MMS22_YEAST
ID MMS22_YEAST Reviewed; 1454 AA.
AC Q06164; D6VYW3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=E3 ubiquitin-protein ligase substrate receptor MMS22;
DE AltName: Full=Methyl methanesulfonate-sensitivity protein 22;
DE AltName: Full=Synthetically lethal with MCM10 protein 2;
GN Name=MMS22; Synonyms=SLM2; OrderedLocusNames=YLR320W;
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=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 [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15718301; DOI=10.1093/nar/gki246;
RA Baldwin E.L., Berger A.C., Corbett A.H., Osheroff N.;
RT "Mms22p protects Saccharomyces cerevisiae from DNA damage induced by
RT topoisomerase II.";
RL Nucleic Acids Res. 33:1021-1030(2005).
RN [7]
RP INTERACTION WITH RTT107.
RX PubMed=16569515; DOI=10.1016/j.dnarep.2006.02.005;
RA Chin J.K., Bashkirov V.I., Heyer W.-D., Romesberg F.E.;
RT "Esc4/Rtt107 and the control of recombination during replication.";
RL DNA Repair 5:618-628(2006).
RN [8]
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 [9]
RP FUNCTION, INTERACTION WITH MMS1, AND IDENTIFICATION IN A COMPLEX WITH
RP RTT101.
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 [10]
RP INTERACTION WITH MMS1; RTT107 AND CTF4.
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 [11]
RP FUNCTION.
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 [12]
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: Substrate targeting component of a cullin-RING-based E3
CC ubiquitin-protein ligase complex RTT101(MMS1-MMS22). RTT101(MMS1-MMS22)
CC promotes 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 {ECO:0000269|PubMed:12482937, ECO:0000269|PubMed:12694535,
CC ECO:0000269|PubMed:15718301, ECO:0000269|PubMed:16024805,
CC ECO:0000269|PubMed:18321796, ECO:0000269|PubMed:18704118,
CC ECO:0000269|PubMed:21593207, ECO:0000269|PubMed:24209620}.
CC -!- SUBUNIT: Component of a cullin-RING ligase (CRL) composed of 4
CC subunits: the RING protein HRT1, the cullin RTT101, a linker protein
CC MMS1, and the substrate receptor MMS22. This complex further interacts
CC with RTT107 and CTF4 to form RTT101-MMS1-MMS22-RTT107 and RTT101-MMS1-
CC MMS22-CTF4 complexes respectively. Interacts (via C-ter) with MMS1 (via
CC N-ter). Interacts with RTT107. {ECO:0000269|PubMed:16569515,
CC ECO:0000269|PubMed:18704118, ECO:0000269|PubMed:20139071}.
CC -!- INTERACTION:
CC Q06164; Q01454: CTF4; NbExp=4; IntAct=EBI-31156, EBI-5209;
CC Q06164; Q06211: MMS1; NbExp=9; IntAct=EBI-31156, EBI-38894;
CC Q06164; P47050: RTT101; NbExp=11; IntAct=EBI-31156, EBI-25861;
CC Q06164; P38850: RTT107; NbExp=9; IntAct=EBI-31156, EBI-24788;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15718301}.
CC Note=Nuclear punctate foci structures.
CC -!- SIMILARITY: Belongs to the MMS22 family. {ECO:0000305}.
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DR EMBL; U20618; AAB64521.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09629.1; -; Genomic_DNA.
DR PIR; S53398; S53398.
DR RefSeq; NP_013424.1; NM_001182209.1.
DR PDB; 6J0X; X-ray; 2.31 A; E/F/G/H=22-37.
DR PDBsum; 6J0X; -.
DR AlphaFoldDB; Q06164; -.
DR SMR; Q06164; -.
DR BioGRID; 31584; 1075.
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 DIP; DIP-6567N; -.
DR IntAct; Q06164; 15.
DR MINT; Q06164; -.
DR STRING; 4932.YLR320W; -.
DR PaxDb; Q06164; -.
DR PRIDE; Q06164; -.
DR EnsemblFungi; YLR320W_mRNA; YLR320W; YLR320W.
DR GeneID; 851030; -.
DR KEGG; sce:YLR320W; -.
DR SGD; S000004312; MMS22.
DR VEuPathDB; FungiDB:YLR320W; -.
DR eggNOG; ENOG502R0S3; Eukaryota.
DR HOGENOM; CLU_251473_0_0_1; -.
DR InParanoid; Q06164; -.
DR OMA; KMPYSLD; -.
DR BioCyc; YEAST:G3O-32404-MON; -.
DR PRO; PR:Q06164; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06164; protein.
