UBE2D1

Ubiquitin-conjugating enzyme E2 D1 is a protein that in humans is encoded by the UBE2D1 gene.[5][6][7]

UBE2D1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesUBE2D1, E2(17)KB1, SFT, UBC4/5, UBCH5, UBCH5A, ubiquitin conjugating enzyme E2 D1
External IDsOMIM: 602961 MGI: 2384911 HomoloGene: 20714 GeneCards: UBE2D1
EC number2.3.2.24
Gene location (Human)
Chr.Chromosome 10 (human)[1]
Band10q21.1Start58,334,979 bp[1]
End58,370,751 bp[1]
RNA expression pattern


More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

7321

216080

Ensembl

ENSG00000072401

ENSMUSG00000019927

UniProt

P51668

P61080

RefSeq (mRNA)

NM_003338
NM_001204880

NM_145420

RefSeq (protein)

NP_001191809
NP_003329

NP_663395

Location (UCSC)Chr 10: 58.33 – 58.37 MbChr 10: 71.25 – 71.29 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

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.[7]

Interactions

UBE2D1 has been shown to interact with:

References

  1. GRCh38: Ensembl release 89: ENSG00000072401 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000019927 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 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. S2CID 3059748.
  6. 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.
  7. "Entrez Gene: UBE2D1 ubiquitin-conjugating enzyme E2D 1 (UBC4/5 homolog, yeast)".
  8. 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.
  9. 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.
  10. 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.
  11. 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.
  12. 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.
  13. 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.
  14. 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.
  15. 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.
  16. 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.
  17. 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.
  18. 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.
  19. 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

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