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P32849 (RAD5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA repair protein RAD5

EC=3.6.4.-
Alternative name(s):
Radiation sensitivity protein 5
Revertibility protein 2
Gene names
Name:RAD5
Synonyms:REV2, SNM2
Ordered Locus Names:YLR032W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1169 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable helicase, member of the UBC2/RAD6 epistasis group. Functions with the DNA repair protein RAD18 in error-free postreplication DNA repair. Involved in the maintenance of wild-type rates of instability of simple repetitive sequences such as poly(GT) repeats. Seems to be involved in maintaining a balance which acts in favor of error-prone non-homologous joining during DNA double-strand breaks repairs. Recruits the UBC13-MMS2 dimer to chromatin for DNA repair. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14

Cofactor

Magnesium, manganese or calcium.

Subunit structure

Homodimer. Interacts with POL30, RAD18, UBC9 and UBC13. Ref.7 Ref.10 Ref.11 Ref.14

Subcellular location

Cytoplasm. Nucleus Ref.7 Ref.12.

Miscellaneous

Present with 1520 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the SNF2/RAD54 helicase family.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 RING-type zinc finger.

Biophysicochemical properties

Kinetic parameters:

KM=525 µM for ATP

pH dependence:

Optimum pH is 7.0. for ATPase activity.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentCytoplasm
Nucleus
   DomainZinc-finger
   LigandATP-binding
DNA-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionHelicase
Hydrolase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay PubMed 17936713. Source: GOC

DNA duplex unwinding

Inferred from direct assay PubMed 17936713. Source: GOC

double-strand break repair

Inferred from mutant phenotype Ref.14. Source: SGD

error-prone translesion synthesis

Inferred from mutant phenotype PubMed 23142547. Source: SGD

free ubiquitin chain polymerization

Inferred from direct assay PubMed 19706603. Source: SGD

postreplication repair

Inferred from direct assay PubMed 17936713. Source: SGD

protein polyubiquitination

Inferred from direct assay PubMed 19706603. Source: SGD

   Cellular_componentchromosome, telomeric region

Inferred from direct assay PubMed 24393774. Source: SGD

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear chromatin

Inferred from direct assay Ref.7. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-dependent ATPase activity

Inferred from direct assay PubMed 17936713. Source: SGD

Y-form DNA binding

Inferred from direct assay PubMed 17936713. Source: SGD

four-way junction DNA binding

Inferred from direct assay PubMed 17936713. Source: SGD

four-way junction helicase activity

Inferred from direct assay PubMed 17936713. Source: SGD

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.17
Chain2 – 11691168DNA repair protein RAD5
PRO_0000056130

Regions

Domain519 – 730212Helicase ATP-binding
Domain995 – 1165171Helicase C-terminal
Nucleotide binding532 – 5398ATP Potential
Zinc finger914 – 96148RING-type
Motif681 – 6844DEGH box
Compositional bias42 – 6019Asp/Glu-rich (acidic)
Compositional bias303 – 31513Arg/Lys-rich (basic)

Amino acid modifications

Modified residue21N-acetylserine Ref.17
Modified residue201Phosphoserine Ref.16
Modified residue231Phosphoserine Ref.16
Modified residue1291Phosphoserine Ref.16
Modified residue1301Phosphoserine Ref.16

Experimental info

Mutagenesis538 – 5392KT → AA: Increased sensitivity toward ionizing radiation. Ref.14
Mutagenesis9141C → S: Abolishes interaction with UBC13. Ref.7 Ref.11 Ref.14
Mutagenesis9161I → A: Abolishes interaction with UBC13. Ref.11 Ref.14
Mutagenesis9441Y → A: Abolishes interaction with UBC13. Ref.11 Ref.14
Mutagenesis9591N → A: Abolishes interaction with UBC13. Ref.11 Ref.14
Sequence conflict4781Q → R in AAB23590. Ref.4
Sequence conflict6351T → N in AAB23590. Ref.4
Sequence conflict8461G → S in AAB23590. Ref.4
Sequence conflict8981R → S in AAB23590. Ref.4
Sequence conflict9731V → A in AAB23590. Ref.4
Sequence conflict10631A → R in AAB23590. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P32849 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 226B720097433EE2

