MMS2_YEAST
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 03-AUG-2022, entry version 182.
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;
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 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 [8]
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 [9]
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: Has a role in the DNA error-free postreplication repair (PRR)
CC pathway. Lacks catalytic activity by itself. The UBC13/MMS2 heterodimer
CC catalyzes the synthesis of non-canonical poly-ubiquitin chains that are
CC linked through 'Lys-63'.
CC -!- SUBUNIT: Heterodimer with UBC13. {ECO:0000269|PubMed:11440714}.
CC -!- INTERACTION:
CC P53152; P52490: UBC13; NbExp=10; IntAct=EBI-11035, EBI-19777;
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 PDBsum; 1JAT; -.
DR PDBsum; 2GMI; -.
DR PDBsum; 5OJW; -.
DR AlphaFoldDB; P53152; -.
DR SMR; P53152; -.
DR BioGRID; 33163; 270.
DR ComplexPortal; CPX-2541; MMS2-UBC13 ubiquitin ligase complex.
DR DIP; DIP-5829N; -.
DR IntAct; P53152; 10.
DR MINT; P53152; -.
DR STRING; 4932.YGL087C; -.
DR iPTMnet; P53152; -.
DR MaxQB; P53152; -.
DR PaxDb; P53152; -.
DR PRIDE; P53152; -.
DR EnsemblFungi; YGL087C_mRNA; YGL087C; YGL087C.
DR GeneID; 852793; -.
DR KEGG; sce:YGL087C; -.
DR SGD; S000003055; MMS2.
DR VEuPathDB; FungiDB:YGL087C; -.
DR eggNOG; KOG0896; Eukaryota.
DR HOGENOM; CLU_063065_4_0_1; -.
DR InParanoid; P53152; -.
DR OMA; NLPCVDQ; -.
DR BioCyc; YEAST:G3O-30588-MON; -.
DR Reactome; R-SCE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-SCE-9020702; Interleukin-1 signaling.
DR Reactome; R-SCE-9646399; Aggrephagy.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
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:0031372; C:UBC13-MMS2 complex; IPI:ComplexPortal.
DR GO; GO:0031371; C:ubiquitin conjugating enzyme complex; IPI:SGD.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:SGD.
DR GO; GO:0010994; P:free ubiquitin chain polymerization; IDA:SGD.
DR GO; GO:0006301; P:postreplication repair; IMP: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 Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ligase; Phosphoprotein; Reference proteome;
KW 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
