RAD2_YEAST
ID RAD2_YEAST Reviewed; 1031 AA.
AC P07276; D6VV38; E9P8X9;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=DNA repair protein RAD2;
DE EC=3.1.-.-;
GN Name=RAD2; OrderedLocusNames=YGR258C;
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=3000874; DOI=10.1016/0378-1119(85)90177-5;
RA Nicolet C.M., Chenevert J.M., Friedberg E.C.;
RT "The RAD2 gene of Saccharomyces cerevisiae: nucleotide sequence and
RT transcript mapping.";
RL Gene 36:225-234(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RX PubMed=3011752; DOI=10.1128/jb.166.3.914-923.1986;
RA Madura K., Prakash S.;
RT "Nucleotide sequence, transcript mapping, and regulation of the RAD2 gene
RT of Saccharomyces cerevisiae.";
RL J. Bacteriol. 166:914-923(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9090059;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<287::aid-yea75>3.0.co;2-5;
RA Clemente M.L., Sartori G., Cardazzo B., Carignani G.;
RT "Analysis of an 11.6 kb region from the right arm of chromosome VII of
RT Saccharomyces cerevisiae between the RAD2 and the MES1 genes reveals the
RT presence of three new genes.";
RL Yeast 13:287-290(1997).
RN [7]
RP FUNCTION.
RX PubMed=8247134; DOI=10.1038/366365a0;
RA Habraken Y., Sung P., Prakash L., Prakash S.;
RT "Yeast excision repair gene RAD2 encodes a single-stranded DNA
RT endonuclease.";
RL Nature 366:365-368(1993).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-367, AND
RP 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: Single-stranded DNA endonuclease involved in excision repair
CC of DNA damaged with UV light, bulky adducts, or cross-linking agents.
CC Essential for the incision step of excision-repair.
CC {ECO:0000269|PubMed:8247134}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. They probably participate in
CC the reaction catalyzed by the enzyme. May bind an additional third
CC magnesium ion after substrate binding. {ECO:0000250};
CC -!- INTERACTION:
CC P07276; P19882: HSP60; NbExp=2; IntAct=EBI-14757, EBI-8586;
CC P07276; Q00416: SEN1; NbExp=3; IntAct=EBI-14757, EBI-16945;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 846 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.
CC {ECO:0000305}.
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DR EMBL; M10275; AAA66928.1; -; Genomic_DNA.
DR EMBL; Y07777; CAA69080.1; -; Genomic_DNA.
DR EMBL; Z73043; CAA97287.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08349.1; -; Genomic_DNA.
DR EMBL; AY692857; AAT92876.1; -; Genomic_DNA.
DR PIR; A29839; A29839.
DR RefSeq; NP_011774.1; NM_001181387.1.
DR PDB; 2LOX; NMR; -; B=642-690.
DR PDB; 4Q0R; X-ray; 2.75 A; A/B=1-111, A/B=732-986.
DR PDB; 4Q0W; X-ray; 2.10 A; A/B=2-111, A/B=732-986.
DR PDB; 4Q0Z; X-ray; 2.40 A; A/B/E/F=2-111, A/B/E/F=732-986.
DR PDB; 4Q10; X-ray; 2.70 A; A/B=2-111, A/B=732-986.
DR PDBsum; 2LOX; -.
DR PDBsum; 4Q0R; -.
DR PDBsum; 4Q0W; -.
DR PDBsum; 4Q0Z; -.
DR PDBsum; 4Q10; -.
DR AlphaFoldDB; P07276; -.
DR SMR; P07276; -.
DR BioGRID; 33510; 74.
DR DIP; DIP-5869N; -.
DR ELM; P07276; -.
DR IntAct; P07276; 7.
DR STRING; 4932.YGR258C; -.
DR iPTMnet; P07276; -.
DR MaxQB; P07276; -.
DR PaxDb; P07276; -.
DR PRIDE; P07276; -.
DR EnsemblFungi; YGR258C_mRNA; YGR258C; YGR258C.
DR GeneID; 853174; -.
DR KEGG; sce:YGR258C; -.
DR SGD; S000003490; RAD2.
DR VEuPathDB; FungiDB:YGR258C; -.
DR eggNOG; KOG2520; Eukaryota.
DR GeneTree; ENSGT00940000163631; -.
DR HOGENOM; CLU_003018_2_0_1; -.
DR InParanoid; P07276; -.
DR OMA; WTVVQPC; -.
DR BioCyc; YEAST:G3O-30928-MON; -.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR PRO; PR:P07276; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P07276; protein.
DR GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IDA:SGD.
DR GO; GO:0006289; P:nucleotide-excision repair; IDA:SGD.
DR GO; GO:0006295; P:nucleotide-excision repair, DNA incision, 3'-to lesion; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:SGD.
DR DisProt; DP01631; -.
DR IDEAL; IID50166; -.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR001044; XPG/Rad2_eukaryotes.
DR InterPro; IPR019974; XPG_CS.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR Pfam; PF00867; XPG_I; 1.
DR Pfam; PF00752; XPG_N; 1.
