BRD8

BRD8
Identifiers
Aliases	BRD8, SMAP, SMAP2, p120, bromodomain containing 8
External IDs	OMIM: 602848; MGI: 1925906; GeneCards: BRD8
Gene location (Human) Chr. Chromosome 5 (human) Band 5q31.2 Start 138,139,770 bp End 138,178,953 bp
Gene location (Mouse) Chr. Chromosome 18 (mouse) Band 18|18 B1 Start 34,731,668 bp End 34,757,654 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right testis left testis ventricular zone pituitary gland anterior pituitary right lobe of thyroid gland right uterine tube left lobe of thyroid gland middle temporal gyrus buccal mucosa cell Top expressed in neural layer of retina Rostral migratory stream ventricular zone tail of embryo genital tubercle spermatocyte blastocyst ganglionic eminence primitive streak yolk sac More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA-binding transcription factor activity protein binding nuclear receptor activity Cellular component mitochondrion nucleus nucleoplasm Swr1 complex NuA4 histone acetyltransferase complex Biological process regulation of transcription by RNA polymerase II histone H2A acetylation regulation of growth cell surface receptor signaling pathway regulation of transcription, DNA-templated transcription, DNA-templated signal transduction histone H4 acetylation positive regulation of transcription by RNA polymerase II intracellular receptor signaling pathway chromatin organization Sources:Amigo / QuickGO
Orthologs Databases NCBI: entry; OMA: entry Species Human Mouse Entrez 10902 78656 Ensembl ENSG00000112983 ENSMUSG00000003778 UniProt Q9H0E9 Q8R3B7 RefSeq (mRNA) NM_001164326 NM_001300961 NM_001300962 NM_001300966 NM_006696 NM_139199 NM_183359 NM_001289606 NM_001289607 NM_030147 NM_001361136 RefSeq (protein) NP_001157798 NP_001287890 NP_001287891 NP_001287895 NP_006687 NP_631938 NP_001276535 NP_001276536 NP_084423 NP_001348065 Location (UCSC) Chr 5: 138.14 – 138.18 Mb Chr 18: 34.73 – 34.76 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Bromodomain-containing protein 8 is a protein that in humans is encoded by the BRD8 gene.

The protein encoded by this gene interacts with thyroid hormone receptor in a ligand-dependent manner and enhances thyroid hormone-dependent activation from thyroid response elements. This protein contains a bromodomain and is thought to be a nuclear receptor coactivator. Three alternatively spliced transcript variants that encode distinct isoforms have been identified.

Interactions

BRD8 has been shown to interact with Thyroid hormone receptor beta and Retinoid X receptor alpha.

External links

• Human BRD8 genome location and BRD8 gene details page in the UCSC Genome Browser.
• Human SMAP2 genome location and SMAP2 gene details page in the UCSC Genome Browser.

Further reading

• Doyon Y, Côté J (April 2004). "The highly conserved and multifunctional NuA4 HAT complex". Current Opinion in Genetics & Development. 14 (2): 147–54. doi:10.1016/j.gde.2004.02.009. PMID 15196461.
• Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Monden T, Kishi M, Hosoya T, Satoh T, Wondisford FE, Hollenberg AN, Yamada M, Mori M (October 1999). "p120 acts as a specific coactivator for 9-cis-retinoic acid receptor (RXR) on peroxisome proliferator-activated receptor-gamma/RXR heterodimers". Molecular Endocrinology. 13 (10): 1695–703. doi:10.1210/mend.13.10.0353. PMID 10517671. S2CID 25098867.
• Lai F, Godley LA, Joslin J, Fernald AA, Liu J, Espinosa R, Zhao N, Pamintuan L, Till BG, Larson RA, Qian Z, Le Beau MM (January 2001). "Transcript map and comparative analysis of the 1.5-Mb commonly deleted segment of human 5q31 in malignant myeloid diseases with a del(5q)". Genomics. 71 (2): 235–45. doi:10.1006/geno.2000.6414. PMID 11161817.
• Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (March 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Research. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
• Cai Y, Jin J, Tomomori-Sato C, Sato S, Sorokina I, Parmely TJ, Conaway RC, Conaway JW (October 2003). "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex". The Journal of Biological Chemistry. 278 (44): 42733–6. doi:10.1074/jbc.C300389200. PMID 12963728.
• Doyon Y, Selleck W, Lane WS, Tan S, Côté J (March 2004). "Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans". Molecular and Cellular Biology. 24 (5): 1884–96. doi:10.1128/MCB.24.5.1884-1896.2004. PMC 350560. PMID 14966270.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (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): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Cai Y, Jin J, Florens L, Swanson SK, Kusch T, Li B, Workman JL, Washburn MP, Conaway RC, Conaway JW (April 2005). "The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60 histone acetyltransferase and SRCAP complexes". The Journal of Biological Chemistry. 280 (14): 13665–70. doi:10.1074/jbc.M500001200. PMID 15647280.
• 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): 623–35. doi:10.1016/j.molcel.2005.05.012. PMID 15949438.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Natsume W, Tanabe K, Kon S, Yoshida N, Watanabe T, Torii T, Satake M (June 2006). "SMAP2, a novel ARF GTPase-activating protein, interacts with clathrin and clathrin assembly protein and functions on the AP-1-positive early endosome/trans-Golgi network". Molecular Biology of the Cell. 17 (6): 2592–603. doi:10.1091/mbc.E05-10-0909. PMC 1475504. PMID 16571680.
• Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (October 2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243. S2CID 14294292.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (November 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.