FASTA1,169134,002
        10         20         30         40         50         60 
MSHIEQEERK RFFNDDLDTS ETSLNFKSEN KESFLFANSH NDDDDDVVVS VSDTTEGEGD 

        70         80         90        100        110        120 
RSIVPVRREI EEEGQNQFIT ELLRIIPEMP KDLVMELNEK FGSQEEGLSL ALSHYFDHNS 

       130        140        150        160        170        180 
GTSISKIPSS PNQLNTLSDT SNSTLSPSSF HPKRRRIYGF RNQTRLEDKV TWKRFIGALQ 

       190        200        210        220        230        240 
VTGMATRPTV RPLKYGSQMK LKRSSEEISA TKVYDSRGRK KASMASLVRI FDIQYDREIG 

       250        260        270        280        290        300 
RVSEDIAQIL YPLLSSHEIS FEVTLIFCDN KRLSIGDSFI LQLDCFLTSL IFEERNDGES 

       310        320        330        340        350        360 
LMKRRRTEGG NKREKDNGNF GRTLTETDEE LESRSKRLAL LKLFDKLRLK PILDEQKALE 

       370        380        390        400        410        420 
KHKIELNSDP EIIDLDNDEI CSNQVTEVHN NLRDTQHEEE TMNLNQLKTF YKAAQSSESL 

       430        440        450        460        470        480 
KSLPETEPSR DVFKLELRNY QKQGLTWMLR REQEFAKAAS DGEASETGAN MINPLWKQFK 

       490        500        510        520        530        540 
WPNDMSWAAQ NLQQDHVNVE DGIFFYANLH SGEFSLAKPI LKTMIKGGIL SDEMGLGKTV 

       550        560        570        580        590        600 
AAYSLVLSCP HDSDVVDKKL FDIENTAVSD NLPSTWQDNK KPYASKTTLI VVPMSLLTQW 

       610        620        630        640        650        660 
SNEFTKANNS PDMYHEVYYG GNVSSLKTLL TKTKTPPTVV LTTYGIVQNE WTKHSKGRMT 

       670        680        690        700        710        720 
DEDVNISSGL FSVNFYRIII DEGHNIRNRT TVTSKAVMAL QGKCKWVLTG TPIINRLDDL 

       730        740        750        760        770        780 
YSLVKFLELD PWRQINYWKT FVSTPFESKN YKQAFDVVNA ILEPVLLRRT KQMKDKDGKP 

       790        800        810        820        830        840 
LVELPPKEVV IKRLPFSKSQ DLLYKFLLDK AEVSVKSGIA RGDLLKKYST ILVHILRLRQ 

       850        860        870        880        890        900 
VCCHPGLIGS QDENDEDLSK NNKLVTEQTV ELDSLMRVVS ERFDNSFSKE ELDAMIQRLK 

       910        920        930        940        950        960 
VKYPDNKSFQ SLECSICTTE PMDLDKALFT ECGHSFCEKC LFEYIEFQNS KNLGLKCPNC 

       970        980        990       1000       1010       1020 
RNQIDACRLL ALVQTNSNSK NLEFKPYSPA SKSSKITALL KELQLLQDSS AGEQVVIFSQ 

      1030       1040       1050       1060       1070       1080 
FSTYLDILEK ELTHTFSKDV AKIYKFDGRL SLKERTSVLA DFAVKDYSRQ KILLLSLKAG 

      1090       1100       1110       1120       1130       1140 
GVGLNLTCAS HAYMMDPWWS PSMEDQAIDR LHRIGQTNSV KVMRFIIQDS IEEKMLRIQE 

