BRD2

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BRD2
Protein BRD2 PDB 1x0j.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases BRD2, D6S113E, FSH, FSRG1, NAT, RING3, RNF3, O27.1.1, bromodomain containing 2
External IDs MGI: 99495 HomoloGene: 74540 GeneCards: BRD2
RNA expression pattern
PBB GE BRD2 214911 s at fs.png

PBB GE BRD2 208685 x at fs.png

PBB GE BRD2 208686 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
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_001191902.1
NP_034368.2
NP_001191902
NP_034368

Location (UCSC) Chr 6: 32.97 – 32.98 Mb Chr 17: 34.11 – 34.12 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/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 [3][4][5]

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.[5]

Functions[edit]

  • BRD2 has been implicated in cancer.[3][6]
  • BRD2 loss in mice causes obesity without diabetes for unknown reasons.[3]
  • BRD2 may have functional overlap with close homolog BRD3.[7]
  • BRD2 function is blocked by BET inhibitors.

Interactions[edit]

BRD2 has been shown to interact with E2F2,[8][9] and many transcription factors including GATA1.[7]

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ 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 3934568Freely accessible. PMID 22722403. 
  4. ^ 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. 
  5. ^ a b "Entrez Gene: BRD2 bromodomain containing 2". 
  6. ^ 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 4236231Freely accessible. PMID 24905006. 
  7. ^ 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. PMC 4424630Freely accessible. PMID 25696920. 
  8. ^ 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. 
  9. ^ 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 3968681Freely accessible. PMID 10965846. 

External links[edit]

Further reading[edit]