Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00042
Entry Name
UniProt Accession
Theoretical PI
4.89
Molecular Weight
23354.05
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Synaptosomal-associated protein 23
Protein Synonyms/Alias
SNAP-23; Vesicle-membrane fusion protein SNAP-23;
Gene Name
SNAP23
Gene Synonyms/Alias
Created Date
30-MAY-2000
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
79
Canonical
TLTELNKCCGLCVCP
[1]
S-Palmitoylation
80
Canonical
LTELNKCCGLCVCPC
[2][3]
S-Palmitoylation
83
Canonical
LNKCCGLCVCPCNRT
[2][3]
S-Palmitoylation
85
Canonical
KCCGLCVCPCNRTKN
[2][3]
S-Palmitoylation
87
Canonical
CGLCVCPCNRTKNFE
[2][3]
S-Palmitoylation
112
Canonical
DGGENSPCNVVSKQP
[3]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Greaves J, Gorleku OA, Salaun C, Chamberlain LH. Palmitoylation of the SNAP25 protein family: specificity and regulation by DHHC palmitoyl transferases. J BiolChem. 2010 Aug 6;285(32):24629-38. doi: 10.1074/jbc.M110.119289. Epub 2010 Jun 2.[PMID:20519516]
[2] Pallavi B, Nagaraj R. Palmitoylated peptides from the cysteine-rich domain of SNAP-23 cause membrane fusion depending on peptide length, position of cysteines,and extent of palmitoylation. J Biol Chem. 2003 Apr 11;278(15):12737-44. Epub2003 Jan 27.[PMID:12551899]
[3] Forrester MT, Hess DT, Thompson JW, Hultman R, Moseley MA, Stamler JS, CaseyPJ. Site-specific analysis of protein S-acylation by resin-assisted capture. JLipid Res. 2011 Feb;52(2):393-8. doi: 10.1194/jlr.D011106. Epub 2010 Nov 2.[PMID:21044946]
Functional Description
Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion.
Sequence Annotation
Domain: 14 76 t-SNARE coiled-coil homology 1.
Domain: 146 208 t-SNARE coiled-coil homology 2.
Modified residue: 1 1 N-acetylmethionine.
Modified residue: 20 20 Phosphoserine.
Modified residue: 23 23 Phosphoserine.
Modified residue: 34 34 Phosphoserine.
Modified residue: 110 110 Phosphoserine.
Protein Length
211 AA.
Protein Sequence
(Canonical)
MDNLSSEEIQ QRAHQITDES LESTRRILGL AIESQDAGIK TITMLDEQKE QLNRIEEGLD  60
QINKDMRETE KTLTELNKCC GLCVCPCNRT KNFESGKAYK TTWGDGGENS PCNVVSKQPG  120
PVTNGQLQQP TTGAASGGYI KRITNDARED EMEENLTQVG SILGNLKDMA LNIGNEIDAQ  180
NPQIKRITDK ADTNRDRIDI ANARAKKLID S                                 211
FASTA
(Canonical)
>LipidDB-9606-00042|O00161
MDNLSSEEIQQRAHQITDESLESTRRILGLAIESQDAGIKTITMLDEQKEQLNRIEEGLD
QINKDMRETEKTLTELNKCCGLCVCPCNRTKNFESGKAYKTTWGDGGENSPCNVVSKQPG
PVTNGQLQQPTTGAASGGYIKRITNDAREDEMEENLTQVGSILGNLKDMALNIGNEIDAQ
NPQIKRITDKADTNRDRIDIANARAKKLIDS
Gene Ontology
GO:0042582; C:azurophil granule; IDA:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005925; C:focal adhesion; IDA:UniProtKB
GO:0043005; C:neuron projection; IEA:UniProtKB-KW
GO:0005634; C:nucleus; IDA:HPA
GO:0005886; C:plasma membrane; IDA:HPA
GO:0042581; C:specific granule; IDA:UniProtKB
GO:0045202; C:synapse; IEA:UniProtKB-KW
GO:0006887; P:exocytosis; IEA:Ensembl
GO:0061025; P:membrane fusion; TAS:ProtInc
GO:0061024; P:membrane organization; TAS:Reactome
GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome
GO:0015031; P:protein transport; IEA:UniProtKB-KW
GO:0006903; P:vesicle targeting; TAS:ProtInc
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