CMR1_YEAST
ID CMR1_YEAST Reviewed; 522 AA.
AC Q12510; D6VRJ4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=DNA damage-binding protein CMR1 {ECO:0000305|PubMed:22367945};
DE AltName: Full=Changed mutation rate protein 1 {ECO:0000303|PubMed:22367945};
GN Name=CMR1 {ECO:0000303|PubMed:22367945};
GN OrderedLocusNames=YDL156W {ECO:0000312|SGD:S000002315}; ORFNames=D1536;
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].
RC STRAIN=ATCC 90840 / EAY235 / FY23;
RX PubMed=8972581;
RX DOI=10.1002/(sici)1097-0061(199612)12:15%3c1587::aid-yea46%3e3.0.co;2-6;
RA Delaveau T.T.D., Blugeon C., Jacq C., Perea J.;
RT "Analysis of a 23 kb region on the left arm of yeast chromosome IV.";
RL Yeast 12:1587-1592(1996).
RN [2]
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 [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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND SER-224, AND
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND IDENTIFICATION BY
RP 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).
RN [9]
RP FUNCTION.
RX PubMed=22367945; DOI=10.1007/s12275-012-1597-4;
RA Choi D.H., Kwon S.H., Kim J.H., Bae S.H.;
RT "Saccharomyces cerevisiae Cmr1 protein preferentially binds to UV-damaged
RT DNA in vitro.";
RL J. Microbiol. 50:112-118(2012).
RN [10]
RP INDUCTION.
RX PubMed=23349438; DOI=10.1098/rsif.2012.0990;
RA Abu-Jamous B., Fa R., Roberts D.J., Nandi A.K.;
RT "Yeast gene CMR1/YDL156W is consistently co-expressed with genes
RT participating in DNA-metabolic processes in a variety of stringent
RT clustering experiments.";
RL J. R. Soc. Interface 10:20120990-20120990(2013).
CC -!- FUNCTION: DNA-binding protein that binds to both single- and double-
CC stranded DNA. Binds preferentially to UV-damaged DNA in vitro
CC (PubMed:22367945). May be involved in DNA-metabolic processes
CC (PubMed:23349438). {ECO:0000269|PubMed:22367945,
CC ECO:0000305|PubMed:23349438}.
CC -!- INTERACTION:
CC Q12510; P43603: LSB3; NbExp=2; IntAct=EBI-35343, EBI-22980;
CC Q12510; P32793: YSC84; NbExp=2; IntAct=EBI-35343, EBI-24460;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Closely coexpressed with replication factor A (RF-A), the
CC cohesion complex and the DNA polymerases alpha, delta and epsilon.
CC {ECO:0000269|PubMed:23349438}.
CC -!- MISCELLANEOUS: Present with 3810 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat DDB2/WDR76 family. {ECO:0000305}.
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DR EMBL; X97751; CAA66335.1; -; Genomic_DNA.
DR EMBL; Z74204; CAA98730.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11704.1; -; Genomic_DNA.
DR PIR; S67704; S67704.
DR RefSeq; NP_010125.1; NM_001180216.1.
DR AlphaFoldDB; Q12510; -.
DR SMR; Q12510; -.
DR BioGRID; 31907; 697.
DR DIP; DIP-1004N; -.
DR IntAct; Q12510; 24.
DR MINT; Q12510; -.
DR STRING; 4932.YDL156W; -.
DR iPTMnet; Q12510; -.
DR MaxQB; Q12510; -.
DR PaxDb; Q12510; -.
DR PRIDE; Q12510; -.
DR EnsemblFungi; YDL156W_mRNA; YDL156W; YDL156W.
DR GeneID; 851399; -.
DR KEGG; sce:YDL156W; -.
DR SGD; S000002315; CMR1.
DR VEuPathDB; FungiDB:YDL156W; -.
DR eggNOG; KOG4328; Eukaryota.
DR GeneTree; ENSGT00510000048144; -.
DR HOGENOM; CLU_017019_1_1_1; -.
DR InParanoid; Q12510; -.
DR OMA; TVVRHNC; -.
DR BioCyc; YEAST:G3O-29551-MON; -.
DR PRO; PR:Q12510; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12510; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:2000001; P:regulation of DNA damage checkpoint; IMP:SGD.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR033052; Cmr1/WDR76.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR14773:SF0; PTHR14773:SF0; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA damage; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..522
FT /note="DNA damage-binding protein CMR1"
FT /id="PRO_0000240874"
FT REPEAT 183..224
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 239..281
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 287..327
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 331..371
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 388..427
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 442..481
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 482..521
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 38..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 522 AA; 59156 MW; 3BE716E4858EF3E8 CRC64;
MPELTEFQKK RLENIKRNND LLKKLHLSGV ASQIKHEAGV LEKSRAPAKK KQKTTNTRAT
KSASPTLPTR RSRRLRGESA DDVKGIPNVN DNQLLKMGSP DGQDKNFIDA IKEKPVIGDV
KLSDLIKDED ESALLEKFKR FNNGNFSSGD FFEEIKKRQG DVTGMDEFDL DLYDVFQPNE
IKITYERISA TYFHPAMEKK LIIAGDTSGT VGFWNVRDEP LADSEEDRME EPDITRVKLF
TKNVGRIDCF PADTSKILLT SYDGSIRSVH LNNLQSEEVL TLKNEYDDSL GISDCQFSYE
NPNVLFLTTL GGEFTTFDTR VKKSEYNLRR LADKKIGSMA INPMRPYEIA TGSLDRTLKI
WDTRNLVKKP EWSQYEDYPS HEIVSTYDSR LSVSAVSYSP TDGTLVCNGY DDTIRLFDVK
SRDHLSAKLE PKLTIQHNCQ TGRWTSILKA RFKPNKNVFA IANMKRAIDI YNSEGQQLAH
LPTATVPAVI SWHPLRNWIA GGNSSGKIFL FTDDSGTIKQ EE
