RAD9_YEAST
ID RAD9_YEAST Reviewed; 1309 AA.
AC P14737; D6VSK0; Q04920;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=DNA repair protein RAD9;
GN Name=RAD9; OrderedLocusNames=YDR217C; ORFNames=YD9934.02C;
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=2664461; DOI=10.1128/mcb.9.5.1882-1896.1989;
RA Schiestl R.H., Reynolds P., Prakash S., Prakash L.;
RT "Cloning and sequence analysis of the Saccharomyces cerevisiae RAD9 gene
RT and further evidence that its product is required for cell cycle arrest
RT induced by DNA damage.";
RL Mol. Cell. Biol. 9:1882-1896(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=2247073; DOI=10.1128/mcb.10.12.6554-6564.1990;
RA Weinert T.A., Hartwell L.H.;
RT "Characterization of RAD9 of Saccharomyces cerevisiae and evidence that its
RT function acts posttranslationally in cell cycle arrest after DNA damage.";
RL Mol. Cell. Biol. 10:6554-6564(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 PHOSPHORYLATION, AND INTERACTION WITH RAD53.
RX PubMed=9755168; DOI=10.1093/emboj/17.19.5679;
RA Vialard J.E., Gilbert C.S., Green C.M., Lowndes N.F.;
RT "The budding yeast Rad9 checkpoint protein is subjected to Mec1/Tel1-
RT dependent hyperphosphorylation and interacts with Rad53 after DNA damage.";
RL EMBO J. 17:5679-5688(1998).
RN [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-56; SER-205; THR-218;
RP SER-248; SER-312; SER-315; SER-462; SER-568 AND SER-729, AND IDENTIFICATION
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-56; SER-315; SER-462;
RP THR-471; THR-474 AND SER-729, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Essential for cell cycle arrest at the G2 stage following DNA
CC damage by X-irradiation or inactivation of DNA ligase.
CC -!- SUBUNIT: Physically associates with RAD53.
CC -!- INTERACTION:
CC P14737; P32562: CDC5; NbExp=2; IntAct=EBI-14788, EBI-4440;
CC P14737; P47027: DPB11; NbExp=13; IntAct=EBI-14788, EBI-25984;
CC P14737; P22216: RAD53; NbExp=12; IntAct=EBI-14788, EBI-17843;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 400 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M26049; AAA34954.1; -; Genomic_DNA.
DR EMBL; Z48612; CAA88497.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12060.1; -; Genomic_DNA.
DR PIR; S59424; BVBYD9.
DR RefSeq; NP_010503.1; NM_001180525.1.
DR PDB; 1FHR; NMR; -; P=826-832.
DR PDB; 1J4K; NMR; -; P=826-832.
DR PDB; 1J4L; NMR; -; P=599-607.
DR PDB; 1J4P; NMR; -; B=149-161.
DR PDB; 1J4Q; NMR; -; B=188-200.
DR PDB; 1K2M; NMR; -; P=826-832.
DR PDB; 1K2N; NMR; -; P=599-607.
DR PDB; 1K3N; NMR; -; B=149-161.
DR PDB; 1K3Q; NMR; -; B=188-200.
DR PDB; 2FF4; X-ray; 1.90 A; E/F=188-195.
DR PDBsum; 1FHR; -.
DR PDBsum; 1J4K; -.
DR PDBsum; 1J4L; -.
DR PDBsum; 1J4P; -.
DR PDBsum; 1J4Q; -.
DR PDBsum; 1K2M; -.
DR PDBsum; 1K2N; -.
DR PDBsum; 1K3N; -.
DR PDBsum; 1K3Q; -.
DR PDBsum; 2FF4; -.
DR AlphaFoldDB; P14737; -.
DR SMR; P14737; -.
DR BioGRID; 32270; 481.
DR DIP; DIP-2516N; -.
DR ELM; P14737; -.
DR IntAct; P14737; 15.
DR MINT; P14737; -.
DR STRING; 4932.YDR217C; -.
DR iPTMnet; P14737; -.
DR MaxQB; P14737; -.
DR PaxDb; P14737; -.
DR PRIDE; P14737; -.
DR EnsemblFungi; YDR217C_mRNA; YDR217C; YDR217C.
DR GeneID; 851803; -.
DR KEGG; sce:YDR217C; -.
DR SGD; S000002625; RAD9.
DR VEuPathDB; FungiDB:YDR217C; -.
DR eggNOG; KOG3548; Eukaryota.
DR HOGENOM; CLU_279536_0_0_1; -.
