Ubiquitin-conjugating enzyme E2E 3 (UBC4/5 homolog, yeast), also known as UBE2E3, is a human gene.cite web | title = Entrez Gene: UBE2E3 ubiquitin-conjugating enzyme E2E 3 (UBC4/5 homolog, yeast)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10477| accessdate = ]

section_title =
summary_text = 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. The encoded protein shares 100% sequence identity with the mouse and rat counterparts, which indicates that this enzyme is highly conserved in eukaryotes. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.cite web | title = Entrez Gene: UBE2E3 ubiquitin-conjugating enzyme E2E 3 (UBC4/5 homolog, yeast)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10477| accessdate = ]


Further reading

citations =
*cite journal | author=Hay RT, Vuillard L, Desterro JM, Rodriguez MS |title=Control of NF-kappa B transcriptional activation by signal induced proteolysis of I kappa B alpha. |journal=Philos. Trans. R. Soc. Lond., B, Biol. Sci. |volume=354 |issue= 1389 |pages= 1601–9 |year= 2000 |pmid= 10582246 |doi= 10.1098/rstb.1999.0504
*cite journal | author=Desterro JM, Thomson J, Hay RT |title=Ubch9 conjugates SUMO but not ubiquitin. |journal=FEBS Lett. |volume=417 |issue= 3 |pages= 297–300 |year= 1998 |pmid= 9409737 |doi=
*cite journal | author=Desterro JM, Rodriguez MS, Hay RT |title=SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation. |journal=Mol. Cell |volume=2 |issue= 2 |pages= 233–9 |year= 1998 |pmid= 9734360 |doi=
*cite journal | author=Desterro JM, Rodriguez MS, Kemp GD, Hay RT |title=Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1. |journal=J. Biol. Chem. |volume=274 |issue= 15 |pages= 10618–24 |year= 1999 |pmid= 10187858 |doi=
*cite journal | author=Ito K, Kato S, Matsuda Y, "et al." |title=cDNA cloning, characterization, and chromosome mapping of UBE2E3 (alias UbcH9), encoding an N-terminally extended human ubiquitin-conjugating enzyme. |journal=Cytogenet. Cell Genet. |volume=84 |issue= 1-2 |pages= 99–104 |year= 1999 |pmid= 10343118 |doi=
*cite journal | author=Zhang QH, Ye M, Wu XY, "et al." |title=Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. |journal=Genome Res. |volume=10 |issue= 10 |pages= 1546–60 |year= 2001 |pmid= 11042152 |doi=
*cite journal | author=Pringa E, Martinez-Noel G, Muller U, Harbers K |title=Interaction of the ring finger-related U-box motif of a nuclear dot protein with ubiquitin-conjugating enzymes. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 19617–23 |year= 2001 |pmid= 11274149 |doi= 10.1074/jbc.M100192200
*cite journal | author=Ito K, Adachi S, Iwakami R, "et al." |title=N-Terminally extended human ubiquitin-conjugating enzymes (E2s) mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8. |journal=Eur. J. Biochem. |volume=268 |issue= 9 |pages= 2725–32 |year= 2001 |pmid= 11322894 |doi=
*cite journal | author=Plafker SM, Macara IG |title=Ribosomal protein L12 uses a distinct nuclear import pathway mediated by importin 11. |journal=Mol. Cell. Biol. |volume=22 |issue= 4 |pages= 1266–75 |year= 2002 |pmid= 11809816 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Lehner B, Semple JI, Brown SE, "et al." |title=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. |journal=Genomics |volume=83 |issue= 1 |pages= 153–67 |year= 2004 |pmid= 14667819 |doi=
*cite journal | author=Beausoleil SA, Jedrychowski M, Schwartz D, "et al." |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Plafker SM, Plafker KS, Weissman AM, Macara IG |title=Ubiquitin charging of human class III ubiquitin-conjugating enzymes triggers their nuclear import. |journal=J. Cell Biol. |volume=167 |issue= 4 |pages= 649–59 |year= 2005 |pmid= 15545318 |doi= 10.1083/jcb.200406001
*cite journal | author=Barrios-Rodiles M, Brown KR, Ozdamar B, "et al." |title=High-throughput mapping of a dynamic signaling network in mammalian cells. |journal=Science |volume=307 |issue= 5715 |pages= 1621–5 |year= 2005 |pmid= 15761153 |doi= 10.1126/science.1105776
*cite journal | author=Hillier LW, Graves TA, Fulton RS, "et al." |title=Generation and annotation of the DNA sequences of human chromosomes 2 and 4. |journal=Nature |volume=434 |issue= 7034 |pages= 724–31 |year= 2005 |pmid= 15815621 |doi= 10.1038/nature03466
*cite journal | author=Rual JF, Venkatesan K, Hao T, "et al." |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209
*cite journal | author=Lim J, Hao T, Shaw C, "et al." |title=A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration. |journal=Cell |volume=125 |issue= 4 |pages= 801–14 |year= 2006 |pmid= 16713569 |doi= 10.1016/j.cell.2006.03.032

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