RAD5_YEAST
ID RAD5_YEAST Reviewed; 1169 AA.
AC P32849; D6VY34;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=DNA repair protein RAD5;
DE EC=3.6.4.-;
DE AltName: Full=Radiation sensitivity protein 5;
DE AltName: Full=Revertibility protein 2;
GN Name=RAD5; Synonyms=REV2, SNM2; OrderedLocusNames=YLR032W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=1324406; DOI=10.1128/mcb.12.9.3807-3818.1992;
RA Johnson R.E., Henderson S.T., Petes T.D., Prakash S., Bankmann M.,
RA Prakash L.;
RT "Saccharomyces cerevisiae RAD5-encoded DNA repair protein contains DNA
RT helicase and zinc-binding sequence motifs and affects the stability of
RT simple repetitive sequences in the genome.";
RL Mol. Cell. Biol. 12:3807-3818(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 402-1063.
RX PubMed=1394508; DOI=10.1007/bf00317921;
RA Ahne F., Baur M., Eckardt-Schupp F.;
RT "The REV2 gene of Saccharomyces cerevisiae: cloning and DNA sequence.";
RL Curr. Genet. 22:277-282(1992).
RN [5]
RP CHARACTERIZATION.
RX PubMed=7961763; DOI=10.1016/s0021-9258(18)46922-0;
RA Johnson R.E., Prakash S., Prakash L.;
RT "Yeast DNA repair protein RAD5 that promotes instability of simple
RT repetitive sequences is a DNA-dependent ATPase.";
RL J. Biol. Chem. 269:28259-28262(1994).
RN [6]
RP FUNCTION.
RX PubMed=9016623; DOI=10.1093/nar/25.4.743;
RA Ahne F., Ja B., Eckardt-Schupp F.;
RT "The RAD5 gene product is involved in the avoidance of non-homologous end-
RT joining of DNA double strand breaks in the yeast Saccharomyces
RT cerevisiae.";
RL Nucleic Acids Res. 25:743-749(1997).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-914, SUBUNIT, AND
RP INTERACTION WITH RAD18 AND UBC13.
RX PubMed=10880451; DOI=10.1093/emboj/19.13.3388;
RA Ulrich H.D., Jentsch S.;
RT "Two RING finger proteins mediate cooperation between ubiquitin-conjugating
RT enzymes in DNA repair.";
RL EMBO J. 19:3388-3397(2000).
RN [8]
RP FUNCTION.
RX PubMed=10924462; DOI=10.1093/genetics/155.4.1633;
RA Xiao W., Chow B.L., Broomfield S., Hanna M.;
RT "The Saccharomyces cerevisiae RAD6 group is composed of an error-prone and
RT two error-free postreplication repair pathways.";
RL Genetics 155:1633-1641(2000).
RN [9]
RP FUNCTION.
RX PubMed=11884624; DOI=10.1128/mcb.22.7.2419-2426.2002;
RA Torres-Ramos C.A., Prakash S., Prakash L.;
RT "Requirement of RAD5 and MMS2 for postreplication repair of UV-damaged DNA
RT in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 22:2419-2426(2002).
RN [10]
RP FUNCTION, AND INTERACTION WITH POL30 AND UBC9.
RX PubMed=12226657; DOI=10.1038/nature00991;
RA Hoege C., Pfander B., Moldovan G.-L., Pyrowolakis G., Jentsch S.;
RT "RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin
RT and SUMO.";
RL Nature 419:135-141(2002).
RN [11]
RP FUNCTION, SUBUNIT, INTERACTION WITH UBC13, AND MUTAGENESIS OF CYS-914;
RP ILE-916; TYR-944 AND ASN-959.
RX PubMed=12496280; DOI=10.1074/jbc.m212195200;
RA Ulrich H.D.;
RT "Protein-protein interactions within an E2-RING finger complex.
RT Implications for ubiquitin-dependent DNA damage repair.";
RL J. Biol. Chem. 278:7051-7058(2003).
RN [12]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [13]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [14]
RP FUNCTION, INTERACTION WITH POL30; RAD18 AND UBC13, AND MUTAGENESIS OF
RP 538-LYS-THR-539.
