MGP Database

New search | Record Overview | Ontology/Pathway Information | Domain Information | UniProt Annotations | Related Proteins
MGP006342

UniProt Annotations

Entry Information
Gene Nametripartite motif containing 9
Protein EntryTRIM9_HUMAN
UniProt IDQ9C026
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=3; Name=1; Synonyms=Beta; IsoId=Q9C026-1; Sequence=Displayed; Name=4; IsoId=Q9C026-4; Sequence=VSP_007922, VSP_007923, VSP_007924; Note=May be due to a competing donor splice site, to exon inclusion and to intron retention.; Name=5; IsoId=Q9C026-5; Sequence=VSP_007925, VSP_007926; Note=May be due to intron retention.;
DomainThe coiled coil domain mediates the interaction with the N-terminal t-SNARE domain of SNAP25. {ECO:0000250}.
FunctionE3 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. {ECO:0000269|PubMed:20085810}.
PathwayProtein modification; protein ubiquitination.
PtmAuto-ubiquitinated. Poly-ubiquitinated in cultured cells, whereas it is monoubiquitinated in vitro. {ECO:0000269|PubMed:20085810}.
Sequence CautionSequence=AAG53490.1; Type=Frameshift; Positions=660; Evidence={ECO:0000305}; Sequence=AAG53492.1; Type=Frameshift; Positions=655; Evidence={ECO:0000305}; Sequence=BAA13398.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; Sequence=BAA13398.2; Type=Frameshift; Positions=660; Evidence={ECO:0000305};
SimilarityBelongs to the TRIM/RBCC family. {ECO:0000305}.
SimilarityContains 1 B30.2/SPRY domain. {ECO:0000255|PROSITE- ProRule:PRU00548}.
SimilarityContains 1 COS domain. {ECO:0000255|PROSITE- ProRule:PRU00586}.
SimilarityContains 1 fibronectin type-III domain. {ECO:0000255|PROSITE-ProRule:PRU00316}.
SimilarityContains 1 RING-type zinc finger. {ECO:0000255|PROSITE-ProRule:PRU00175}.
SimilarityContains 2 B box-type zinc fingers. {ECO:0000255|PROSITE-ProRule:PRU00024}.
Subcellular LocationCytoplasm {ECO:0000269|PubMed:20085810}. Cell projection, dendrite {ECO:0000269|PubMed:20085810}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250}. Cell junction, synapse {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. 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. {ECO:0000250}.
SubunitInteracts with SNAP25. {ECO:0000250}.
Tissue SpecificityBrain. Highly expressed in the cerebral cortex (at protein level). Severely decreased in the affected brain areas in Parkinson disease and dementia with Lewy bodies. {ECO:0000269|PubMed:20085810}.
  logo