ID STXB1_HUMAN Reviewed; 594 AA. AC P61764; B1AM97; Q28208; Q62759; Q64320; Q68CM6; Q96TG8; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2004, sequence version 1. DT 24-JAN-2024, entry version 180. DE RecName: Full=Syntaxin-binding protein 1; DE AltName: Full=MUNC18-1; DE AltName: Full=N-Sec1; DE AltName: Full=Protein unc-18 homolog 1; DE Short=Unc18-1; DE AltName: Full=Protein unc-18 homolog A; DE Short=Unc-18A; DE AltName: Full=p67; GN Name=STXBP1; Synonyms=UNC18A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Fetal brain; RX PubMed=8824310; DOI=10.1523/jneurosci.16-21-06695.1996; RA Gengyo-Ando K., Kitayama H., Mukaida M., Ikawa Y.; RT "A murine neural-specific homolog corrects cholinergic defects in RT Caenorhabditis elegans unc-18 mutants."; RL J. Neurosci. 16:6695-6702(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RX PubMed=9545644; DOI=10.1006/geno.1997.5202; RA Swanson D.A., Steel J.M., Valle D.; RT "Identification and characterization of the human ortholog of rat STXBP1, a RT protein implicated in vesicle trafficking and neurotransmitter release."; RL Genomics 48:373-376(1998). RN [3] {ECO:0000312|EMBL:CAA73255.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain {ECO:0000312|EMBL:CAA73255.1}; RA Franco B.; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP INTERACTION WITH STX1A. RX PubMed=12730201; DOI=10.1074/jbc.m300492200; RA Tian J.H., Das S., Sheng Z.H.; RT "Ca2+-dependent phosphorylation of syntaxin-1A by the death-associated RT protein (DAP) kinase regulates its interaction with Munc18."; RL J. Biol. Chem. 278:26265-26274(2003). RN [8] RP INTERACTION WITH ALPHA-SYNUCLEIN/SNCA. RX PubMed=27597756; DOI=10.1083/jcb.201512016; RA Chai Y.J., Sierecki E., Tomatis V.M., Gormal R.S., Giles N., Morrow I.C., RA Xia D., Goetz J., Parton R.G., Collins B.M., Gambin Y., Meunier F.A.; RT "Munc18-1 is a molecular chaperone for alpha-synuclein, controlling its RT self-replicating aggregation."; RL J. Cell Biol. 214:705-718(2016). RN [9] RP INVOLVEMENT IN DEE4, VARIANTS DEE4 ASP-84; TYR-180; ARG-443 AND ASP-544, RP AND CHARACTERIZATION OF VARIANTS DEE4 ASP-84; TYR-180; ARG-443 AND ASP-544. RX PubMed=18469812; DOI=10.1038/ng.150; RA Saitsu H., Kato M., Mizuguchi T., Hamada K., Osaka H., Tohyama J., RA Uruno K., Kumada S., Nishiyama K., Nishimura A., Okada I., Yoshimura Y., RA Hirai S., Kumada T., Hayasaka K., Fukuda A., Ogata K., Matsumoto N.; RT "De novo mutations in the gene encoding STXBP1 (MUNC18-1) cause early RT infantile epileptic encephalopathy."; RL Nat. Genet. 40:782-788(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [13] RP VARIANT DEE4 HIS-406, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF RP VARIANTS ILE-84 AND LEU-431. RX PubMed=20887364; DOI=10.1111/j.1528-1167.2010.02728.x; RA Saitsu H., Kato M., Okada I., Orii K.E., Higuchi T., Hoshino H., Kubota M., RA Arai H., Tagawa T., Kimura S., Sudo A., Miyama S., Takami Y., Watanabe T., RA Nishimura A., Nishiyama K., Miyake N., Wada T., Osaka H., Kondo N., RA Hayasaka K., Matsumoto N.; RT "STXBP1 mutations in early infantile epileptic encephalopathy with RT suppression-burst pattern."; RL Epilepsia 51:2397-2405(2010). RN [14] RP VARIANTS DEE4 ARG-183; LEU-480 AND PRO-574. RX PubMed=21770924; DOI=10.1111/j.1528-1167.2011.03181.x; RA Milh M., Villeneuve