DR GO; GO:0035361; C:Cul8-RING ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:SGD.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0045144; P:meiotic sister chromatid segregation; IMP:SGD.
DR GO; GO:0006334; P:nucleosome assembly; IC:ComplexPortal.
DR GO; GO:0000725; P:recombinational repair; IMP:SGD.
DR GO; GO:0031297; P:replication fork processing; IMP:SGD.
DR InterPro; IPR019021; Mms22.
DR InterPro; IPR013220; Mms22_budding_yeast.
DR PANTHER; PTHR28122; PTHR28122; 4.
DR Pfam; PF09462; Mus7; 1.
DR PIRSF; PIRSF007808; MMS22; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; DNA damage; DNA repair; Nucleus;
KW Reference proteome.
FT CHAIN 1..1454
FT /note="E3 ubiquitin-protein ligase substrate receptor
FT MMS22"
FT /id="PRO_0000257821"
FT REGION 159..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1454
FT /note="Required for interaction with MMS1"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:6J0X"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:6J0X"
SQ SEQUENCE 1454 AA; 167683 MW; EE9797D4A12A7488 CRC64;
MDVDEPNPIV ISDSEATDEE ISIIYEPEFN ENYLWAEENV QEASRSQKIV TERLSLDSTA
GESCTPSVVT DTQVTTGLRW SLRKRKAIQK MPYSLERIKH RQLLEGYDIS SFDSISNQLT
LPKNASTVIH SNDILLTKRT GKPLDEQKDV TIDSIKPENS SVQSQRYDSD EEIPKKRHRT
FKDLDQDIVF QSGDSTEDEQ DLASTNLQNT QNDEVIFRGR VLNVRTGYRG VLPRVAWEKS
LQKQQSSKVT KRKTQLLNHK GVAKRKMNRS AHIEDEEQNL LNDLIAPDDE LDIEENAPPD
IYLGNLPEDR EANEKELKEL QEYYESKYSE DAQSAGTSGF NLNEEYRNEP VYELEYDGPG
SCISHVSYKD QPIIYLNSRH SDSGFSEQYN ISAEDNQSVI SLDAAEEHND GIIDKMLVKP
KRIKATNDAN FLNTKSKRVR RYKYKYRNSC LAPSTKAIKV GKRSAHKSHL AANNPVSFVS
KKNHVIDDYF FEELESQSLE QDDSSSLKPQ KKRRKKKAPI YSSFSADLES RRKPVFNTVV
EVPTNRYAFT KPNVRNRDSI NHDMEFEEED SNQELGPIMV VLDSILLKKP FEPPNFFKIQ
LSDKSFLLSK LNPADIATSL QKIFRVIIDK GITDTELVHF NESLIAFLVH LDMPELFDLI
GEFHREFRSK VNSLRKKAKP IHFFQIAACQ LMFLEISRYN KISAAAKFDM DVKLLDHIVS
FFKLLSVCYD SVMKNPMQYL YTSYYILSAV VDVIHKKEAL WDLFQKHPFS PHISLLLVNI
FPTKVCRWQV LRLDSEFQPL SSAFRFINYC IETCNWNVTN SLILSLDRIF KRRRFSDFEE
ESDLSQNNKI IYPPTNQLTS RLMFNRYLHL LTLCELSSSD TQRVIPMGDI SMNDSLSVLK
NRLNLLIVLA TRFDLNLEKR FQELTRPLYS KEYLNLHTQN TVRTITTLIM QASLSFLEIS
RIKNHPFSGK FIASLFDKLV LQQPSISGVT ENFLKEFTNL VSKMKRKSVS MLKFLYPSLV
AMSQENIFES SFFLLLQVYL KSLDVLGPTW VQNYLFQFIK SKAQENERWI ECYCQIGKFL
VDSGIFTWWT FFTYNGLDAA LHFQLAFHSL IIDFCDTDSF ELLKKPLYSI ASDLLLISKD
DAFYHFLSNL LKRAHIIVAD LKPVSDENEL LRLAYIFSKA LKKNAYQDLL AVFLSLAKKH
YDEGDISRNF LAKYLEFLNK NCLTELRNNQ LFISLRRELG ISSDEDEKCA FWDSFNEAGD
ILSKAAFVET GIVQACCTGN EIDGYLDNLS TLFTSTMLES PFAFFSDLVI AHIFENRPFF
DVNIKNFLLS HFIDLFNKVL KMKFEQVSPD EFAELCKVYR ALCIECATDD TFNSNSDLIA
AKDAFLVSVL RIADGFWEHD KLLQLRMLDS NMNIPNQIPH TTLQSSLSAI VIKIIESNIG
KIEASEPFKT FKNT
