UBE2D1

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Ubiquitin-conjugating enzyme E2D 1
Protein UBE2D1 PDB 2c4p.png
PDB rendering based on 2c4p.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols UBE2D1 ; E2(17)KB1; SFT; UBC4/5; UBCH5; UBCH5A
External IDs OMIM602961 MGI2384911 HomoloGene20714 GeneCards: UBE2D1 Gene
EC number 6.3.2.19
RNA expression pattern
PBB GE UBE2D1 214590 s at tn.png
PBB GE UBE2D1 211764 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 7321 216080
Ensembl ENSG00000072401 ENSMUSG00000019927
UniProt P51668 P61080
RefSeq (mRNA) NM_001204880 NM_145420
RefSeq (protein) NP_001191809 NP_663395
Location (UCSC) Chr 10:
58.33 – 58.37 Mb
Chr 10:
71.25 – 71.29 Mb
PubMed search [1] [2]

Ubiquitin-conjugating enzyme E2 D1 is a protein that in humans is encoded by the UBE2D1 gene.[1][2][3]

Function[edit]

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[edit]

UBE2D1 has been shown to interact with:

References[edit]

  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. ^ a b "Entrez Gene: UBE2D1 ubiquitin-conjugating enzyme E2D 1 (UBC4/5 homolog, yeast)". 
  4. ^ a b Mallery DL, Vandenberg CJ, Hiom K (Dec 2002). "Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains". EMBO J. 21 (24): 6755–62. doi:10.1093/emboj/cdf691. PMC 139111. PMID 12485996. 
  5. ^ a b Kentsis A, Gordon RE, Borden KL (November 2002). "Control of biochemical reactions through supramolecular RING domain self-assembly". Proc. Natl. Acad. Sci. U.S.A. 99 (24): 15404–9. doi:10.1073/pnas.202608799. PMC 137729. PMID 12438698. 
  6. ^ a b Chen A, Kleiman FE, Manley JL, Ouchi T, Pan ZQ (June 2002). "Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase". J. Biol. Chem. 277 (24): 22085–92. doi:10.1074/jbc.M201252200. PMID 11927591. 
  7. ^ a b Dong Y, Hakimi MA, Chen X, Kumaraswamy E, Cooch NS, Godwin AK, Shiekhattar R (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 12 (5): 1087–99. doi:10.1016/s1097-2765(03)00424-6. PMID 14636569. 
  8. ^ a b Sato K, Hayami R, Wu W, Nishikawa T, Nishikawa H, Okuda Y, Ogata H, Fukuda M, Ohta T (July 2004). "Nucleophosmin/B23 is a candidate substrate for the BRCA1-BARD1 ubiquitin ligase". J. Biol. Chem. 279 (30): 30919–22. doi:10.1074/jbc.C400169200. PMID 15184379. 
  9. ^ a b Wu-Baer F, Lagrazon K, Yuan W, Baer R (September 2003). "The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin". J. Biol. Chem. 278 (37): 34743–6. doi:10.1074/jbc.C300249200. PMID 12890688. 
  10. ^ a b Vandenberg CJ, Gergely F, Ong CY, Pace P, Mallery DL, Hiom K, Patel KJ (July 2003). "BRCA1-independent ubiquitination of FANCD2". Mol. Cell 12 (1): 247–54. doi:10.1016/s1097-2765(03)00281-8. PMID 12887909. 
  11. ^ a b 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. 276 (18): 14537–40. doi:10.1074/jbc.C000881200. PMID 11278247. 
  12. ^ Brzovic PS, Keeffe JR, Nishikawa H, Miyamoto K, Fox D, Fukuda M, Ohta T, Klevit R (May 2003). "Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex". Proc. Natl. Acad. Sci. U.S.A. 100 (10): 5646–51. doi:10.1073/pnas.0836054100. PMC 156255. PMID 12732733. 
  13. ^ Nishikawa H, Ooka S, Sato K, Arima K, Okamoto J, Klevit RE, Fukuda M, Ohta T (February 2004). "Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase". J. Biol. Chem. 279 (6): 3916–24. doi:10.1074/jbc.M308540200. PMID 14638690. 
  14. ^ 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. 271 (5): 2795–800. doi:10.1074/jbc.271.5.2795. PMID 8576257. 
  15. ^ 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. 274 (11): 7576–82. doi:10.1074/jbc.274.11.7576. PMID 10066826. 

Further reading[edit]