Recombinant Human Histone-lysine N-methyltransferase SETMAR (SETMAR)

1. Various SETMAR proteins can be synthesized in human glioblastoma that may each have specific biophysical and/or biochemical properties and characteristics. PMID:28038463
2. These results suggest that Metnase enhances Exo1-mediated exonuclease activity on the lagging strand DNA by facilitating Exo1 loading onto a single strand gap at the stalled replication fork. PMID:27974460
3. The SET domain is needed for the 5' end of ss-overhang cleavage with fork and non-fork DNA without affecting the Metnase-DNA interaction. This domain has a positive role in restart of replication fork and the 5' end of ss-overhang cleavage. PMID:26437079
4. methylation of snRNP70 by SETMAR regulates constitutive and/or alternative splicing PMID:25795785
5. Metnase may possess an important role in DNA repair, topoisomerase II function, and the maintenance of stemness during colon cancer development. PMID:25333365
6. 293 T transfected with Metnase revealed a large number of rescued plasmids. PMID:24655462
7. found known and novel SETMAR splice variants to be significantly increased in acute myeloid leukemia PMID:24607956
8. a single mutation DDN(610) --> DDD(610), which restores the ancestral catalytic site, results in loss of function in Metnase PMID:24573677
9. phosphorylation of Metnase S495 differentiates between these two functions, enhancing DSB repair and repressing replication fork restart. PMID:22231448
10. a role for Metnase's endonuclease activity in promoting the joining of noncompatible ends PMID:21491884
11. Data show that DBN1, SETMAR and HIG2 are direct transcriptional targets of the SOX11 protein. PMID:21124928
12. DNA repair protein Metnase (also SETMAR), which has a SET histone methylase domain, localized to an induced DSB and directly mediated the formation of H3K36me2 near the induced DSB PMID:21187428
13. results establish Metnase as a key factor that promotes restart of stalled replication forks, and implicate Metnase in the repair of collapsed forks. PMID:20457750
14. hPso4, once it forms a complex with Metnase, negatively regulates Metnase's TIR binding activity PMID:20416268
15. Metnase is a nonhomologous end-joining repair protein that regulates genomic integration of exogenous DNA and establishes a relationship among histone modification, DNA repair, and integration. PMID:16332963
16. These data suggest that vectors based on the Himar1 transposable element, in conjunction with the hyperactive mutant transposase C9, may be suitable vectors for gene therapy applications. PMID:16989604
17. SETMAR is unlikely to catalyze transposition in the human genome, although the nicking activity may have a role in the DNA repair phenotype. PMID:17130240
18. The activities of the SETMAR protein on transposon ends are described. PMID:17403897
19. Results suggest that Metnase's DNA cleavage activity, unlike those of other eukaryotic transposases, is not coupled to its sequence-specific DNA binding. PMID:17877369
20. hPso4 is necessary to bring Metnase to the DSB sites for its function(s) in DNA repair PMID:18263876
21. Metnase physically interacts and co-localizes with Topoisomerase IIalpha, the key chromosome decatenating enzyme. PMID:18790802
22. myeloid leukemia cells fail to arrest at the mitotic decatenation checkpoint, and their progression through this checkpoint is regulated by the DNA repair component Metnase (also termed SETMAR) PMID:19458360

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HGNC: 10762

UNIGENE: Hs.475300

KEGG: hsa:6419

STRING: 9606.ENSP00000373354

OMIM: 609834