SIN3B: Difference between revisions
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*{{cite journal | author=Ayer DE, Lawrence QA, Eisenman RN |title=Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3 |journal=Cell |volume=80 |issue= 5 |pages= 767–76 |year= 1995 |pmid= 7889570 |doi=10.1016/0092-8674(95)90355-0 }} |
*{{cite journal | author=Ayer DE, Lawrence QA, Eisenman RN |title=Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3 |journal=Cell |volume=80 |issue= 5 |pages= 767–76 |year= 1995 |pmid= 7889570 |doi=10.1016/0092-8674(95)90355-0 }} |
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*{{cite journal |
*{{cite journal |vauthors=David G, Alland L, Hong SH, etal |title=Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein |journal=Oncogene |volume=16 |issue= 19 |pages= 2549–56 |year= 1998 |pmid= 9627120 |doi= 10.1038/sj.onc.1202043 }} |
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*{{cite journal | author=Koipally J, Renold A, Kim J, Georgopoulos K |title=Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes |journal=EMBO J. |volume=18 |issue= 11 |pages= 3090–100 |year= 1999 |pmid= 10357820 |doi= 10.1093/emboj/18.11.3090 | pmc=1171390 }} |
*{{cite journal | author=Koipally J, Renold A, Kim J, Georgopoulos K |title=Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes |journal=EMBO J. |volume=18 |issue= 11 |pages= 3090–100 |year= 1999 |pmid= 10357820 |doi= 10.1093/emboj/18.11.3090 | pmc=1171390 }} |
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*{{cite journal | author=Naruse Y, Aoki T, Kojima T, Mori N |title=Neural restrictive silencer factor recruits mSin3 and histone deacetylase complex to repress neuron-specific target genes |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 24 |pages= 13691–6 |year= 2000 |pmid= 10570134 |doi=10.1073/pnas.96.24.13691 | pmc=24126 }} |
*{{cite journal | author=Naruse Y, Aoki T, Kojima T, Mori N |title=Neural restrictive silencer factor recruits mSin3 and histone deacetylase complex to repress neuron-specific target genes |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 24 |pages= 13691–6 |year= 2000 |pmid= 10570134 |doi=10.1073/pnas.96.24.13691 | pmc=24126 }} |
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*{{cite journal |
*{{cite journal |vauthors=Spronk CA, Tessari M, Kaan AM, etal |title=The Mad1-Sin3B interaction involves a novel helical fold |journal=Nat. Struct. Biol. |volume=7 |issue= 12 |pages= 1100–4 |year= 2001 |pmid= 11101889 |doi= 10.1038/81944 }} |
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*{{cite journal |
*{{cite journal |vauthors=Spronk CA, Jansen JF, Tessari M, etal |title=Sequence-specific assignment of the PAH2 domain of Sin3B free and bound to Mad1 |journal=J. Biomol. NMR |volume=19 |issue= 4 |pages= 377–8 |year= 2001 |pmid= 11370785 |doi=10.1023/A:1011262214741 }} |
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*{{cite journal |
*{{cite journal |vauthors=Alland L, David G, Shen-Li H, etal |title=Identification of Mammalian Sds3 as an Integral Component of the Sin3/Histone Deacetylase Corepressor Complex |journal=Mol. Cell. Biol. |volume=22 |issue= 8 |pages= 2743–50 |year= 2002 |pmid= 11909966 |doi=10.1128/MCB.22.8.2743-2750.2002 | pmc=133736 }} |
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*{{cite journal |
*{{cite journal |vauthors=Rayman JB, Takahashi Y, Indjeian VB, etal |title=E2F mediates cell cycle-dependent transcriptional repression in vivo by recruitment of an HDAC1/mSin3B corepressor complex |journal=Genes Dev. |volume=16 |issue= 8 |pages= 933–47 |year= 2002 |pmid= 11959842 |doi= 10.1101/gad.969202 | pmc=152357 }} |
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*{{cite journal | author=Koipally J, Georgopoulos K |title=A molecular dissection of the repression circuitry of Ikaros |journal=J. Biol. Chem. |volume=277 |issue= 31 |pages= 27697–705 |year= 2002 |pmid= 12015313 |doi= 10.1074/jbc.M201694200 }} |
*{{cite journal | author=Koipally J, Georgopoulos K |title=A molecular dissection of the repression circuitry of Ikaros |journal=J. Biol. Chem. |volume=277 |issue= 31 |pages= 27697–705 |year= 2002 |pmid= 12015313 |doi= 10.1074/jbc.M201694200 }} |
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*{{cite journal |
*{{cite journal |vauthors=Yang L, Mei Q, Zielinska-Kwiatkowska A, etal |title=An ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/B |journal=Biochem. J. |volume=369 |issue= Pt 3 |pages= 651–7 |year= 2003 |pmid= 12398767 |doi= 10.1042/BJ20020854 | pmc=1223118 }} |
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*{{cite journal |
*{{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 }} |
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*{{cite journal |
