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-JUN-1994 (REL. 29, LAST ANNOTATION UPDATE) DE UBIQUITIN-CONJUGATING ENZYME E2-16 KD (EC 6.3.2.19) (UBIQUITIN-PROTEIN DE LIGASE) (UBIQUITIN CARRIER PROTEIN). GN UBC4. 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. RM 90151631 RA SEUFERT W., JENTSCH S.; RL EMBO J. 9:543-550(1990). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). RM 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 -!- A CYSTEINE RESIDUE IS REQUIRED FOR UBIQUITIN-THIOLESTER CC FORMATION. 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; SCUBC4. DR PIR; S22857; S22857. DR PDB; 2UCE; 31-JAN-94. DR PROSITE; PS00183; UBIQUITIN_CONJUGAT. KW UBIQUITIN CONJUGATION; LIGASE; MULTIGENE FAMILY; 3D-STRUCTURE. FT MOD_RES 1 1 BLOCKED. FT BINDING 86 86 UBIQUITIN. SQ SEQUENCE 148 AA; 16456 MW; 118864 CN; MSSSKRIAKE LSDLERDPPT SCSAGPVGDD LYHWQASIMG PADSPYAGGV FFLSIHFPTD YPFKPPKISF TTKIYHPNIN ANGNICLDIL KDQWSPALTL SKVLLSICSL LTDANPDDPL VPEIAHIYKT DRPKYEATAR EWTKKYAV //