MMS1_YEAST
ID MMS1_YEAST Reviewed; 1407 AA.
AC Q06211; D6W4G5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=E3 ubiquitin-protein ligase linker protein MMS1;
DE AltName: Full=Methyl methanesulfonate-sensitivity protein 1;
DE AltName: Full=Regulator of Ty1 transposition protein 108;
DE AltName: Full=Synthetically lethal with MCM10 protein 6;
GN Name=MMS1; Synonyms=KIM3, RTT108, SLM6; OrderedLocusNames=YPR164W;
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=S288c / GRF88;
RA Xiao W.;
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 FUNCTION.
RX PubMed=11779788; DOI=10.1093/genetics/159.4.1449;
RA Scholes D.T., Banerjee M., Bowen B., Curcio M.J.;
RT "Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have
RT conserved roles in genome maintenance.";
RL Genetics 159:1449-1465(2001).
RN [5]
RP FUNCTION.
RX PubMed=11810260; DOI=10.1007/s00438-001-0605-x;
RA Hryciw T., Tang M., Fontanie T., Xiao W.;
RT "MMS1 protects against replication-dependent DNA damage in Saccharomyces
RT cerevisiae.";
RL Mol. Genet. Genomics 266:848-857(2002).
RN [6]
RP FUNCTION.
RX PubMed=12482937; DOI=10.1073/pnas.262669299;
RA Chang M., Bellaoui M., Boone C., Brown G.W.;
RT "A genome-wide screen for methyl methanesulfonate-sensitive mutants reveals
RT genes required for S phase progression in the presence of DNA damage.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16934-16939(2002).
RN [7]
RP FUNCTION.
RX PubMed=12694535; DOI=10.1046/j.1365-2443.2003.00648.x;
RA Araki Y., Kawasaki Y., Sasanuma H., Tye B.K., Sugino A.;
RT "Budding yeast mcm10/dna43 mutant requires a novel repair pathway for
RT viability.";
RL Genes Cells 8:465-480(2003).
RN [8]
RP FUNCTION.
RX PubMed=16024805; DOI=10.1128/mcb.25.15.6707-6721.2005;
RA Archambault V., Ikui A.E., Drapkin B.J., Cross F.R.;
RT "Disruption of mechanisms that prevent rereplication triggers a DNA damage
RT response.";
RL Mol. Cell. Biol. 25:6707-6721(2005).
RN [9]
RP FUNCTION.
RX PubMed=16121259; DOI=10.1371/journal.pgen.0010024;
RA Lee W., St Onge R.P., Proctor M., Flaherty P., Jordan M.I., Arkin A.P.,
RA Davis R.W., Nislow C., Giaever G.;
RT "Genome-wide requirements for resistance to functionally distinct DNA-
RT damaging agents.";
RL PLoS Genet. 1:235-246(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1294, AND IDENTIFICATION BY
RP 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 [11]
RP FUNCTION.
RX PubMed=18321796; DOI=10.1016/j.dnarep.2008.01.007;
RA Duro E., Vaisica J.A., Brown G.W., Rouse J.;
RT "Budding yeast Mms22 and Mms1 regulate homologous recombination induced by
RT replisome blockage.";
RL DNA Repair 7:811-818(2008).
RN [12]
RP FUNCTION, AND INTERACTION WITH RTT101; MMS22 AND CRT10.
RX PubMed=18704118; DOI=10.1038/embor.2008.155;
RA Zaidi I.W., Rabut G., Poveda A., Scheel H., Malmstrom J., Ulrich H.,
RA Hofmann K., Pasero P., Peter M., Luke B.;
RT "Rtt101 and Mms1 in budding yeast form a CUL4(DDB1)-like ubiquitin ligase
RT that promotes replication through damaged DNA.";
RL EMBO Rep. 9:1034-1040(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1294, 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).
RN [14]
RP FUNCTION.
RX PubMed=19390089; DOI=10.1101/gad.1775609;
RA Fujii K., Kitabatake M., Sakata T., Miyata A., Ohno M.;
RT "A role for ubiquitin in the clearance of nonfunctional rRNAs.";
RL Genes Dev. 23:963-974(2009).
RN [15]
RP INTERACTION WITH RTT101; MMS22; ESC2 AND ORC5.
RX PubMed=20139071; DOI=10.1074/jbc.m109.082107;
RA Mimura S., Yamaguchi T., Ishii S., Noro E., Katsura T., Obuse C.,
RA Kamura T.;
RT "Cul8/Rtt101 forms a variety of protein complexes that regulate DNA damage
RT response and transcriptional silencing.";
RL J. Biol. Chem. 285:9858-9867(2010).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21593207; DOI=10.1091/mbc.e10-10-0848;
RA Vaisica J.A., Baryshnikova A., Costanzo M., Boone C., Brown G.W.;
RT "Mms1 and Mms22 stabilize the replisome during replication stress.";
RL Mol. Biol. Cell 22:2396-2408(2011).
RN [17]
RP FUNCTION IN UBIQUITINATION OF H3.
