Dataset Information
FilaminC pull-down experiment from myotube lysates
Ontology highlight
ABSTRACT:
INSTRUMENT(S): Q Exactive
ORGANISM(S): Homo Sapiens (human) Mus Musculus (mouse)
TISSUE(S): Myotube
SUBMITTER: 
Friedel Drepper
LAB HEAD: Bettina Warscheid
PROVIDER: PXD017670 | Pride | 2020-05-25
REPOSITORIES: Pride
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| QEplus025629.index | Other | |||
| QEplus025629.raw | Raw | |||
| QEplus025644.index | Other | |||
| QEplus025644.raw | Raw | |||
| UniProt_KB_Mouse_Isoform_with_FLNc1821_FLNc1_3.fasta | Fasta |
Items per page: 1 - 5 of 7 |
Publications
Phosphoproteomics identifies dual-site phosphorylation in an extended basophilic motif regulating FILIP1-mediated degradation of filamin-C.
Communications biology 20200522 1
The PI3K/Akt pathway promotes skeletal muscle growth and myogenic differentiation. Although its importance in skeletal muscle biology is well documented, many of its substrates remain to be identified. We here studied PI3K/Akt signaling in contracting skeletal muscle cells by quantitative phosphoproteomics. We identified the extended basophilic phosphosite motif RxRxxp[S/T]xxp[S/T] in various proteins including filamin-C (FLNc). Importantly, this extended motif, located in a unique insert in Ig- ...[more]
