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DNA repair protein RAD5 (EC 3.6.4.-) (Radiation sensitivity protein 5) (Revertibility protein 2)

 RAD5_YEAST              Reviewed;        1169 AA.
P32849; D6VY34;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
20-JUN-2018, entry version 172.
RecName: Full=DNA repair protein RAD5;
EC=3.6.4.-;
AltName: Full=Radiation sensitivity protein 5;
AltName: Full=Revertibility protein 2;
Name=RAD5; Synonyms=REV2, SNM2; OrderedLocusNames=YLR032W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=1324406; DOI=10.1128/MCB.12.9.3807;
Johnson R.E., Henderson S.T., Petes T.D., Prakash S., Bankmann M.,
Prakash L.;
"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.";
Mol. Cell. Biol. 12:3807-3818(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
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., 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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 402-1063.
PubMed=1394508; DOI=10.1007/BF00317921;
Ahne F., Baur M., Eckardt-Schupp F.;
"The REV2 gene of Saccharomyces cerevisiae: cloning and DNA
sequence.";
Curr. Genet. 22:277-282(1992).
[5]
CHARACTERIZATION.
PubMed=7961763;
Johnson R.E., Prakash S., Prakash L.;
"Yeast DNA repair protein RAD5 that promotes instability of simple
repetitive sequences is a DNA-dependent ATPase.";
J. Biol. Chem. 269:28259-28262(1994).
[6]
FUNCTION.
PubMed=9016623; DOI=10.1093/nar/25.4.743;
Ahne F., Ja B., Eckardt-Schupp F.;
"The RAD5 gene product is involved in the avoidance of non-homologous
end-joining of DNA double strand breaks in the yeast Saccharomyces
cerevisiae.";
Nucleic Acids Res. 25:743-749(1997).
[7]
FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-914, SUBUNIT, AND
INTERACTION WITH RAD18 AND UBC13.
PubMed=10880451; DOI=10.1093/emboj/19.13.3388;
Ulrich H.D., Jentsch S.;
"Two RING finger proteins mediate cooperation between ubiquitin-
conjugating enzymes in DNA repair.";
EMBO J. 19:3388-3397(2000).
[8]
FUNCTION.
PubMed=10924462;
Xiao W., Chow B.L., Broomfield S., Hanna M.;
"The Saccharomyces cerevisiae RAD6 group is composed of an error-prone
and two error-free postreplication repair pathways.";
Genetics 155:1633-1641(2000).
[9]
FUNCTION.
PubMed=11884624; DOI=10.1128/MCB.22.7.2419-2426.2002;
Torres-Ramos C.A., Prakash S., Prakash L.;
"Requirement of RAD5 and MMS2 for postreplication repair of UV-damaged
DNA in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 22:2419-2426(2002).
[10]
FUNCTION, AND INTERACTION WITH POL30 AND UBC9.
PubMed=12226657; DOI=10.1038/nature00991;
Hoege C., Pfander B., Moldovan G.-L., Pyrowolakis G., Jentsch S.;
"RAD6-dependent DNA repair is linked to modification of PCNA by
ubiquitin and SUMO.";
Nature 419:135-141(2002).
[11]
FUNCTION, SUBUNIT, INTERACTION WITH UBC13, AND MUTAGENESIS OF CYS-914;
ILE-916; TYR-944 AND ASN-959.
PubMed=12496280; DOI=10.1074/jbc.M212195200;
Ulrich H.D.;
"Protein-protein interactions within an E2-RING finger complex.
Implications for ubiquitin-dependent DNA damage repair.";
J. Biol. Chem. 278:7051-7058(2003).
[12]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[13]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[14]
FUNCTION, INTERACTION WITH POL30; RAD18 AND UBC13, AND MUTAGENESIS OF
538-LYS-THR-539.
PubMed=16224103; DOI=10.1093/nar/gki902;
Chen S., Davies A.A., Sagan D., Ulrich H.D.;
"The RING finger ATPase Rad5p of Saccharomyces cerevisiae contributes
to DNA double-strand break repair in a ubiquitin-independent manner.";
Nucleic Acids Res. 33:5878-5886(2005).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-129 AND
SER-130, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
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.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- 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. {ECO:0000269|PubMed:10880451,
ECO:0000269|PubMed:10924462, ECO:0000269|PubMed:11884624,
ECO:0000269|PubMed:12226657, ECO:0000269|PubMed:12496280,
ECO:0000269|PubMed:1324406, ECO:0000269|PubMed:16224103,
ECO:0000269|PubMed:9016623}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=525 uM for ATP;
pH dependence:
Optimum pH is 7.0. for ATPase activity.;
-!- SUBUNIT: Homodimer. Interacts with POL30, RAD18, UBC9 and UBC13.