RX PubMed=24209620; DOI=10.1016/j.cell.2013.10.014;
RA Han J., Zhang H., Zhang H., Wang Z., Zhou H., Zhang Z.;
RT "A Cul4 E3 ubiquitin ligase regulates histone hand-off during nucleosome
RT assembly.";
RL Cell 155:817-829(2013).
CC -!- FUNCTION: Component of multiple cullin-RING-based E3 ubiquitin-protein
CC ligase complexes (CRLs), which mediate the ubiquitination of target
CC proteins. The CRL associates with CDC34 as the E2 ubiquitin-conjugating
CC enzyme. The functional specificity of the CRL depends on the type of
CC the associated substrate receptor protein. RTT101(MMS1-MMS22) promotes
CC fork progression through damaged DNA or natural pause sites by
CC stabilizing replication proteins like the replication fork-pausing
CC complex (FPC) and leading-strand polymerase at stalled replication
CC forks. RTT101(MMS1-MMS22) ubiquitinates the acetylated histones
CC H3K56ac-H4 at lysine residues H3K121, H3K122 and H3K125. Ubiquitination
CC is required for efficient histone deposition during replication-coupled
CC nucleosome assembly, probably by facilitating the transfer of H3-H4
CC from ASF1 to other chaperones involved in histone deposition.
CC RTT101(MMS1-CRT10) may regulate nucleotide synthesis through
CC transcriptional regulation of ribonucleotide reductase. RTT101(MMS1) is
CC also involved in the non-functional rRNA decay (NRD) of 25S rRNA
CC through the selective, ubiquitination-dependent degradation of
CC nonfunctional ribosomal particles. Involved in the regulation of TY1
CC transposition. {ECO:0000269|PubMed:11779788,
CC ECO:0000269|PubMed:11810260, ECO:0000269|PubMed:12482937,
CC ECO:0000269|PubMed:12694535, ECO:0000269|PubMed:16024805,
CC ECO:0000269|PubMed:16121259, ECO:0000269|PubMed:18321796,
CC ECO:0000269|PubMed:18704118, ECO:0000269|PubMed:19390089,
CC ECO:0000269|PubMed:21593207, ECO:0000269|PubMed:24209620}.
CC -!- SUBUNIT: Component of multiple cullin-RING ligases (CRLs) composed of 4
CC subunits: the RING protein HRT1, the cullin RTT101, a linker protein
CC MMS1, and one of many alternative substrate receptors belonging to a
CC protein family described as DCAF (DDB1- and CUL4-associated factor).
CC Component of a RTT101(MMS1-MMS22) complex with the substrate receptor
CC MMS22. This complex further interacts with RTT107 and CTF4 to form
CC RTT101-MMS1-MMS22-RTT107 and RTT101-MMS1-MMS22-CTF4 complexes
CC respectively. Component of a RTT101(MSS1-CRT10) complex with the
CC substrate receptor CRT10. Component of a RTT101(MSS1-ESC2) complex with
CC the potential substrate receptor ESC2. Component of a RTT101(MSS1-ORC5)
CC complex with the potential substrate receptor ORC5. Interacts with
CC RTT101 (via N-ter). Interacts (via N-ter) with MMS22 (via C-ter).
CC Interacts with CRT10. {ECO:0000269|PubMed:18704118,
CC ECO:0000269|PubMed:20139071}.
CC -!- INTERACTION:
CC Q06211; Q06340: ESC2; NbExp=5; IntAct=EBI-38894, EBI-33799;
CC Q06211; Q08273: HRT1; NbExp=3; IntAct=EBI-38894, EBI-31686;
CC Q06211; Q06164: MMS22; NbExp=9; IntAct=EBI-38894, EBI-31156;
CC Q06211; P50874: ORC5; NbExp=4; IntAct=EBI-38894, EBI-12584;
CC Q06211; P47050: RTT101; NbExp=12; IntAct=EBI-38894, EBI-25861;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21593207}.
CC Note=Enriched on chromatin at sites where replication forks have
CC stalled.
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DR EMBL; U25840; AAB68151.1; -; Genomic_DNA.
DR EMBL; U14001; AAG02022.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11581.1; -; Genomic_DNA.
DR PIR; S59823; S59823.
DR RefSeq; NP_015490.1; NM_001184261.1.
DR AlphaFoldDB; Q06211; -.
DR SMR; Q06211; -.
DR BioGRID; 36337; 285.
DR ComplexPortal; CPX-1157; CUL8-MMS1-MMS22-ESC4 E3 ubiquitin ligase complex.
DR ComplexPortal; CPX-1165; CUL8-MMS1-MMS22-CTF4 E3 ubiquitin ligase complex.
DR ComplexPortal; CPX-1166; CUL8-MMS1-ESC2 E3 ubiquitin ligase complex.
DR ComplexPortal; CPX-1167; CUL8-MMS1-ORC5 E3 ubiquitin ligase complex.
DR DIP; DIP-6310N; -.
DR IntAct; Q06211; 10.
DR MINT; Q06211; -.
DR STRING; 4932.YPR164W; -.
DR iPTMnet; Q06211; -.
DR MaxQB; Q06211; -.
