UBE2L3
Ubiquitin-conjugating enzyme E2L 3 | |||||||||||||
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File:PBB Protein UBE2L3 image.jpg PDB rendering based on 1c4z. | |||||||||||||
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Identifiers | |||||||||||||
Symbols | UBE2L3 ; L-UBC; E2-F1; UBCH7; UbcM4 | ||||||||||||
External IDs | Template:OMIM5 Template:MGI HomoloGene: 43226 | ||||||||||||
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RNA expression pattern | |||||||||||||
File:PBB GE UBE2L3 200682 s at tn.png | |||||||||||||
File:PBB GE UBE2L3 200676 s at tn.png | |||||||||||||
File:PBB GE UBE2L3 200683 s at tn.png | |||||||||||||
More reference expression data | |||||||||||||
Orthologs | |||||||||||||
Template:GNF Ortholog box | |||||||||||||
Species | Human | Mouse | |||||||||||
Entrez | n/a | n/a | |||||||||||
Ensembl | n/a | n/a | |||||||||||
UniProt | n/a | n/a | |||||||||||
RefSeq (mRNA) | n/a | n/a | |||||||||||
RefSeq (protein) | n/a | n/a | |||||||||||
Location (UCSC) | n/a | n/a | |||||||||||
PubMed search | n/a | n/a |
Ubiquitin-conjugating enzyme E2L 3, also known as UBE2L3, 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 (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is demonstrated to participate in the ubiquitination of p53, c-Fos, and the NF-kB precursor p105 in vitro. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.[1]
References
Further reading
- Blumenfeld N, Gonen H, Mayer A; et al. (1994). "Purification and characterization of a novel species of ubiquitin-carrier protein, E2, that is involved in degradation of non-"N-end rule" protein substrates". J. Biol. Chem. 269 (13): 9574–81. PMID 8144544.
- Robinson PA, Leek JP, Thompson J; et al. (1996). "A human ubiquitin conjugating enzyme, L-UBC, maps in the Alzheimer's disease locus on chromosome 14q24.3". Mamm. Genome. 6 (10): 725–31. PMID 8563171.
- Nuber U, Schwarz S, Kaiser P; et al. (1996). "Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5". J. Biol. Chem. 271 (5): 2795–800. PMID 8576257.
- Moynihan TP, Ardley HC, Leek JP; et al. (1996). "Characterization of a human ubiquitin-conjugating enzyme gene UBE2L3". Mamm. Genome. 7 (7): 520–5. PMID 8672131.
- Kumar S, Kao WH, Howley PM (1997). "Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativity". J. Biol. Chem. 272 (21): 13548–54. PMID 9153201.
- Moynihan TP, Cole CG, Dunham I; et al. (1998). "Fine-mapping, genomic organization, and transcript analysis of the human ubiquitin-conjugating enzyme gene UBE2L3". Genomics. 51 (1): 124–7. doi:10.1006/geno.1998.5257. PMID 9693040.
- 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.
- Martinez-Noel G, Niedenthal R, Tamura T, Harbers K (1999). "A family of structurally related RING finger proteins interacts specifically with the ubiquitin-conjugating enzyme UbcM4". FEBS Lett. 454 (3): 257–61. PMID 10431818.
- Moynihan TP, Ardley HC, Nuber U; et al. (1999). "The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with RING finger/IBR motif-containing domains of HHARI and H7-AP1". J. Biol. Chem. 274 (43): 30963–8. PMID 10521492.
- Yokouchi M, Kondo T, Houghton A; et al. (1999). "Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7". J. Biol. Chem. 274 (44): 31707–12. PMID 10531381.
- Huang L, Kinnucan E, Wang G; et al. (1999). "Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade". Science. 286 (5443): 1321–6. PMID 10558980.
- Ardley HC, Moynihan TP, Markham AF, Robinson PA (2000). "Promoter analysis of the human ubiquitin-conjugating enzyme gene family UBE2L1-4, including UBE2L3 which encodes UbcH7". Biochim. Biophys. Acta. 1491 (1–3): 57–64. PMID 10760570.
- Zheng N, Wang P, Jeffrey PD, Pavletich NP (2000). "Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases". Cell. 102 (4): 533–9. PMID 10966114.
- Zhang Y, Gao J, Chung KK; et al. (2001). "Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1". Proc. Natl. Acad. Sci. U.S.A. 97 (24): 13354–9. doi:10.1073/pnas.240347797. PMID 11078524.
- Niwa J, Ishigaki S, Doyu M; et al. (2001). "A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase activity". Biochem. Biophys. Res. Commun. 281 (3): 706–13. doi:10.1006/bbrc.2001.4414. PMID 11237715.
- Pringa E, Martinez-Noel G, Muller U, Harbers K (2001). "Interaction of the ring finger-related U-box motif of a nuclear dot protein with ubiquitin-conjugating enzymes". J. Biol. Chem. 276 (22): 19617–23. doi:10.1074/jbc.M100192200. PMID 11274149.
- Ardley HC, Tan NG, Rose SA; et al. (2001). "Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, Ubch7". J. Biol. Chem. 276 (22): 19640–7. doi:10.1074/jbc.M011028200. PMID 11278816.
- 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.
- Wong ES, Fong CW, Lim J; et al. (2002). "Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling". EMBO J. 21 (18): 4796–808. PMID 12234920.
- 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.
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