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Protein Page:
SNAP-25 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
SNAP-25 a presynaptic plasma membrane protein involved in the regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Part of the SNARE core complex containing SNAP25, VAMP2 and syntaxin 1A. Associates with proteins involved in vesicle docking and membrane fusion. Two alternatively spliced isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: Vesicle protein
Chromosomal Location of Human Ortholog: 20p12-p11.2
Cellular Component: SNARE complex; neuron projection; growth cone; membrane; perinuclear region of cytoplasm; cytoplasm; plasma membrane; synapse; trans-Golgi network; cell junction
Molecular Function: SNARE binding; protein binding
Biological Process: synaptic transmission; glutamate secretion; neurotransmitter secretion; energy reserve metabolic process; neurotransmitter uptake; regulation of insulin secretion; synaptic vesicle docking during exocytosis
Reference #:  P60880 (UniProtKB)
Alt. Names/Synonyms: bA416N4.2; dJ1068F16.2; FLJ23079; resistance to inhibitors of cholinesterase 4 homolog; RIC-4; RIC4; SEC9; SNAP; SNAP-25; SNAP25; SNP25; SUP; Super protein; Synaptosomal-associated 25 kDa protein; Synaptosomal-associated protein 25; synaptosomal-associated protein, 25kDa
Gene Symbols: SNAP25
Molecular weight: 23,315 Da
Basal Isoelectric point: 4.66  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

SNAP-25

Protein Structure Not Found.


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Sites Implicated In
exocytosis, altered: S187‑p
activity, induced: S187‑p
molecular association, regulation: T138‑p, S187‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 3 S25 ADQLADESLEstRRM
1 0 S28-p LADESLEstRRMLQL
1 1 T29-p ADESLEstRRMLQLV
0 1 S39 MLQLVEESKDAGIRT
0 12 K40 LQLVEESKDAGIRTL
0 1 K69 EGMDQINKDMKEAEK
0 3 K72 DQINKDMKEAEKNLT
0 3 K76 KDMKEAEKNLTDLGK
0 1 K76 KDMKEAEKNLTDLGK
0 2 K102 LKSSDAYKKAWGNNQ
0 3 K103 KSSDAYKKAWGNNQD
0 1 S115 NQDGVVASQPARVVD
0 3 S130 EREQMAISGGFIRRV
4 5 T138-p GGFIRRVtNDARENE
0 2 S154 DENLEQVSGIIGNLR
0 6 K184 QIDRIMEKADsNKTR
12 0 S187-p RIMEKADsNKTRIDE
0 5 K189 MEKADsNKTRIDEAN
  SNAP-25 iso2  
S25 ADQLADESLESTRRM
S28 LADESLESTRRMLQL
T29 ADESLESTRRMLQLV
S39 MLQLVEESKDAGIRT
K40 LQLVEESKDAGIRTL
Q69 EGMNHINQDMKEAEk
K72 NHINQDMKEAEkNLK
K76 QDMKEAEKNLKDLGK
K76-ac QDMKEAEkNLKDLGK
K102 LKSSDAYKKAWGNNQ
K103 KSSDAYKKAWGNNQD
S115 NQDGVVASQPARVVD
S130 EREQMAISGGFIRRV
T138 GGFIRRVTNDARENE
S154 DENLEQVSGIIGNLR
K184 QIDRIMEKADSNKTR
S187 RIMEKADSNKTRIDE
K189 MEKADSNKTRIDEAN
  mouse

 
S25-p ADQLADEsLEStRRM
S28 LADEsLEStRRMLQL
T29-p ADEsLEStRRMLQLV
S39-p MLQLVEEskDAGIRT
K40-ub LQLVEEskDAGIRTL
K69-ub EGMDQINkDMkEAEk
K72-ub DQINkDMkEAEkNLT
K76-ub kDMkEAEkNLTDLGK
K76 kDMkEAEKNLTDLGK
K102 LKSSDAYKkAWGNNQ
K103-ub KSSDAYKkAWGNNQD
S115-p NQDGVVAsQPARVVD
S130-p EREQMAIsGGFIRRV
T138-p GGFIRRVtNDARENE
S154-p DENLEQVsGIIGNLR
K184-ub QIDRIMEkADsNkTR
S187-p RIMEkADsNkTRIDE
K189-ub MEkADsNkTRIDEAN
  rat

 
S25 ADQLADESLESTRRM
S28 LADESLESTRRMLQL
T29 ADESLESTRRMLQLV
S39 MLQLVEESkDAGIRT
K40-ub LQLVEESkDAGIRTL
K69 EGMDQINKDMkEAEK
K72-ub DQINKDMkEAEKNLT
K76 KDMkEAEKNLTDLGK
K76 KDMkEAEKNLTDLGK
K102-ub LKSSDAYkkAWGNNQ
K103-ub KSSDAYkkAWGNNQD
S115 NQDGVVASQPARVVD
S130 EREQMAISGGFIRRV
T138-p GGFIRRVtNDARENE
S154 DENLEQVSGIIGNLR
K184-ub QIDRIMEkADsNkTR
S187-p RIMEkADsNkTRIDE
K189-ub MEkADsNkTRIDEAN
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