| Tissue Specificity | Brain. Highly expressed in the cerebral cortex (at protein level). Severely decreased in the affected brain areas in Parkinson disease and dementia with Lewy bodies. |
| Post Translational Modifications | Auto-ubiquitinated. Poly-ubiquitinated in cultured cells, whereas it is monoubiquitinated in vitro. |
| Function | E3 ubiquitin-protein ligase which ubiquitinates itself in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting signal for proteasomal degradation. May play a role in regulation of neuronal functions and may also participate in the formation or breakdown of abnormal inclusions in neurodegenerative disorders. May act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for the SNARE complex formation. |
| Protein Name | E3 Ubiquitin-Protein Ligase Trim9Ring Finger Protein 91Ring-Type E3 Ubiquitin Transferase Trim9Tripartite Motif-Containing Protein 9 |
| Database Links | Reactome: R-HSA-983168 |
| Cellular Localisation | CytoplasmCell ProjectionDendriteCytoplasmic VesicleSecretory VesicleSynaptic VesicleSynapseCytoskeletonEnriched At Synaptic Terminals Where It Exists In A Soluble Form And A Synaptic Vesicle-Associated FormAssociated With The CytoskeletonFound In Proximal Dendrites Of Pyramidal Neurons In The Cerebral Cortex And HippocampusAnd Purkinje Cells In The Cerebellum |
| Alternative Antibody Names | Anti-E3 Ubiquitin-Protein Ligase Trim9 antibodyAnti-Ring Finger Protein 91 antibodyAnti-Ring-Type E3 Ubiquitin Transferase Trim9 antibodyAnti-Tripartite Motif-Containing Protein 9 antibodyAnti-TRIM9 antibodyAnti-KIAA0282 antibodyAnti-RNF91 antibody |
Information sourced from Uniprot.org
