UBE2D3

From Wikipedia, the free encyclopedia


Ubiquitin-conjugating enzyme E2D 3 (UBC4/5 homolog, yeast)
PDB rendering based on 1ur6.
Available structures: 1ur6, 1w4u, 1x23, 1z2u, 2c4o, 2esk, 2eso, 2esp, 2esq, 2fuh
Identifiers
Symbol(s) UBE2D3; UBC4/5; E2(17)KB3; MGC43926; MGC5416; UBCH5C
External IDs OMIM: 602963 MGI1913355 HomoloGene2506
Orthologs
Human Mouse
Entrez 7323 66105


Refseq NM_003340 (mRNA)
NP_003331 (protein)
NM_025356 (mRNA)
NP_079632 (protein)
Pubmed search [1] [2]

Ubiquitin-conjugating enzyme E2D 3 (UBC4/5 homolog, yeast), also known as UBE2D3, is a human gene.[1]

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.[1]

[edit] References

[edit] 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. PMID 8090726. 
  • Jensen JP, Bates PW, Yang M, et al. (1996). "Identification of a family of closely related human ubiquitin conjugating enzymes.". J. Biol. Chem. 270 (51): 30408–14. PMID 8530467. 
  • 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. 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. 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. 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. PMID 10835356. 
  • 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. PMID 11485561. 
  • 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. PMID 12477932. 
  • 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. PMID 12732733. 
  • 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. PMID 14562029. 
  • 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. 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. PMID 15489334. 
  • 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. PMID 16344560.