Syntaxin-1A

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• ATP-dependent protein binding Source: RGD <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Myosin-Va regulates exocytosis through the submicromolar Ca2+-dependent binding of syntaxin-1A."
    Watanabe M., Nomura K., Ohyama A., Ishikawa R., Komiya Y., Hosaka K., Yamauchi E., Taniguchi H., Sasakawa N., Kumakura K., Ushiki T., Sato O., Ikebe M., Igarashi M.
    Mol. Biol. Cell 16:4519-4530(2005) [PubMed] [Europe PMC] [Abstract]
• calcium channel inhibitor activity Source: RGDInferred from sequence orthologyⁱ
  • "Syntaxin 1 interacts with the L(D) subtype of voltage-gated Ca(2+) channels in pancreatic beta cells."
    Yang S.N., Larsson O., Branstrom R., Bertorello A.M., Leibiger B., Leibiger I.B., Moede T., Kohler M., Meister B., Berggren P.O.
    Proc. Natl. Acad. Sci. U.S.A. 96:10164-10169(1999) [PubMed] [Europe PMC] [Abstract]
• calcium-dependent protein binding Source: RGDInferred from physical interactionⁱ
  • "Myosin-Va regulates exocytosis through the submicromolar Ca2+-dependent binding of syntaxin-1A."
    Watanabe M., Nomura K., Ohyama A., Ishikawa R., Komiya Y., Hosaka K., Yamauchi E., Taniguchi H., Sasakawa N., Kumakura K., Ushiki T., Sato O., Ikebe M., Igarashi M.
    Mol. Biol. Cell 16:4519-4530(2005) [PubMed] [Europe PMC] [Abstract]
• chloride channel inhibitor activity Source: RGDInferred from sequence orthologyⁱ
  • "Endosomal SNARE proteins regulate CFTR activity and trafficking in epithelial cells."
    Bilan F., Nacfer M., Fresquet F., Norez C., Melin P., Martin-Berge A., Costa de Beauregard M.A., Becq F., Kitzis A., Thoreau V.
    Exp. Cell Res. 314:2199-2211(2008) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: RGDInferred from sequence orthologyⁱ
  • "Protein interaction network of alternatively spliced isoforms from brain links genetic risk factors for autism."
    Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M., Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J.

    , Vacic V., Calderwood M.A., Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D., Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.
    Nat. Commun. 5:3650-3650(2014) [PubMed] [Europe PMC] [Abstract]
• ion channel binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.14

    "K+ channel facilitation of exocytosis by dynamic interaction with syntaxin."
    Singer-Lahat D., Sheinin A., Chikvashvili D., Tsuk S., Greitzer D., Friedrich R., Feinshreiber L., Ashery U., Benveniste M., Levitan E.S., Lotan I.
    J. Neurosci. 27:1651-1658(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH KCNB1, SUBCELLULAR LOCATION.
  • Ref.15

    "Direct interaction of endogenous Kv channels with syntaxin enhances exocytosis by neuroendocrine cells."
    Singer-Lahat D., Chikvashvili D., Lotan I.
    PLoS ONE 3:E1381-E1381(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH KCNB1, SUBCELLULAR LOCATION.
  • "The Kv2.1 channels mediate neuronal apoptosis induced by excitotoxicity."
    Yao H., Zhou K., Yan D., Li M., Wang Y.
    J. Neurochem. 108:909-919(2009) [PubMed] [Europe PMC] [Abstract]
  • Ref.17

    "Non-conducting function of the Kv2.1 channel enables it to recruit vesicles for release in neuroendocrine and nerve cells."
    Feinshreiber L., Singer-Lahat D., Friedrich R., Matti U., Sheinin A., Yizhar O., Nachman R., Chikvashvili D., Rettig J., Ashery U., Lotan I.
    J. Cell Sci. 123:1940-1947(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH KCNB1, SUBCELLULAR LOCATION.
• kinase binding Source: RGDInferred from sequence orthologyⁱ
  • Ref.11

