Proteomics

Dataset Information

1

Identification of covalent SUMO1 aceptor lysines


ABSTRACT: SUMO1 modified proteins were identified in a site specific manner.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo sapiens  

TISSUE(S): Tissue Not Applicable To Dataset

DISEASE(S): Not Available

SUBMITTER: Román González-Prieto  

LAB HEAD: Alfred C.O. Vertegaal

PROVIDER: PXD013844 | Pride | 2021-01-29

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
MaxQuant output.txt.zip Txt
Sample numbering- SUMO1 sites.xlsx Xlsx
q102866a.raw Raw
q102867a.raw Raw
q102867b.raw Raw
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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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