BRD2

BRD2
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
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1X0J, 2DVQ, 2DVR, 2DVS, 2DVV, 2E3K, 2G4A, 2YDW, 2YEK, 3AQA, 3ONI, 4A9E, 4A9F, 4A9H, 4A9I, 4A9J, 4A9M, 4A9N, 4A9O, 4AKN, 4ALG, 4ALH, 4J1P, 4MR5, 4MR6, 4QEU, 4QEV, 4QEW, 4UYF, 4UYG, 4UYH, 5BT5, 5DFD, 5HEM, 5DFB, 5HEL, 5HFQ, 5HEN, 5DFC, 5IG6, 5IBN, 5DW1
Gene location (Human)
Chr.	Chromosome 6 (human)
End	32,981,505 bp
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)
End	34,341,608 bp
RNA expression pattern
	Top expressed in
	ventricular zone; ; granulocyte; ; ganglionic eminence; ; left lobe of thyroid gland; ; right testis; ; right lobe of thyroid gland; ; left testis; ; pituitary gland; ; anterior pituitary; ; cerebellar hemisphere;
	Top expressed in
	tail of embryo; ; genital tubercle; ; Rostral migratory stream; ; lacrimal gland; ; internal carotid artery; ; neural layer of retina; ; ventricular zone; ; yolk sac; ; external carotid artery; ; granulocyte;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	chromatin binding; protein binding; lysine-acetylated histone binding;
Cellular component	cytoplasm; nucleus; nucleoplasm; nuclear speck;
Biological process	regulation of transcription by RNA polymerase II; nucleosome assembly; regulation of transcription, DNA-templated; transcription, DNA-templated; spermatogenesis; chromatin organization; viral process;
	Sources:Amigo / QuickGO
Orthologs
	6046
	14312
ENSG00000215077; ENSG00000234507; ENSG00000230678; ENSG00000204256; ENSG00000235307;
	ENSG00000236227; ENSG00000234704
	ENSMUSG00000024335
	P25440
	Q7JJ13
	NM_001113182; NM_001199455; NM_001199456; NM_001291986; NM_005104
	NM_001025387; NM_001204973; NM_010238
	NP_001106653; NP_001186384; NP_001186385; NP_001278915; NP_005095
	NP_001191902; NP_034368
	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

BRD2 may have functional overlap with close homolog BRD3.^[8]
BRD2 function is blocked by BET inhibitors.

Clinical significance

BRD2 has been implicated in cancer.^[5]^[9]
BRD2 loss in mice causes obesity without diabetes for unknown reasons.^[5]

Interactions

BRD2 has been shown to interact with E2F2,^[10]^[11] and many transcription factors including GATA1.^[8]

References

1 2 3 ENSG00000234507, ENSG00000230678, ENSG00000204256, ENSG00000235307, ENSG00000236227, ENSG00000234704 GRCh38: Ensembl release 89: ENSG00000215077, ENSG00000234507, ENSG00000230678, ENSG00000204256, ENSG00000235307, ENSG00000236227, ENSG00000234704 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024335 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
1 2 3 Belkina AC, Denis GV (June 2012). "BET domain co-regulators in obesity, inflammation and cancer". Nature Reviews. Cancer. 12 (7): 465–477. doi:10.1038/nrc3256. PMC 3934568. PMID 22722403.
↑ Thorpe KL, Abdulla S, Kaufman J, Trowsdale J, Beck S (October 1996). "Phylogeny and structure of the RING3 gene". Immunogenetics. 44 (5): 391–396. doi:10.1007/BF02602785. PMID 8781126. S2CID 44613743.
1 2 "BRD2 bromodomain containing 2 [ Homo sapiens (human) ]".
1 2 Stonestrom AJ, Hsu SC, Jahn KS, Huang P, Keller CA, Giardine BM, et al. (April 2015). "Functions of BET proteins in erythroid gene expression". Blood. 125 (18): 2825–2834. doi:10.1182/blood-2014-10-607309. PMC 4424630. PMID 25696920.
↑ Shi J, Vakoc CR (June 2014). "The mechanisms behind the therapeutic activity of BET bromodomain inhibition". Molecular Cell. 54 (5): 728–736. doi:10.1016/j.molcel.2014.05.016. PMC 4236231. PMID 24905006.
↑ Crowley TE, Kaine EM, Yoshida M, Nandi A, Wolgemuth DJ (August 2002). "Reproductive cycle regulation of nuclear import, euchromatic localization, and association with components of Pol II mediator of a mammalian double-bromodomain protein". Molecular Endocrinology. 16 (8). Baltimore, Md.: 1727–1737. doi:10.1210/me.2001-0353. PMID 12145330.
↑ Denis GV, Vaziri C, Guo N, Faller DV (August 2000). "RING3 kinase transactivates promoters of cell cycle regulatory genes through E2F". Cell Growth & Differentiation. 11 (8): 417–424. PMC 3968681. PMID 10965846.

External links

Human BRD2 genome location and BRD2 gene details page in the UCSC Genome Browser.

