ID UBC4_YEAST STANDARD; PRT; 148 AA. AC P15731; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 07-FEB-2006, entry version 63. DE Ubiquitin-conjugating enzyme E2 4 (EC 6.3.2.19) (Ubiquitin-protein DE ligase 4) (Ubiquitin carrier protein 4). GN Name=UBC4; OrderedLocusNames=YBR082C; ORFNames=YBR0745; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 40-64 AND RP 119-125. RX MEDLINE=90151631; PubMed=2154373; RA Seufert W., Jentsch S.; RT "Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective RT degradation of short-lived and abnormal proteins."; RL EMBO J. 9:543-550(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=S288c; RX MEDLINE=95076715; PubMed=7985423; RA van der Aart Q.J.M., Barthe C., Doignon F., Aigle M., Crouzet M., RA Steensma H.Y.; RT "Sequence analysis of a 31 kb DNA fragment from the right arm of RT Saccharomyces cerevisiae chromosome II."; RL Yeast 10:959-964(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S288c; RX MEDLINE=95112788; PubMed=7813418; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., RA Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., RA Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., RA Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., RA Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., RA Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., RA Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., RA Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., RA Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., RA Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., RA Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., RA van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., RA Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., RA Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). RN [4] RP INTERACTION WITH TUL1. RX MEDLINE=21824231; PubMed=11788821; DOI=10.1038/ncb743; RA Reggiori F., Pelham H.R.B.; RT "A transmembrane ubiquitin ligase required to sort membrane proteins RT into multivesicular bodies."; RL Nat. Cell Biol. 4:117-123(2002). RN [5] RP LEVEL OF PROTEIN EXPRESSION. 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 [6] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). RX MEDLINE=94092661; PubMed=8268156; RA Cook W.J., Jeffrey L.C., Xu Y., Chau V.; RT "Tertiary structures of class I ubiquitin-conjugating enzymes are RT highly conserved: crystal structure of yeast Ubc4."; RL Biochemistry 32:13809-13817(1993). CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other CC proteins. Mediates the selective degradation of short-lived and CC abnormal proteins. CC -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP + CC diphosphate + protein N-ubiquityllysine. CC -!- PATHWAY: Ubiquitin conjugation; second step. CC -!- SUBUNIT: Interacts with TUL1. CC -!- INDUCTION: By heat shock and cadmium. CC -!- PTM: The N-terminus is blocked. CC -!- MISCELLANEOUS: Present with 13500 molecules/cell. CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme 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; X17493; CAA35528.1; -; Genomic_DNA. DR EMBL; X76294; CAA53942.1; -; Genomic_DNA. DR EMBL; Z35951; CAA85027.1; -; Genomic_DNA. DR PIR; S22857; S22857. DR PDB; 1QCQ; X-ray; A=1-148. DR IntAct; P15731; -. DR GermOnline; 138625; -. DR Ensembl; YBR082C; Saccharomyces cerevisiae. DR SGD; S000000286; UBC4. DR BioCyc; SCER-S28-01:SCER-S28-01-000343-MONOMER; -. DR LinkHub; P15731; -. DR GO; GO:0000502; C:proteasome complex (sensu Eukaryota); IPI. DR GO; GO:0004840; F:ubiquitin conjugating enzyme activity; IDA. DR GO; GO:0006513; P:protein monoubiquitination; IDA. DR GO; GO:0000209; P:protein polyubiquitination; IDA. DR GO; GO:0006950; P:response to stress; IDA. DR GO; GO:0030437; P:sporulation (sensu Fungi); TAS. DR GO; GO:0043162; P:ubiquitin-dependent protein catabolism via ...; IMP. DR InterPro; IPR000608; UBQ-conjugat_E2. 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. KW 3D-structure; Complete proteome; Direct protein sequencing; Ligase; KW Ubl conjugation pathway. FT CHAIN 1 148 Ubiquitin-conjugating enzyme E2 4. FT /FTId=PRO_0000082545. FT ACT_SITE 86 86 Glycyl thioester intermediate. FT HELIX 2 14 FT TURN 15 16 FT STRAND 22 27 FT TURN 28 29 FT STRAND 30 40 FT TURN 42 43 FT TURN 45 46 FT STRAND 47 47 FT TURN 48 48 FT STRAND 50 56 FT TURN 59 62 FT STRAND 67 70 FT STRAND 76 76 FT TURN 77 78 FT STRAND 79 79 FT TURN 81 82 FT STRAND 84 85 FT HELIX 88 90 FT TURN 91 93 FT TURN 96 97 FT HELIX 100 112 FT TURN 116 117 FT HELIX 122 130 FT HELIX 132 146 SQ SEQUENCE 148 AA; 16456 MW; 8E96137D3EB20F80 CRC64; MSSSKRIAKE LSDLERDPPT SCSAGPVGDD LYHWQASIMG PADSPYAGGV FFLSIHFPTD YPFKPPKISF TTKIYHPNIN ANGNICLDIL KDQWSPALTL SKVLLSICSL LTDANPDDPL VPEIAHIYKT DRPKYEATAR EWTKKYAV //