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Mediator of replication checkpoint protein 1 (DNA replication checkpoint mediator MRC1)

 MRC1_YEAST              Reviewed;        1096 AA.
P25588; D6VQV6; P25589; P27513; P87003; Q07218; Q8NIN2;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
19-SEP-2003, sequence version 3.
23-MAY-2018, entry version 147.
RecName: Full=Mediator of replication checkpoint protein 1;
AltName: Full=DNA replication checkpoint mediator MRC1;
Name=MRC1; OrderedLocusNames=YCL061C; ORFNames=YCL61C/YCL60C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=1574125; DOI=10.1038/357038a0;
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M.,
Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W.,
Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H.,
Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V.,
Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A.,
de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H.,
Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K.,
Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B.,
Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A.,
Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y.,
Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R.,
Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G.,
Tzermia M., Urrestarazu L.A., Valle G., Vetter I.,
van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H.,
Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C.,
Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.;
"The complete DNA sequence of yeast chromosome III.";
Nature 357:38-46(1992).
[2]
SEQUENCE REVISION.
Gromadka R.;
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
[3]
SEQUENCE REVISION.
Valles G., Volckaerts G.;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 660-839.
STRAIN=ATCC 28383 / FL100 / VTT C-80102;
PubMed=2169608; DOI=10.1093/nar/18.17.5279;
Kern L.;
"The URK1 gene of Saccharomyces cerevisiae encoding uridine kinase.";
Nucleic Acids Res. 18:5279-5279(1990).
[6]
FUNCTION, AND PHOSPHORYLATION.
PubMed=11715016; DOI=10.1038/ncb1101-958;
Alcasabas A.A., Osborn A.J., Bachant J., Hu F., Werler P.J.,
Bousset K., Furuya K., Diffley J.F., Carr A.M., Elledge S.J.;
"Mrc1 transduces signals of DNA replication stress to activate
Rad53.";
Nat. Cell Biol. 3:958-965(2001).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12865299; DOI=10.1101/gad.1098303;
Osborn A.J., Elledge S.J.;
"Mrc1 is a replication fork component whose phosphorylation in
response to DNA replication stress activates Rad53.";
Genes Dev. 17:1755-1767(2003).
[8]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=14690591; DOI=10.1016/S1097-2765(03)00476-3;
Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B.,
Riffle M., Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H.,
Snydsman B.E., Bradley P., Muller E.G.D., Fields S., Baker D.,
Yates J.R. III, Davis T.N.;
"Assigning function to yeast proteins by integration of
technologies.";
Mol. Cell 12:1353-1365(2003).
[9]
INTERACTION WITH CDC45.
PubMed=12944972; DOI=10.1038/nature01900;
Katou Y., Kanoh Y., Bando M., Noguchi H., Tanaka H., Ashikari T.,
Sugimoto K., Shirahige K.;
"S-phase checkpoint proteins Tof1 and Mrc1 form a stable replication-
pausing complex.";
Nature 424:1078-1083(2003).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605 AND SER-607, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605 AND THR-609, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144; SER-434 AND
SER-911, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409; SER-411; SER-605;
SER-607; SER-801 AND SER-807, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Required for normal DNA replication. Phosphorylated in
response to DNA replication stress. Phosphorylation allows it to
mediate the activation of RAD53. {ECO:0000269|PubMed:11715016,
ECO:0000269|PubMed:12865299}.
-!- SUBUNIT: Interacts with CDC45 in S phase.
{ECO:0000269|PubMed:12944972}.
-!- INTERACTION:
Q08032:CDC45; NbExp=4; IntAct=EBI-412442, EBI-4292;
Q08496:DIA2; NbExp=11; IntAct=EBI-412442, EBI-31943;
P32485:HOG1; NbExp=4; IntAct=EBI-412442, EBI-8437;
P53840:TOF1; NbExp=4; IntAct=EBI-412442, EBI-28257;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12865299}.
Note=Associated with chromatin during S phase.
-!- PTM: Phosphorylated by MEC1 and RAD53.
{ECO:0000269|PubMed:11715016}.
-!- MISCELLANEOUS: Present with 721 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
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EMBL; X59720; CAC42953.1; -; Genomic_DNA.
EMBL; X53998; CAA37945.1; -; Genomic_DNA.
EMBL; BK006937; DAA07425.1; -; Genomic_DNA.
PIR; S74279; S74279.
RefSeq; NP_009871.2; NM_001178704.1.
ProteinModelPortal; P25588; -.
BioGrid; 30926; 435.
DIP; DIP-1017N; -.
IntAct; P25588; 19.
MINT; P25588; -.
STRING; 4932.YCL061C; -.
CarbonylDB; P25588; -.
iPTMnet; P25588; -.
MaxQB; P25588; -.
PaxDb; P25588; -.
PRIDE; P25588; -.
EnsemblFungi; CAC42953; CAC42953; CAC42953.
EnsemblFungi; YCL061C; YCL061C; YCL061C.
GeneID; 850297; -.
KEGG; sce:YCL061C; -.
EuPathDB; FungiDB:YCL061C; -.
SGD; S000000566; MRC1.
InParanoid; P25588; -.
KO; K11272; -.
OMA; EDEWHGI; -.
OrthoDB; EOG092C0DFP; -.
BioCyc; YEAST:G3O-29311-MONOMER; -.
PRO; PR:P25588; -.
Proteomes; UP000002311; Chromosome III.
GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
GO; GO:0000228; C:nuclear chromosome; IPI:SGD.
GO; GO:0034399; C:nuclear periphery; IDA:SGD.
GO; GO:0043596; C:nuclear replication fork; IDA:SGD.
GO; GO:0031298; C:replication fork protection complex; IDA:SGD.
GO; GO:0030466; P:chromatin silencing at silent mating-type cassette; IMP:SGD.
GO; GO:0006348; P:chromatin silencing at telomere; IMP:SGD.
GO; GO:0006281; P:DNA repair; IMP:SGD.
GO; GO:0006260; P:DNA replication; IMP:SGD.
GO; GO:0000076; P:DNA replication checkpoint; IMP:SGD.
GO; GO:0031573; P:intra-S DNA damage checkpoint; IMP:SGD.
GO; GO:0043570; P:maintenance of DNA repeat elements; IMP:SGD.
GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
GO; GO:0033262; P:regulation of nuclear cell cycle DNA replication; IMP:SGD.
GO; GO:0048478; P:replication fork protection; IMP:SGD.
GO; GO:0000723; P:telomere maintenance; IMP:SGD.
InterPro; IPR018564; Repl_chkpnt_MRC1_dom.
Pfam; PF09444; MRC1; 1.
1: Evidence at protein level;
Coiled coil; Complete proteome; DNA replication; Nucleus;
Phosphoprotein; Reference proteome.
CHAIN 1 1096 Mediator of replication checkpoint
protein 1.
/FTId=PRO_0000096574.
COILED 488 542 {ECO:0000255}.
COILED 652 716 {ECO:0000255}.
MOD_RES 144 144 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 409 409 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 411 411 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 605 605 Phosphoserine.
{ECO:0000244|PubMed:17287358,
ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 607 607 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 609 609 Phosphothreonine.
{ECO:0000244|PubMed:17287358}.
MOD_RES 801 801 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 807 807 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 911 911 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
CONFLICT 748 748 L -> V (in Ref. 5; CAA37945).
{ECO:0000305}.
CONFLICT 808 808 Missing (in Ref. 5; CAA37945).
{ECO:0000305}.
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


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