Haynes SR, Dollard C, Winston F, Beck S, Trowsdale J, Dawid IB (May 1992). "The bromodomain: a conserved sequence found in human, Drosophila and yeast proteins". Nucleic Acids Research. 20 (10): 2603. doi:10.1093/nar/20.10.2603. PMC 312404. PMID 1350857.
Okamoto N, Ando A, Kawai J, Yoshiwara T, Tsuji K, Inoko H (November 1991). "Orientation of HLA-DNA gene and identification of a CpG island-associated gene adjacent to DNA in human major histocompatibility complex class II region". Human Immunology. 32 (3): 221–228. doi:10.1016/0198-8859(91)90059-I. PMID 1663500.
Denis GV, Green MR (1996). "A novel, mitogen-activated nuclear kinase is related to a Drosophila developmental regulator". Genes & Development. 10 (3): 261–271. doi:10.1101/gad.10.3.261. PMID 8595877.
Thorpe KL, Gorman P, Thomas C, Sheer D, Trowsdale J, Beck S (October 1997). "Chromosomal localization, gene structure and transcription pattern of the ORFX gene, a homologue of the MHC-linked RING3 gene". Gene. 200 (1–2): 177–183. doi:10.1016/S0378-1119(97)00415-0. PMID 9373153.
Taniguchi Y, Matsuzaka Y, Fujimoto H, Miyado K, Kohda A, Okumura K, et al. (July 1998). "Nucleotide sequence of the ring3 gene in the class II region of the mouse MHC and its abundant expression in testicular germ cells". Genomics. 51 (1): 114–123. doi:10.1006/geno.1998.5262. PMID 9693039.
Guo N, Faller DV, Denis GV (2000). "Activation-induced nuclear translocation of RING3". Journal of Cell Science. 113 (17): 3085–3091. doi:10.1242/jcs.113.17.3085. PMC 3936601. PMID 10934046.
BelAiba RS, Baril P, Chebloune Y, Tabone E, Boukerche H (August 2001). "Identification and cloning of an 85-kDa protein homologous to RING3 that is upregulated in proliferating endothelial cells". European Journal of Biochemistry. 268 (16): 4398–4407. doi:10.1046/j.1432-1327.2001.02355.x. PMID 11502199.
Zhou M, Peng C, Nie XM, Zhang BC, Zhu SG, Yu Y, et al. (February 2003). "[Expression of BRD7-interacting proteins,BRD2 and BRD3, in nasopharyngeal carcinoma tissues]". Ai Zheng = Aizheng = Chinese Journal of Cancer. 22 (2): 123–127. PMID 12600283.
Pal DK, Evgrafov OV, Tabares P, Zhang F, Durner M, Greenberg DA (August 2003). "BRD2 (RING3) is a probable major susceptibility gene for common juvenile myoclonic epilepsy". American Journal of Human Genetics. 73 (2): 261–270. doi:10.1086/377006. PMC 1180366. PMID 12830434.
Kanno T, Kanno Y, Siegel RM, Jang MK, Lenardo MJ, Ozato K (January 2004). "Selective recognition of acetylated histones by bromodomain proteins visualized in living cells". Molecular Cell. 13 (1): 33–43. doi:10.1016/S1097-2765(03)00482-9. PMID 14731392.
Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, et al. (August 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–12135. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
Benevolenskaya EV, Murray HL, Branton P, Young RA, Kaelin WG (June 2005). "Binding of pRB to the PHD protein RBP2 promotes cellular differentiation". Molecular Cell. 18 (6): 623–635. doi:10.1016/j.molcel.2005.05.012. PMID 15949438.

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[refGRCh38Ensembl-1] 1 2 3 ENSG00000234507, ENSG00000230678, ENSG00000204256, ENSG00000235307, ENSG00000236227, ENSG00000234704 GRCh38: Ensembl release 89: ENSG00000215077, ENSG00000234507, ENSG00000230678, ENSG00000204256, ENSG00000235307, ENSG00000236227, ENSG00000234704 – Ensembl, May 2017

[refGRCm38Ensembl-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.

[Belkina_2012-5] 1 2 3 Belkina AC, Denis GV (June 2012). "BET domain co-regulators in obesity, inflammation and cancer". Nature Reviews. Cancer. 12 (7): 465–477. doi:10.1038/nrc3256. PMC 3934568. PMID 22722403.

[Thorpe_1996-6] Thorpe KL, Abdulla S, Kaufman J, Trowsdale J, Beck S (October 1996). "Phylogeny and structure of the RING3 gene". Immunogenetics. 44 (5): 391–396. doi:10.1007/BF02602785. PMID 8781126. S2CID 44613743.

[entrez-7] 1 2 "BRD2 bromodomain containing 2 [ Homo sapiens (human) ]".

[Stonestrom_2015-8] 1 2 Stonestrom AJ, Hsu SC, Jahn KS, Huang P, Keller CA, Giardine BM, et al. (April 2015). "Functions of BET proteins in erythroid gene expression". Blood. 125 (18): 2825–2834. doi:10.1182/blood-2014-10-607309. PMC 4424630. PMID 25696920.

[9] Shi J, Vakoc CR (June 2014). "The mechanisms behind the therapeutic activity of BET bromodomain inhibition". Molecular Cell. 54 (5): 728–736. doi:10.1016/j.molcel.2014.05.016. PMC 4236231. PMID 24905006.

[Crowley_2002-10] Crowley TE, Kaine EM, Yoshida M, Nandi A, Wolgemuth DJ (August 2002). "Reproductive cycle regulation of nuclear import, euchromatic localization, and association with components of Pol II mediator of a mammalian double-bromodomain protein". Molecular Endocrinology. 16 (8). Baltimore, Md.: 1727–1737. doi:10.1210/me.2001-0353. PMID 12145330.

[Denis_2000-11] Denis GV, Vaziri C, Guo N, Faller DV (August 2000). "RING3 kinase transactivates promoters of cell cycle regulatory genes through E2F". Cell Growth & Differentiation. 11 (8): 417–424. PMC 3968681. PMID 10965846.

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