Proteomics

Dataset Information

0

Proteome-wide identification of SUMO2 modification sites


ABSTRACT: 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 substrates, methods to identify the modified lysines on a proteome-wide scale are lacking. We developed a method that enabled large-scale identification of sumoylated lysines and involved the expression of polyhistidine (6His)–tagged SUMO2 with Thr90 mutated to Lys. Digestion of 6His-SUMO2(T90K)–modified proteins with an endoproteinase Lys-C produces a diGly remnant on SUMO2(T90K)-conjugated lysines, enabling a specific immunoprecipitation of modified peptides with diGly-Lys-specific antibody and producing a unique mass-to-charge signature. Mass spectrometry analysis of SUMO2-enriched peptides from human cell lysates revealed more than 1000 sumoylated lysines in 539 proteins, including many functionally related proteins involved in cell cycle, transcription, and DNA repair. Not only can this strategy be used to study the dynamics of sumoylation and other potentially similar posttranslational modifications, but also, these data provide an unprecedented resource for future research on the role of sumoylation in cellular physiology and disease.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Ronald T. Hay  

PROVIDER: MSV000080741 | MassIVE | Wed Mar 29 04:14:00 BST 2017

SECONDARY ACCESSION(S): PXD001281

REPOSITORIES: MassIVE

Dataset's files

Source:
Action DRS
Other
Items per page:
1 - 1 of 1
altmetric image

Publications

Proteome-wide identification of SUMO2 modification sites.

Tammsalu Triin T   Matic Ivan I   Jaffray Ellis G EG   Ibrahim Adel F M AFM   Tatham Michael H MH   Hay Ronald T RT  

Science signaling 20140429 323


Posttranslational modification with small ubiquitin-like modifiers (SUMOs) alters the function of proteins involved in diverse cellular processes. SUMO-specific enzymes conjugate SUMOs to lysine residues in target proteins. Although proteomic studies have identified hundreds of sumoylated substrates, methods to identify the modified lysines on a proteomic scale are lacking. We developed a method that enabled proteome-wide identification of sumoylated lysines that involves the expression of polyh  ...[more]

Similar Datasets

2014-10-15 | PXD001281 | Pride
2021-12-31 | GSE163682 | GEO
2017-01-24 | PXD004927 | Pride
2017-01-24 | PXD005296 | Pride
2017-03-30 | MSV000080812 | MassIVE
2017-04-01 | MSV000080869 | MassIVE
2018-06-26 | PXD008003 | Pride
2024-04-06 | GSE255803 | GEO
2024-04-06 | GSE254892 | GEO
2023-10-05 | GSE217604 | GEO