BAIT
MAPT
AI413597, AW045860, Mtapt, Tau, RP23-136D4.1
microtubule-associated protein tau
GO Process (16)
GO Function (10)
GO Component (15)
Gene Ontology Biological Process
- adult walking behavior [IGI]
- apoptotic process [ISO]
- axon cargo transport [IGI]
- axon extension [IMP]
- axonogenesis [IGI]
- intrinsic apoptotic signaling pathway in response to oxidative stress [ISO]
- microtubule cytoskeleton organization [IMP, ISO]
- mitochondrion transport along microtubule [IMP]
- negative regulation of intracellular transport [IMP]
- neuron migration [IMP]
- positive regulation of axon extension [IMP, ISO]
- positive regulation of microtubule polymerization [ISO]
- regulation of autophagy [ISO]
- regulation of microtubule-based movement [IDA]
- response to nutrient [ISO]
- response to organic substance [ISO]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- axon [IDA, ISO]
- axonal growth cone [ISO]
- axoneme [IDA]
- cell [IGI]
- cytoplasm [IDA]
- cytoplasmic ribonucleoprotein granule [ISO]
- growth cone [ISO]
- intracellular [IGI]
- microtubule cytoskeleton [IDA]
- neuron projection [ISO]
- nuclear periphery [ISO]
- nucleus [IDA]
- plasma membrane [ISO]
- postsynaptic density [IDA]
- tubulin complex [ISO]
Mus musculus
PREY
CKB
B-CK, Bck, Ck-3, Ck3, Ckbb
creatine kinase, brain
GO Process (1)
GO Function (1)
GO Component (4)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Mus musculus
Affinity Capture-MS
An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.
Publication
Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-Tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation.
One of the key pathological hallmarks of Alzheimer disease (AD) is the accumulation of paired helical filaments (PHFs) of hyperphosphorylated microtubule-associated protein Tau. Tandem mass spectrometry was employed to examine PHF-Tau post-translational modifications, in particular protein phosphorylation and ubiquitination, to shed light on their role in the early stages of Alzheimer disease. PHF-Tau from Alzheimer disease brain was affinity-purified by ... [more]
J. Biol. Chem. Apr. 21, 2006; 281(16);10825-38 [Pubmed: 16443603]
Throughput
- High Throughput
Curated By
- BioGRID