N., Chouchane M., Kaminska A., Laroche C., RA Barthez M.A., Gitiaux C., Bartoli C., Borges-Correia A., Cacciagli P., RA Mignon-Ravix C., Cuberos H., Chabrol B., Villard L.; RT "Epileptic and nonepileptic features in patients with early onset epileptic RT encephalopathy and STXBP1 mutations."; RL Epilepsia 52:1828-1834(2011). RN [15] RP INVOLVEMENT IN DEE4. RX PubMed=23662938; DOI=10.1111/epi.12203; RA Kodera H., Kato M., Nord A.S., Walsh T., Lee M., Yamanaka G., Tohyama J., RA Nakamura K., Nakagawa E., Ikeda T., Ben-Zeev B., Lev D., Lerman-Sagie T., RA Straussberg R., Tanabe S., Ueda K., Amamoto M., Ohta S., Nonoda Y., RA Nishiyama K., Tsurusaki Y., Nakashima M., Miyake N., Hayasaka K., RA King M.C., Matsumoto N., Saitsu H.; RT "Targeted capture and sequencing for detection of mutations causing early RT onset epileptic encephalopathy."; RL Epilepsia 54:1262-1269(2013). RN [16] RP VARIANTS DEE4 PHE-42; TRP-190 AND ARG-354, AND VARIANTS PRO-80; CYS-544 AND RP ALA-570. RX PubMed=23708187; DOI=10.1038/ng.2646; RA Carvill G.L., Heavin S.B., Yendle S.C., McMahon J.M., O'Roak B.J., Cook J., RA Khan A., Dorschner M.O., Weaver M., Calvert S., Malone S., Wallace G., RA Stanley T., Bye A.M., Bleasel A., Howell K.B., Kivity S., Mackay M.T., RA Rodriguez-Casero V., Webster R., Korczyn A., Afawi Z., Zelnick N., RA Lerman-Sagie T., Lev D., Moeller R.S., Gill D., Andrade D.M., Freeman J.L., RA Sadleir L.G., Shendure J., Berkovic S.F., Scheffer I.E., Mefford H.C.; RT "Targeted resequencing in epileptic encephalopathies identifies de novo RT mutations in CHD2 and SYNGAP1."; RL Nat. Genet. 45:825-830(2013). RN [17] RP VARIANT DEE4 THR-251. RX PubMed=24170257; DOI=10.1177/0883073813506936; RA Romaniello R., Zucca C., Tenderini E., Arrigoni F., Ragona F., Zorzi G., RA Bassi M.T., Borgatti R.; RT "A novel mutation in STXBP1 gene in a child with epileptic encephalopathy RT and an atypical electroclinical pattern."; RL J. Child Neurol. 29:249-253(2014). RN [18] RP VARIANTS DEE4 LYS-283; TYR-285 AND PRO-445. RX PubMed=24623842; DOI=10.1212/wnl.0000000000000291; RA Carvill G.L., Weckhuysen S., McMahon J.M., Hartmann C., Moller R.S., RA Hjalgrim H., Cook J., Geraghty E., O'Roak B.J., Petrou S., Clarke A., RA Gill D., Sadleir L.G., Muhle H., von Spiczak S., Nikanorova M., RA Hodgson B.L., Gazina E.V., Suls A., Shendure J., Dibbens L.M., RA De Jonghe P., Helbig I., Berkovic S.F., Scheffer I.E., Mefford H.C.; RT "GABRA1 and STXBP1: novel genetic causes of Dravet syndrome."; RL Neurology 82:1245-1253(2014). RN [19] RP VARIANT DEE4 122-ARG--SER-594 DEL. RX PubMed=25818041; DOI=10.1111/epi.12954; RA Mercimek-Mahmutoglu S., Patel J., Cordeiro D., Hewson S., Callen D., RA Donner E.J., Hahn C.D., Kannu P., Kobayashi J., Minassian B.A., Moharir M., RA Siriwardena K., Weiss S.K., Weksberg R., Snead O.C. III; RT "Diagnostic yield of genetic testing in epileptic encephalopathy in RT childhood."; RL Epilepsia 56:707-716(2015). RN [20] RP VARIANT DEE4 HIS-406. RX PubMed=25714420; DOI=10.1097/wnr.0000000000000337; RA Romaniello R., Saettini F., Panzeri E., Arrigoni F., Bassi M.T., RA Borgatti R.; RT "A de-novo STXBP1 gene mutation in a patient showing the Rett syndrome RT phenotype."; RL NeuroReport 26:254-257(2015). RN [21] RP VARIANTS DEE4 PRO-281 AND HIS-292. RX PubMed=26993267; DOI=10.1136/jmedgenet-2015-103263; RA Trump N., McTague A., Brittain H., Papandreou A., Meyer E., Ngoh A., RA Palmer R., Morrogh D., Boustred C., Hurst J.A., Jenkins L., Kurian M.A., RA Scott R.H.; RT "Improving diagnosis and broadening the phenotypes in early-onset seizure RT and severe developmental delay disorders through gene panel analysis."; RL J. Med. Genet. 