Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00433
Entry Name
UniProt Accession
Theoretical PI
4.66
Molecular Weight
23315.08
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Synaptosomal-associated protein 25
Protein Synonyms/Alias
SNAP-25; Super protein; SUP; Synaptosomal-associated 25 kDa protein;
Gene Name
SNAP25
Gene Synonyms/Alias
SNAP;
Created Date
13-APR-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
85
Canonical
LTDLGKFCGLCVCPC
[1][2]
S-Palmitoylation
88
Canonical
LGKFCGLCVCPCNKL
[1][2]
S-Palmitoylation
90
Canonical
KFCGLCVCPCNKLKS
[1][2]
S-Palmitoylation
92
Canonical
CGLCVCPCNKLKSSD
[1][2]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Lane SR, Liu Y. Characterization of the palmitoylation domain of SNAP-25. JNeurochem. 1997 Nov;69(5):1864-9.[PMID:9349529]
[2] Salaün C, Gould GW, Chamberlain LH. The SNARE proteins SNAP-25 and SNAP-23display different affinities for lipid rafts in PC12 cells. Regulation bydistinct cysteine-rich domains. J Biol Chem. 2005 Jan 14;280(2):1236-40. Epub2004 Nov 12.[PMID:15542596]
Functional Description
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.
Sequence Annotation
Domain: 19 81 t-SNARE coiled-coil homology 1.
Domain: 140 202 t-SNARE coiled-coil homology 2.
Region: 1 75 Interaction with CENPF.
Functional site: 180 181 Cleavage; by BONT/E.
Modified residue: 138 138 Phosphothreonine.
Modified residue: 187 187 Phosphoserine.
Protein Length
206 AA.
Protein Sequence
(Canonical)
MAEDADMRNE LEEMQRRADQ LADESLESTR RMLQLVEESK DAGIRTLVML DEQGEQLERI  60
EEGMDQINKD MKEAEKNLTD LGKFCGLCVC PCNKLKSSDA YKKAWGNNQD GVVASQPARV  120
VDEREQMAIS GGFIRRVTND ARENEMDENL EQVSGIIGNL RHMALDMGNE IDTQNRQIDR  180
IMEKADSNKT RIDEANQRAT KMLGSG                                       206
FASTA
(Canonical)
>LipidDB-9606-00433|P60880
MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERI
EEGMDQINKDMKEAEKNLTDLGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARV
VDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNLRHMALDMGNEIDTQNRQIDR
IMEKADSNKTRIDEANQRATKMLGSG
Gene Ontology
GO:0030054; C:cell junction; IEA:UniProtKB-KW
GO:0005737; C:cytoplasm; ISS:UniProtKB
GO:0030426; C:growth cone; ISS:HGNC
GO:0016020; C:membrane; ISS:UniProtKB
GO:0043005; C:neuron projection; ISS:HGNC
GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0042734; C:presynaptic membrane; TAS:ParkinsonsUK-UCL
GO:0031201; C:SNARE complex; IDA:UniProtKB
GO:0070032; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex; IEA:Ensembl
GO:0005802; C:trans-Golgi network; IEA:Ensembl
GO:0048306; F:calcium-dependent protein binding; ISS:ParkinsonsUK-UCL
GO:0006112; P:energy reserve metabolic process; TAS:Reactome
GO:0014047; P:glutamate secretion; TAS:Reactome
GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl
GO:0007269; P:neurotransmitter secretion; TAS:Reactome
GO:0001504; P:neurotransmitter uptake; NAS:UniProtKB
GO:0070201; P:regulation of establishment of protein localization; IEA:Ensembl
GO:0050796; P:regulation of insulin secretion; TAS:UniProtKB
GO:0010975; P:regulation of neuron projection development; IEA:Ensembl
GO:0044281; P:small molecule metabolic process; TAS:Reactome
GO:0007268; P:synaptic transmission; NAS:UniProtKB
GO:0016081; P:synaptic vesicle docking involved in exocytosis; NAS:UniProtKB
GO:0016079; P:synaptic vesicle exocytosis; TAS:ParkinsonsUK-UCL
Interpro
InterPro; IPR000928; SNAP-25
InterPro; IPR000727; T_SNARE_dom
Pfam
Pfam; PF00835; SNAP-25;
Pfam; PF05739; SNARE;
SMART
SMART; SM00397; t_SNARE;
PROSITE
PROSITE; PS50192; T_SNARE;
PRINTS