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ProteomicsUncovering Global SUMOylation Signaling Networks in a Site-Specific Manner
SUMOylation is a reversible post-translational modification essential for genome stability. Using high-resolution mass spectrometry, we have studied global SUMOylation in mammalian cells and in a site-specific manner, identifying a total of over 4,300 SUMOylation sites in over 1,600 proteins. Moreov...
ORGANISM(S): Homo sapiens (Human) 
2014-09-04 | PXD001061 | Pride
Sumo-2 Qqtgg Sumo Sumo2 Q87r 
UnknownNoncovalent structure of SENP1 in complex with SUMO2.
Not available
S-EPMC6497105 | biostudies-literature
ProteomicsSUMO-2 Orchestrates Chromatin Modifiers in Response to DNA Damage
Small Ubiquitin-like Modifiers play critical roles in the DNA Damage Response (DDR). To increase our understanding of SUMOylation in the mammalian DDR, we employed a quantitative proteomics approach to identify dynamically regulated SUMO-2 conjugates and modification sites upon treatment with the DN...
ORGANISM(S): Homo sapiens (Human) 
2015-03-16 | PXD001810 | Pride
Dna Damage Mms Sumo-2 Sumo Chromatin Repair Site 
ProteomicsSystem-wide analysis of SUMOylation dynamics in response to replication stress reveals novel SUMO target proteins and acceptor lysines relevant for genome stability
Genotoxic agents can cause replication fork stalling in dividing cells due to DNA lesions, eventually leading to replication fork collapse when the damage is not repaired. Small Ubiquitin-like Modifiers (SUMOs) are known to counteract replication stress, nevertheless, only a small number of relevant...
ORGANISM(S): Homo sapiens (Human) 
2015-03-12 | PXD001736 | Pride
Affinity purification Dna damage Label free quantification 
ProteomicsSite-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation (part 1)
Small ubiquitin-like modifiers (SUMOs) are post-translational modifications (PTMs) that regulate nuclear cellular processes. Here we used an augmented K0–SUMO proteomics strategy to identify 40,765 SUMO acceptor sites and quantify their fractional contribution for 6,747 human proteins. Structural–pr...
ORGANISM(S): Homo sapiens (Human) 
2017-01-24 | PXD004927 | Pride
Sumo Phosphorylation Deep Proteome K0-sumo 
ProteomicsSite-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation (part 2)
Small ubiquitin-like modifiers (SUMOs) are post-translational modifications (PTMs) that regulate nuclear cellular processes. Here we used an augmented K0–SUMO proteomics strategy to identify 40,765 SUMO acceptor sites and quantify their fractional contribution for 6,747 human proteins. Structural–pr...
ORGANISM(S): Homo sapiens (Human) 
2017-01-24 | PXD005296 | Pride
Sumo Phosphorylation Deep Proteome K0-sumo 
ProteomicsSUMO Activated Target Traps (SATTs) enable the identification of a comprehensive E3-specific SUMO proteome
Ubiquitin and ubiquitin-like conjugation cascades consist of dedicated E1, E2 and E3 enzymes with E3s providing substrate specificity. Mass spectrometry-based approaches have enabled the identification of more than 60,000 acceptor sites for ubiquitin and 40,000 acceptor sites for SUMO2/3. However, E...
ORGANISM(S): Homo sapiens (Human) 
2023-08-03 | PXD038326 | Pride
E3 enzymes Sumo1 Sumo2 
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 
ProteomicsRNF212B E3 ligase is essential for crossover designation and maturation during male and female meiosis in the mouse
Meiosis, a reductional cell division, relies on precise initiation, maturation and resolution of crossovers (COs) during prophase I to ensure the accurate segregation of homologous chromosomes during metaphase I. This process is regulated by the interplay of RING-E3 ligases such as RNF212 and HEI10 ...
ORGANISM(S): Homo sapiens (Human) 
2024-05-31 | PXD047332 | Pride
Meiosis Sumo Ubiquitin 
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
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