ID STX1B_HUMAN Reviewed; 288 AA. AC P61266; Q15531; Q2VPS2; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2004, sequence version 1. DT 27-MAR-2024, entry version 159. DE RecName: Full=Syntaxin-1B; DE AltName: Full=Syntaxin-1B1; DE AltName: Full=Syntaxin-1B2; GN Name=STX1B; Synonyms=STX1B1, STX1B2; 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 2), AND SUBCELLULAR LOCATION (ISOFORM RP 2). RX PubMed=18691641; DOI=10.1016/j.gene.2008.07.010; RA Pereira S., Massacrier A., Roll P., Verine A., Etienne-Grimaldi M.C., RA Poitelon Y., Robaglia-Schlupp A., Jamali S., Roeckel-Trevisiol N., RA Royer B., Pontarotti P., Leveque C., Seagar M., Levy N., Cau P., RA Szepetowski P.; RT "Nuclear localization of a novel human syntaxin 1B isoform."; RL Gene 423:160-171(2008). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Fujiwara T., Genda M., Akagawa K.; RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Gastaldi M., Massacrier A., Pereira S., Roll P., Robaglia-Schlupp A., RA Cau P., Szepetowski P.; RT "STX1B2, a new member of the syntaxin gene family."; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Eye; 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [7] RP INVOLVEMENT IN GEFSP9, VARIANTS GEFSP9 GLU-216 AND ARG-226, AND RP CHARACTERIZATION OF VARIANT GEFSP9 GLU-216. RX PubMed=25362483; DOI=10.1038/ng.3130; RG EuroEPINOMICS RES Consortium; RA Schubert J., Siekierska A., Langlois M., May P., Huneau C., Becker F., RA Muhle H., Suls A., Lemke J.R., de Kovel C.G., Thiele H., Konrad K., RA Kawalia A., Toliat M.R., Sander T., Rueschendorf F., Caliebe A., Nagel I., RA Kohl B., Kecskes A., Jacmin M., Hardies K., Weckhuysen S., Riesch E., RA Dorn T., Brilstra E.H., Baulac S., Moeller R.S., Hjalgrim H., RA Koeleman B.P., Jurkat-Rott K., Lehman-Horn F., Roach J.C., Glusman G., RA Hood L., Galas D.J., Martin B., de Witte P.A., Biskup S., De Jonghe P., RA Helbig I., Balling R., Nuernberg P., Crawford A.D., Esguerra C.V., RA Weber Y.G., Lerche H.; RT "Mutations in STX1B, encoding a presynaptic protein, cause fever-associated RT epilepsy syndromes."; RL Nat. Genet. 46:1327-1332(2014). CC -!- FUNCTION: Potentially involved in docking of synaptic vesicles at CC presynaptic active zones. May mediate Ca(2+)-regulation of exocytosis CC acrosomal reaction in sperm (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with OTOF. Interacts with SYT6 and SYT8; the CC interaction is Ca(2+)-dependent (By similarity). {ECO:0000250}. CC -!- INTERACTION: CC P61266; O95870: ABHD16A; NbExp=3; IntAct=EBI-9071709, EBI-348517; CC P61266; Q5T8D3-2: ACBD5; NbExp=3; IntAct=EBI-9071709, EBI-10961679; CC P61266; Q13520: AQP6; NbExp=3; IntAct=EBI-9071709, EBI-13059134; CC P61266; O15155: BET1; NbExp=3; IntAct=EBI-9071709, EBI-749204; CC P61266; Q15125: EBP; NbExp=3; IntAct=EBI-9071709, EBI-3915253; CC P61266; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-9071709, EBI-781551; CC P61266; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-9071709, EBI-7225287; CC P61266; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-9071709, EBI-18304435; CC P61266; Q8TBF8: FAM81A; NbExp=3; IntAct=EBI-9071709, EBI-11993062; CC P61266; Q9NVF7: FBXO28; NbExp=3; IntAct=EBI-9071709, EBI-740282; CC P61266; P02671-2: FGA; NbExp=3; IntAct=EBI-9071709, EBI-9640259; CC P61266; P48165: GJA8; NbExp=3; IntAct=EBI-9071709, EBI-17458373; CC