gopubmed logo
 
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

SET and MYND domain containing 3

SMYD3, SET and MYND domain-containing protein 3, SET and MYND domain containing 3
This gene encodes a histone methyltransferase which functions in RNA polymerase II complexes by an interaction with a specific RNA helicase. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Dec 2011] (from NCBI)
Top mentioned proteins: Histone, SET, POLYMERASE, CAN, c-Myc
Papers on SMYD3
Interaction of the hepatitis B virus X protein with the lysine methyltransferase SET and MYND domain-containing 3 induces activator protein 1 activation.
New
Hotta et al., Kōbe, Japan. In Microbiol Immunol, Jan 2016
Recently, the nonstructural protein 5A (NS5A) of hepatitis C virus has been reported to interact with methyltransferase SET and MYND domain-containing 3 (SMYD3), which is implicated in chromatin modification and development of cancer.
A novel nuclear Src and p300 signaling axis controls migratory and invasive behavior in pancreatic cancer.
New
Turkson et al., Honolulu, United States. In Oncotarget, Jan 2016
Moreover, analyses of human pancreatic ductal adenocarcinoma (PDAC) tumor tissues detected the association of nuclear Src with the HMGA2 and SMYD3 gene promoters.
Upregulated SMYD3 promotes bladder cancer progression by targeting BCLAF1 and activating autophagy.
New
Fan et al., Shanghai, China. In Tumour Biol, Jan 2016
SMYD3, a histone methyltransferase, is associated with poor prognosis of patients with prostate and gastric cancer.
SET and MYND domain-containing protein 3 is overexpressed in human glioma and contributes to tumorigenicity.
New
Zhang et al., Beijing, China. In Oncol Rep, Nov 2015
SET and MYND domain-containing protein 3 (SMYD3) is a histone H3 lysine 4 (H3K4) di- and tri-methyltransferase that forms a transcriptional complex with RNA polymerase II and plays an important role in early embryonic lineage commitment through the activation of lineage-specific genes.
Cooperation between SMYD3 and PC4 drives a distinct transcriptional program in cancer cells.
New
An et al., Los Angeles, United States. In Nucleic Acids Res, Nov 2015
SET and MYND domain containing protein 3 (SMYD3) is a histone methyltransferase, which has been implicated in cell growth and cancer pathogenesis.
Elevated Levels of SET and MYND Domain-Containing Protein 3 Are Correlated with Overexpression of Transforming Growth Factor-β1 in Gastric Cancer.
New
Jia et al., Tianjin, China. In J Am Coll Surg, Aug 2015
BACKGROUND: The aim of this study was to investigate the messenger RNA and protein expressions of SET and MYND domain-containing protein 3 (SMYD3) and transforming growth factor-β1 (TGF-β1) in gastric cancer (GC) and to explore the correlations between these proteins and the biologic behavior of GC.
Histone methyltransferase Smyd3 regulates early embryonic lineage commitment in mice.
New
Minami et al., Kyoto, Japan. In Reproduction, Jul 2015
SET and MYND domain-containing protein 3 (Smyd3) is a histone H3 lysine 4 (H3K4) di- and tri-methyltransferase that forms a transcriptional complex with RNA polymerase II and activates the transcription of oncogenes and cell cycle genes in human cancer cells.
Proper Activity of Histone H3 Lysine 4 (H3K4) Methyltransferase Is Required for Morphogenesis during Zebrafish Cardiogenesis.
New
Huh et al., Taegu, South Korea. In Mol Cells, Jun 2015
Here, we elucidate the functions of two histone H3 lysine 4 (H3K4) methylation enzymes, SMYD3 and SETD7, during zebrafish heart morphogenesis using gene expression profiling by whole mount in situ hybridization and antisense morpholino oligonucleotide (MO)-based gene knockdown.
SMYD3 contributes to a more aggressive phenotype of prostate cancer and targets Cyclin D2 through H4K20me3.
New
Jerónimo et al., Porto, Portugal. In Oncotarget, Jun 2015
