MRC1_YEAST
ID MRC1_YEAST Reviewed; 1096 AA.
AC P25588; D6VQV6; P25589; P27513; P87003; Q07218; Q8NIN2;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Mediator of replication checkpoint protein 1;
DE AltName: Full=DNA replication checkpoint mediator MRC1;
GN Name=MRC1; OrderedLocusNames=YCL061C; ORFNames=YCL61C/YCL60C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [2]
RP SEQUENCE REVISION.
RA Gromadka R.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE REVISION.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
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] OF 660-839.
RC STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX PubMed=2169608; DOI=10.1093/nar/18.17.5279;
RA Kern L.;
RT "The URK1 gene of Saccharomyces cerevisiae encoding uridine kinase.";
RL Nucleic Acids Res. 18:5279-5279(1990).
RN [6]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=11715016; DOI=10.1038/ncb1101-958;
RA Alcasabas A.A., Osborn A.J., Bachant J., Hu F., Werler P.J., Bousset K.,
RA Furuya K., Diffley J.F., Carr A.M., Elledge S.J.;
RT "Mrc1 transduces signals of DNA replication stress to activate Rad53.";
RL Nat. Cell Biol. 3:958-965(2001).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12865299; DOI=10.1101/gad.1098303;
RA Osborn A.J., Elledge S.J.;
RT "Mrc1 is a replication fork component whose phosphorylation in response to
RT DNA replication stress activates Rad53.";
RL Genes Dev. 17:1755-1767(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [9]
RP INTERACTION WITH CDC45.
RX PubMed=12944972; DOI=10.1038/nature01900;
RA Katou Y., Kanoh Y., Bando M., Noguchi H., Tanaka H., Ashikari T.,
RA Sugimoto K., Shirahige K.;
RT "S-phase checkpoint proteins Tof1 and Mrc1 form a stable replication-
RT pausing complex.";
RL Nature 424:1078-1083(2003).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605 AND SER-607, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605 AND THR-609, AND
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144; SER-434 AND SER-911, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409; SER-411; SER-605;
RP SER-607; SER-801 AND SER-807, 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: Required for normal DNA replication. Phosphorylated in
CC response to DNA replication stress. Phosphorylation allows it to
CC mediate the activation of RAD53. {ECO:0000269|PubMed:11715016,
CC ECO:0000269|PubMed:12865299}.
CC -!- SUBUNIT: Interacts with CDC45 in S phase.
CC {ECO:0000269|PubMed:12944972}.
CC -!- INTERACTION:
CC P25588; Q08032: CDC45; NbExp=4; IntAct=EBI-412442, EBI-4292;
CC P25588; Q08496: DIA2; NbExp=11; IntAct=EBI-412442, EBI-31943;
CC P25588; P32485: HOG1; NbExp=4; IntAct=EBI-412442, EBI-8437;
CC P25588; P53840: TOF1; NbExp=4; IntAct=EBI-412442, EBI-28257;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12865299}.
CC Note=Associated with chromatin during S phase.
CC -!- PTM: Phosphorylated by MEC1 and RAD53. {ECO:0000269|PubMed:11715016}.
CC -!- MISCELLANEOUS: Present with 721 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X59720; CAC42953.1; -; Genomic_DNA.
DR EMBL; X53998; CAA37945.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07425.1; -; Genomic_DNA.
DR PIR; S74279; S74279.
DR RefSeq; NP_009871.2; NM_001178704.1.
DR AlphaFoldDB; P25588; -.
DR BioGRID; 30926; 464.
DR DIP; DIP-1017N; -.
DR IntAct; P25588; 19.
DR MINT; P25588; -.
DR STRING; 4932.YCL061C; -.
DR CarbonylDB; P25588; -.
DR iPTMnet; P25588; -.
DR MaxQB; P25588; -.
DR PaxDb; P25588; -.
DR PRIDE; P25588; -.
DR EnsemblFungi; YCL061C_mRNA; YCL061C; YCL061C.
DR GeneID; 850297; -.
DR KEGG; sce:YCL061C; -.
DR SGD; S000000566; MRC1.
DR VEuPathDB; FungiDB:YCL061C; -.
