BRD2: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
m (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}}))
 
imported>Bibcode Bot
m (Adding 0 arxiv eprint(s), 2 bibcode(s) and 0 doi(s). Did it miss something? Report bugs, errors, and suggestions at User talk:Bibcode Bot)
 
(One intermediate revision by one other user not shown)
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''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 <ref name="pmid22722403">{{Cite journal
| update_page = yes
  | pmid = 22722403
| require_manual_inspection = no
| pmc = 3934568
| update_protein_box = yes
| year = 2012
| update_summary = yes
| author1 = Belkina
| update_citations = yes
| first1 = A. C.
}}
| title = BET domain co-regulators in obesity, inflammation and cancer
 
| journal = Nature Reviews Cancer
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
| volume = 12
{{GNF_Protein_box
| issue = 7
  | image = PBB_Protein_BRD2_image.jpg
| pages = 465–77
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1x0j.
| last2 = Denis
| PDB = {{PDB2|1x0j}}, {{PDB2|2g4a}}
| first2 = G. V.
| Name = Bromodomain containing 2
| doi = 10.1038/nrc3256
| HGNCid = 1103
}}</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 | pmc =  | doi =10.1007/BF02602785 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: BRD2 bromodomain containing 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6046| accessdate = }}</ref>
| Symbol = BRD2
| AltSymbols =; D6S113E; DKFZp686N0336; FLJ31942; FSRG1; KIAA9001; NAT; RING3; RNF3
| OMIM = 601540
| ECnumber =
| Homologene = 74540
| MGIid = 99495
| GeneAtlas_image1 = PBB_GE_BRD2_214911_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_BRD2_208685_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_BRD2_208686_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}}  
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0007283 |text = spermatogenesis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6046
    | Hs_Ensembl = ENSG00000112526
    | Hs_RefseqProtein = NP_005095
    | Hs_RefseqmRNA = NM_005104
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = c6_COX
    | Hs_GenLoc_start = 33005845
    | Hs_GenLoc_end = 33018495
    | Hs_Uniprot = P25440
    | Mm_EntrezGene = 14312
    | Mm_Ensembl = ENSMUSG00000024335
    | Mm_RefseqmRNA = NM_001025387
    | Mm_RefseqProtein = NP_001020558
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 33722473
    | Mm_GenLoc_end = 33730354
    | Mm_Uniprot = Q7JJ13
  }}
}}
'''Bromodomain containing 2''', also known as '''BRD2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BRD2 bromodomain containing 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6046| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = This gene encodes a mitogen-activated kinase which localizes to the nucleus. The gene maps to the major histocompatability 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.<ref name="entrez">{{cite web | title = Entrez Gene: BRD2 bromodomain containing 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6046| accessdate = }}</ref>
| summary_text = 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.<ref name="entrez"/>
}}
}}
==Functions==
*BRD2 has been implicated in cancer.<ref name="pmid22722403"/><ref>{{Cite journal
| pmid = 24905006
| pmc = 4236231
| year = 2014
| author1 = 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
| author1 = 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
| pages=2825–34
| pmc=4424630
}}</ref>
*BRD2 function is blocked by [[BET inhibitor]]s.
==Interactions==
BRD2 has been shown to [[Protein-protein interaction|interact]] with [[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 |publisher= |location = United States| issn = 0888-8809| pmid = 12145330 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</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 |publisher= |location = UNITED STATES| issn = 1044-9523| pmid = 10965846 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = | pmc=3968681}}</ref> and many transcription factors including [[GATA1]].<ref name="pmid25696920"/>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|BRD2}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Haynes SR, Dollard C, Winston F, ''et al.'' |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=  }}
*{{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  | author=Beck S, Hanson I, Kelly A, ''et al.'' |title=A homologue of the Drosophila female sterile homeotic (fsh) gene in the class II region of the human MHC. |journal=DNA Seq. |volume=2 |issue= 4 |pages= 203-10 |year= 1992 |pmid= 1352711 |doi= }}
*{{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  | author=Okamoto N, Ando A, Kawai J, ''et al.'' |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=  }}
*{{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 }}
*{{cite journal  | author=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=  }}
*{{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  | author=Thorpe KL, Abdulla S, Kaufman J, ''et al.'' |title=Phylogeny and structure of the RING3 gene. |journal=Immunogenetics |volume=44 |issue= 5 |pages= 391-6 |year= 1996 |pmid= 8781126 |doi= }}
*{{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  | author=Thorpe KL, Gorman P, Thomas C, ''et al.'' |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=  }}
*{{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 |pmid= 10934046 |doi=  }}
*{{cite journal  | author=Taniguchi Y, Matsuzaka Y, Fujimoto H, ''et al.'' |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 }}
*{{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 |doi= |pmc=3968681}}
*{{cite journal  | author=Guo N, Faller DV, Denis GV |title=Activation-induced nuclear translocation of RING3. |journal=J. Cell. Sci. |volume=113 ( Pt 17) |issue= |pages= 3085-91 |year= 2000 |pmid= 10934046 |doi=  }}
*{{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}}
*{{cite journal  | author=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 |doi=  }}
*{{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}}
*{{cite journal  | author=BelAiba RS, Baril P, Chebloune Y, ''et al.'' |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=  }}
*{{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 }}
*{{cite journal  | author=Crowley TE, Kaine EM, Yoshida M, ''et al.'' |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=  }}
*{{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 |doi=  |display-authors=etal}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
*{{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  | author=Zhou M, Peng C, Nie XM, ''et al.'' |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 |doi= }}
*{{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}}
*{{cite journal  | author=Pal DK, Evgrafov OV, Tabares P, ''et al.'' |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= }}
*{{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}}
*{{cite journal  | author=Mungall AJ, Palmer SA, Sims SK, ''et al.'' |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 }}
*{{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}}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |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 }}
*{{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 }}
*{{cite journal  | author=Kanno T, Kanno Y, Siegel RM, ''et al.'' |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=  }}
*{{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  | author=Beausoleil SA, Jedrychowski M, Schwartz D, ''et al.'' |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 }}
*{{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}}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |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 }}
*{{cite journal  | author=Benevolenskaya EV, Murray HL, Branton P, ''et al.'' |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 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=6046}}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


{{protein-stub}}
{{protein-stub}}
{{WikiDoc Sources}}

Latest revision as of 21:57, 22 June 2018

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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 [1][2][3]

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.[3]

Functions

  • BRD2 has been implicated in cancer.[1][4]
  • BRD2 loss in mice causes obesity without diabetes for unknown reasons.[1]
  • BRD2 may have functional overlap with close homolog BRD3.[5]
  • BRD2 function is blocked by BET inhibitors.

Interactions

BRD2 has been shown to interact with E2F2,[6][7] and many transcription factors including GATA1.[5]

References

  1. ↑ 1.0 1.1 1.2 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.
  2. ↑ 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.
  3. ↑ 3.0 3.1 "Entrez Gene: BRD2 bromodomain containing 2".
  4. ↑ 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.
  5. ↑ 5.0 5.1 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 4424630. PMID 25696920.
  6. ↑ 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.
  7. ↑ 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.

External links

Further reading



Retrieved from "https://www.wikidoc.org/index.php?title=BRD2&oldid=1533182"