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SETMAR methyl-lysine (3xMBT) pull-down

ABSTRACT: 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 incubation with SETMAR.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell

SUBMITTER: Scott Carlson

LAB HEAD: Or Gozani

PROVIDER: PXD001635 | Pride | 2016-06-24

REPOSITORIES: Pride

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			Action	DRS
	SETMARRAW.zip	Other
	SETMARSEARCH.zip	Other

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Publications

A Proteomic Strategy Identifies Lysine Methylation of Splicing Factor snRNP70 by the SETMAR Enzyme.

Carlson Scott M SM Moore Kaitlyn E KE Sankaran Saumya M SM Reynoird Nicolas N Elias Joshua E JE Gozani Or O

The Journal of biological chemistry 20150320 19

The lysine methyltransferase (KMT) SETMAR is implicated in the response to and repair of DNA damage, but its molecular function is not clear. SETMAR has been associated with dimethylation of histone H3 lysine 36 (H3K36) at sites of DNA damage. However, SETMAR does not methylate H3K36 in vitro. This and the observation that SETMAR is not active on nucleosomes suggest that H3K36 methylation is not a physiologically relevant activity. To identify potential non-histone substrates, we utilized a stra ...[more]

PMID: 25795785

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