| IED ID | IndEnz0002010562 |
| Enzyme Type ID | protease010562 |
| Protein Name |
Synaptosomal-associated protein 25 SNAP-25 Super protein SUP Synaptosomal-associated 25 kDa protein |
| Gene Name | SNAP25 SNAP |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTDLGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG |
| Enzyme Length | 206 |
| Uniprot Accession Number | P60880 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | 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}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Beta strand (1); Chain (1); Domain (2); Helix (2); Lipidation (4); Modified residue (3); Mutagenesis (12); Natural variant (1); Region (3); Sequence conflict (1); Site (3) |
| Keywords | 3D-structure;Alternative splicing;Cell junction;Cell membrane;Coiled coil;Congenital myasthenic syndrome;Cytoplasm;Disease variant;Lipoprotein;Membrane;Mental retardation;Palmitate;Phosphoprotein;Reference proteome;Repeat;Synapse;Synaptosome |
| Interact With | Q16623; Q8IUH5; P0DTD1; O14810; P42858; O75558; Q8N4C7; Q16623; Q9BRT2; Q13360-2; P32851 |
| Induction | |
| Subcellular Location | 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}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P60879}. Note=Membrane association requires palmitoylation. Expressed throughout cytoplasm, concentrating at the perinuclear region. Colocalizes with KCNB1 at the cell membrane (By similarity). Colocalizes with PLCL1 at the cell membrane (By similarity). {ECO:0000250|UniProtKB:P60879, ECO:0000250|UniProtKB:P60881}. |
| Modified Residue | MOD_RES 138; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P60879; MOD_RES 154; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P60879; MOD_RES 187; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P60879 |
| Post Translational Modification | PTM: Palmitoylated (PubMed:28757145). Cys-85 appears to be the main site, and palmitoylation is required for membrane association (By similarity). {ECO:0000250|UniProtKB:P60879, ECO:0000269|PubMed:28757145}.; PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type A (BoNT/A, botA) which hydrolyzes the 197-Gln-|-Arg-198 bond and inhibits neurotransmitter release (PubMed:15592454, PubMed:9886085). {ECO:0000269|PubMed:9886085, ECO:0000305|PubMed:15592454}.; PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type C (BoNT/C) which hydrolyzes the 198-Arg-|-Ala-199 bond and inhibits neurotransmitter release (PubMed:9886085, PubMed:17718519). C.botulinum type C only rarely infects humans. {ECO:0000269|PubMed:17718519, ECO:0000269|PubMed:9886085}.; PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type E (BoNT/E) which hydrolyzes the 180-Arg-|-Ile-181 bond and inhibits neurotransmitter release (PubMed:9886085). {ECO:0000269|PubMed:9886085}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (1); X-ray crystallography (11) |
| Cross Reference PDB | 1KIL; 1XTG; 2N1T; 3DDA; 3DDB; 3RK2; 3RK3; 3RL0; 3ZUR; 5W7I; 5W7J; 6JLH; |
| Mapped Pubmed ID | 10440375; 10480595; 10889551; 11017172; 11163272; 11287790; 11309201; 11815450; 11815463; 11873862; 11920846; 12114505; 12403834; 12475239; 12499044; 12519779; 12558796; 12660803; 12684222; 12691775; 12750892; 12814864; 12887316; 14514350; 14529723; 14676208; 14709554; 14766180; 15007392; 15121806; 15217342; 15537656; 15572341; 15603740; 15717291; 15728193; 15752769; 15823421; 15829963; 15935055; 16088329; 16099818; 16169070; 16189514; 16443778; 16714477; 16720719; 16722236; 16801949; 16874303; 16939418; 17055430; 17301226; 17325194; 17325713; 17325714; 17427194; 17455213; 17478680; 17500595; 17501935; 17502420; 17702749; 17877635; 17891149; 17900700; 17908175; 17989281; 18041776; 18162464; 18171919; 18191416; 18250960; 18347838; 18457912; 18512733; 18519826; 18596234; 18617262; 18617632; 18633321; 18658150; 18726138; 18818739; 18821565; 18821566; 18957941; 19004828; 19058789; 19060904; 19086053; 19099826; 19125158; 19132710; 19156089; 19156168; 19188424; 19193342; 19375301; 19506906; 19557857; 19695183; 19713048; 19721846; 19724880; 19806613; 19858760; 19913510; 20029029; 20235792; 20333500; 20379614; 20519516; 20599404; 20677014; 20679152; 20921140; 20950795; 21073671; 21092861; 21378164; 21497654; 21526988; 21557260; 21756448; 21785414; 21916482; 21996783; 22139146; 22193912; 22311984; 22732502; 22762387; 22940547; 23242284; 23341457; 23403573; 23463002; 23593184; 23612411; 23650620; 23872233; 23888754; 23936420; 24164654; 24176595; 24362847; 24391914; 24478316; 24769566; 24778312; 24885975; 25024311; 25122888; 25418885; 25445064; 25629685; 25650683; 25655772; 25698757; 25766323; 26030874; 26204769; 26241848; 26395074; 26779543; 26821215; 26929012; 26941099; 26971072; 27184832; 27380186; 27627841; 27815333; 27888397; 28176268; 28339008; 28356525; 28412278; 28486561; 28495859; 28575017; 28696301; 28855684; 28972123; 29111973; 29130426; 29158500; 29361339; 29491473; 30092259; 30144541; 30334187; 30607888; 30610939; 30680692; 30916996; 31653583; 31694913; 31794878; 32051343; 32156735; 32317281; 32412599; 32479779; 32675412; 33028119; 33147442; 33217562; 33299146; 33765432; 34289870; 7556990; 7641683; 8243676; 8294407; 8402889; 8611567; 8997178; 9701566; 9914469; |
| Motif | |
| Gene Encoded By | |
| Mass | 23,315 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |