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ProteomicsSETMAR methyl-lysine (3xMBT) pull-down
SILAC labeled HT-1080 cell lysate (K0R0 and K8R10) were treated with active or catalytic inactive SETMAR methyltransferase enzyme. Samples were combined and proteins modified by methyl-lysine enriched by 3xMBT. Quantitative comparison identified candidate proteins with increase methylation following...
ORGANISM(S): Homo sapiens (Human) 
2016-06-24 | PXD001635 | Pride
Methylation Setmar 
GenomicsSETMAR regulates gene expression and alternative splicing
SETMAR regulates gene expression and alternative splicing
PRJNA754125 | ENA
GenomicsS-SETMAR in the biogenesis of glioblastoma : a protective role ?
S-SETMAR in the biogenesis of glioblastoma : a protective role ?
PRJNA1076261 | ENA
TranscriptomicsS-SETMAR in the biogenesis of glioblastoma : a protective role ?
Born 45 million years ago, SETMAR is a fusion gene only present in higher primates. It is made of three exons, the two first given by the SET gene and coding for methyltransferase functions, the third given by the Hsmar1 transposase gene and coding for recombinase functions. The full length SETMAR p...
ORGANISM(S): Homo sapiens 
2025-10-10 | GSE255745 | GEO
GenomicsGenome-wide mapping of SETMAR transposase binding sites in the human genome
Genome-wide mapping of SETMAR transposase binding sites in the human genome
PRJNA733352 | ENA
GenomicsSETMAR functions in illegitimate DNA recombination and non-homologous end joining repair
SETMAR functions in illegitimate DNA recombination and non-homologous end joining repair
PRJNA533076 | ENA
UnknownSETMAR isoforms in glioblastoma: A matter of protein stability.
Not available
S-EPMC5354774 | biostudies-literature
GenomicsSETMAR binding sites
Diversity of genomic targets of SETMAR isoforms in two colorectal cell lines
PRJEB19196 | ENA
UnknownSETMAR Shorter Isoform: A New Prognostic Factor in Glioblastoma.
Not available
S-EPMC8761672 | biostudies-literature
GenomicsGenome-wide mapping of SETMAR transposase binding sites in the human genome
SETMAR/Metnase is a naturally occurring fusion protein that consists of a histone-lysine methyltransferase domain and an HsMar1 transposase. To elucidate the biological role of SETMAR, it is crucial to identify genomic targets to which SETMAR specifically binds and link these sites to the regulation...
ORGANISM(S): Homo sapiens 
2021-07-14 | GSE175725 | GEO
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