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Synaptosomal-associated protein 25 (SNAP-25) (Super protein) (SUP) (Synaptosomal-associated 25 kDa protein)

 SNP25_HUMAN             Reviewed;         206 AA.
P60880; B2RAU4; D3DW16; D3DW17; P13795; P36974; P70557; P70558;
Q53EM2; Q5U0B5; Q8IXK3; Q96FM2; Q9BR45;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
13-APR-2004, sequence version 1.
25-OCT-2017, entry version 150.
RecName: Full=Synaptosomal-associated protein 25;
Short=SNAP-25;
AltName: Full=Super protein;
Short=SUP;
AltName: Full=Synaptosomal-associated 25 kDa protein;
Name=SNAP25; Synonyms=SNAP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Fetal brain, and Temporal cortex;
PubMed=8112622; DOI=10.1016/0378-1119(94)90773-0;
Bark I.C., Wilson M.C.;
"Human cDNA clones encoding two different isoforms of the nerve
terminal protein SNAP-25.";
Gene 139:291-292(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Frontal cortex;
PubMed=8056350; DOI=10.1016/0378-1119(94)90027-2;
Zhao N., Hashida H., Takahashi N., Sakaki Y.;
"Cloning and sequence analysis of the human SNAP25 cDNA.";
Gene 145:313-314(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
TISSUE=Skeletal muscle;
PubMed=8760387; DOI=10.1042/bj3170945;
Jagadish M.N., Fernandez C.S., Hewish D.R., Macaulay S.L., Gough K.H.,
Grusovin J., Verkuylen A., Cosgrove L., Alafaci A., Frenkel M.J.,
Ward C.W.;
"Insulin-responsive tissues contain the core complex protein SNAP-25
(synaptosomal-associated protein 25) A and B isoforms in addition to
syntaxin 4 and synaptobrevins 1 and 2.";
Biochem. J. 317:945-954(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Amygdala, and Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PUTATIVE IRON-SULFUR CLUSTER.
PubMed=18375205; DOI=10.1016/j.febslet.2008.03.028;
Huang Q., Hong X., Hao Q.;
"SNAP-25 is also an iron-sulfur protein.";
FEBS Lett. 582:1431-1436(2008).
[11]
ASSOCIATION WITH THE BLOC-1 COMPLEX, AND INTERACTION WITH BLOC1S6.
PubMed=19546860; DOI=10.1038/mp.2009.58;
Ghiani C.A., Starcevic M., Rodriguez-Fernandez I.A., Nazarian R.,
Cheli V.T., Chan L.N., Malvar J.S., de Vellis J., Sabatti C.,
Dell'Angelica E.C.;
"The dysbindin-containing complex (BLOC-1) in brain: developmental
regulation, interaction with SNARE proteins and role in neurite
outgrowth.";
Mol. Psychiatry 15:204-215(2010).
[12]
INVOLVEMENT IN CMS18, VARIANT CMS18 ASN-67, AND CHARACTERIZATION OF
VARIANT CMS18 ASN-67.
PubMed=25381298; DOI=10.1212/WNL.0000000000001079;
Shen X.M., Selcen D., Brengman J., Engel A.G.;
"Mutant SNAP25B causes myasthenia, cortical hyperexcitability, ataxia,
and intellectual disability.";
Neurology 83:2247-2255(2014).
[13]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 11-81 AND 141-202 IN COMPLEX
WITH STX1A; CPLX1 AND VAMP2, AND STRUCTURE BY NMR.
PubMed=11832227; DOI=10.1016/S0896-6273(02)00583-4;
Chen X., Tomchick D.R., Kovrigin E., Arac D., Machius M.,
Suedhof T.C., Rizo J.;
"Three-dimensional structure of the complexin/SNARE complex.";
Neuron 33:397-409(2002).
-!- FUNCTION: t-SNARE involved in the molecular regulation of
neurotransmitter release. May play an important role in the
synaptic function of specific neuronal systems. Associates with
proteins involved in vesicle docking and membrane fusion.