DR InParanoid; P14737; -.
DR OMA; FDAMADV; -.
DR BioCyc; YEAST:G3O-29798-MON; -.
DR Reactome; R-SCE-3232118; SUMOylation of transcription factors.
DR Reactome; R-SCE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR EvolutionaryTrace; P14737; -.
DR PRO; PR:P14737; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P14737; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0008047; F:enzyme activator activity; IMP:SGD.
DR GO; GO:0042393; F:histone binding; IDA:SGD.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:SGD.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:0031571; P:mitotic G1 DNA damage checkpoint signaling; IMP:SGD.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:SGD.
DR GO; GO:0110027; P:negative regulation of DNA strand resection involved in replication fork processing; IMP:SGD.
DR GO; GO:0006289; P:nucleotide-excision repair; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:SGD.
DR Gene3D; 3.40.50.10190; -; 1.
DR IDEAL; IID50198; -.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR013914; Rad9_Rad53-bd_dom_fun.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF08605; Rad9_Rad53_bind; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; DNA damage; DNA replication inhibitor; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1309
FT /note="DNA repair protein RAD9"
FT /id="PRO_0000097158"
FT DOMAIN 994..1122
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 218
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 471
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 474
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 433
FT /note="S -> C (in Ref. 1; AAA34954 and 2; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:1K3Q"
SQ SEQUENCE 1309 AA; 148398 MW; FCDAC16694484D8D CRC64;
MSGQLVQWKS SPDRVTQSAI KEALHSPLAD GDMNEMNVPV DPLENKVNST NIIEGSPKAN
PNPVKFMNTS EIFQKSLGLL DESPRHDDEL NIEVGDNDRP NANILHNERT PDLDRIANFF
KSNRTPGKEN LLTKYQSSDL EDTPLMLRKK MTFQTPTDPL EQKTFKKLKS DTGFCYYGEQ
NDGEENASLE VTEADATFVQ MAERSADNYD CALEGIVTPK RYKDELSKSG GMQDERVQKT
QIMISAESPN SISSYDKNKI TGNGRTTRNV NKVFNNNEDN IGAIEEKNPV KKKSENYSSD
DLRERNNQII QSNESEEINE LEKNLNVSGR ENDVNNLDID INSAVSGTPS RNNAEEEMYS
SESVNNREPS KKWIFRYSKD KTENNSNRST QIVNNPRTQE MPLDSISIDT QPLSKSFNTE
TNNELETQII VSSLSQGISA QKGPVFHSTG QTEEIKTQII NSPEQNALNA TFETPVTLSR
INFEPILEVP ETSSPSKNTM SKPSNSSPIP KEKDTFNIHE REVETNNVFS NDIQNSSNAA
TRDDIIIAGS SDFNEQKEIT DRIYLQLSGK QISDSGSDET ERMSPNELDT KKESTIMSEV
ELTQELPEVE EQQDLQTSPK KLVVEEETLM EIKKSKGNSL QLHDDNKECN SDKQDGTESL
DVALIEHESK GQSSELQKNL MQLFPSESQE IIQNRRTIKR RQKDTIEIGE EEENRSTKTS
PTKHLKRNSD LDAASIKREP SCSITIQTGE TGSGKDSKEQ SYVFPEGIRT ADNSFLSKDD
IIFGNAVWCQ YTWNYKFYPG ILLEVDTNQD GCWIYFETGR SLTKDEDIYY LDIRIGDAVT
FDGNEYVVVG LECRSHDLNI IRCIRGYDTV HLKKKNASGL LGKRTLIKAL SSISLDLSEW
AKRAKIILED NEKNKGDAYR YLRHPIRGRK SMTNVLSPKK HTDDEKDINT HTEVYNNEIE
SSSEKKEIVK KDSRDALAEH AGAPSLLFSS GEIRTGNVFD KCIFVLTSLF ENREELRQTI
ESQGGTVIES GFSTLFNFTH PLAKSLVNKG NTDNIRELAL KLAWKPHSLF ADCRFACLIT
KRHLRSLKYL ETLALGWPTL HWKFISACIE KKRIVPHLIY QYLLPSGESF RLSLDSPSKG
GIIKSNNIFS FYTQFLRGSN LRDQICGVKK MLNDYIVIVW GRSELDSFVK FAFACLSAGR
MLTIDLPNID VDDTEPLLNA LDSLVPRIGS ELSNRKLKFL IYANENNGKS QMKLLERLRS
QISLKFKKFN YIFHTESKEW LIQTIINEDT GFHDDITDND IYNTISEVR
