BRD3 has been implicated in nucleosome remodeling in the context of transcription.[11] In addition, BRD3 has been shown to interact with RNA molecules and form protein-RNA aggregates.[12]
BRD2 and BRD3 perform overlapping cellular functions.[13]
Clinical significanceedit
Chromosomal translocation of BRD3 with the NUT gene has been implicated in NUT midline carcinoma.[14] BRD3-NUT driven cancers are histopathologically indistinguishable from BRD4-NUT driven cancers, likely because these translocations involve the N-terminal portion bromodomain-containing portion of these proteins which are highly conserved.
Depletion of BRD3 slows growth in cancer models including prostate cancer and medulloblastoma. The effect of BRD3 depletion is milder than that of other BET proteins BRD2 and BRD4 when each is tested in isolation.[15][16]BET inhibitors target highly conserved BET bromodomains and displace BRD2, BRD3, and BRD4 from chromatin simultaneously. Functional redundancy between BRD2 and BRD3 suggests that their simultaneous disruption of these proteins may be more important than is appreciated by depletion of these proteins individually.[17]
Referencesedit
^ abcGRCh38: Ensembl release 89: ENSG00000169925 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000026918 - 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.
^Nomura N, Nagase T, Miyajima N, Sazuka T, Tanaka A, Sato S, Seki N, Kawarabayasi Y, Ishikawa K, Tabata S (Dec 1995). "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1". DNA Research. 1 (5): 223–9. doi:10.1093/dnares/1.5.223. PMID 7584044.
^Thorpe KL, Abdulla S, Kaufman J, Trowsdale J, Beck S (Oct 1996). "Phylogeny and structure of the RING3 gene". Immunogenetics. 44 (5): 391–6. doi:10.1007/BF02602785. PMID 8781126. S2CID 44613743.
^Gamsjaeger R, Webb SR, Lamonica JM, Billin A, Blobel GA, Mackay JP (Jul 2011). "Structural basis and specificity of acetylated transcription factor GATA1 recognition by BET family bromodomain protein Brd3". Molecular and Cellular Biology. 31 (13): 2632–40. doi:10.1128/MCB.05413-11. PMC3133386. PMID 21555453.
^Lamonica JM, Deng W, Kadauke S, Campbell AE, Gamsjaeger R, Wang H, Cheng Y, Billin AN, Hardison RC, Mackay JP, Blobel GA (May 2011). "Bromodomain protein Brd3 associates with acetylated GATA1 to promote its chromatin occupancy at erythroid target genes". Proceedings of the National Academy of Sciences of the United States of America. 108 (22): E159-68. doi:10.1073/pnas.1102140108. PMC3107332. PMID 21536911.
^LeRoy G, Rickards B, Flint SJ (Apr 2008). "The double bromodomain proteins Brd2 and Brd3 couple histone acetylation to transcription". Molecular Cell. 30 (1): 51–60. doi:10.1016/j.molcel.2008.01.018. PMC2387119. PMID 18406326.
^Daneshvar K, Ardehali MB, Klein IA, Hsieh FK, Kratkiewicz AJ, Mahpour A; et al. (2020). "lncRNA DIGIT and BRD3 protein form phase-separated condensates to regulate endoderm differentiation". Nat Cell Biol. 22 (10): 1211–1222. doi:10.1038/s41556-020-0572-2. PMC8008247. PMID 32895492.{{cite journal}}: CS1 maint: multiple names: authors list (link)
^Stonestrom AJ, Hsu SC, Jahn KS, Huang P, Keller CA, Giardine BM, Kadauke S, Campbell AE, Evans P, Hardison RC, Blobel GA (Feb 2015). "Functions of BET proteins in erythroid gene expression". Blood. 125 (18): 2825–34. doi:10.1182/blood-2014-10-607309. PMC4424630. PMID 25696920.
^French CA (2012). "Pathogenesis of NUT midline carcinoma". Annual Review of Pathology. 7: 247–65. doi:10.1146/annurev-pathol-011811-132438. PMID 22017582.
^Asangani IA, Dommeti VL, Wang X, Malik R, Cieslik M, Yang R, Escara-Wilke J, Wilder-Romans K, Dhanireddy S, Engelke C, Iyer MK, Jing X, Wu YM, Cao X, Qin ZS, Wang S, Feng FY, Chinnaiyan AM (Jun 2014). "Therapeutic targeting of BET bromodomain proteins in castration-resistant prostate cancer". Nature. 510 (7504): 278–82. Bibcode:2014Natur.510..278A. doi:10.1038/nature13229. PMC4075966. PMID 24759320.
^Tang Y, Gholamin S, Schubert S, Willardson MI, Lee A, Bandopadhayay P, Bergthold G, Masoud S, Nguyen B, Vue N, Balansay B, Yu F, Oh S, Woo P, Chen S, Ponnuswami A, Monje M, Atwood SX, Whitson RJ, Mitra S, Cheshier SH, Qi J, Beroukhim R, Tang JY, Wechsler-Reya R, Oro AE, Link BA, Bradner JE, Cho YJ (Jul 2014). "Epigenetic targeting of Hedgehog pathway transcriptional output through BET bromodomain inhibition" (PDF). Nature Medicine. 20 (7): 732–40. doi:10.1038/nm.3613. PMC4108909. PMID 24973920.
^Stonestrom AJ, Hsu SC, Jahn KS, Huang P, Keller CA, Giardine BM, Kadauke S, Campbell AE, Evans P, Hardison RC, Blobel GA (Apr 2015). "Functions of BET proteins in erythroid gene expression". Blood. 125 (18): 2825–34. doi:10.1182/blood-2014-10-607309. PMC4424630. PMID 25696920.
External linksedit
Human BRD3 genome location and BRD3 gene details page in the UCSC Genome Browser.
Further readingedit
Thorpe KL, Gorman P, Thomas C, Sheer D, Trowsdale J, Beck S (Oct 1997). "Chromosomal localization, gene structure and transcription pattern of the ORFX gene, a homologue of the MHC-linked RING3 gene". Gene. 200 (1–2): 177–83. doi:10.1016/S0378-1119(97)00415-0. PMID 9373153.
Kaneko H, Inoue R, Teramoto T, Morimoto W, Isogai K, Kasahara K, Kondo N (2003). "Detection of the genes induced in activated lymphocytes by modified differential display". Journal of Investigational Allergology & Clinical Immunology. 12 (2): 86–90. PMID 12371535.
Zhou M, Peng C, Nie XM, Zhang BC, Zhu SG, Yu Y, Li XL, Li GY (Feb 2003). "[Expression of BRD7-interacting proteins,BRD2 and BRD3, in nasopharyngeal carcinoma tissues]". AI Zheng = Aizheng = Chinese Journal of Cancer. 22 (2): 123–7. PMID 12600283.
Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (Aug 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC514446. PMID 15302935.
Ishii H, Mimori K, Mori M, Vecchione A (Jul 2005). "Differentially expressed genes in endothelial differentiation". DNA and Cell Biology. 24 (7): 432–7. doi:10.1089/dna.2005.24.432. PMID 16008511.
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
This article on a gene on human chromosome 9 is a stub. You can help Wikipedia by expanding it.
