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-1996 (REL. 34, LAST ANNOTATION UPDATE) DE UBIQUITIN-CONJUGATING ENZYME E2-16 KD (EC 6.3.2.19) (UBIQUITIN-PROTEIN DE LIGASE) (UBIQUITIN CARRIER PROTEIN). GN UBC4 OR YBR082C OR YBR0745. OS SACCHAROMYCES CEREVISIAE (BAKER'S YEAST). OC EUKARYOTA; FUNGI; ASCOMYCOTINA; HEMIASCOMYCETES. RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 40-64 AND 119-125. RX MEDLINE; 90151631. RA SEUFERT W., JENTSCH S.; RL EMBO J. 9:543-550(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=S288C; RX MEDLINE; 95076715. RA VAN DER AART Q.J.M., BARTHE C., DOIGNON F., AIGLE M., CROUZET M., RA STEENSMA H.Y.; 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 EMBL/GENBANK/DDBJ DATA BANKS. RN [4] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). RX MEDLINE; 94092661. RA COOK W.J., JEFFREY L.C., XU Y., CHAU V.; RL BIOCHEMISTRY 32:13809-13817(1993). CC -!- FUNCTION: CATALYSES THE COVALENT ATTACHMENT OF UBIQUITIN TO CC OTHER PROTEINS. MEDIATE 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 -!- A CYSTEINE RESIDUE IS REQUIRED FOR UBIQUITIN-THIOLESTER FORMATION. CC -!- INDUCTION: ACTIVATED BOTH BY HEAT SHOCK AND CADMIUM. CC -!- SIMILARITY: TO THE OTHER UBIQUITIN-CONJUGATING ENZYMES. 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; G295933; -. DR EMBL; X76294; E264676; -. DR EMBL; Z35951; G536344; -. DR PIR; S22857; S22857. DR PDB; 2UCE; 31-JAN-94. DR LISTA; SC01350; UBC4. DR SGD; L0002407; UBC4. DR PROSITE; PS00183; UBIQUITIN_CONJUGAT. 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; 1BF7783A CRC32; MSSSKRIAKE LSDLERDPPT SCSAGPVGDD LYHWQASIMG PADSPYAGGV FFLSIHFPTD YPFKPPKISF TTKIYHPNIN ANGNICLDIL KDQWSPALTL SKVLLSICSL LTDANPDDPL VPEIAHIYKT DRPKYEATAR EWTKKYAV //