      1150       1160 
KKRTIGEAMD TDEDERRKRR IEEIQMLFE 

« Hide

References

« Hide 'large scale' references
[1]"Saccharomyces cerevisiae RAD5-encoded DNA repair protein contains DNA helicase and zinc-binding sequence motifs and affects the stability of simple repetitive sequences in the genome."
Johnson R.E., Henderson S.T., Petes T.D., Prakash S., Bankmann M., Prakash L.
Mol. Cell. Biol. 12:3807-3818(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"The REV2 gene of Saccharomyces cerevisiae: cloning and DNA sequence."
Ahne F., Baur M., Eckardt-Schupp F.
Curr. Genet. 22:277-282(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 402-1063.
[5]"Yeast DNA repair protein RAD5 that promotes instability of simple repetitive sequences is a DNA-dependent ATPase."
Johnson R.E., Prakash S., Prakash L.
J. Biol. Chem. 269:28259-28262(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"The RAD5 gene product is involved in the avoidance of non-homologous end-joining of DNA double strand breaks in the yeast Saccharomyces cerevisiae."
Ahne F., Ja B., Eckardt-Schupp F.
Nucleic Acids Res. 25:743-749(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"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, MUTAGENESIS OF CYS-914, SUBUNIT, INTERACTION WITH RAD18 AND UBC13.
[8]"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.
[9]"Requirement of RAD5 and MMS2 for postreplication repair of UV-damaged DNA in Saccharomyces cerevisiae."
Torres-Ramos C.A., Prakash S., Prakash L.
Mol. Cell. Biol. 22:2419-2426(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[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]"Protein-protein interactions within an E2-RING finger complex. Implications for ubiquitin-dependent DNA damage repair."
Ulrich H.D.
J. Biol. Chem. 278:7051-7058(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH UBC13, MUTAGENESIS OF CYS-914; ILE-916; TYR-944 AND ASN-959.
[12]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[13]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[14]"The RING finger ATPase Rad5p of Saccharomyces cerevisiae contributes to DNA double-strand break repair in a ubiquitin-independent manner."
Chen S., Davies A.A., Sagan D., Ulrich H.D.
Nucleic Acids Res. 33:5878-5886(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH POL30; RAD18 AND UBC13, MUTAGENESIS OF 538-LYS-THR-539.
[15]"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].
[16]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-129 AND SER-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96644 Genomic DNA. Translation: AAA34951.1.
Z73204 Genomic DNA. Translation: CAA97556.1.
S46103 Genomic DNA. Translation: AAB23590.1.
BK006945 Genomic DNA. Translation: DAA09350.1.
PIRS64859.
RefSeqNP_013132.1. NM_001181919.1.

3D structure databases

ProteinModelPortalP32849.
SMRP32849. Positions 527-900, 910-960, 993-1168.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31306. 154 interactions.
DIPDIP-5830N.
IntActP32849. 3 interactions.
MINTMINT-2784640.
STRING4932.YLR032W.

Proteomic databases

PaxDbP32849.
PeptideAtlasP32849.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR032W; YLR032W; YLR032W.
GeneID850719.
KEGGsce:YLR032W.

Organism-specific databases

CYGDYLR032w.
SGDS000004022. RAD5.

Phylogenomic databases

eggNOGCOG0553.
GeneTreeENSGT00740000115627.
HOGENOMHOG000040492.
KOK15505.
OMAKHGLSWM.
OrthoDBEOG7PCJR9.

Enzyme and pathway databases

BioCycYEAST:G3O-32191-MONOMER.

Gene expression databases

GenevestigatorP32849.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
3.40.50.300. 4 hits.
InterProIPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014905. HIP116_Rad5p_N.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF00271. Helicase_C. 1 hit.
PF08797. HIRAN. 1 hit.
PF00176. SNF2_N. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SM00910. HIRAN. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 4 hits.
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio966793.

Entry information

Entry nameRAD5_YEAST
AccessionPrimary (citable) accession number: P32849
Secondary accession number(s): D6VY34
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families