P10862 · RAD18_YEAST

Function

function

E3 RING-finger protein, member of the UBC2/RAD6 epistasis group. Associates to the E2 ubiquitin conjugating enzyme UBC2/RAD6 to form the UBC2-RAD18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA. The UBC2-RAD18 complex cooperates with RAD5 and the UBC13-MMS2 dimer to attach mono-ubiquitin chains on 'Lys-164' of POL30, which is necessary for PRR. The UBC2-RAD18 complex is also involved in prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine.

Miscellaneous

Present with 206 molecules/cell in log phase SD medium.

Catalytic activity

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.
    EC:2.3.2.27 (UniProtKB | ENZYME | Rhea)

Pathway

Protein modification; protein ubiquitination.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site190Zn2+ (UniProtKB | ChEBI)
Binding site193Zn2+ (UniProtKB | ChEBI)
Binding site206Zn2+ (UniProtKB | ChEBI)
Binding site210Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentchromatin
Cellular Componentnucleus
Cellular ComponentRad6-Rad18 complex
Molecular Functionmetal ion binding
Molecular Functionsingle-stranded DNA binding
Molecular Functionubiquitin protein ligase activity
Biological ProcessDNA duplex unwinding
Biological Processerror-free postreplication DNA repair
Biological Processerror-free translesion synthesis
Biological Processerror-prone translesion synthesis
Biological Processpostreplication repair
Biological Processprotein monoubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Postreplication repair E3 ubiquitin-protein ligase RAD18
  • EC number
  • Alternative names
    • RING-type E3 ubiquitin transferase RAD18
    • Radiation sensitivity protein 18

Gene names

    • Name
      RAD18
    • ORF names
      YCR66W
    • Ordered locus names
      YCR066W

Organism names

Accessions

  • Primary accession
    P10862
  • Secondary accessions
    • D6VR69
    • Q58AT6

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue, cross-link.

TypeIDPosition(s)Description
ChainPRO_00000561611-487Postreplication repair E3 ubiquitin-protein ligase RAD18
Modified residue155Phosphothreonine
Modified residue174Phosphoserine
Cross-link204Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Homodimer. Interacts with E2 UBC2, forming a complex with ubiquitin ligase activity. The UBC2-RAD18 complex interacts itself with the UBC13-MMS2 ubiquitin ligase complex through direct interactions of both RAD18 and UBC13 with RAD5. Interacts also with UBC9. Binds single strand DNA.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P10862RAD6 P061045EBI-14659, EBI-19722
View interactors in UniProtKB
View CPX-2902 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for zinc finger, compositional bias, region, domain.

TypeIDPosition(s)Description
Zinc finger28-66RING-type
Zinc finger187-215UBZ4-type
Compositional bias222-238Polar residues
Region222-254Disordered
Compositional bias239-254Basic and acidic residues
Domain278-312SAP
Region407-487Disordered
Compositional bias425-478Basic and acidic residues

Sequence similarities

Belongs to the RAD18 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    487
  • Mass (Da)
    55,230
  • Last updated
    1989-07-01 v1
  • Checksum
    70F5F12A3FA99532
MDHQITTASDFTTTSIPSLYQLDTLLRCHICKDFLKVPVLTPCGHTFCSLCIRTHLNNQPNCPLCLFEFRESLLRSEFLVSEIIQSYTSLRSSLLDALRIPKPTPVPENEEVPGPENSSWIELISESESDSVNAADDDLQIVATSERKLAKRSMTDILPLSSKPSKRNFAMFRSERIKKKSKPNEQMAQCPICQQFYPLKALEKTHLDECLTLQSLGKKPKISTTFPTESNPHNKSSSRFKVRTPEVDKSSCGETSHVDKYLNSMMSAEHQRLPKINFTSMTQSQIKQKLSSLGLSTNGTRQNMIKRYNHYEMLWNSNFCDSLEPVDEAELKRQLLSWDVSHNKTPQNSSNKGGISKLMIMKSNGKSSSYRKLLENFKNDKFNRKGWMVMFRKDFARLIREAKMKIKTGSSDSSGSVGHSNDGDGVEKVQSDQGTEDQQMEKDQDTVINEDRVAGERNLPNEDSTDADLSRELMDLNEYSKDPPGNN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias222-238Polar residues
Compositional bias239-254Basic and acidic residues
Compositional bias425-478Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X12542
EMBL· GenBank· DDBJ
CAA31059.1
EMBL· GenBank· DDBJ
Genomic DNA
M36405
EMBL· GenBank· DDBJ
AAA34932.1
EMBL· GenBank· DDBJ
Genomic DNA
X12588
EMBL· GenBank· DDBJ
CAA31101.1
EMBL· GenBank· DDBJ
Genomic DNA
X59720
EMBL· GenBank· DDBJ
CAA42281.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006937
EMBL· GenBank· DDBJ
DAA07538.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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