# BRD2

> Mediated Wiki article. Canonical URL: https://mediated.wiki/source/BRD2
> Markdown URL: https://mediated.wiki/source/BRD2.md
> Source: https://en.wikipedia.org/wiki/BRD2
> Source revision: 1301003216
> License: Creative Commons Attribution-ShareAlike 4.0 International (https://creativecommons.org/licenses/by-sa/4.0/)

{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
'''Bromodomain-containing protein 2''' is a [protein](/source/protein) that in humans is encoded by the ''BRD2'' [gene](/source/gene). BRD2 is part of the Bromodomain and Extra-Terminal motif (BET) protein family that also contains [BRD3](/source/BRD3), [BRD4](/source/BRD4), and [BRDT](/source/BRDT) in mammals <ref name="pmid22722403">{{Cite journal
 | pmid = 22722403
| pmc = 3934568
| year = 2012
| last1 = Belkina
| first1 = A. C.
| title = BET domain co-regulators in obesity, inflammation and cancer
| journal = Nature Reviews Cancer
| volume = 12
| issue = 7
| pages = 465–77
| last2 = Denis
| first2 = G. V.
| doi = 10.1038/nrc3256
}}</ref><ref name="pmid8781126">{{cite journal | vauthors = Thorpe KL, Abdulla S, Kaufman J, Trowsdale J, Beck S | title = Phylogeny and structure of the RING3 gene | journal = Immunogenetics | volume = 44 | issue = 5 | pages = 391–6 |date=October 1996 | pmid = 8781126 | doi =10.1007/BF02602785  | s2cid = 44613743 }}</ref><ref name="entrez">{{cite web | title = BRD2 bromodomain containing 2 [ Homo sapiens (human) ]| url = https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=6046}}</ref>

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](/source/MHC_class_II) region on [chromosome 6p21.3](/source/Human_leukocyte_antigen) but sequence comparison suggests that the protein is not involved in the immune response. Homology to the ''[Drosophila](/source/Drosophila)'' gene female sterile homeotic suggests that this human gene may be part of a [signal transduction pathway](/source/signal_transduction_pathway) involved in growth control.<ref name="entrez"/>

==Functions==
*BRD2 has been implicated in cancer.<ref name="pmid22722403"/><ref>{{Cite journal
 | pmid = 24905006
| pmc = 4236231
| year = 2014
| last1 = Shi
| first1 = J
| title = The mechanisms behind the therapeutic activity of BET bromodomain inhibition
| journal = Molecular Cell
| volume = 54
| issue = 5
| pages = 728–36
| last2 = Vakoc
| first2 = C. R.
| doi = 10.1016/j.molcel.2014.05.016
}}</ref>
*BRD2 loss in mice causes obesity without diabetes for unknown reasons.<ref name="pmid22722403"/>
*BRD2 may have functional overlap with close homolog BRD3.<ref name="pmid25696920">{{Cite journal
 | pmid = 25696920
| year = 2015
| last1 = Stonestrom
| first1 = A. J.
| title = Functions of BET proteins in erythroid gene expression
| journal = Blood
| last2 = Hsu
| first2 = S. C.
| last3 = Jahn
| first3 = K. S.
| last4 = Huang
| first4 = P
| last5 = Keller
| first5 = C. A.
| last6 = Giardine
| first6 = B. M.
| last7 = Kadauke
| first7 = S
| last8 = Campbell
| first8 = A. E.
| last9 = Evans
| first9 = P
| last10 = Hardison
| first10 = R. C.
| last11 = Blobel
| first11 = G. A.
| doi = 10.1182/blood-2014-10-607309
 | volume=125
 | issue = 18
| pages=2825–34
 | pmc=4424630
}}</ref>
*BRD2 function is blocked by [BET inhibitor](/source/BET_inhibitor)s.

==Interactions==
BRD2 has been shown to [interact](/source/Protein-protein_interaction) with [E2F2](/source/E2F2),<ref name=pmid12145330>{{cite journal |doi=10.1210/me.2001-0353 |last=Crowley |first=Thomas E |author2=Kaine Emily M |author3=Yoshida Manabu |author4=Nandi Anindita |author5=Wolgemuth Debra J  |date=August 2002  |title=Reproductive cycle regulation of nuclear import, euchromatic localization, and association with components of Pol II mediator of a mammalian double-bromodomain protein |journal=Mol. Endocrinol. |volume=16 |issue=8 |pages=1727–37 |location = United States| issn = 0888-8809| pmid = 12145330 |doi-access=free }}</ref><ref name=pmid10965846>{{cite journal |last=Denis |first=G V |author2=Vaziri C |author3=Guo N |author4=Faller D V  |date=August 2000  |title=RING3 kinase transactivates promoters of cell cycle regulatory genes through E2F |journal=Cell Growth Differ. |volume=11 |issue=8 |pages=417–24 |location = UNITED STATES| issn = 1044-9523| pmid = 10965846 | pmc=3968681}}</ref> and many transcription factors including [GATA1](/source/GATA1).<ref name="pmid25696920"/>

==References==
{{reflist}}

==External links==
* {{UCSC gene info|BRD2}}

==Further reading==
{{refbegin | 2}}
*{{cite journal  | vauthors=Haynes SR, Dollard C, Winston F |title=The bromodomain: a conserved sequence found in human, Drosophila and yeast proteins. |journal=Nucleic Acids Res. |volume=20 |issue= 10 |pages= 2603 |year= 1992 |pmid= 1350857 |doi=10.1093/nar/20.10.2603  | pmc=312404  |display-authors=etal}}
*{{cite journal  | vauthors=Okamoto N, Ando A, Kawai J |title=Orientation of HLA-DNA gene and identification of a CpG island-associated gene adjacent to DNA in human major histocompatibility complex class II region. |journal=Hum. Immunol. |volume=32 |issue= 3 |pages= 221–8 |year= 1992 |pmid= 1663500 |doi=10.1016/0198-8859(91)90059-I  |display-authors=etal}}
*{{cite journal  | vauthors=Denis GV, Green MR |title=A novel, mitogen-activated nuclear kinase is related to a Drosophila developmental regulator. |journal=Genes Dev. |volume=10 |issue= 3 |pages= 261–71 |year= 1996 |pmid= 8595877 |doi=10.1101/gad.10.3.261  |url=https://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1597&context=oapubs |doi-access=free }}
*{{cite journal  | vauthors=Thorpe KL, Gorman P, Thomas C |title=Chromosomal localization, gene structure and transcription pattern of the ORFX gene, a homologue of the MHC-linked RING3 gene. |journal=Gene |volume=200 |issue= 1–2 |pages= 177–83 |year= 1997 |pmid= 9373153 |doi=10.1016/S0378-1119(97)00415-0  |display-authors=etal}}
*{{cite journal  | vauthors=Taniguchi Y, Matsuzaka Y, Fujimoto H |title=Nucleotide sequence of the ring3 gene in the class II region of the mouse MHC and its abundant expression in testicular germ cells. |journal=Genomics |volume=51 |issue= 1 |pages= 114–23 |year= 1998 |pmid= 9693039 |doi= 10.1006/geno.1998.5262 |display-authors=etal}}
*{{cite journal  | vauthors=Guo N, Faller DV, Denis GV |title=Activation-induced nuclear translocation of RING3. |journal=J. Cell Sci. |volume=113 |issue=  17|pages= 3085–91 |year= 2000 |doi=10.1242/jcs.113.17.3085 |pmid= 10934046 |pmc=3936601 }}
*{{cite journal  | vauthors=Denis GV, Vaziri C, Guo N, Faller DV |title=RING3 kinase transactivates promoters of cell cycle regulatory genes through E2F. |journal=Cell Growth Differ. |volume=11 |issue= 8 |pages= 417–24 |year= 2001 |pmid= 10965846 |pmc=3968681}}
*{{cite journal  | vauthors=BelAiba RS, Baril P, Chebloune Y |title=Identification and cloning of an 85-kDa protein homologous to RING3 that is upregulated in proliferating endothelial cells. |journal=Eur. J. Biochem. |volume=268 |issue= 16 |pages= 4398–407 |year= 2001 |pmid= 11502199 |doi=10.1046/j.1432-1327.2001.02355.x  |display-authors=etal|doi-access=free }}
*{{cite journal  | vauthors=Crowley TE, Kaine EM, Yoshida M |title=Reproductive cycle regulation of nuclear import, euchromatic localization, and association with components of Pol II mediator of a mammalian double-bromodomain protein. |journal=Mol. Endocrinol. |volume=16 |issue= 8 |pages= 1727–37 |year= 2003 |pmid= 12145330 |doi=10.1210/me.2001-0353  |display-authors=etal|doi-access=free }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |display-authors=etal|bibcode=2002PNAS...9916899M |doi-access=free }}
*{{cite journal  | vauthors=Zhou M, Peng C, Nie XM |title=[Expression of BRD7-interacting proteins, BRD2 and BRD3, in nasopharyngeal carcinoma tissues] |journal=AI Zheng |volume=22 |issue= 2 |pages= 123–7 |year= 2003 |pmid= 12600283 |display-authors=etal}}
*{{cite journal  | vauthors=Pal DK, Evgrafov OV, Tabares P |title=BRD2 (RING3) is a probable major susceptibility gene for common juvenile myoclonic epilepsy. |journal=Am. J. Hum. Genet. |volume=73 |issue= 2 |pages= 261–70 |year= 2003 |pmid= 12830434 |doi=10.1086/377006  | pmc=1180366  |display-authors=etal}}
*{{cite journal  | vauthors=Mungall AJ, Palmer SA, Sims SK |title=The DNA sequence and analysis of human chromosome 6. |journal=Nature |volume=425 |issue= 6960 |pages= 805–11 |year= 2003 |pmid= 14574404 |doi= 10.1038/nature02055 |display-authors=etal|doi-access=free |bibcode=2003Natur.425..805M }}
*{{cite journal  | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal|doi-access=free }}
*{{cite journal  | vauthors=Kanno T, Kanno Y, Siegel RM |title=Selective recognition of acetylated histones by bromodomain proteins visualized in living cells. |journal=Mol. Cell |volume=13 |issue= 1 |pages= 33–43 |year= 2004 |pmid= 14731392 |doi=10.1016/S1097-2765(03)00482-9  |display-authors=etal|doi-access=free }}
*{{cite journal  | vauthors=Beausoleil SA, Jedrychowski M, Schwartz D |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101  | pmc=514446 |display-authors=etal|bibcode=2004PNAS..10112130B |doi-access=free }}
*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 |display-authors=etal}}
*{{cite journal  | vauthors=Benevolenskaya EV, Murray HL, Branton P |title=Binding of pRB to the PHD protein RBP2 promotes cellular differentiation. |journal=Mol. Cell |volume=18 |issue= 6 |pages= 623–35 |year= 2005 |pmid= 15949438 |doi= 10.1016/j.molcel.2005.05.012 |display-authors=etal|doi-access=free }}
{{refend}}
{{PDB Gallery|geneid=6046}}

{{protein-stub}}

---
Adapted from the Wikipedia article [BRD2](https://en.wikipedia.org/wiki/BRD2) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/BRD2?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.