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 MGI: 1913355 HomoloGene: 2506 | ||||||||||
|
|||||||||||
| 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:. 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:. 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:. 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:. 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:. 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:. 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:. 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:. 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:. 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:. 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:. 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:. 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:. PMID 16344560.

