ID UBC4_YEAST Reviewed; 148 AA. AC P15731; D6VQ81; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 04-FEB-2015, entry version 153. DE RecName: Full=Ubiquitin-conjugating enzyme E2 4; DE EC=6.3.2.19; DE AltName: Full=Ubiquitin carrier protein 4; DE AltName: Full=Ubiquitin-protein ligase 4; GN Name=UBC4; OrderedLocusNames=YBR082C; ORFNames=YBR0745; 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 [GENOMIC DNA], AND PROTEIN SEQUENCE OF 40-64 AND RP 119-125. RX 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=ATCC 204508 / S288c; RX PubMed=7985423; DOI=10.1002/yea.320100711; 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=ATCC 204508 / S288c; RX 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 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., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT now."; RL G3 (Bethesda) 4:389-398(2014). RN [5] RP INTERACTION WITH TUL1. RX 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 [6] 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., 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 [7] RP FUNCTION. RX PubMed=17550898; DOI=10.1074/jbc.M702038200; RA Williams C., van den Berg M., Sprenger R.R., Distel B.; RT "A conserved cysteine is essential for Pex4p-dependent ubiquitination RT of the peroxisomal import receptor Pex5p."; RL J. Biol. Chem. 282:22534-22543(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION RP BY 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 RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22106047; DOI=10.1002/pmic.201100166; RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.; RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae."; RL Proteomics 12:236-240(2012). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). RX PubMed=8268156; DOI=10.1021/bi00213a009; 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. Mediates ubiquitination of PEX5. CC {ECO:0000255|PROSITE-ProRule:PRU00388, CC ECO:0000269|PubMed:17550898}. CC -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP + CC diphosphate + protein N-ubiquityllysine. {ECO:0000255|PROSITE- CC ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000255|PROSITE-ProRule:PRU00388}. CC -!- SUBUNIT: Interacts with TUL1. {ECO:0000269|PubMed:11788821}. CC -!- INTERACTION: CC P38879:EGD2; NbExp=2; IntAct=EBI-19735, EBI-6379; CC -!- INDUCTION: By heat shock and cadmium. CC -!- PTM: The N-terminus is blocked. CC -!- MISCELLANEOUS: Present with 13500 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. CC {ECO:0000255|PROSITE-ProRule:PRU00388}. 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 EMBL; BK006936; DAA07201.1; -; Genomic_DNA. DR PIR; S22857; S22857. DR RefSeq; NP_009638.1; NM_001178430.1. DR PDB; 1QCQ; X-ray; 2.70 A; A=1-148. DR PDBsum; 1QCQ; -. DR ProteinModelPortal; P15731; -. DR SMR; P15731; 1-148. DR BioGrid; 32786; 262. DR DIP; DIP-6596N; -. DR IntAct; P15731; 4. DR MINT; MINT-677321; -. DR STRING; 4932.YBR082C; -. DR MaxQB; P15731; -. DR PeptideAtlas; P15731; -. DR PRIDE; P15731; -. DR EnsemblFungi; YBR082C; YBR082C; YBR082C. DR GeneID; 852376; -. DR KEGG; sce:YBR082C; -. DR CYGD; YBR082c; -. DR SGD; S000000286; UBC4. DR GeneTree; ENSGT00760000119012; -. DR HOGENOM; HOG000233455; -. DR InParanoid; P15731; -. DR KO; K06689; -. DR OMA; YAGGVYF; -. DR OrthoDB; EOG7SBP18; -. DR BioCyc; YEAST:G3O-29050-MONOMER; -. DR UniPathway; UPA00143; -. DR EvolutionaryTrace; P15731; -. DR NextBio; 971168; -. DR Proteomes; UP000002311; Chromosome II. DR Genevestigator; P15731; -. DR GO; GO:0000502; C:proteasome complex; IPI:SGD. DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0030674; F:protein binding, bridging; IDA:SGD. DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IMP:UniProtKB. DR GO; GO:0034605; P:cellular response to heat; IDA:SGD. DR GO; GO:0006513; P:protein monoubiquitination; IDA:SGD. DR GO; GO:0000209; P:protein polyubiquitination; IMP:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; IDA:SGD. DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:SGD. DR Gene3D; 3.10.110.10; -; 1. DR InterPro; IPR000608; UBQ-conjugat_E2. DR InterPro; IPR023313; UBQ-conjugating_AS. DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD. DR Pfam; PF00179; UQ_con; 1. DR SUPFAM; SSF54495; SSF54495; 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; KW Direct protein sequencing; Ligase; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Stress response; 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 MOD_RES 12 12 Phosphoserine. FT {ECO:0000269|PubMed:18407956}. FT HELIX 2 14 {ECO:0000244|PDB:1QCQ}. FT STRAND 20 27 {ECO:0000244|PDB:1QCQ}. FT STRAND 30 40 {ECO:0000244|PDB:1QCQ}. FT STRAND 50 56 {ECO:0000244|PDB:1QCQ}. FT TURN 59 62 {ECO:0000244|PDB:1QCQ}. FT STRAND 67 70 {ECO:0000244|PDB:1QCQ}. FT HELIX 88 90 {ECO:0000244|PDB:1QCQ}. FT TURN 91 93 {ECO:0000244|PDB:1QCQ}. FT HELIX 100 112 {ECO:0000244|PDB:1QCQ}. FT HELIX 122 130 {ECO:0000244|PDB:1QCQ}. FT HELIX 132 146 {ECO:0000244|PDB:1QCQ}. SQ SEQUENCE 148 AA; 16456 MW; 8E96137D3EB20F80 CRC64; MSSSKRIAKE LSDLERDPPT SCSAGPVGDD LYHWQASIMG PADSPYAGGV FFLSIHFPTD YPFKPPKISF TTKIYHPNIN ANGNICLDIL KDQWSPALTL SKVLLSICSL LTDANPDDPL VPEIAHIYKT DRPKYEATAR EWTKKYAV //