P61266; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-9071709, EBI-13345167; CC P61266; O15554: KCNN4; NbExp=3; IntAct=EBI-9071709, EBI-2924473; CC P61266; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-9071709, EBI-6163737; CC P61266; Q9H115: NAPB; NbExp=5; IntAct=EBI-9071709, EBI-3921185; CC P61266; O95721: SNAP29; NbExp=3; IntAct=EBI-9071709, EBI-490676; CC P61266; Q5SQN1: SNAP47; NbExp=3; IntAct=EBI-9071709, EBI-10244848; CC P61266; P32856-2: STX2; NbExp=3; IntAct=EBI-9071709, EBI-11956649; CC P61266; Q12846: STX4; NbExp=3; IntAct=EBI-9071709, EBI-744942; CC P61266; Q9NRX6: TMEM167B; NbExp=3; IntAct=EBI-9071709, EBI-17684533; CC P61266; P40222: TXLNA; NbExp=3; IntAct=EBI-9071709, EBI-359793; CC P61266; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-9071709, EBI-10180829; CC P61266; P23763-3: VAMP1; NbExp=3; IntAct=EBI-9071709, EBI-12097582; CC P61266; P63027: VAMP2; NbExp=3; IntAct=EBI-9071709, EBI-520113; CC P61266; O95183: VAMP5; NbExp=3; IntAct=EBI-9071709, EBI-10191195; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane {ECO:0000305}; Single-pass CC type IV membrane protein {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus CC {ECO:0000269|PubMed:18691641}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000269|PubMed:18691641}. Cytoplasm, CC cytoskeleton, spindle {ECO:0000269|PubMed:18691641}. Note=Colocalizes CC with Lamin A/C and NuMA in interphasic nuclei, and with NuMA and gamma- CC tubulin in the pericentrosomal region of the mitotic spindle in CC dividing cells. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P61266-1; Sequence=Displayed; CC Name=2; Synonyms=STX1B-DeltaTMD; CC IsoId=P61266-2; Sequence=VSP_047681; CC -!- PTM: Phosphorylated by CK2. {ECO:0000250}. CC -!- DISEASE: Generalized epilepsy with febrile seizures plus 9 (GEFSP9) CC [MIM:616172]: An autosomal dominant neurologic disorder characterized CC by febrile and/or afebrile seizures manifesting in early childhood. CC Seizure are variable and include generalized tonic-clonic, atonic, CC myoclonic, complex partial, and absence types. Most patients have CC remission of seizures later in childhood with no residual neurologic CC deficits. Rarely, patients may show mild developmental delay or mild CC intellectual disabilities. {ECO:0000269|PubMed:25362483}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: [Isoform 2]: The glycine-rich C-terminus serves as an CC unconventional nuclear localization signal. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the syntaxin 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; AY995211; AAY45889.1; -; mRNA. DR EMBL; D37933; BAA07152.1; -; mRNA. DR EMBL; AY028792; AAK27267.1; -; mRNA. DR EMBL; AC135048; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC135050; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC062298; AAH62298.1; -; mRNA. DR CCDS; CCDS10699.1; -. [P61266-1] DR RefSeq; NP_443106.1; NM_052874.4. [P61266-1] DR AlphaFoldDB; P61266; -. DR SMR; P61266; -. DR BioGRID; 125203; 39. DR IntAct; P61266; 37. DR MINT; P61266; -. DR STRING; 9606.ENSP00000215095; -. DR GlyGen; P61266; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P61266; -. DR PhosphoSitePlus; P61266; -. DR SwissPalm; P61266; -. DR BioMuta; STX1B; -. DR DMDM; 47117086; -. DR EPD; P61266; -. DR jPOST; P61266; -. DR MassIVE; P61266; -. DR MaxQB; P61266; -. DR PaxDb; 9606-ENSP00000215095; -. DR PeptideAtlas; P61266; -. DR ProteomicsDB; 