ID UB2D2_HUMAN STANDARD; PRT; 147 AA. AC P62837; P51669; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 19-SEP-2006, entry version 30. 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. 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. 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 MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; 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 human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). 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 RZPD-ProtExp; I0377; -. DR RZPD-ProtExp; I0378; -. DR RZPD-ProtExp; IOH43701; -. DR RZPD-ProtExp; RZPDo834H1015; -. DR GO; GO:0005515; F:protein binding; IPI. DR InterPro; IPR000608; UBQ-conjugat_E2. DR Pfam; PF00179; UQ_con; 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 3 9 FT TURN 10 11 FT HELIX 12 15 FT STRAND 16 16 FT STRAND 19 20 FT STRAND 26 29 FT TURN 30 31 FT STRAND 32 38 FT STRAND 41 42 FT TURN 44 47 FT STRAND 49 55 FT STRAND 57 58 FT TURN 60 61 FT STRAND 62 62 FT STRAND 66 71 FT STRAND 75 75 FT TURN 76 77 FT STRAND 78 78 FT TURN 80 81 FT STRAND 82 84 FT HELIX 87 90 FT TURN 91 91 FT STRAND 92 92 FT TURN 95 96 FT HELIX 99 111 FT STRAND 112 112 FT STRAND 115 115 FT STRAND 120 120 FT TURN 121 122 FT HELIX 123 128 FT TURN 129 129 FT HELIX 131 144 FT TURN 145 146 SQ SEQUENCE 147 AA; 16735 MW; C942BE7853CBC355 CRC64; MALKRIHKEL NDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV PEIARIYKTD REKYNRIARE WTQKYAM //