53:310-317(2016). RN [22] RP VARIANT DEE4 CYS-406. RX PubMed=27864847; DOI=10.1002/humu.23149; RG Clinical Study Group; RA Parrini E., Marini C., Mei D., Galuppi A., Cellini E., Pucatti D., RA Chiti L., Rutigliano D., Bianchini C., Virdo S., De Vita D., Bigoni S., RA Barba C., Mari F., Montomoli M., Pisano T., Rosati A., Guerrini R.; RT "Diagnostic targeted resequencing in 349 patients with drug-resistant RT pediatric epilepsies identifies causative mutations in 30 different RT genes."; RL Hum. Mutat. 38:216-225(2017). CC -!- FUNCTION: Participates in the regulation of synaptic vesicle docking CC and fusion through interaction with GTP-binding proteins (By CC similarity). Essential for neurotransmission and binds syntaxin, a CC component of the synaptic vesicle fusion machinery probably in a 1:1 CC ratio. Can interact with syntaxins 1, 2, and 3 but not syntaxin 4. CC Involved in the release of neurotransmitters from neurons through CC interacting with SNARE complex component STX1A and mediating the CC assembly of the SNARE complex at synaptic membranes (By similarity). CC May play a role in determining the specificity of intracellular fusion CC reactions. {ECO:0000250|UniProtKB:O08599, CC ECO:0000250|UniProtKB:P61765}. CC -!- SUBUNIT: Interacts with SYTL4 (By similarity). Interacts with STX1A CC (PubMed:12730201). The interaction recruits SNARE complex components CC SNAP25 and VAMP2 and mediates neurotransmitter release from neurons (By CC similarity). Interacts with alpha-synuclein/SNCA; this interaction CC controls SNCA self-replicating aggregation (PubMed:27597756). Interacts CC with RAB3A; this interaction promotes RAB3A dissociation from the CC vesicle membrane (By similarity). Interacts with CABP5 (By similarity). CC {ECO:0000250|UniProtKB:O08599, ECO:0000250|UniProtKB:P61763, CC ECO:0000250|UniProtKB:P61765, ECO:0000269|PubMed:12730201, CC ECO:0000269|PubMed:27597756}. CC -!- INTERACTION: CC P61764; P05067: APP; NbExp=7; IntAct=EBI-960169, EBI-77613; CC P61764; Q0VDD7: BRME1; NbExp=3; IntAct=EBI-960169, EBI-741210; CC P61764; Q6IPU0: CENPP; NbExp=3; IntAct=EBI-960169, EBI-10250303; CC P61764; P21917: DRD4; NbExp=3; IntAct=EBI-960169, EBI-8592297; CC P61764; P11142: HSPA8; NbExp=2; IntAct=EBI-960169, EBI-351896; CC P61764; P42858: HTT; NbExp=7; IntAct=EBI-960169, EBI-466029; CC P61764; O14901: KLF11; NbExp=3; IntAct=EBI-960169, EBI-948266; CC P61764; P28482: MAPK1; NbExp=3; IntAct=EBI-960169, EBI-959949; CC P61764; P50222: MEOX2; NbExp=3; IntAct=EBI-960169, EBI-748397; CC P61764; O75376: NCOR1; NbExp=3; IntAct=EBI-960169, EBI-347233; CC P61764; Q8N0Z3: SPICE1; NbExp=3; IntAct=EBI-960169, EBI-2361917; CC P61764; O75558: STX11; NbExp=6; IntAct=EBI-960169, EBI-714135; CC P61764; Q8N4C7: STX19; NbExp=9; IntAct=EBI-960169, EBI-8484990; CC P61764; Q13190: STX5; NbExp=6; IntAct=EBI-960169, EBI-714206; CC P61764; Q96C24: SYTL4; NbExp=3; IntAct=EBI-960169, EBI-747142; CC P61764; O00635: TRIM38; NbExp=9; IntAct=EBI-960169, EBI-2130415; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20887364}. CC Membrane; Peripheral membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=A; CC IsoId=P61764-1, Q64320-1; Sequence=Displayed; CC Name=2; Synonyms=BE, HUNC18b; CC IsoId=P61764-2, Q64320-2; Sequence=VSP_006713; CC -!