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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)DescriptionActionsGraphical viewLength
Metal bindingi307Zinc1 Publication1
Metal bindingi310Zinc1 Publication1
Metal bindingi361Zinc1 Publication1
Metal bindingi365Zinc1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi223 – 418Sequence analysisAdd BLAST196

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
  • transcription regulatory region DNA binding Source: InterPro
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi544K → L: Disrupts homodimer formation. 1 Publication1
Mutagenesisi551R → L: Disrupts homodimer formation. 1 Publication1
Mutagenesisi552E → L: Disrupts homodimer formation. 1 Publication1

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003712481 – 644Transcription factor cep-1Add BLAST644

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.
PeptideAtlasiQ20646.

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

Gene expression databases

BgeeiWBGene00000467.

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 interactors.
IntActiQ20646. 1 interactor.
MINTiMINT-3386616.
STRINGi6239.F52B5.5a.1.

Structurei

Secondary structure

1644
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi225 – 230Combined sources6
Helixi232 – 235Combined sources4
Beta strandi239 – 245Combined sources7
Beta strandi251 – 255Combined sources5
Beta strandi261 – 268Combined sources8
Turni271 – 275Combined sources5
Beta strandi279 – 287Combined sources9
Beta strandi289 – 291Combined sources3
Helixi293 – 296Combined sources4
Helixi308 – 312Combined sources5
Beta strandi316 – 318Combined sources3
Beta strandi322 – 327Combined sources6
Beta strandi329 – 335Combined sources7
Beta strandi339 – 345Combined sources7
Beta strandi352 – 361Combined sources10
Helixi363 – 365Combined sources3
Helixi368 – 371Combined sources4
Beta strandi373 – 382Combined sources10
Beta strandi388 – 399Combined sources12
Helixi403 – 416Combined sources14
Beta strandi532 – 538Combined sources7
Helixi539 – 554Combined sources16
Beta strandi559 – 561Combined sources3
Helixi563 – 566Combined sources4
Turni571 – 573Combined sources3
Helixi576 – 581Combined sources6
Turni585 – 587Combined sources3
Helixi588 – 594Combined sources7
Helixi601 – 608Combined sources8
Helixi612 – 616Combined sources5
Helixi620 – 622Combined sources3
Helixi623 – 641Combined sources19

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ20646.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni528 – 555Required for tertiary structure stability of the protein1 PublicationAdd BLAST28

Sequence similaritiesi

Belongs to the p53 family.Curated

Phylogenomic databases

eggNOGiENOG410K8NG. Eukaryota.
ENOG4110K6I. LUCA.
HOGENOMiHOG000111546.
InParanoidiQ20646.
OMAiVAYPRRD.
OrthoDBiEOG091G0O0N.

Family and domain databases

CDDicd08367. P53. 1 hit.
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)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0530851 – 447Missing in isoform b. 1 PublicationAdd BLAST447

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.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T4WX-ray2.10A223-418[»]
2RP5NMR-A/B514-644[»]
ProteinModelPortaliQ20646.
SMRiQ20646.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi38050. 2 interactors.
IntActiQ20646. 1 interactor.
MINTiMINT-3386616.
STRINGi6239.F52B5.5a.1.

Proteomic databases

EPDiQ20646.
PaxDbiQ20646.
PeptideAtlasiQ20646.

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.

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.
OrthoDBiEOG091G0O0N.

Miscellaneous databases

EvolutionaryTraceiQ20646.
PROiQ20646.

Gene expression databases

BgeeiWBGene00000467.

Family and domain databases

CDDicd08367. P53. 1 hit.
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...

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: November 2, 2016
This is version 119 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.