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Protein

Postreplication repair E3 ubiquitin-protein ligase RAD18

Gene

RAD18

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.8 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri28 – 6639RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri190 – 21021UBZ-typeAdd
BLAST

GO - Molecular functioni

  • damaged DNA binding Source: InterPro
  • ligase activity Source: UniProtKB-KW
  • single-stranded DNA binding Source: SGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • error-free postreplication DNA repair Source: SGD
  • error-free translesion synthesis Source: SGD
  • error-prone translesion synthesis Source: SGD
  • protein monoubiquitination Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-29369-MONOMER.
ReactomeiR-SCE-110314. Recognition of DNA damage by PCNA-containing replication complex.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Postreplication repair E3 ubiquitin-protein ligase RAD18 (EC:6.3.2.-)
Alternative name(s):
Radiation sensitivity protein 18
Gene namesi
Name:RAD18
Ordered Locus Names:YCR066W
ORF Names:YCR66W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:YCR066W.
SGDiS000000662. RAD18.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • nuclear chromatin Source: SGD
  • nucleus Source: SGD
  • Rad6-Rad18 complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 487487Postreplication repair E3 ubiquitin-protein ligase RAD18PRO_0000056161Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei155 – 1551PhosphothreonineCombined sources
Modified residuei174 – 1741PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP10862.

PTM databases

iPTMnetiP10862.

Interactioni

Subunit structurei

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.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RAD6P061044EBI-14659,EBI-19722

Protein-protein interaction databases

BioGridi31042. 194 interactions.
DIPiDIP-1172N.
IntActiP10862. 10 interactions.
MINTiMINT-394603.

Structurei

3D structure databases

ProteinModelPortaliP10862.
SMRiP10862. Positions 22-95.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini278 – 31235SAPPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the RAD18 family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
Contains 1 SAP domain.PROSITE-ProRule annotation
Contains 1 UBZ-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri28 – 6639RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri190 – 21021UBZ-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00390000011230.
HOGENOMiHOG000248313.
InParanoidiP10862.
KOiK10627.
OMAiMFRSERI.
OrthoDBiEOG7H1K05.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR004580. Rad18.
IPR003034. SAP_dom.
IPR006642. Znf_Rad18_put.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF02037. SAP. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00513. SAP. 1 hit.
SM00734. ZnF_Rad18. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00599. rad18. 1 hit.
PROSITEiPS50800. SAP. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10862-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDHQITTASD FTTTSIPSLY QLDTLLRCHI CKDFLKVPVL TPCGHTFCSL
60 70 80 90 100
CIRTHLNNQP NCPLCLFEFR ESLLRSEFLV SEIIQSYTSL RSSLLDALRI
110 120 130 140 150
PKPTPVPENE EVPGPENSSW IELISESESD SVNAADDDLQ IVATSERKLA
160 170 180 190 200
KRSMTDILPL SSKPSKRNFA MFRSERIKKK SKPNEQMAQC PICQQFYPLK
210 220 230 240 250
ALEKTHLDEC LTLQSLGKKP KISTTFPTES NPHNKSSSRF KVRTPEVDKS
260 270 280 290 300
SCGETSHVDK YLNSMMSAEH QRLPKINFTS MTQSQIKQKL SSLGLSTNGT
310 320 330 340 350
RQNMIKRYNH YEMLWNSNFC DSLEPVDEAE LKRQLLSWDV SHNKTPQNSS
360 370 380 390 400
NKGGISKLMI MKSNGKSSSY RKLLENFKND KFNRKGWMVM FRKDFARLIR
410 420 430 440 450
EAKMKIKTGS SDSSGSVGHS NDGDGVEKVQ SDQGTEDQQM EKDQDTVINE
460 470 480
DRVAGERNLP NEDSTDADLS RELMDLNEYS KDPPGNN
Length:487
Mass (Da):55,230
Last modified:July 1, 1989 - v1
Checksum:i70F5F12A3FA99532
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12542 Genomic DNA. Translation: CAA31059.1.
M36405 Genomic DNA. Translation: AAA34932.1.
X12588 Genomic DNA. Translation: CAA31101.1.
X59720 Genomic DNA. Translation: CAA42281.1.
BK006937 Genomic DNA. Translation: DAA07538.1.
PIRiS05802. DDBY18.
RefSeqiNP_009992.1. NM_001178777.1.