- TISSUE SPECIFICITY: Brain and spinal cord. Highly enriched in axons. CC -!- DISEASE: Developmental and epileptic encephalopathy 4 (DEE4) CC [MIM:612164]: A severe form of epilepsy characterized by frequent tonic CC seizures or spasms beginning in infancy with a specific EEG finding of CC suppression-burst patterns, characterized by high-voltage bursts CC alternating with almost flat suppression phases. Affected individuals CC have neonatal or infantile onset of seizures, profound intellectual CC disability, and MRI evidence of brain hypomyelination. CC {ECO:0000269|PubMed:18469812, ECO:0000269|PubMed:20887364, CC ECO:0000269|PubMed:21770924, ECO:0000269|PubMed:23662938, CC ECO:0000269|PubMed:23708187, ECO:0000269|PubMed:24170257, CC ECO:0000269|PubMed:24623842, ECO:0000269|PubMed:25714420, CC ECO:0000269|PubMed:25818041, ECO:0000269|PubMed:26993267, CC ECO:0000269|PubMed:27864847}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D63851; BAA19483.1; -; mRNA. DR EMBL; AF004562; AAC39688.1; -; mRNA. DR EMBL; AF004563; AAC39689.1; -; mRNA. DR EMBL; Y12723; CAA73255.1; -; mRNA. DR EMBL; AL162426; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471090; EAW87679.1; -; Genomic_DNA. DR EMBL; CH471090; EAW87681.1; -; Genomic_DNA. DR EMBL; BC015749; AAH15749.1; -; mRNA. DR CCDS; CCDS35146.1; -. DR CCDS; CCDS6874.1; -. [P61764-2] DR RefSeq; NP_001027392.1; NM_001032221.3. [P61764-1] DR RefSeq; NP_003156.1; NM_003165.3. [P61764-2] DR PDB; 6L03; X-ray; 2.08 A; F=141-149. DR PDBsum; 6L03; -. DR AlphaFoldDB; P61764; -. DR SMR; P61764; -. DR BioGRID; 112681; 119. DR IntAct; P61764; 80. DR MINT; P61764; -. DR STRING; 9606.ENSP00000362399; -. DR TCDB; 1.F.1.1.3; the synaptosomal vesicle fusion pore (svf-pore) family. DR GlyGen; P61764; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P61764; -. DR MetOSite; P61764; -. DR PhosphoSitePlus; P61764; -. DR SwissPalm; P61764; -. DR BioMuta; STXBP1; -. DR DMDM; 50403646; -. DR EPD; P61764; -. DR jPOST; P61764; -. DR MassIVE; P61764; -. DR MaxQB; P61764; -. DR PaxDb; 9606-ENSP00000362399; -. DR PeptideAtlas; P61764; -. DR ProteomicsDB; 57331; -. DR ProteomicsDB; 57332; -. [P61764-2] DR Pumba; P61764; -. DR Antibodypedia; 2191; 568 antibodies from 41 providers. DR DNASU; 6812; -. DR Ensembl; ENST00000373299.5; ENSP00000362396.2; ENSG00000136854.25. [P61764-1] DR Ensembl; ENST00000373302.8; ENSP00000362399.3; ENSG00000136854.25. [P61764-2] DR GeneID; 6812; -. DR KEGG; hsa:6812; -. DR MANE-Select; ENST00000373299.5; ENSP00000362396.2; NM_001032221.6; NP_001027392.1. DR UCSC; uc004brk.2; human. DR UCSC; uc004brl.3; human. DR AGR; HGNC:11444; -. DR CTD; 6812; -. DR DisGeNET; 6812; -. DR GeneCards; STXBP1; -. DR GeneReviews; STXBP1; -. DR HGNC; HGNC:11444; STXBP1. DR HPA; ENSG00000136854; Tissue enhanced (brain, retina). DR MalaCards; STXBP1; -. DR MIM; 602926; gene. DR MIM; 612164; phenotype. DR neXtProt; NX_P61764; -. DR OpenTargets; ENSG00000136854; -. DR Orphanet; 495818; 