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ELC1 elongin C [ Saccharomyces cerevisiae S288C ]

Gene ID: 856061, updated on 3-Jun-2026
Official Symbol
ELC1
Official Full Name
elongin C
Primary source
SGD:S000005967
Locus tag
YPL046C
See related
AllianceGenome:SGD:S000005967; FungiDB:YPL046C; VEuPathDB:YPL046C
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary
Contributes to ubiquitin-protein transferase activity. Involved in global genome nucleotide-excision repair and ubiquitin-dependent protein catabolic process. Part of Cul3-RING ubiquitin ligase complex; elongin complex; and nucleotide-excision repair factor 4 complex. Orthologous to human ELOC (elongin C). [provided by Alliance of Genome Resources, Jul 2025]
Orthologs
all
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See ELC1 in Genome Data Viewer
Location:
chromosome: XVI
Exon count:
1
Sequence:
Chromosome: XVI; NC_001148.4 (466644..466943, complement)

Chromosome XVI - NC_001148.4Genomic Context describing neighboring genes Neighboring gene translation elongation factor EF1B gamma Neighboring gene SAGA histone acetyltransferase complex subunit SGF11 Neighboring gene tethering complex subunit VPS16 Neighboring gene mRNA-binding ribosome biosynthesis protein NOP4

Genomic Sequence:
NC_001148.4

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Elongin from Saccharomyces cerevisiae. Koth CM, et al. J Biol Chem, 2000 Apr 14. PMID 10753924
  2. Binding of elongin A or a von Hippel-Lindau peptide stabilizes the structure of yeast elongin C. Botuyan MV, et al. Proc Natl Acad Sci U S A, 1999 Aug 3. PMID 10430890, Free PMC Article
  3. Biophysical characterization of elongin C from Saccharomyces cerevisiae. Buchberger A, et al. Biochemistry, 2000 Sep 12. PMID 10998253
  4. Solution structure and dynamics of yeast elongin C in complex with a von Hippel-Lindau peptide. Botuyan MV, et al. J Mol Biol, 2001 Sep 7. PMID 11545595
  5. Molecular cloning of DNAs encoding the regulatory subunits of elongin from Saccharomyces cerevisiae and Drosophila melanogaster. Aso T, et al. Biochem Biophys Res Commun, 1997 Dec 18. PMID 9425272

See all (40) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. miR-137 was able to promote sensitivity of PC cells to chemotherapy via inhibition of autophagy mediated by ATG5
    Title: Crystal structure of the yeast Rad7-Elc1 complex and assembly of the Rad7-Rad16-Elc1-Cul3 complex.
  2. In contrast to the DNA damage-dependent pathway, Rpb1 degradation of DNA damage-independently stalled RNAPII is independent of the E3 ligase Elc1.
    Title: Degradation of DNA damage-independently stalled RNA polymerase II is independent of the E3 ligase Elc1.
  3. that Elc1 has no function in TCR but plays an important role in GGR. Furthermore, the role of Elc1 in GGR may not be subsidiary to that of Rad7 and Rad16.
    Title: Yeast Elc1 plays an important role in global genomic repair but not in transcription coupled repair.
  4. Elongin A (Ela1) and cullin 3 (Cul3) are required for Pol II polyubiquitylation and degradation in yeast cells and an E3 comprised of elongin C (Elc1), Ela1, Cul3, and the RING finger protein Roc1 (Rbx1) mediates this process.
    Title: ELA1 and CUL3 are required along with ELC1 for RNA polymerase II polyubiquitylation and degradation in DNA-damaged yeast cells.
  5. A novel role for the yeast Elc1 protein in mediating Pol II polyubiquitylation and degradation in DNA-damaged yeast cells and propose the involvement of a ubiquitin ligase, of which Elc1 is a component, in this process.
    Title: Requirement of ELC1 for RNA polymerase II polyubiquitylation and degradation in response to DNA damage in Saccharomyces cerevisiae.
Submit: New GeneRIF Correction
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein-macromolecule adaptor activity IBA
Inferred from Biological aspect of Ancestor
more info
  
contributes_to ubiquitin-protein transferase activity IDA
Inferred from Direct Assay
more info
 PubMed 
Process Evidence Code Pubs
involved_in cellular response to UV IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in global genome nucleotide-excision repair IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in global genome nucleotide-excision repair NAS
Non-traceable Author Statement
more info
 PubMed 
involved_in nucleotide-excision repair NAS
Non-traceable Author Statement
more info
 PubMed 
involved_in response to UV IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in ubiquitin-dependent protein catabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in ubiquitin-dependent protein catabolic process IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in ubiquitin-dependent protein catabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in ubiquitin-dependent protein catabolic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in ubiquitin-dependent protein catabolic process NAS
Non-traceable Author Statement
more info
 PubMed 
Component Evidence Code Pubs
part_of Cul3-RING ubiquitin ligase complex IMP
Inferred from Mutant Phenotype
more info
 PubMed 
part_of Cul3-RING ubiquitin ligase complex IPI
Inferred from Physical Interaction
more info
 PubMed 
part_of Cul3-RING ubiquitin ligase complex NAS
Non-traceable Author Statement
more info
 PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
part_of elongin complex IBA
Inferred from Biological aspect of Ancestor
more info
  
part_of elongin complex IPI
Inferred from Physical Interaction
more info
 PubMed 
part_of nucleotide-excision repair factor 4 complex IDA
Inferred from Direct Assay
more info
 PubMed 
located_in nucleus IEA
Inferred from Electronic Annotation
more info
  
Preferred Names
elongin C
NP_015279.1
  • Elongin C, conserved among eukaryotes; forms a complex with Cul3p that polyubiquitylates monoubiquitylated RNA polymerase II to trigger its proteolysis; plays a role in global genomic repair

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001148.4 Reference assembly

    Range
    466644..466943 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001183860.1 → NP_015279.1  elongin C

    See identical proteins and their annotated locations for NP_015279.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6W3W8, O13292, Q03071
    UniProtKB/TrEMBL
    A6ZWK2, B3LL21, C7GU08, C8ZIY3, G2WPD2, N1NVZ0
    Conserved Domains (1) summary
    cd18321
    Location:5 → 99
    BTB_POZ_EloC; BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in Elongin-C (EloC) and similar proteins
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q03071.1

Gene LinkOut

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