Q9UJD0 · RIMS3_HUMAN
- ProteinRegulating synaptic membrane exocytosis protein 3
- GeneRIMS3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids308 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Regulates synaptic membrane exocytosis.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoskeleton of presynaptic active zone | |
Cellular Component | presynaptic active zone | |
Cellular Component | presynaptic membrane | |
Molecular Function | small GTPase binding | |
Molecular Function | transmembrane transporter binding | |
Biological Process | calcium ion-regulated exocytosis of neurotransmitter | |
Biological Process | calcium-ion regulated exocytosis | |
Biological Process | positive regulation of synaptic transmission | |
Biological Process | regulation of membrane potential | |
Biological Process | regulation of synaptic plasticity | |
Biological Process | regulation of synaptic vesicle exocytosis |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRegulating synaptic membrane exocytosis protein 3
- Short namesNim3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UJD0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 383 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000190204 | 1-308 | UniProt | Regulating synaptic membrane exocytosis protein 3 | |||
Sequence: MFNGEPGPASSGASRNVVRSSSISGEICGSQQAGGGAGTTTAKKRRSSLGAKMVAIVGLTQWSKSTLQLPQPEGATKKLRSNIRRSTETGIAVEMRSRVTRQGSRESTDGSTNSNSSDGTFIFPTTRLGAESQFSDFLDGLGPAQIVGRQTLATPPMGDVHIAIMDRSGQLEVEVIEARGLTPKPGSKSLPATYIKVYLLENGACLAKKKTKMTKKTCDPLYQQALLFDEGPQGKVLQVIVWGDYGRMDHKCFMGMAQIMLDELDLSAAVTGWYKLFPTSSVADSTLGSLTRRLSQSSLESATSPSCS | |||||||
Modified residue (large scale data) | 116 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 295 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 295 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 297 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 298 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 298 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 301 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Binds PPFIA3 (By similarity).
Does not bind RAB3
Does not bind RAB3
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9UJD0 | COMT P21964-2 | 3 | EBI-3909436, EBI-10200977 | |
BINARY | Q9UJD0 | HLA-A Q5SUL5 | 3 | EBI-3909436, EBI-8561769 | |
BINARY | Q9UJD0 | KAT5 Q92993 | 3 | EBI-3909436, EBI-399080 | |
BINARY | Q9UJD0 | LMO3 Q8TAP4-4 | 3 | EBI-3909436, EBI-11742507 | |
BINARY | Q9UJD0 | MEOX2 Q6FHY5 | 3 | EBI-3909436, EBI-16439278 | |
BINARY | Q9UJD0 | PECAM1 P16284 | 3 | EBI-3909436, EBI-716404 | |
BINARY | Q9UJD0 | PICK1 Q9NRD5 | 3 | EBI-3909436, EBI-79165 | |
BINARY | Q9UJD0 | SETDB1 Q15047-2 | 3 | EBI-3909436, EBI-9090795 | |
BINARY | Q9UJD0 | VIM P08670 | 3 | EBI-3909436, EBI-353844 | |
BINARY | Q9UJD0 | YWHAG P61981 | 5 | EBI-3909436, EBI-359832 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 86-120 | Disordered | ||||
Sequence: STETGIAVEMRSRVTRQGSRESTDGSTNSNSSDGT | ||||||
Compositional bias | 104-120 | Polar residues | ||||
Sequence: SRESTDGSTNSNSSDGT | ||||||
Domain | 156-274 | C2 | ||||
Sequence: PMGDVHIAIMDRSGQLEVEVIEARGLTPKPGSKSLPATYIKVYLLENGACLAKKKTKMTKKTCDPLYQQALLFDEGPQGKVLQVIVWGDYGRMDHKCFMGMAQIMLDELDLSAAVTGWY |
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9UJD0-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length308
- Mass (Da)32,796
- Last updated2000-05-01 v1
- ChecksumEDB57162FC75DF5F
Q9UJD0-2
- Name2
Sequence caution
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 24 | in Ref. 3; BAA13243 | ||||
Sequence: S → G | ||||||
Compositional bias | 104-120 | Polar residues | ||||
Sequence: SRESTDGSTNSNSSDGT | ||||||
Alternative sequence | VSP_055836 | 121-153 | in isoform 2 | |||
Sequence: FIFPTTRLGAESQFSDFLDGLGPAQIVGRQTLA → CVQPRAVVPSLLLGPPVTEPLGRVHLPHYPARG | ||||||
Alternative sequence | VSP_055837 | 154-308 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY326956 EMBL· GenBank· DDBJ | AAQ01683.1 EMBL· GenBank· DDBJ | mRNA | ||
KJ535026 EMBL· GenBank· DDBJ | AHW56665.1 EMBL· GenBank· DDBJ | mRNA | ||
D87074 EMBL· GenBank· DDBJ | BAA13243.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL031289 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471059 EMBL· GenBank· DDBJ | EAX07206.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471059 EMBL· GenBank· DDBJ | EAX07207.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC003103 EMBL· GenBank· DDBJ | AAH03103.1 EMBL· GenBank· DDBJ | mRNA |