9q33.3q34.11 microdeletion syndrome. DR Orphanet; 599373; STXBP1-related encephalopathy. DR PharmGKB; PA36241; -. DR VEuPathDB; HostDB:ENSG00000136854; -. DR eggNOG; KOG1300; Eukaryota. DR GeneTree; ENSGT00940000155127; -. DR HOGENOM; CLU_009210_2_0_1; -. DR InParanoid; P61764; -. DR OMA; PFTRPHT; -. DR OrthoDB; 4609640at2759; -. DR PhylomeDB; P61764; -. DR TreeFam; TF313242; -. DR PathwayCommons; P61764; -. DR Reactome; R-HSA-181429; Serotonin Neurotransmitter Release Cycle. [P61764-1] DR Reactome; R-HSA-181430; Norepinephrine Neurotransmitter Release Cycle. [P61764-1] DR Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle. [P61764-1] DR Reactome; R-HSA-212676; Dopamine Neurotransmitter Release Cycle. [P61764-1] DR Reactome; R-HSA-264642; Acetylcholine Neurotransmitter Release Cycle. [P61764-1] DR Reactome; R-HSA-422356; Regulation of insulin secretion. DR Reactome; R-HSA-6794361; Neurexins and neuroligins. DR Reactome; R-HSA-888590; GABA synthesis, release, reuptake and degradation. [P61764-1] DR SignaLink; P61764; -. DR SIGNOR; P61764; -. DR BioGRID-ORCS; 6812; 49 hits in 1155 CRISPR screens. DR ChiTaRS; STXBP1; human. DR GeneWiki; STXBP1; -. DR GenomeRNAi; 6812; -. DR Pharos; P61764; Tbio. DR PRO; PR:P61764; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P61764; Protein. DR Bgee; ENSG00000136854; Expressed in middle temporal gyrus and 196 other cell types or tissues. DR ExpressionAtlas; P61764; baseline and differential. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0098888; C:extrinsic component of presynaptic membrane; IEA:Ensembl. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IEA:Ensembl. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0031091; C:platelet alpha granule; IDA:UniProtKB. DR GO; GO:0098794; C:postsynapse; IEA:Ensembl. DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IEA:Ensembl. DR GO; GO:0048787; C:presynaptic active zone membrane; IEA:Ensembl. DR GO; GO:0099523; C:presynaptic cytosol; IEA:Ensembl. DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB. DR GO; GO:0030141; C:secretory granule; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB. DR GO; GO:0043274; F:phospholipase binding; IEA:Ensembl. DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl. DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0000149; F:SNARE binding; ISS:UniProtKB. DR GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB. DR GO; GO:0017075; F:syntaxin-1 binding; IPI:UniProtKB. DR GO; GO:0007412; P:axon target recognition; ISS:UniProtKB. DR GO; GO:0071346; P:cellular response to type II interferon; IEA:Ensembl. DR GO; GO:0003006; P:developmental process involved in reproduction; IEA:Ensembl. DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central. DR GO; GO:0060292; P:long-term synaptic depression; IEA:Ensembl. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl. DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IEA:Ensembl. DR GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; ISS:UniProtKB. DR GO; GO:0007274; P:neuromuscular synaptic transmission; IEA:Ensembl. DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl. DR GO; GO:0007269; P:neurotransmitter secretion; IBA:GO_Central. DR GO; GO:0070527; P:platelet aggregation; IMP:UniProtKB. DR GO; GO:0002576; P:platelet