SMYD3 transcript levels have prognostic value and discriminate among PCa with different clinical aggressiveness, so we decided to investigate its putative oncogenic role on PCa.We silenced SMYD3 and assess its impact through in vitro (cell viability, cell cycle, apoptosis, migration, invasion assays) and in vivo (tumor formation, angiogenesis).
C-terminal domain of SMYD3 serves as a unique HSP90-regulated motif in oncogenesis.
New
Tucker et al., Fort Collins, United States. In Oncotarget, Mar 2015
The SMYD3 histone methyl transferase (HMTase) and the nuclear chaperone, HSP90, have been independently implicated as proto-oncogenes in several human malignancies.
Lysine methylation in cancer: SMYD3-MAP3K2 teaches us new lessons in the Ras-ERK pathway.
Review
Crespo et al., Santander, Spain. In Bioessays, 2014
In this realm, a new discovery has unveiled the methyltransferase SMYD3 as an enhancer of Ras-driven cancer.
SMYD3 links lysine methylation of MAP3K2 to Ras-driven cancer.
Impact
Gozani et al., Stanford, United States. In Nature, 2014
The largely cytoplasmic KMT SMYD3 (SET and MYND domain containing protein 3) is overexpressed in numerous human tumours.
Smyd3 regulates cancer cell phenotypes and catalyzes histone H4 lysine 5 methylation.
GeneRIF
Kruger et al., United States. In Epigenetics, 2012
Depletion of Smyd3 leads to diminished cell proliferation in HeLa cell line.
SMYD3 promotes cancer invasion by epigenetic upregulation of the metalloproteinase MMP-9.
GeneRIF
Weitzman et al., Paris, France. In Cancer Res, 2012
Results show SMYD3 as an important new regulator of MMP-9 transcription, and provide a molecular link between SMYD3 overexpression and metastatic cancer progression.
Structural and biochemical studies of human lysine methyltransferase Smyd3 reveal the important functional roles of its post-SET and TPR domains and the regulation of its activity by DNA binding.
GeneRIF
Ding et al., Shanghai, China. In Nucleic Acids Res, 2011
Structural analysis shows that the previously uncharacterized C-terminal domain of Smyd3 contains a tetratrico-peptide repeat domain which together with the SET and post-SET domains forms a deep, narrow substrate binding pocket.
Hepatitis C virus core upregulates the methylation status of the RASSF1A promoter through regulation of SMYD3 in hilar cholangiocarcinoma cells.
GeneRIF
Lin et al., Guangzhou, China. In Acta Biochim Biophys Sin (shanghai), 2011
HCVc could upregulate the methylation status of the RASSF1A promoter through regulation of SMYD3, and histone methylation may affect the DNA methylation of downstream gene by an unknown mechanism
Structural and functional profiling of the human histone methyltransferase SMYD3.
GeneRIF
Tucker et al., New York City, United States. In Plos One, 2010
The structure revealed an overall compact architecture in which the "split-SET" domain adopts a canonical SET domain fold and closely assembles with a Zn-binding MYND domain and a C-terminal superhelical 9 alpha-helical bundle.
A variable number of tandem repeats polymorphism in an E2F-1 binding element in the 5' flanking region of SMYD3 is a risk factor for human cancers.
Impact
GeneRIF
Nakamura et al., Tokyo, Japan. In Nat Genet, 2005
The common variable number of tandem repeats polymorphism in SMYD3 is a susceptibility factor for some types of human cancer.
Hsp90 and environmental impacts on epigenetic states: a model for the trans-generational effects of diethylstibesterol on uterine development and cancer.
Review
Lu et al., Birmingham, United States. In Hum Mol Genet, 2005
For example, Hsp90 has recently been shown to increase the activity of the histone H3 lysine-4 methyltransferase SMYD3, which activates the chromatin of target genes.
SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells.
Impact
GeneRIF
Nakamura et al., Tokyo, Japan. In Nat Cell Biol, 2004
SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells.
share on facebooktweetadd +1mail to friends