SIN3A

Protein-coding gene in the species Homo sapiens
SIN3A
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1PO4

Identifiers
AliasesSIN3A, Paired amphipathic helix protein Sin3a, SIN3 transcription regulator family member A, WITKOS
External IDsOMIM: 607776 MGI: 107157 HomoloGene: 32124 GeneCards: SIN3A
Gene location (Human)
Chromosome 15 (human)
Chr.Chromosome 15 (human)[1]
Chromosome 15 (human)
Genomic location for SIN3A
Genomic location for SIN3A
Band15q24.2Start75,369,379 bp[1]
End75,455,842 bp[1]
Gene location (Mouse)
Chromosome 9 (mouse)
Chr.Chromosome 9 (mouse)[2]
Chromosome 9 (mouse)
Genomic location for SIN3A
Genomic location for SIN3A
Band9 B|9 30.89 cMStart56,979,324 bp[2]
End57,035,650 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • secondary oocyte

  • pancreatic ductal cell

  • bone marrow cells

  • ganglionic eminence

  • Achilles tendon

  • skin of limb

  • canal of the cervix

  • sural nerve

  • skin of abdomen

  • islet of Langerhans
Top expressed in
  • secondary oocyte

  • ectoderm

  • otic placode

  • saccule

  • medullary collecting duct

  • yolk sac

  • spermatid

  • renal corpuscle

  • spermatocyte

  • thymus
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • DNA binding
  • transcription corepressor activity
  • histone deacetylase activity
  • DNA-binding transcription factor activity
  • protein deacetylase activity
  • transcription factor binding
  • chromatin binding
  • transcription cis-regulatory region binding
  • protein binding
  • RNA binding
  • protein-containing complex binding
Cellular component
  • transcription regulator complex
  • transcription repressor complex
  • nucleoplasm
  • nucleolus
  • chromatin
  • nucleus
  • kinetochore
  • Sin3 complex
  • protein-containing complex
Biological process
  • negative regulation of protein localization to nucleus
  • regulation of transcription, DNA-templated
  • regulation of transcription from RNA polymerase II promoter in response to oxidative stress
  • rhythmic process
  • cellular response to dopamine
  • response to methylglyoxal
  • negative regulation of circadian rhythm
  • regulation of hormone levels
  • human ageing
  • negative regulation of apoptotic process
  • in utero embryonic development
  • negative regulation of transcription by RNA polymerase II
  • transcription, DNA-templated
  • protein deacetylation
  • DNA replication
  • negative regulation of transcription regulatory region DNA binding
  • response to organonitrogen compound
  • hematopoietic progenitor cell differentiation
  • activation of innate immune response
  • positive regulation of G2/M transition of mitotic cell cycle
  • negative regulation of transcription, DNA-templated
  • histone deacetylation
  • negative regulation of histone H3-K27 acetylation
  • cellular response to glucose stimulus
  • positive regulation of transcription by RNA polymerase II
  • positive regulation of defense response to virus by host
  • regulation of lipid metabolic process
  • regulation of megakaryocyte differentiation
  • negative regulation of nucleic acid-templated transcription
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

