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P25588 (MRC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mediator of replication checkpoint protein 1
Alternative name(s):
DNA replication checkpoint mediator MRC1
Gene names
Name:MRC1
Ordered Locus Names:YCL061C
ORF Names:YCL61C/YCL60C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length1096 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for normal DNA replication. Phosphorylated in response to DNA replication stress. Phosphorylation allows it to mediate the activation of RAD53. Ref.6 Ref.7

Subunit structure

Interacts with CDC45 in S phase. Ref.8

Subcellular location

Nucleus. Note: Associated with chromatin during S phase. Ref.7

Post-translational modification

Phosphorylated by MEC1 and RAD53. Ref.6 Ref.10 Ref.11 Ref.12 Ref.13

Miscellaneous

Present with 721 molecules/cell in log phase SD medium. Ref.9

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CDC45Q080323EBI-412442,EBI-4292

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10961096Mediator of replication checkpoint protein 1
PRO_0000096574

Regions

Coiled coil488 – 54255 Potential
Coiled coil652 – 71665 Potential

Amino acid modifications

Modified residue871Phosphoserine Ref.13
Modified residue1141Phosphoserine Ref.13
Modified residue1201Phosphoserine Ref.13
Modified residue1211Phosphoserine Ref.13
Modified residue1231Phosphothreonine Ref.13
Modified residue1441Phosphoserine Ref.13
Modified residue1641Phosphoserine Ref.13
Modified residue1841Phosphoserine Ref.13
Modified residue1891Phosphoserine Ref.13
Modified residue1911Phosphothreonine Ref.13
Modified residue2071Phosphoserine Ref.13
Modified residue2151Phosphoserine Ref.13
Modified residue2291Phosphoserine Ref.13
Modified residue3001Phosphoserine Ref.13
Modified residue3671Phosphoserine Ref.13
Modified residue3731Phosphothreonine Ref.13
Modified residue3881Phosphoserine Ref.13
Modified residue4111Phosphoserine
Modified residue4341Phosphoserine Ref.13
Modified residue4371Phosphoserine Ref.13
Modified residue5791Phosphoserine Ref.13
Modified residue5811Phosphoserine Ref.13
Modified residue6051Phosphoserine Ref.10 Ref.11 Ref.12 Ref.13
Modified residue6071Phosphoserine Ref.10 Ref.12 Ref.13
Modified residue6091Phosphothreonine Ref.11
Modified residue6221Phosphoserine Ref.12 Ref.13
Modified residue8011Phosphoserine Ref.13
Modified residue8071Phosphoserine Ref.13
Modified residue9111Phosphoserine Ref.13
Modified residue9181Phosphoserine Ref.13
Modified residue9201Phosphoserine Ref.13
Modified residue9321Phosphothreonine Ref.13
Modified residue9371Phosphoserine Ref.13
Modified residue9631Phosphothreonine Ref.13
Modified residue9651Phosphoserine Ref.13
Modified residue9691Phosphoserine Ref.13
Modified residue9971Phosphoserine Ref.13
Modified residue10061Phosphoserine Ref.13
Modified residue10931Phosphoserine Ref.13

Experimental info

Sequence conflict7481L → V in CAA37945. Ref.5
Sequence conflict8081Missing in CAA37945. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P25588 [UniParc].

Last modified September 19, 2003. Version 3.
Checksum: 378345EE503FFA81

FASTA1,096124,326
        10         20         30         40         50         60 
MDDALHALSS LTAKKRTTTY KKVAVPILDE NDNTNGNGPN DIDNPPELTG NGFLFANATL 

        70         80         90        100        110        120 
NRVKNRLEGK KAPEQNHNNG KDRSENSLPT QLISNLYDGG EELEKSEVKD NSYSEKNVSS 

       130        140        150        160        170        180 
SFTQTQRIPV SIQQDKVFNV PIHSVNDGKP TQLIKEDGLV NETSQALKTP LTTGRPGATQ 

       190        200        210        220        230        240 
RIDSSGATSQ TQPIKSIEPQ SQIITTSSNH SNALSPKIPI IPTELIGTSP LFQSIQNRGP 

       250        260        270        280        290        300 
DTQMDVPPQT AHDEDKTQAI GIPQATHQEQ KTQIDTVAQT LQDEVPHTLK IREIQSELAS 

       310        320        330        340        350        360 
EDSKREKARN VEYKKPQKPI PTKKFFSKES FLADFDDSSS NEDDDIKLEN AHPKPVQNDD 

       370        380        390        400        410        420 
ELHENKSVEL NLTDETRINE KRVPLLSSYA NNLKREIDSS KCITLDLDSD SDEYGDDDMD 

       430        440        450        460        470        480 
SIKLSKDESV LPISQLSKAT ILNLKARLSK QNQKLSQRPN KSKDPKVDHN VLLNTLRKAS 

       490        500        510        520        530        540 
RKQILDHQKE VIETKGLKLE DMAKEKEIVE NLLEQEILRN KRIRQKEKRR EKLEENDFQL 

