UBE2D2
Gene Ontology Biological Process
- MyD88-independent toll-like receptor signaling pathway [TAS]
- TRIF-dependent toll-like receptor signaling pathway [TAS]
- cellular protein modification process [TAS]
- cellular response to hypoxia [TAS]
- innate immune response [TAS]
- protein K48-linked ubiquitination [IDA]
- protein polyubiquitination [IDA]
- protein ubiquitination [IDA]
- regulation of transcription from RNA polymerase II promoter in response to hypoxia [TAS]
- toll-like receptor 3 signaling pathway [TAS]
- toll-like receptor 4 signaling pathway [TAS]
- toll-like receptor signaling pathway [TAS]
- ubiquitin-dependent protein catabolic process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
MAPT
Gene Ontology Biological Process
- apoptotic process [TAS]
- cellular component disassembly involved in execution phase of apoptosis [TAS]
- generation of neurons [NAS]
- microtubule cytoskeleton organization [IDA]
- positive regulation of axon extension [IDA]
- positive regulation of microtubule polymerization [IDA]
- regulation of autophagy [IGI]
- regulation of microtubule polymerization [NAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Biochemical Activity (Ubiquitination)
An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.
Publication
CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival.
The microtubule-binding protein tau has been implicated in the neurofibrillary pathology of Alzheimer's disease. Within affected cells, ubiquitinated and hyperphosphorylated tau assembles into massive filamentous polymers. Eventually these tangle-bearing neurons die. The formation of neurofibrillary tangles closely parallels the progression and anatomic distribution of neuronal loss in Alzheimer's disease, suggesting that these lesions play a role in the disease pathogenesis. ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID