Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Exploring the interactome of human METTL9

ABSTRACT: Exploring the interactome of the human putative methyltransferase enzyme METTL9.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Magnus Jakobsson

LAB HEAD: Jesper Olsen

PROVIDER: PXD016408 | Pride | 2020-11-19

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	20171128_QE5_nLC3_MJ_GFPonly_Rep1_5ul.raw	Raw
	20171128_QE5_nLC3_MJ_GFPonly_Rep2_5ul.raw	Raw
	20171128_QE5_nLC3_MJ_GFPonly_Rep3_5ul.raw	Raw
	20171128_QE5_nLC3_MJ_MT9GFPclone5_Rep1_5ul.raw	Raw
	20171128_QE5_nLC3_MJ_MT9GFPclone5_Rep2_5ul.raw	Raw

Items per page:

1 - 5 of 7

Similar Datasets

METTL9 methylates H2B a-N-proline and suppresses human retrotransposition

Project description:The methylation of residues within histones plays a central role in regulating genome function; however, little is known about the biological importance of a-N-terminal histone methylation. Here we explored the function of the previously uncharacterized a-N methylation of mammalian histone 2B proline 1 (H2BP1me). Genome-wide analyses revealed an enrichment of H2BP1 methylation at certain transposable elements (TEs) and repetitive genomic sequences. We identified a novel histone methyltransferase, METTL9, which specifically methylates H2BP1. Depletion of METTL9 led to reduced H2BP1me2 levels, an accumulation of gH2A.X, expression activation of some TEs, and increased retrotransposition of a human LINE-1 containing a reporter gene; the latter being a unique feature amongst histone modifiers described to date. These data suggest that reduced H2BP1 methylation may lead to increased TE activity and genome instability. Indeed, decreased levels of H2BP1 methylation in colon tumors correlated with an increase in LINE-1 protein expression. Furthermore, METTL9 depletion in cultured cells led to an enhancement of cellular proliferation, invasion, and migration, suggesting that a loss of H2BP1 methylation could play a role in cancer progression. Thus, we have identified a new role for H2BP1 N-terminal histone methylation in regulating chromatin function and perhaps disease progression, thereby highlighting the role of METTL9 as a novel guardian of genomic stability.

2018-12-02 | GSE60176 | GEO

METTL9 sustains vertebrate neural development primarily via non-catalytic functions

Project description:METTL9 is an enzyme catalysing histidine N1-methylation (1-MH). Given the high levels of this methyltransferase during vertebrate nervous system development, we dissected the roles of Mettl9 during this relevant physiological process. We generated three mouse embryonic stem cell lines featuring a complete Mettl9 knock-out, an inducible degron system, and the endogenous expression of a catalytically inactive protein. Additionally, we employed Xenopus laevis to down-regulate Mettl9 during neural development in vivo. Our multi-omic data indicate that METTL9 exerts a conserved role in sustaining vertebrate neurogenesis. Surprisingly, both perturbation of METTL9 catalytic activity and depletion of METTL9 protein levels without affecting global 1-MH levels show milder neural commitment defects, suggesting a role for both METTL9 catalytic and non-enzymatic activities. These converge towards the secretory pathway, where METTL9 co-localises with the Golgi apparatus and interacts with key regulators of cellular transport, endocytosis and Golgi integrity.

2025-07-29 | PXD053437 | Pride

Characterization of HAP-1 METTL9 KO cells

Project description:LAbel free quantitation of HAP1 WT and METTL9 KO cells. METTL9 is a recently established human histidine specific methyltransferase.

2021-04-28 | PXD023075 | Pride

Proteomics exploration of the human RPL3 interactome

Project description:Exploring the interactome of human RPL3 by MS-based proteomics.

2021-09-08 | PXD016055 | Pride

Characterization of METTL9-mediated methylation of DNAJB12

Project description:The analysis is part of a study aimed at characterizing a new human histidine-specific methyltransferase denoted METTL9. The putative METTL9 substrate DNAJB12 was immunoprecipitated from HEK293 cells and its PTM status was assessed by LC-MSMS.

2020-11-19 | PXD020010 | Pride

The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes

Project description:Post-translational methylation plays a crucial role in regulating and optimizing protein function. Protein histidine methylation, occurring as the two isomers 1- and 3- methylhistidine (1MH and 3MH), was first reported five decades ago, but remains largely unexplored. Here we report that METTL9 is a broad-specificity methyltransferase (MTase) that mediates the formation of the majority of 1MH present in mouse and human proteomes. The minimal requirement for METTL9-catalyzed methylation is a His-x-His (HxH) motif, where "x" is preferably a small amino acid, allowing METTL9 to methylate a number of HxH-containing proteins. Here, we show that the immunomodulatory protein S100A9 and the NDUFB3 subunit of mitochondrial respiratory Complex I are methylated at HxH motif using MALDI-TOF MS.

