMPST SHCTPPPPYP 550 560 570 580 590 600 TDCSIVSFLA RLGCSSCLDY FTTQGLTTIY QIEHYSMDDL ASLKIPEQFR HAIWKGILDH 610 620 630 640 650 660 RQLHEFSSPS HLLRTPSSAS TVSVGSSETR GERVIDAVRF TLRQTISFPP RDEWNDFNFD 670 MDARRNKQQR IKEEGE
	Isoform 12 [UniParc]. Checksum: A2DC3D2E13B6B531	FASTA	582	65,288
	10 20 30 40 50 60 MLYLENNAQT QFSEPQYTNL GLLNSMDQQI QNGSSSTSPY NTDHAQNSVT APSPYAQPSS 70 80 90 100 110 120 TFDALSPSPA IPSNTDYPGP HSFDVSFQQS STAKSATWTY STELKKLYCQ IAKTCPIQIK 130 140 150 160 170 180 VMTPPPQGAV IRAMPVYKKA EHVTEVVKRC PNHELSREFN EGQIAPPSHL IRVEGNSHAQ 190 200 210 220 230 240 YVEDPITGRQ SVLVPYEPPQ VGTEFTTVLY NFMCNSSCVG GMNRRPILII VTLETRDGQV 250 260 270 280 290 300 LGRRCFEARI CACPGRDRKA DEDSIRKQQV SDSTKNGDAF RQNTHGIQMT SIKKRRSPDD 310 320 330 340 350 360 ELLYLPVRGR ETYEMLLKIK ESLELMQYLP QHTIETYRQQ QQQQHQHLLQ KQTSIQSPSS 370 380 390 400 410 420 YGNSSPPLNK MNSMNKLPSV SQLINPQQRN ALTPTTIPDG MGANIPMMGT HMPMAGDMNG 430 440 450 460 470 480 LSPTQALPPP LSMPSTSHCT PPPPYPTDCS IVSFLARLGC SSCLDYFTTQ GLTTIYQIEH 490 500 510 520 530 540 YSMDDLASLK IPEQFRHAIW KGILDHRQLH EFSSPSHLLR TPSSASTVSV GSSETRGERV 550 560 570 580 IDAVRFTLRQ TISFPPRDEW NDFNFDMDAR RNKQQRIKEE GE

References

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[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. , 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.

Web resources

GeneReviews

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 , 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.

IPI

IPI00184272.
IPI00301360.
IPI00479019.
IPI00513733.
IPI00514017.
IPI00514155.
IPI00514298.
IPI00514384.
IPI00514665.
IPI00514807.
IPI00514871.
IPI00514961.

RefSeq

NP_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.

UniGene

Hs.137569.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RG6	NMR	-	A	540-610	[»]
2RMN	NMR	-	A	153-388	[»]
2Y9T	NMR	-	A	543-622	[»]
2Y9U	X-ray	1.60	A	545-611	[»]
3QYM	X-ray	3.20	A/B/C/D/E/F/G/H	166-362	[»]
3QYN	X-ray	2.50	A/B/C/D	166-362	[»]
3US0	X-ray	2.50	A/B/C/D	166-362	[»]
3US1	X-ray	2.80	A/D	166-362	[»]
3US2	X-ray	4.20	A/B/C/D/G/H/I/J	166-362	[»]
3ZY0	X-ray	1.90	A/B/C/D	398-427	[»]
3ZY1	X-ray	2.15	A	398-441	[»]
4A9Z	X-ray	2.29	A/B/C/D	397-455	[»]

ProteinModelPortal

Q9H3D4.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29588N.

IntAct

Q9H3D4. 61 interactions.

MINT

MINT-190238.

PTM databases

PhosphoSite

Q9H3D4.

Polymorphism databases

DMDM

57013009.

Proteomic databases

PaxDb

Q9H3D4.

PRIDE

Q9H3D4.

Protocols and materials databases

DNASU

8626.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264731; ENSP00000264731; ENSG00000073282.
ENST00000320472; ENSP00000317510; ENSG00000073282.
ENST00000354600; ENSP00000346614; ENSG00000073282.
ENST00000382063; ENSP00000371495; ENSG00000073282.
ENST00000392460; ENSP00000376253; ENSG00000073282.
ENST00000392461; ENSP00000376254; ENSG00000073282.
ENST00000392463; ENSP00000376256; ENSG00000073282.
ENST00000418709; ENSP00000407144; ENSG00000073282.
ENST00000437221; ENSP00000392488; ENSG00000073282.
ENST00000440651; ENSP00000394337; ENSG00000073282.
ENST00000449992; ENSP00000387839; ENSG00000073282.
ENST00000456148; ENSP00000389485; ENSG00000073282.

GeneID

8626.

KEGG

hsa:8626.

UCSC

uc003frx.2. human.
uc003fry.2. human.
uc003frz.2. human.
uc003fsb.2. human.
uc003fsc.2. human.
uc003fsd.2. human.
uc010hzc.1. human.
uc010hzd.1. human.

Organism-specific databases

CTD

8626.

GeneCards

GC03P189349.

HGNC

HGNC:15979. TP63.

HPA

CAB000083.
HPA006288.
HPA007010.

MIM

103285. phenotype.
106260. phenotype.
129400. phenotype.
603273. gene.
603543. phenotype.
604292. phenotype.
605289. phenotype.

neXtProt

NX_Q9H3D4.

Orphanet

978. ADULT syndrome.
1071. Ankyloblepharon - ectodermal defects - cleft lip/palate.
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.

PharmGKB

PA162406776.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG80479.

HOVERGEN

HBG005201.

InParanoid

Q9H3D4.

KO

K10149.

OMA

GTTNKIE.

OrthoDB

EOG4V6ZG6.

PhylomeDB

Q9H3D4.

Gene expression databases

ArrayExpress

Q9H3D4.

Bgee

Q9H3D4.

Genevestigator

Q9H3D4.

GermOnline

ENSG00000073282. Homo sapiens.

Family and domain databases

Gene3D

1.10.150.50. 1 hit.
2.60.40.720. 1 hit.
4.10.170.10. 1 hit.

InterPro

IPR008967. p53-like_TF_DNA-bd.
IPR012346. p53/RUNT-type_TF_DNA-bd.
IPR011615. p53_DNA-bd.
IPR010991. p53_tetrameristn.
IPR002117. p53_tumour_suppressor.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
[Graphical view]

PANTHER

PTHR11447. PTHR11447. 1 hit.

Pfam

PF00870. P53. 1 hit.
PF07710. P53_tetramer. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]

PRINTS

PR00386. P53SUPPRESSR.

SMART

SM00454. SAM. 1 hit.
[Graphical view]

SUPFAM

SSF49417. P53_like_DNA_bnd. 1 hit.
SSF47719. p53_tetrameristn. 1 hit.
SSF47769. SAM_homology. 1 hit.

PROSITE

PS00348. P53. 1 hit.
PS50105. SAM_DOMAIN. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

TP63. human.

EvolutionaryTrace

Q9H3D4.

GenomeRNAi

8626.

NextBio

32339.

SOURCE

Search...

Entry information

Entry name

P63_HUMAN

Accession

Primary (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 history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 130 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.