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TranscriptomicsNOTCH1 activation in breast cancer confers sensitivity to inhibition of SUMOylation
Breast cancer is genetically heterogeneous, and recent studies have underlined a prominent contribution of epigenetics to the development of this disease. To uncover new synthetic lethalities with known breast cancer oncogenes, we screened an epigenome-focused short hairpin RNA library on a panel...
ORGANISM(S): Homo sapiens 
2014-11-21 | E-GEOD-61727 | biostudies-arrayexpress
TranscriptomicsDisrupting SUMOylation potentiates transactivation function and ameliorates polyglutamine AR-mediated disease
Our findings demonstrate beneficial effects of enhancing transactivation function of the ligand-activated polyQ AR and indicate that the SUMOylation pathway may provide new targets for therapeutic intervention. We mutated conserved lysines in the polyQ AR that are targeted by SUMO, a modification th...
ORGANISM(S): Mus musculus 
2015-12-21 | E-GEOD-60691 | biostudies-arrayexpress
ProteomicsA short SUMOylation tag modulates transcription factor activity
This research demonstrates that a short peptide, composed of residues 24-55 of ZNF451, is sufficient to induce SUMOylation of target proteins, both in vitro and in human cells. Increased SUMOylation of the transcription factor p53 via fusion with the ZNF451 peptide inhibits its transcriptional activ...
ORGANISM(S): Homo sapiens (Human) 
2025-12-01 | PXD068083 | Pride
Sumo e3 ligase Small ubiquitin-like modifier (sumo) Transcription factor Sumoylation tag Znf451 Sumoylation P53 
Proteomicsinterferon-induced global cellular SUMOylation Changes
This proteomics dataset was generated to study the changes in SUMO site abundances between control cells and Interferon-alpha treated cells using SILAC. Cells were first fractionated into the cytoplasmic and nuclear fractions. SUMOylated proteins were then purified from these extracts by Ni-NTA via ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
MSV000081525 | MassIVE
UnknownA short SUMOylation tag modulates transcription factor activity.
Not available
S-EPMC12630355 | biostudies-literature
ProteomicsBioID of SUMOylation-deficient glucocorticoid receptor GR3KR
Purpose of these experiments was to assess the effect of glucocorticoid receptor SUMOylation on its protein-protein interactions using BioID. Experiments were performed with SUMOylation deficient GR3KR (K277,293,703R) fused to the BirA* biotin ligase tag.
ORGANISM(S): Homo sapiens (Human) 
2021-01-11 | PXD017713 | Pride
Human Glucocorticoid receptor Bira Gr Bioid Hek293 Sumo 
ProteomicsA ZNF-nanobody fusion reveals SUMOylation-dependent changes in protein localization
SUMOylation is a post-translational modification regulating protein localization, stability, and activity, with effects varying depending on the identity of the conjugated SUMO protein (SUMO1 or SUMO2/3) and type of SUMOylation (mono-, multi-, or poly-). We previously developed a small 32 amino acid...
ORGANISM(S): Homo sapiens (Human) 
2026-03-24 | PXD069854 | Pride
UnknownIn vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification.
Not available
S-EPMC2885211 | biostudies-literature
ProteomicsQuantitative proteomic analysis of SUMOylation in renal cortical collecting duct cells after aldosterone stimulation
SILAC was employed to investigate the effect of aldosterone stimulation on SUMOylation of cortical collecting duct (mpkCCD) cells.
ORGANISM(S): Mus musculus (Mouse) 
2019-10-07 | PXD013363 | Pride
Collecting duct Quantitative Renal Silac Kidney Sumoylation 
ProteomicsSequential Peptide Immunopurification Methodology to Monitor the Crosstalk between SUMOylation and Ubiquitylation
We describe a method that permits the identification of proteins that are modified by both SUMOylation and ubiquitylation to better understand the role of this crosstalk. The procedure requires 3 days when starting from cell pellets and can yield more than 8000 SUMO sites and 3500 ubiquitin sites fr...
ORGANISM(S): Homo sapiens (Human) 
2018-03-27 | PXD006545 | Pride
Sumo Ubiquitin Shotgun proteomics 
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