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Protein Page:
VAMP2 (human)
rdtyret
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
VAMP2 a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein SNAP25 are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. Thought to participate in neurotransmitter release at a step between docking and fusion. The protein forms a stable complex with syntaxin, synaptosomal-associated protein, 25 kD, and synaptotagmin. It also forms a distinct complex with synaptophysin. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, integral; Motility/polarity/chemotaxis; Vesicle
Chromosomal Location of Human Ortholog: 17p13.1
Cellular Component: cell junction; clathrin-coated vesicle; cytoplasmic vesicle; cytosol; integral to plasma membrane; intracellular membrane-bound organelle; membrane; neuron projection; perinuclear region of cytoplasm; plasma membrane; secretory granule; secretory granule membrane; SNARE complex; synapse; synaptic vesicle; synaptic vesicle membrane; terminal button; trans-Golgi network; vesicle; voltage-gated potassium channel complex; zymogen granule membrane
Molecular Function: calcium-dependent protein binding; calmodulin binding; identical protein binding; myosin binding; phospholipid binding; protein binding; protein C-terminus binding; protein complex binding; protein self-association; SNAP receptor activity; SNARE binding; syntaxin binding; syntaxin-1 binding
Biological Process: calcium ion-dependent exocytosis; cellular protein metabolic process; cellular response to insulin stimulus; energy reserve metabolic process; eosinophil degranulation; exocytosis; glutamate secretion; Golgi to plasma membrane protein transport; natural killer cell degranulation; neurotransmitter secretion; neutrophil degranulation; post-Golgi vesicle-mediated transport; protein complex assembly; protein transport; regulation of exocytosis; regulation of insulin secretion; response to glucose stimulus; synaptic transmission; synaptic vesicle exocytosis; vesicle fusion; vesicle-mediated transport
Reference #:  P63027 (UniProtKB)
Alt. Names/Synonyms: FLJ11460; SYB2; synaptobrevin 2; Synaptobrevin-2; VAMP-2; VAMP2; vesicle associated membrane protein 2; Vesicle-associated membrane protein 2; vesicle-associated membrane protein 2 (synaptobrevin 2)
Gene Symbols: VAMP2
Molecular weight: 12,663 Da
Basal Isoelectric point: 7.84  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

VAMP2

Protein Structure Not Found.


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Modification Sites and Domains  
Click here to view other types of protein modifications

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: 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.


 HTP 

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


       human

 
1 0 T35 SNRRLQQTQAQVDEV
0 101 K52‑ub IMRVNVDkVLERDQk
0 98 K59‑ub kVLERDQkLsELDDR
1 29 S61‑p LERDQkLsELDDRAD
0 46 S75‑p DALQAGAsQFEtsAA
0 2 T79‑p AGAsQFEtsAAkLkR
0 10 S80‑p GAsQFEtsAAkLkRK
0 17 K83‑ub QFEtsAAkLkRKYWW
0 6 K85‑ub EtsAAkLkRKYWWKN
  mouse

 
T35‑p SNRRLQQtQAQVDEV
K52‑ub IMRVNVDkVLERDQk
K59‑ub kVLERDQkLsELDDR
S61‑p LERDQkLsELDDRAD
S75‑p DALQAGAsQFEtsAA
T79‑p AGAsQFEtsAAkLKR
S80‑p GAsQFEtsAAkLKRK
K83‑ub QFEtsAAkLKRKYWW
K85 EtsAAkLKRKYWWKN
  rat

 
T35 SNRRLQQTQAQVDEV
K52‑ub IMRVNVDkVLERDQk
K59‑ub kVLERDQkLsELDDR
S61‑p LERDQkLsELDDRAD
S75‑p DALQAGAsQFETSAA
T79 AGAsQFETSAAKLkR
S80 GAsQFETSAAKLkRK
K83 QFETSAAKLkRKYWW
K85‑ub ETSAAKLkRKYWWKN
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