UBE2W
Gene Ontology Biological Process
Gene Ontology Molecular Function
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
Co-crystal Structure
Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.
Publication
Intrinsic disorder drives N-terminal ubiquitination by Ube2w.
Ubiquitination of the αN-terminus of protein substrates has been reported sporadically since the early 1980s. However, the identity of an enzyme responsible for this unique ubiquitin (Ub) modification has only recently been elucidated. We show the Ub-conjugating enzyme (E2) Ube2w uses a unique mechanism to facilitate the specific ubiquitination of the α-amino group of its substrates that involves recognition of ... [more]
Throughput
- Low Throughput
Additional Notes
- NMR
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
UBE2W MAPT | Biochemical Activity Biochemical Activity 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. | Low | - | BioGRID | 2877704 |
Curated By
- BioGRID