DR PRINTS; PR00853; XPGRADSUPER.
DR PRINTS; PR00066; XRODRMPGMNTG.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00484; XPGI; 1.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF47807; SSF47807; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
DR TIGRFAMs; TIGR00600; rad2; 1.
DR PROSITE; PS00841; XPG_1; 1.
DR PROSITE; PS00842; XPG_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; Endonuclease; Hydrolase; Magnesium;
KW Metal-binding; Nuclease; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1031
FT /note="DNA repair protein RAD2"
FT /id="PRO_0000154035"
FT REGION 1..95
FT /note="N-domain"
FT REGION 342..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..884
FT /note="I-domain"
FT COMPBIAS 459..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 792
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 794
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 813
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 815
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 864
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 782
FT /note="F -> L (in Ref. 5; AAT92876)"
FT /evidence="ECO:0000305"
FT STRAND 667..669
FT /evidence="ECO:0007829|PDB:2LOX"
FT HELIX 769..781
FT /evidence="ECO:0007829|PDB:4Q0W"
FT STRAND 786..788
FT /evidence="ECO:0007829|PDB:4Q0W"
FT HELIX 793..802
FT /evidence="ECO:0007829|PDB:4Q0W"
FT STRAND 807..810
FT /evidence="ECO:0007829|PDB:4Q0W"
FT HELIX 815..818
FT /evidence="ECO:0007829|PDB:4Q0W"
FT STRAND 823..827
FT /evidence="ECO:0007829|PDB:4Q0W"
FT STRAND 830..839
FT /evidence="ECO:0007829|PDB:4Q0W"
FT HELIX 840..847
FT /evidence="ECO:0007829|PDB:4Q0W"
FT HELIX 851..861
FT /evidence="ECO:0007829|PDB:4Q0W"
FT HELIX 874..884
FT /evidence="ECO:0007829|PDB:4Q0W"
FT HELIX 887..899
FT /evidence="ECO:0007829|PDB:4Q0W"
FT HELIX 901..904
FT /evidence="ECO:0007829|PDB:4Q0W"
FT HELIX 909..920
FT /evidence="ECO:0007829|PDB:4Q0W"
FT HELIX 932..939
FT /evidence="ECO:0007829|PDB:4Q0W"
FT HELIX 957..968
FT /evidence="ECO:0007829|PDB:4Q0W"
FT HELIX 972..982
FT /evidence="ECO:0007829|PDB:4Q0W"
SQ SEQUENCE 1031 AA; 117838 MW; 682D4AECFBD7F0F3 CRC64;
MGVHSFWDIA GPTARPVRLE SLEDKRMAVD ASIWIYQFLK AVRDQEGNAV KNSHITGFFR
RICKLLYFGI RPVFVFDGGV PVLKRETIRQ RKERRQGKRE SAKSTARKLL ALQLQNGSND
NVKNSTPSSG SSVQIFKPQD EWDLPDIPGF KYDKEDARVN SNKTFEKLMN SINGDGLEDI
DLDTINPASA EFEELPKATQ YLILSSLRLK SRLRMGYSKE QLETIFPNSM DFSRFQIDMV
KRRNFFTQKL INTTGFQDGG ASKLNEEVIN RISGQKSKEY KLTKTNNGWI LGLGANDGSD
AQKAIVIDDK DAGALVKQLD SNAEDGDVLR WDDLEDNSLK IVRHESSNAT TAPQKRSNRS
EDEGCDSDEC EWEEVELKPK NVKFVEDFSL KAARLPYMGQ SLNNAGSKSF LDKRHDQASP
SKTTPTMRIS RISVEDDDED YLKQIEEIEM MEAVQLSKME KKPEADDKSK IAKPVTSKGT
EARPPIVQYG LLGAQPDSKQ PYHVTNLNSK SESVIKRTSK TVLSEFRPPS QQEDKGAILT
EGEQNLNFIS HKIPQFDFNN ENSLLFQKNT ESNVSQEATK EKSPIPEMPS WFSSTASQQL
YNPYNTTNFV EDKNVRNEQE SGAETTNKGS SYELLTGLNA TEILERESEK ESSNDENKDD
DLEVLSEELF EDVPTKSQIS KEAEDNDSRK VESINKEHRK PLIFDYDFSE DEEDNIVENM
IKEQEEFDTF KNTTLSTSAE RNVAENAFVE DELFEQQMKD KRDSDEVTMD MIKEVQELLS
RFGIPYITAP MEAEAQCAEL LQLNLVDGII TDDSDVFLFG GTKIYKNMFH EKNYVEFYDA
ESILKLLGLD RKNMIELAQL LGSDYTNGLK GMGPVSSIEV IAEFGNLKNF KDWYNNGQFD
KRKQETENKF EKDLRKKLVN NEIILDDDFP SVMVYDAYMR PEVDHDTTPF VWGVPDLDML
RSFMKTQLGW PHEKSDEILI PLIRDVNKRK KKGKQKRINE FFPREYISGD KKLNTSKRIS
TATGKLKKRK M
