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ProteomicsIdentification of proximal SUMO-dependent interactors using SUMO-ID
To study the function of SUMOylation and SUMO-SIM interactions for particular substrates poses several challenges. SUMOylation occurs transiently and often in a small percentage of the total copy numbers of a given substrate. Modified proteins can be readily deSUMOylated and SUMO can be recycled and...
ORGANISM(S): Homo sapiens (Human) 
2021-09-21 | PXD021923 | Pride
Human Turbo-id Proximity labeling Sall1 Sumo-id Sumo 
ProteomicsIdentification of proximal SUMO-dependent interactors using SUMO-ID
Proximity-dependent labelling (PL) methods are based on promiscuous labeling enzymes that produce reactive molecules that covalently bind neighbor proteins. Labeled proteins can be then purified and identified using affinity-purification coupled to mass spectrometry methods39. Proximity-dependent bi...
ORGANISM(S): Homo sapiens (Human) 
2021-09-20 | PXD021770 | Pride
Pml Sumo Turboid Protein-protein interaction Bioid 
ProteomicsIdentification of proximal SUMO-dependent interactors using SUMO-ID
Proximity-dependent labelling (PL) methods are based on promiscuous labeling enzymes that produce reactive molecules that covalently bind neighbor proteins. Labeled proteins can be then purified and identified using affinity-purification coupled to mass spectrometry methods39. Proximity-dependent bi...
ORGANISM(S): Homo sapiens (Human) 
2021-09-20 | PXD021809 | Pride
Pml Proximity-dependent labelling Sumo Turboid Protein interaction 
ProteomicsIdentification of proximal SUMO-dependent interactors using SUMO-ID
Proximity-dependent labelling methods are based on promiscuous labeling enzymes that produce reactive molecules that covalently bind neighbor proteins. Labeled proteins can be then purified and identified using affinity-purification coupled to mass spectrometry methods23. Proximity-dependent biotin ...
ORGANISM(S): Homo sapiens (Human) 
2021-09-20 | PXD027759 | Pride
Proteomics Lcms 
UnknownIdentification of proximal SUMO-dependent interactors using SUMO-ID.
Not available
S-EPMC8602451 | biostudies-literature
ProteomicsA Split-SUMO-ID proteomics approach to identify the Rad52 and SUMO-dependent interactome of Schizosaccharomyces pombe
A PTM known as sumoylation, manifested by an attachment of a SUMO molecule (small ubiquition-like modifier) to target proteins, may lead to changes in the tagged protein’s function, localization or stability. This PTM is present in all eukaryotes. In fission yeast, Rad52 is a DNA repair mediator pro...
ORGANISM(S): Schizosaccharomyces pombe 
2025-10-31 | PXD055556 | Pride
UnknownUbiquitin-SUMO circuitry controls activated fanconi anemia ID complex dosage in response to DNA damage.
Not available
S-EPMC4416315 | biostudies-literature
GenomicsPolySUMOylation of PCNA and Rad52 restricts centromeric recombination in fission yeast
SUMOylation, a conserved post-translational modification in eukaryotes, regulates protein function, localization, and stability. However, the role of SUMO chains in genome maintenance is still emerging. Using Schizosaccharomyces pombe, we show that loss of SUMO chains results in spontaneous replicat...
ORGANISM(S): Schizosaccharomyces pombe 
2024-09-15 | GSE276805 | GEO
ProteomicsThe ubiquitin-like modifier FAT10 interferes with SUMO activation
In this study, the proteins SumoE1 and Fat10 or Fat10-AV mutant were crosslinked using the crosslinking reagent H12/D12 BS3 in order to determine specific interaction sites of Fat10 and SumoE1. Furthermore, quantitative chemical crosslinking coupled to mass spectrometry (q-XL-MS) was used to compare...
ORGANISM(S): Homo sapiens (Human) 
2019-10-08 | PXD012592 | Pride
Fat10 Q-xl-ms Xl-ms Sumoe1 
ProteomicsProfiling Endogenous SUMO and Ub Modifications Side-by-Side under Native Conditions
Datasets of the proteome-wide profiling of native SUMO post-translational modifications in HCT and HELA cells using a novel method to isolate modified peptides through a diglycyl lysine remnant, as previously used for proteome-wide ubiquitin profiling. Includes ID experiments for the identification ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) Mus Musculus (ncbitaxon:10090) 
2017-04-27 | MSV000081018 | MassIVE
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