Regulates plasma membrane recycling through its interaction with
CENPF. Modulates the gating characteristics of the delayed
rectifier voltage-dependent potassium channel KCNB1 in pancreatic
beta cells. {ECO:0000250|UniProtKB:P60881}.
-!- SUBUNIT: Part of the SNARE core complex containing SNAP25, VAMP2
and STX1A; this complex binds CPLX1 (PubMed:11832227). Found in a
complex containing SYT1, SV2B and syntaxin-1 (By similarity).
Found in a ternary complex with STX1A and VAMP8 (By similarity).
Isoform 1 and isoform 2 interact with BLOC1S6 (PubMed:19546860).
Interacts with CENPF (By similarity). Interacts with EQTN (By
similarity). Interacts with HGS (By similarity). Interacts with
KCNB1 (via N-terminus); reduces the voltage-dependent potassium
channel KCNB1 activity in pancreatic beta cells (By similarity).
Interacts with OTOF (By similarity). Interacts with RIMS1 (By
similarity). Interacts with SNAPIN (By similarity). Interacts with
STXBP6 (By similarity). Interacts with TRIM9 (By similarity).
Interacts with ZDHHC13 (via ANK repeats) (By similarity).
Interacts with ZDHHC17 (via ANK repeats) (By similarity).
Interacts with PLCL1 (via C2 domain) (By similarity). Associates
with the BLOC-1 complex (PubMed:19546860).
{ECO:0000250|UniProtKB:P60879, ECO:0000250|UniProtKB:P60881,
ECO:0000269|PubMed:11832227, ECO:0000269|PubMed:19546860}.
-!- INTERACTION:
O14810:CPLX1; NbExp=6; IntAct=EBI-12177361, EBI-2691813;
P32851:Stx1a (xeno); NbExp=4; IntAct=EBI-12177361, EBI-539720;
Q8IUH5:ZDHHC17; NbExp=3; IntAct=EBI-524785, EBI-524753;
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
{ECO:0000250|UniProtKB:P60879}. Cell membrane
{ECO:0000250|UniProtKB:P60881}; Lipid-anchor
{ECO:0000250|UniProtKB:P60879}. Cell junction, synapse,
synaptosome {ECO:0000250|UniProtKB:P60879}. Note=Membrane
association requires palmitoylation. Expressed throughout
cytoplasm, concentrating at the perinuclear region. Colocalizes
with KCNB1 at the cell membrane. {ECO:0000250|UniProtKB:P60879,
ECO:0000250|UniProtKB:P60881}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Isoforms differ by the usage of two alternative
homologous exons (5a and 5b) which code for positions 56 to 94
and differ only in 9 positions out of 39.;
Name=1; Synonyms=SNAP-25b;
IsoId=P60880-1, P13795-1;
Sequence=Displayed;
Name=2; Synonyms=SNAP-25a;
IsoId=P60880-2, P13795-2;
Sequence=VSP_006186;
-!- TISSUE SPECIFICITY: Neurons of the neocortex, hippocampus,
piriform cortex, anterior thalamic nuclei, pontine nuclei, and
granule cells of the cerebellum.
-!- PTM: Palmitoylated. Cys-85 appears to be the main site, and
palmitoylation is required for membrane association (By
similarity). {ECO:0000250}.
-!- DISEASE: Myasthenic syndrome, congenital, 18 (CMS18) [MIM:616330]:
A form of congenital myasthenic syndrome, a group of disorders
characterized by failure of neuromuscular transmission, including
pre-synaptic, synaptic, and post-synaptic disorders that are not
of autoimmune origin. Clinical features are easy fatigability and
muscle weakness affecting the axial and limb muscles (with
hypotonia in early-onset forms), the ocular muscles (leading to
ptosis and ophthalmoplegia), and the facial and bulbar musculature
(affecting sucking and swallowing, and leading to dysphonia). The
symptoms fluctuate and worsen with physical effort. CMS18 is an
autosomal dominant presynaptic disorder clinically characterized
by early-onset muscle weakness and easy fatigability associated
with delayed psychomotor development and ataxia.
{ECO:0000269|PubMed:25381298}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: When cloned and expressed in Eschericia coli, where
protein palmitoylation does not occur, Cys-85, Cys-88, Cys-90 and
Cys-92 in the protein sequence readily form an iron-sulfur cluster
instead.
-!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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EMBL; L19760; AAC37545.1; -; mRNA.
EMBL; L19761; AAC37546.1; -; mRNA.
EMBL; D21267; BAA22370.1; -; mRNA.
EMBL; BT019684; AAV38490.1; -; mRNA.
EMBL; AK223617; BAD97337.1; -; mRNA.
EMBL; AK289647; BAF82336.1; -; mRNA.
EMBL; AK314359; BAG36991.1; -; mRNA.
EMBL; AL023913; CAB42860.1; -; Genomic_DNA.
EMBL; AL023913; CAC34534.1; -; Genomic_DNA.
EMBL; AL023913; CAD56158.1; -; Genomic_DNA.
EMBL; CH471133; EAX10346.1; -; Genomic_DNA.
EMBL; CH471133; EAX10349.1; -; Genomic_DNA.
EMBL; CH471133; EAX10350.1; -; Genomic_DNA.
EMBL; CH471133; EAX10352.1; -; Genomic_DNA.
EMBL; BC010647; AAH10647.1; -; mRNA.
CCDS; CCDS13109.1; -. [P60880-2]
CCDS; CCDS13110.1; -.
PIR; I53735; I53735.
PIR; I67823; I67823.
RefSeq; NP_001309831.1; NM_001322902.1. [P60880-2]
RefSeq; NP_001309832.1; NM_001322903.1. [P60880-1]
RefSeq; NP_001309833.1; NM_001322904.1. [P60880-1]
RefSeq; NP_001309834.1; NM_001322905.1. [P60880-1]
RefSeq; NP_001309835.1; NM_001322906.1. [P60880-1]
RefSeq; NP_001309836.1; NM_001322907.1. [P60880-1]
RefSeq; NP_001309837.1; NM_001322908.1. [P60880-1]
RefSeq; NP_001309838.1; NM_001322909.1. [P60880-1]
RefSeq; NP_001309839.1; NM_001322910.1. [P60880-1]
RefSeq; NP_003072.2; NM_003081.4. [P60880-2]
RefSeq; NP_570824.1; NM_130811.3. [P60880-1]
RefSeq; XP_005260865.1; XM_005260808.4. [P60880-1]
RefSeq; XP_016883510.1; XM_017028021.1. [P60880-2]
RefSeq; XP_016883511.1; XM_017028022.1. [P60880-2]
UniGene; Hs.167317; -.
PDB; 1KIL; X-ray; 2.30 A; C=10-81, D=139-204.
PDB; 1XTG; X-ray; 2.10 A; B=146-204.
PDB; 2N1T; NMR; -; C=7-83, D=131-204.
PDB; 3DDA; X-ray; 1.50 A; B=197-202.
PDB; 3DDB; X-ray; 1.60 A; B=198-202.
PDB; 3RK2; X-ray; 2.20 A; C/G=7-82, D/H=141-203.
PDB; 3RK3; X-ray; 3.50 A; C=7-82, D=141-203.
PDB; 3RL0; X-ray; 3.80 A; C/G/K/O/S/W/a/e=7-82, D/H/L/P/T/X/b/f=141-203.
PDB; 3ZUR; X-ray; 2.71 A; A/B=145-206.
PDBsum; 1KIL; -.
PDBsum; 1XTG; -.
PDBsum; 2N1T; -.
PDBsum; 3DDA; -.
PDBsum; 3DDB; -.
PDBsum; 3RK2; -.
PDBsum; 3RK3; -.
PDBsum; 3RL0; -.
PDBsum; 3ZUR; -.
ProteinModelPortal; P60880; -.
SMR; P60880; -.
BioGrid; 112500; 33.
CORUM; P60880; -.
DIP; DIP-34554N; -.
