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2KOG

lipid-bound synaptobrevin solution NMR structure

Functional Information from GO Data
ChainGOidnamespacecontents
A0000149molecular_functionSNARE binding
A0000322cellular_componentstorage vacuole
A0005484molecular_functionSNAP receptor activity
A0005515molecular_functionprotein binding
A0005516molecular_functioncalmodulin binding
A0005543molecular_functionphospholipid binding
A0005737cellular_componentcytoplasm
A0005802cellular_componenttrans-Golgi network
A0005886cellular_componentplasma membrane
A0006906biological_processvesicle fusion
A0008021cellular_componentsynaptic vesicle
A0008076cellular_componentvoltage-gated potassium channel complex
A0008289molecular_functionlipid binding
A0009749biological_processresponse to glucose
A0014069cellular_componentpostsynaptic density
A0016020cellular_componentmembrane
A0016079biological_processsynaptic vesicle exocytosis
A0016081biological_processsynaptic vesicle docking
A0016192biological_processvesicle-mediated transport
A0017022molecular_functionmyosin binding
A0017075molecular_functionsyntaxin-1 binding
A0017156biological_processcalcium-ion regulated exocytosis
A0017157biological_processregulation of exocytosis
A0019905molecular_functionsyntaxin binding
A0030136cellular_componentclathrin-coated vesicle
A0030141cellular_componentsecretory granule
A0030659cellular_componentcytoplasmic vesicle membrane
A0030667cellular_componentsecretory granule membrane
A0030672cellular_componentsynaptic vesicle membrane
A0031201cellular_componentSNARE complex
A0031410cellular_componentcytoplasmic vesicle
A0031982cellular_componentvesicle
A0032869biological_processcellular response to insulin stimulus
A0035493biological_processSNARE complex assembly
A0042589cellular_componentzymogen granule membrane
A0042802molecular_functionidentical protein binding
A0043001biological_processGolgi to plasma membrane protein transport
A0043195cellular_componentterminal bouton
A0043308biological_processeosinophil degranulation
A0043312biological_processneutrophil degranulation
A0043320biological_processnatural killer cell degranulation
A0044306cellular_componentneuron projection terminus
A0044325molecular_functiontransmembrane transporter binding
A0044877molecular_functionprotein-containing complex binding
A0045055biological_processregulated exocytosis
A0045202cellular_componentsynapse
A0046879biological_processhormone secretion
A0048306molecular_functioncalcium-dependent protein binding
A0048471cellular_componentperinuclear region of cytoplasm
A0048488biological_processsynaptic vesicle endocytosis
A0051649biological_processestablishment of localization in cell
A0060090molecular_functionmolecular adaptor activity
A0060291biological_processlong-term synaptic potentiation
A0060627biological_processregulation of vesicle-mediated transport
A0061025biological_processmembrane fusion
A0065003biological_processprotein-containing complex assembly
A0070032cellular_componentsynaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex
A0070033cellular_componentsynaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex
A0070044cellular_componentsynaptobrevin 2-SNAP-25-syntaxin-1a complex
A0070254biological_processmucus secretion
A0090316biological_processpositive regulation of intracellular protein transport
A0098967biological_processexocytic insertion of neurotransmitter receptor to postsynaptic membrane
A0098978cellular_componentglutamatergic synapse
A0099003biological_processvesicle-mediated transport in synapse
A0099524cellular_componentpostsynaptic cytosol
A1902259biological_processregulation of delayed rectifier potassium channel activity
A1903421biological_processregulation of synaptic vesicle recycling
A1903593biological_processregulation of histamine secretion by mast cell
Functional Information from PROSITE/UniProt
site_idPS00417
Number of Residues20
DetailsSYNAPTOBREVIN Synaptobrevin signature. NVDKVlERdqKLSeLdDRAD
ChainResidueDetails
AASN49-ASP68

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues92
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
ASER2-LYS94

site_idSWS_FT_FI2
Number of Residues19
DetailsTRANSMEM: Helical; Anchor for type IV membrane protein => ECO:0000255
ChainResidueDetails
AMET95-PHE114

site_idSWS_FT_FI3
Number of Residues1
DetailsTOPO_DOM: Vesicular => ECO:0000255
ChainResidueDetails
ASER115-THR116

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: (Microbial infection) Cleavage; by C.botulinum neurotoxin type F (BoNT/F, botF) => ECO:0000269|PubMed:8505288
ChainResidueDetails
AGLN58

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: (Microbial infection) Cleavage; by C.botulinum neurotoxin type D (BoNT/D, botD) => ECO:0000269|PubMed:8175689
ChainResidueDetails
ALYS59

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: (Microbial infection) Cleavage; by C.botulinum neurotoxin type X (BoNT/X) => ECO:0000269|PubMed:28770820
ChainResidueDetails
AARG66

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: (Microbial infection) Cleavage; by C.tetani tetanus toxin (tetX) => ECO:0000269|PubMed:1331807
ChainResidueDetails
AGLN76

site_idSWS_FT_FI8
Number of Residues1
DetailsSITE: (Microbial infection) Cleavage; by C.botulinum neurotoxin type G (BoNT/G, botG) => ECO:0000269|PubMed:7910017
ChainResidueDetails
AALA81

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P63026
ChainResidueDetails
ASER2

227111

PDB entries from 2024-11-06

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