bromodomain, containing, protein, brd3, also, known, ring3, like, protein, ring3l, protein, that, humans, encoded, brd3, gene, this, gene, identified, based, homology, gene, encoding, ring3, brd2, protein, serine, threonine, kinase, gene, maps, 9q34, region, w. Bromodomain containing protein 3 BRD3 also known as RING3 like protein RING3L is a protein that in humans is encoded by the BRD3 gene 5 6 7 This gene was identified based on its homology to the gene encoding the RING3 BRD2 protein a serine threonine kinase The gene maps to 9q34 a region which contains several major histocompatibility complex MHC genes BRD3Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes2E7N 2NXB 2OO1 2YW5 3S91 3S92 5HFR 5A7C 5HJCIdentifiersAliasesBRD3 ORFX RING3L bromodomain containing 3External IDsOMIM 601541 MGI 1914632 HomoloGene 81801 GeneCards BRD3Gene location Human Chr Chromosome 9 human 1 Band9q34 2Start134 030 305 bp 1 End134 068 535 bp 1 Gene location Mouse Chr Chromosome 2 mouse 2 Band2 2 A3Start27 335 591 bp 2 End27 397 674 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed innippleinternal globus pallidusoptic nerveoocyteinferior ganglion of vagus nervepylorussecondary oocyteventral tegmental areaexternal globus pallidusganglionic eminenceTop expressed inganglionic eminencecumulus cellmaxillary prominenceinternal carotid arteryureterseminiferous tubuleabdominal wallpineal glandhandmorulaMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionprotein binding chromatin binding lysine acetylated histone bindingCellular componentnucleusBiological processregulation of transcription DNA templated regulation of transcription by RNA polymerase II transcription DNA templated chromatin organizationSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez801967382EnsemblENSG00000169925ENSMUSG00000026918UniProtQ15059Q8K2F0RefSeq mRNA NM 007371NM 001113573NM 001113574NM 023336RefSeq protein NP 031397NP 031397 1NP 001107045NP 001107046NP 075825Location UCSC Chr 9 134 03 134 07 MbChr 2 27 34 27 4 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Structure 2 Function 3 Clinical significance 4 References 5 External links 6 Further readingStructure editBRD3 is a member of the Bromodomain and Extra Terminal motif BET protein family Like other BET family members it contains two tandem homologous bromodomains and an Extra Terminal motif BRD3 similar to BRD2 does not have a long C terminal domain as BET family proteins BRD4 and BRDT do 8 Function editLike other BET protein family members BRD3 associates with acetylated lysine residues on histones and transcription factors 9 10 BRD3 has been implicated in nucleosome remodeling in the context of transcription 11 In addition BRD3 has been shown to interact with RNA molecules and form protein RNA aggregates 12 BRD2 and BRD3 perform overlapping cellular functions 13 Clinical significance editChromosomal translocation of BRD3 with the NUT gene has been implicated in NUT midline carcinoma 14 BRD3 NUT driven cancers are histopathologically indistinguishable from BRD4 NUT driven cancers likely because these translocations involve the N terminal portion bromodomain containing portion of these proteins which are highly conserved Depletion of BRD3 slows growth in cancer models including prostate cancer and medulloblastoma The effect of BRD3 depletion is milder than that of other BET proteins BRD2 and BRD4 when each is tested in isolation 15 16 BET inhibitors target highly conserved BET bromodomains and displace BRD2 BRD3 and BRD4 from chromatin simultaneously Functional redundancy between BRD2 and BRD3 suggests that their simultaneous disruption of these proteins may be more important than is appreciated by depletion of these proteins individually 17 References edit a b c GRCh38 Ensembl release 89 ENSG00000169925 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000026918 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 Nomura N Nagase T Miyajima N Sazuka T Tanaka A Sato S Seki N Kawarabayasi Y Ishikawa K Tabata S Dec 1995 Prediction of the coding sequences of unidentified human genes II The coding sequences of 40 new genes KIAA0041 KIAA0080 deduced by analysis of cDNA clones from human cell line KG 1 DNA Research 1 5 223 9 doi 10 1093 dnares 1 5 223 PMID 7584044 Thorpe KL Abdulla S Kaufman J Trowsdale J Beck S Oct 1996 Phylogeny and structure of the RING3 gene