ID UB2D2_HUMAN Reviewed; 147 AA. AC P62837; P51669; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 23-JAN-2007, entry version 36. DE Ubiquitin-conjugating enzyme E2 D2 (EC 6.3.2.19) (Ubiquitin-protein DE ligase D2) (Ubiquitin carrier protein D2) (Ubiquitin-conjugating DE enzyme E2-17 kDa 2) (E2(17)KB 2). GN Name=UBE2D2; Synonyms=UBC4, UBCH5B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=96107191; PubMed=8530467; DOI=10.1074/jbc.270.51.30408; RA Jensen J.P., Bates P.W., Yang M., Vierstra R.D., Weissman A.M.; RT "Identification of a family of closely related human ubiquitin RT conjugating enzymes."; RL J. Biol. Chem. 270:30408-30414(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=95241484; PubMed=7724550; RA Rolfe M., Beer-Romero P., Glass S., Eckstein J., Berdo I., RA Theodoras A., Pagano M., Draetta G.; RT "Reconstitution of p53-ubiquitinylation reactions from purified RT components: the role of human ubiquitin-conjugating enzyme UBC4 and RT E6-associated protein (E6AP)."; RL Proc. Natl. Acad. Sci. U.S.A. 92:3264-3268(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP INTERACTION WITH SCF COMPLEX. RX MEDLINE=20379358; PubMed=10918611; DOI=10.1038/sj.onc.1203647; RA Strack P., Caligiuri M., Pelletier M., Boisclair M., Theodoras A., RA Beer-Romero P., Glass S., Parsons T., Copeland R.A., Auger K.R., RA Benfield P., Brizuela L., Rolfe M.; RT "SCF(beta-TRCP) and phosphorylation dependent ubiquitination of I RT kappa B alpha catalyzed by Ubc3 and Ubc4."; RL Oncogene 19:3529-3536(2000). CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other CC proteins. Mediates the selective degradation of short-lived and CC abnormal proteins. Functions in the E6/E6-AP-induced CC ubiquitination of p53/TP53. CC -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP + CC diphosphate + protein N-ubiquityllysine. CC -!- PATHWAY: Ubiquitin conjugation; second step. CC -!- SUBUNIT: Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin CC ligase complex. CC -!- INTERACTION: CC Q99942:RNF5; NbExp=1; IntAct=EBI-347677, EBI-348482; CC Q9C035-4:TRIM5; NbExp=1; IntAct=EBI-347677, EBI-924243; 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; U39317; AAA91460.1; -; mRNA. DR EMBL; L40146; AAC41750.1; -; Genomic_DNA. DR EMBL; BC033349; AAH33349.1; -; mRNA. DR PIR; I59365; I59365. DR UniGene; Hs.108332; -. DR PDB; 1UR6; Model; A=1-147. DR PDB; 1W4U; NMR; A=1-147. DR PDB; 2ESK; X-ray; A=1-147. DR PDB; 2ESO; X-ray; A=1-147. DR PDB; 2ESP; X-ray; A=1-147. DR PDB; 2ESQ; X-ray; A=1-147. DR IntAct; P62837; -. DR Ensembl; ENSG00000131508; Homo sapiens. DR KEGG; hsa:7322; -. DR HGNC; HGNC:12475; UBE2D2. DR MIM; 602962; gene. DR LinkHub; P62837; -. DR ArrayExpress; P62837; -. DR GermOnline; ENSG00000109332; Homo sapiens. DR RZPD-ProtExp; I0377; -. DR RZPD-ProtExp; I0378; -. DR RZPD-ProtExp; IOH43701; -. DR RZPD-ProtExp; RZPDo834H1015; -. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0004840; F:ubiquitin conjugating enzyme activity; TAS:ProtInc. DR GO; GO:0004842; F:ubiquitin-protein ligase activity; TAS:ProtInc. DR GO; GO:0006464; P:protein modification; TAS:ProtInc. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolism; TAS:ProtInc. DR InterPro; IPR000608; UBQ-conjugat_E2. DR Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1. 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 3D-structure; Ligase; Ubl conjugation pathway. FT CHAIN 1 147 Ubiquitin-conjugating enzyme E2 D2. FT /FTId=PRO_0000082462. FT ACT_SITE 85 85 Glycyl thioester intermediate (By FT similarity). FT CONFLICT 128 128 K -> Q (in Ref. 2). FT HELIX 1 15 FT STRAND 19 28 FT TURN 30 31 FT STRAND 32 38 FT TURN 41 42 FT TURN 44 47 FT STRAND 49 55 FT TURN 58 61 FT STRAND 66 71 FT TURN 76 77 FT TURN 80 81 FT HELIX 87 89 FT TURN 90 92 FT TURN 95 96 FT HELIX 99 111 FT TURN 115 116 FT HELIX 121 129 FT HELIX 131 145 SQ SEQUENCE 147 AA; 16735 MW; C942BE7853CBC355 CRC64; MALKRIHKEL NDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV PEIARIYKTD REKYNRIARE WTQKYAM //