25942

20466

Ensembl

ENSG00000169375

ENSMUSG00000042557

UniProt

Q96ST3

Q60520

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: ENSG00000169375 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000042557 - Ensembl, 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.
  11. ^ Yao YL, Yang WM (October 2003). "The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity". The Journal of Biological Chemistry. 278 (43): 42560–8. doi:10.1074/jbc.M302955200. PMID 12920132.
  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.
  13. ^ a b Yang L, Mei Q, Zielinska-Kwiatkowska A, Matsui Y, Blackburn ML, Benedetti D, Krumm AA, Taborsky GJ, Chansky HA (February 2003). "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. doi:10.1042/BJ20020854. PMC 1223118. PMID 12398767.
  14. ^ Grozinger CM, Hassig CA, Schreiber SL (April 1999). "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. Bibcode:1999PNAS...96.4868G. doi:10.1073/pnas.96.9.4868. PMC 21783. PMID 10220385.
  15. ^ Zhang J, Kalkum M, Chait BT, Roeder RG (March 2002). "The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2". Molecular Cell. 9 (3): 611–23. doi:10.1016/S1097-2765(02)00468-9. PMID 11931768.
  16. ^ You A, Tong JK, Grozinger CM, Schreiber SL (February 2001). "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. Bibcode:2001PNAS...98.1454Y. doi:10.1073/pnas.98.4.1454. PMC 29278. PMID 11171972.
  17. ^ a b Zhang Y, Ng HH, 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 & Development. 13 (15): 1924–35. doi:10.1101/gad.13.15.1924. PMC 316920. PMID 10444591.
  18. ^ a b Zhang Y, Dufau ML (September 2002). "Silencing of transcription of the human luteinizing hormone receptor gene by histone deacetylase-mSin3A complex". The Journal of Biological Chemistry. 277 (36): 33431–8. doi:10.1074/jbc.M204417200. PMID 12091390.
  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.
  20. ^ Hassig CA, Tong JK, Fleischer TC, Owa T, Grable PG, Ayer DE, Schreiber SL (March 1998). "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. Bibcode:1998PNAS...95.3519H. doi:10.1073/pnas.95.7.3519. PMC 19868. PMID 9520398.
  21. ^ Yasui D, Miyano M, Cai S, Varga-Weisz P, Kohwi-Shigematsu T (October 2002). "SATB1 targets chromatin remodelling to regulate genes over long distances". Nature. 419 (6907): 641–5. Bibcode:2002Natur.419..641Y. doi:10.1038/nature01084. PMID 12374985. S2CID 25822700.
  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.
  24. ^ a b Koipally J, Georgopoulos K (June 2002). "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. doi:10.1074/jbc.M202079200. PMID 11959865.
  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.
  26. ^ Hakimi MA, Dong Y, Lane WS, Speicher DW, Shiekhattar R (February 2003). "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. doi:10.1074/jbc.M208992200. PMID 12493763.
  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.
  30. ^ Koipally J, Renold A, Kim J, Georgopoulos K (June 1999). "Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes". The EMBO Journal. 18 (11): 3090–100. doi:10.1093/emboj/18.11.3090. PMC 1171390. PMID 10357820.
  31. ^ Koipally J, Georgopoulos K (August 2002). "A molecular dissection of the repression circuitry of Ikaros". The Journal of Biological Chemistry. 277 (31): 27697–705. doi:10.1074/jbc.M201694200. PMID 12015313.
  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.
  34. ^ Meroni G, Reymond A, Alcalay M, Borsani G, Tanigami A, Tonlorenzi R, Lo Nigro C, Messali S, Zollo M, Ledbetter DH, Brent R, Ballabio A, Carrozzo R (May 1997). "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. doi:10.1093/emboj/16.10.2892. PMC 1169897. PMID 9184233.