Immunogenetics 44 5 391 6 doi 10 1007 BF02602785 PMID 8781126 S2CID 44613743 Entrez Gene BRD3 bromodomain containing 3 Belkina AC Denis GV Jul 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 Gamsjaeger R Webb SR Lamonica JM Billin A Blobel GA Mackay JP Jul 2011 Structural basis and specificity of acetylated transcription factor GATA1 recognition by BET family bromodomain protein Brd3 Molecular and Cellular Biology 31 13 2632 40 doi 10 1128 MCB 05413 11 PMC 3133386 PMID 21555453 Lamonica JM Deng W Kadauke S Campbell AE Gamsjaeger R Wang H Cheng Y Billin AN Hardison RC Mackay JP Blobel GA May 2011 Bromodomain protein Brd3 associates with acetylated GATA1 to promote its chromatin occupancy at erythroid target genes Proceedings of the National Academy of Sciences of the United States of America 108 22 E159 68 doi 10 1073 pnas 1102140108 PMC 3107332 PMID 21536911 LeRoy G Rickards B Flint SJ Apr 2008 The double bromodomain proteins Brd2 and Brd3 couple histone acetylation to transcription Molecular Cell 30 1 51 60 doi 10 1016 j molcel 2008 01 018 PMC 2387119 PMID 18406326 Daneshvar K Ardehali MB Klein IA Hsieh FK Kratkiewicz AJ Mahpour A et al 2020 lncRNA DIGIT and BRD3 protein form phase separated condensates to regulate endoderm differentiation Nat Cell Biol 22 10 1211 1222 doi 10 1038 s41556 020 0572 2 PMC 8008247 PMID 32895492 a href Template Cite journal html title Template Cite journal cite journal a CS1 maint multiple names authors list link Stonestrom AJ Hsu SC Jahn KS Huang P Keller CA Giardine BM Kadauke S Campbell AE Evans P Hardison RC Blobel GA Feb 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 French CA 2012 Pathogenesis of NUT midline carcinoma Annual Review of Pathology 7 247 65 doi 10 1146 annurev pathol 011811 132438 PMID 22017582 Asangani IA Dommeti VL Wang X Malik R Cieslik M Yang R Escara Wilke J Wilder Romans K Dhanireddy S Engelke C Iyer MK Jing X Wu YM Cao X Qin ZS Wang S Feng FY Chinnaiyan AM Jun 2014 Therapeutic targeting of BET bromodomain proteins in castration resistant prostate cancer Nature 510 7504 278 82 Bibcode 2014Natur 510 278A doi 10 1038 nature13229 PMC 4075966 PMID 24759320 Tang Y Gholamin S Schubert S Willardson MI Lee A Bandopadhayay P Bergthold G Masoud S Nguyen B Vue N Balansay B Yu F Oh S Woo P Chen S Ponnuswami A Monje M Atwood SX Whitson RJ Mitra S Cheshier SH Qi J Beroukhim R Tang JY Wechsler Reya R Oro AE Link BA Bradner JE Cho YJ Jul 2014 Epigenetic targeting of Hedgehog pathway transcriptional output through BET bromodomain inhibition PDF Nature Medicine 20 7 732 40 doi 10 1038 nm 3613 PMC 4108909 PMID 24973920 Stonestrom AJ Hsu SC Jahn KS Huang P Keller CA Giardine BM Kadauke S Campbell AE Evans P Hardison RC Blobel GA Apr 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 External links editHuman BRD3 genome location and BRD3 gene details page in the UCSC Genome Browser Further reading editThorpe KL Gorman P Thomas C Sheer D Trowsdale J Beck S Oct 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 83 doi 10 1016 S0378 1119 97 00415 0 PMID 9373153 Kaneko H Inoue R Teramoto T Morimoto W Isogai K Kasahara K Kondo N 2003 Detection of the genes induced in activated lymphocytes by modified differential display Journal of Investigational Allergology amp Clinical Immunology 12 2 86 90 PMID 12371535 Zhou M Peng C Nie XM Zhang BC Zhu SG Yu Y Li XL Li GY Feb 2003 Expression of BRD7 interacting proteins BRD2 and BRD3 in nasopharyngeal carcinoma tissues AI Zheng Aizheng Chinese Journal of Cancer 22 2 123 7 PMID 12600283 Beausoleil SA Jedrychowski M Schwartz D Elias JE Villen J Li J Cohn MA Cantley LC Gygi SP Aug 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 5 Bibcode 2004PNAS 10112130B doi 10 1073 pnas 0404720101 PMC 514446 PMID 15302935 Ishii H Mimori K Mori M Vecchione A Jul 2005 Differentially expressed genes in endothelial differentiation DNA and Cell Biology 24 7 432 7 doi 10 1089 dna 2005 24 432 PMID 16008511 Olsen JV Blagoev B Gnad F Macek B Kumar C Mortensen P Mann M Nov 2006 Global in vivo and site specific phosphorylation dynamics in signaling networks Cell 127 3 635 48 doi 10 1016 j cell 2006 09 026 PMID 17081983 S2CID 7827573 nbsp This article on a gene on human chromosome 9 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Bromodomain containing protein 3 amp oldid 1079671929, wikipedia, wiki, book, books, library,