*{{cite journal |vauthors=Petrie K, Guidez F, Howell L, etal |title=The histone deacetylase 9 gene encodes multiple protein isoforms |journal=J. Biol. Chem. |volume=278 |issue= 18 |pages= 16059–72 |year= 2003 |pmid= 12590135 |doi= 10.1074/jbc.M212935200 }} |
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*{{cite journal |
*{{cite journal |vauthors=Wysocka J, Myers MP, Laherty CD, etal |title=Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1 |journal=Genes Dev. |volume=17 |issue= 7 |pages= 896–911 |year= 2003 |pmid= 12670868 |doi= 10.1101/gad.252103 | pmc=196026 }} |
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*{{cite journal |
*{{cite journal |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |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 }} |
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*{{cite journal |
*{{cite journal |vauthors=Dugast-Darzacq C, Pirity M, Blanck JK, etal |title=Mxi1-SRalpha: a novel Mxi1 isoform with enhanced transcriptional repression potential |journal=Oncogene |volume=23 |issue= 55 |pages= 8887–99 |year= 2004 |pmid= 15467743 |doi= 10.1038/sj.onc.1208107 }} |
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*{{cite journal |
*{{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |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 }} |
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*{{cite journal |
*{{cite journal |vauthors=Rampalli S, Pavithra L, Bhatt A, etal |title=Tumor Suppressor SMAR1 Mediates Cyclin D1 Repression by Recruitment of the SIN3/Histone Deacetylase 1 Complex |journal=Mol. Cell. Biol. |volume=25 |issue= 19 |pages= 8415–29 |year= 2005 |pmid= 16166625 |doi= 10.1128/MCB.25.19.8415-8429.2005 | pmc=1265755 }} |
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*{{cite journal | author=Xu Y, Sengupta PK, Seto E, Smith BD |title=RFX family proteins differentially interact with HDACs to repress collagen alpha 2(I) gene (COL1A2) expression |journal=J. Biol. Chem. |volume=281 |issue= 14 |pages= 9260–70 |year= 2006 |pmid= 16464847 |doi= 10.1074/jbc.M511724200 | pmc=1434794 }} |
*{{cite journal | author=Xu Y, Sengupta PK, Seto E, Smith BD |title=RFX family proteins differentially interact with HDACs to repress collagen alpha 2(I) gene (COL1A2) expression |journal=J. Biol. Chem. |volume=281 |issue= 14 |pages= 9260–70 |year= 2006 |pmid= 16464847 |doi= 10.1074/jbc.M511724200 | pmc=1434794 }} |
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Revision as of 03:19, 2 September 2015
Template:PBB Paired amphipathic helix protein Sin3b is a protein that in humans is encoded by the SIN3B gene.[1][2]
Interactions
SIN3B has been shown to interact with HDAC1,[3][4] Zinc finger and BTB domain-containing protein 16,[5] SUDS3[6] and IKZF1.[4][7]
See also
References
- ^ Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (December 1998). "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res. 5 (3): 169–76. doi:10.1093/dnares/5.3.169. PMID 9734811.
{{cite journal}}
: CS1 maint: multiple names: authors list (link) - ^ "Entrez Gene: SIN3B SIN3 homolog B, transcription regulator (yeast)".
- ^ Zhang, Y; Ng H H; Erdjument-Bromage H; Tempst P; Bird A; Reinberg D (August 1999). "Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation". Genes Dev. 13 (15). UNITED STATES: 1924–35. doi:10.1101/gad.13.15.1924. ISSN 0890-9369. PMC 316920. PMID 10444591.
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(help) - ^ a b Koipally, J; Renold A; Kim J; Georgopoulos K (June 1999). "Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes". EMBO J. 18 (11). ENGLAND: 3090–100. doi:10.1093/emboj/18.11.3090. ISSN 0261-4189. PMC 1171390. PMID 10357820.
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(help) - ^ David, G; Alland L; Hong S H; Wong C W; DePinho R A; Dejean A (May 1998). "Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein". Oncogene. 16 (19). ENGLAND: 2549–56. doi:10.1038/sj.onc.1202043. ISSN 0950-9232. PMID 9627120.
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(help) - ^ Alland, Leila (April 2002). "Identification of Mammalian Sds3 as an Integral Component of the Sin3/Histone Deacetylase Corepressor Complex". Mol. Cell. Biol. 22 (8). United States: 2743–50. doi:10.1128/MCB.22.8.2743-2750.2002. ISSN 0270-7306. PMC 133736. PMID 11909966.
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suggested) (help) - ^ Koipally, Joseph; Georgopoulos Katia (August 2002). "A molecular dissection of the repression circuitry of Ikaros". J. Biol. Chem. 277 (31). United States: 27697–705. doi:10.1074/jbc.M201694200. ISSN 0021-9258. PMID 12015313.
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Further reading
External links
- SIN3B+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.