about
P688
Huntingtin interacting proteins are genetic modifiers of neurodegenerationComplexins: cytosolic proteins that regulate SNAP receptor functionLRRK2 phosphorylates Snapin and inhibits interaction of Snapin with SNAP-25The dysbindin-containing complex (BLOC-1) in brain: developmental regulation, interaction with SNARE proteins and role in neurite outgrowthAlpha-synuclein promotes SNARE-complex assembly in vivo and in vitroLTP requires a unique postsynaptic SNARE fusion machineryUltrahigh-resolution imaging reveals formation of neuronal SNARE/Munc18 complexes in situCSPα knockout causes neurodegeneration by impairing SNAP-25 functionConformational switch of syntaxin-1 controls synaptic vesicle fusionOtoferlin, defective in a human deafness form, is essential for exocytosis at the auditory ribbon synapseCytLEK1 is a regulator of plasma membrane recycling through its interaction with SNAP-25The Golgi S-acylation machinery comprises zDHHC enzymes with major differences in substrate affinity and S-acylation activitySomatodendritic dopamine release requires synaptotagmin 4 and 7 and the participation of voltage-gated calcium channelsDynamin-1 co-associates with native mouse brain BKCa channels: proteomics analysis of synaptic protein complexesCalmodulin and lipid binding to synaptobrevin regulates calcium-dependent exocytosisType VI adenylyl cyclase regulates neurite extension by binding to Snapin and Snap25Spatial, temporal and subcellular localization of islet-brain 1 (IB1), a homologue of JIP-1, in mouse brainSynaptotagmin-mediated bending of the target membrane is a critical step in Ca(2+)-regulated fusionAcrosome formation-associated factor is involved in fertilizationSNARE protein recycling by αSNAP and βSNAP supports synaptic vesicle primingEpileptiform activity and cognitive deficits in SNAP-25(+/-) mice are normalized by antiepileptic drugsA role for SNAP25 in internalization of kainate receptors and synaptic plasticityPhosphorylation of syntaxin 3B by CaMKII regulates the formation of t-SNARE complexesGenetic ablation of the t-SNARE SNAP-25 distinguishes mechanisms of neuroexocytosisScrg1, a novel protein of the CNS is targeted to the large dense-core vesicles in neuronal cellsMurine CENPF interacts with syntaxin 4 in the regulation of vesicular transportA dominant mutation in Snap25 causes impaired vesicle trafficking, sensorimotor gating, and ataxia in the blind-drunk mouse.CAPS drives trans-SNARE complex formation and membrane fusion through syntaxin interactionsPRRT2 Is a Key Component of the Ca(2+)-Dependent Neurotransmitter Release Machinery.Ca(2+)-synaptotagmin directly regulates t-SNARE function during reconstituted membrane fusion.The SNARE Sec22b has a non-fusogenic function in plasma membrane expansion.PRRT2 deficiency induces paroxysmal kinesigenic dyskinesia by regulating synaptic transmission in cerebellum.Differential Abilities of SNAP-25 Homologs to Support Neuronal Function
P921
Q21145230-D11C8489-0379-4EA2-BE85-1F5C7D827D26Q24309091-55D1FC42-04A5-453B-8396-2D06B156C1B1Q24317760-032DDEDF-4B80-49A8-8C7E-0FC3171354B8Q24338919-6C4A5693-306D-4845-916D-224FB7EFCF7DQ24629968-C3ABE4B1-58E1-45C4-B56F-AA2AD854748EQ26269854-8150D462-C558-4EC2-A3DF-83FB861D1F32Q26269856-B8229FD4-39DC-4C10-A944-818226E06784Q26269887-7CD82774-FEA6-441C-BC1F-ACBF9BE695E3Q26270279-5A9A8F18-C37B-4907-9D07-0F4C3D102CD8Q28269823-A736A5A7-3C11-48F9-8EC7-8A45B15BE6E9Q28507056-B8D8E9EE-F994-4CDE-BCFC-8BDE926A8B15Q28507488-09014000-6E29-4D58-AEF7-B6064592BA0DQ28507955-28CBA4D7-99B4-4A68-9F5F-80A62F133DC0Q28508367-05B52FA4-96EC-406C-BE57-B94B0BB4CEF4Q28509919-E1CAF9F3-CE8B-4604-A3F4-2D727E45B779Q28511414-34D89155-1762-48AB-8E7B-4443445691DEQ28581943-1AB5A82B-5F92-420B-8AA6-1E6A881ADCD8Q28584744-A03CFB13-5948-45D0-8474-4A33D8E46280Q28585615-CD18817F-1D75-4A19-AEA1-1378A613D7FCQ28589671-264FD20C-56A2-4765-A857-F0B0840BD973Q28590796-153C460B-9719-43F0-B04A-A0EB7C22A925Q28591013-67EC48E1-A544-4511-8589-4002BF28C06CQ28591181-BF927FC2-B86E-4062-BAFF-79308142E1EBQ28591459-7EB4F906-95F0-4A89-9EA0-19139E1B6AA2Q28593629-A048A9DB-13F2-425F-8C4D-199F90AB450AQ28593991-7A1B74C9-7555-43DB-82CF-48DAE40C13EDQ30542925-2F0E6EED-4E02-4810-8C8A-F33218B85552Q37394786-33D9197F-B949-4F4E-B995-9F348B296DD2Q40002241-856EBB0B-6921-4345-914B-7AFCAC5E2CAEQ41791620-851E625C-D124-4771-998E-D6E186002DDBQ41791643-7AA68483-4082-4FE1-9BE8-B79D9A63035EQ47619364-DA89109E-9AE7-4876-812E-A34287558E0DQ58361567-6C565434-093D-4784-85C7-D7F0381750F0
P921
description
mammalian protein found in Mus musculus
@en
protein
@id
proteinë
@sq
proteïne in Synaptosomal-associated protein 25
@nl
protèin
@ace
بروتين في فأر المنازل
@ar
name
Synaptosomal-associated protein 25
@en
Synaptosomal-associated protein 25
@nl
type
label
Synaptosomal-associated protein 25
@en
Synaptosomal-associated protein 25
@nl
altLabel
SUP
@en
Snap25
@en
blind drunk
@en
super protein
@en
synaptosomal-associated 25 kDa protein
@en
synaptosomal-associated protein 25
@en
synaptosomal-associated protein, 25 kDa
@en
prefLabel
Synaptosomal-associated protein 25
@en
Synaptosomal-associated protein 25
@nl
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NP_001277985
NP_001342183
NP_001342184
XP_017172249
XP_017172250
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ENSMUSP00000028727
ENSMUSP00000105725