BRD2

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]

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
Orthologs
SpeciesHumanMouse
Entrez

6046

14312

Ensembl

ENSMUSG00000024335

UniProt

P25440

Q7JJ13

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

Early descriptions demonstrated that BRD2 gene product is a mitogen-activated kinase which localizes to the nucleus. The gene maps to the major histocompatibility complex (MHC) class II region on chromosome 6p21.3 but sequence comparison suggests that the protein is not involved in the immune response. Homology to the Drosophila gene female sterile homeotic suggests that this human gene may be part of a signal transduction pathway involved in growth control.[7]

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. ENSG00000234507, ENSG00000230678, ENSG00000204256, ENSG00000235307, ENSG00000236227, ENSG00000234704 GRCh38: Ensembl release 89: ENSG00000215077, ENSG00000234507, ENSG00000230678, ENSG00000204256, ENSG00000235307, ENSG00000236227, ENSG00000234704 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000024335 - 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. 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. S2CID 44613743.
  7. "BRD2 bromodomain containing 2 [ Homo sapiens (human) ]".
  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. 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 (18): 2825–34. doi:10.1182/blood-2014-10-607309. PMC 4424630. 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. United States. 16 (8): 1727–37. doi:10.1210/me.2001-0353. ISSN 0888-8809. PMID 12145330.
  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. UNITED STATES. 11 (8): 417–24. ISSN 1044-9523. PMC 3968681. PMID 10965846.

Further reading


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