ID   MMS2_YEAST              Reviewed;         137 AA.
AC   P53152; D6VU57;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 200.
DE   RecName: Full=Ubiquitin-conjugating enzyme variant MMS2;
DE            Short=UEV MMS2;
GN   Name=MMS2; OrderedLocusNames=YGL087C;
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], AND CHARACTERIZATION.
RX   PubMed=9576943; DOI=10.1073/pnas.95.10.5678;
RA   Broomfield S., Chow B.L., Xiao W.;
RT   "MMS2, encoding a ubiquitin-conjugating-enzyme-like protein, is a member of
RT   the yeast error-free postreplication repair pathway.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:5678-5683(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9290212;
RX   DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA   Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT   "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT   chromosome VII.";
RL   Yeast 13:1077-1090(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869; DOI=10.1038/387s081;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [4]
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   [5]
RP   CHARACTERIZATION.
RX   PubMed=9705497; DOI=10.1093/nar/26.17.3908;
RA   Xiao W., Lin S.L., Broomfield S., Chow B.L., Wei Y.-F.;
RT   "The products of the yeast MMS2 and two human homologs (hMMS2 and CROC-1)
RT   define a structurally and functionally conserved Ubc-like protein family.";
RL   Nucleic Acids Res. 26:3908-3914(1998).
RN   [6]
RP   CHARACTERIZATION.
RX   PubMed=10089880; DOI=10.1016/s0092-8674(00)80575-9;
RA   Hofmann R.M., Pickart C.M.;
RT   "Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in
RT   assembly of novel polyubiquitin chains for DNA repair.";
RL   Cell 96:645-653(1999).
RN   [7]
RP   FUNCTION, INTERACTION WITH UBC13, AND SUBCELLULAR LOCATION.
RX   PubMed=10880451; DOI=10.1093/emboj/19.13.3388;
RA   Ulrich H.D., Jentsch S.;
RT   "Two RING finger proteins mediate cooperation between ubiquitin-conjugating
RT   enzymes in DNA repair.";
RL   EMBO J. 19:3388-3397(2000).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, 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   [10]
RP   FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RX   PubMed=25690888; DOI=10.1093/nar/gkv004;
RA   Choi K., Batke S., Szakal B., Lowther J., Hao F., Sarangi P., Branzei D.,
RA   Ulrich H.D., Zhao X.;
RT   "Concerted and differential actions of two enzymatic domains underlie Rad5
RT   contributions to DNA damage tolerance.";
RL   Nucleic Acids Res. 43:2666-2677(2015).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH UBC13, AND
RP   MUTAGENESIS OF PHE-8.
RX   PubMed=11440714; DOI=10.1016/s0092-8674(01)00387-7;
RA   VanDemark A.P., Hofmann R.M., Tsui C., Pickart C.M., Wolberger C.;
RT   "Molecular insights into polyubiquitin chain assembly: crystal structure of
RT   the Mms2/Ubc13 heterodimer.";
RL   Cell 105:711-720(2001).
CC   -!- FUNCTION: Promotes the template-switching (TS) branch of the DNA damage
CC       tolerance (DDT) pathway (also known as the post-replication repair
CC       (PRR) pathway), that bypasses replication-blocking lesions without
CC       removing them (PubMed:10880451). Together with ubiquitin-protein ligase
CC       RAD5 and ubiquitin-conjugating enzyme UBC13, synthesizes 'Lys-63'-
CC       linked polyubiquitin chains on monoubiquitinated POL30/PCNA, to promote
CC       template-switching to the newly synthesized sister chromatid for error-
CC       free synthesis past the DNA lesion (PubMed:10880451, PubMed:25690888).
CC       {ECO:0000269|PubMed:10880451, ECO:0000269|PubMed:25690888}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000269|PubMed:25690888}.
CC   -!- SUBUNIT: Heterodimer with UBC13. {ECO:0000269|PubMed:10880451,
CC       ECO:0000269|PubMed:11440714}.
CC   -!- INTERACTION:
CC       P53152; P52490: UBC13; NbExp=10; IntAct=EBI-11035, EBI-19777;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10880451}.
CC       Nucleus {ECO:0000269|PubMed:10880451}. Note=Localizes to the nucleus
CC       upon DNA damage. {ECO:0000269|PubMed:10880451}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes polyubiqitination of POL30/PCNA.
CC       {ECO:0000269|PubMed:25690888}.
CC   -!- MISCELLANEOUS: Present with 2760 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; U66724; AAC24241.1; -; Genomic_DNA.
DR   EMBL; Z72609; CAA96792.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08018.1; -; Genomic_DNA.