2020-11-23 | PXD022067 | Pride

ProSeAM SILAC MS screening for METTL9 substrates

Project description:Click chemistry based substrates screening for METTL9 in Mettl9 KO MEF cells.

2020-11-19 | PXD016823 | JPOST Repository

RNAi profiling of human cells with MYC or PIM1 silencing

Project description:It has been estimated that about 11% of cellular genes present a functional E box to which MYC can associate on the genome. MYC silencing demonstrated that MYC recruits PIM1 at specific MYC binding sites and confocal microscopy following growth factor treatment, showed an elevated degree of nuclear co-localization of PIM1 with nascent transcripts and with MYC suggesting that PIM1 is recruited by MYC to a large number of sites. To understand the actual extension of PIM1 and MYC co-operation in gene transcription we performed expression profile analysis of 293 cells silenced either for MYC or PIM1 at 120 minutes after serum treatment. MYC silencing affected the expression of 1026 genes of which 818 were up-regulated and 208 were down-regulated. Comparison of genes regulated by MYC with those regulated by PIM1, by RNAi silencing, showed that PIM1 contributes to the regulation of 207 genes out of the 1026 MYC-regulated genes. Thus, a subset of 20% of MYC-regulated genes, are also regulated by PIM1. The co-regulated includes genes involved in cell metabolism, protein synthesis, cycle progression, and oncogenesis. Interestingly, a large number of genes are transcriptional factors, which suggests that PIM1 participates in MYC-dependent regulatory networks. Experiment Overall Design: The gene expression analysis was performed by hybridizing RNA samples to the Whole Human Genome Oligo Microarray from Agilent Technologies. Samples were obtained from 293 cells, treated with serum for 120 minutes, expressing either two independent MYC shRNA (shMYC#1 and shMYC#2) or their relative scrambled shRNA (shsM#1 and shsM#2) for MYC expression analysis; two independent PIM1 shRNA (shPIM1#1 and shPIM1#2) or their relative scrambled shRNA (shsP#1 and shsP#2) for PIM1 expression analysis.

2008-06-15 | E-GEOD-7960 | biostudies-arrayexpress

Comprehensive proteomics analysis of polyhydroxyalkanoate (PHA) biology in Pseudomonas putida KT2440: the outer membrane lipoprotein OprL is a newly identified phasin Dataset 3

Project description:Pseudomonas putida KT2440 is an important bioplastic-producing industrial microorganism capable of synthesizing the polymeric carbon-rich storage material, polyhydroxyalkanoate (PHA). PHA is sequestered in discrete PHA granules, or carbonosomes, and accumulates under conditions of stress, for example low levels of available nitrogen. The pha locus responsible for PHA metabolism encodes both anabolic and catabolic enzymes, a transcription factor, and carbonosome-localized proteins termed phasins. The functions of phasins are incompletely understood but genetic disruption of their function causes PHA-related phenotypes. To improve our understanding of these proteins, we investigated the PHA pathways of P.putida KT2440 using three types of experiment. First, we profiled cells grown in nitrogen-limited and nitrogen-excess media using global expression proteomics, identifying sets of proteins found to co-ordinately increase or decrease within clustered pathway. Next, we analysed the protein composition of isolated carbonosomes, identifying two new putative components. We carried out physical interaction screens focused on PHA-related proteins, generating a protein-protein network comprising 434 connected proteins. Finally, we confirmed that the outer membrane protein OprL (the Pal component of the Pal-Tol system) localizes to the carbonosome and shows a PHA-related phenotype, and therefore is a novel phasin. The combined datasets represent a valuable overview of the protein components of the PHA system in P.putida highlighting the complex nature of regulatory interactions responsive to nutrient stress.

2024-06-16 | PXD045993 | Pride

LIN28 binds messenger RNAs at GGAGA motifs and regulates splicing factor abundance

Project description:This SuperSeries is composed of the following subset Series: GSE39855: LIN28 binds messenger RNAs at GGAGA motifs and regulates splicing factor abundance (splicing array) GSE39872: LIN28 binds messenger RNAs at GGAGA motifs and regulates splicing factor abundance (HTS) Refer to individual Series

2012-09-10 | E-GEOD-39873 | biostudies-arrayexpress

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data