SMYD3 Antibodies

Histone-lysine N-methyltransferase SMYD3 (SMYD3)

Histone methyltransferase. Specifically methylates'Lys- 4' of histone H3, inducing di- and tri-methylation, but not monomethylation (PubMed:15235609, PubMed:22419068).

Additionally methylates'Lys-5' of histone H4 (PubMed:22419068). Plays an important role in transcriptional activation as a member of an RNA polymerase complex (PubMed:15235609).

Gene Information

Human
Gene Name:	SMYD3
Uniprot:	Q9H7B4
Entrez:	64754

Family

Belongs to:
class V-like SAM-binding methyltransferase superfamily

Alternative Names

bA74P14.1 (novel protein); bA74P14.1; EC 2.1.1; EC 2.1.1.43; FLJ21080; KMT3E; MGC104324; MYND domain containing 1; SET and MYND domain containing 3; SET and MYND domain-containing protein 3; Zinc finger MYND domain-containing protein 1; zinc finger protein, subfamily 3A (MYND domain containing), 1; ZMYND1; ZNFN3A1

Molecular Weight

Mass (kDA):
49.097 kDA

Genomic Context

Human
Location:	1q44
Sequence:	1; NC_000001.11 (245749340..246507279, complement)

Tissue Specificity

Expressed in skeletal muscles and testis. Overexpressed in a majority of colorectal and hepatocellular carcinomas.

Subcellular Localizations

Cytoplasm. Nucleus. Mainly cytoplasmic when cells are arrested at G0/G1. Accumulates in the nucleus at S phase and G2/M.

Diseases

• Malignant Neoplasms
• Neoplasms
• Carcinoma
• Liver Carcinoma
• Carcinogenesis
• Malignant Neoplasm Of Breast
• Liver Neoplasms
• Colorectal Cancer
• Mammary Neoplasms
• Cell Transformation, Neoplastic
• Neoplasm Invasiveness
• Hepatitis
• Malignant Paraganglionic Neoplasm

• Cell Invasion
• Neoplasm Metastasis
• Colorectal Neoplasms
• Variable Number Tandem Repeat
• Cholangiocarcinoma
• Hepatitis B
• Microcephaly

Interacting Proteins

• MAP3K2

Pathways

• Methylation
• Cell Proliferation
• Histone Methylation
• Cell Growth
• Cell Cycle
• Rna Interference
• Cell Migration
• Dna Methylation
• Gene Silencing
• Regulation Of Gene Expression
• Cell Cycle Arrest
• Reverse Transcription
• Translation

• Induction Of Apoptosis
• Localization
• Demethylation
• Histone H3 Acetylation
• Heart Development
• Cell Adhesion
• Histone Modification

PTMs

• Methylation
• Demethylation

• Acetylation
• Phosphorylation

• Cleavage

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/SMYD3

Best Uses Of The SMYD3 Marker

The SMYD3 Marker has recently been discovered by researchers and used in several cancer cell studies. It has been shown to have epigenetic modifier functions and can be useful in detecting cancer cells. However, more is still needed to understand this protein and its uses. In this article, we'll explore the benefits of using this biomarker in research. We'll also examine how it can be applied to other scientific applications.

SMYD3 Marker

A new genetic variant in the SMYD3 gene has been identified in a BC high-risk family. The R265H form of SMYD3 has stronger interactions with ATM than the wild-type protein. SMYD3-R265H also localizes at DNA lesions like wild-type, but does not interact with CHK2 and BIRC3 proteins, preventing recruitment of the DNA repair complex to damage sites.

The SMYD3 gene has several functions in the body, including promoting the development of various cancer types. It regulates multiple cancer-related signaling pathways and promotes tumorigenesis. It has also been linked to gastrointestinal tumors. Additionally, it plays a protective role against genotoxic stress and promotes cell proliferation. However, SMYD3 overexpression appears to promote tumorigenesis and alter cell sensitivity to genotoxic cancer therapies.

The SMYD3 gene is a versatile coregulator of multiple oncogenic pathways. It influences gene expression and protein transactivation, as well as other cellular signaling processes. Therefore, it may be useful to target the SMYD3 gene in cancer research. But before you use the SMYD3 gene in your research, it's best to learn more about the function of this gene.

In addition to promoting cancer, SMYD3 also plays a role in reprogramming the transcriptional response. It interacts with histone proteins and other molecules to control gene expression. It also binds to DNA sequences that regulate cell proliferation and migration. It is a component of the transcriptional complex formed by RNA polymerase II, which acts as a coactivator.

The combined use of SMYD3 inhibitors and PARPi has shown cytotoxic effects in cancer cell lines. This synthetic lethality approach is expected to be useful in a fraction of human tumors. Several chemical compounds that inhibit SMYD3 enzymatic activity have been identified through virtual screening. Interestingly, BCI-121, the first SMYD3 inhibitor, showed anti-growth properties in cancer cell lines. Epizyme then went on to develop three more potent SMYD3 inhibitors, SMYD3is, and nanomolar SMYD3i.

The SMYD3 protein catalyzes lysine methylation by binding to the SET domain of the SMYD3 gene. However, it requires flanking regions, called MYND, that promote its activity. This is because SMYD3 proteins require flanking regions that are positively charged in order to be able to interact with protein-protein molecules.

Polymorphisms in the SMYD3 gene are thought to be associated with susceptibility to breast cancer. The gene has been implicated in familial breast cancer, and has been linked with the susceptibility to colon cancer. However, further research is needed to determine if SMYD3 polymorphisms contribute to this risk. It is important to note that the polymorphisms in the SMYD3 gene have a profound impact on the risk of breast cancer.

