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 22-APR-2020, entry version 133. 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}. 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 PDB; 6J0X; X-ray; 2.31 A; E/F/G/H=22-37. DR PDBsum; 6J0X; -. DR SMR; Q06164; -. DR BioGrid; 31584; 1074. 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 EuPathDB; FungiDB:YLR320W; -. DR SGD; S000004312; MMS22. DR HOGENOM; CLU_251473_0_0_1; -. DR InParanoid; Q06164; -. DR OMA; IHFYQIA; -. DR BioCyc; YEAST:G3O-32404-MONOMER; -. 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: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 1201..1454 FT /note="Required for interaction with MMS1" FT STRAND 23..25 FT /evidence="ECO:0000244|PDB:6J0X" FT HELIX 33..35 FT /evidence="ECO:0000244|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 //