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SIN3A

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SIN3A
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesSIN3A, Paired amphipathic helix protein Sin3a, SIN3 transcription regulator family member A, WITKOS
External IDsOMIM: 607776; MGI: 107157; HomoloGene: 32124; GeneCards: SIN3A; OMA:SIN3A - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001145357
NM_001145358
NM_015477

NM_001110350
NM_001110351
NM_011378
NM_001357754

RefSeq (protein)

NP_001138829
NP_001138830
NP_056292

NP_001103820
NP_001103821
NP_035508
NP_001344683

Location (UCSC)Chr 15: 75.37 – 75.46 MbChr 9: 56.98 – 57.04 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Paired amphipathic helix protein Sin3a is a protein that in humans is encoded by the SIN3A gene.[5][6]

Function

The protein encoded by this gene is a transcriptional regulatory protein. It contains paired amphipathic helix (PAH) domains, which are important for protein-protein interactions and may mediate repression by the Mad-Max complex.[7]

Interactions

SIN3A has been shown to interact with:

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000169375Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000042557Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Yu F, Thiesen J, Strätling WH (May 2000). "Histone deacetylase-independent transcriptional repression by methyl-CpG-binding protein 2". Nucleic Acids Research. 28 (10): 2201–6. doi:10.1093/nar/28.10.2201. PMC 105362. PMID 10773092.
  6. ^ Halleck MS, Pownall S, Harder KW, Duncan AM, Jirik FR, Schlegel RA (March 1995). "A widely distributed putative mammalian transcriptional regulator containing multiple paired amphipathic helices, with similarity to yeast SIN3". Genomics. 26 (2): 403–6. doi:10.1016/0888-7543(95)80229-F. PMID 7601471.
  7. ^ "Entrez Gene: SIN3A SIN3 homolog A, transcription regulator (yeast)".
  8. ^ Youn HD, Liu JO (July 2000). "Cabin1 represses MEF2-dependent Nur77 expression and T cell apoptosis by controlling association of histone deacetylases and acetylases with MEF2". Immunity. 13 (1): 85–94. doi:10.1016/S1074-7613(00)00010-8. PMID 10933397.
  9. ^ a b Swanson KA, Knoepfler PS, Huang K, Kang RS, Cowley SM, Laherty CD, Eisenman RN, Radhakrishnan I (August 2004). "HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations". Nature Structural & Molecular Biology. 11 (8): 738–46. doi:10.1038/nsmb798. PMID 15235594. S2CID 44324333.
  10. ^ a b Zhang Y, Dufau ML (June 2003). "Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes". The Journal of Steroid Biochemistry and Molecular Biology. 85 (2–5): 401–14. doi:10.1016/S0960-0760(03)00230-9. PMID 12943729. S2CID 28512341.
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  12. ^ a b c d e Fleischer TC, Yun UJ, Ayer DE (May 2003). "Identification and characterization of three new components of the mSin3A corepressor complex". Molecular and Cellular Biology. 23 (10): 3456–67. doi:10.1128/MCB.23.10.3456-3467.2003. PMC 164750. PMID 12724404.
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  19. ^ a b Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL (October 1998). "Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex". Nature. 395 (6705): 917–21. Bibcode:1998Natur.395..917T. doi:10.1038/27699. PMID 9804427. S2CID 4355885.
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  22. ^ a b Huang EY, Zhang J, Miska EA, Guenther MG, Kouzarides T, Lazar MA (January 2000). "Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway". Genes & Development. 14 (1): 45–54. doi:10.1101/gad.14.1.45. PMC 316335. PMID 10640275.
  23. ^ a b c d e f Kuzmichev A, Zhang Y, Erdjument-Bromage H, Tempst P, Reinberg D (February 2002). "Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)". Molecular and Cellular Biology. 22 (3): 835–48. doi:10.1128/MCB.22.3.835-848.2002. PMC 133546. PMID 11784859.
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  25. ^ Petrie K, Guidez F, Howell L, Healy L, Waxman S, Greaves M, Zelent A (May 2003). "The histone deacetylase 9 gene encodes multiple protein isoforms". The Journal of Biological Chemistry. 278 (18): 16059–72. doi:10.1074/jbc.M212935200. PMID 12590135.
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  27. ^ Laherty CD, Yang WM, Sun JM, Davie JR, Seto E, Eisenman RN (May 1997). "Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression". Cell. 89 (3): 349–56. doi:10.1016/S0092-8674(00)80215-9. PMID 9150134. S2CID 13490886.
  28. ^ Yokoyama A, Wang Z, Wysocka J, Sanyal M, Aufiero DJ, Kitabayashi I, Herr W, Cleary ML (July 2004). "Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression". Molecular and Cellular Biology. 24 (13): 5639–49. doi:10.1128/MCB.24.13.5639-5649.2004. PMC 480881. PMID 15199122.
  29. ^ Wysocka J, Myers MP, Laherty CD, Eisenman RN, Herr W (April 2003). "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1". Genes & Development. 17 (7): 896–911. doi:10.1101/gad.252103. PMC 196026. PMID 12670868.
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  32. ^ Zhang JS, Moncrieffe MC, Kaczynski J, Ellenrieder V, Prendergast FG, Urrutia R (August 2001). "A conserved alpha-helical motif mediates the interaction of Sp1-like transcriptional repressors with the corepressor mSin3A". Molecular and Cellular Biology. 21 (15): 5041–9. doi:10.1128/MCB.21.15.5041-5049.2001. PMC 87230. PMID 11438660.
  33. ^ Ellenrieder V, Zhang JS, Kaczynski J, Urrutia R (May 2002). "Signaling disrupts mSin3A binding to the Mad1-like Sin3-interacting domain of TIEG2, an Sp1-like repressor". The EMBO Journal. 21 (10): 2451–60. doi:10.1093/emboj/21.10.2451. PMC 126002. PMID 12006497.
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  35. ^ Brubaker K, Cowley SM, Huang K, Loo L, Yochum GS, Ayer DE, Eisenman RN, Radhakrishnan I (November 2000). "Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex". Cell. 103 (4): 655–65. doi:10.1016/S0092-8674(00)00168-9. PMID 11106735. S2CID 17476603.
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Further reading


This article incorporates text from the United States National Library of Medicine, which is in the public domain.