Biology:SIN3A

From HandWiki
Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Paired amphipathic helix protein Sin3a is a protein that in humans is encoded by the SIN3A gene.[1][2]

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.[3]

Interactions

SIN3A has been shown to interact with:

See also

References

  1. ↑ "Histone deacetylase-independent transcriptional repression by methyl-CpG-binding protein 2". Nucleic Acids Research 28 (10): 2201–6. May 2000. doi:10.1093/nar/28.10.2201. PMID 10773092. 
  2. ↑ "A widely distributed putative mammalian transcriptional regulator containing multiple paired amphipathic helices, with similarity to yeast SIN3". Genomics 26 (2): 403–6. March 1995. doi:10.1016/0888-7543(95)80229-F. PMID 7601471. 
  3. ↑ "Entrez Gene: SIN3A SIN3 homolog A, transcription regulator (yeast)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=25942. 
  4. ↑ "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. July 2000. doi:10.1016/S1074-7613(00)00010-8. PMID 10933397. 
  5. ↑ 5.0 5.1 "HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations". Nature Structural & Molecular Biology 11 (8): 738–46. August 2004. doi:10.1038/nsmb798. PMID 15235594. 
  6. ↑ 6.0 6.1 "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. June 2003. doi:10.1016/S0960-0760(03)00230-9. PMID 12943729. https://zenodo.org/record/1260176. 
  7. ↑ "The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity". The Journal of Biological Chemistry 278 (43): 42560–8. October 2003. doi:10.1074/jbc.M302955200. PMID 12920132. 
  8. ↑ 8.0 8.1 8.2 8.3 8.4 "Identification and characterization of three new components of the mSin3A corepressor complex". Molecular and Cellular Biology 23 (10): 3456–67. May 2003. doi:10.1128/MCB.23.10.3456-3467.2003. PMID 12724404. 
  9. ↑ 9.0 9.1 "An ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/B". The Biochemical Journal 369 (Pt 3): 651–7. February 2003. doi:10.1042/BJ20020854. PMID 12398767. 
  10. ↑ "Three proteins define a class of human histone deacetylases related to yeast Hda1p". Proceedings of the National Academy of Sciences of the United States of America 96 (9): 4868–73. April 1999. doi:10.1073/pnas.96.9.4868. PMID 10220385. Bibcode: 1999PNAS...96.4868G. 
  11. ↑ "The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2". Molecular Cell 9 (3): 611–23. March 2002. doi:10.1016/S1097-2765(02)00468-9. PMID 11931768. 
  12. ↑ "CoREST is an integral component of the CoREST- human histone deacetylase complex". Proceedings of the National Academy of Sciences of the United States of America 98 (4): 1454–8. February 2001. doi:10.1073/pnas.98.4.1454. PMID 11171972. Bibcode: 2001PNAS...98.1454Y. 
  13. ↑ 13.0 13.1 "Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation". Genes & Development 13 (15): 1924–35. August 1999. doi:10.1101/gad.13.15.1924. PMID 10444591. 
  14. ↑ 14.0 14.1 "Silencing of transcription of the human luteinizing hormone receptor gene by histone deacetylase-mSin3A complex". The Journal of Biological Chemistry 277 (36): 33431–8. September 2002. doi:10.1074/jbc.M204417200. PMID 12091390. 
  15. ↑ 15.0 15.1 "Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex". Nature 395 (6705): 917–21. October 1998. doi:10.1038/27699. PMID 9804427. Bibcode: 1998Natur.395..917T. 
  16. ↑ "A role for histone deacetylase activity in HDAC1-mediated transcriptional repression". Proceedings of the National Academy of Sciences of the United States of America 95 (7): 3519–24. March 1998. doi:10.1073/pnas.95.7.3519. PMID 9520398. Bibcode: 1998PNAS...95.3519H. 
  17. ↑ "SATB1 targets chromatin remodelling to regulate genes over long distances". Nature 419 (6907): 641–5. October 2002. doi:10.1038/nature01084. PMID 12374985. Bibcode: 2002Natur.419..641Y. https://digital.library.unt.edu/ark:/67531/metadc733622/. 
  18. ↑ 18.0 18.1 "Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway". Genes & Development 14 (1): 45–54. January 2000. doi:10.1101/gad.14.1.45. PMID 10640275. 
  19. ↑ 19.0 19.1 19.2 19.3 19.4 19.5 "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. February 2002. doi:10.1128/MCB.22.3.835-848.2002. PMID 11784859. 
  20. ↑ 20.0 20.1 "Ikaros-CtIP interactions do not require C-terminal binding protein and participate in a deacetylase-independent mode of repression". The Journal of Biological Chemistry 277 (26): 23143–9. June 2002. doi:10.1074/jbc.M202079200. PMID 11959865. 
  21. ↑ "The histone deacetylase 9 gene encodes multiple protein isoforms". The Journal of Biological Chemistry 278 (18): 16059–72. May 2003. doi:10.1074/jbc.M212935200. PMID 12590135. 
  22. ↑ "A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes". The Journal of Biological Chemistry 278 (9): 7234–9. February 2003. doi:10.1074/jbc.M208992200. PMID 12493763. 
