UBE2L3

From Wikipedia, the free encyclopedia
Ubiquitin-conjugating enzyme E2L 3

PDB rendering based on 1c4z.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsUBE2L3; E2-F1; L-UBC; UBCH7; UbcM4
External IDsOMIM: 603721 MGI: 109240 HomoloGene: 43226 GeneCards: UBE2L3 Gene
EC number6.3.2.19
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez733222195
EnsemblENSG00000185651ENSMUSG00000038965
UniProtP68036P68037
RefSeq (mRNA)NM_001256355NM_009456
RefSeq (protein)NP_001243284NP_033482
Location (UCSC)Chr 22:
21.9 – 21.98 Mb		Chr 16:
17.15 – 17.2 Mb
PubMed search
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Ubiquitin-conjugating enzyme E2 L3 is a protein that in humans is encoded by the UBE2L3 gene.[1][2][3]

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.[3]

Interactions

UBE2L3 has been shown to interact with UBOX5,[4] ARIH1,[5][6][7] Cbl gene,[8][9][10] UBE3A[11][12][13] and NEDD4.[11][14]

References

  1. ↑ Moynihan TP, Ardley HC, Leek JP, Thompson J, Brindle NS, Markham AF, Robinson PA (October 1996). "Characterization of a human ubiquitin-conjugating enzyme gene UBE2L3". Mamm Genome 7 (7): 520–5. doi:10.1007/s003359900155. PMID 8672131. 
  2. ↑ Moynihan TP, Cole CG, Dunham I, O'Neil L, Markham AF, Robinson PA (September 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. 
  3. ↑ 3.0 3.1 "Entrez Gene: UBE2L3 ubiquitin-conjugating enzyme E2L 3". 
  4. ↑ Pringa, E; Martinez-Noel G, Muller U, Harbers K (June 2001). "Interaction of the ring finger-related U-box motif of a nuclear dot protein with ubiquitin-conjugating enzymes". J. Biol. Chem. (United States) 276 (22): 19617–23. doi:10.1074/jbc.M100192200. ISSN 0021-9258. PMID 11274149. 
  5. ↑ Tan, Nancy G S; Ardley Helen C, Scott Gina B, Rose Stephen A, Markham Alexander F, Robinson Philip A (November 2003). "Human homologue of ariadne promotes the ubiquitylation of translation initiation factor 4E homologous protein, 4EHP". FEBS Lett. (Netherlands) 554 (3): 501–4. doi:10.1016/S0014-5793(03)01235-3. ISSN 0014-5793. PMID 14623119. 
  6. ↑ Moynihan, T P; Ardley H C, Nuber U, Rose S A, Jones P F, Markham A F, Scheffner M, Robinson P A (October 1999). "The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with RING finger/IBR motif-containing domains of HHARI and H7-AP1". J. Biol. Chem. (UNITED STATES) 274 (43): 30963–8. doi:10.1074/jbc.274.43.30963. ISSN 0021-9258. PMID 10521492. 
  7. ↑ Ardley, H C; Tan N G, Rose S A, Markham A F, Robinson P A (June 2001). "Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, Ubch7". J. Biol. Chem. (United States) 276 (22): 19640–7. doi:10.1074/jbc.M011028200. ISSN 0021-9258. PMID 11278816. 
  8. ↑ Yokouchi, M; Kondo T, Houghton A, Bartkiewicz M, Horne W C, Zhang H, Yoshimura A, Baron R (October 1999). "Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7". J. Biol. Chem. (UNITED STATES) 274 (44): 31707–12. doi:10.1074/jbc.274.44.31707. ISSN 0021-9258. PMID 10531381. 
  9. ↑ Zheng, N; Wang P, Jeffrey P D, Pavletich N P (August 2000). "Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases". Cell (UNITED STATES) 102 (4): 533–9. doi:10.1016/S0092-8674(00)00057-X. ISSN 0092-8674. PMID 10966114. 
  10. ↑ Wong, Esther Sook Miin; Fong Chee Wai, Lim Jormay, Yusoff Permeen, Low Boon Chuan, Langdon Wallace Y, Guy Graeme R (September 2002). "Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling". EMBO J. (England) 21 (18): 4796–808. doi:10.1093/emboj/cdf493. ISSN 0261-4189. PMC 126289. PMID 12234920. 
  11. ↑ 11.0 11.1 Anan, T; Nagata Y, Koga H, Honda Y, Yabuki N, Miyamoto C, Kuwano A, Matsuda I, Endo F, Saya H, Nakao M (November 1998). "Human ubiquitin-protein ligase Nedd4: expression, subcellular localization and selective interaction with ubiquitin-conjugating enzymes". Genes Cells (ENGLAND) 3 (11): 751–63. doi:10.1046/j.1365-2443.1998.00227.x. ISSN 1356-9597. PMID 9990509. 
  12. ↑ Nuber, U; Schwarz S, Kaiser P, Schneider R, Scheffner M (February 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. (UNITED STATES) 271 (5): 2795–800. doi:10.1074/jbc.271.5.2795. ISSN 0021-9258. PMID 8576257. 
  13. ↑ Huang, L; Kinnucan E, Wang G, Beaudenon S, Howley P M, Huibregtse J M, Pavletich N P (November 1999). "Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade". Science (UNITED STATES) 286 (5443): 1321–6. doi:10.1126/science.286.5443.1321. ISSN 0036-8075. PMID 10558980. 
  14. ↑ Bruce, M Christine; Kanelis Voula, Fouladkou Fatemeh, Debonneville Anne, Staub Olivier, Rotin Daniela (October 2008). "Regulation of Nedd4-2 self-ubiquitination and stability by a PY motif located within its HECT-domain". Biochem. J. (England) 415 (1): 155–63. doi:10.1042/BJ20071708. PMID 18498246. 

Further reading

Chaperones/
protein folding
Heat shock proteins/
Chaperonins
Other
Protein targeting
Ubiquitin
Other
See also: posttranslational modification disorders
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)


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