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ProteomicsSystematic discovery of Short Linear Motifs decodes calcineurin phosphatase signaling
Short linear motifs (SLiMs) form dynamic protein-protein interactions essential for signaling; however, sequence degeneracy and low binding affinities make them difficult to identify. In this study, we employed multiple, unbiased systematic approaches for SLiM discovery to elucidate the regulatory n...
ORGANISM(S): Homo sapiens (Human) 
2020-12-02 | PXD017868 | Pride
Signaling Calcium Short linear motifs (slims) Nuclear pore complex (npc) Intrinsically disordered proteins (idps) Phosphatase 
ProteomicsDe novo BCR-ABL linear kinase motifs revealed by phosphoproteomics in yeast
Protein tyrosine phosphorylation (pY) is central to many cellular signaling pathways. Deregulation of pY can lead to malignancies such as leukemia. Thus, assigning kinase-substrate relations is imperative to understand disease alterations. However, such efforts are complicated by kinase redundancy, ...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2023-07-20 | PXD038551 | Pride
Bcr-abl Ksea Phosphoproteomics Abl Linear sequence motif Protein tyrosine phosphorylation 
ProteomicsWigington_calcineurinphosphatasesignaling_SWATH_2019
The files are associated with a manuscript submitted for publication by Callie P. Wigington et al. The main goal of this paper was to identify how calcineurin (CN) binds substrates via PxIxIT and LxVP motifs, elucidated through short linear motifs (SLiM) discovery.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2019-04-16 | MSV000083697 | MassIVE
ProteomicsWigington_calcineurinphosphatasesignaling_2019
The files are associated with a manuscript submitted for publication by Callie P. Wigington et al. The main goal of this paper was to identify how calcineurin (CN) binds substrates via PxIxIT and LxVP motifs, elucidated through short linear motifs (SLiM) discovery.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2019-04-16 | MSV000083695 | MassIVE
ProteomicsWigington_CalcineurinPhosphataseSignaling
The files are associated with a manuscript submitted for publication by Callie P. Wigington et al. The main goal of this paper was to identify how calcineurin (CN) binds substrates via PxIxIT and LxVP motifs, elucidated through short linear motifs (SLiM) discovery.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2019-04-15 | MSV000083685 | MassIVE
TranscriptomicsActivity motifs reveal principles of timing in transcriptional control of the yeast metabolic network
Significant insight about biological networks arises from the study of network motifs –overly abundant network subgraphs, but such wiring patterns do not specify when and how potential routes within a cellular network are used. To address this limitation, we introduce activity motifs, which captur...
ORGANISM(S): Saccharomyces cerevisiae 
2010-06-25 | E-GEOD-13219 | biostudies-arrayexpress
ProteomicsA proteome-wide dependency map of protein interaction motifs
Short linear motifs (SLiMs) are the most ubiquitous protein interaction modules in the unstructured regions of the human proteome. Despite their central role in protein function, our understanding of the contribution of SLiMs to cellular homeostasis remains limited. To address this, we designed base...
ORGANISM(S): Homo sapiens (Human) 
2026-01-14 | PXD055750 | Pride
Cellular homeostasis Short linear motifs Proteome 
UnknownELM--the database of eukaryotic linear motifs.
Not available
S-EPMC3245074 | biostudies-literature
UnknownPrediction of virus-host protein-protein interactions mediated by short linear motifs.
Not available
S-EPMC5345135 | biostudies-literature
UnknownEnhancing prediction of short linear protein motifs with Wregex 3.0.
Not available
S-EPMC11318550 | biostudies-literature
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