RAD7_YEAST
ID RAD7_YEAST Reviewed; 565 AA.
AC P06779; D6VWM3;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=DNA repair protein RAD7;
GN Name=RAD7; OrderedLocusNames=YJR052W; ORFNames=J1665;
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=2158927; DOI=10.1016/0378-1119(90)90297-5;
RA Melnick L., Sherman F.;
RT "Nucleotide sequence of the COR region: a cluster of six genes in the yeast
RT Saccharomyces cerevisiae.";
RL Gene 87:157-166(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RX PubMed=3023893; DOI=10.1128/mcb.6.5.1497-1507.1986;
RA Perozzi G., Prakash S.;
RT "RAD7 gene of Saccharomyces cerevisiae: transcripts, nucleotide sequence
RT analysis, and functional relationship between the RAD7 and RAD23 gene
RT products.";
RL Mol. Cell. Biol. 6:1497-1507(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7975898; DOI=10.1002/yea.320100611;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Revised nucleotide sequence of the COR region of yeast Saccharomyces
RT cerevisiae chromosome X.";
RL Yeast 10:811-818(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [5]
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 [6]
RP IDENTIFICATION IN THE GGR COMPLEX, AND FUNCTION.
RX PubMed=10601031; DOI=10.1101/gad.13.23.3052;
RA Reed S.H., Akiyama M., Stillman B., Friedberg E.C.;
RT "Yeast autonomously replicating sequence binding factor is involved in
RT nucleotide excision repair.";
RL Genes Dev. 13:3052-3058(1999).
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 FUNCTION OF THE GGR COMPLEX.
RX PubMed=15177043; DOI=10.1016/j.dnarep.2003.11.004;
RA Yu S., Owen-Hughes T., Friedberg E.C., Waters R., Reed S.H.;
RT "The yeast Rad7/Rad16/Abf1 complex generates superhelical torsion in DNA
RT that is required for nucleotide excision repair.";
RL DNA Repair 3:277-287(2004).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND SER-85, 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: Component of the global genome repair (GGR) complex which
CC promotes global genome nucleotide excision repair (GG-NER) which
CC removes DNA damage from nontranscribing DNA. This protein is one of 10
CC proteins (RAD1, 2,3,4,7,10,14, 16,23 and MMS19) involved in excision
CC repair of DNA damaged with UV light, bulky adducts, or cross-linking
CC agents. {ECO:0000269|PubMed:10601031, ECO:0000269|PubMed:15177043}.
CC -!- SUBUNIT: Component of the global genome repair (GGR) complex composed
CC of at least ABF1, RAD7 and RAD16. {ECO:0000269|PubMed:10601031}.
CC -!- INTERACTION:
CC P06779; Q03071: ELC1; NbExp=4; IntAct=EBI-14780, EBI-30154;
CC P06779; P31244: RAD16; NbExp=5; IntAct=EBI-14780, EBI-14645;
CC P06779; P0CS90: SSC1; NbExp=2; IntAct=EBI-14780, EBI-8637;
CC -!- DISRUPTION PHENOTYPE: Mutants with mutations in the RAD7, RAD14, RAD16,
CC and RAD23 genes show partial incision defectiveness.
CC {ECO:0000269|PubMed:3023893}.
CC -!- MISCELLANEOUS: Present with 937 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: To S.pombe SpCC613.14. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M37696; AAB59347.1; -; Genomic_DNA.
DR EMBL; M13015; AAA34953.1; -; Genomic_DNA.
DR EMBL; L26347; AAA62860.1; -; Genomic_DNA.
DR EMBL; L36344; AAA88755.1; -; Genomic_DNA.
DR EMBL; Z49552; CAA89580.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08839.1; -; Genomic_DNA.
DR PIR; A25226; A25226.
DR RefSeq; NP_012586.1; NM_001181710.1.
DR PDB; 5ZB2; X-ray; 2.30 A; A=165-565.
DR PDBsum; 5ZB2; -.
DR AlphaFoldDB; P06779; -.
DR SMR; P06779; -.
DR BioGRID; 33806; 97.
DR ComplexPortal; CPX-1191; Global genome repair CUL3/RAD7/RAD16/ELC1 ubiquitin ligase complex.
DR ComplexPortal; CPX-1709; Nucleotide excision repair factor 4 complex.
DR DIP; DIP-2484N; -.
DR IntAct; P06779; 14.
DR MINT; P06779; -.
DR STRING; 4932.YJR052W; -.
DR iPTMnet; P06779; -.
DR MaxQB; P06779; -.
DR PaxDb; P06779; -.
DR PRIDE; P06779; -.
DR EnsemblFungi; YJR052W_mRNA; YJR052W; YJR052W.
DR GeneID; 853512; -.
DR KEGG; sce:YJR052W; -.
DR SGD; S000003813; RAD7.
DR VEuPathDB; FungiDB:YJR052W; -.
DR eggNOG; KOG1947; Eukaryota.
DR HOGENOM; CLU_006598_2_1_1; -.
DR InParanoid; P06779; -.
DR OMA; HISNTHR; -.
DR BioCyc; YEAST:G3O-31686-MON; -.
DR PRO; PR:P06779; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P06779; protein.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0000113; C:nucleotide-excision repair factor 4 complex; IDA:SGD.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0070911; P:global genome nucleotide-excision repair; IDA:ComplexPortal.
DR GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; IDA:SGD.
DR GO; GO:0008104; P:protein localization; IDA:SGD.
DR GO; GO:0016567; P:protein ubiquitination; IEA:GOC.
DR GO; GO:0009411; P:response to UV; IDA:ComplexPortal.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:ComplexPortal.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR SMART; SM00367; LRR_CC; 4.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; Phosphoprotein; Reference proteome.
FT CHAIN 1..565
FT /note="DNA repair protein RAD7"
FT /id="PRO_0000097155"
FT REGION 1..200
FT /note="Hydrophilic"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 278..279
FT /note="LL -> FV (in Ref. 1; AAB59347)"
FT /evidence="ECO:0000305"
FT CONFLICT 504..505
FT /note="AC -> RP (in Ref. 1; AAB59347)"
FT /evidence="ECO:0000305"
FT HELIX 168..201
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 210..219
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 227..231
FT /evidence="ECO:0007829|PDB:5ZB2"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 249..258
FT /evidence="ECO:0007829|PDB:5ZB2"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 275..284
FT /evidence="ECO:0007829|PDB:5ZB2"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:5ZB2"
FT TURN 311..314
FT /evidence="ECO:0007829|PDB:5ZB2"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 328..338
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:5ZB2"
FT STRAND 343..349
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 359..362
FT /evidence="ECO:0007829|PDB:5ZB2"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 384..394
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:5ZB2"
FT STRAND 400..405
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 411..416
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 418..421
FT /evidence="ECO:0007829|PDB:5ZB2"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 441..450
FT /evidence="ECO:0007829|PDB:5ZB2"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 469..477
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:5ZB2"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 497..501
FT /evidence="ECO:0007829|PDB:5ZB2"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 521..530
FT /evidence="ECO:0007829|PDB:5ZB2"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:5ZB2"
FT STRAND 556..559
FT /evidence="ECO:0007829|PDB:5ZB2"
FT HELIX 561..563
FT /evidence="ECO:0007829|PDB:5ZB2"
SQ SEQUENCE 565 AA; 63777 MW; 85C77357DC99737A CRC64;
MYRSRNRPKR GGENEVKGPN SALTQFLREE GISAENIKQK WYQRQSKKQE DATDEKKGKA
EDDSFTAEIS RVVEDEEIDE IGTGSGTETE RAQVSYDARM KLVPADSDEE EYETSHISDT
PVSLSSANDR ESLTKKRQNT AKIIQNRRRK RKRAADLLDR RVNKVSSLQS LCITKISENI
SKWQKEADES SKLVFNKLRD VLGGVSTANL NNLAKALSKN RALNDHTLQL FLKTDLKRLT
FSDCSKISFD GYKTLAIFSP HLTELSLQMC GQLNHESLLY IAEKLPNLKS LNLDGPFLIN
EDTWEKFFVI MKGRLEEFHI SNTHRFTDKS LSNLLINCGS TLVSLGLSRL DSISNYALLP
QYLVNDEFHS LCIEYPFNEE DVNDEIIINL LGQIGRTLRK LVLNGCIDLT DSMIINGLTA
FIPEKCPLEV LSLEESDQIT TDSLSYFFSK VELNNLIECS FRRCLQLGDM AIIELLLNGA
RDSLRSLNLN SLKELTKEAF VALACPNLTY LDLGFVRCVD DSVIQMLGEQ NPNLTVIDVF
GDNLVTEKAT MRPGLTLIGR QSDSI
