Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
RGD ISO annotations to rat from other mammalian species
Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex.
Munc 18a binding to syntaxin 1A and 1B isoforms defines its localization at the plasma membrane and blocks SNARE assembly in a three-hybrid system assay.
Co-purification and localization of Munc18-1 (p67) and Cdk5 with neuronal cytoskeletal proteins.
Munc-18-1 inhibits phospholipase D activity by direct interaction in an epidermal growth factor-reversible manner.
Munc18-1 regulates early and late stages of exocytosis via syntaxin-independent protein interactions.
Nuclear localization of Munc18-1 (p67) in the adult rat brain and PC12 cells.
Munc18-1 stabilizes syntaxin 1, but is not essential for syntaxin 1 targeting and SNARE complex formation.
Munc18 plays an important role in the regulation of glutamate release during female puberty onset.
Munc18-1 binds directly to the neuronal SNARE complex.
A cytosolic splice variant of Cab45 interacts with Munc18b and impacts on amylase secretion by pancreatic acini.
Binding of the Munc13-1 MUN domain to membrane-anchored SNARE complexes.
Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide.
Munc18-1 binding to the neuronal SNARE complex controls synaptic vesicle priming.
Vesicle fusion probability is determined by the specific interactions of munc18.
Possible roles for Munc18-1 domain 3a and Syntaxin1 N-peptide and C-terminal anchor in SNARE complex formation.
Involvement of Rab3A in vesicle priming during exocytosis: interaction with Munc13-1 and Munc18-1.
SNAREpin assembly by Munc18-1 requires previous vesicle docking by synaptotagmin 1.
Crucial role of the hydrophobic pocket region of Munc18 protein in mast cell degranulation.
An extended helical conformation in domain 3a of Munc18-1 provides a template for SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) complex assembly.
Composition of isolated synaptic boutons reveals the amounts of vesicle trafficking proteins.
Syntaxin opening by the MUN domain underlies the function of Munc13 in synaptic-vesicle priming.
The Q-soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor (Q-SNARE) SNAP-47 Regulates Trafficking of Selected Vesicle-associated Membrane Proteins (VAMPs).
Munc18-1 and the Syntaxin-1 N Terminus Regulate Open-Closed States in a t-SNARE Complex.
Complexins: cytosolic proteins that regulate SNAP receptor function.
Mints, Munc18-interacting proteins in synaptic vesicle exocytosis.
A role for Sec1/Munc18 proteins in platelet exocytosis.
Munc18-1 controls SNARE protein complex assembly during human sperm acrosomal exocytosis.
Role of H(abc) domain in membrane trafficking and targeting of syntaxin 1A.
UniProtKB P61765 STXB1_RAT record
Manual literature synthesis for rat Stxbp1