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TRIM9 iso5
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. Belongs to the TRIM/RBCC family. 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. 3 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
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| Protein type: EC 6.3.2.-; Ubiquitin conjugating system; Ubiquitin ligase |
| Chromosomal Location of human Ortholog: 14q22.1 |
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Cellular Component:
cytoplasm; cytoskeleton; dendrite; synaptic vesicle
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Molecular Function:
protein binding; protein domain specific binding; protein homodimerization activity; ubiquitin protein ligase activity; zinc ion binding
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Biological Process:
proteasome-mediated ubiquitin-dependent protein catabolic process; protein ubiquitination
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Reference #:
Q9C026-5
(UniProtKB)
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Alt. Names/Synonyms: E3 ubiquitin-protein ligase TRIM9; homolog of rat RING finger Spring; KIAA0282; RING finger protein 91; RING-type E3 ubiquitin transferase TRIM9; RNF91; SNAP-25-interacting RING finger protein; SPRING; TRIM9; TRIM9 iso5; tripartite motif containing 9; tripartite motif-containing 9; Tripartite motif-containing protein 9
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Gene Symbols: TRIM9
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Molecular weight:
61,346 Da
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Basal Isoelectric point:
7.2
Predict pI for various phosphorylation states
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Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology®
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