ID SNP23_HUMAN Reviewed; 211 AA. AC O00161; O00162; Q13602; Q6IAE3; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 02-SEP-2026, entry version 233. DE RecName: Full=Synaptosomal-associated protein 23 {ECO:0000305|PubMed:11354632}; DE Short=SNAP-23 {ECO:0000303|PubMed:8663154}; DE AltName: Full=Vesicle-membrane fusion protein SNAP-23 {ECO:0000303|PubMed:9070898}; GN Name=SNAP23 {ECO:0000312|HGNC:HGNC:11131}; 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 SNAP-23A). RC TISSUE=B-cell; RX PubMed=8663154; DOI=10.1074/jbc.271.23.13300; RA Ravichandran V., Chawla A., Roche P.A.; RT "Identification of a novel syntaxin- and synaptobrevin/VAMP-binding RT protein, SNAP-23, expressed in non-neuronal tissues."; RL J. Biol. Chem. 271:13300-13303(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SNAP-23A AND SNAP-23B). RC TISSUE=Neutrophil; RX PubMed=9070898; DOI=10.1006/bbrc.1997.6196; RA Mollinedo F., Lazo P.A.; RT "Identification of two isoforms of the vesicle-membrane fusion protein RT SNAP-23 in human neutrophils and HL-60 cells."; RL Biochem. Biophys. Res. Commun. 231:808-812(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING. RX PubMed=11354632; DOI=10.1007/s004390100480; RA Lazo P.A., Nadal M., Ferrer M., Area E., Hernandez-Torres J., RA Nabokina S.M., Mollinedo F., Estivill X.; RT "Genomic organization, chromosomal localization, alternative splicing, and RT isoforms of human Synaptosome associated protein-23 gene implicated in RT vesicle-membrane fusion."; RL Hum. Genet. 108:211-215(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNAP-23A). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNAP-23A). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNAP-23A). RC TISSUE=Cervix, Placenta, and Testis; 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 PROTEIN SEQUENCE OF 1-12, AND ACETYLATION AT MET-1. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [8] RP PROTEIN SEQUENCE OF 1-12 AND 55-64, ACETYLATION AT MET-1, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Ovarian carcinoma; RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.; RL Submitted (DEC-2008) to UniProtKB. RN [9] RP FUNCTION, AND INTERACTION WITH STX11. RC TISSUE=Placenta; RX PubMed=10036234; DOI=10.1242/jcs.112.6.845; RA Valdez A.C., Cabaniols J.-P., Brown M.J., Roche P.A.; RT "Syntaxin 11 is associated with SNAP-23 on late endosomes and the trans- RT Golgi network."; RL J. Cell Sci. 112:845-854(1999). RN [10] RP IDENTIFICATION IN A COMPLEX WITH VAMP8 AND STX1A. RX PubMed=12130530; DOI=10.1182/blood.v100.3.1081; RA Polgar J., Chung S.H., Reed G.L.; RT "Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in RT human platelets and are required for granule secretion."; RL Blood 100:1081-1083(2002). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND IDENTIFICATION BY RP 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 [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-110, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] 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 [15] RP PALMITOYLATION AT CYS-79; CYS-80; CYS-83; CYS-85; CYS-87 AND CYS-112. RX PubMed=21044946; DOI=10.1194/jlr.d011106; RA Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A., RA Stamler J.S., Casey P.J.; RT "Site-specific analysis of protein S-acylation by resin-assisted capture."; RL J. Lipid Res. 52:393-398(2011). