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Protein

Transcription factor cep-1

Gene

cep-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional activator that binds the same DNA consensus sequence as p53 (PubMed:11696333, PubMed:15242600). Has a role in normal development to ensure proper meiotic chromosome segregation (PubMed:11557844, PubMed:12445383). Promotes apoptosis under conditions of cellular and genotoxic stress in response to DNA damage, hypoxia, or starvation (PubMed:11696333, PubMed:11557844, PubMed:12445383, PubMed:15273685, PubMed:17186023, PubMed:18836529, PubMed:21901106). However, not required for DNA repair in response to UV-C or to regulate cell-cycle progression (PubMed:17347667). Regulates germline apoptosis in response to DNA damage (PubMed:11696333, PubMed:15273685, PubMed:15707894, PubMed:16319925, PubMed:17276923, PubMed:17186023, PubMed:19015549).Required for induction of ced-13 in response to DNA damage (PubMed:15605074). Regulates germline proliferation by activating phg-1 (PubMed:17186023). Regulates DNA damage-induced apoptosis by inducing transcription of the programmed cell death activator egl-1 (PubMed:12445383, PubMed:19521535). Negatively regulates lifespan (PubMed:17895432, PubMed:18836529).17 Publications

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi307 – 3071Zinc1 Publication
Metal bindingi310 – 3101Zinc1 Publication
Metal bindingi361 – 3611Zinc1 Publication
Metal bindingi365 – 3651Zinc1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi223 – 418196Sequence analysisAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: WormBase
  • protein homodimerization activity Source: UniProtKB
  • sequence-specific DNA binding Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • determination of adult lifespan Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
  • meiotic chromosome segregation Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: WormBase
  • regulation of transcription, DNA-templated Source: UniProtKB
  • response to hypoxia Source: UniProtKB
  • response to oxidative stress Source: UniProtKB
  • response to starvation Source: WormBase
  • signal transduction in response to DNA damage Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor cep-1Imported
Alternative name(s):
C.elegans p53-like protein 1
Gene namesi
Name:cep-1Imported
ORF Names:F52B5.5
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome I

Organism-specific databases

WormBaseiF52B5.5a; CE29805; WBGene00000467; cep-1.
F52B5.5b; CE38369; WBGene00000467; cep-1.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • nucleolus Source: WormBase
  • nucleoplasm Source: WormBase
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

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. In cep-1 and prmt-5 double mutants, germline cell death and up-regulation of egl-1 mRNA induced by gamma irradiation is prevented (PubMed:19521535).6 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi544 – 5441K → L: Disrupts homodimer formation. 1 Publication
Mutagenesisi551 – 5511R → L: Disrupts homodimer formation. 1 Publication
Mutagenesisi552 – 5521E → L: Disrupts homodimer formation. 1 Publication

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 644644Transcription factor cep-1PRO_0000371248Add
BLAST

Post-translational modificationi

Phosphorylated in response to IR-induced DNA damage which is thought to be mediated by akt-1.1 Publication

Proteomic databases

EPDiQ20646.
PaxDbiQ20646.

Expressioni

Tissue specificityi

Expressed in pharyngeal muscle and neurons.1 Publication

Developmental stagei

Expressed in embryos and larvae (PubMed:11557844, PubMed:15707894). Expressed in the distal zone of mitotic germline and in late pachytene, diplotene and diakinesis stages of meiotic germline (PubMed:11557844, PubMed:15707894, PubMed:21901106).3 Publications

Inductioni

By DNA damage.1 Publication

Interactioni

Subunit structurei

Homodimer (PubMed:15707894). Interacts (via C-terminus domain) with prmt-5; not methylated by prmt-5 (PubMed:19521535). Interacts with cbp-1 (via HAT domain); cep-1 transcriptional activity may be inhibited by interaction with methylated cbp-1 (PubMed:19521535). Component of a complex that contains prmt-5 and cbp-1 (PubMed:19521535).1 Publication2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi38050. 2 interactions.
IntActiQ20646. 1 interaction.
MINTiMINT-3386616.
STRINGi6239.F52B5.5a.1.