57288; -. [P61266-1] DR ProteomicsDB; 61523; -. DR Antibodypedia; 67397; 81 antibodies from 19 providers. DR DNASU; 112755; -. DR Ensembl; ENST00000215095.11; ENSP00000215095.5; ENSG00000099365.11. [P61266-1] DR Ensembl; ENST00000565419.2; ENSP00000455899.1; ENSG00000099365.11. [P61266-2] DR GeneID; 112755; -. DR KEGG; hsa:112755; -. DR MANE-Select; ENST00000215095.11; ENSP00000215095.5; NM_052874.5; NP_443106.1. DR UCSC; uc010cad.3; human. [P61266-1] DR AGR; HGNC:18539; -. DR CTD; 112755; -. DR DisGeNET; 112755; -. DR GeneCards; STX1B; -. DR GeneReviews; STX1B; -. DR HGNC; HGNC:18539; STX1B. DR HPA; ENSG00000099365; Tissue enriched (brain). DR MalaCards; STX1B; -. DR MIM; 601485; gene. DR MIM; 616172; phenotype. DR neXtProt; NX_P61266; -. DR OpenTargets; ENSG00000099365; -. DR Orphanet; 36387; Generalized epilepsy with febrile seizures-plus. DR PharmGKB; PA38345; -. DR VEuPathDB; HostDB:ENSG00000099365; -. DR eggNOG; KOG0810; Eukaryota. DR GeneTree; ENSGT01030000234627; -. DR HOGENOM; CLU_042423_2_2_1; -. DR InParanoid; P61266; -. DR OMA; ANIEQKG; -. DR OrthoDB; 2876074at2759; -. DR PhylomeDB; P61266; -. DR TreeFam; TF313763; -. DR PathwayCommons; P61266; -. DR Reactome; R-HSA-5250971; Toxicity of botulinum toxin type C (botC). DR Reactome; R-HSA-5682910; LGI-ADAM interactions. DR SignaLink; P61266; -. DR BioGRID-ORCS; 112755; 7 hits in 1157 CRISPR screens. DR ChiTaRS; STX1B; human. DR GeneWiki; STX1B; -. DR GenomeRNAi; 112755; -. DR Pharos; P61266; Tbio. DR PRO; PR:P61266; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; P61266; Protein. DR Bgee; ENSG00000099365; Expressed in right hemisphere of cerebellum and 115 other cell types or tissues. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0005813; C:centrosome; IDA:ParkinsonsUK-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central. DR GO; GO:0016020; C:membrane; ISS:ParkinsonsUK-UCL. DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl. DR GO; GO:0005652; C:nuclear lamina; IDA:ParkinsonsUK-UCL. DR GO; GO:0005654; C:nucleoplasm; IDA:ParkinsonsUK-UCL. DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL. DR GO; GO:0005886; C:plasma membrane; ISS:ParkinsonsUK-UCL. DR GO; GO:0098793; C:presynapse; IEA:Ensembl. DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central. DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell. DR GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL. DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl. DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central. DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central. DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IEA:Ensembl. DR GO; GO:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; IBA:GO_Central. DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central. DR GO; GO:1905302; P:negative regulation of macropinocytosis; ISS:ParkinsonsUK-UCL. DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:ParkinsonsUK-UCL. DR GO; GO:1903422; P:negative regulation of synaptic vesicle recycling; IEA:Ensembl. DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:ParkinsonsUK-UCL. DR GO; GO:0001956; P:positive regulation of neurotransmitter secretion; ISS:ParkinsonsUK-UCL. DR GO; GO:1904050; P:positive regulation of spontaneous neurotransmitter secretion; IEA:Ensembl. DR GO; GO:0010468; P:regulation of gene expression; ISS:ParkinsonsUK-UCL. DR