RAD1_YEAST
ID RAD1_YEAST Reviewed; 1100 AA.
AC P06777; D6W3Z0;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=DNA repair protein RAD1;
GN Name=RAD1; OrderedLocusNames=YPL022W;
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].
RX PubMed=3550428; DOI=10.1128/mcb.7.3.1012-1020.1987;
RA Reynolds P., Prakash L., Prakash S.;
RT "Nucleotide sequence and functional analysis of the RAD1 gene of
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 7:1012-1020(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 1-1035.
RX PubMed=6095044; DOI=10.1128/mcb.4.10.2161-2169.1984;
RA Yang E., Friedberg E.C.;
RT "Molecular cloning and nucleotide sequence analysis of the Saccharomyces
RT cerevisiae RAD1 gene.";
RL Mol. Cell. Biol. 4:2161-2169(1984).
RN [5]
RP FUNCTION, AND INTERACTION WITH RAD10.
RX PubMed=8479526; DOI=10.1038/362860a0;
RA Tomkinson A.E., Bardwell A.J., Bardwell L., Tappe N.J., Friedberg E.C.;
RT "Yeast DNA repair and recombination proteins Rad1 and Rad10 constitute a
RT single-stranded-DNA endonuclease.";
RL Nature 362:860-862(1993).
RN [6]
RP IDENTIFICATION IN THE NEF1 COMPLEX.
RX PubMed=8621533; DOI=10.1074/jbc.271.15.8903;
RA Guzder S.N., Sung P., Prakash L., Prakash S.;
RT "Nucleotide excision repair in yeast is mediated by sequential assembly of
RT repair factors and not by a pre-assembled repairosome.";
RL J. Biol. Chem. 271:8903-8910(1996).
RN [7]
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 [8]
RP INTERACTION WITH SAW1.
RX PubMed=17989249; DOI=10.1101/gr.6667007;
RA Suter B., Fetchko M.J., Imhof R., Graham C.I., Stoffel-Studer I.,
RA Zbinden C., Raghavan M., Lopez L., Beneti L., Hort J., Fillingham J.,
RA Greenblatt J.F., Giaever G., Nislow C., Stagljar I.;
RT "Examining protein protein interactions using endogenously tagged yeast
RT arrays: the cross-and-capture system.";
RL Genome Res. 17:1774-1782(2007).
RN [9]
RP INTERACTION WITH SAW1.
RX PubMed=18471978; DOI=10.1016/j.molcel.2008.02.028;
RA Li F., Dong J., Pan X., Oum J.-H., Boeke J.D., Lee S.E.;
RT "Microarray-based genetic screen defines SAW1, a gene required for
RT Rad1/Rad10-dependent processing of recombination intermediates.";
RL Mol. Cell 30:325-335(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613; SER-1071 AND THR-1072,
RP 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).
CC -!- FUNCTION: Involved in nucleotide excision repair of DNA damaged with UV
CC light, bulky adducts, or cross-linking agents. Along with RAD10 forms
CC an endonuclease that specifically degrades single-stranded DNA.
CC {ECO:0000269|PubMed:8479526}.
CC -!- SUBUNIT: Component of the nucleotide excision repair factor 1 (NEF1)
CC complex consisting of RAD1, RAD10 and RAD14. Interacts with SAW1.
CC {ECO:0000269|PubMed:17989249, ECO:0000269|PubMed:18471978,
CC ECO:0000269|PubMed:8479526, ECO:0000269|PubMed:8621533}.
CC -!- INTERACTION:
CC P06777; P06838: RAD10; NbExp=11; IntAct=EBI-14752, EBI-14637;
CC P06777; P28519: RAD14; NbExp=4; IntAct=EBI-14752, EBI-14641;
CC P06777; P39735: SAW1; NbExp=4; IntAct=EBI-14752, EBI-20627;
CC P06777; Q12098: SLX4; NbExp=3; IntAct=EBI-14752, EBI-37788;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 1400 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the XPF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA34929.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M15435; AAA34934.1; -; Genomic_DNA.
DR EMBL; U36624; AAB68165.1; -; Genomic_DNA.
DR EMBL; K02070; AAA34929.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006949; DAA11406.1; -; Genomic_DNA.
DR PIR; A26129; DDBYD1.
DR RefSeq; NP_015303.1; NM_001183836.1.
DR AlphaFoldDB; P06777; -.
DR SMR; P06777; -.
DR BioGRID; 36155; 488.
DR ComplexPortal; CPX-1362; SLX4-RAD1-RAD10 endonuclease complex.
DR ComplexPortal; CPX-1363; SAW1-RAD1-RAD10 endonuclease complex.
DR ComplexPortal; CPX-1708; Nucleotide-excision repair factor 1 complex.
DR DIP; DIP-2424N; -.
DR IntAct; P06777; 45.
DR MINT; P06777; -.
DR STRING; 4932.YPL022W; -.
DR iPTMnet; P06777; -.
DR MaxQB; P06777; -.
DR PaxDb; P06777; -.
DR PRIDE; P06777; -.
DR EnsemblFungi; YPL022W_mRNA; YPL022W; YPL022W.
DR GeneID; 856085; -.
DR KEGG; sce:YPL022W; -.
DR SGD; S000005943; RAD1.
DR VEuPathDB; FungiDB:YPL022W; -.
DR eggNOG; KOG0442; Eukaryota.
DR GeneTree; ENSGT00390000004394; -.
DR HOGENOM; CLU_002265_2_0_1; -.
DR InParanoid; P06777; -.
DR OMA; FHKILQA; -.
DR BioCyc; YEAST:G3O-33940-MON; -.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR PRO; PR:P06777; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P06777; protein.
DR GO; GO:1905348; C:endonuclease complex; IPI:ComplexPortal.
DR GO; GO:0000110; C:nucleotide-excision repair factor 1 complex; IPI:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR GO; GO:0006277; P:DNA amplification; IMP:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0000736; P:double-strand break repair via single-strand annealing, removal of nonhomologous ends; IMP:SGD.
DR GO; GO:0000710; P:meiotic mismatch repair; IMP:SGD.
DR GO; GO:0006312; P:mitotic recombination; IMP:SGD.
DR GO; GO:0006289; P:nucleotide-excision repair; IDA:SGD.
DR GO; GO:1901255; P:nucleotide-excision repair involved in interstrand cross-link repair; IBA:GO_Central.
DR GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; IDA:ComplexPortal.
DR GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; IBA:GO_Central.
DR GO; GO:0000735; P:removal of nonhomologous ends; IMP:SGD.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR InterPro; IPR006166; ERCC4_domain.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR006167; XPF.
DR Pfam; PF02732; ERCC4; 1.
DR SMART; SM00891; ERCC4; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR TIGRFAMs; TIGR00596; rad1; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1100
FT /note="DNA repair protein RAD1"
FT /id="PRO_0000198857"
FT DOMAIN 821..901
FT /note="ERCC4"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1071
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1072
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 223
FT /note="D -> N (in Ref. 4; AAA34929)"
FT /evidence="ECO:0000305"
FT CONFLICT 883
FT /note="C -> Y (in Ref. 4; AAA34929)"
FT /evidence="ECO:0000305"
FT CONFLICT 886
FT /note="M -> I (in Ref. 4; AAA34929)"
FT /evidence="ECO:0000305"
FT CONFLICT 912
FT /note="E -> K (in Ref. 4; AAA34929)"
FT /evidence="ECO:0000305"
FT CONFLICT 924
FT /note="V -> I (in Ref. 4; AAA34929)"
FT /evidence="ECO:0000305"
FT CONFLICT 1016
FT /note="G -> R (in Ref. 4; AAA34929)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1100 AA; 126370 MW; 06FDA601F3F59B10 CRC64;
MSQLFYQGDS DDELQEELTR QTTQASQSSK IKNEDEPDDS NHLNEVENED SKVLDDDAVL
YPLIPNEPDD IETSKPNIND IRPVDIQLTL PLPFQQKVVE NSLITEDALI IMGKGLGLLD
IVANLLHVLA TPTSINGQLK RALVLVLNAK PIDNVRIKEA LEELSWFSNT GKDDDDTAVE
SDDELFERPF NVVTADSLSI EKRRKLYISG GILSITSRIL IVDLLSGIVH PNRVTGMLVL
NADSLRHNSN ESFILEIYRS KNTWGFIKAF SEAPETFVME FSPLRTKMKE LRLKNVLLWP
RFRVEVSSCL NATNKTSHNK VIEVKVSLTN SMSQIQFGLM ECLKKCIAEL SRKNPELALD
WWNMENVLDI NFIRSIDSVM VPNWHRISYE SKQLVKDIRF LRHLLKMLVT SDAVDFFGEI
QLSLDANKPS VSRKYSESPW LLVDEAQLVI SYAKKRIFYK NEYTLEENPK WEQLIHILHD
ISHERMTNHL QGPTLVACSD NLTCLELAKV LNASNKKRGV RQVLLNKLKW YRKQREETKK
LVKEVQSQDT FPENATLNVS STFSKEQVTT KRRRTRGASQ VAAVEKLRNA GTNVDMEVVF
EDHKLSEEIK KGSGDDLDDG QEENAANDSK IFEIQEQENE ILIDDGDAEF DNGELEYVGD
LPQHITTHFN KDLWAEHCNE YEYVDRQDEI LISTFKSLND NCSLQEMMPS YIIMFEPDIS
FIRQIEVYKA IVKDLQPKVY FMYYGESIEE QSHLTAIKRE KDAFTKLIRE NANLSHHFET
NEDLSHYKNL AERKLKLSKL RKSNTRNAGG QQGFHNLTQD VVIVDTREFN ASLPGLLYRY
GIRVIPCMLT VGDYVITPDI CLERKSISDL IGSLQNNRLA NQCKKMLKYY AYPTLLIEFD
EGQSFSLEPF SERRNYKNKD ISTVHPISSK LSQDEIQLKL AKLVLRFPTL KIIWSSSPLQ
TVNIILELKL GREQPDPSNA VILGTNKVRS DFNSTAKGLK DGDNESKFKR LLNVPGVSKI
DYFNLRKKIK SFNKLQKLSW NEINELINDE DLTDRIYYFL RTEKEEQEQE STDENLESPG
KTTDDNALHD HHNDVPEAPV