RX PubMed=16224103; DOI=10.1093/nar/gki902;
RA Chen S., Davies A.A., Sagan D., Ulrich H.D.;
RT "The RING finger ATPase Rad5p of Saccharomyces cerevisiae contributes to
RT DNA double-strand break repair in a ubiquitin-independent manner.";
RL Nucleic Acids Res. 33:5878-5886(2005).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-129 AND
RP SER-130, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Probable helicase, member of the UBC2/RAD6 epistasis group.
CC Functions with the DNA repair protein RAD18 in error-free
CC postreplication DNA repair. Involved in the maintenance of wild-type
CC rates of instability of simple repetitive sequences such as poly(GT)
CC repeats. Seems to be involved in maintaining a balance which acts in
CC favor of error-prone non-homologous joining during DNA double-strand
CC breaks repairs. Recruits the UBC13-MMS2 dimer to chromatin for DNA
CC repair. {ECO:0000269|PubMed:10880451, ECO:0000269|PubMed:10924462,
CC ECO:0000269|PubMed:11884624, ECO:0000269|PubMed:12226657,
CC ECO:0000269|PubMed:12496280, ECO:0000269|PubMed:1324406,
CC ECO:0000269|PubMed:16224103, ECO:0000269|PubMed:9016623}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=525 uM for ATP;
CC pH dependence:
CC Optimum pH is 7.0. for ATPase activity.;
CC -!- SUBUNIT: Homodimer. Interacts with POL30, RAD18, UBC9 and UBC13.
CC {ECO:0000269|PubMed:10880451, ECO:0000269|PubMed:12226657,
CC ECO:0000269|PubMed:12496280, ECO:0000269|PubMed:16224103}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- MISCELLANEOUS: Present with 1520 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; M96644; AAA34951.1; -; Genomic_DNA.
DR EMBL; Z73204; CAA97556.1; -; Genomic_DNA.
DR EMBL; S46103; AAB23590.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09350.1; -; Genomic_DNA.
DR PIR; S64859; S64859.
DR RefSeq; NP_013132.1; NM_001181919.1.
DR PDB; 5YRQ; X-ray; 2.00 A; A/B/D/E=5-20.
DR PDBsum; 5YRQ; -.
DR AlphaFoldDB; P32849; -.
DR SASBDB; P32849; -.
DR SMR; P32849; -.
DR BioGRID; 31306; 356.
DR DIP; DIP-5830N; -.
DR IntAct; P32849; 5.
DR MINT; P32849; -.
DR STRING; 4932.YLR032W; -.
DR iPTMnet; P32849; -.
DR MaxQB; P32849; -.
DR PaxDb; P32849; -.
DR PRIDE; P32849; -.
DR EnsemblFungi; YLR032W_mRNA; YLR032W; YLR032W.
DR GeneID; 850719; -.
DR KEGG; sce:YLR032W; -.
DR SGD; S000004022; RAD5.
DR VEuPathDB; FungiDB:YLR032W; -.
DR eggNOG; KOG1001; Eukaryota.
DR GeneTree; ENSGT00940000165376; -.
DR HOGENOM; CLU_000315_2_5_1; -.
DR InParanoid; P32849; -.
DR OMA; WSNFSFW; -.
DR BioCyc; YEAST:G3O-32191-MON; -.
DR PRO; PR:P32849; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P32849; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:SGD.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0000400; F:four-way junction DNA binding; IDA:SGD.
DR GO; GO:0009378; F:four-way junction helicase activity; IDA:SGD.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0000403; F:Y-form DNA binding; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:0042275; P:error-free postreplication DNA repair; IMP:SGD.
DR GO; GO:0070987; P:error-free translesion synthesis; IDA:SGD.
DR GO; GO:0042276; P:error-prone translesion synthesis; IDA:SGD.
DR GO; GO:0010994; P:free ubiquitin chain polymerization; IDA:SGD.
DR GO; GO:0006301; P:postreplication repair; IDA:SGD.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:SGD.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014905; HIRAN.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08797; HIRAN; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00910; HIRAN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm; DNA damage; DNA repair;
KW DNA-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1169
FT /note="DNA repair protein RAD5"
FT /id="PRO_0000056130"
FT DOMAIN 519..730
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 995..1165
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 914..961
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 302..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 681..684
FT /note="DEGH box"
FT BINDING 532..539
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 538..539
FT /note="KT->AA: Increased sensitivity toward ionizing
FT radiation."
FT /evidence="ECO:0000269|PubMed:16224103"
FT MUTAGEN 914
FT /note="C->S: Abolishes interaction with UBC13."
