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BRD2

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BRD2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesBRD2, D6S113E, FSH, FSRG1, NAT, RING3, RNF3, O27.1.1, bromodomain containing 2, BRD2-IT1
External IDsOMIM: 601540; MGI: 99495; HomoloGene: 74540; GeneCards: BRD2; OMA:BRD2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001113182
NM_001199455
NM_001199456
NM_001291986
NM_005104

NM_001025387
NM_001204973
NM_010238

RefSeq (protein)

NP_001106653
NP_001186384
NP_001186385
NP_001278915
NP_005095

NP_001191902
NP_034368

Location (UCSC)Chr 6: 32.97 – 32.98 MbChr 17: 34.33 – 34.34 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Bromodomain-containing protein 2 is a protein that in humans is encoded by the BRD2 gene. BRD2 is part of the Bromodomain and Extra-Terminal motif (BET) protein family that also contains BRD3, BRD4, and BRDT in mammals [5][6][7]

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Functions

  • BRD2 has been implicated in cancer.[5][8]
  • BRD2 loss in mice causes obesity without diabetes for unknown reasons.[5]
  • BRD2 may have functional overlap with close homolog BRD3.[9]
  • BRD2 function is blocked by BET inhibitors.

Interactions

BRD2 has been shown to interact with E2F2,[10][11] and many transcription factors including GATA1.[9]

References

  1. ^ a b c ENSG00000234507, ENSG00000230678, ENSG00000204256, ENSG00000235307, ENSG00000236227, ENSG00000234704 GRCh38: Ensembl release 89: ENSG00000215077, ENSG00000234507, ENSG00000230678, ENSG00000204256, ENSG00000235307, ENSG00000236227, ENSG00000234704Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024335Ensembl, 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. ^ a b c Belkina, A. C.; Denis, G. V. (2012). "BET domain co-regulators in obesity, inflammation and cancer". Nature Reviews Cancer. 12 (7): 465–77. doi:10.1038/nrc3256. PMC 3934568. PMID 22722403.
  6. ^ Thorpe KL, Abdulla S, Kaufman J, Trowsdale J, Beck S (October 1996). "Phylogeny and structure of the RING3 gene". Immunogenetics. 44 (5): 391–6. doi:10.1007/BF02602785. PMID 8781126.
  7. ^ "Entrez Gene: BRD2 bromodomain containing 2".
  8. ^ Shi, J; Vakoc, C. R. (2014). "The mechanisms behind the therapeutic activity of BET bromodomain inhibition". Molecular Cell. 54 (5): 728–36. doi:10.1016/j.molcel.2014.05.016. PMC 4236231. PMID 24905006.
  9. ^ a b Stonestrom, A. J.; Hsu, S. C.; Jahn, K. S.; Huang, P; Keller, C. A.; Giardine, B. M.; Kadauke, S; Campbell, A. E.; Evans, P; Hardison, R. C.; Blobel, G. A. (2015). "Functions of BET proteins in erythroid gene expression". Blood. 125: 2825–34. doi:10.1182/blood-2014-10-607309. PMID 25696920.
  10. ^ Crowley, Thomas E; Kaine Emily M; Yoshida Manabu; Nandi Anindita; Wolgemuth Debra J (August 2002). "Reproductive cycle regulation of nuclear import, euchromatic localization, and association with components of Pol II mediator of a mammalian double-bromodomain protein". Mol. Endocrinol. 16 (8). United States: 1727–37. doi:10.1210/me.2001-0353. ISSN 0888-8809. PMID 12145330. {{cite journal}}: Cite has empty unknown parameters: |laydate=, |laysource=, and |laysummary= (help)
  11. ^ Denis, G V; Vaziri C; Guo N; Faller D V (August 2000). "RING3 kinase transactivates promoters of cell cycle regulatory genes through E2F". Cell Growth Differ. 11 (8). UNITED STATES: 417–24. ISSN 1044-9523. PMC 3968681. PMID 10965846. {{cite journal}}: Cite has empty unknown parameters: |laysummary=, |laydate=, and |laysource= (help)

Further reading

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