    "Ca2+-dependent phosphorylation of syntaxin-1A by the death-associated protein (DAP) kinase regulates its interaction with Munc18."
    Tian J.H., Das S., Sheng Z.H.
    J. Biol. Chem. 278:26265-26274(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: PHOSPHORYLATION AT SER-188, INTERACTION WITH STXBP1.
• myosin binding Source: RGDInferred from physical interactionⁱ
  • "Myosin-Va regulates exocytosis through the submicromolar Ca2+-dependent binding of syntaxin-1A."
    Watanabe M., Nomura K., Ohyama A., Ishikawa R., Komiya Y., Hosaka K., Yamauchi E., Taniguchi H., Sasakawa N., Kumakura K., Ushiki T., Sato O., Ikebe M., Igarashi M.
    Mol. Biol. Cell 16:4519-4530(2005) [PubMed] [Europe PMC] [Abstract]
• myosin head/neck binding Source: RGDInferred from physical interactionⁱ
  • "Myosin-Va regulates exocytosis through the submicromolar Ca2+-dependent binding of syntaxin-1A."
    Watanabe M., Nomura K., Ohyama A., Ishikawa R., Komiya Y., Hosaka K., Yamauchi E., Taniguchi H., Sasakawa N., Kumakura K., Ushiki T., Sato O., Ikebe M., Igarashi M.
    Mol. Biol. Cell 16:4519-4530(2005) [PubMed] [Europe PMC] [Abstract]
• protein-containing complex binding Source: RGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Myosin-Va regulates exocytosis through the submicromolar Ca2+-dependent binding of syntaxin-1A."
    Watanabe M., Nomura K., Ohyama A., Ishikawa R., Komiya Y., Hosaka K., Yamauchi E., Taniguchi H., Sasakawa N., Kumakura K., Ushiki T., Sato O., Ikebe M., Igarashi M.
    Mol. Biol. Cell 16:4519-4530(2005) [PubMed] [Europe PMC] [Abstract]
• protein domain specific binding Source: RGDInferred from physical interactionⁱ
  • "Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin."
    Betz A., Okamoto M., Benseler F., Brose N.
    J. Biol. Chem. 272:2520-2526(1997) [PubMed] [Europe PMC] [Abstract]
• protein-macromolecule adaptor activity Source: RGDInferred from physical interactionⁱ
  • "Myosin-Va regulates exocytosis through the submicromolar Ca2+-dependent binding of syntaxin-1A."
    Watanabe M., Nomura K., Ohyama A., Ishikawa R., Komiya Y., Hosaka K., Yamauchi E., Taniguchi H., Sasakawa N., Kumakura K., Ushiki T., Sato O., Ikebe M., Igarashi M.
    Mol. Biol. Cell 16:4519-4530(2005) [PubMed] [Europe PMC] [Abstract]
• protein N-terminus binding Source: RGDInferred from direct assayⁱ
  • "Munc18-1 binding to the neuronal SNARE complex controls synaptic vesicle priming."
    Deak F., Xu Y., Chang W.P., Dulubova I., Khvotchev M., Liu X., Sudhof T.C., Rizo J.
    J. Cell Biol. 184:751-764(2009) [PubMed] [Europe PMC] [Abstract]
• SNAP receptor activity Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• SNARE binding Source: MGIInferred from direct assayⁱ
  • "Complexins: cytosolic proteins that regulate SNAP receptor function."
    McMahon H.T., Missler M., Li C., Suedhof T.C.
    Cell 83:111-119(1995) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• calcium-ion regulated exocytosis Source: RGDInferred from sequence orthologyⁱ
  • "Syntaxin 1 interacts with the L(D) subtype of voltage-gated Ca(2+) channels in pancreatic beta cells."
    Yang S.N., Larsson O., Branstrom R., Bertorello A.M., Leibiger B., Leibiger I.B., Moede T., Kohler M., Meister B., Berggren P.O.
    Proc. Natl. Acad. Sci. U.S.A. 96:10164-10169(1999) [PubMed] [Europe PMC] [Abstract]
• exocytosis Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• hormone secretion Source: RGDInferred from sequence orthologyⁱ
  • "The SNARE protein syntaxin-1a Plays an essential role in biphasic exocytosis of the incretin hormone glucagon-like peptide 1."
    Wheeler S.E., Stacey H.M., Nahaei Y., Hale S.J., Hardy A.B., Reimann F., Gribble F.M., Larraufie P., Gaisano H.Y., Brubaker P.L.
    Diabetes 66:2327-2338(2017) [PubMed] [Europe PMC] [Abstract]
• insulin secretion Source: RGDInferred from sequence orthologyⁱ
  • "Imaging analysis reveals mechanistic differences between first- and second-phase insulin exocytosis."
    Ohara-Imaizumi M., Fujiwara T., Nakamichi Y., Okamura T., Akimoto Y., Kawai J., Matsushima S., Kawakami H., Watanabe T., Akagawa K., Nagamatsu S.
    J. Cell Biol. 177:695-705(2007) [PubMed] [Europe PMC] [Abstract]
• intracellular protein transport Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• modulation of excitatory postsynaptic potential Source: ParkinsonsUK-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Conformational switch of syntaxin-1 controls synaptic vesicle fusion."
    Gerber S.H., Rah J.C., Min S.W., Liu X., de Wit H., Dulubova I., Meyer A.C., Rizo J., Arancillo M., Hammer R.E., Verhage M., Rosenmund C., Sudhof T.C.
    Science 321:1507-1510(2008) [PubMed] [Europe PMC] [Abstract]
• neurotransmitter transport Source: RGD <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • "Identification of syntaxin-1A sites of phosphorylation by casein kinase I and casein kinase II."
    Dubois T., Kerai P., Learmonth M., Cronshaw A., Aitken A.
    Eur. J. Biochem. 269:909-914(2002) [PubMed] [Europe PMC] [Abstract]
• positive regulation of calcium ion-dependent exocytosis Source: UniProtKBInferred from direct assayⁱ
  • Ref.14

    "K+ channel facilitation of exocytosis by dynamic interaction with syntaxin."
    Singer-Lahat D., Sheinin A., Chikvashvili D., Tsuk S., Greitzer D., Friedrich R., Feinshreiber L., Ashery U., Benveniste M., Levitan E.S., Lotan I.
    J. Neurosci. 27:1651-1658(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH KCNB1, SUBCELLULAR LOCATION.
  • Ref.15

    "Direct interaction of endogenous Kv channels with syntaxin enhances exocytosis by neuroendocrine cells."
    Singer-Lahat D., Chikvashvili D., Lotan I.
    PLoS ONE 3:E1381-E1381(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH KCNB1, SUBCELLULAR LOCATION.
  • Ref.17

    "Non-conducting function of the Kv2.1 channel enables it to recruit vesicles for release in neuroendocrine and nerve cells."
    Feinshreiber L., Singer-Lahat D., Friedrich R., Matti U., Sheinin A., Yizhar O., Nachman R., Chikvashvili D., Rettig J., Ashery U., Lotan I.
    J. Cell Sci. 123:1940-1947(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH KCNB1, SUBCELLULAR LOCATION.
• positive regulation of catecholamine secretion Source: UniProtKBInferred from direct assayⁱ
  • Ref.17

    "Non-conducting function of the Kv2.1 channel enables it to recruit vesicles for release in neuroendocrine and nerve cells."
    Feinshreiber L., Singer-Lahat D., Friedrich R., Matti U., Sheinin A., Yizhar O., Nachman R., Chikvashvili D., Rettig J., Ashery U., Lotan I.
    J. Cell Sci. 123:1940-1947(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH KCNB1, SUBCELLULAR LOCATION.
• positive regulation of excitatory postsynaptic potential Source: RGDInferred from sequence orthologyⁱ
  • "Titration of Syntaxin1 in mammalian synapses reveals multiple roles in vesicle docking, priming, and release probability."
    Arancillo M., Min S.W., Gerber S., Munster-Wandowski A., Wu Y.J., Herman M., Trimbuch T., Rah J.C., Ahnert-Hilger G., Riedel D., Sudhof T.C., Rosenmund C.
    J. Neurosci. 33:16698-16714(2013) [PubMed] [Europe PMC] [Abstract]
• positive regulation of exocytosis Source: RGDInferred from direct assayⁱ
  • "SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis."
    Lang T., Bruns D., Wenzel D., Riedel D., Holroyd P., Thiele C., Jahn R.
    EMBO J. 20:2202-2213(2001) [PubMed] [Europe PMC] [Abstract]
• positive regulation of neurotransmitter secretion Source: RGDInferred from mutant phenotypeⁱ
  • "Reduction of neurotransmitter release by the exogenous H3 domain peptide of HPC-1/syntaxin 1A in cultured rat hippocampal neurons."
    Mishima T., Fujiwara T., Akagawa K.
    Neurosci. Lett. 329:273-276(2002) [PubMed] [Europe PMC] [Abstract]
• positive regulation of norepinephrine secretion Source: UniProtKBInferred from direct assayⁱ
  • Ref.15

    "Direct interaction of endogenous Kv channels with syntaxin enhances exocytosis by neuroendocrine cells."
    Singer-Lahat D., Chikvashvili D., Lotan I.
    PLoS ONE 3:E1381-E1381(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH KCNB1, SUBCELLULAR LOCATION.
• protein localization to membrane Source: ParkinsonsUK-UCLInferred from direct assayⁱ
  • "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."
    Perez-Branguli F., Muhaisen A., Blasi J.
    Mol. Cell. Neurosci. 20:169-180(2002) [PubMed] [Europe PMC] [Abstract]
• protein sumoylation Source: RGDInferred from sequence orthologyⁱ
  • "SUMOylation of Syntaxin1A regulates presynaptic endocytosis."
    Craig T.J., Anderson D., Evans A.J., Girach F., Henley J.M.
    Sci. Rep. 5:17669-17669(2015) [PubMed] [Europe PMC] [Abstract]
• regulated exocytosis Source: RGDInferred from sequence orthologyⁱ
  • "Imaging analysis reveals mechanistic differences between first- and second-phase insulin exocytosis."
    Ohara-Imaizumi M., Fujiwara T., Nakamichi Y., Okamura T., Akimoto Y., Kawai J., Matsushima S., Kawakami H., Watanabe T., Akagawa K., Nagamatsu S.
    J. Cell Biol. 177:695-705(2007) [PubMed] [Europe PMC] [Abstract]
• regulation of exocytosis Source: RGDInferred from mutant phenotypeⁱ
  • "Myosin-Va regulates exocytosis through the submicromolar Ca2+-dependent binding of syntaxin-1A."
    Watanabe M., Nomura K., Ohyama A., Ishikawa R., Komiya Y., Hosaka K., Yamauchi E., Taniguchi H., Sasakawa N., Kumakura K., Ushiki T., Sato O., Ikebe M., Igarashi M.
    Mol. Biol. Cell 16:4519-4530(2005) [PubMed] [Europe PMC] [Abstract]
• regulation of synaptic vesicle priming Source: RGDInferred from sequence orthologyⁱ
  • "Titration of Syntaxin1 in mammalian synapses reveals multiple roles in vesicle docking, priming, and release probability."
    Arancillo M., Min S.W., Gerber S., Munster-Wandowski A., Wu Y.J., Herman M., Trimbuch T., Rah J.C., Ahnert-Hilger G., Riedel D., Sudhof T.C., Rosenmund C.
    J. Neurosci. 33:16698-16714(2013) [PubMed] [Europe PMC] [Abstract]
• response to gravity Source: RGDInferred from direct assayⁱ
  • "The effect of hypergravity on the inner ear: CREB and syntaxin are up-regulated."
    Iijima N., Suzuki N., Oguchi T., Hashimoto S., Takumi Y., Sugahara K., Okuda T., Yamashita H., Usami S.
    Neuroreport 15:965-969(2004) [PubMed] [Europe PMC] [Abstract]
• secretion by cell Source: RGDInferred from sequence orthologyⁱ
  • "Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion."
    Polgar J., Chung S.H., Reed G.L.
    Blood 100:1081-1083(2002) [PubMed] [Europe PMC] [Abstract]
• SNARE complex assembly Source: CAFAInferred from mutant phenotypeⁱ
  • "The Habc domain and the SNARE core complex are connected by a highly flexible linker."
    Margittai M., Fasshauer D., Jahn R., Langen R.
    Biochemistry 42:4009-4014(2003) [PubMed] [Europe PMC] [Abstract]
  • "Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly."
    Fasshauer D., Eliason W.K., Brunger A.T., Jahn R.
    Biochemistry 37:10354-10362(1998) [PubMed] [Europe PMC] [Abstract]
• synaptic vesicle docking Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ
  • Ref.3

    "Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones."
    Bennett M.K., Calakos N., Scheller R.H.
    Science 257:255-259(1992) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-288, PROTEIN SEQUENCE OF 4-16 AND 31-56.
• synaptic vesicle endocytosis Source: RGDInferred from sequence orthologyⁱ
  • "SUMOylation of Syntaxin1A regulates presynaptic endocytosis."
    Craig T.J., Anderson D., Evans A.J., Girach F., Henley J.M.
    Sci. Rep. 5:17669-17669(2015) [PubMed] [Europe PMC] [Abstract]
• synaptic vesicle exocytosis Source: SynGOInferred from direct assayⁱ
  • Ref.5

    "Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin."
    Blasi J., Chapman E.R., Yamasaki S., Binz T., Niemann H., Jahn R.
    EMBO J. 12:4821-4828(1993) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM NEUROTOXIN TYPE C.
• synaptic vesicle fusion to presynaptic active zone membrane Source: SynGO <p>Inferred from Genetic Interaction</p> <p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "Conformational switch of syntaxin-1 controls synaptic vesicle fusion."
    Gerber S.H., Rah J.C., Min S.W., Liu X., de Wit H., Dulubova I., Meyer A.C., Rizo J., Arancillo M., Hammer R.E., Verhage M., Rosenmund C., Sudhof T.C.
    Science 321:1507-1510(2008) [PubMed] [Europe PMC] [Abstract]
• vesicle docking Source: RGDInferred from sequence orthologyⁱ
  • "Imaging analysis reveals mechanistic differences between first- and second-phase insulin exocytosis."
    Ohara-Imaizumi M., Fujiwara T., Nakamichi Y., Okamura T., Akimoto Y., Kawai J., Matsushima S., Kawakami H., Watanabe T., Akagawa K., Nagamatsu S.
    J. Cell Biol. 177:695-705(2007) [PubMed] [Europe PMC] [Abstract]
• vesicle fusion Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Topology

Keywords - Cellular componentⁱ

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• ATP-dependent protein binding Source: RGDInferred from physical interactionⁱ
  • "Myosin-Va regulates exocytosis through the submicromolar Ca2+-dependent binding of syntaxin-1A."
    Watanabe M., Nomura K., Ohyama A., Ishikawa R., Komiya Y., Hosaka K., Yamauchi E., Taniguchi H., Sasakawa N., Kumakura K., Ushiki T., Sato O., Ikebe M., Igarashi M.
    Mol. Biol. Cell 16:4519-4530(2005) [PubMed] [Europe PMC] [Abstract]
• calcium-dependent protein binding Source: RGDInferred from physical interactionⁱ
  • "Myosin-Va regulates exocytosis through the submicromolar Ca2+-dependent binding of syntaxin-1A."
    Watanabe M., Nomura K., Ohyama A., Ishikawa R., Komiya Y., Hosaka K., Yamauchi E., Taniguchi H., Sasakawa N., Kumakura K., Ushiki T., Sato O., Ikebe M., Igarashi M.
    Mol. Biol. Cell 16:4519-4530(2005) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: RGDInferred from sequence orthologyⁱ
  • "Protein interaction network of alternatively spliced isoforms from brain links genetic risk factors for autism."
    Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M., Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J.

    , Vacic V., Calderwood M.A., Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D., Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.
    Nat. Commun. 5:3650-3650(2014) [PubMed] [Europe PMC] [Abstract]
• ion channel binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.14

    "K+ channel facilitation of exocytosis by dynamic interaction with syntaxin."
    Singer-Lahat D., Sheinin A., Chikvashvili D., Tsuk S., Greitzer D., Friedrich R., Feinshreiber L., Ashery U., Benveniste M., Levitan E.S., Lotan I.
    J. Neurosci. 27:1651-1658(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH KCNB1, SUBCELLULAR LOCATION.
  • Ref.15

    "Direct interaction of endogenous Kv channels with syntaxin enhances exocytosis by neuroendocrine cells."
    Singer-Lahat D., Chikvashvili D., Lotan I.
    PLoS ONE 3:E1381-E1381(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH KCNB1, SUBCELLULAR LOCATION.
  • "The Kv2.1 channels mediate neuronal apoptosis induced by excitotoxicity."
    Yao H., Zhou K., Yan D., Li M., Wang Y.
    J. Neurochem. 108:909-919(2009) [PubMed] [Europe PMC] [Abstract]
  • Ref.17

    "Non-conducting function of the Kv2.1 channel enables it to recruit vesicles for release in neuroendocrine and nerve cells."
    Feinshreiber L., Singer-Lahat D., Friedrich R., Matti U., Sheinin A., Yizhar O., Nachman R., Chikvashvili D., Rettig J., Ashery U., Lotan I.
    J. Cell Sci. 123:1940-1947(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH KCNB1, SUBCELLULAR LOCATION.
• kinase binding Source: RGDInferred from sequence orthologyⁱ
  • Ref.11

    "Ca2+-dependent phosphorylation of syntaxin-1A by the death-associated protein (DAP) kinase regulates its interaction with Munc18."
    Tian J.H., Das S., Sheng Z.H.
    J. Biol. Chem. 278:26265-26274(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: PHOSPHORYLATION AT SER-188, INTERACTION WITH STXBP1.
• myosin binding Source: RGDInferred from physical interactionⁱ
  • "Myosin-Va regulates exocytosis through the submicromolar Ca2+-dependent binding of syntaxin-1A."
    Watanabe M., Nomura K., Ohyama A., Ishikawa R., Komiya Y., Hosaka K., Yamauchi E., Taniguchi H., Sasakawa N., Kumakura K., Ushiki T., Sato O., Ikebe M., Igarashi M.
    Mol. Biol. Cell 16:4519-4530(2005) [PubMed] [Europe PMC] [Abstract]
• myosin head/neck binding Source: RGDInferred from physical interactionⁱ
  • "Myosin-Va regulates exocytosis through the submicromolar Ca2+-dependent binding of syntaxin-1A."
    Watanabe M., Nomura K., Ohyama A., Ishikawa R., Komiya Y., Hosaka K., Yamauchi E., Taniguchi H., Sasakawa N., Kumakura K., Ushiki T., Sato O., Ikebe M., Igarashi M.
    Mol. Biol. Cell 16:4519-4530(2005) [PubMed] [Europe PMC] [Abstract]
• protein domain specific binding Source: RGDInferred from physical interactionⁱ
  • "Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin."
    Betz A., Okamoto M., Benseler F., Brose N.
    J. Biol. Chem. 272:2520-2526(1997) [PubMed] [Europe PMC] [Abstract]
• protein-macromolecule adaptor activity Source: RGDInferred from physical interactionⁱ
  • "Myosin-Va regulates exocytosis through the submicromolar Ca2+-dependent binding of syntaxin-1A."
    Watanabe M., Nomura K., Ohyama A., Ishikawa R., Komiya Y., Hosaka K., Yamauchi E., Taniguchi H., Sasakawa N., Kumakura K., Ushiki T., Sato O., Ikebe M., Igarashi M.
    Mol. Biol. Cell 16:4519-4530(2005) [PubMed] [Europe PMC] [Abstract]
• protein N-terminus binding Source: RGDInferred from direct assayⁱ
  • "Munc18-1 binding to the neuronal SNARE complex controls synaptic vesicle priming."
    Deak F., Xu Y., Chang W.P., Dulubova I., Khvotchev M., Liu X., Sudhof T.C., Rizo J.
    J. Cell Biol. 184:751-764(2009) [PubMed] [Europe PMC] [Abstract]
• SNAP receptor activity Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• SNARE binding Source: MGIInferred from direct assayⁱ
  • "Complexins: cytosolic proteins that regulate SNAP receptor function."
    McMahon H.T., Missler M., Li C., Suedhof T.C.
    Cell 83:111-119(1995) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Coiled coil

Compositional bias

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        10         20         30         40         50
MKDRTQELRT AKDSDDDDDV TVTVDRDRFM DEFFEQVEEI RGFIDKIAEN 
        60         70         80         90        100
VEEVKRKHSA ILASPNPDEK TKEELEELMS DIKKTANKVR SKLKSIEQSI 
       110        120        130        140        150
EQEEGLNRSS ADLRIRKTQH STLSRKFVEV MSEYNATQSD YRERCKGRIQ 
       160        170        180        190        200
RQLEITGRTT TSEELEDMLE SGNPAIFASG IIMDSSISKQ ALSEIETRHS 
       210        220        230        240        250
EIIKLENSIR ELHDMFMDMA MLVESQGEMI DRIEYNVEHA VDYVERAVSD 
       260        270        280 
TKKAVKYQSK ARRKKIMIII CCVILGIIIA STIGGIFG              

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautionⁱ

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. SIMILARITY comments
   Index of protein domains and families