GO; GO:0060025; P:regulation of synaptic activity; ISS:ParkinsonsUK-UCL. DR GO; GO:0010807; P:regulation of synaptic vesicle priming; ISS:ParkinsonsUK-UCL. DR GO; GO:0061669; P:spontaneous neurotransmitter secretion; IEA:Ensembl. DR GO; GO:0016081; P:synaptic vesicle docking; ISS:ParkinsonsUK-UCL. DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IEA:Ensembl. DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central. DR GO; GO:0006904; P:vesicle docking involved in exocytosis; ISS:ParkinsonsUK-UCL. DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central. DR CDD; cd15880; SNARE_syntaxin1; 1. DR CDD; cd00179; SynN; 1. DR Gene3D; 1.20.5.110; -; 1. DR Gene3D; 1.20.58.70; -; 1. DR InterPro; IPR010989; SNARE. DR InterPro; IPR045242; Syntaxin. DR InterPro; IPR006012; Syntaxin/epimorphin_CS. DR InterPro; IPR006011; Syntaxin_N. DR InterPro; IPR000727; T_SNARE_dom. DR PANTHER; PTHR19957; SYNTAXIN; 1. DR PANTHER; PTHR19957:SF334; SYNTAXIN-1B; 1. DR Pfam; PF05739; SNARE; 1. DR Pfam; PF00804; Syntaxin; 1. DR SMART; SM00503; SynN; 1. DR SMART; SM00397; t_SNARE; 1. DR SUPFAM; SSF47661; t-snare proteins; 1. DR PROSITE; PS00914; SYNTAXIN; 1. DR PROSITE; PS50192; T_SNARE; 1. DR Genevisible; P61266; HS. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; KW Disease variant; Epilepsy; Membrane; Neurotransmitter transport; Nucleus; KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1..288 FT /note="Syntaxin-1B" FT /id="PRO_0000210192" FT TOPO_DOM 1..264 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 265..288 FT /note="Helical; Anchor for type IV membrane protein" FT /evidence="ECO:0000255" FT DOMAIN 191..253 FT /note="t-SNARE coiled-coil homology" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 29..104 FT /evidence="ECO:0000255" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P61264" FT MOD_RES 14 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT VAR_SEQ 263..288 FT /note="KKIMIIICCVVLGVVLASSIGGTLGL -> VSGAGGLGVGGGAQG (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:18691641" FT /id="VSP_047681" FT VARIANT 216 FT /note="V -> E (in GEFSP9; loss of function mutation; FT dbSNP:rs724159974)" FT /evidence="ECO:0000269|PubMed:25362483" FT /id="VAR_072675" FT VARIANT 226 FT /note="G -> R (in GEFSP9; dbSNP:rs727502806)" FT /evidence="ECO:0000269|PubMed:25362483" FT /id="VAR_072676" FT CONFLICT 7..13 FT /note="ELRSAKD -> VLRTRRN (in Ref. 2; BAA07152)" FT /evidence="ECO:0000305" FT CONFLICT 17 FT /note="E -> K (in Ref. 2; BAA07152)" FT /evidence="ECO:0000305" FT CONFLICT 36 FT /note="V -> E (in Ref. 2; BAA07152)" FT /evidence="ECO:0000305" FT CONFLICT 69 FT /note="K -> R (in Ref. 2; BAA07152)" FT /evidence="ECO:0000305" FT CONFLICT 105..111 FT /note="LNRSSAD -> STAPRPI (in Ref. 2; BAA07152)" FT /evidence="ECO:0000305" FT CONFLICT 174 FT /note="A -> P (in Ref. 2; BAA07152)" FT /evidence="ECO:0000305" FT CONFLICT 266 FT /note="M -> I (in Ref. 2; BAA07152)" FT /evidence="ECO:0000305" FT CONFLICT 284 FT /note="G -> C (in Ref. 2; BAA07152)" FT /evidence="ECO:0000305" SQ SEQUENCE 288 AA; 33245 MW; 2733497E02978BEB CRC64; MKDRTQELRS AKDSDDEEEV VHVDRDHFMD EFFEQVEEIR GCIEKLSEDV EQVKKQHSAI LAAPNPDEKT KQELEDLTAD IKKTANKVRS KLKAIEQSIE QEEGLNRSSA DLRIRKTQHS TLSRKFVEVM TEYNATQSKY RDRCKDRIQR QLEITGRTTT NEELEDMLES GKLAIFTDDI KMDSQMTKQA LNEIETRHNE IIKLETSIRE LHDMFVDMAM LVESQGEMID RIEYNVEHSV DYVERAVSDT KKAVKYQSKA RRKKIMIIIC CVVLGVVLAS SIGGTLGL //