  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.
  36. ^ Ayer DE, Lawrence QA, Eisenman RN (March 1995). "Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3". Cell. 80 (5): 767–76. doi:10.1016/0092-8674(95)90355-0. PMID 7889570. S2CID 8749951.
  37. ^ Boeke J, Ammerpohl O, Kegel S, Moehren U, Renkawitz R (November 2000). "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. doi:10.1074/jbc.M005929200. PMID 10950960.
  38. ^ Li J, Wang J, Wang J, Nawaz Z, Liu JM, Qin J, Wong J (August 2000). "Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3". The EMBO Journal. 19 (16): 4342–50. doi:10.1093/emboj/19.16.4342. PMC 302030. PMID 10944117.
  39. ^ Yang X, Zhang F, Kudlow JE (July 2002). "Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression". Cell. 110 (1): 69–80. doi:10.1016/S0092-8674(02)00810-3. PMID 12150998. S2CID 2380973.
  40. ^ a b Yochum GS, Ayer DE (July 2001). "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. doi:10.1128/MCB.21.13.4110-4118.2001. PMC 87072. PMID 11390640.
  41. ^ Khan MM, Nomura T, Kim H, Kaul SC, Wadhwa R, Shinagawa T, Ichikawa-Iwata E, Zhong S, Pandolfi PP, Ishii S (June 2001). "Role of PML and PML-RARalpha in Mad-mediated transcriptional repression". Molecular Cell. 7 (6): 1233–43. doi:10.1016/S1097-2765(01)00257-X. PMID 11430826.
  42. ^ Hassig CA, Fleischer TC, Billin AN, Schreiber SL, Ayer DE (May 1997). "Histone deacetylase activity is required for full transcriptional repression by mSin3A". Cell. 89 (3): 341–7. doi:10.1016/S0092-8674(00)80214-7. PMID 9150133. S2CID 14233219.
  43. ^ a b c Zhang Y, Sun ZW, Iratni R, Erdjument-Bromage H, Tempst P, Hampsey M, Reinberg D (June 1998). "SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex". Molecular Cell. 1 (7): 1021–31. doi:10.1016/S1097-2765(00)80102-1. PMID 9651585.
  44. ^ Laherty CD, Billin AN, Lavinsky RM, Yochum GS, Bush AC, Sun JM, Mullen TM, Davie JR, Rose DW, Glass CK, Rosenfeld MG, Ayer DE, Eisenman RN (July 1998). "SAP30, a component of the mSin3 corepressor complex involved in N-CoR-mediated repression by specific transcription factors". Molecular Cell. 2 (1): 33–42. doi:10.1016/S1097-2765(00)80111-2. PMID 9702189.
  45. ^ a b c Sif S, Saurin AJ, Imbalzano AN, Kingston RE (March 2001). "Purification and characterization of mSin3A-containing Brg1 and hBrm chromatin remodeling complexes". Genes & Development. 15 (5): 603–18. doi:10.1101/gad.872801. PMC 312641. PMID 11238380.
  46. ^ Alland L, David G, Shen-Li H, Potes J, Muhle R, Lee HC, Hou H, Chen K, DePinho RA (April 2002). "Identification of mammalian Sds3 as an integral component of the Sin3/histone deacetylase corepressor complex". Molecular and Cellular Biology. 22 (8): 2743–50. doi:10.1128/MCB.22.8.2743-2750.2002. PMC 133736. PMID 11909966.
  47. ^ Huang S, Brandt SJ (March 2000). "mSin3A regulates murine erythroleukemia cell differentiation through association with the TAL1 (or SCL) transcription factor". Molecular and Cellular Biology. 20 (6): 2248–59. doi:10.1128/MCB.20.6.2248-2259.2000. PMC 110841. PMID 10688671.
  48. ^ David G, Alland L, Hong SH, Wong CW, DePinho RA, Dejean A (May 1998). "Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein". Oncogene. 16 (19): 2549–56. doi:10.1038/sj.onc.1202043. PMID 9627120. S2CID 655636.
  49. ^ Ward JO, McConnell MJ, Carlile GW, Pandolfi PP, Licht JD, Freedman LP (December 2001). "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. doi:10.1182/blood.V98.12.3290. PMID 11719366.
  50. ^ Wong CW, Privalsky ML (October 1998). "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. doi:10.1074/jbc.273.42.27695. PMID 9765306.

