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TranscriptomicsThe conserved ubiquitin-like protein Hub1 plays a critical role in splicing in human cells
Different from canonical ubiquitin-like proteins, Hub1 does not form covalent conjugates with substrates but binds proteins non-covalently. In Saccharomyces cerevisiae, Hub1 associates with spliceosomes and mediates alternative splicing of SRC1, without affecting pre-mRNA splicing generally. Human H...
ORGANISM(S): Homo sapiens 
2014-05-30 | E-GEOD-56878 | biostudies-arrayexpress
ProteomicsProteome-wide analysis of SUMO2 targets in response to pathological DNA replication stress in human cells
SUMOylation is a form of post-translational modification involving covalent attachment of SUMO (Small Ubiquitin-like Modifier) polypeptides to specific lysine residues in the target protein. In human cells, there are four SUMO proteins, SUMO1–4, with SUMO2 and SUMO3 forming a closely related subfami...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-28 | MSV000080699 | MassIVE
ProteomicsProteome-wide identification of SUMO2 modification sites
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 su...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080741 | MassIVE
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 
GenomicsGenome-wide analysis of insulin-like growth factor 1 receptor (IGF1R) binding sites in DFB cells
The insulin-like growth factor 1 receptor (IGF-1R) plays crucial roles in developmental and cancer biology. Most of its biological effects have been ascribed to its tyrosine kinase activity. We report that IGF-1 promotes the modification of IGF-1R by small ubiquitin-like modifier protein-1 (SUMO-1) ...
ORGANISM(S): Homo sapiens 
2010-08-25 | E-GEOD-23792 | biostudies-arrayexpress
UnknownUbiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax volcanii.
Not available
S-EPMC2872088 | biostudies-literature
UnknownActivation of the Slx5-Slx8 ubiquitin ligase by poly-small ubiquitin-like modifier conjugates.
Not available
S-EPMC2459270 | biostudies-literature
UnknownIonic strength-dependent conformations of a ubiquitin-like small archaeal modifier protein (SAMP2) from Haloferax volcanii.
Not available
S-EPMC3701171 | biostudies-literature
TranscriptomicsMultiple Arkadia/RNF111 structures coordinate its Polycomb body association and transcriptional control
The RING domain protein Arkadia/RNF111 is a ubiquitin ligase in the transforming growth factor beta (TGFβ) pathway. We previously identified Arkadia as a small ubiquitin-like modifier (SUMO)-binding protein with clustered SUMO-interacting motifs (SIMs) that together form a SUMO-binding domain (SBD)....
ORGANISM(S): Mus musculus 
2015-02-11 | E-GEOD-65796 | biostudies-arrayexpress
UnknownPoly-small ubiquitin-like modifier (PolySUMO)-binding proteins identified through a string search.
Not available
S-EPMC3516753 | biostudies-literature
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