IntAct; P60880; 17.
MINT; MINT-1403389; -.
STRING; 9606.ENSP00000254976; -.
ChEMBL; CHEMBL2364159; -.
DrugBank; DB00083; Botulinum Toxin Type A.
TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family.
iPTMnet; P60880; -.
PhosphoSitePlus; P60880; -.
SwissPalm; P60880; -.
BioMuta; SNAP25; -.
DMDM; 46397726; -.
EPD; P60880; -.
MaxQB; P60880; -.
PaxDb; P60880; -.
PeptideAtlas; P60880; -.
PRIDE; P60880; -.
DNASU; 6616; -.
Ensembl; ENST00000254976; ENSP00000254976; ENSG00000132639. [P60880-1]
Ensembl; ENST00000304886; ENSP00000307341; ENSG00000132639. [P60880-2]
GeneID; 6616; -.
KEGG; hsa:6616; -.
UCSC; uc002wnq.3; human.
CTD; 6616; -.
DisGeNET; 6616; -.
EuPathDB; HostDB:ENSG00000132639.12; -.
GeneCards; SNAP25; -.
HGNC; HGNC:11132; SNAP25.
HPA; CAB000360; -.
HPA; HPA001830; -.
MalaCards; SNAP25; -.
MIM; 600322; gene.
MIM; 616330; phenotype.
neXtProt; NX_P60880; -.
OpenTargets; ENSG00000132639; -.
PharmGKB; PA35980; -.
eggNOG; KOG3065; Eukaryota.
eggNOG; ENOG410Y3Y0; LUCA.
GeneTree; ENSGT00390000012186; -.
HOVERGEN; HBG056971; -.
InParanoid; P60880; -.
KO; K18211; -.
OMA; GEMDENL; -.
OrthoDB; EOG091G0N7J; -.
PhylomeDB; P60880; -.
TreeFam; TF315125; -.
Reactome; R-HSA-181429; Serotonin Neurotransmitter Release Cycle.
Reactome; R-HSA-181430; Norepinephrine Neurotransmitter Release Cycle.
Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle.
Reactome; R-HSA-212676; Dopamine Neurotransmitter Release Cycle.
Reactome; R-HSA-264642; Acetylcholine Neurotransmitter Release Cycle.
Reactome; R-HSA-422356; Regulation of insulin secretion.
Reactome; R-HSA-5250968; Toxicity of botulinum toxin type A (BoNT/A).
Reactome; R-HSA-5250971; Toxicity of botulinum toxin type C (BoNT/C).
Reactome; R-HSA-5250992; Toxicity of botulinum toxin type E (BoNT/E).
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-888590; GABA synthesis, release, reuptake and degradation.
SIGNOR; P60880; -.
ChiTaRS; SNAP25; human.
EvolutionaryTrace; P60880; -.
GeneWiki; SNAP25; -.
GenomeRNAi; 6616; -.
PMAP-CutDB; Q5U0B5; -.
PRO; PR:P60880; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000132639; -.
CleanEx; HS_SNAP25; -.
ExpressionAtlas; P60880; baseline and differential.
Genevisible; P60880; HS.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IEA:Ensembl.
GO; GO:0030426; C:growth cone; ISS:HGNC.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; ISS:HGNC.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0098794; C:postsynapse; IEA:Ensembl.
GO; GO:0042734; C:presynaptic membrane; TAS:ParkinsonsUK-UCL.
GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
GO; GO:0036477; C:somatodendritic compartment; IEA:Ensembl.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
GO; GO:0070032; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex; IBA:GO_Central.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
GO; GO:0048306; F:calcium-dependent protein binding; ISS:ParkinsonsUK-UCL.
GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
GO; GO:0017075; F:syntaxin-1 binding; IPI:UniProtKB.
GO; GO:0008306; P:associative learning; IEA:Ensembl.
GO; GO:0007268; P:chemical synaptic transmission; NAS:UniProtKB.
GO; GO:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; IEA:Ensembl.
