P10862 · RAD18_YEAST
- ProteinPostreplication repair E3 ubiquitin-protein ligase RAD18
- GeneRAD18
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids487 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
Pathway
Protein modification; protein ubiquitination.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromatin | |
Cellular Component | nucleus | |
Cellular Component | Rad6-Rad18 complex | |
Molecular Function | metal ion binding | |
Molecular Function | single-stranded DNA binding | |
Molecular Function | ubiquitin protein ligase activity | |
Biological Process | DNA duplex unwinding | |
Biological Process | error-free postreplication DNA repair | |
Biological Process | error-free translesion synthesis | |
Biological Process | error-prone translesion synthesis | |
Biological Process | postreplication repair | |
Biological Process | protein monoubiquitination |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePostreplication repair E3 ubiquitin-protein ligase RAD18
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP10862
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000056161 | 1-487 | Postreplication repair E3 ubiquitin-protein ligase RAD18 | |||
Sequence: MDHQITTASDFTTTSIPSLYQLDTLLRCHICKDFLKVPVLTPCGHTFCSLCIRTHLNNQPNCPLCLFEFRESLLRSEFLVSEIIQSYTSLRSSLLDALRIPKPTPVPENEEVPGPENSSWIELISESESDSVNAADDDLQIVATSERKLAKRSMTDILPLSSKPSKRNFAMFRSERIKKKSKPNEQMAQCPICQQFYPLKALEKTHLDECLTLQSLGKKPKISTTFPTESNPHNKSSSRFKVRTPEVDKSSCGETSHVDKYLNSMMSAEHQRLPKINFTSMTQSQIKQKLSSLGLSTNGTRQNMIKRYNHYEMLWNSNFCDSLEPVDEAELKRQLLSWDVSHNKTPQNSSNKGGISKLMIMKSNGKSSSYRKLLENFKNDKFNRKGWMVMFRKDFARLIREAKMKIKTGSSDSSGSVGHSNDGDGVEKVQSDQGTEDQQMEKDQDTVINEDRVAGERNLPNEDSTDADLSRELMDLNEYSKDPPGNN | ||||||
Modified residue | 155 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 174 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 204 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Keywords
- PTM
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P10862 | RAD6 P06104 | 5 | EBI-14659, EBI-19722 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for zinc finger, compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 28-66 | RING-type | ||||
Sequence: CHICKDFLKVPVLTPCGHTFCSLCIRTHLNNQPNCPLCL | ||||||
Zinc finger | 187-215 | UBZ4-type | ||||
Sequence: MAQCPICQQFYPLKALEKTHLDECLTLQS | ||||||
Compositional bias | 222-238 | Polar residues | ||||
Sequence: ISTTFPTESNPHNKSSS | ||||||
Region | 222-254 | Disordered | ||||
Sequence: ISTTFPTESNPHNKSSSRFKVRTPEVDKSSCGE | ||||||
Compositional bias | 239-254 | Basic and acidic residues | ||||
Sequence: RFKVRTPEVDKSSCGE | ||||||
Domain | 278-312 | SAP | ||||
Sequence: FTSMTQSQIKQKLSSLGLSTNGTRQNMIKRYNHYE | ||||||
Region | 407-487 | Disordered | ||||
Sequence: KTGSSDSSGSVGHSNDGDGVEKVQSDQGTEDQQMEKDQDTVINEDRVAGERNLPNEDSTDADLSRELMDLNEYSKDPPGNN | ||||||
Compositional bias | 425-478 | Basic and acidic residues | ||||
Sequence: GVEKVQSDQGTEDQQMEKDQDTVINEDRVAGERNLPNEDSTDADLSRELMDLNE |
Sequence similarities
Belongs to the RAD18 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length487
- Mass (Da)55,230
- Last updated1989-07-01 v1
- Checksum70F5F12A3FA99532
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 222-238 | Polar residues | ||||
Sequence: ISTTFPTESNPHNKSSS | ||||||
Compositional bias | 239-254 | Basic and acidic residues | ||||
Sequence: RFKVRTPEVDKSSCGE | ||||||
Compositional bias | 425-478 | Basic and acidic residues | ||||
Sequence: GVEKVQSDQGTEDQQMEKDQDTVINEDRVAGERNLPNEDSTDADLSRELMDLNE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |