STX1A

680420907ENSG00000106089ENSMUSG00000007207Q16623Q75ME0O35526NM_001165903NM_004603NM_016801NM_001359179NP_001159375NP_004594NP_004594.1NP_058081NP_001346108Syntaxin-1A is a protein that in humans is encoded by the STX1A gene.1br0: THREE DIMENSIONAL STRUCTURE OF THE N-TERMINAL DOMAIN OF SYNTAXIN 1A1dn1:1ez3: CRYSTAL STRUCTURE OF THE NEURONAL T-SNARE SYNTAXIN-1A1hvv: SELF-ASSOCIATION OF THE H3 REGION OF SYNTAXIN 1A: IMPLICATIONS FOR SNARE COMPLEX ASSEMBLY1jth: Crystal structure and biophysical properties of a complex between the N-terminal region of SNAP25 and the SNARE region of syntaxin 1a1kil: Three-dimensional structure of the complexin/SNARE complex1n7s: High Resolution Structure of a Truncated Neuronal SNARE Complex1sfc: NEURONAL SYNAPTIC FUSION COMPLEX1urq: CRYSTAL STRUCTURE OF NEURONAL Q-SNARES IN COMPLEX WITH R-SNARE MOTIF OF TOMOSYN Syntaxin-1A is a protein that in humans is encoded by the STX1A gene. Synaptic vesicles store neurotransmitters that are released during calcium-regulated exocytosis. The specificity of neurotransmitter release requires the localization of both synaptic vesicles and calcium channels to the presynaptic active zone. Syntaxins function in this vesicle fusion process. Syntaxin-1A is a member of the syntaxin superfamily. Syntaxins are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane. Syntaxins possess a single C-terminal transmembrane domain, a SNARE domain (known as H3), and an N-terminal regulatory domain (Habc). Syntaxins bind synaptotagmin in a calcium-dependent fashion and interact with voltage dependent calcium and potassium channels via the C-terminal H3 domain. Syntaxin-1A is a key protein in ion channel regulation and synaptic exocytosis. Syntaxins serve as a substrate for botulinum neurotoxin type C, a metalloprotease that blocks exocytosis and has high affinity for a molecular complex that includes the alpha-latrotoxin receptor which produces explosive exocytosis. The expression level of STX1A is directly correlated with intelligence in Williams syndrome. Click on genes, proteins and metabolites below to link to respective articles. STX1A has been shown to interact with: This article incorporates text from the United States National Library of Medicine, which is in the public domain.