| Tag | Content |
|---|
| CPLM ID | CPLM-003849 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Postreplication repair E3 ubiquitin-protein ligase RAD18 |
Protein Synonyms/Alias | Radiation sensitivity protein 18 |
Gene Name | RAD18 |
Gene Synonyms/Alias | YCR066W; YCR66W |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 200 | CQQFYPLKALEKTHL | ubiquitination | [1] | | 204 | YPLKALEKTHLDECL | ubiquitination | [1, 2] |
|
Reference | [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J. Nat Methods. 2013 Jul;10(7):676-82. [ PMID: 23749301] [2] Sites of ubiquitin attachment in Saccharomyces cerevisiae. Starita LM, Lo RS, Eng JK, von Haller PD, Fields S. Proteomics. 2012 Jan;12(2):236-40. [ PMID: 22106047] |
Functional Description | 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. |
Sequence Annotation | DOMAIN 278 312 SAP.
ZN_FING 28 66 RING-type.
ZN_FING 190 210 UBZ-type.
MOD_RES 174 174 Phosphoserine. |
Keyword | Complete proteome; DNA damage; DNA repair; DNA-binding; Ligase; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 487 AA |
Protein Sequence | MDHQITTASD FTTTSIPSLY QLDTLLRCHI CKDFLKVPVL TPCGHTFCSL CIRTHLNNQP 60
NCPLCLFEFR ESLLRSEFLV SEIIQSYTSL RSSLLDALRI PKPTPVPENE EVPGPENSSW 120
IELISESESD SVNAADDDLQ IVATSERKLA KRSMTDILPL SSKPSKRNFA MFRSERIKKK 180
SKPNEQMAQC PICQQFYPLK ALEKTHLDEC LTLQSLGKKP KISTTFPTES NPHNKSSSRF 240
KVRTPEVDKS SCGETSHVDK YLNSMMSAEH QRLPKINFTS MTQSQIKQKL SSLGLSTNGT 300
RQNMIKRYNH YEMLWNSNFC DSLEPVDEAE LKRQLLSWDV SHNKTPQNSS NKGGISKLMI 360
MKSNGKSSSY RKLLENFKND KFNRKGWMVM FRKDFARLIR EAKMKIKTGS SDSSGSVGHS 420
NDGDGVEKVQ SDQGTEDQQM EKDQDTVINE DRVAGERNLP NEDSTDADLS RELMDLNEYS 480
KDPPGNN 487 |
Gene Ontology | GO:0000790; C:nuclear chromatin; IDA:SGD. GO:0003684; F:damaged DNA binding; IEA:InterPro. GO:0003697; F:single-stranded DNA binding; IDA:SGD. GO:0004842; F:ubiquitin-protein ligase activity; IPI:SGD. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0042275; P:error-free postreplication DNA repair; IGI:SGD. GO:0070987; P:error-free translesion synthesis; IGI:SGD. GO:0042276; P:error-prone translesion synthesis; IGI:SGD. GO:0006513; P:protein monoubiquitination; IMP:SGD. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |