MEC3_YEAST
ID MEC3_YEAST Reviewed; 474 AA.
AC Q02574; D6VYT4; P87260; Q05887;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=DNA damage checkpoint control protein MEC3;
GN Name=MEC3; Synonyms=PIP3, PSO9; OrderedLocusNames=YLR288C;
GN ORFNames=L8003.15;
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=7491494; DOI=10.1126/science.270.5241.1488;
RA Lydall D., Weinert T.A.;
RT "Yeast checkpoint genes in DNA damage processing: implications for repair
RT and arrest.";
RL Science 270:1488-1491(1995).
RN [2]
RP SEQUENCE REVISION TO 27; 411; 415-222 AND 454.
RA Lydall D., Weinert T.A.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 INTERACTION WITH DDC1.
RX PubMed=9670034; DOI=10.1093/emboj/17.14.4199;
RA Paciotti V., Lucchini G., Plevani P., Longhese M.P.;
RT "Mec1p is essential for phosphorylation of the yeast DNA damage checkpoint
RT protein Ddc1p, which physically interacts with Mec3p.";
RL EMBO J. 17:4199-4209(1998).
RN [6]
RP IDENTIFICATION IN THE CHECKPOINT CLAMP COMPLEX, AND FUNCTION OF THE
RP CHECKPOINT CLAMP COMPLEX.
RX PubMed=9891048; DOI=10.1128/mcb.19.2.1136;
RA Kondo T., Matsumoto K., Sugimoto K.;
RT "Role of a complex containing Rad17, Mec3, and Ddc1 in the yeast DNA damage
RT checkpoint pathway.";
RL Mol. Cell. Biol. 19:1136-1143(1999).
RN [7]
RP FUNCTION, AND INTERACTION WITH SET1.
RX PubMed=9988274; DOI=10.1038/5991;
RA Corda Y., Schramke V., Longhese M.P., Smokvina T., Paciotti V., Brevet V.,
RA Gilson E., Geli V.;
RT "Interaction between Set1p and checkpoint protein Mec3p in DNA repair and
RT telomere functions.";
RL Nat. Genet. 21:204-208(1999).
RN [8]
RP FUNCTION OF THE CHECKPOINT CLAMP COMPLEX.
RX PubMed=12271137; DOI=10.1073/pnas.202463999;
RA Giannattasio M., Sommariva E., Vercillo R., Lippi-Boncambi F., Liberi G.,
RA Foiani M., Plevani P., Muzi-Falconi M.;
RT "A dominant-negative MEC3 mutant uncovers new functions for the Rad17
RT complex and Tel1.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12997-13002(2002).
RN [9]
RP IDENTIFICATION IN THE CHECKPOINT CLAMP COMPLEX, AND FUNCTION OF THE
RP CHECKPOINT CLAMP COMPLEX.
RX PubMed=12672803; DOI=10.1074/jbc.m301260200;
RA Giannattasio M., Sabbioneda S., Minuzzo M., Plevani P., Muzi-Falconi M.;
RT "Correlation between checkpoint activation and in vivo assembly of the
RT yeast checkpoint complex Rad17-Mec3-Ddc1.";
RL J. Biol. Chem. 278:22303-22308(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 INTERACTION OF THE CHECKPOINT CLAMP COMPLEX WITH THE RFC-RAD24 CHECKPOINT
RP CLAMP LOADER COMPLEX, AND FUNCTION OF THE CHECKPOINT CLAMP COMPLEX.
RX PubMed=12604797; DOI=10.1073/pnas.0437148100;
RA Majka J., Burgers P.M.J.;
RT "Yeast Rad17/Mec3/Ddc1: a sliding clamp for the DNA damage checkpoint.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2249-2254(2003).
RN [12]
RP INTERACTION OF THE CHECKPOINT CLAMP COMPLEX WITH THE RFC-RAD24 CHECKPOINT
RP CLAMP LOADER COMPLEX.
RX PubMed=15014082; DOI=10.1074/jbc.m400898200;
RA Majka J., Chung B.Y., Burgers P.M.J.;
RT "Requirement for ATP by the DNA damage checkpoint clamp loader.";
RL J. Biol. Chem. 279:20921-20926(2004).
RN [13]
RP IDENTIFICATION IN THE CHECKPOINT CLAMP COMPLEX, AND FUNCTION OF THE
RP CHECKPOINT CLAMP COMPLEX.
RX PubMed=16137930; DOI=10.1016/j.dnarep.2005.07.008;
RA Majka J., Burgers P.M.J.;
RT "Function of Rad17/Mec3/Ddc1 and its partial complexes in the DNA damage
RT checkpoint.";
RL DNA Repair 4:1189-1194(2005).
RN [14]
RP INTERACTION WITH REV7, AND FUNCTION OF THE CHECKPOINT CLAMP COMPLEX.
RX PubMed=16169844; DOI=10.1074/jbc.m507638200;
RA Sabbioneda S., Minesinger B.K., Giannattasio M., Plevani P.,
RA Muzi-Falconi M., Jinks-Robertson S.;
RT "The 9-1-1 checkpoint clamp physically interacts with polzeta and is
RT partially required for spontaneous polzeta-dependent mutagenesis in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:38657-38665(2005).
RN [15]
RP FUNCTION, AND INTERACTION WITH DDC1 AND RAD17.
RX PubMed=16202664; DOI=10.1016/j.dnarep.2005.08.018;
RA Cardone J.M., Revers L.F., Machado R.M., Bonatto D., Brendel M.,
RA Henriques J.A.P.;
RT "Psoralen-sensitive mutant pso9-1 of Saccharomyces cerevisiae contains a
RT mutant allele of the DNA damage checkpoint gene MEC3.";
RL DNA Repair 5:163-171(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Component of the checkpoint clamp complex involved in the
CC surveillance mechanism that allows the DNA repair pathways to act to
CC restore the integrity of the DNA prior to DNA synthesis or separation
CC of the replicated chromosomes. Associates with sites of DNA damage and
CC modulates the MEC1 signaling pathway and the activation of RAD53 in
CC response to DNA damage at phase G1. The complex also physically
CC regulates DNA polymerase zeta-dependent mutagenesis by controlling the
CC access of polymerase zeta to damaged DNA. {ECO:0000269|PubMed:12271137,
CC ECO:0000269|PubMed:12604797, ECO:0000269|PubMed:12672803,
CC ECO:0000269|PubMed:16137930, ECO:0000269|PubMed:16169844,
CC ECO:0000269|PubMed:16202664, ECO:0000269|PubMed:9891048,
CC ECO:0000269|PubMed:9988274}.
CC -!- SUBUNIT: Component of the checkpoint clamp complex composed of DDC1,
CC MEC3 and RAD17. The interaction with MEC3 is performed in a RAD17-
CC dependent manner. The checkpoint clamp complex loads onto DNA.
CC Interacts with the DNA polymerase zeta subunit REV7. Forms also a
CC heterotrimer with 2 RAD17 subunits. Interacts with SET1.
CC {ECO:0000269|PubMed:12604797, ECO:0000269|PubMed:12672803,
CC ECO:0000269|PubMed:15014082, ECO:0000269|PubMed:16137930,
CC ECO:0000269|PubMed:16169844, ECO:0000269|PubMed:16202664,
CC ECO:0000269|PubMed:9670034, ECO:0000269|PubMed:9891048,
CC ECO:0000269|PubMed:9988274}.
CC -!- INTERACTION:
CC Q02574; Q08949: DDC1; NbExp=5; IntAct=EBI-10658, EBI-30769;
CC Q02574; P48581: RAD17; NbExp=11; IntAct=EBI-10658, EBI-14652;
CC Q02574; P38927: REV7; NbExp=3; IntAct=EBI-10658, EBI-14960;
CC Q02574; P38827: SET1; NbExp=3; IntAct=EBI-10658, EBI-16977;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 414 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MEC3 family. {ECO:0000305}.
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DR EMBL; U30906; AAB61448.1; -; Genomic_DNA.
DR EMBL; U17243; AAB67334.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09600.1; -; Genomic_DNA.
DR PIR; S50373; S50373.
DR RefSeq; NP_013391.1; NM_001182176.1.
DR PDB; 7ST9; EM; 2.20 A; H=1-474.
DR PDB; 7STB; EM; 2.72 A; H=1-474.
DR PDBsum; 7ST9; -.
DR PDBsum; 7STB; -.
DR AlphaFoldDB; Q02574; -.
DR BioGRID; 31554; 170.
DR ComplexPortal; CPX-1806; Rad17-Mec3-Ddc1 checkpoint clamp complex.
DR DIP; DIP-1432N; -.
DR IntAct; Q02574; 26.
DR MINT; Q02574; -.
DR STRING; 4932.YLR288C; -.
DR iPTMnet; Q02574; -.
DR MaxQB; Q02574; -.
DR PaxDb; Q02574; -.
DR EnsemblFungi; YLR288C_mRNA; YLR288C; YLR288C.
DR GeneID; 850995; -.
DR KEGG; sce:YLR288C; -.
DR SGD; S000004279; MEC3.
DR VEuPathDB; FungiDB:YLR288C; -.
DR eggNOG; ENOG502RA7D; Eukaryota.
DR HOGENOM; CLU_597417_0_0_1; -.
DR InParanoid; Q02574; -.
DR OMA; EPQVWCK; -.
DR BioCyc; YEAST:G3O-32383-MON; -.
DR Reactome; R-SCE-176187; Activation of ATR in response to replication stress.
DR PRO; PR:Q02574; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q02574; protein.
DR GO; GO:0030896; C:checkpoint clamp complex; IDA:SGD.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IDA:ComplexPortal.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0044778; P:meiotic DNA integrity checkpoint signaling; IBA:GO_Central.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IBA:GO_Central.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR GO; GO:0000722; P:telomere maintenance via recombination; IGI:SGD.
DR InterPro; IPR007150; Hus1/Mec3.
DR Pfam; PF04005; Hus1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; DNA damage; DNA repair; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..474
FT /note="DNA damage checkpoint control protein MEC3"
FT /id="PRO_0000096344"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 120
FT /note="T -> I (in Ref. 1; AAB61448)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="N -> D (in Ref. 1; AAB61448)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="D -> E (in Ref. 1; AAB61448)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 53146 MW; 4385CEFA9130FEA3 CRC64;
MKLKLIVNGC EAPDDYKLLR TTINTVASLR KTAILRFNSE RLTIISTPKS SLNSSNNGTI
LRGDTGQLWC TIPHDVFRLY TVISARELNT ITMECNCDSL LSVFKRYDRV MNQGSSSNMT
IKLQSMPEWN TNNGTLSGGT AGGVDTTSKP NPICALGITF EEIVHTSGPN DAIVMNGGVD
EHNGLPTTVG TGNLLASNKV IMHSFKVPVK LLFRAQDTRI QEPMINYIQL MMYKLPPISG
EFGSAFHGFI RRVERYSNVN HIHLMGVKKK EHGNEGDDVE LKIIVNELDW HLEICWNGPL
DSVIQRQEGL TDNPSQNQHI DTDGRQEEGS LPIIEADKPM SSLYTNTRDR EMEENIRYDE
DLLRIEDSSI ADTRGNIYTA DTSGDTEFND ISVMVEKAEQ ESSSTHEVII RCKDWKVCSK
LYAAFEEVVL AISHDESCVF HCSLDRGSLE DSEDVEKPRE RGQIIYYIAR SKGL
