ID O76069 PRELIMINARY; PRT; 183 AA. AC O76069; DT 01-NOV-1998 (TREMBLREL. 08, CREATED) DT 01-NOV-1998 (TREMBLREL. 08, LAST SEQUENCE UPDATE) DT 01-NOV-1998 (TREMBLREL. 08, LAST ANNOTATION UPDATE) DE UBIQUITIN-CONJUGATING ENZYME E2 (EC 6.3.2.19) DE (UBIQUITIN-PROTEIN LIGASE) (UBIQUITIN CARRIER PROTEIN). GN UBC12. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; MAMMALIA; EUTHERIA; PRIMATES; OC CATARRHINI; HOMINIDAE; HOMO. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA GONG L., YEH E.T.H.; RT "Identification of the Activating and Conjugating Enzymes of the RT NEDD8-Conjugation Pathway."; RL SUBMITTED (JUN-1998) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [2] RP SEQUENCE FROM N.A. RX MEDLINE; 98361870. RA OSAKA F., KAWASAKI H., AIDA N., SAEKI M., CHIBA T., KAWASHIMA S., RA TANAKA K., KATO S.; RT "A new NEDD8-ligating system for cullin-4A."; RL GENES DEV. 12:2263-2268(1998). CC -!- FUNCTION: CATALYSES THE COVALENT ATTACHMENT OF UBIQUITIN TO OTHER CC 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 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; AF075599; G3309661; -. DR EMBL; AB012191; D1034111; -. DR PROSITE; PS00183; UBIQUITIN_CONJUGAT; 1. KW UBIQUITIN CONJUGATION; LIGASE. FT BINDING 111 111 UBIQUITIN (BY SIMILARITY). SQ SEQUENCE 183 AA; 20900 MW; 3727524D CRC32; MIKLFSLKQQ KKEEESAGGT KGSSKKASAA QLRIQKDINE LNLPKTCDIS FSDPDDLLNF KLVICPDEGF YKSGKFVFSF KVGQGYPHDP PKVKCETMVY HPNIDLEGNV CLNILREDWK PVLTINSIIY GLQYLFLEPN PEDPLNKEAA EVLQNNRRLF EQNVQRSMRG GYIGSTYFER CLK //