Q20646 (CEP1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription factor cep-1

Alternative name(s):
C.elegans p53-like protein 1

Gene names

Name:	cep-1
ORF Names:	F52B5.5

Organism

Caenorhabditis elegans

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	644 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcriptional activator that binds the same DNA consensus sequence as p53. Has a role in normal development to ensure proper meiotic chromosome segregation. Promotes apoptosis under conditions of cellular and genotoxic stress in response to DNA damage, hypoxia, or starvation. However, not required for DNA repair in response to UV-C or to regulate cell-cycle progression. Required for induction of ced-13 in response to DNA damage. Regulates germline proliferation by activating phg-1. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15
Cofactor	Binds 1 zinc ion per subunit. Ref.17
Subunit structure	Homodimer. Ref.6 Ref.17
Subcellular location	Nucleus Ref.3.
Tissue specificity	Expressed in pharyngeal muscle and neurons. Ref.3
Developmental stage	Expressed in embryos and larvae. Protein levels increase during late pachytene cells. Ref.3 Ref.6
Induction	By DNA damage. Ref.9
Post-translational modification	Phosphorylated in response to IR-induced DNA damage which is thought to be mediated by akt-1. Ref.9
Disruption phenotype	Reduced numbers of germ cell corpses, hypersensitive to the lethal effects of hypoxia, increase in production of males (Him phenotype), decreased lifepan and in extreme cases embryonic lethality. Ref.1 Ref.3 Ref.5 Ref.12 Ref.15
Sequence similarities	Belongs to the p53 family.

Ontologies

Keywords
Biological process	Apoptosis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Tumor suppressor
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis Inferred from direct assay Ref.10Ref.13. Source: UniProtKB apoptotic process Inferred from mutant phenotype Ref.3. Source: WormBase dauer entry Inferred from mutant phenotype Ref.12. Source: WormBase determination of adult lifespan Inferred from mutant phenotype Ref.3Ref.14. Source: UniProtKB embryo development ending in birth or egg hatching Inferred from mutant phenotype Ref.3. Source: WormBase meiotic chromosome segregation Inferred from mutant phenotype Ref.3. Source: UniProtKB response to hypoxia Inferred from mutant phenotype Ref.3. Source: UniProtKB response to oxidative stress Inferred from mutant phenotype Ref.14. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleolus Inferred from direct assay Ref.3. Source: WormBase nucleoplasm Inferred from direct assay Ref.6. Source: WormBase
Molecular function	protein homodimerization activity Inferred from direct assay Ref.17. Source: UniProtKB sequence-specific DNA binding Inferred from direct assay Ref.16. Source: UniProtKB sequence-specific DNA binding transcription factor activity Inferred from direct assay Ref.1Ref.13. Source: UniProtKB zinc ion binding Inferred from direct assay Ref.17. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform a Ref.1 (identifier: Q20646-1)

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.

Isoform b Ref.2 (identifier: Q20646-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-447: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 644

644

Transcription factor cep-1

PRO_0000371248

Regions

DNA binding

223 – 418

196

Ref.16

Region

528 – 555

28

Required for tertiary structure stability of the protein Ref.17

Sites

Metal binding

307

1

Zinc Ref.17

Metal binding

310

1

Zinc Ref.17

Metal binding

361

1

Zinc Ref.17

Metal binding

365

1

Zinc Ref.17

Natural variations

Alternative sequence

1 – 447

447

Missing in isoform b. Ref.2

VSP_053085

Experimental info

Mutagenesis

544

1

K → L: Disrupts homodimer formation. Ref.17

Mutagenesis

551

1

R → L: Disrupts homodimer formation. Ref.17

Mutagenesis

552

1

E → L: Disrupts homodimer formation. Ref.17

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

644

Helix Strand Turn

Details...

Beta strand

225 – 230

6

Helix

232 – 235

4

Beta strand

239 – 245

7

Beta strand

251 – 255

5

Beta strand

261 – 268

8

Turn

271 – 275

5

Beta strand

279 – 287

9

Beta strand

289 – 291

3

Helix

293 – 296

4

Helix

308 – 312

5

Beta strand

316 – 318

3

Beta strand

322 – 327

6

Beta strand

329 – 335

7

Beta strand

341 – 345

5

Beta strand

352 – 361

10

Helix

363 – 365

3

Helix

368 – 371

4

Beta strand

373 – 382

10

Beta strand

388 – 399

12

Helix

403 – 416

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform a [UniParc]. Last modified March 1, 2002. Version 2. Checksum: AED566E5461212B0	FASTA	644	74,569
	10 20 30 40 50 60 MEPDDSQLSD ILKDARIPDS QDIGVNLTQN LSFDTVQKMI DGVFTPIFSQ GTEDSLEKDI 70 80 90 100 110 120 LKTPGISTIY NGILGNGEET KKRTPKISDA FEPDLNTSGD VFDSDKSEDG LMNDESYLSN 130 140 150 160 170 180 TTLSQVVLDS QKYEYLRVRT EEEQQLVIEK RARERFIRKS MKIAEETALS YENDGSRELS 190 200 210 220 230 240 ETMTQKVTQM DFTETNVPFD GNDESSNLAV RVQSDMNLNE DCEKWMEIDV LKQKVAKSSD 250 260 270 280 290 300 MAFAISSEHE KYLWTKMGCL VPIQVKWKLD KRHFNSNLSL RIRFVKYDKK ENVEYAIRNP 310 320 330 340 350 360 RSDVMKCRSH TEREQHFPFD SFFYIRNSEH EFSYSAEKGS TFTLIMYPGA VQANFDIIFM 370 380 390 400 410 420 CQEKCLDLDD RRKTMCLAVF LDDENGNEIL HAYIKQVRIV AYPRRDWKNF CEREDAKQKD 430 440 450 460 470 480 FRFPELPAYK KASLESINIK QEVNLENMFN VTNTTAQMEP STSYSSPSNS NNRKRFLNEC 490 500 510 520 530 540 DSPNNDYTMM HRTPPVTGYA SRLHGCVPPI ETEHENCQSP SMKRSRCTNY SFRTLTLSTA 550 560 570 580 590 600 EYTKVVEFLA REAKVPRYTW VPTQVVSHIL PTEGLERFLT AIKAGHDSVL FNANGIYTMG 610 620 630 640 DMIREFEKHN DIFERIGIDS SKLSKYYEAF LSFYRIQEAM KLPK
	Isoform b [UniParc]. Checksum: 2CB433F379CF8608	FASTA	197	22,646
	10 20 30 40 50 60 MFNVTNTTAQ MEPSTSYSSP SNSNNRKRFL NECDSPNNDY TMMHRTPPVT GYASRLHGCV 70 80 90 100 110 120 PPIETEHENC QSPSMKRSRC TNYSFRTLTL STAEYTKVVE FLAREAKVPR YTWVPTQVVS 130 140 150 160 170 180 HILPTEGLER FLTAIKAGHD SVLFNANGIY TMGDMIREFE KHNDIFERIG IDSSKLSKYY 190 EAFLSFYRIQ EAMKLPK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The C. elegans homolog of the p53 tumor suppressor is required for DNA damage-induced apoptosis." Schumacher B., Hofmann K., Boulton S.J., Gartner A. Curr. Biol. 11:1722-1727(2001) [PubMed: 11696333] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, DISRUPTION PHENOTYPE.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING. Strain: Bristol N2.
[3]	"Caenorhabditis elegans p53: role in apoptosis, meiosis, and stress resistance." Derry W.B., Putzke A.P., Rothman J.H. Science 294:591-595(2001) [PubMed: 11557844] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[4]	"Caenorhabditis elegans HUS-1 is a DNA damage checkpoint protein required for genome stability and EGL-1-mediated apoptosis." Hofmann E.R., Milstein S., Boulton S.J., Ye M., Hofmann J.J., Stergiou L., Gartner A., Vidal M., Hengartner M.O. Curr. Biol. 12:1908-1918(2002) [PubMed: 12445383] [Abstract] Cited for: FUNCTION.
[5]	"Caenorhabditis elegans ABL-1 antagonizes p53-mediated germline apoptosis after ionizing irradiation." Deng X., Hofmann E.R., Villanueva A., Hobert O., Capodieci P., Veach D.R., Yin X., Campodonico L., Glekas A., Cordon-Cardo C., Clarkson B., Bornmann W.G., Fuks Z., Hengartner M.O., Kolesnick R. Nat. Genet. 36:906-912(2004) [PubMed: 15273685] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[6]	"Translational repression of C. elegans p53 by GLD-1 regulates DNA damage-induced apoptosis." Schumacher B., Hanazawa M., Lee M.-H., Nayak S., Volkmann K., Hofmann E.R., Hengartner M.O., Schedl T., Gartner A. Cell 120:357-368(2005) [PubMed: 15707894] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE.
[7]	"C. elegans ced-13 can promote apoptosis and is induced in response to DNA damage." Schumacher B., Schertel C., Wittenburg N., Tuck S., Mitani S., Gartner A., Conradt B., Shaham S. Cell Death Differ. 12:153-161(2005) [PubMed: 15605074] [Abstract] Cited for: FUNCTION.
[8]	"Distinct modes of ATR activation after replication stress and DNA double-strand breaks in Caenorhabditis elegans." Garcia-Muse T., Boulton S.J. EMBO J. 24:4345-4355(2005) [PubMed: 16319925] [Abstract] Cited for: FUNCTION.
[9]	"AKT-1 regulates DNA-damage-induced germline apoptosis in C. elegans." Quevedo C., Kaplan D.R., Derry W.B. Curr. Biol. 17:286-292(2007) [PubMed: 17276923] [Abstract] Cited for: FUNCTION, INDUCTION, PHOSPHORYLATION.
[10]	"Regulation of developmental rate and germ cell proliferation in Caenorhabditis elegans by the p53 gene network." Derry W.B., Bierings R., van Iersel M., Satkunendran T., Reinke V., Rothman J.H. Cell Death Differ. 14:662-670(2007) [PubMed: 17186023] [Abstract] Cited for: FUNCTION.
[11]	"The nucleotide excision repair pathway is required for UV-C-induced apoptosis in Caenorhabditis elegans." Stergiou L., Doukoumetzidis K., Sendoel A., Hengartner M.O. Cell Death Differ. 14:1129-1138(2007) [PubMed: 17347667] [Abstract] Cited for: FUNCTION.
[12]	"Reduced expression of the Caenorhabditis elegans p53 ortholog cep-1 results in increased longevity." Arum O., Johnson T.E. J. Gerontol. 62:951-959(2007) [PubMed: 17895432] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[13]	"Transcriptional profiling in C. elegans suggests DNA damage dependent apoptosis as an ancient function of the p53 family." Greiss S., Schumacher B., Grandien K., Rothblatt J., Gartner A. BMC Genomics 9:334-334(2008) [PubMed: 18627611] [Abstract] Cited for: FUNCTION.
[14]	"A novel role for the SMG-1 kinase in lifespan and oxidative stress resistance in Caenorhabditis elegans." Masse I., Molin L., Mouchiroud L., Vanhems P., Palladino F., Billaud M., Solari F. PLoS ONE 3:E3354-E3354(2008) [PubMed: 18836529] [Abstract] Cited for: FUNCTION.
[15]	"The Caenorhabditis elegans ing-3 gene regulates ionizing radiation-induced germ-cell apoptosis in a p53-associated pathway." Luo J., Shah S., Riabowol K., Mains P.E. Genetics 181:473-482(2009) [PubMed: 19015549] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[16]	"Structural differences in the DNA binding domains of human p53 and its C. elegans ortholog Cep-1." Huyen Y., Jeffrey P.D., Derry W.B., Rothman J.H., Pavletich N.P., Stavridi E.S., Halazonetis T.D. Structure 12:1237-1243(2004) [PubMed: 15242600] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), DNA-BINDING.
[17]	"Structural evolution of C-terminal domains in the p53 family." Ou H.D., Loehr F., Vogel V., Maentele W., Doetsch V. EMBO J. 26:3463-3473(2007) [PubMed: 17581633] [Abstract] Cited for: STRUCTURE BY NMR OF 514-644, DIMERIZATION, MUTAGENESIS OF LYS-544; ARG-551 AND GLU-552, ZINC-BINDING SITES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF440800 mRNA. Translation: AAL28139.1.
Z75541 Genomic DNA. Translation: CAA99857.2.
Z75541 Genomic DNA. Translation: CAI79201.1.