Structurei

Secondary structure

1
644
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi225 – 2306Combined sources
Helixi232 – 2354Combined sources
Beta strandi239 – 2457Combined sources
Beta strandi251 – 2555Combined sources
Beta strandi261 – 2688Combined sources
Turni271 – 2755Combined sources
Beta strandi279 – 2879Combined sources
Beta strandi289 – 2913Combined sources
Helixi293 – 2964Combined sources
Helixi308 – 3125Combined sources
Beta strandi316 – 3183Combined sources
Beta strandi322 – 3276Combined sources
Beta strandi329 – 3357Combined sources
Beta strandi339 – 3457Combined sources
Beta strandi352 – 36110Combined sources
Helixi363 – 3653Combined sources
Helixi368 – 3714Combined sources
Beta strandi373 – 38210Combined sources
Beta strandi388 – 39912Combined sources
Helixi403 – 41614Combined sources
Beta strandi532 – 5387Combined sources
Helixi539 – 55416Combined sources
Beta strandi559 – 5613Combined sources
Helixi563 – 5664Combined sources
Turni571 – 5733Combined sources
Helixi576 – 5816Combined sources
Turni585 – 5873Combined sources
Helixi588 – 5947Combined sources
Helixi601 – 6088Combined sources
Helixi612 – 6165Combined sources
Helixi620 – 6223Combined sources
Helixi623 – 64119Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T4WX-ray2.10A223-418[»]
2RP5NMR-A/B514-644[»]
ProteinModelPortaliQ20646.
SMRiQ20646. Positions 223-418, 528-644.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ20646.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni528 – 55528Required for tertiary structure stability of the protein1 PublicationAdd
BLAST

Sequence similaritiesi

Belongs to the p53 family.Curated

Phylogenomic databases

eggNOGiENOG410K8NG. Eukaryota.
ENOG4110K6I. LUCA.
HOGENOMiHOG000111546.
InParanoidiQ20646.
OMAiVAYPRRD.
OrthoDBiEOG7TF7F6.

Family and domain databases

Gene3Di2.60.40.720. 1 hit.
InterProiIPR008967. p53-like_TF_DNA-bd.
IPR012346. p53/RUNT-type_TF_DNA-bd.
IPR011615. p53_DNA-bd.
IPR015367. Trans_fact_CEP1_DNA-bd.
[Graphical view]
PfamiPF09287. CEP1-DNA_bind. 1 hit.
[Graphical view]
SUPFAMiSSF49417. SSF49417. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform a1 Publication (identifier: Q20646-1) [UniParc]FASTAAdd to basket

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
MEPDDSQLSD ILKDARIPDS QDIGVNLTQN LSFDTVQKMI DGVFTPIFSQ
60 70 80 90 100
GTEDSLEKDI LKTPGISTIY NGILGNGEET KKRTPKISDA FEPDLNTSGD
110 120 130 140 150
VFDSDKSEDG LMNDESYLSN TTLSQVVLDS QKYEYLRVRT EEEQQLVIEK
160 170 180 190 200
RARERFIRKS MKIAEETALS YENDGSRELS ETMTQKVTQM DFTETNVPFD
210 220 230 240 250
GNDESSNLAV RVQSDMNLNE DCEKWMEIDV LKQKVAKSSD MAFAISSEHE
260 270 280 290 300
KYLWTKMGCL VPIQVKWKLD KRHFNSNLSL RIRFVKYDKK ENVEYAIRNP
310 320 330 340 350
RSDVMKCRSH TEREQHFPFD SFFYIRNSEH EFSYSAEKGS TFTLIMYPGA
360 370 380 390 400
VQANFDIIFM CQEKCLDLDD RRKTMCLAVF LDDENGNEIL HAYIKQVRIV
410 420 430 440 450
AYPRRDWKNF CEREDAKQKD FRFPELPAYK KASLESINIK QEVNLENMFN
460 470 480 490 500
VTNTTAQMEP STSYSSPSNS NNRKRFLNEC DSPNNDYTMM HRTPPVTGYA
510 520 530 540 550
SRLHGCVPPI ETEHENCQSP SMKRSRCTNY SFRTLTLSTA EYTKVVEFLA
560 570 580 590 600
REAKVPRYTW VPTQVVSHIL PTEGLERFLT AIKAGHDSVL FNANGIYTMG
610 620 630 640
DMIREFEKHN DIFERIGIDS SKLSKYYEAF LSFYRIQEAM KLPK
Length:644
Mass (Da):74,569
Last modified:March 1, 2002 - v2
Checksum:iAED566E5461212B0
GO
Isoform b1 Publication (identifier: Q20646-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.Curated
Show »
Length:197
Mass (Da):22,646
Checksum:i2CB433F379CF8608
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 447447Missing in isoform b. 1 PublicationVSP_053085Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF440800 mRNA. Translation: AAL28139.1.
Z75541 Genomic DNA. Translation: CAA99857.2.
Z75541 Genomic DNA. Translation: CAI79201.1.
PIRiT22495.
RefSeqiNP_001021478.1. NM_001026307.5. [Q20646-1]
NP_001021479.1. NM_001026308.4. [Q20646-2]
UniGeneiCel.18659.