Further reading

  • 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.
  • Ayer DE, Lawrence QA, Eisenman RN (March 1995). "Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3". Cell. 80 (5): 767–76. doi:10.1016/0092-8674(95)90355-0. PMID 7889570. S2CID 8749951.
  • Hurlin PJ, Quéva C, Koskinen PJ, Steingrímsson E, Ayer DE, Copeland NG, Jenkins NA, Eisenman RN (November 1995). "Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation". The EMBO Journal. 14 (22): 5646–59. doi:10.1002/j.1460-2075.1995.tb00252.x. PMC 394680. PMID 8521822.
  • Hassig CA, Fleischer TC, Billin AN, Schreiber SL, Ayer DE (May 1997). "Histone deacetylase activity is required for full transcriptional repression by mSin3A". Cell. 89 (3): 341–7. doi:10.1016/S0092-8674(00)80214-7. PMID 9150133. S2CID 14233219.
  • 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.
  • Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D (May 1997). "Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex". Cell. 89 (3): 357–64. doi:10.1016/S0092-8674(00)80216-0. PMID 9150135.
  • Meroni G, Reymond A, Alcalay M, Borsani G, Tanigami A, Tonlorenzi R, Lo Nigro C, Messali S, Zollo M, Ledbetter DH, Brent R, Ballabio A, Carrozzo R (May 1997). "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. doi:10.1093/emboj/16.10.2892. PMC 1169897. PMID 9184233.
  • Lin RJ, Nagy L, Inoue S, Shao W, Miller WH, Evans RM (February 1998). "Role of the histone deacetylase complex in acute promyelocytic leukaemia". Nature. 391 (6669): 811–4. Bibcode:1998Natur.391..811L. doi:10.1038/35895. PMID 9486654. S2CID 4383951.
  • David G, Alland L, Hong SH, Wong CW, DePinho RA, Dejean A (May 1998). "Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein". Oncogene. 16 (19): 2549–56. doi:10.1038/sj.onc.1202043. PMID 9627120. S2CID 655636.
  • Wong CW, Privalsky ML (October 1998). "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. doi:10.1074/jbc.273.42.27695. PMID 9765306.
  • Zhang Y, LeRoy G, Seelig HP, Lane WS, Reinberg D (October 1998). "The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities". Cell. 95 (2): 279–89. doi:10.1016/S0092-8674(00)81758-4. PMID 9790534. S2CID 18786866.
  • 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.
  • Koipally J, Renold A, Kim J, Georgopoulos K (June 1999). "Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes". The EMBO Journal. 18 (11): 3090–100. doi:10.1093/emboj/18.11.3090. PMC 1171390. PMID 10357820.
  • Boutell JM, Thomas P, Neal JW, Weston VJ, Duce J, Harper PS, Jones AL (September 1999). "Aberrant interactions of transcriptional repressor proteins with the Huntington's disease gene product, huntingtin". Human Molecular Genetics. 8 (9): 1647–55. doi:10.1093/hmg/8.9.1647. PMID 10441327.
  • Zhang Y, Ng HH, 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 & Development. 13 (15): 1924–35. doi:10.1101/gad.13.15.1924. PMC 316920. PMID 10444591.
  • Kao HY, Downes M, Ordentlich P, Evans RM (January 2000). "Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression". Genes & Development. 14 (1): 55–66. doi:10.1101/gad.14.1.55. PMC 316336. PMID 10640276.
  • Huang S, Brandt SJ (March 2000). "mSin3A regulates murine erythroleukemia cell differentiation through association with the TAL1 (or SCL) transcription factor". Molecular and Cellular Biology. 20 (6): 2248–59. doi:10.1128/MCB.20.6.2248-2259.2000. PMC 110841. PMID 10688671.
  • Koipally J, Georgopoulos K (June 2000). "Ikaros interactions with CtBP reveal a repression mechanism that is independent of histone deacetylase activity". The Journal of Biological Chemistry. 275 (26): 19594–602. doi:10.1074/jbc.M000254200. PMID 10766745.

External links

  • v
  • t
  • e
  • 1g1e: NMR STRUCTURE OF THE HUMAN MAD1 TRANSREPRESSION DOMAIN SID IN COMPLEX WITH MAMMALIAN SIN3A PAH2 DOMAIN
    1g1e: NMR STRUCTURE OF THE HUMAN MAD1 TRANSREPRESSION DOMAIN SID IN COMPLEX WITH MAMMALIAN SIN3A PAH2 DOMAIN
  • 1s5q: Solution Structure of Mad1 SID-mSin3A PAH2 Complex
    1s5q: Solution Structure of Mad1 SID-mSin3A PAH2 Complex
  • 1s5r: Solution Structure of HBP1 SID-mSin3A PAH2 Complex
    1s5r: Solution Structure of HBP1 SID-mSin3A PAH2 Complex
  • v
  • t
  • e
Coactivators
Corepressors
ATP-dependent remodeling factors
  • Chromatin Structure Remodeling (RSC) Complex
  • SWI/SNF


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