Genome annotation databases

EnsemblFungiiCAA42281; CAA42281; CAA42281.
YCR066W; YCR066W; YCR066W.
GeneIDi850430.
KEGGisce:YCR066W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12542 Genomic DNA. Translation: CAA31059.1.
M36405 Genomic DNA. Translation: AAA34932.1.
X12588 Genomic DNA. Translation: CAA31101.1.
X59720 Genomic DNA. Translation: CAA42281.1.
BK006937 Genomic DNA. Translation: DAA07538.1.
PIRiS05802. DDBY18.
RefSeqiNP_009992.1. NM_001178777.1.

3D structure databases

ProteinModelPortaliP10862.
SMRiP10862. Positions 22-95.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31042. 194 interactions.
DIPiDIP-1172N.
IntActiP10862. 10 interactions.
MINTiMINT-394603.

PTM databases

iPTMnetiP10862.

Proteomic databases

MaxQBiP10862.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAA42281; CAA42281; CAA42281.
YCR066W; YCR066W; YCR066W.
GeneIDi850430.
KEGGisce:YCR066W.

Organism-specific databases

EuPathDBiFungiDB:YCR066W.
SGDiS000000662. RAD18.

Phylogenomic databases

GeneTreeiENSGT00390000011230.
HOGENOMiHOG000248313.
InParanoidiP10862.
KOiK10627.
OMAiMFRSERI.
OrthoDBiEOG7H1K05.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciYEAST:G3O-29369-MONOMER.
ReactomeiR-SCE-110314. Recognition of DNA damage by PCNA-containing replication complex.

Miscellaneous databases

PROiP10862.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR004580. Rad18.
IPR003034. SAP_dom.
IPR006642. Znf_Rad18_put.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF02037. SAP. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00513. SAP. 1 hit.
SM00734. ZnF_Rad18. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00599. rad18. 1 hit.
PROSITEiPS50800. SAP. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Potential DNA-binding domains in the RAD18 gene product of Saccharomyces cerevisiae."
    Chanet R., Magana-Schwencke N., Fabre F.
    Gene 74:543-547(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The Saccharomyces cerevisiae RAD18 gene encodes a protein that contains potential zinc finger domains for nucleic acid binding and a putative nucleotide binding sequence."
    Jones J.S., Weber S., Prakash L.
    Nucleic Acids Res. 16:7119-7131(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Sequence of the sup61-RAD18 region on chromosome III of Saccharomyces cerevisiae."
    Benit P., Chanet R., Fabre F., Faye G., Fukuhara H., Sor F.
    Yeast 8:147-153(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "Specific complex formation between yeast RAD6 and RAD18 proteins: a potential mechanism for targeting RAD6 ubiquitin-conjugating activity to DNA damage sites."
    Bailly V., Lamb J., Sung P., Prakash S., Prakash L.
    Genes Dev. 8:811-820(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SINGLE STRAND DNA-BINDING, INTERACTION WITH UBC2.
  7. "Yeast DNA repair proteins Rad6 and Rad18 form a heterodimer that has ubiquitin conjugating, DNA binding, and ATP hydrolytic activities."
    Bailly V., Lauder S., Prakash S., Prakash L.
    J. Biol. Chem. 272:23360-23365(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH UBC2.
  8. "Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair."
    Ulrich H.D., Jentsch S.
    EMBO J. 19:3388-3397(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH RAD5 AND UBC13.
  9. "The Saccharomyces cerevisiae RAD6 group is composed of an error-prone and two error-free postreplication repair pathways."
    Xiao W., Chow B.L., Broomfield S., Hanna M.
    Genetics 155:1633-1641(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE UBC13-MMS2 COMPLEX.
  10. "RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO."
    Hoege C., Pfander B., Moldovan G.-L., Pyrowolakis G., Jentsch S.
    Nature 419:135-141(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH POL30 AND UBC9.
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. "Rad18/Rad5/Mms2-mediated polyubiquitination of PCNA is implicated in replication completion during replication stress."
    Branzei D., Seki M., Enomoto T.
    Genes Cells 9:1031-1042(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "The post-replication repair RAD18 and RAD6 genes are involved in the prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine in Saccharomyces cerevisiae."
    de Padula M., Slezak G., Auffret van Der Kemp P., Boiteux S.
    Nucleic Acids Res. 32:5003-5010(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "The error-free component of the RAD6/RAD18 DNA damage tolerance pathway of budding yeast employs sister-strand recombination."
    Zhang H., Lawrence C.W.
    Proc. Natl. Acad. Sci. U.S.A. 102:15954-15959(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-155 AND SER-174, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRAD18_YEAST
AccessioniPrimary (citable) accession number: P10862
Secondary accession number(s): D6VR69, Q58AT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 8, 2016
This is version 167 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 206 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome III
    Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

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.