       550        560        570        580        590        600 
NAHDSGSDSG SESSGFALSG NEIADYESSG SENDNRRESD SEKEDDEIIL KQKKSHHVKH 

       610        620        630        640        650        660 
IINESDSDTE VEAKPKEKAD ESLPKRIAIN LGHYGDNIGE DTDKFQETNV LDTQNIEEVM 

       670        680        690        700        710        720 
AERNTIENEV KDDVYVNEEA DEAIRRQLID KEKLQLKQKE KEHEAKIKEL KKRGVTNFFE 

       730        740        750        760        770        780 
MEAEESEDEW HGIGGADGEG SDDYDSDLEK MIDDYSKNNF NPHEIREMLA AENKEMDIKM 

       790        800        810        820        830        840 
INKILYDIKN GGFRNKRAKN SLELELSDDD EDDVLQQYRL KRRELMRKRR LEIGDDAKLV 

       850        860        870        880        890        900 
KNPKSSAFFE SMVEDIIEYK NPFGAEEEYN LDITSTATDL DTQDNSINVG DNTGNNEQKP 

       910        920        930        940        950        960 
VDQKNKKVII SEDFVQKSLS FLKSNNYEDF ETDKELSRIQ HGNDEAIEDL YTLKQNSSIK 

       970        980        990       1000       1010       1020 
SFTNSQTDST TSKTVNTIID LEKRPEDEDE VENGDTSLVG VFKHPSIIKS FASRTDINDK 

      1030       1040       1050       1060       1070       1080 
FKEGNKTVKI LKSYKTVGSS KASITYMGKT RKLIAPKRKT EGSHRYHHDH HNKKMKMKTK 

      1090 
TKSNKLFESG QDSFDN

« Hide

References

« Hide 'large scale' references
[1]"The complete DNA sequence of yeast chromosome III."
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. expand/collapse author list , 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.
Nature 357:38-46(1992) [PubMed: 1574125] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Gromadka R.
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]Valles G., Volckaerts G.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"The URK1 gene of Saccharomyces cerevisiae encoding uridine kinase."
Kern L.
Nucleic Acids Res. 18:5279-5279(1990) [PubMed: 2169608] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 660-839.
Strain: ATCC 28383 / FL100 / VTT C-80102.
[6]"Mrc1 transduces signals of DNA replication stress to activate Rad53."
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.
Nat. Cell Biol. 3:958-965(2001) [PubMed: 11715016] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION.
[7]"Mrc1 is a replication fork component whose phosphorylation in response to DNA replication stress activates Rad53."
Osborn A.J., Elledge S.J.
Genes Dev. 17:1755-1767(2003) [PubMed: 12865299] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"S-phase checkpoint proteins Tof1 and Mrc1 form a stable replication-pausing complex."
Katou Y., Kanoh Y., Bando M., Noguchi H., Tanaka H., Ashikari T., Sugimoto K., Shirahige K.
Nature 424:1078-1083(2003) [PubMed: 12944972] [Abstract]
Cited for: INTERACTION WITH CDC45.
[9]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605 AND SER-607, MASS SPECTROMETRY.
Strain: ADR376.
[11]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
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.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605 AND THR-609, MASS SPECTROMETRY.
[12]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605; SER-607 AND SER-622, MASS SPECTROMETRY.
[13]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-114; SER-120; SER-121; THR-123; SER-144; SER-164; SER-184; SER-189; THR-191; SER-207; SER-215; SER-229; SER-300; SER-367; THR-373; SER-388; SER-434; SER-437; SER-579; SER-581; SER-605; SER-607; SER-622; SER-801; SER-807; SER-911; SER-918; SER-920; THR-932; SER-937; THR-963; SER-965; SER-969; SER-997; SER-1006 AND SER-1093, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X59720 Genomic DNA. Translation: CAC42953.1.
X53998 Genomic DNA. Translation: CAA37945.1.
BK006937 Genomic DNA. Translation: DAA07425.1.
PIRS74279.
RefSeqNP_009871.2. NM_001178704.1.

3D structure databases

ProteinModelPortalP25588.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1017N.
IntActP25588. 13 interactions.
MINTMINT-2732058.
STRINGP25588.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCL061C; YCL061C; YCL061C.
GeneID850297.
KEGGsce:YCL061C.
NMPDRfig|4932.3.peg.589.

Organism-specific databases

CYGDYCL061c.
SGDS000000566. MRC1.

Phylogenomic databases

eggNOGfuNOG08021.
GeneTreeEFGT00050000000138.
OMADSEVEKM.
OrthoDBEOG4WDHM4.

Gene expression databases

ArrayExpressP25588.
GenevestigatorP25588.
GermOnlineYCL061C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR018564. Repl_chkpnt_MRC1_dom.
[Graphical view]
KOK11272.
PfamPF09444. MRC1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio965670.

Entry information

Entry nameMRC1_YEAST
AccessionPrimary (citable) accession number: P25588
Secondary accession number(s): D6VQV6 expand/collapse secondary AC list , P25589, P27513, P87003, Q07218, Q8NIN2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: September 19, 2003
Last modified: December 14, 2011
This is version 92 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

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