Q15836 · VAMP3_HUMAN
- ProteinVesicle-associated membrane protein 3
- GeneVAMP3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids100 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 41-42 | (Microbial infection) Cleavage; by C.botulinum neurotoxin type F (BoNT/F, botF) | ||||
Sequence: QK | ||||||
Site | 42-43 | (Microbial infection) Cleavage; by C.botulinum neurotoxin type D (BoNT/D, botD) | ||||
Sequence: KL | ||||||
Site | 58-59 | (Microbial infection) Cleavage; by C.botulinum neurotoxin type B (BoNT/B, botB) | ||||
Sequence: SQ |
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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Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameVesicle-associated membrane protein 3
- Short namesVAMP-3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ15836
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Early endosome membrane ; Single-pass type IV membrane protein
Recycling endosome membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 2-77 | Cytoplasmic | ||||
Sequence: STGPTAATGSNRRLQQTQNQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAAKLKRKYWWKNCK | ||||||
Transmembrane | 78-98 | Helical; Anchor for type IV membrane protein | ||||
Sequence: MWAIGITVLVIFIIIIIVWVV | ||||||
Topological domain | 99-100 | Vesicular | ||||
Sequence: SS |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 66-68 | Abolished ubiquitination by RNF167; when associated with R-77. | ||||
Sequence: KLK → RLR | ||||||
Mutagenesis | 77 | Abolished ubiquitination by RNF167; when associated with 66-R--R-68. | ||||
Sequence: K → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 114 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 initiator methionine, modified residue, modified residue (large scale data), chain, cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 2 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Chain | PRO_0000206728 | 2-100 | UniProt | Vesicle-associated membrane protein 3 | |||
Sequence: STGPTAATGSNRRLQQTQNQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAAKLKRKYWWKNCKMWAIGITVLVIFIIIIIVWVVSS | |||||||
Modified residue (large scale data) | 3 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 6 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 9 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 11 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 44 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 58 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 62 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 63 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 66 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Cross-link | 68 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Cross-link | 77 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K |
Post-translational modification
Ubiquitinated by RNF167 at Lys-66, Lys-68 and Lys-77, regulating the recycling endosome pathway.
(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type B (BoNT/B, botB) which hydrolyzes the 59-Gln-|-Phe-60 bond and probably inhibits neurotransmitter release (PubMed:22289120).
(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type D (BoNT/D, botD) which hydrolyzes the 42-Lys-|-Leu-43 bond and probably inhibits neurotransmitter release (PubMed:22289120).
Note that humans are not known to be infected by C.botulinum type D
Note that humans are not known to be infected by C.botulinum type D
(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type F (BoNT/F, botF) which hydrolyzes the 41-Gln-|-Lys-42 bond and probably inhibits neurotransmitter release (PubMed:22289120).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with BVES (via the C-terminus cytoplasmic tail). Interacts with BCAP31; involved in VAMP3 export from the endoplasmic reticulum (By similarity).
Interacts with BAIAP3; this interaction is increased in the presence of calcium (PubMed:28626000).
Interacts with PICALM
Interacts with BAIAP3; this interaction is increased in the presence of calcium (PubMed:28626000).
Interacts with PICALM
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-74 | v-SNARE coiled-coil homology | ||||
Sequence: RLQQTQNQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAAKLKRKYWWK |
Sequence similarities
Belongs to the synaptobrevin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length100
- Mass (Da)11,309
- Last updated2007-01-23 v3
- Checksum347E9163157AFF42
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
K7EKX0 | K7EKX0_HUMAN | VAMP3 | 72 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 77 | in Ref. 3; AAH05941 | ||||
Sequence: K → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U64520 EMBL· GenBank· DDBJ | AAB05814.1 EMBL· GenBank· DDBJ | mRNA | ||
BT007327 EMBL· GenBank· DDBJ | AAP35991.1 EMBL· GenBank· DDBJ | mRNA | ||
Z98884 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC003570 EMBL· GenBank· DDBJ | AAH03570.1 EMBL· GenBank· DDBJ | mRNA | ||
BC005941 EMBL· GenBank· DDBJ | AAH05941.1 EMBL· GenBank· DDBJ | mRNA | ||
BC007050 EMBL· GenBank· DDBJ | AAH07050.1 EMBL· GenBank· DDBJ | mRNA |