DR   PIR; S64094; S64094.
DR   RefSeq; NP_011428.1; NM_001180952.1.
DR   PDB; 1JAT; X-ray; 1.60 A; B=1-137.
DR   PDB; 2GMI; X-ray; 2.50 A; B=1-137.
DR   PDB; 5OJW; X-ray; 2.00 A; B=1-137.
DR   AlphaFoldDB; P53152; -.
DR   SMR; P53152; -.
DR   BioGRID; 33163; 279.
DR   ComplexPortal; CPX-2541; MMS2-UBC13 ubiquitin ligase complex.
DR   DIP; DIP-5829N; -.
DR   FunCoup; P53152; 1340.
DR   IntAct; P53152; 12.
DR   MINT; P53152; -.
DR   STRING; 4932.YGL087C; -.
DR   iPTMnet; P53152; -.
DR   PaxDb; 4932-YGL087C; -.
DR   PeptideAtlas; P53152; -.
DR   EnsemblFungi; YGL087C_mRNA; YGL087C; YGL087C.
DR   GeneID; 852793; -.
DR   KEGG; sce:YGL087C; -.
DR   AGR; SGD:S000003055; -.
DR   SGD; S000003055; MMS2.
DR   VEuPathDB; FungiDB:YGL087C; -.
DR   eggNOG; KOG0896; Eukaryota.
DR   HOGENOM; CLU_063065_4_0_1; -.
DR   InParanoid; P53152; -.
DR   OMA; GPESCSY; -.
DR   OrthoDB; 6508832at2759; -.
DR   BioCyc; YEAST:G3O-30588-MONOMER; -.
DR   Reactome; R-SCE-9646399; Aggrephagy.
DR   Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 852793; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P53152; -.
DR   PRO; PR:P53152; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53152; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0031371; C:ubiquitin conjugating enzyme complex; IPI:SGD.
DR   GO; GO:0006301; P:DNA damage tolerance; IMP:SGD.
DR   GO; GO:0010994; P:free ubiquitin chain polymerization; IDA:SGD.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IDA:SGD.
DR   GO; GO:0044395; P:protein targeting to vacuolar membrane; IMP:SGD.
DR   CDD; cd23807; UEV_UBE2V; 1.
DR   FunFam; 3.10.110.10:FF:000026; Ubiquitin-conjugating enzyme E2 variant; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBC.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24068; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS50127; UBC_2; 1.
DR   PDBsum; 1JAT; -.
DR   PDBsum; 2GMI; -.
DR   PDBsum; 5OJW; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; DNA damage; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..137
FT                   /note="Ubiquitin-conjugating enzyme variant MMS2"
FT                   /id="PRO_0000082598"
FT   DOMAIN          5..137
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   MOD_RES         71
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MUTAGEN         8
FT                   /note="F->A: Strongly reduces UBC13 binding and interferes
FT                   with error-free DNA repair."
FT                   /evidence="ECO:0000269|PubMed:11440714"
FT   HELIX           6..18
FT                   /evidence="ECO:0007829|PDB:1JAT"
FT   STRAND          26..32
FT                   /evidence="ECO:0007829|PDB:1JAT"
FT   STRAND          40..46
FT                   /evidence="ECO:0007829|PDB:1JAT"
FT   STRAND          49..51
FT                   /evidence="ECO:0007829|PDB:1JAT"
FT   TURN            52..55
FT                   /evidence="ECO:0007829|PDB:1JAT"
FT   STRAND          57..63
FT                   /evidence="ECO:0007829|PDB:1JAT"
FT   TURN            66..70
FT                   /evidence="ECO:0007829|PDB:1JAT"
FT   STRAND          74..79
FT                   /evidence="ECO:0007829|PDB:1JAT"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:2GMI"
FT   TURN            88..90
FT                   /evidence="ECO:0007829|PDB:1JAT"
FT   HELIX           98..101
FT                   /evidence="ECO:0007829|PDB:1JAT"
FT   HELIX           109..120
FT                   /evidence="ECO:0007829|PDB:1JAT"
FT   HELIX           123..126
FT                   /evidence="ECO:0007829|PDB:1JAT"
SQ   SEQUENCE   137 AA;  15545 MW;  E1DA713C94378795 CRC64;
     MSKVPRNFRL LEELEKGEKG FGPESCSYGL ADSDDITMTK WNGTILGPPH SNHENRIYSL
     SIDCGPNYPD SPPKVTFISK INLPCVNPTT GEVQTDFHTL RDWKRAYTME TLLLDLRKEM
     ATPANKKLRQ PKEGETF
//