degranulation; IMP:UniProtKB. DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IEA:Ensembl. DR GO; GO:1903296; P:positive regulation of glutamate secretion, neurotransmission; IEA:Ensembl. DR GO; GO:0043306; P:positive regulation of mast cell degranulation; IEA:Ensembl. DR GO; GO:0106022; P:positive regulation of vesicle docking; IEA:Ensembl. DR GO; GO:0099525; P:presynaptic dense core vesicle exocytosis; IEA:Ensembl. DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB. DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl. DR GO; GO:2000367; P:regulation of acrosomal vesicle exocytosis; IMP:UniProtKB. DR GO; GO:0035542; P:regulation of SNARE complex assembly; TAS:ParkinsonsUK-UCL. DR GO; GO:0031630; P:regulation of synaptic vesicle fusion to presynaptic active zone membrane; TAS:ParkinsonsUK-UCL. DR GO; GO:0010807; P:regulation of synaptic vesicle priming; ISS:UniProtKB. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0035493; P:SNARE complex assembly; IMP:UniProtKB. DR GO; GO:0016188; P:synaptic vesicle maturation; ISS:UniProtKB. DR GO; GO:0016082; P:synaptic vesicle priming; IEA:Ensembl. DR GO; GO:0006904; P:vesicle docking involved in exocytosis; ISS:ParkinsonsUK-UCL. DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central. DR Gene3D; 1.25.40.60; -; 1. DR Gene3D; 3.40.50.1910; -; 1. DR Gene3D; 3.40.50.2060; -; 1. DR InterPro; IPR043154; Sec-1-like_dom1. DR InterPro; IPR043127; Sec-1-like_dom3a. DR InterPro; IPR001619; Sec1-like. DR InterPro; IPR027482; Sec1-like_dom2. DR InterPro; IPR036045; Sec1-like_sf. DR PANTHER; PTHR11679:SF35; SYNTAXIN-BINDING PROTEIN 1; 1. DR PANTHER; PTHR11679; VESICLE PROTEIN SORTING-ASSOCIATED; 1. DR Pfam; PF00995; Sec1; 1. DR PIRSF; PIRSF005715; VPS45_Sec1; 1. DR SUPFAM; SSF56815; Sec1/munc18-like (SM) proteins; 1. DR Genevisible; P61764; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant; Epilepsy; KW Intellectual disability; Membrane; Phosphoprotein; Protein transport; KW Reference proteome; Transport. FT CHAIN 1..594 FT /note="Syntaxin-binding protein 1" FT /id="PRO_0000206277" FT MOD_RES 476 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P61765" FT MOD_RES 509 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O08599" FT MOD_RES 511 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O08599" FT MOD_RES 516 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O08599" FT MOD_RES 593 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P61765" FT VAR_SEQ 576..594 FT /note="QKLLDTLKKLNKTDEEISS -> TKFLMDLRHPDFRESSRVSFEDQAPTME FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9545644" FT /id="VSP_006713" FT VARIANT 42 FT /note="S -> F (in DEE4)" FT /evidence="ECO:0000269|PubMed:23708187" FT /id="VAR_078631" FT VARIANT 80 FT /note="S -> P (found in a patient with epileptic FT encephalopathy; likely pathogenic; dbSNP:rs1840867221)" FT /evidence="ECO:0000269|PubMed:23708187" FT /id="VAR_078632" FT VARIANT 84 FT /note="V -> D (in DEE4; may alter protein structure; FT dbSNP:rs121918320)" FT /evidence="ECO:0000269|PubMed:18469812" FT /id="VAR_046205" FT VARIANT 84 FT /note="V -> I (no effect on subcellular location; FT dbSNP:rs34830702)" FT /evidence="ECO:0000269|PubMed:20887364" FT /id="VAR_073148" FT VARIANT 122..594 FT /note="Missing (in DEE4)" FT /evidence="ECO:0000269|PubMed:25818041" FT /id="VAR_078757" FT VARIANT 180 FT /note="C -> Y (in DEE4; reduced thermostability; decreased FT binding to STX1A; dbSNP:rs121918318)" FT /evidence="ECO:0000269|PubMed:18469812" FT /id="VAR_046206" FT VARIANT 183 FT /note="L -> R (in DEE4)" FT /evidence="ECO:0000269|PubMed:21770924" FT /id="VAR_073149" FT VARIANT 190 FT /note="R -> W (in DEE4; dbSNP:rs796053355)" FT /evidence="ECO:0000269|PubMed:23708187" FT /id="VAR_078633" FT VARIANT 251 FT /note="A -> T (in DEE4)" FT /evidence="ECO:0000269|PubMed:24170257" FT /id="VAR_073150" FT VARIANT 281 FT /note="L -> P (in DEE4)" FT /evidence="ECO:0000269|PubMed:26993267" FT /id="VAR_078758" FT VARIANT 283 FT /note="E -> K (in DEE4; dbSNP:rs587777310)" FT /evidence="ECO:0000269|PubMed:24623842" FT /id="VAR_071814" FT VARIANT 285 FT /note="D -> Y (in DEE4)" FT /evidence="ECO:0000269|PubMed:24623842" FT /id="VAR_071815" FT VARIANT 292 FT /note="R -> H (in DEE4; dbSNP:rs796053361)" FT /evidence="ECO:0000269|PubMed:26993267" FT /id="VAR_078759" FT VARIANT 354 FT /note="C -> R (in DEE4; dbSNP:rs886041337)" FT /evidence="ECO:0000269|PubMed:23708187" FT /id="VAR_078634" FT VARIANT 406 FT /note="R -> C (in DEE4; dbSNP:rs796053367)" FT /evidence="ECO:0000269|PubMed:27864847" FT /id="VAR_078218" FT VARIANT 406 FT /note="R -> H (in DEE4; dbSNP:rs886041246)" FT /evidence="ECO:0000269|PubMed:20887364, FT ECO:0000269|PubMed:25714420" FT /id="VAR_073151" FT VARIANT 431 FT /note="Q -> L (expressed at low levels compared with FT wild-type; no effect on subcellular location)" FT /evidence="ECO:0000269|PubMed:20887364" FT /id="VAR_073152" FT VARIANT 443 FT /note="M -> R (in DEE4; may alter protein structure; FT dbSNP:rs121918319)" FT /evidence="ECO:0000269|PubMed:18469812" FT /id="VAR_046207" FT VARIANT 445 FT /note="H -> P (in DEE4)" FT /evidence="ECO:0000269|PubMed:24623842" FT /id="VAR_071816" FT VARIANT 480 FT /note="P -> L (in DEE4; dbSNP:rs796053368)" FT /evidence="ECO:0000269|PubMed:21770924" FT /id="VAR_073153" FT VARIANT 544 FT /note="G -> C (found in a patient with Lennox-Gastaut FT syndrome; uncertain significance; dbSNP:rs1842044505)" FT /evidence="ECO:0000269|PubMed:23708187" FT /id="VAR_078635" FT VARIANT 544 FT /note="G -> D (in DEE4; may alter protein structure; FT dbSNP:rs121918317)" FT /evidence="ECO:0000269|PubMed:18469812" FT /id="VAR_046208" FT VARIANT 570 FT /note="T -> A (found in a patient with epileptic FT encephalopathy; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:23708187" FT /id="VAR_078636" FT VARIANT 574 FT /note="T -> P (in DEE4)" FT /evidence="ECO:0000269|PubMed:21770924" FT /id="VAR_073154" SQ SEQUENCE 594 AA; 67569 MW; 2DD0715F875CE0F3 CRC64; MAPIGLKAVV GEKIMHDVIK KVKKKGEWKV LVVDQLSMRM LSSCCKMTDI MTEGITIVED INKRREPLPS LEAVYLITPS EKSVHSLISD FKDPPTAKYR AAHVFFTDSC PDALFNELVK SRAAKVIKTL TEINIAFLPY ESQVYSLDSA DSFQSFYSPH KAQMKNPILE RLAEQIATLC ATLKEYPAVR YRGEYKDNAL LAQLIQDKLD AYKADDPTMG EGPDKARSQL LILDRGFDPS SPVLHELTFQ AMSYDLLPIE NDVYKYETSG IGEARVKEVL LDEDDDLWIA LRHKHIAEVS QEVTRSLKDF SSSKRMNTGE KTTMRDLSQM LKKMPQYQKE LSKYSTHLHL AEDCMKHYQG TVDKLCRVEQ DLAMGTDAEG EKIKDPMRAI VPILLDANVS TYDKIRIILL YIFLKNGITE ENLNKLIQHA QIPPEDSEII TNMAHLGVPI VTDSTLRRRS KPERKERISE QTYQLSRWTP IIKDIMEDTI EDKLDTKHYP YISTRSSASF STTAVSARYG HWHKNKAPGE YRSGPRLIIF ILGGVSLNEM RCAYEVTQAN GKWEVLIGST HILTPQKLLD TLKKLNKTDE EISS //