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UnknownSite-specific Interaction Mapping of Phosphorylated Ubiquitin to Uncover Parkin Activation.
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S-EPMC4646171 | biostudies-literature
ProteomicsUbiquitination at the Parkin ubiquitin-like domain suggests a new mechanism for Parkin activation
The mitochondrial kinase PINK1 and the cytosolic ubiquitin ligase (E3) Parkin is involved in mitochondrial quality control. PINK1, which phosphorylates ubiquitin at serine 65 residue and the ubiquitin-like (Ubl) domain of Parkin at serine 65 residue, promotes the Parkin activation and translocation ...
ORGANISM(S): Homo Sapiens (human) 
2022-08-24 | PXD026554 | JPOST Repository
ProteomicsUbiquitin S65 proteomics: Targets of ubiquitin phosphorylation
Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2015-07-07 | PXD002201 | Pride
Yeast Orbitrap Phosphorylation Ubiquitin 
ProteomicsUbiquitin S65 proteomics: Association of ubiquitin mutants with ubiqiutin binding domains
Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2015-07-07 | PXD002202 | Pride
Yeast Orbitrap Phosphorylation Ubiquitin 
ProteomicsUbiquitin S65 proteomics: H2O2 whole cell lysate protein response
Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2015-07-07 | PXD002197 | Pride
Yeast Orbitrap Phosphorylation Ubiquitin 
ProteomicsUbiquitin S65 proteomics: H2O2 ubiquitylation response
Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2015-07-07 | PXD002200 | Pride
Yeast Orbitrap Phosphorylation Ubiquitin 
ProteomicsUbiquitin S65 proteomics: H2O2 phosphorylation response
Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2015-07-07 | PXD002198 | Pride
Yeast Orbitrap Phosphorylation Ubiquitin 
ProteomicsThe interactome of tau phosphorylated at T217 in Alzheimers disease human brain tissue
Tau phosphorylation and aggregation are pathological features of Alzheimers disease. Tau phosphorylated at threonine 217 (pT217) and threonine 231 (pT231) are early fluid biomarkers of Alzheimers disease, suggesting early involvement in disease. However, little is known about the specific actions of...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2024-11-11 | MSV000096377 | MassIVE
ProteomicsUbiquitin S65 proteomics: H2O2 Histag affinity purification protein response
Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2015-07-07 | PXD002199 | Pride
Yeast Orbitrap Phosphorylation Ubiquitin 
ProteomicsUbiquitin S65 proteomics: S65E Ubiquitin full replacement protein quantitation
Ubiquitylation is an essential post-translational modification that regulates numerous cellular processes, most notably protein degradation. Ubiquitin itself can be post-translationally modified by phosphorylation, with nearly every serine, threonine, and tyrosine residue having the potential to be...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2015-07-07 | PXD002204 | Pride
Yeast Orbitrap Phosphorylation Ubiquitin 
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