PIR

T22495.

RefSeq

NP_001021478.1. NM_001026307.4.
NP_001021479.1. NM_001026308.3.

UniGene

Cel.18659.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1T4W	X-ray	2.10	A	223-418	[»]
2RP5	NMR	-	A/B	514-644	[»]

ProteinModelPortal

Q20646.

SMR

Q20646. Positions 223-418, 528-644.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-3386616.

STRING

Q20646.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

F52B5.5a.1; F52B5.5a.1; F52B5.5.
F52B5.5a.2; F52B5.5a.2; F52B5.5.

GeneID

172616.

KEGG

cel:F52B5.5.

UCSC

F52B5.5a.1. c. elegans.

Organism-specific databases

CTD

172616.

WormBase

F52B5.5a; CE29805; WBGene00000467; cep-1.
F52B5.5b; CE38369; WBGene00000467; cep-1.

Phylogenomic databases

GeneTree

EMGT00050000020401.

HOGENOM

HBG379245.

InParanoid

Q20646.

OMA

VAYPRRD.

Gene expression databases

ArrayExpress

Q20646.

Family and domain databases

InterPro

IPR008967. p53-like_TF_DNA-bd.
IPR012346. p53/RUNT-type_TF_DNA-bd.
IPR015367. Trans_fact_CEP1_DNA-bd.
[Graphical view]

Gene3D

G3DSA:2.60.40.720. p53_RUNT_DNA_bd. 1 hit.

Pfam

PF09287. CEP1-DNA_bind. 1 hit.
[Graphical view]

SUPFAM

SSF49417. P53_like_DNA_bnd. 1 hit.

ProtoNet

Search...

Other

NextBio

876273.

Entry information

Entry name

CEP1_CAEEL

Accession

Primary (citable) accession number: Q20646
Secondary accession number(s): Q564Z1, Q95V13

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	March 1, 2002
Last modified:	December 14, 2011
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project