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Protein Page:
VAMP3 (human)
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
VAMP3 SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. Belongs to the synaptobrevin family. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, integral
Chromosomal Location of Human Ortholog: 1p36.23
Cellular Component: apical plasma membrane; cell junction; cell surface; clathrin coated vesicle membrane; clathrin-coated vesicle; cytosol; integral to membrane; intracellular; intracellular membrane-bound organelle; neuron projection; plasma membrane; recycling endosome; secretory granule; SNARE complex; synapse
Molecular Function: protein binding; SNAP receptor activity; SNARE binding; syntaxin-1 binding
Biological Process: calcium ion-dependent exocytosis; exocytosis; Golgi to plasma membrane protein transport; positive regulation of immunoglobulin secretion; positive regulation of receptor recycling; protein complex assembly; retrograde transport, endosome to Golgi; vesicle docking during exocytosis; vesicle fusion; vesicle-mediated transport
Reference #:  Q15836 (UniProtKB)
Alt. Names/Synonyms: CEB; Cellubrevin; SYB3; Synaptobrevin-3; VAMP-3; VAMP3; Vesicle-associated membrane protein 3; vesicle-associated membrane protein 3 (cellubrevin)
Gene Symbols: VAMP3
Molecular weight: 11,309 Da
Basal Isoelectric point: 8.89  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

VAMP3

Protein Structure Not Found.


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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


 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

 
0 2 S2‑p ______MstGPTAAt
0 1 T3‑p _____MstGPTAAtG
0 1 T6 __MstGPTAAtGsNR
0 1 T9‑p stGPTAAtGsNRRLQ
0 6 S11‑p GPTAAtGsNRRLQQt
0 1 T18‑p sNRRLQQtQNQVDEV
0 92 K35‑ub IMRVNVDkVLERDQk
0 89 K42‑ub kVLERDQkLsELDDR
0 32 S44‑p LERDQkLsELDDRAD
0 45 S58‑p DALQAGAsQFETsAA
0 10 S63‑p GAsQFETsAAkLkRK
0 17 K66‑ub QFETsAAkLkRKYWW
0 5 K68‑ub ETsAAkLkRKYWWKN
  mouse

 
S2‑p ______MsTGVPSGS
S7 _MsTGVPSGSsAATG
S10‑p TGVPSGSsAATGsNR
T13 PSGSsAATGsNRRLQ
S15‑p GSsAATGsNRRLQQT
T22 sNRRLQQTQNQVDEV
K39‑ub IMRVNVDkVLERDQk
K46‑ub kVLERDQkLsELDDR
S48‑p LERDQkLsELDDRAD
S62‑p DALQAGAsQFETsAA
S67‑p GAsQFETsAAkLKRK
K70‑ub QFETsAAkLKRKYWW
K72 ETsAAkLKRKYWWKN
  rat

 
S2 ______MSTGVPSGS
T3 _____MSTGVPSGSS
S10 TGVPSGSSAATGSNR
T13 PSGSSAATGSNRRLQ
S15 GSSAATGSNRRLQQT
T22 SNRRLQQTQNQVDEV
K39 IMRVNVDKVLERDQK
K46 KVLERDQKLsELDDR
S48‑p LERDQKLsELDDRAD
S62‑p DALQAGAsQFETSAA
S67 GAsQFETSAAKLKRK
K70 QFETSAAKLKRKYWW
K72 ETSAAKLKRKYWWKN
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