ID UBC4_YEAST STANDARD; PRT; 148 AA. AC P15731; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 01-OCT-2000 (Rel. 40, Last annotation update) DE UBIQUITIN-CONJUGATING ENZYME E2-16 KDA (EC 6.3.2.19) DE (UBIQUITIN-PROTEIN LIGASE) (UBIQUITIN CARRIER PROTEIN). GN UBC4 OR YBR082C OR YBR0745. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycetes; Saccharomycetales; OC Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 40-64 AND 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 SEQUENCE FROM N.A. 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 SEQUENCE FROM N.A. RC STRAIN=S288C; RA Andre B., Cziepluch C., Hein C., Jauniaux J.C., Urrestarazu A., RA Vissers S.; RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases. RN [4] 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 CC OTHER PROTEINS. MEDIATES THE SELECTIVE DEGRADATION OF SHORT-LIVED CC AND ABNORMAL PROTEINS. CC -!- CATALYTIC ACTIVITY: ATP + UBIQUITIN + PROTEIN LYSINE = AMP + CC PYROPHOSPHATE + PROTEIN N-UBIQUITYLLYSINE. CC -!- PATHWAY: SECOND STEP IN UBIQUITIN CONJUGATION. CC -!- INDUCTION: ACTIVATED BOTH BY HEAT SHOCK AND CADMIUM. CC -!- MISCELLANEOUS: A CYSTEINE RESIDUE IS REQUIRED FOR CC UBIQUITIN-THIOLESTER FORMATION. 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; -. DR EMBL; X76294; CAA53942.1; -. DR EMBL; Z35951; CAA85027.1; -. DR PIR; S22857; S22857. DR PDB; 1QCQ; 06-MAR-00. DR SGD; S0000286; UBC4. DR INTERPRO; IPR000608; -. DR PFAM; PF00179; UQ_con; 1. DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1. DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1. KW Ubiquitin conjugation; Ligase; Multigene family; 3D-structure. FT MOD_RES 1 1 BLOCKED. FT BINDING 86 86 UBIQUITIN. FT HELIX 4 13 FT TURN 14 14 FT STRAND 22 27 FT TURN 28 29 FT STRAND 30 39 FT TURN 42 43 FT TURN 45 48 FT STRAND 50 56 FT TURN 59 62 FT STRAND 67 70 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 100 110 FT TURN 111 112 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 //