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-34 AND SER-110, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-6; SER-20; SER-34 AND RP SER-110, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-110 AND SER-161, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [21] RP INTERACTION WITH STX11. RX PubMed=24910990; DOI=10.1371/journal.pone.0098900; RA Hellewell A.L., Foresti O., Gover N., Porter M.Y., Hewitt E.W.; RT "Analysis of familial hemophagocytic lymphohistiocytosis type 4 (FHL-4) RT mutant proteins reveals that S-acylation is required for the function of RT syntaxin 11 in natural killer cells."; RL PLoS ONE 9:e98900-e98900(2014). RN [22] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [23] RP INTERACTION WITH ZDHHC17. RX PubMed=28882895; DOI=10.1074/jbc.m117.799650; RA Lemonidis K., MacLeod R., Baillie G.S., Chamberlain L.H.; RT "Peptide array based screening reveals a large number of proteins RT interacting with the ankyrin repeat domain of the zDHHC17 S- RT acyltransferase."; RL J. Biol. Chem. 292:17190-17202(2017). RN [24] RP FUNCTION, INTERACTION WITH STX11, AND SUBCELLULAR LOCATION. RX PubMed=30811271; DOI=10.1091/mbc.e18-10-0653; RA Kinoshita D., Sakurai C., Morita M., Tsunematsu M., Hori N., Hatsuzawa K.; RT "Syntaxin 11 regulates the stimulus-dependent transport of Toll-like RT receptor 4 to the plasma membrane by cooperating with SNAP-23 in RT macrophages."; RL Mol. Biol. Cell 30:1085-1097(2019). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 23-76, COILED-COIL DOMAIN, AND RP SUBUNIT. RX PubMed=12556468; DOI=10.1074/jbc.m210483200; RA Freedman S.J., Song H.K., Xu Y., Sun Z.Y., Eck M.J.; RT "Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain."; RL J. Biol. Chem. 278:13462-13467(2003). CC -!- FUNCTION: SNAREs (soluble N-ethylmaleimide-sensitive factor-attachment CC protein receptors) are essential proteins for intracellular membrane CC fusion. SNAREs localized on opposing membranes assemble to form a CC trans-SNARE complex, an extended, parallel four-helix bundle whose CC assembly releases energy that drives membrane fusion. The core SNARE CC complex typically consists of four alpha-helical domains, three from CC target membrane SNAREs (t-SNAREs) and one from a vesicle SNARE (v- CC SNARE) (PubMed:10036234, PubMed:11354632, PubMed:8663154, CC PubMed:9070898). SNAP23 is a t-SNARE (target-SNARE) that resides on CC target membrane and functions in the fusion of transport vesicles with CC the plasma membrane in immune cells (PubMed:30811271). In macrophages, CC regulates the stimulus-dependent vesicular transport of TLR4 from CC recycling endosomes to the plasma membrane by cooperating with STX11 CC and thereby plays a critical role in the recognition of microbial CC components and the induction of innate and adaptive immunity CC (PubMed:30811271). In skeletal muscle satellite cells, SNAP23 CC cooperates with its cognate SNAREs VAMP4 and STX11 to facilitate CD36 CC vesicular transport from endosomes to the plasma membrane, an essential CC step in muscle regeneration (By similarity). CC {ECO:0000250|UniProtKB:O09044, ECO:0000269|PubMed:10036234, CC ECO:0000269|PubMed:11354632, ECO:0000269|PubMed:30811271, CC ECO:0000269|PubMed:8663154, ECO:0000269|PubMed:9070898}. CC -!