UBE2D3

Ubiquitin-conjugating enzyme E2D 3
PDB rendering based on 1ur6.
Available structures PDB 1X23, 2FUH, 3L1Z
Identifiers
Symbols	UBE2D3; E2(17)KB3; MGC43926; MGC5416; UBC4/5; UBCH5C
External IDs	OMIM: 602963 MGI: 1913355 HomoloGene: 123914 GeneCards: UBE2D3 Gene
EC number	6.3.2.19
Gene Ontology Molecular function • nucleotide binding • ubiquitin-protein ligase activity • protein binding • ATP binding • ligase activity • acid-amino acid ligase activity Cellular component • endosome • plasma membrane • endosome membrane Biological process • protein polyubiquitination • DNA repair • protein modification process • ubiquitin-dependent protein catabolic process • protein monoubiquitination • apoptosis • transforming growth factor beta receptor signaling pathway • protein ubiquitination • protein ubiquitination • BMP signaling pathway • negative regulation of type I interferon production • proteasomal ubiquitin-dependent protein catabolic process • protein K48-linked ubiquitination • protein K11-linked ubiquitination Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	7323	66105
Ensembl	ENSG00000109332	ENSMUSG00000078578
UniProt	P61077	P61079
RefSeq (mRNA)	NM_003340.5	NM_025356.4
RefSeq (protein)	NP_003331.1	NP_079632.1
Location (UCSC)	Chr 4: 103.72 – 103.79 Mb	Chr 3: 135.1 – 135.13 Mb
PubMed search	[1]	[2]

Ubiquitin-conjugating enzyme E2 D3 is a protein that in humans is encoded by the UBE2D3 gene.

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme functions in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase. Multiple spliced transcript variants have been found for this gene, but the full-length nature of some variants has not been determined.

Interactions

UBE2D3 has been shown to interact with NEDD4.

Further reading

• Scheffner M, Huibregtse JM, Howley PM (1994). "Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53.". Proc. Natl. Acad. Sci. U.S.A. 91 (19): 8797–801. doi:10.1073/pnas.91.19.8797. PMC 44693. PMID 8090726. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=44693. 
• Rogakou EP, Pilch DR, Orr AH, et al. (1998). "DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139.". J. Biol. Chem. 273 (10): 5858–68. doi:10.1074/jbc.273.10.5858. PMID 9488723. 
• Anan T, Nagata Y, Koga H, et al. (1999). "Human ubiquitin-protein ligase Nedd4: expression, subcellular localization and selective interaction with ubiquitin-conjugating enzymes.". Genes Cells 3 (11): 751–63. doi:10.1046/j.1365-2443.1998.00227.x. PMID 9990509. 
• Gonen H, Bercovich B, Orian A, et al. (1999). "Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha.". J. Biol. Chem. 274 (21): 14823–30. doi:10.1074/jbc.274.21.14823. PMID 10329681. 
• Orian A, Gonen H, Bercovich B, et al. (2000). "SCF(beta)(-TrCP) ubiquitin ligase-mediated processing of NF-kappaB p105 requires phosphorylation of its C-terminus by IkappaB kinase.". EMBO J. 19 (11): 2580–91. doi:10.1093/emboj/19.11.2580. PMC 212749. PMID 10835356. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=212749. 
• Coleman CS, Pegg AE (2001). "Polyamine analogues inhibit the ubiquitination of spermidine/spermine N1-acetyltransferase and prevent its targeting to the proteasome for degradation.". Biochem. J. 358 (Pt 1): 137–45. doi:10.1042/0264-6021:3580137. PMC 1222041. PMID 11485561. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222041. 
• Chen A, Kleiman FE, Manley JL, et al. (2002). "Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase.". J. Biol. Chem. 277 (24): 22085–92. doi:10.1074/jbc.M201252200. PMID 11927591. 
• Obin M, Lee BY, Meinke G, et al. (2003). "Ubiquitylation of the transducin betagamma subunit complex. Regulation by phosducin.". J. Biol. Chem. 277 (46): 44566–75. doi:10.1074/jbc.M205308200. PMID 12215439. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Takeyama K, Aguiar RC, Gu L, et al. (2003). "The BAL-binding protein BBAP and related Deltex family members exhibit ubiquitin-protein isopeptide ligase activity.". J. Biol. Chem. 278 (24): 21930–7. doi:10.1074/jbc.M301157200. PMID 12670957. 
• Brzovic PS, Keeffe JR, Nishikawa H, et al. (2003). "Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex.". Proc. Natl. Acad. Sci. U.S.A. 100 (10): 5646–51. doi:10.1073/pnas.0836054100. PMC 156255. PMID 12732733. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=156255. 
• Tang ED, Wang CY, Xiong Y, Guan KL (2003). "A role for NF-kappaB essential modifier/IkappaB kinase-gamma (NEMO/IKKgamma) ubiquitination in the activation of the IkappaB kinase complex by tumor necrosis factor-alpha.". J. Biol. Chem. 278 (39): 37297–305. doi:10.1074/jbc.M303389200. PMID 12867425. 
• Subramaniam V, Li H, Wong M, et al. (2003). "The RING-H2 protein RNF11 is overexpressed in breast cancer and is a target of Smurf2 E3 ligase.". Br. J. Cancer 89 (8): 1538–44. doi:10.1038/sj.bjc.6601301. PMC 2394340. PMID 14562029. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2394340. 
• Lehner B, Semple JI, Brown SE, et al. (2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region.". Genomics 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. PMID 14667819. 
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• Saville MK, Sparks A, Xirodimas DP, et al. (2004). "Regulation of p53 by the ubiquitin-conjugating enzymes UbcH5B/C in vivo.". J. Biol. Chem. 279 (40): 42169–81. doi:10.1074/jbc.M403362200. PMID 15280377. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129.