FT /evidence="ECO:0000269|PubMed:10880451,
FT ECO:0000269|PubMed:12496280"
FT MUTAGEN 916
FT /note="I->A: Abolishes interaction with UBC13."
FT /evidence="ECO:0000269|PubMed:12496280"
FT MUTAGEN 944
FT /note="Y->A: Abolishes interaction with UBC13."
FT /evidence="ECO:0000269|PubMed:12496280"
FT MUTAGEN 959
FT /note="N->A: Abolishes interaction with UBC13."
FT /evidence="ECO:0000269|PubMed:12496280"
FT CONFLICT 478
FT /note="Q -> R (in Ref. 4; AAB23590)"
FT /evidence="ECO:0000305"
FT CONFLICT 635
FT /note="T -> N (in Ref. 4; AAB23590)"
FT /evidence="ECO:0000305"
FT CONFLICT 846
FT /note="G -> S (in Ref. 4; AAB23590)"
FT /evidence="ECO:0000305"
FT CONFLICT 898
FT /note="R -> S (in Ref. 4; AAB23590)"
FT /evidence="ECO:0000305"
FT CONFLICT 973
FT /note="V -> A (in Ref. 4; AAB23590)"
FT /evidence="ECO:0000305"
FT CONFLICT 1063
FT /note="A -> R (in Ref. 4; AAB23590)"
FT /evidence="ECO:0000305"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:5YRQ"
SQ SEQUENCE 1169 AA; 134002 MW; 226B720097433EE2 CRC64;
MSHIEQEERK RFFNDDLDTS ETSLNFKSEN KESFLFANSH NDDDDDVVVS VSDTTEGEGD
RSIVPVRREI EEEGQNQFIT ELLRIIPEMP KDLVMELNEK FGSQEEGLSL ALSHYFDHNS
GTSISKIPSS PNQLNTLSDT SNSTLSPSSF HPKRRRIYGF RNQTRLEDKV TWKRFIGALQ
VTGMATRPTV RPLKYGSQMK LKRSSEEISA TKVYDSRGRK KASMASLVRI FDIQYDREIG
RVSEDIAQIL YPLLSSHEIS FEVTLIFCDN KRLSIGDSFI LQLDCFLTSL IFEERNDGES
LMKRRRTEGG NKREKDNGNF GRTLTETDEE LESRSKRLAL LKLFDKLRLK PILDEQKALE
KHKIELNSDP EIIDLDNDEI CSNQVTEVHN NLRDTQHEEE TMNLNQLKTF YKAAQSSESL
KSLPETEPSR DVFKLELRNY QKQGLTWMLR REQEFAKAAS DGEASETGAN MINPLWKQFK
WPNDMSWAAQ NLQQDHVNVE DGIFFYANLH SGEFSLAKPI LKTMIKGGIL SDEMGLGKTV
AAYSLVLSCP HDSDVVDKKL FDIENTAVSD NLPSTWQDNK KPYASKTTLI VVPMSLLTQW
SNEFTKANNS PDMYHEVYYG GNVSSLKTLL TKTKTPPTVV LTTYGIVQNE WTKHSKGRMT
DEDVNISSGL FSVNFYRIII DEGHNIRNRT TVTSKAVMAL QGKCKWVLTG TPIINRLDDL
YSLVKFLELD PWRQINYWKT FVSTPFESKN YKQAFDVVNA ILEPVLLRRT KQMKDKDGKP
LVELPPKEVV IKRLPFSKSQ DLLYKFLLDK AEVSVKSGIA RGDLLKKYST ILVHILRLRQ
VCCHPGLIGS QDENDEDLSK NNKLVTEQTV ELDSLMRVVS ERFDNSFSKE ELDAMIQRLK
VKYPDNKSFQ SLECSICTTE PMDLDKALFT ECGHSFCEKC LFEYIEFQNS KNLGLKCPNC
RNQIDACRLL ALVQTNSNSK NLEFKPYSPA SKSSKITALL KELQLLQDSS AGEQVVIFSQ
FSTYLDILEK ELTHTFSKDV AKIYKFDGRL SLKERTSVLA DFAVKDYSRQ KILLLSLKAG
GVGLNLTCAS HAYMMDPWWS PSMEDQAIDR LHRIGQTNSV KVMRFIIQDS IEEKMLRIQE
KKRTIGEAMD TDEDERRKRR IEEIQMLFE
