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-JUL-2019, entry version 127. 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; OC Saccharomycetes; 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., RA Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., RA Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., RA Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., RA Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., RA Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., RA Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., RA Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., RA Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., RA Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., RA Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., RA 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., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT 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 RT reveals genes required for S phase progression in the presence of DNA RT 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 RT damage 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 RT induced by 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 RT ligase 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 RT damage 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 RT nucleosome 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- CC MMS22) promotes fork progression through damaged DNA or natural CC pause sites by stabilizing replication proteins like the CC replication fork-pausing complex (FPC) and leading-strand CC polymerase at stalled replication forks. RTT101(MMS1-MMS22) CC ubiquitinates the acetylated histones H3K56ac-H4 at lysine CC residues H3K121, H3K122 and H3K125. Ubiquitination is required for CC efficient histone deposition during replication-coupled nucleosome CC assembly, probably by facilitating the transfer of H3-H4 from ASF1 CC 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 CC protein MMS1, and the substrate receptor MMS22. This complex CC further interacts with RTT107 and CTF4 to form RTT101-MMS1-MMS22- CC RTT107 and RTT101-MMS1-MMS22-CTF4 complexes respectively. CC Interacts (via C-ter) with MMS1 (via N-ter). Interacts with CC RTT107. {ECO:0000269|PubMed:16569515, ECO:0000269|PubMed:18704118, CC ECO:0000269|PubMed:20139071}. CC -!- INTERACTION: CC Q01454:CTF4; NbExp=4; IntAct=EBI-31156, EBI-5209; CC Q06211:MMS1; NbExp=9; IntAct=EBI-31156, EBI-38894; CC P47050:RTT101; NbExp=11; IntAct=EBI-31156, EBI-25861; CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; Q06164; -. DR BioGrid; 31584; 1071. 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_mRNA; YLR320W. DR GeneID; 851030; -. DR KEGG; sce:YLR320W; -. DR EuPathDB; FungiDB:YLR320W; -. DR SGD; S000004312; MMS22. DR InParanoid; Q06164; -. DR OMA; IHFYQIA; -. DR BioCyc; YEAST:G3O-32404-MONOMER; -. DR PRO; PR:Q06164; -. DR Proteomes; UP000002311; Chromosome XII. 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: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 Cell cycle; Cell division; Complete proteome; DNA damage; DNA repair; KW Nucleus; Reference proteome. FT CHAIN 1 1454 E3 ubiquitin-protein ligase substrate FT receptor MMS22. FT /FTId=PRO_0000257821. FT REGION 1201 1454 Required for interaction with MMS1. 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 //