- SUBUNIT: Homotetramer (via coiled-coil domain), also forms CC heterotetramers with STX4 and VAMP3 (PubMed:12556468). Forms a SNARE CC complex composed of STX4, SNAP23 and VAMP7 that functions in lysosomal CC exocytosis (By similarity). Forms a SNARE complex with VAMP4 and STX11; CC involved in vesicular transport from endosomes to the plasma membrane CC (PubMed:10036234, PubMed:24910990, PubMed:30811271). Found in a complex CC with VAMP8 and STX1A (PubMed:12130530). Found in a complex with VAMP8 CC and STX4 in pancreas (By similarity). Interacts with STX12 (By CC similarity). Interacts with ZDHHC13 (via ANK repeats) (By similarity). CC Interacts with ZDHHC17 (via ANK repeats) (PubMed:28882895). CC {ECO:0000250|UniProtKB:O09044, ECO:0000250|UniProtKB:O70377, CC ECO:0000269|PubMed:10036234, ECO:0000269|PubMed:12130530, CC ECO:0000269|PubMed:12556468, ECO:0000269|PubMed:24910990, CC ECO:0000269|PubMed:28882895, ECO:0000269|PubMed:30811271}. CC -!- INTERACTION: CC O00161; P54920: NAPA; NbExp=5; IntAct=EBI-745000, EBI-749652; CC O00161; Q9H115: NAPB; NbExp=3; IntAct=EBI-745000, EBI-3921185; CC O00161; O76038: SCGN; NbExp=3; IntAct=EBI-745000, EBI-749420; CC O00161; O75558: STX11; NbExp=12; IntAct=EBI-745000, EBI-714135; CC O00161; Q13277: STX3; NbExp=3; IntAct=EBI-745000, EBI-1394295; CC O00161; Q15836: VAMP3; NbExp=3; IntAct=EBI-745000, EBI-722343; CC O00161; Q8IUH5: ZDHHC17; NbExp=4; IntAct=EBI-745000, EBI-524753; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30811271}; CC Lipid-anchor {ECO:0000269|PubMed:21044946}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=SNAP-23a; CC IsoId=O00161-1; Sequence=Displayed; CC Name=SNAP-23b; CC IsoId=O00161-2; Sequence=VSP_006187, VSP_006188; CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest levels where found in placenta. CC -!- SIMILARITY: Belongs to the SNAP-25 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; U55936; AAC50537.1; -; mRNA. DR EMBL; Y09567; CAA70760.1; -; mRNA. DR EMBL; Y09568; CAA70761.1; -; mRNA. DR EMBL; AJ011915; CAA09864.1; -; mRNA. DR EMBL; AJ278972; CAC07504.1; -; Genomic_DNA. DR EMBL; AJ278973; CAC07504.1; JOINED; Genomic_DNA. DR EMBL; AJ278974; CAC07504.1; JOINED; Genomic_DNA. DR EMBL; BT006916; AAP35562.1; -; mRNA. DR EMBL; CR457212; CAG33493.1; -; mRNA. DR EMBL; BC000148; AAH00148.1; -; mRNA. DR EMBL; BC003686; AAH03686.1; -; mRNA. DR EMBL; BC022890; AAH22890.1; -; mRNA. DR CCDS; CCDS10087.1; -. [O00161-1] DR CCDS; CCDS10088.1; -. [O00161-2] DR PIR; JC5296; JC5296. DR PIR; JC5297; JC5297. DR RefSeq; NP_003816.2; NM_003825.4. [O00161-1] DR RefSeq; NP_570710.1; NM_130798.3. [O00161-2] DR RefSeq; XP_016878183.2; XM_017022694.2. [O00161-1] DR RefSeq; XP_047289158.1; XM_047433202.1. [O00161-1] DR RefSeq; XP_047289159.1; XM_047433203.1. [O00161-1] DR RefSeq; XP_054235016.1; XM_054379041.1. [O00161-1] DR RefSeq; XP_054235017.1; XM_054379042.1. [O00161-1] DR RefSeq; XP_054235018.1; XM_054379043.1. [O00161-1] DR PDB; 1NHL; X-ray; 2.30 A; A=23-76. DR PDB; 3ZUS; X-ray; 2.95 A; A/B/C/D=150-211. DR AlphaFoldDB; O00161; -. DR SMR; O00161; -. DR BioGRID; 114303; 225. DR CORUM; O00161; -. DR FunCoup; O00161; 1218. DR IntAct; O00161; 83. DR MINT; O00161; -. DR NDEx; IQUERY-CP-SNAP23; 4 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000249647; -. DR BindingDB; O00161; -. DR ChEMBL; CHEMBL6066300; -. DR TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family. DR GlyGen; O00161; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR iPTMnet; O00161; -. DR MetOSite; O00161; -. DR PhosphoSitePlus; O00161; -. DR SwissPalm; O00161; -. DR BioMuta; SNAP23; -. DR OGP; O00161; -. DR jPOST; O00161; -. DR MassIVE; O00161; -. DR PaxDb; 9606-ENSP00000249647; -. DR PeptideAtlas; O00161; -. DR ProteomicsDB; 47748; -. [O00161-1] DR ProteomicsDB; 