ID UB2D2_HUMAN Reviewed; 147 AA. AC P62837; P51669; Q3MN78; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 02-MAR-2010, entry version 75. DE RecName: Full=Ubiquitin-conjugating enzyme E2 D2; DE EC=6.3.2.19; DE AltName: Full=Ubiquitin-protein ligase D2; DE AltName: Full=Ubiquitin carrier protein D2; DE AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa 2; DE AltName: Full=Ubiquitin-conjugating enzyme 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; DOI=10.1073/pnas.92.8.3264; 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 [MRNA]. RX PubMed=16112646; DOI=10.1016/j.bbrc.2005.08.024; RA Guinn B.-A., Bland E.A., Lodi U., Liggins A.P., Tobal K., Petters S., RA Wells J.W., Banham A.H., Mufti G.J.; RT "Humoral detection of leukaemia-associated antigens in presentation RT acute myeloid leukaemia."; RL Biochem. Biophys. Res. Commun. 335:1293-1304(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] 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 [7] RP PROTEIN SEQUENCE OF 73-90, AND MASS SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Afjehi-Sadat L.; RL Submitted (MAR-2007) to UniProtKB. RN [8] 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). RN [9] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8, AND MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). 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: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin CC ligase complex and with E3 ubiquitin-protein ligase PJA2 (By CC similarity). CC -!- INTERACTION: CC Q6PCD5:RFWD3; NbExp=2; IntAct=EBI-347677, EBI-2129159; CC Q9Y3C5:RNF11; NbExp=3; IntAct=EBI-347677, EBI-396669; CC Q6ZNA4:RNF111; NbExp=2; IntAct=EBI-347677, EBI-2129175; CC Q96BH1:RNF25; NbExp=2; IntAct=EBI-347677, EBI-2129220; CC Q99942:RNF5; NbExp=2; IntAct=EBI-347677, EBI-348482; CC Q8IUQ4:SIAH1; NbExp=2; IntAct=EBI-347677, EBI-747107; CC Q9Y4K3:TRAF6; NbExp=1; IntAct=EBI-347677, EBI-359276; CC Q9C035-4:TRIM5; NbExp=1; IntAct=EBI-347677, EBI-924243; CC P98170:XIAP; NbExp=1; IntAct=EBI-347677, EBI-517127; CC Q8ND25:ZNRF1; NbExp=3; IntAct=EBI-347677, EBI-2129250; 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; AY651263; AAX35690.1; -; mRNA. DR EMBL; AK001311; BAG50891.1; -; mRNA. DR EMBL; AK001428; BAG50911.1; -; mRNA. DR EMBL; CH471062; EAW62095.1; -; Genomic_DNA. DR EMBL; BC033349; AAH33349.1; -; mRNA. DR IPI; IPI00332376; -. DR PIR; I59365; I59365. DR RefSeq; NP_003330.1; -. DR RefSeq; NP_862821.1; -. DR UniGene; Hs.108332; -. DR PDB; 1UR6; NMR; -; A=1-147. DR PDB; 1W4U; NMR; -; A=1-147. DR PDB; 2C4O; X-ray; 1.94 A; A/B/C/D=1-147. DR PDB; 2CLW; X-ray; 1.94 A; A/B/C/D=1-147. DR PDB; 2ESK; X-ray; 1.36 A; A=1-147. DR PDB; 2ESO; X-ray; 1.50 A; A=1-147. DR PDB; 2ESP; X-ray; 1.52 A; A=1-147. DR PDB; 2ESQ; X-ray; 1.44 A; A=1-147. DR PDB; 3A33; X-ray; 2.20 A; A=1-147. DR PDBsum; 1UR6; -. DR PDBsum; 1W4U; -. DR PDBsum; 2C4O; -. DR PDBsum; 2CLW; -. DR PDBsum; 2ESK; -. DR PDBsum; 2ESO; -. DR PDBsum; 2ESP; -. DR PDBsum; 2ESQ; -. DR PDBsum; 3A33; -. DR DIP; DIP-29267N; -. DR IntAct; P62837; 93. DR STRING; P62837; -. DR PRIDE; P62837; -. DR Ensembl; ENST00000398733; ENSP00000381717; ENSG00000131508; Homo sapiens. DR GeneID; 7322; -. DR KEGG; hsa:7322; -. DR UCSC; uc003ler.1; human. DR CTD; 7322; -. DR GeneCards; GC05P138920; -. DR H-InvDB; HIX0005224; -. DR H-InvDB; HIX0019025; -. DR H-InvDB; HIX0028451; -. DR HGNC; HGNC:12475; UBE2D2. DR HPA; HPA003920; -. DR MIM; 602962; gene. DR PharmGKB; PA37125; -. DR HOGENOM; HBG756483; -. DR HOVERGEN; HBG063308; -. DR OMA; RKKYEAT; -. DR PhylomeDB; P62837; -. DR BRENDA; 6.3.2.19; 247. DR NextBio; 28630; -. DR ArrayExpress; P62837; -. DR Bgee; P62837; -. DR CleanEx; HS_UBE2D2; -. DR Genevestigator; P62837; -. DR GermOnline; ENSG00000131508; Homo sapiens. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0004842; F:ubiquitin-protein ligase activity; TAS:ProtInc. DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB. DR GO; GO:0051246; P:regulation of protein metabolic process; IEA:InterPro. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc. DR InterPro; IPR016135; UBQ-conjugat/RWD-like. DR InterPro; IPR000608; UBQ-conjugat_E2. DR Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1. DR Pfam; PF00179; UQ_con; 1. DR SMART; SM00212; UBCc; 1. DR SUPFAM; SSF54495; UBQ-conjugat/RWD-like; 1. DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1. DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Complete proteome; KW Direct protein sequencing; Ligase; Nucleotide-binding; KW 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 MOD_RES 8 8 N6-acetyllysine. FT CONFLICT 128 128 K -> Q (in Ref. 2; AAC41750). FT HELIX 1 15 FT STRAND 19 28 FT STRAND 32 38 FT TURN 44 47 FT STRAND 49 55 FT TURN 58 61 FT STRAND 66 71 FT HELIX 87 89 FT TURN 90 92 FT HELIX 99 111 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 //