UBE2L3

Ubiquitin-conjugating enzyme E2L 3
PDB rendering based on 1c4z.
Available structures PDB PDBe, RCSB
Identifiers
Symbols	UBE2L3; E2-F1; L-UBC; UBCH7; UbcM4
External IDs	OMIM: 603721 MGI: 109240 HomoloGene: 43226 GeneCards: UBE2L3 Gene
EC number	6.3.2.19
Gene Ontology Molecular function • nucleotide binding • transcription coactivator activity • ubiquitin-protein ligase activity • ubiquitin-protein ligase activity • ubiquitin-protein ligase activity • protein binding • ATP binding • ligase activity • acid-amino acid ligase activity • enzyme binding • ubiquitin protein ligase binding Cellular component • ubiquitin ligase complex • nucleus • cytoplasm Biological process • protein polyubiquitination • regulation of transcription, DNA-dependent • regulation of transcription, DNA-dependent • protein modification process • ubiquitin-dependent protein catabolic process • regulation of S phase of mitotic cell cycle • cell proliferation • protein ubiquitination • protein ubiquitination • protein ubiquitination • protein K11-linked ubiquitination • cellular response to steroid hormone stimulus • cellular response to glucocorticoid stimulus Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	7332	22195
Ensembl	ENSG00000185651	ENSMUSG00000038965
UniProt	P68036	Q3TIH9
RefSeq (mRNA)	NM_003347.2	NM_009456.2
RefSeq (protein)	NP_003338	NP_033482.1
Location (UCSC)	Chr 22: 21.9 – 21.98 Mb	Chr 16: 17.07 – 17.12 Mb
PubMed search	[1]	[2]

Ubiquitin-conjugating enzyme E2 L3 is a protein that in humans is encoded by the UBE2L3 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 (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-κB precursor p105 in vitro. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.

Interactions

UBE2L3 has been shown to interact with UBOX5, ARIH1, Cbl gene, UBE3A and NEDD4.

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. doi:10.1007/BF00354295. 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. doi:10.1074/jbc.271.5.2795. PMID 8576257. 
• 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. doi:10.1074/jbc.272.21.13548. PMID 9153201. 
• 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. 
• 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. doi:10.1016/S0014-5793(99)00823-6. 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. doi:10.1074/jbc.274.43.30963. 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. doi:10.1074/jbc.274.44.31707. 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. doi:10.1126/science.286.5443.1321. 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. doi:10.1016/S0092-8674(00)00057-X. 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. PMC 27228. PMID 11078524. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=27228. 
• 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. doi:10.1093/emboj/cdf493. PMC 126289. PMID 12234920. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=126289. 
• 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.