• negative regulation of transcription from RNA polymerase II promoter
• in utero embryonic development
• activation of innate immune response
• positive regulation of defense response to virus by host
• DNA replication
• transcription, DNA-templated
• protein deacetylation
• aging
• blood coagulation
• response to organonitrogen compound
• positive regulation of G2/M transition of mitotic cell cycle
• positive regulation of chromatin silencing
• cellular protein localization
• negative regulation of circadian rhythm
• negative regulation of apoptotic process
• regulation of transcription from RNA polymerase II promoter in response to oxidative stress
• cellular lipid metabolic process
• small molecule metabolic process
• negative regulation of transcription, DNA-templated
• positive regulation of transcription from RNA polymerase II promoter
• rhythmic process
• response to methylglyoxal
• cellular response to glucose stimulus
• negative regulation of protein localization to nucleus
• negative regulation of histone H3-K27 acetylation
• negative regulation of transcription regulatory region DNA binding
Белок, кодируемый этим геном — регулятор транскрипции. Он содержит в парной амфипатической спирали (PAH) домены, которые важны для белок-белковых взаимодействий и могут опосредовать репрессию при помощи Mad-Max комплекса[3].
Entrez Gene: SIN3A SIN3 homolog A, transcription regulator (yeast).
PMID 10933397.
↑ PMID 15235594.
↑ PMID 12943729.
PMID 12920132.
↑ PMID 12724404.
↑ PMID 12398767.
PMID 10220385.
PMID 11931768.
PMID 11171972.
↑ PMID 10444591.
↑ PMID 12091390.
↑ PMID 9804427.
PMID 9520398.
PMID 12374985.
↑ PMID 10640275.
↑ PMID 11784859.
↑ PMID 11959865.
PMID 12590135.
PMID 12493763.
PMID 9150134.
PMID 15199122.
PMID 12670868.
PMID 10357820.
PMID 12015313.
PMID 11438660.
PMID 12006497.
PMID 9184233.
PMID 11106735.
PMID 7889570.
PMID 10950960.
PMID 10944117.
PMID 12150998.
↑ PMID 11390640.
PMID 11430826.
PMID 9150133.
↑ PMID 9651585.
PMID 9702189.
↑ PMID 11238380.
PMID 11909966.
PMID 10688671.
PMID 9627120.
PMID 11719366.
PMID 9765306.
Литература
Zhang Y, Dufau ML (2003). «Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes.». J. Steroid Biochem. Mol. Biol.85 (2-5): 401–14. PMID 12943729.
Ayer DE, Lawrence QA, Eisenman RN (1995). «Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3.». Cell80 (5): 767–76. PMID 7889570.
Hurlin PJ, Quéva C, Koskinen PJ, et al. (1996). «Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation.». EMBO J.14 (22): 5646–59. PMID 8521822.
Hassig CA, Fleischer TC, Billin AN, et al. (1997). «Histone deacetylase activity is required for full transcriptional repression by mSin3A.». Cell89 (3): 341–7. PMID 9150133.
Laherty CD, Yang WM, Sun JM, et al. (1997). «Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression.». Cell89 (3): 349–56. PMID 9150134.
Zhang Y, Iratni R, Erdjument-Bromage H, et al. (1997). «Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex.». Cell89 (3): 357–64. PMID 9150135.
Meroni G, Reymond A, Alcalay M, et al. (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.». EMBO J.16 (10): 2892–906. PMID 9184233.
Lin RJ, Nagy L, Inoue S, et al. (1998). «Role of the histone deacetylase complex in acute promyelocytic leukaemia.». Nature391 (6669): 811–4. PMID 9486654.
David G, Alland L, Hong SH, et al. (1998). «Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein.». Oncogene16 (19): 2549–56. PMID 9627120.
Wong CW, Privalsky ML (1998). «Components of the SMRT corepressor complex exhibit distinctive interactions with the POZ domain oncoproteins PLZF, PLZF-RARalpha, and BCL-6.». J. Biol. Chem.273 (42): 27695–702. PMID 9765306.
Zhang Y, LeRoy G, Seelig HP, et al. (1998). «The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities.». Cell95 (2): 279–89. PMID 9790534.
Tong JK, Hassig CA, Schnitzler GR, et al. (1998). «Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex.». Nature395 (6705): 917–21. PMID 9804427.
Koipally J, Renold A, Kim J, Georgopoulos K (1999). «Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes.». EMBO J.18 (11): 3090–100. PMID 10357820.
Boutell JM, Thomas P, Neal JW, et al. (2000). «Aberrant interactions of transcriptional repressor proteins with the Huntington's disease gene product, huntingtin.». Hum. Mol. Genet.8 (9): 1647–55. PMID 10441327.
Zhang Y, Ng HH, Erdjument-Bromage H, et al. (1999). «Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation.». Genes Dev.13 (15): 1924–35. PMID 10444591.
Kao HY, Downes M, Ordentlich P, Evans RM (2000). «Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression.». Genes Dev.14 (1): 55–66. PMID 10640276.
Huang S, Brandt SJ (2000). «mSin3A regulates murine erythroleukemia cell differentiation through association with the TAL1 (or SCL) transcription factor.». Mol. Cell. Biol.20 (6): 2248–59. PMID 10688671.
Koipally J, Georgopoulos K (2000). «Ikaros interactions with CtBP reveal a repression mechanism that is independent of histone deacetylase activity.». J. Biol. Chem.275 (26): 19594–602. PMID 10766745.