UBE2D1

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Ubiquitin-conjugating enzyme E2D 1 (UBC4/5 homolog, yeast)
File:PBB Protein UBE2D1 image.jpg
PDB rendering based on 2c4p.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols UBE2D1 ; E2(17)KB1; SFT; UBC4/5; UBCH5; UBCH5A
External IDs Template:OMIM5 Template:MGI HomoloGene20714
RNA expression pattern
File:PBB GE UBE2D1 214590 s at tn.png
File:PBB GE UBE2D1 211764 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Ubiquitin-conjugating enzyme E2D 1 (UBC4/5 homolog, yeast), also known as UBE2D1, 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, 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.[1]

References

  1. 1.0 1.1 "Entrez Gene: UBE2D1 ubiquitin-conjugating enzyme E2D 1 (UBC4/5 homolog, yeast)".

Further reading

  • Scheffner M, Huibregtse JM, Howley PM (1994). "Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53". Proc. Natl. Acad. Sci. U.S.A. 91 (19): 8797–801. PMID 8090726.
  • Jensen JP, Bates PW, Yang M; et al. (1996). "Identification of a family of closely related human ubiquitin conjugating enzymes". J. Biol. Chem. 270 (51): 30408–14. PMID 8530467.
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. PMID 8889548.
  • Hatakeyama S, Jensen JP, Weissman AM (1997). "Subcellular localization and ubiquitin-conjugating enzyme (E2) interactions of mammalian HECT family ubiquitin protein ligases". J. Biol. Chem. 272 (24): 15085–92. PMID 9182527.
  • Gutierrez JA, Yu J, Rivera S, Wessling-Resnick M (1997). "Functional expression cloning and characterization of SFT, a stimulator of Fe transport". J. Cell Biol. 139 (4): 895–905. PMID 9362508.
  • Gutierrez JA, Yu J, Wessling-Resnick M (1999). "Characterization and chromosomal mapping of the human gene for SFT, a stimulator of Fe transport". Biochem. Biophys. Res. Commun. 253 (3): 739–42. doi:10.1006/bbrc.1998.9836. PMID 9918797.
  • Nuber U, Scheffner M (1999). "Identification of determinants in E2 ubiquitin-conjugating enzymes required for hect E3 ubiquitin-protein ligase interaction". J. Biol. Chem. 274 (11): 7576–82. PMID 10066826.
  • Robinson PA, Leek JP, Ardley HC; et al. (1999). "Assignment of UBE2D1 to human chromosome bands 10q11.2-->q21 by in situ hybridization". Cytogenet. Cell Genet. 83 (3–4): 247–8. PMID 10072594.
  • Kamura T, Sato S, Iwai K; et al. (2000). "Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex". Proc. Natl. Acad. Sci. U.S.A. 97 (19): 10430–5. doi:10.1073/pnas.190332597. PMID 10973499.
  • 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.
  • Hashizume R, Fukuda M, Maeda I; et al. (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.
  • Matsuzawa SI, Reed JC (2001). "Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses". Mol. Cell. 7 (5): 915–26. PMID 11389839.
  • Jiang J, Ballinger CA, Wu Y; et al. (2001). "CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation". J. Biol. Chem. 276 (46): 42938–44. doi:10.1074/jbc.M101968200. PMID 11557750.
  • Chen A, Kleiman FE, Manley JL; et al. (2002). "Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase". J. Biol. Chem. 277 (24): 22085–92. doi:10.1074/jbc.M201252200. PMID 11927591.
  • Badciong JC, Haas AL (2003). "MdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination". J. Biol. Chem. 277 (51): 49668–75. doi:10.1074/jbc.M208593200. PMID 12393902.
  • Kentsis A, Gordon RE, Borden KL (2003). "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. PMID 12438698.
  • 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.
  • Gehrke SG, Riedel HD, Herrmann T; et al. (2003). "UbcH5A, a member of human E2 ubiquitin-conjugating enzymes, is closely related to SFT, a stimulator of iron transport, and is up-regulated in hereditary hemochromatosis". Blood. 101 (8): 3288–93. doi:10.1182/blood-2002-07-2192. PMID 12480712.
  • Mallery DL, Vandenberg CJ, Hiom K (2004). "Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains". EMBO J. 21 (24): 6755–62. PMID 12485996.
  • Takeyama K, Aguiar RC, Gu L; et al. (2003). "The BAL-binding protein BBAP and related Deltex family members exhibit ubiquitin-protein isopeptide ligase activity". J. Biol. Chem. 278 (24): 21930–7. doi:10.1074/jbc.M301157200. PMID 12670957.

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