DR eggNOG; ENOG502QSP5; Eukaryota.
DR HOGENOM; CLU_007004_0_0_1; -.
DR InParanoid; P25588; -.
DR OMA; EDEWHGI; -.
DR BioCyc; YEAST:G3O-29311-MON; -.
DR PRO; PR:P25588; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25588; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR GO; GO:0043596; C:nuclear replication fork; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0031298; C:replication fork protection complex; IDA:SGD.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR GO; GO:0006260; P:DNA replication; IMP:SGD.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; IMP:SGD.
DR GO; GO:0043570; P:maintenance of DNA repeat elements; IMP:SGD.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:SGD.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
DR GO; GO:0033262; P:regulation of nuclear cell cycle DNA replication; IMP:SGD.
DR GO; GO:0048478; P:replication fork protection; IMP:SGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR InterPro; IPR018564; Repl_chkpnt_MRC1_dom.
DR Pfam; PF09444; MRC1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; DNA replication; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1096
FT /note="Mediator of replication checkpoint protein 1"
FT /id="PRO_0000096574"
FT REGION 68..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 488..542
FT /evidence="ECO:0000255"
FT COILED 652..716
FT /evidence="ECO:0000255"
FT COMPBIAS 344..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..899
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1080
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 609
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 807
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 748
FT /note="L -> V (in Ref. 5; CAA37945)"
FT /evidence="ECO:0000305"
FT CONFLICT 808
FT /note="Missing (in Ref. 5; CAA37945)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1096 AA; 124326 MW; 378345EE503FFA81 CRC64;
MDDALHALSS LTAKKRTTTY KKVAVPILDE NDNTNGNGPN DIDNPPELTG NGFLFANATL
NRVKNRLEGK KAPEQNHNNG KDRSENSLPT QLISNLYDGG EELEKSEVKD NSYSEKNVSS
SFTQTQRIPV SIQQDKVFNV PIHSVNDGKP TQLIKEDGLV NETSQALKTP LTTGRPGATQ
RIDSSGATSQ TQPIKSIEPQ SQIITTSSNH SNALSPKIPI IPTELIGTSP LFQSIQNRGP
DTQMDVPPQT AHDEDKTQAI GIPQATHQEQ KTQIDTVAQT LQDEVPHTLK IREIQSELAS
EDSKREKARN VEYKKPQKPI PTKKFFSKES FLADFDDSSS NEDDDIKLEN AHPKPVQNDD
ELHENKSVEL NLTDETRINE KRVPLLSSYA NNLKREIDSS KCITLDLDSD SDEYGDDDMD
SIKLSKDESV LPISQLSKAT ILNLKARLSK QNQKLSQRPN KSKDPKVDHN VLLNTLRKAS
RKQILDHQKE VIETKGLKLE DMAKEKEIVE NLLEQEILRN KRIRQKEKRR EKLEENDFQL
NAHDSGSDSG SESSGFALSG NEIADYESSG SENDNRRESD SEKEDDEIIL KQKKSHHVKH
IINESDSDTE VEAKPKEKAD ESLPKRIAIN LGHYGDNIGE DTDKFQETNV LDTQNIEEVM
AERNTIENEV KDDVYVNEEA DEAIRRQLID KEKLQLKQKE KEHEAKIKEL KKRGVTNFFE
MEAEESEDEW HGIGGADGEG SDDYDSDLEK MIDDYSKNNF NPHEIREMLA AENKEMDIKM
INKILYDIKN GGFRNKRAKN SLELELSDDD EDDVLQQYRL KRRELMRKRR LEIGDDAKLV
KNPKSSAFFE SMVEDIIEYK NPFGAEEEYN LDITSTATDL DTQDNSINVG DNTGNNEQKP
VDQKNKKVII SEDFVQKSLS FLKSNNYEDF ETDKELSRIQ HGNDEAIEDL YTLKQNSSIK
SFTNSQTDST TSKTVNTIID LEKRPEDEDE VENGDTSLVG VFKHPSIIKS FASRTDINDK
FKEGNKTVKI LKSYKTVGSS KASITYMGKT RKLIAPKRKT EGSHRYHHDH HNKKMKMKTK
TKSNKLFESG QDSFDN
