ID UBC13_YEAST Reviewed; 153 AA. AC P52490; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 16-JUN-2009, entry version 85. DE RecName: Full=Ubiquitin-conjugating enzyme E2 13; DE EC=6.3.2.19; DE AltName: Full=Ubiquitin-protein ligase 13; DE AltName: Full=Ubiquitin carrier protein 13; GN Name=UBC13; OrderedLocusNames=YDR092W; ORFNames=YD6652.04; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 200912 / DF5; RX MEDLINE=96162026; PubMed=8576256; DOI=10.1074/jbc.271.5.2789; RA Matuschewski K., Hauser H.P., Treier M., Jentsch S.; RT "Identification of a novel family of ubiquitin-conjugating enzymes RT with distinct amino-terminal extensions."; RL J. Biol. Chem. 271:2789-2794(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX MEDLINE=97313263; PubMed=9169867; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., RA Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., RA Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., RA Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., RA Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., RA Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., RA Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., RA Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., RA Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., RA Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., RA Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., RA Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., RA Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., RA Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., RA Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., RA Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., RA Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., RA Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., RA Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., RA Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., RA Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., RA Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(1997). RN [3] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH MMS2, AND RP MUTAGENESIS OF GLU-55. 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 RT structure of the Mms2/Ubc13 heterodimer."; RL Cell 105:711-720(2001). CC -!- FUNCTION: Has a role in the DNA error-free postreplication repair CC (PRR) pathway. The UBC13/MMS2 heterodimer catalyzes the synthesis CC of non-canonical poly-ubiquitin chains that are linked through CC 'Lys-63'. CC -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP + CC diphosphate + protein N-ubiquityllysine. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Heterodimer with MMS2. CC -!- INTERACTION: CC P39525:CEM1; NbExp=1; IntAct=EBI-19777, EBI-4467; CC P10174:COX7; NbExp=1; IntAct=EBI-19777, EBI-2050505; CC P53152:MMS2; NbExp=2; IntAct=EBI-19777, EBI-11035; CC Q06651:PIB1; NbExp=1; IntAct=EBI-19777, EBI-35947; CC P09938:RNR2; NbExp=1; IntAct=EBI-19777, EBI-15240; CC P40210:SIP5; NbExp=1; IntAct=EBI-19777, EBI-27280; CC P41896:TFG2; NbExp=1; IntAct=EBI-19777, EBI-18916; CC P38988:YHM1; NbExp=1; IntAct=EBI-19777, EBI-24559; CC -!- MISCELLANEOUS: Present with 8970 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X99443; CAA67806.1; -; Genomic_DNA. DR EMBL; Z50111; CAA90451.1; -; Genomic_DNA. DR PIR; S58092; S58092. DR RefSeq; NP_010377.1; -. DR PDB; 1JAT; X-ray; 1.60 A; A=2-153. DR PDB; 1JBB; X-ray; 2.00 A; A/B=1-153. DR PDB; 2GMI; X-ray; 2.50 A; A=1-152. DR PDBsum; 1JAT; -. DR PDBsum; 1JBB; -. DR PDBsum; 2GMI; -. DR DIP; DIP:5486N; -. DR IntAct; P52490; 47. DR PeptideAtlas; P52490; -. DR PRIDE; P52490; -. DR Ensembl; YDR092W; Saccharomyces cerevisiae. DR GeneID; 851666; -. DR GenomeReviews; Z71256_GR; YDR092W. DR KEGG; sce:YDR092W; -. DR NMPDR; fig|4932.3.peg.1123; -. DR CYGD; YDR092w; -. DR SGD; S000002499; UBC13. DR HOGENOM; P52490; -. DR OMA; P52490; LGAPNPD. DR BRENDA; 6.3.2.19; 250. DR NextBio; 969283; -. DR ArrayExpress; P52490; -. DR GermOnline; YDR092W; Saccharomyces cerevisiae. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0031371; C:ubiquitin conjugating enzyme complex; IPI:SGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:EC. DR GO; GO:0019941; P:modification-dependent protein catabolic pr...; IEA:UniProtKB-KW. DR GO; GO:0006301; P:postreplication repair; IGI:SGD. DR GO; GO:0006513; P:protein monoubiquitination; TAS:SGD. DR GO; GO:0000209; P:protein polyubiquitination; IDA:SGD. DR GO; GO:0051246; P:regulation of protein metabolic process; IEA:InterPro. DR InterPro; IPR016135; UBQ-conjugat/RWD-like. DR InterPro; IPR000608; UBQ-conjugat_E2. DR Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1. DR Pfam; PF00179; UQ_con; 1. DR ProDom; PD000461; UBQ_conjugat; 1. DR SMART; SM00212; UBCc; 1. DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1. DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Ligase; KW Nucleotide-binding; Ubl conjugation pathway. FT CHAIN 1 153 Ubiquitin-conjugating enzyme E2 13. FT /FTId=PRO_0000082565. FT ACT_SITE 87 87 Glycyl thioester intermediate. FT MUTAGEN 55 55 E->A: Strongly reduces MMS2 binding and FT interferes with error-free DNA repair. FT MUTAGEN 81 81 D->R: Abolishes ubiquitin chain FT elongation. No effect on thioester FT formation at the active site. FT MUTAGEN 110 110 A->R: Lowers rate of ubiquitin chain FT elongation. No effect on thioester FT formation at the active site. FT HELIX 6 17 FT STRAND 23 28 FT STRAND 31 40 FT TURN 46 49 FT STRAND 50 57 FT TURN 60 64 FT STRAND 68 71 FT HELIX 89 91 FT TURN 92 94 FT HELIX 101 113 FT HELIX 126 131 FT HELIX 133 147 FT STRAND 148 150 SQ SEQUENCE 153 AA; 17468 MW; 445558F8F193275B CRC64; MASLPKRIIK ETEKLVSDPV PGITAEPHDD NLRYFQVTIE GPEQSPYEDG IFELELYLPD DYPMEAPKVR FLTKIYHPNI DRLGRICLDV LKTNWSPALQ IRTVLLSIQA LLASPNPNDP LANDVAEDWI KNEQGAKAKA REWTKLYAKK KPE //