Knockdown of SMYD3 inhibits ovarian cancer carcinogenesis in vivo. Cells in the HEY group and the shSMYD3 group were compared to see which group exhibits fewer tumors. Compared to the HEY-NC group, the SMYD3 knockdown mice showed fewer tumors after immunohistochemistry, with a mean IOD of 1.4. The two groups were then separated and the tumors were collected.

It was used to detect cancer cells

Earlier this year, researchers published a study revealing that a protein known as SMYD3, which is part of a family of proteins called matrix metalloproteinases (MMPs), is expressed more prominently in cancer cells. The protein was found to regulate MMP-9 expression in human cancer cells. These results show that the protein could be used to detect cancer cells in the future.

The overexpression of SMYD3 has been found in several cancers, including ovarian and colorectal cancers. It has also been implicated in cell proliferation, migration, invasion, and epithelial-mesenchymal transition. Several studies have found that overexpression of SMYD3 is associated with increased risks of breast and colorectal cancer, but not for NSCLC.

Using this gene as a biomarker for cancer cells, researchers found that SMYD3 promoted MMP-9 expression in human fibrosarcoma cells. The authors then performed an assay comparing luciferase activity of the integrated MMP-9 reporter construct to that of nontransfected control cells. The results revealed that SMYD3 promoted trimethylation of H3K4 at the promoter of MMP-9 in a reversible model of cancer. These results suggest that other MMPs might also be involved in the SMYD3-mediated migration and invasion of cancer cells. Further research needs to confirm these hypotheses.

Besides the immunohistochemistry analysis, SMYD3 expression in NSCLC cells has predictive value in cancer patients. The expression of SMYD3 in cancer cells was correlated with poor DFS and poor OS. Age and PI were independent predictors of poor DFS and poor OS in multivariate Cox regression. These findings suggest that the protein may be an oncogene in NSCLC cell proliferation.

Further studies are needed to establish if the expression of SMYD3 in NSCLC cells is related to the prognosis of the disease. The authors noted that the gene was associated with aggressive clinicopathological characteristics in NSCLC. They further concluded that SMYD3 might play a role in the development and progression of NSCLC. In addition, this marker is related to the activation of caspases, which are essential for the death of cancer cells.

Researchers recently discovered that the SMYD3 marker is a key component of ovarian cancer metastasis. Despite its role in cancer metastasis, it also regulates integrins. The enzyme SMYD3 is responsible for regulating integrins and ligands in the ovaries. These findings suggest that the SMYD3-integrin pathway is essential for ovarian cancer metastasis.

SMYD3 stimulates the TGFb1/Smad3 signaling pathway and upregulates Snail and Vimentin. These molecules also promote the EMT process. Therefore, the SMYD3 protein is an important part of the immune system. In addition to its immune-reactive role in cancer, it is also involved in the regulation of inflammatory processes and in tumor metastasis.

It was used to detect epigenetic modifier genes

Epigenetic regulation has been implicated in cancer development, and SMYD3 is a promising therapeutic target. This histone methyltransferase promotes oncogenic progression by methylating lysines to integrate cytoplasmic kinectin. Its overexpression in cancer cells can predict the risk of disease progression and outcome. However, there are some drawbacks.

SMYD3 is an epigenetic gene that is known to regulate chromatin structure. Detection of this gene can be difficult due to poor tissue accessibility in patients. However, this new method has some advantages. It can detect cancer cells even before cancer patients are symptomatic. Furthermore, it allows physicians to develop tailored therapeutic regimens for individual patients. In addition, it provides a better mechanistic understanding of the mechanisms by which epigenetic regulators influence gene expression, which will enable the development of clinical tests.

The SMYD3 gene is found in the spliceosome and has two functional domains. The SET domain is required for lysine methylation, and has flanking domains that play important roles in protein-protein interaction. In addition to this, the SMYD3 gene contains the MYND domain, a cysteine-rich zinc finger motif that mediates protein-protein interaction. The N-SET domain encloses the pre-SET domain, which acts as an inhibitory region.

SMYD3 has an important role in the progression of cancer in vivo. Mutational analysis has revealed that the SMYD3 gene plays a role in tumorigenesis. However, it is unclear whether the mutations found in the mice are related to the SMYD3 gene or not. The SMYD3 gene is involved in cancer development, which is a common reason why it is so difficult to detect epigenetic modifier genes.

SMYD3 promotes cell proliferation, metastasis, and cell cycle. Moreover, it is important for genome stability since it is an important player in HR repair. Therefore, high proliferative cells rely on HR-mediated DSB repair to restart stalled replication forks in the S phase. If you have a cancer gene, it is highly likely that the SMYD3 gene is involved in the disease.

SMYD3 is essential for the DNA repair machinery. Knocking down the SMYD3 gene impairs clonogenic survival. Knockdown of SMYD3 inhibits the removal of gH2A.X foci in the shSMYD3 MDA-MB-231 cells. The knockdown of SMYD3 causes cells to undergo mitosis later, generating more micronuclei, chromosome segregation, and ultimately apoptosis.

Knockdown of SMYD3 downregulates HR activity and the expression of HR genes. The knockdown effectiveness of cells was confirmed by qRT-PCR. In addition, exogenous expression of SMYD3 restored HR activity in shSMYD3 cells. These results also demonstrate the potential of epigenetic modifications to detect cancer. However, their potential diagnostic applications are limited.