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ProteomicsScreening for covalent SUMOylation and noncovalent SUMO interactions with SIM-binding groove SUMO mutants
Small ubiquitin-like modifier (SUMO) proteins affect protein function through both covalent modification of target proteins and noncovalent protein-protein interactions. The best characterized mode of SUMO interaction involves binding of a SUMO-interaction motif (SIM) to a conserved binding groove i...
ORGANISM(S): Homo sapiens (Human) 
2025-04-03 | PXD050651 | Pride
Sumo Protein interactions Sim 
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
UnknownA global S. cerevisiae small ubiquitin-related modifier (SUMO) system interactome.
Not available
S-EPMC4039371 | biostudies-literature
ProteomicsRhes, a striatal enriched protein regulates post-translational Small-Ubiquitin like-Modifier (SUMO) Modification of nuclear proteins and alters gene expression
Rhes (Ras homolog enriched in the striatum) is a multifunctional protein that orchestrates striatal toxicity, motor behaviors and abnormal movements associated with dopaminergic signaling, Huntington disease and Parkinson disease signaling in the striatum. Rhes engineers membranous tunneling nanotub...
ORGANISM(S): Homo sapiens (Human) 
2024-06-10 | PXD023394 | Pride
Perinuclear membrane Morphology Brain Medium spiny neurons Differentiation Gene regulation Sumo e3-ligase Signaling 
UnknownInteraction networks of SIM-binding groove mutants reveal alternate modes of SUMO binding and profound impact on SUMO conjugation.
Not available
S-EPMC12077520 | biostudies-literature
ProteomicsO-GlcNAcase SUMOylation studies identify the SUMO-code in chaperone-mediated autophagy
O-GlcNAcase (OGA) is the sole eraser for the intracellular O-linked N-acetylglucosamine (O-GlcNAc). OGA has many roles in diverse processes, such as cancer and embryonic stem cells, but its exact regulating mechanism is far from understood. Herein we studied small ubiquitin-like modifier (SUMO) modi...
ORGANISM(S): Homo Sapiens 
PXD056772 |
ProteomicsSpatial-temporal protein interactome profiling via condensation enhanced crosslinking
MS data for the verification of metabolic incorporation of δ-photolysine, calculation for the crosslinking distance by DegP crosslinking, and the proteomics analysis for the dynamic direct interactome of NPM1 as well as the SG-specific interactomes of SARS-CoV-2 Nucleocapsid protein and YTHDF1/2.
ORGANISM(S): Homo Sapiens Escherichia Coli Severe Acute Respiratory Syndrome Coronavirus 2 
PXD052099 |
UnknownSUMO Interacting Motifs: Structure and Function.
Not available
S-EPMC8616421 | biostudies-literature
UnknownRhes, a striatal enriched protein, regulates post-translational small-ubiquitin-like-modifier (SUMO) modification of nuclear proteins and alters gene expression.
Not available
S-EPMC11001699 | biostudies-literature
ProteomicsExpanding the substantial interactome of NEMO using protein microarrays
Signal transduction by the NF-kappaB pathway is a key regulator of a host of cellular responses to extracellular and intracellular messages. The NEMO adaptor protein lies at the top of this pathway and serves as a molecular conduit, connecting signals transmitted from upstream sensors to the downstr...
ORGANISM(S): Homo sapiens 
2010-06-19 | E-GEOD-19841 | biostudies-arrayexpress
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