Sort   by:  
 Page size 
GenomicsChromatin modification by SUMO-1 stimulates the promoters of translation machinery genes
We determined the occupancy of SUMO-1 on chromatin in HeLa cells by use of chromatin affinity purification coupled with next generation sequencing 18 samples examined in syncrhonized HeLa cells: Cells in G1, early S (S0)/mid (S3)/ late S phase (S6), and mitosis (M), triplicates for each sample. 1 Ch...
ORGANISM(S): Homo sapiens 
2012-10-02 | E-GEOD-41264 | 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
Genomicsheat shock SUMO-2 ChIP-seq
Analysis of changes in SUMO-2 binding to chromatin in response to heat shock in human U2OS cells
ORGANISM(S): Homo sapiens 
2015-07-13 | E-MTAB-2368 | biostudies-arrayexpress
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
ProteomicsIDENTIFICATION OF SUMO-2/3 MODIFIED PROTEINS ASSOCIATED WITH MITOTIC CHROMOSOMES
Sumoylation is essential for progression through mitosis, but the specific protein targets and functions remain poorly understood. In this study, we used chromosome spreads to more precisely define the localization of SUMO-2/3 to the inner-centromere and protein scaffold of mitotic chromosomes. We a...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2014-10-07 | MSV000078890 | MassIVE
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 (ncbitaxon:9606) 
2017-03-31 | MSV000080851 | MassIVE
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
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
OtherSystem-wide analysis of SUMOylation dynamics in response to replication stress reveals novel SUMO target proteins and acceptor lysines relevant for genome stability.
Data from ProteomeXchange, PXD ID: PXD001736. File: 20140408_QE_UP_U2OS1222_2h_04a.mzml. Published as part of . From the Abstract: {{i}} To address this, we have purified and identified SUMO-2 target proteins regulated by replication stress in human cells. The developed methodology enabled single s...
ORGANISM(S): Homo_sapiens_viruses, Human_female 
GPM32310018476 | GPMDB
Resource Reanalysis 
Sort   by:  
 Page size