  23. ↑ "Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression". Cell 89 (3): 349–56. May 1997. doi:10.1016/S0092-8674(00)80215-9. PMID 9150134. 
  24. ↑ "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. July 2004. doi:10.1128/MCB.24.13.5639-5649.2004. PMID 15199122. 
  25. ↑ "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. April 2003. doi:10.1101/gad.252103. PMID 12670868. 
  26. ↑ "Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes". The EMBO Journal 18 (11): 3090–100. June 1999. doi:10.1093/emboj/18.11.3090. PMID 10357820. 
  27. ↑ "A molecular dissection of the repression circuitry of Ikaros". The Journal of Biological Chemistry 277 (31): 27697–705. August 2002. doi:10.1074/jbc.M201694200. PMID 12015313. 
  28. ↑ "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. August 2001. doi:10.1128/MCB.21.15.5041-5049.2001. PMID 11438660. 
  29. ↑ "Signaling disrupts mSin3A binding to the Mad1-like Sin3-interacting domain of TIEG2, an Sp1-like repressor". The EMBO Journal 21 (10): 2451–60. May 2002. doi:10.1093/emboj/21.10.2451. PMID 12006497. 
  30. ↑ "Rox, a novel bHLHZip protein expressed in quiescent cells that heterodimerizes with Max, binds a non-canonical E box and acts as a transcriptional repressor". The EMBO Journal 16 (10): 2892–906. May 1997. doi:10.1093/emboj/16.10.2892. PMID 9184233. 
  31. ↑ "Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex". Cell 103 (4): 655–65. November 2000. doi:10.1016/S0092-8674(00)00168-9. PMID 11106735. 
  32. ↑ "Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3". Cell 80 (5): 767–76. March 1995. doi:10.1016/0092-8674(95)90355-0. PMID 7889570. 
  33. ↑ "The minimal repression domain of MBD2b overlaps with the methyl-CpG-binding domain and binds directly to Sin3A". The Journal of Biological Chemistry 275 (45): 34963–7. November 2000. doi:10.1074/jbc.M005929200. PMID 10950960. 
  34. ↑ "Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3". The EMBO Journal 19 (16): 4342–50. August 2000. doi:10.1093/emboj/19.16.4342. PMID 10944117. 
  35. ↑ "Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression". Cell 110 (1): 69–80. July 2002. doi:10.1016/S0092-8674(02)00810-3. PMID 12150998. 
  36. ↑ 36.0 36.1 "Pf1, a novel PHD zinc finger protein that links the TLE corepressor to the mSin3A-histone deacetylase complex". Molecular and Cellular Biology 21 (13): 4110–8. July 2001. doi:10.1128/MCB.21.13.4110-4118.2001. PMID 11390640. 
  37. ↑ "Role of PML and PML-RARalpha in Mad-mediated transcriptional repression". Molecular Cell 7 (6): 1233–43. June 2001. doi:10.1016/S1097-2765(01)00257-X. PMID 11430826. 
  38. ↑ "Histone deacetylase activity is required for full transcriptional repression by mSin3A". Cell 89 (3): 341–7. May 1997. doi:10.1016/S0092-8674(00)80214-7. PMID 9150133. 
  39. ↑ 39.0 39.1 39.2 "SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex". Molecular Cell 1 (7): 1021–31. June 1998. doi:10.1016/S1097-2765(00)80102-1. PMID 9651585. 
  40. ↑ "SAP30, a component of the mSin3 corepressor complex involved in N-CoR-mediated repression by specific transcription factors". Molecular Cell 2 (1): 33–42. July 1998. doi:10.1016/S1097-2765(00)80111-2. PMID 9702189. 
  41. ↑ 41.0 41.1 41.2 "Purification and characterization of mSin3A-containing Brg1 and hBrm chromatin remodeling complexes". Genes & Development 15 (5): 603–18. March 2001. doi:10.1101/gad.872801. PMID 11238380. 
  42. ↑ "Identification of mammalian Sds3 as an integral component of the Sin3/histone deacetylase corepressor complex". Molecular and Cellular Biology 22 (8): 2743–50. April 2002. doi:10.1128/MCB.22.8.2743-2750.2002. PMID 11909966. 
  43. ↑ "mSin3A regulates murine erythroleukemia cell differentiation through association with the TAL1 (or SCL) transcription factor". Molecular and Cellular Biology 20 (6): 2248–59. March 2000. doi:10.1128/MCB.20.6.2248-2259.2000. PMID 10688671. 
  44. ↑ "Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein". Oncogene 16 (19): 2549–56. May 1998. doi:10.1038/sj.onc.1202043. PMID 9627120. 
  45. ↑ "The acute promyelocytic leukemia-associated protein, promyelocytic leukemia zinc finger, regulates 1,25-dihydroxyvitamin D(3)-induced monocytic differentiation of U937 cells through a physical interaction with vitamin D(3) receptor". Blood 98 (12): 3290–300. December 2001. doi:10.1182/blood.V98.12.3290. PMID 11719366. 
  46. ↑ "Components of the SMRT corepressor complex exhibit distinctive interactions with the POZ domain oncoproteins PLZF, PLZF-RARalpha, and BCL-6". The Journal of Biological Chemistry 273 (42): 27695–702. October 1998. doi:10.1074/jbc.273.42.27695. PMID 9765306. 

Further reading


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



Retrieved from "https://handwiki.org/wiki/index.php?title=Biology:SIN3A&oldid=459671"