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ProteomicsSystem-Wide Identification of Wild-Type SUMO-2 Conjugation Sites
SUMOylation is a reversible post-translational modification regulating all nuclear processes. Identification of SUMOylation sites by mass spectrometry has been hampered by bulky tryptic fragments, which thus far necessitated the use of mutated SUMO. Here, we present a dataset generated through a SUM...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-28 | MSV000080714 | MassIVE
Genomicsheat shock SUMO-2 ChIP-seq
Analysis of changes in SUMO-2 binding to chromatin in response to heat shock in human U2OS cells
ORGANISM(S): Homo sapiens 
2015-07-13 | E-MTAB-2368 | biostudies-arrayexpress
ProteomicsSite-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation (part 1)
Small ubiquitin-like modifiers (SUMOs) are post-translational modifications (PTMs) that regulate nuclear cellular processes. Here we used an augmented K0â??SUMO proteomics strategy to identify 40,765 SUMO acceptor sites and quantify their fractional contribution for 6,747 human proteins. Structuralâ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-30 | MSV000080812 | MassIVE
ProteomicsSite-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation (part 2)
Small ubiquitin-like modifiers (SUMOs) are post-translational modifications (PTMs) that regulate nuclear cellular processes. Here we used an augmented K0â??SUMO proteomics strategy to identify 40,765 SUMO acceptor sites and quantify their fractional contribution for 6,747 human proteins. Structuralâ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-04-01 | MSV000080869 | MassIVE
ProteomicsProteome-wide identification of SUMO2 modification sites
Posttranslational modification with small ubiquitin-like modifiers (SUMOs) alters the function of proteins involved in diverse cellular processes. SUMOs are conjugated to lysine residues in target proteins by SUMO-specific enzymes. Although proteomic studies have identified hundreds of sumoylated su...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080741 | MassIVE
ProteomicsSystem-Wide Identification of Wild-Type SUMO-2 Conjugation Sites
SUMOylation is a reversible post-translational modification regulating all nuclear processes. Identification of SUMOylation sites by mass spectrometry has been hampered by bulky tryptic fragments, which thus far necessitated the use of mutated SUMO. Here, we present a dataset generated through a SUM...
ORGANISM(S): Homo sapiens (Human) 
2015-06-15 | PXD001798 | Pride
Endogenous Wild-type Sumo-2 Site Sumo System-wide 
ProteomicsIdentification of SUMO sites by LC-MSMS
We developed a novel method for the identification of SUMO sites by expression of His-tagged SUMO mutants and affinity purification of SUMOylated proteins, followed by trypsin digestion and immunocapture of peptides containing diglycine signature tags. Lab Head: Dr Pascale Cossart, pascale.co...
ORGANISM(S): Homo sapiens (Human) 
2014-07-29 | PXD000459 | Pride
Lc-msms Hela cells Sumo Silac Immunocapture 
ProteomicsUncovering Global SUMOylation Signaling Networks in a Site-Specific Manner
SUMOylation is a reversible post-translational modification essential for genome stability. Using high-resolution mass spectrometry, we have studied global SUMOylation in mammalian cells and in a site-specific manner, identifying a total of over 4,300 SUMOylation sites in over 1,600 proteins. Moreov...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080793 | MassIVE
ProteomicsSite-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation (part 2)
Small ubiquitin-like modifiers (SUMOs) are post-translational modifications (PTMs) that regulate nuclear cellular processes. Here we used an augmented K0–SUMO proteomics strategy to identify 40,765 SUMO acceptor sites and quantify their fractional contribution for 6,747 human proteins. Structural–pr...
ORGANISM(S): Homo sapiens (Human) 
2017-01-24 | PXD005296 | Pride
Sumo Phosphorylation Deep Proteome K0-sumo 
ProteomicsSite-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation (part 1)
Small ubiquitin-like modifiers (SUMOs) are post-translational modifications (PTMs) that regulate nuclear cellular processes. Here we used an augmented K0–SUMO proteomics strategy to identify 40,765 SUMO acceptor sites and quantify their fractional contribution for 6,747 human proteins. Structural–pr...
ORGANISM(S): Homo sapiens (Human) 
2017-01-24 | PXD004927 | Pride
Sumo Phosphorylation Deep Proteome K0-sumo 
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