SMYD2 Antibody

1. We show that tool compounds as well as CRISPR/Cas9 fail to reproduce many of the cell proliferation findings associated with SMYD2 and SMYD3 inhibition previously obtained with RNAi based approaches and with early stage chemical probes. PMID: 29856759
2. Lysine methylation represses p53 activity in teratocarcinoma cancer cells via up-regulation of SMYD2 and PR-Set7 and perpetuation of cancer cells proliferation. PMID: 27535933
3. SMYD2-H4K20me1-L3MBTL1 axis contributes to HIV-1 latency and can be targeted with small-molecule SMYD2 inhibitors. PMID: 28494238
4. identifie novel cellular substrates of the lysine methyltransferase SMYD2. Of the 14 novel putative SMYD2 substrates identified, six were confirmed in cells by immunoprecipitation: MAPT, CCAR2, EEF2, NCOA3, STUB1, and UTP14A. Treatment with the selective SMYD2 inhibitor BAY-598 abrogated the methylation signal, indicating that methylation of these novel substrates was dependent on the catalytic activity of SMYD2 PMID: 27163177
5. The SMYD2 may promote BMP signaling by directly methylating BMPR2, which, in turn, stimulates BMPR2 kinase activity and activation of the BMP pathway. PMID: 28588028
6. Knockdown of SMYD2 as well as treatment with a SMYD2 inhibitor in two NSCLC cell lines with an EML4-ALK gene significantly attenuated the phosphorylation levels of the EML4-ALK protein. PMID: 28370702
7. SMYD2 knockdown confers relative resistance to human AML cells against multiple classes of DNA damaging agents. PMID: 28187429
8. Substrate crevices of Smyd2 and Smyd3 show distinct features in terms of spatial, hydration, and electrostatic properties that emphasize their characteristic modes of substrates interaction and entry pathways for inhibitor binding. PMID: 27959541
9. High expression of SMYD2 is associated with chronic lymphocytic leukemia. PMID: 26790435
10. Study reveals a collection of 10 enriched sequence motifs in Kme1 sites that were identified upon SMYD2 overexpression which were also downregulated in response to SMYD2 knockdown. These findings suggest that these motifs reflect the substrate specificity of SMYD2 in esophageal squamous cell carcinoma cell line. PMID: 26750096
11. Results show that high expression levels of SMYD2, SETD3, and NO66 in renal cell tumors. Their low expression levels were significantly associated with shorter disease-specific and disease-free survival. PMID: 26488939
12. Suggest that SMYD2 plays a role in tumor progression and might be a useful prognosticator in HPV-unrelated, nonmultiple head and neck squamous cell carcinomas. PMID: 26826421
13. SMYD2-mediated methylation negatively regulates PTEN tumor suppressor activity and results in activation of the phosphatidylinositol 3-kinase-AKT pathway. PMID: 25925379
14. Comprehensive motif-based searches and mutational analysis further established four additional substrates of SMYD2. PMID: 25533488
15. in addition to esophageal squamous cell carcinoma, SMYD2 is also amplified and/or overexpressed in breast and liver primary tumors PMID: 25825497
16. a novel mechanism of PARP1 in human cancer through its methylation by SMYD2 PMID: 24726141
17. SMYD2 has a crucial role in tumor cell proliferation by its overexpression and highlight its usefulness as a prognostic factor and potential therapeutic target in gastric cancer. PMID: 25321194
18. Data indicate that irect estrogen receptor alpha (ERalpha) methylation by histone methyltransferase SMYD2 regulates estrogen signaling. PMID: 24594358
19. A novel mechanism for human carcinogenesis via methylation of HSP90AB1 by SMYD2. PMID: 24880080
20. SMYD2 expression is altered in acute lymphoblastic leukemia bone marrow samples and its high expression was correlated with a bad prognosis. Moreover, SMYD2 expression level significantly decreases in patients that respond to chemotherapy treatment. PMID: 24631370
21. Findings suggest that SMYD2 (SET and MYND domain containing protein 2), a histone lysine methyltransferase, in embryonic stem (ES) cell differentiation. PMID: 23873367
22. Data suggest that SMYD2-mediated estrogen receptor alpha (ERalpha) protein methylation and p300/cAMP response element-binding protein-binding protein-dependent ERalpha acetylation play an important role in the estrogen-induced gene expression profiles. PMID: 24101509
23. -dependent RB1 methylation at lysine 810 promotes cell cycle progression of cancer cells. Further study may explore SMYD2-dependent RB1 methylation as a potential therapeutic target in human cancer. PMID: 22787429
24. Data report the crystal structure of the full-length human Smyd2 in complex with S-adenosyl-L-homocysteine (AdoHcy). PMID: 21724641
25. Data highlights the ability of SMYD proteins to form unique protein complexes that may underlie their various biological functions and the SMYD2-mediated methylation of the key molecular chaperone HSP90. PMID: 22028380
26. SMYD2 has a role in specifically recognizing and regulating functions of p53 tumor suppressor through Lys-370 monomethylation PMID: 21880715
27. Structural basis of substrate methylation and inhibition of SMYD2 PMID: 21782458
28. Substrate specificity and product analysis studies established SMYD2 as a monomethyltransferase that prefers nonmethylated p53 peptide substrate. PMID: 21678921
29. SMYD2 gene expression is decreased in both classic and follicular variants of papillary thyroid carcinoma. PMID: 21509594
30. RB monomethylation at lysine 860 by SMYD2 provides a direct binding site for L3MBTL1. PMID: 20870719
31. The combination of the SMYD2 interactome with the gene expression data suggests that some of the genes regulated by SMYD2 are closely associated with SMYD2-interacting proteins. PMID: 18065756
32. SMYD2 plays an important role in tumor cell proliferation through its activation/overexpression and highlight its usefulness as a prognosticator and potential therapeutic target in ESCC. PMID: 19423649

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HGNC: 20982

OMIM: 610663

KEGG: hsa:56950

STRING: 9606.ENSP00000355924

UniGene: Hs.66170