Identification of covalent SUMO1 aceptor lysines
Ontology highlight
ABSTRACT:
INSTRUMENT(S): Q Exactive
ORGANISM(S): Homo Sapiens (human)
SUBMITTER: 
Román González-Prieto
LAB HEAD: Alfred C.O. Vertegaal
PROVIDER: PXD013844 | Pride | 2021-01-29
REPOSITORIES: Pride
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| MaxQuantoutput.txt.zip | Txt | |||
| Samplenumbering-SUMO1sites.xlsx | Xlsx | |||
| q102866a.raw | Raw | |||
| q102867a.raw | Raw | |||
| q102867b.raw | Raw |
Items per page: 5 1 - 5 of 14 |
Publications
Global non-covalent SUMO interaction networks reveal SUMO-dependent stabilization of the non-homologous end joining complex.
González-Prieto Román R Eifler-Olivi Karolin K Claessens Laura A LA Willemstein Edwin E Xiao Zhenyu Z Talavera Ormeno Cami M P CMP Ovaa Huib H Ulrich Helle D HD Vertegaal Alfred C O ACO
Cell reports 20210101 4
In contrast to our extensive knowledge on covalent small ubiquitin-like modifier (SUMO) target proteins, we are limited in our understanding of non-covalent SUMO-binding proteins. We identify interactors of different SUMO isoforms-monomeric SUMO1, monomeric SUMO2, or linear trimeric SUMO2 chains-using a mass spectrometry-based proteomics approach. We identify 379 proteins that bind to different SUMO isoforms, mainly in a preferential manner. Interestingly, XRCC4 is the only DNA repair protein in ...[more]
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