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   27-MAR-2024, entry version 203.
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; 498.
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; 4932-YDR217C; -.
DR   PeptideAtlas; P14737; -.
DR   EnsemblFungi; YDR217C_mRNA; YDR217C; YDR217C.
DR   GeneID; 851803; -.
DR   KEGG; sce:YDR217C; -.
DR   AGR; SGD:S000002625; -.
DR   SGD; S000002625; RAD9.
DR   VEuPathDB; FungiDB:YDR217C; -.
DR   eggNOG; KOG3548; Eukaryota.
DR   HOGENOM; CLU_279536_0_0_1; -.
DR   InParanoid; P14737; -.
DR   OMA; DYKFACL; -.
DR   OrthoDB; 2056928at2759; -.
DR   BioCyc; YEAST:G3O-29798-MONOMER; -.
DR   Reactome; R-SCE-3232118; SUMOylation of transcription factors.
DR   BioGRID-ORCS; 851803; 2 hits in 10 CRISPR screens.
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   CDD; cd17745; BRCT_p53bp1_rpt1; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   IDEAL; IID50198; -.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR047249; BRCT_p53bp1-like_rpt1.
DR   InterPro; IPR013914; Rad9_Rad53-bd_dom_fun.
DR   InterPro; IPR047252; TP53BP1-like.
DR   PANTHER; PTHR15321:SF3; TP53-BINDING PROTEIN 1; 1.
DR   PANTHER; PTHR15321; TUMOR SUPPRESSOR P53-BINDING PROTEIN 1; 1.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF08605; Rad9_Rad53_bind; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SUPFAM; SSF52113; BRCT domain; 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
//