47749; -. [O00161-2] DR Pumba; O00161; -. DR Antibodypedia; 712; 441 antibodies from 38 providers. DR DNASU; 8773; -. DR Ensembl; ENST00000249647.8; ENSP00000249647.3; ENSG00000092531.11. [O00161-1] DR Ensembl; ENST00000349777.5; ENSP00000207062.1; ENSG00000092531.11. [O00161-2] DR Ensembl; ENST00000397138.5; ENSP00000380327.1; ENSG00000092531.11. [O00161-2] DR Ensembl; ENST00000873737.1; ENSP00000543796.1; ENSG00000092531.11. [O00161-1] DR Ensembl; ENST00000873739.1; ENSP00000543798.1; ENSG00000092531.11. [O00161-1] DR Ensembl; ENST00000873740.1; ENSP00000543799.1; ENSG00000092531.11. [O00161-1] DR Ensembl; ENST00000873743.1; ENSP00000543802.1; ENSG00000092531.11. [O00161-1] DR Ensembl; ENST00000873744.1; ENSP00000543803.1; ENSG00000092531.11. [O00161-1] DR Ensembl; ENST00000960520.1; ENSP00000630579.1; ENSG00000092531.11. [O00161-1] DR Ensembl; ENST00000960521.1; ENSP00000630580.1; ENSG00000092531.11. [O00161-1] DR Ensembl; ENST00000960522.1; ENSP00000630581.1; ENSG00000092531.11. [O00161-1] DR GeneID; 8773; -. DR KEGG; hsa:8773; -. DR MANE-Select; ENST00000249647.8; ENSP00000249647.3; NM_003825.4; NP_003816.2. DR UCSC; uc001zpz.3; human. [O00161-1] DR AGR; HGNC:11131; -. DR ClinPGx; PA35979; -. DR CTD; 8773; -. DR DisGeNET; 8773; -. DR GeneCards; SNAP23; -. DR HGNC; HGNC:11131; SNAP23. DR HPA; ENSG00000092531; Low tissue specificity. DR MIM; 602534; gene. DR OpenTargets; ENSG00000092531; -. DR VEuPathDB; HostDB:ENSG00000092531; -. DR eggNOG; KOG3065; Eukaryota. DR GeneTree; ENSGT00950000182843; -. DR HOGENOM; CLU_096939_0_0_1; -. DR InParanoid; O00161; -. DR OMA; MNTEIER; -. DR OrthoDB; 19261at2759; -. DR PAN-GO; O00161; 7 GO annotations based on evolutionary models. DR PhylomeDB; O00161; -. DR PathwayCommons; O00161; -. DR Reactome; R-HSA-1236974; ER-Phagosome pathway. DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane. DR Reactome; R-HSA-199992; trans-Golgi Network Vesicle Budding. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-8980692; RHOA GTPase cycle. DR Reactome; R-HSA-9013026; RHOB GTPase cycle. DR Reactome; R-HSA-9013148; CDC42 GTPase cycle. DR Reactome; R-HSA-9013149; RAC1 GTPase cycle. DR Reactome; R-HSA-9013406; RHOQ GTPase cycle. DR Reactome; R-HSA-9013409; RHOJ GTPase cycle. DR Reactome; R-HSA-9013423; RAC3 GTPase cycle. DR Reactome; R-HSA-9035034; RHOF GTPase cycle. DR SignaLink; O00161; -. DR SIGNOR; O00161; -. DR Agora; ENSG00000092531; -. DR BioGRID-ORCS; 8773; 439 hits in 1169 CRISPR screens. DR ChiTaRS; SNAP23; human. DR EvolutionaryTrace; O00161; -. DR GeneWiki; SNAP23; -. DR GenomeRNAi; 8773; -. DR Pharos; O00161; Tbio. DR PRO; PR:O00161; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; O00161; protein. DR Bgee; ENSG00000092531; Expressed in monocyte and 205 other cell types or tissues. DR ExpressionAtlas; O00161; baseline and differential. DR GO; GO:0005912; C:adherens junction; IDA:BHF-UCL. DR GO; GO:0042582; C:azurophil granule; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0098562; C:cytoplasmic side of membrane; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0001772; C:immunological synapse; IDA:UniProt. DR GO; GO:0005739; C:mitochondrion; IDA:CACAO. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0098793; C:presynapse; IEA:GOC. DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB. DR GO; GO:0042581; C:specific granule; IDA:UniProtKB. DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome. DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome. DR GO; GO:0005484; F:SNAP receptor activity; IDA:UniProtKB. DR GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB. DR GO; GO:0043316; P:cytotoxic T cell degranulation; IMP:UniProtKB. DR GO; GO:0099638; P:endosome to plasma membrane protein transport; IDA:UniProtKB. DR GO; GO:0006887; P:exocytosis; IBA:GO_Central. DR GO; GO:0002553; P:histamine secretion by mast cell; IMP:UniProtKB. DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central. DR GO; GO:0016082; P:synaptic vesicle priming; IBA:GO_Central. DR GO; GO:0006906; P:vesicle fusion; IDA:UniProt. DR CDD; cd15884; SNARE_SNAP23C; 1. DR CDD; cd15895; SNARE_SNAP23N; 1. DR FunFam; 1.20.5.110:FF:000007; Synaptosomal-associated protein; 1. DR FunFam; 1.20.5.110:FF:000018; Synaptosomal-associated protein; 1. DR Gene3D; 1.20.5.110; -; 2. DR InterPro; IPR000928; SNAP-25_dom. DR InterPro; IPR000727; T_SNARE_dom. DR PANTHER; PTHR19305; SYNAPTOSOMAL ASSOCIATED PROTEIN; 1. DR PANTHER; PTHR19305:SF4; SYNAPTOSOMAL-ASSOCIATED PROTEIN 23; 1. DR Pfam; PF00835; SNAP-25; 1. DR SMART; SM00397; t_SNARE; 2. DR SUPFAM; SSF58038; SNARE fusion complex; 2. DR PROSITE; PS50192; T_SNARE; 2. DR PDBsum; 1NHL; -. DR PDBsum; 3ZUS; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cell membrane; KW Coiled coil; Direct protein sequencing; Lipoprotein; Membrane; Palmitate; KW Phosphoprotein; Protein transport; Proteomics identification; KW Reference proteome; Repeat; Transport. FT CHAIN 1..211 FT /note="Synaptosomal-associated protein 23" FT /id="PRO_0000213598" FT DOMAIN 14..76 FT /note="t-SNARE coiled-coil homology 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202" FT DOMAIN 146..208 FT /note="t-SNARE coiled-coil homology 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202" FT COILED 23..76 FT /evidence="ECO:0000269|PubMed:12556468" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.8, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712" FT MOD_RES 5 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 6 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 20 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 23 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O09044" FT MOD_RES 34 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 110 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 161 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT LIPID 79 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:21044946" FT LIPID 80 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:21044946" FT LIPID 83 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:21044946" FT LIPID 85 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:21044946" FT LIPID 87 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:21044946" FT LIPID 112 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000269|PubMed:21044946" FT VAR_SEQ 89 FT /note="R -> S (in isoform SNAP-23b)" FT /evidence="ECO:0000303|PubMed:9070898" FT /id="VSP_006187" FT VAR_SEQ 90..142 FT /note="Missing (in isoform SNAP-23b)" FT /evidence="ECO:0000303|PubMed:9070898" FT /id="VSP_006188" FT CONFLICT 135 FT /note="A -> V (in Ref. 1; AAC50537)" FT /evidence="ECO:0000305" FT HELIX 24..74 FT /evidence="ECO:0007829|PDB:1NHL" SQ SEQUENCE 211 AA; 23354 MW; AC378E9786C3A239 CRC64; MDNLSSEEIQ QRAHQITDES LESTRRILGL AIESQDAGIK TITMLDEQKE QLNRIEEGLD QINKDMRETE KTLTELNKCC GLCVCPCNRT KNFESGKAYK TTWGDGGENS PCNVVSKQPG PVTNGQLQQP TTGAASGGYI KRITNDARED EMEENLTQVG SILGNLKDMA LNIGNEIDAQ NPQIKRITDK ADTNRDRIDI ANARAKKLID S //