Genome annotation databases

EnsemblMetazoaiF52B5.5a.1; F52B5.5a.1; WBGene00000467. [Q20646-1]
F52B5.5a.2; F52B5.5a.2; WBGene00000467. [Q20646-1]
GeneIDi172616.
KEGGicel:CELE_F52B5.5.
UCSCiF52B5.5a.1. c. elegans. [Q20646-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF440800 mRNA. Translation: AAL28139.1.
Z75541 Genomic DNA. Translation: CAA99857.2.
Z75541 Genomic DNA. Translation: CAI79201.1.
PIRiT22495.
RefSeqiNP_001021478.1. NM_001026307.5. [Q20646-1]
NP_001021479.1. NM_001026308.4. [Q20646-2]
UniGeneiCel.18659.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T4WX-ray2.10A223-418[»]
2RP5NMR-A/B514-644[»]
ProteinModelPortaliQ20646.
SMRiQ20646. Positions 223-418, 528-644.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi38050. 2 interactions.
IntActiQ20646. 1 interaction.
MINTiMINT-3386616.
STRINGi6239.F52B5.5a.1.

Proteomic databases

EPDiQ20646.
PaxDbiQ20646.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF52B5.5a.1; F52B5.5a.1; WBGene00000467. [Q20646-1]
F52B5.5a.2; F52B5.5a.2; WBGene00000467. [Q20646-1]
GeneIDi172616.
KEGGicel:CELE_F52B5.5.
UCSCiF52B5.5a.1. c. elegans. [Q20646-1]

Organism-specific databases

CTDi172616.
WormBaseiF52B5.5a; CE29805; WBGene00000467; cep-1.
F52B5.5b; CE38369; WBGene00000467; cep-1.

Phylogenomic databases

eggNOGiENOG410K8NG. Eukaryota.
ENOG4110K6I. LUCA.
HOGENOMiHOG000111546.
InParanoidiQ20646.
OMAiVAYPRRD.
OrthoDBiEOG7TF7F6.

Miscellaneous databases

EvolutionaryTraceiQ20646.
PROiQ20646.

Family and domain databases

Gene3Di2.60.40.720. 1 hit.
InterProiIPR008967. p53-like_TF_DNA-bd.
IPR012346. p53/RUNT-type_TF_DNA-bd.
IPR011615. p53_DNA-bd.
IPR015367. Trans_fact_CEP1_DNA-bd.
[Graphical view]
PfamiPF09287. CEP1-DNA_bind. 1 hit.
[Graphical view]
SUPFAMiSSF49417. SSF49417. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  16. "Caenorhabditis elegans protein arginine methyltransferase PRMT-5 negatively regulates DNA damage-induced apoptosis."
    Yang M., Sun J., Sun X., Shen Q., Gao Z., Yang C.
    PLoS Genet. 5:E1000514-E1000514(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRMT-5 AND CBP-1, DISRUPTION PHENOTYPE.
  17. "Regulation of Caenorhabditis elegans p53/CEP-1-dependent germ cell apoptosis by Ras/MAPK signaling."
    Rutkowski R., Dickinson R., Stewart G., Craig A., Schimpl M., Keyse S.M., Gartner A.
    PLoS Genet. 7:E1002238-E1002238(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.
  18. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), FUNCTION, DNA-BINDING.
  19. "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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 514-644, DIMERIZATION, MUTAGENESIS OF LYS-544; ARG-551 AND GLU-552, ZINC-BINDING SITES.

Entry informationi

Entry nameiCEP1_CAEEL
AccessioniPrimary (citable) accession number: Q20646
Secondary accession number(s): Q564Z1, Q95V13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: March 1, 2002
Last modified: July 6, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.