ID UBCM_HUMAN STANDARD; PRT; 183 AA. AC O76069; Q8VC50; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Ubiquitin-conjugating enzyme E2 M (EC 6.3.2.19) (Ubiquitin-protein DE ligase M) (Ubiquitin carrier protein M) (Nedd8-conjugating enzyme DE Ubc12). GN UBE2M OR UBC12 OR UBC-RS2. OS Homo sapiens (Human), and OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606, 10090; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=Human; 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 the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC SPECIES=Human; RX MEDLINE=98361870; PubMed=9694792; 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). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=Human; TISSUE=Eye; RA Strausberg R.; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC SPECIES=Mouse; TISSUE=Kidney; RA Strausberg R.; RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin-like CC protein NEDD8 to other proteins. CC -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP + CC diphosphate + protein N-ubiquityllysine. CC -!- PATHWAY: Ubiquitin conjugation; second step. CC -!- MISCELLANEOUS: A cysteine residue is required for ubiquitin- CC thiolester formation (By similarity). 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; AF075599; AAC26141.1; -. DR EMBL; AB012191; BAA33145.1; -. DR EMBL; BC007657; AAH07657.1; -. DR EMBL; BC021792; AAH21792.1; -. DR HSSP; Q95044; 2E2C. DR Genew; HGNC:12491; UBE2M. DR MIM; 603173; -. DR MGD; MGI:108278; Ubc-rs2. DR GO; GO:0004840; F:ubiquitin conjugating enzyme activity; TAS. DR GO; GO:0004842; F:ubiquitin-protein ligase activity; TAS. DR GO; GO:0006464; P:protein modification; TAS. DR InterPro; IPR000608; UBQ_conjugat. DR Pfam; PF00179; UQ_con; 1. DR ProDom; PD000461; UBQ_conjugat; 1. DR SMART; SM00212; UBCc; 1. DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1. DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1. KW Ubl conjugation pathway; Ligase; Multigene family. FT BINDING 111 111 UBIQUITIN (BY SIMILARITY). SQ SEQUENCE 183 AA; 20900 MW; E3C288CA6A98BC5C CRC64; MIKLFSLKQQ KKEEESAGGT KGSSKKASAA QLRIQKDINE LNLPKTCDIS FSDPDDLLNF KLVICPDEGF YKSGKFVFSF KVGQGYPHDP PKVKCETMVY HPNIDLEGNV CLNILREDWK PVLTINSIIY GLQYLFLEPN PEDPLNKEAA EVLQNNRRLF EQNVQRSMRG GYIGSTYFER CLK //