Proteomics

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The interactome of a family of potential methyltransferases

ABSTRACT: Human methytransferase like proteins (METTL) are part of a large protein family characterized by the presence of binding domains for S-adenosyl methionine, a co-substrate in most methylation reactions. Despite the fact that members of this protein family were shown or predicted to be DNA, RNA or protein methyltransferases, most METTL proteins are still poorly characterized. Identification of the complexes in which these potential enzymes act could help to understand their function(s) and substrate specificities. Here we systematically studied interacting partners of METTL protein family members using label-free quantitative mass spectrometry.

INSTRUMENT(S): Orbitrap Fusion ETD

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Epithelial Cell Of Cervix

SUBMITTER: Pascal Jansen  

LAB HEAD: Robert Schneider

PROVIDER: PXD011125 | Pride | 2019-05-06

REPOSITORIES: Pride

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Dataset's files

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Action DRS
20160805_Fusion1_SA_PJ_RSext_HelaFRT_methylases_wce_M8_GFP1.raw Raw
20160805_Fusion1_SA_PJ_RSext_HelaFRT_methylases_wce_M8_GFP2.raw Raw
20160805_Fusion1_SA_PJ_RSext_HelaFRT_methylases_wce_M8_GFP3.raw Raw
20160805_Fusion1_SA_PJ_RSext_HelaFRT_wt_wce_GFP1.raw Raw
20160805_Fusion1_SA_PJ_RSext_HelaFRT_wt_wce_GFP2.raw Raw
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Publications

The interactome of a family of potential methyltransferases in HeLa cells.

Ignatova Valentina V VV   Jansen Pascal W T C PWTC   Baltissen Marijke P MP   Vermeulen Michiel M   Schneider Robert R  

Scientific reports 20190429 1

Human methytransferase like proteins (METTL) are part of a large protein family characterized by the presence of binding domains for S-adenosyl methionine, a co-substrate for methylation reactions. Despite the fact that members of this protein family were shown or predicted to be DNA, RNA or protein methyltransferases, most METTL proteins are still poorly characterized. Identification of complexes in which these potential enzymes act could help to understand their function(s) and substrate speci  ...[more]

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