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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

SDS3 Sds3p

Sds3, mSds3, SUDS3, Sds3p
SDS3 is a subunit of the histone deacetylase (see HDAC1; MIM 601241)-dependent SIN3A (MIM 607776) corepressor complex (Fleischer et al., 2003 [PubMed 12724404]).[supplied by OMIM, Mar 2008] (from NCBI)
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Top mentioned proteins: Histone, mSin3A, HDAC, RPD3, CAN
Papers on Sds3
A genomewide association mapping study using ultrasound-scanned information identifies potential genomic regions and candidate genes affecting carcass traits in Nellore cattle.
Ferraz et al., Pirassununga, Brazil. In J Anim Breed Genet, Dec 2015
Several of the significant markers detected were mapped onto functional candidate genes including ARFGAP3, CLSTN2 and DPYD for REA; OSBPL3 and SUDS3 for BFT; and RARRES1 and VEPH1 for RFT.
Human family with sequence similarity 60 member A (FAM60A) protein: a new subunit of the Sin3 deacetylase complex.
Workman et al., Kansas City, United States. In Mol Cell Proteomics, 2012
Moreover, our studies reveal that loss of FAM60A or another component of the Sin3 complex, SDS3, leads to a change in cell morphology and an increase in cell migration.
Cdk5 phosphorylates a component of the HDAC complex and regulates histone acetylation during neuronal cell death.
Ip et al., Hong Kong, Hong Kong. In Neurosignals, 2012
We have previously found that p35, a Cdk5 activator, interacts with mSds3, an integral component of the histone deacetylase complex in vitro, suggesting a functional role of Cdk5 in gene regulation through modulation of chromatin integrity.
SDS3 interacts with ARNT in an AhR ligand-specific manner regulating expression of cKrox and S100A4 in CD4+CD8+ DPK thymocytes differentiation.
Park et al., Ch'angwŏn, South Korea. In Environ Toxicol Pharmacol, 2012
Immunoprecipitation using anti-ARNT Ab revealed that SDS3, a component of the Sin3/HDAC repressor complex, was associated with ARNT only when DPK cells were incubated with TCDD.
Foxk1 recruits the Sds3 complex and represses gene expression in myogenic progenitors.
Garry et al., Minneapolis, United States. In Biochem J, 2012
the identification of Sds3 (suppressor of defective silencing 3) as an adaptor protein that recruits the Sin3 [SWI (switch)-independent 3]-HDAC (histone deacetylase) repression complex and binds Foxk1.
Hyaluronan binding motifs of USP17 and SDS3 exhibit anti-tumor activity.
Baek et al., South Korea. In Plos One, 2011
BACKGROUND: We previously reported that the USP17 deubiquitinating enzyme having hyaluronan binding motifs (HABMs) interacts with human SDS3 (suppressor of defective silencing 3) and specifically deubiquitinates Lys-63 branched polyubiquitination of SDS3 resulting in negative regulation of histone deacetylase (HDAC) activity in cancer cells.
Lys-63-specific deubiquitination of SDS3 by USP17 regulates HDAC activity.
Baek et al., Seoul, South Korea. In J Biol Chem, 2011
SDS3, being a substrate of USP17, may play an important role in developing a novel therapeutic means to inhibit specific HDAC activities in cancer.
Over-expression of the BRMS1 family member SUDS3 does not suppress metastasis of human cancer cells.
Welch et al., Birmingham, United States. In Cancer Lett, 2009
the composition of SIN3-HDAC (BRMS1/SUDS3) complexes uniquely affects protein expression and biological behaviors
Isolation and characterization of sexual dimorphism genes expressed in chicken embryonic gonads.
Gong et al., Wuhan, China. In Acta Biochim Biophys Sin (shanghai), 2009
Quantitative real-time PCR analysis of eight genes involved in epigenetic and transcription regulation showed significantly different expression between sexes of CDK2AP1, SMARCE1, SAP18, SUDS3, and PQBP1 appeared at the early stage in gonad development (E4).
Different genetic functions for the Rpd3(L) and Rpd3(S) complexes suggest competition between NuA4 and Rpd3(S).
Stillman et al., Salt Lake City, United States. In Mol Cell Biol, 2008
Disruption of the GCN5 histone acetyltransferase gene shows a strong synthetic phenotype when combined with either an sds3 mutation affecting only the Rpd3(L) complex or an rco1 mutation affecting only Rpd3(S).
Identification of differentially expressed genes induced by hydroxyurea in reticulocytes from sickle cell anaemia patients.
Costa et al., Campinas, Brazil. In Clin Exp Pharmacol Physiol, 2008
5. Genes identified with altered expression included SUDS3, FZD5 and PHC3, which may be associated with the regulation of globin expression.
Systematic, genome-wide, sex-specific linkage of cardiovascular traits in French Canadians.
Hamet et al., Montréal, Canada. In Hypertension, 2008
Detailed interrogation of this locus revealed a 220-kb block overlapping parts of TAO-kinase 3 and SUDS3 genes.
Haploinsufficiency of the mSds3 chromatin regulator promotes chromosomal instability and cancer only upon complete neutralization of p53.
Depinho et al., Boston, United States. In Oncogene, 2006
capacity of mSds3 to cooperate with p53 deficiency in cancer predisposition relates to its specific role in chromosome segregation, rather than its central role in maintaining a functional mSin3A complex
Cdk5/p35 phosphorylates mSds3 and regulates mSds3-mediated repression of transcription.
Ip et al., Hong Kong, Hong Kong. In J Biol Chem, 2005
Here, we report a physical and functional interaction between the Cdk5/p35 complex and mouse Sds3 (mSds3), an essential component of mSin3-histone deacetylase (HDAC) co-repressor complex.
Tetraiodophenolsulfonphthalein as a spectral substitute to characterize the complexation between cationic and anionic surfactant.
Hu et al., Shanghai, China. In J Colloid Interface Sci, 2004
The aggregates TIPST-CTAB, TIPST2-CTAB3, SDS3-CTAB2, and SDBS3-CTAB2 were formed at 20 degrees C and the binding constants of all the aggregates were determined.
Identification of a novel BRMS1-homologue protein p40 as a component of the mSin3A/p33(ING1b)/HDAC1 deacetylase complex.
Gu et al., New York City, United States. In Biochem Biophys Res Commun, 2004
p40 bears homology to both yeast Sds3, a component of yeast histone deacetylase complexes, and its mammalian homologue mSds3.
mSin3-associated protein, mSds3, is essential for pericentric heterochromatin formation and chromosome segregation in mammalian cells.
DePinho et al., Boston, United States. In Genes Dev, 2003
mSds3 and its associated mSin3/HDAC components play a central role in initiating the cascade of pericentric heterochromatin-specific modifications necessary for the proper distribution of chromosomes during cell division in mammalian cells.
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