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 24-JUL-2013, entry version 83. DE RecName: 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 204511 / S288c / AB972; 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; RG Saccharomyces Genome Database; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. 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). CC -!- FUNCTION: With MMS1, involved in protection against replication- CC dependent DNA damage. May act by restoring active replication CC forks, repairing unusual DNA structures, and/or preventing CC aberrant DNA rearrangement at arrested replication forks. CC -!- SUBUNIT: Interacts with RTT107. CC -!- INTERACTION: CC P20449:DBP5; NbExp=1; IntAct=EBI-31156, EBI-5617; CC P36156:ECM4; NbExp=1; IntAct=EBI-31156, EBI-2042717; CC P39005:KRE9; NbExp=1; IntAct=EBI-31156, EBI-9930; CC P38799:YHR078W; NbExp=1; IntAct=EBI-31156, EBI-24593; CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Nuclear punctate foci CC structures. CC -!- SIMILARITY: Belongs to the MMS22 family. 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 ProteinModelPortal; Q06164; -. DR DIP; DIP-6567N; -. DR IntAct; Q06164; 5. DR MINT; MINT-683733; -. DR STRING; 4932.YLR320W; -. DR PaxDb; Q06164; -. DR EnsemblFungi; YLR320W; YLR320W; YLR320W. DR GeneID; 851030; -. DR KEGG; sce:YLR320W; -. DR CYGD; YLR320w; -. DR SGD; S000004312; MMS22. DR eggNOG; NOG44623; -. DR OMA; IQKMPYS; -. DR OrthoDB; EOG43R6W7; -. DR BioCyc; YEAST:G3O-32404-MONOMER; -. DR NextBio; 967616; -. DR Genevestigator; Q06164; -. DR GO; GO:0035361; C:Cul8-RING ubiquitin ligase complex; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0006302; P:double-strand break repair; IMP:SGD. 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; MeCH4sulfonate_sens_MMS22. DR InterPro; IPR013220; MMS22_budding_yeast. DR Pfam; PF09462; Mus7; 1. DR PIRSF; PIRSF007808; MMS22; 1. PE 1: Evidence at protein level; KW Complete proteome; DNA damage; DNA repair; Nucleus; KW Reference proteome. FT CHAIN 1 1454 Methyl methanesulfonate-sensitivity FT protein 22. FT /FTId=PRO_0000257821. 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 //