UBE2D1

From Wikipedia, the free encyclopedia
Ubiquitin-conjugating enzyme E2D 1

PDB rendering based on 2c4p.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsUBE2D1; E2(17)KB1; SFT; UBC4/5; UBCH5; UBCH5A
External IDsOMIM: 602961 MGI: 2384911 HomoloGene: 20714 GeneCards: UBE2D1 Gene
EC number6.3.2.19
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez7321216080
EnsemblENSG00000072401ENSMUSG00000019927
UniProtP51668P61080
RefSeq (mRNA)NM_001204880NM_145420
RefSeq (protein)NP_001191809NP_663395
Location (UCSC)Chr 10:
60.09 – 60.13 Mb
Chr 10:
71.25 – 71.29 Mb
PubMed search

Ubiquitin-conjugating enzyme E2 D1 is a protein that in humans is encoded by the UBE2D1 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, 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. This enzyme is closely related to a stimulator of iron transport (SFT), and is up-regulated in hereditary hemochromatosis. It also functions in the ubiquitination of the tumor-suppressor protein p53 and the hypoxia-inducible transcription factor HIF1alpha by interacting with the E1 ubiquitin-activating enzyme and the E3 ubiquitin-protein ligases.[3]

Interactions

UBE2D1 has been shown to interact with BARD1,[4][5][6][7][8][9][10][11] UBE3A[12][13] and BRCA1.[4][5][6][7][8][9][10][11][14][15]

References

  1. Robinson PA, Leek JP, Ardley HC, Thompson J, Rose SA, Markham AF (March 1999). "Assignment of UBE2D1 to human chromosome bands 10q11.2→q21 by in situ hybridization". Cytogenet Cell Genet 83 (3–4): 247–8. doi:10.1159/000015195. PMID 10072594. 
  2. Jensen JP, Bates PW, Yang M, Vierstra RD, Weissman AM (January 1996). "Identification of a family of closely related human ubiquitin conjugating enzymes". J Biol Chem 270 (51): 30408–14. doi:10.1074/jbc.270.51.30408. PMID 8530467. 
  3. 3.0 3.1 "Entrez Gene: UBE2D1 ubiquitin-conjugating enzyme E2D 1 (UBC4/5 homolog, yeast)". 
  4. 4.0 4.1 Mallery, Donna L; Vandenberg Cassandra J, Hiom Kevin (Dec 2002). "Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains". EMBO J. (England) 21 (24): 6755–62. doi:10.1093/emboj/cdf691. ISSN 0261-4189. PMC 139111. PMID 12485996. 
  5. 5.0 5.1 Kentsis, Alex; Gordon Ronald E, Borden Katherine L B (November 2002). "Control of biochemical reactions through supramolecular RING domain self-assembly". Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (24): 15404–9. doi:10.1073/pnas.202608799. ISSN 0027-8424. PMC 137729. PMID 12438698. 
  6. 6.0 6.1 Chen, Angus; Kleiman Frida E, Manley James L, Ouchi Toru, Pan Zhen-Qiang (June 2002). "Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase". J. Biol. Chem. (United States) 277 (24): 22085–92. doi:10.1074/jbc.M201252200. ISSN 0021-9258. PMID 11927591. 
  7. 7.0 7.1 Dong, Yuanshu; Hakimi Mohamed-Ali, Chen Xiaowei, Kumaraswamy Easwari, Cooch Neil S, Godwin Andrew K, Shiekhattar Ramin (November 2003). "Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a signalosome-like subunit and its role in DNA repair". Mol. Cell (United States) 12 (5): 1087–99. doi:10.1016/S1097-2765(03)00424-6. ISSN 1097-2765. PMID 14636569. 
  8. 8.0 8.1 Sato, Ko; Hayami Ryosuke, Wu Wenwen, Nishikawa Toru, Nishikawa Hiroyuki, Okuda Yoshiko, Ogata Haruki, Fukuda Mamoru, Ohta Tomohiko (July 2004). "Nucleophosmin/B23 is a candidate substrate for the BRCA1-BARD1 ubiquitin ligase". J. Biol. Chem. (United States) 279 (30): 30919–22. doi:10.1074/jbc.C400169200. ISSN 0021-9258. PMID 15184379. 
  9. 9.0 9.1 Wu-Baer, Foon; Lagrazon Karen, Yuan Wei, Baer Richard (September 2003). "The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin". J. Biol. Chem. (United States) 278 (37): 34743–6. doi:10.1074/jbc.C300249200. ISSN 0021-9258. PMID 12890688. 
  10. 10.0 10.1 Vandenberg, Cassandra J; Gergely Fanni, Ong Chong Yi, Pace Paul, Mallery Donna L, Hiom Kevin, Patel Ketan J (July 2003). "BRCA1-independent ubiquitination of FANCD2". Mol. Cell (United States) 12 (1): 247–54. doi:10.1016/S1097-2765(03)00281-8. ISSN 1097-2765. PMID 12887909. 
  11. 11.0 11.1 Hashizume, R; Fukuda M, Maeda I, Nishikawa H, Oyake D, Yabuki Y, Ogata H, Ohta T (May 2001). "The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation". J. Biol. Chem. (United States) 276 (18): 14537–40. doi:10.1074/jbc.C000881200. ISSN 0021-9258. PMID 11278247. 
  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. Nuber, U; Scheffner M (March 1999). "Identification of determinants in E2 ubiquitin-conjugating enzymes required for hect E3 ubiquitin-protein ligase interaction". J. Biol. Chem. (UNITED STATES) 274 (11): 7576–82. doi:10.1074/jbc.274.11.7576. ISSN 0021-9258. PMID 10066826. 
  14. Brzovic, Peter S; Keeffe Jennifer R, Nishikawa Hiroyuki, Miyamoto Keiko, Fox David, Fukuda Mamoru, Ohta Tomohiko, Klevit Rachel (May 2003). "Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex". Proc. Natl. Acad. Sci. U.S.A. (United States) 100 (10): 5646–51. doi:10.1073/pnas.0836054100. ISSN 0027-8424. PMC 156255. PMID 12732733. 
  15. Nishikawa, Hiroyuki; Ooka Seido, Sato Ko, Arima Kei, Okamoto Joji, Klevit Rachel E, Fukuda Mamoru, Ohta Tomohiko (February 2004). "Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase". J. Biol. Chem. (United States) 279 (6): 3916–24. doi:10.1074/jbc.M308540200. ISSN 0021-9258. PMID 14638690. 

Further reading


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