GO; GO:0014047; P:glutamate secretion; TAS:Reactome.
GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
GO; GO:0099590; P:neurotransmitter receptor internalization; IEA:Ensembl.
GO; GO:0007269; P:neurotransmitter secretion; TAS:Reactome.
GO; GO:0001504; P:neurotransmitter uptake; NAS:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0031915; P:positive regulation of synaptic plasticity; IEA:Ensembl.
GO; GO:0050796; P:regulation of insulin secretion; TAS:UniProtKB.
GO; GO:0010975; P:regulation of neuron projection development; IEA:Ensembl.
GO; GO:1990926; P:short-term synaptic potentiation; IEA:Ensembl.
GO; GO:0016081; P:synaptic vesicle docking; NAS:UniProtKB.
GO; GO:0016079; P:synaptic vesicle exocytosis; TAS:ParkinsonsUK-UCL.
GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
GO; GO:0016082; P:synaptic vesicle priming; IBA:GO_Central.
InterPro; IPR000928; SNAP-25.
InterPro; IPR000727; T_SNARE_dom.
Pfam; PF00835; SNAP-25; 1.
SMART; SM00397; t_SNARE; 2.
PROSITE; PS50192; T_SNARE; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Coiled coil; Complete proteome; Congenital myasthenic syndrome;
Cytoplasm; Disease mutation; Lipoprotein; Membrane;
Mental retardation; Palmitate; Phosphoprotein; Reference proteome;
Repeat; Synapse; Synaptosome.
CHAIN 1 206 Synaptosomal-associated protein 25.
/FTId=PRO_0000213587.
DOMAIN 19 81 t-SNARE coiled-coil homology 1.
{ECO:0000255|PROSITE-ProRule:PRU00202}.
DOMAIN 140 202 t-SNARE coiled-coil homology 2.
{ECO:0000255|PROSITE-ProRule:PRU00202}.
REGION 1 75 Interaction with CENPF. {ECO:0000250}.
COMPBIAS 85 92 Cys-rich.
SITE 180 181 Cleavage; by BONT/E.
MOD_RES 138 138 Phosphothreonine.
{ECO:0000250|UniProtKB:P60879}.
MOD_RES 154 154 Phosphoserine.
{ECO:0000250|UniProtKB:P60879}.
MOD_RES 187 187 Phosphoserine.
{ECO:0000250|UniProtKB:P60879}.
LIPID 85 85 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P60879}.
LIPID 88 88 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P60879}.
LIPID 90 90 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P60879}.
LIPID 92 92 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P60879}.
VAR_SEQ 58 89 ERIEEGMDQINKDMKEAEKNLTDLGKFCGLCV -> DRVEE
GMNHINQDMKEAEKNLKDLGKCCGLFI (in isoform
2). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8056350,
ECO:0000303|PubMed:8112622,
ECO:0000303|Ref.4}.
/FTId=VSP_006186.
VARIANT 67 67 I -> N (in CMS18; interfers with calcium-
induced fusion; inhibits exocytosis of
catecholamine-containing vesicles).
{ECO:0000269|PubMed:25381298}.
/FTId=VAR_073698.
CONFLICT 44 44 I -> V (in Ref. 5; BAD97337).
{ECO:0000305}.
HELIX 8 80 {ECO:0000244|PDB:3RK2}.
HELIX 148 167 {ECO:0000244|PDB:1XTG}.
STRAND 191 193 {ECO:0000244|PDB:1XTG}.
SEQUENCE 206 AA; 23315 MW; FBED2B082A4CB6A6 CRC64;
MAEDADMRNE LEEMQRRADQ LADESLESTR RMLQLVEESK DAGIRTLVML DEQGEQLERI
EEGMDQINKD MKEAEKNLTD LGKFCGLCVC PCNKLKSSDA YKKAWGNNQD GVVASQPARV
VDEREQMAIS GGFIRRVTND ARENEMDENL EQVSGIIGNL RHMALDMGNE IDTQNRQIDR
IMEKADSNKT RIDEANQRAT KMLGSG


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