UBE2L3

From Wikipedia, the free encyclopedia

Ubiquitin-conjugating enzyme E2L 3

PDB rendering based on 1c4z.

Available structures: 1c4z, 1fbv

Identifiers

Symbol(s)

UBE2L3; L-UBC; E2-F1; UBCH7; UbcM4

External IDs

OMIM: 603721 MGI: 109240 HomoloGene: 43226

Gene ontology
Molecular Function:	• ubiquitin-protein ligase activity • ligase activity • enzyme binding
Cellular Component:	• ubiquitin ligase complex
Biological Process:	• ubiquitin-dependent protein catabolic process • ubiquitin cycle

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003347 (mRNA)
NP_003338 (protein)

NM_009456 (mRNA)
NP_033482 (protein)

Location

Chr 22: 20.25 - 20.31 Mb

Chr 16: 17.07 - 17.12 Mb

Pubmed search

[1]

[2]

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]

[edit] References

^ ^a ^b Entrez Gene: UBE2L3 ubiquitin-conjugating enzyme E2L 3.

[edit] 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.