{ECO:0000269|PubMed:10880451, ECO:0000269|PubMed:12226657,
ECO:0000269|PubMed:12496280, ECO:0000269|PubMed:16224103}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
-!- MISCELLANEOUS: Present with 1520 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M96644; AAA34951.1; -; Genomic_DNA.
EMBL; Z73204; CAA97556.1; -; Genomic_DNA.
EMBL; S46103; AAB23590.1; -; Genomic_DNA.
EMBL; BK006945; DAA09350.1; -; Genomic_DNA.
PIR; S64859; S64859.
RefSeq; NP_013132.1; NM_001181919.1.
ProteinModelPortal; P32849; -.
SMR; P32849; -.
BioGrid; 31306; 249.
DIP; DIP-5830N; -.
IntAct; P32849; 5.
MINT; P32849; -.
STRING; 4932.YLR032W; -.
iPTMnet; P32849; -.
MaxQB; P32849; -.
PaxDb; P32849; -.
PRIDE; P32849; -.
EnsemblFungi; YLR032W; YLR032W; YLR032W.
GeneID; 850719; -.
KEGG; sce:YLR032W; -.
EuPathDB; FungiDB:YLR032W; -.
SGD; S000004022; RAD5.
GeneTree; ENSGT00910000144263; -.
HOGENOM; HOG000040492; -.
InParanoid; P32849; -.
KO; K15505; -.
OMA; GQNRPKE; -.
OrthoDB; EOG092C0L0F; -.
BioCyc; YEAST:G3O-32191-MONOMER; -.
Reactome; R-SCE-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
PRO; PR:P32849; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0000781; C:chromosome, telomeric region; IDA:SGD.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0000790; C:nuclear chromatin; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008094; F:DNA-dependent ATPase activity; IDA:SGD.
GO; GO:0000400; F:four-way junction DNA binding; IDA:SGD.
GO; GO:0009378; F:four-way junction helicase activity; IDA:SGD.
GO; GO:0000403; F:Y-form DNA binding; IDA:SGD.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006302; P:double-strand break repair; IMP:SGD.
GO; GO:0042275; P:error-free postreplication DNA repair; IMP:SGD.
GO; GO:0070987; P:error-free translesion synthesis; IDA:SGD.
GO; GO:0042276; P:error-prone translesion synthesis; IDA:SGD.
GO; GO:0010994; P:free ubiquitin chain polymerization; IDA:SGD.
GO; GO:0006301; P:postreplication repair; IDA:SGD.
GO; GO:0000209; P:protein polyubiquitination; IDA:SGD.
CDD; cd00079; HELICc; 1.
Gene3D; 3.30.40.10; -; 1.
Gene3D; 3.40.50.10810; -; 1.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014905; HIRAN.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR038718; SNF2-like_sf.
InterPro; IPR000330; SNF2_N.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF08797; HIRAN; 1.
Pfam; PF00176; SNF2_N; 1.
Pfam; PF13639; zf-RING_2; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SMART; SM00910; HIRAN; 1.
SMART; SM00184; RING; 1.
SUPFAM; SSF52540; SSF52540; 4.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Complete proteome; Cytoplasm; DNA damage;
DNA repair; DNA-binding; Helicase; Hydrolase; Metal-binding;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 1169 DNA repair protein RAD5.
/FTId=PRO_0000056130.
DOMAIN 519 730 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 995 1165 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
NP_BIND 532 539 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
ZN_FING 914 961 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
MOTIF 681 684 DEGH box.
COMPBIAS 42 60 Asp/Glu-rich (acidic).
COMPBIAS 303 315 Arg/Lys-rich (basic).
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 129 129 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 130 130 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MUTAGEN 538 539 KT->AA: Increased sensitivity toward
ionizing radiation.
{ECO:0000269|PubMed:16224103}.
MUTAGEN 914 914 C->S: Abolishes interaction with UBC13.
{ECO:0000269|PubMed:10880451,
ECO:0000269|PubMed:12496280}.
MUTAGEN 916 916 I->A: Abolishes interaction with UBC13.
{ECO:0000269|PubMed:12496280}.
MUTAGEN 944 944 Y->A: Abolishes interaction with UBC13.
{ECO:0000269|PubMed:12496280}.
MUTAGEN 959 959 N->A: Abolishes interaction with UBC13.
{ECO:0000269|PubMed:12496280}.
CONFLICT 478 478 Q -> R (in Ref. 4; AAB23590).
{ECO:0000305}.
CONFLICT 635 635 T -> N (in Ref. 4; AAB23590).
{ECO:0000305}.
CONFLICT 846 846 G -> S (in Ref. 4; AAB23590).
{ECO:0000305}.
CONFLICT 898 898 R -> S (in Ref. 4; AAB23590).
{ECO:0000305}.
CONFLICT 973 973 V -> A (in Ref. 4; AAB23590).
{ECO:0000305}.
CONFLICT 1063 1063 A -> R (in Ref. 4; AAB23590).
{ECO:0000305}.
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


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