DR PaxDb; Q06211; -.
DR PRIDE; Q06211; -.
DR TopDownProteomics; Q06211; -.
DR EnsemblFungi; YPR164W_mRNA; YPR164W; YPR164W.
DR GeneID; 856293; -.
DR KEGG; sce:YPR164W; -.
DR SGD; S000006368; MMS1.
DR VEuPathDB; FungiDB:YPR164W; -.
DR eggNOG; ENOG502R4DC; Eukaryota.
DR HOGENOM; CLU_004250_0_0_1; -.
DR InParanoid; Q06211; -.
DR OMA; CKTIRHD; -.
DR BioCyc; YEAST:G3O-34293-MON; -.
DR PRO; PR:Q06211; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06211; protein.
DR GO; GO:0035361; C:Cul8-RING ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010526; P:negative regulation of transposition, RNA-mediated; IMP:SGD.
DR GO; GO:0070651; P:nonfunctional rRNA decay; IMP:SGD.
DR GO; GO:0006334; P:nucleosome assembly; IC:ComplexPortal.
DR GO; GO:0000725; P:recombinational repair; IMP:SGD.
DR GO; GO:0006275; P:regulation of DNA replication; IC:ComplexPortal.
DR GO; GO:0031297; P:replication fork processing; IMP:SGD.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; DNA damage; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1407
FT /note="E3 ubiquitin-protein ligase linker protein MMS1"
FT /id="PRO_0000257820"
FT REGION 1..600
FT /note="Required for interaction with MMS22"
FT MOD_RES 1294
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
SQ SEQUENCE 1407 AA; 161238 MW; CC698C422631A7D7 CRC64;
MLGLRTHGLD RYEHYIRRPS DFGKLELQDW LNHKSFRVSP NLLIDSSTTR EWNEPELFYQ
NTEDETWVRP CVGPKLEPSM MMLRYHDSNI GQMPQFCYPI SSPINFKPVL KYILQERSEL
SDGFPQKYNT LIGSLFDIDK NPETLDDSDI EALDDIEMSS DSGNVKEPKI ELQALEEIQQ
KHFSLIVSNN GIFQTGSTSI TYIQSGISGS IAIKPNNVAI LILLTQPSGH LLSILPLDDG
KETYLLQYWN LGQKGQWNII KHQNEKQFVL IHKELGICKF FEFHLPFTFQ LVNNLTLTDS
VIMNGSFFPT NYTDLDPYFI IFITAIRYER IVYFVIEWNN NEIKKKEVYQ LTVFDGEKTN
MTIPIGLNAC LVETPLKFSL VSANQIMSGE TEFHSFQLKA LKGIKSFFPA PLLLLKLQEL
HPHTFKKFQY CTIISSSTGN ICFCVTERST IVNGNLKFYE LTRFKGLKSI SPLPSNPINL
DSRSSSYVLV VISFSRTLEL TLSLEDLRCL DKKDVIKPLK NITFKHTIDS STEENSQILA
FTSSKFYNTH TGSNINDTRN SQVWLTSPNA ITQPCIDYKL RKTHQLIHLK QFQIFRHLRI
WKCKNLDIAL LQRLGINQSN TESSLIFATD AVSNNRIFLL DLTMTTTIDN DDPVQGLINI
EDLLCDTENE TILLNFTKNN LIQVTRDTIY IDPIGGDKEL RKISPGWEFE NVTYNDGILI
VWNAGLGCVS YIENIDAVDE SGALVSNLSS SKGMSKFFKQ LGTVTSVNFQ IKESTDDPTK
YDIWILLPDC VIRTPFSDWI SDSLDFSDVY ILSVQQALIN GPYFCSLDYE SYFEVHTLQN
NCFKKGSRCT SRVNFQGKDI KFRSFGVNQC LAFSAFEIFV INLTPIHDSR ELDFYKLKLP
HLGNNNSILE VCPDIENNQL FILYSDGLRI LELSYLTSNN GNFLLKSTRS KNKKFLYLDK
INRMLVLNQD LREWECIRLS DGKAVGLDSQ LLKDDSEEIL EIKELPIATE DNPLEKKTVL
LISFTSSLKL VLLTAAKNKI SNQIIDSYKL DNSRLLNHLV ITPRGEIFFL DYKVMGTDNE
MSFNKLKVTK HCIDQEERNN TTLRLTLETR FTFKSWSTVK TFTVVGDNII ATTNMGEKLY
LIKDFSSSSD ESRRVYPLEM YPDSKVQKII PLNECCFVVA AYCGNRNDLD SRLIFYSLPT
IKVGLNNETG SLPDEYGNGR VDDIFEVDFP EGFQFGTMAL YDVLHGERHV NRYSEGIRSE
NDEAEVALRQ RRNLLLFWRN HSSTPKPSLR RAATIVYEDH VSSRYFEDIS SILGSTAMRT
KRLSPYNAVA LDKPIQDISY DPAVQTLYVL MADQTIHKFG KDRLPCQDEY EPRWNSGYLV
SRRSIVKSDL ICEVGLWNLS DNCKNTV
