BRD2

Last updated
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, BRD2-IT1
External IDs OMIM: 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 Mb Chr 17: 34.33 – 34.34 Mb
PubMed search [3] [4]
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 [5] [6] [7]

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

Interactions

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

References

  1. 1 2 3 ENSG00000234507, ENSG00000230678, ENSG00000204256, ENSG00000235307, ENSG00000236227, ENSG00000234704 GRCh38: Ensembl release 89: ENSG00000215077, ENSG00000234507, ENSG00000230678, ENSG00000204256, ENSG00000235307, ENSG00000236227, ENSG00000234704 Ensembl, May 2017
  2. 1 2 3 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. 1 2 3 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. 1 2 "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. 1 2 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. 16 (8). United States: 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. 11 (8). UNITED STATES: 417–24. ISSN   1044-9523. PMC   3968681 . PMID   10965846.

Further reading