Mouse Anti-SETMAR Recombinant Antibody (CBXS-0290) (CBMAB-S3265-CQ)

SET Domain And Mariner Transposase Fusion Gene

This gene encodes a fusion protein that contains an N-terminal histone-lysine N-methyltransferase domain and a C-terminal mariner transposase domain. The encoded protein binds DNA and functions in DNA repair activities including non-homologous end joining and double strand break repair. The SET domain portion of this protein specifically methylates histone H3 lysines 4 and 36. This gene exists as a fusion gene only in anthropoid primates, other organisms lack mariner transposase domain. Alternate splicing results in multiple transcript variants.

SET Domain And Mariner Transposase Fusion Gene; SET Domain And Mariner Transposase Fusion Protein; METNASE; SET Domain And Mariner Transposase Fusion Gene-Containing Protein; Histone-Lysine N-Methyltransferase SETMAR; EC 2.1.1.43; Mar1;

Protein derived from the fusion of a methylase with the transposase of an Hsmar1 transposon that plays a role in DNA double-strand break repair, stalled replication fork restart and DNA integration. DNA-binding protein, it is indirectly recruited to sites of DNA damage through protein-protein interactions. Has also kept a sequence-specific DNA-binding activity recognizing the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element and displays a DNA nicking and end joining activity (PubMed:16332963, PubMed:16672366, PubMed:17877369, PubMed:17403897, PubMed:18263876, PubMed:22231448, PubMed:24573677, PubMed:20521842).
In parallel, has a histone methyltransferase activity and methylates 'Lys-4' and 'Lys-36' of histone H3. Specifically mediates dimethylation of H3 'Lys-36' at sites of DNA double-strand break and may recruit proteins required for efficient DSB repair through non-homologous end-joining (PubMed:16332963, PubMed:21187428, PubMed:22231448).
Also regulates replication fork processing, promoting replication fork restart and regulating DNA decatenation through stimulation of the topoisomerase activity of TOP2A (PubMed:18790802, PubMed:20457750).

Biological Process cell population proliferationManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process chromatin organizationIEA:UniProtKB-KW
Biological Process DNA catabolic process, endonucleolyticManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process DNA double-strand break processingManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process DNA integrationManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process double-strand break repair via nonhomologous end joiningManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process histone H3-K36 dimethylationManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process histone H3-K36 methylationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process histone H3-K4 methylationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process mitotic DNA integrity checkpoint signalingManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process negative regulation of chromosome organizationManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process nucleic acid phosphodiester bond hydrolysisManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process positive regulation of DNA topoisomerase (ATP-hydrolyzing) activityManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process positive regulation of double-strand break repair via nonhomologous end joiningManual Assertion Based On ExperimentIDA:UniProtKB
Biological Process replication fork processingManual Assertion Based On ExperimentIMP:UniProtKB

Nucleus
Chromosome
Recruited on damaged DNA at sites of double-strand breaks.

Methylated. Methylation regulates activity in DNA decatenation.
Phosphorylated at Ser-508 by CHEK1 and dephosphorylated by protein phosphatase 2A/PP2A. Phosphorylation at Ser-508 is enhanced by DNA damage and promotes recruitment to damaged DNA. It stimulates DNA repair and impairs replication fork restart.