Human Gene TRIM9 (ENST00000298355.7) from GENCODE V44
Description: 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. (from UniProt Q9C026) RefSeq Summary (NM_015163): The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes to cytoplasmic bodies. Its function has not been identified. Alternate splicing of this gene generates two transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008]. Gencode Transcript: ENST00000298355.7 Gencode Gene: ENSG00000100505.14 Transcript (Including UTRs) Position: hg38 chr14:50,975,262-51,096,061 Size: 120,800 Total Exon Count: 10 Strand: - Coding Region Position: hg38 chr14:50,977,291-51,094,939 Size: 117,649 Coding Exon Count: 10
ID:TRIM9_HUMAN DESCRIPTION: RecName: Full=E3 ubiquitin-protein ligase TRIM9; EC=6.3.2.-; AltName: Full=RING finger protein 91; AltName: Full=Tripartite motif-containing protein 9; 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. PATHWAY: Protein modification; protein ubiquitination. SUBUNIT: Interacts with SNAP25 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Cell projection, dendrite. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle (By similarity). Cell junction, synapse (By similarity). Cytoplasm, cytoskeleton (By similarity). Note=Enriched at synaptic terminals where it exists in a soluble form and a synaptic vesicle- associated form. Associated with the cytoskeleton (By similarity). Found in proximal dendrites of pyramidal neurons in the cerebral cortex and hippocampus, and Purkinje cells in the cerebellum. 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. DOMAIN: The coiled coil domain mediates the interaction with the N-terminal t-SNARE domain of SNAP25 (By similarity). PTM: Auto-ubiquitinated. Poly-ubiquitinated in cultured cells, whereas it is monoubiquitinated in vitro. SIMILARITY: Belongs to the TRIM/RBCC family. SIMILARITY: Contains 2 B box-type zinc fingers. SIMILARITY: Contains 1 B30.2/SPRY domain. SIMILARITY: Contains 1 COS domain. SIMILARITY: Contains 1 fibronectin type-III domain. SIMILARITY: Contains 1 RING-type zinc finger. SEQUENCE CAUTION: Sequence=AAG53490.1; Type=Frameshift; Positions=660; Sequence=AAG53492.1; Type=Frameshift; Positions=655; Sequence=BAA13398.2; Type=Erroneous initiation; Note=Translation N-terminally shortened; Sequence=BAA13398.2; Type=Frameshift; Positions=660;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9C026
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.