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 10-OCT-2003 (Rel. 42, 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; RX MEDLINE=22388257; PubMed=12477932; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length RT human and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). 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 //