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Protein

Vesicle-associated membrane protein 2

Gene

VAMP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in the targeting and/or fusion of transport vesicles to their target membrane. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1.By similarity

Caution

A structure of a fragment of this protein in complex with the catalytic domain of C.botulinum neurotoxin type B (BoNT/B, botB) was reported; because of the lack of clear and continuous electron density for the VAMP2 peptide in the complex structure, the paper was retracted (PubMed:10932255, PubMed:19578378). However this protein is a substrate for BoNT/B (PubMed:7803399, PubMed:22289120).1 Publication3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei58 – 59(Microbial infection) Cleavage; by C.botulinum neurotoxin type F (BoNT/F, botF)1 Publication2
Sitei76 – 77(Microbial infection) Cleavage; by C.botulinum neurotoxin type D (BoNT/D, botD)1 Publication2
Sitei76 – 77(Microbial infection) Cleavage; by C.tetani toxin (tetX)1 Publication2

GO - Molecular functioni

  • calcium-dependent protein binding Source: ParkinsonsUK-UCL
  • calmodulin binding Source: ParkinsonsUK-UCL
  • phospholipid binding Source: ParkinsonsUK-UCL
  • protein self-association Source: ParkinsonsUK-UCL
  • SNAP receptor activity Source: GO_Central
  • SNARE binding Source: ParkinsonsUK-UCL
  • syntaxin-1 binding Source: ParkinsonsUK-UCL
  • syntaxin binding Source: UniProtKB

GO - Biological processi

Enzyme and pathway databases

ReactomeiR-HSA-1445148 Translocation of GLUT4 to the plasma membrane
R-HSA-181429 Serotonin Neurotransmitter Release Cycle
R-HSA-181430 Norepinephrine Neurotransmitter Release Cycle
R-HSA-210500 Glutamate Neurotransmitter Release Cycle
R-HSA-212676 Dopamine Neurotransmitter Release Cycle
R-HSA-264642 Acetylcholine Neurotransmitter Release Cycle
R-HSA-264876 Insulin processing
R-HSA-421837 Clathrin derived vesicle budding
R-HSA-422356 Regulation of insulin secretion
R-HSA-432720 Lysosome Vesicle Biogenesis
R-HSA-432722 Golgi Associated Vesicle Biogenesis
R-HSA-449836 Other interleukin signaling
R-HSA-5250955 Toxicity of botulinum toxin type D (BoNT/D)
R-HSA-5250958 Toxicity of botulinum toxin type B (BoNT/B)
R-HSA-5250981 Toxicity of botulinum toxin type F (BoNT/F)
R-HSA-5250982 Toxicity of tetanus toxin (TeNT)
R-HSA-5250989 Toxicity of botulinum toxin type G (BoNT/G)
R-HSA-8856825 Cargo recognition for clathrin-mediated endocytosis
R-HSA-8856828 Clathrin-mediated endocytosis
R-HSA-888590 GABA synthesis, release, reuptake and degradation

Protein family/group databases

TCDBi1.F.1.1.1 the synaptosomal vesicle fusion pore (svf-pore) family

Names & Taxonomyi

Protein namesi
Recommended name:
Vesicle-associated membrane protein 2
Short name:
VAMP-2
Alternative name(s):
Synaptobrevin-2
Gene namesi
Name:VAMP2
Synonyms:SYB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000220205.8
HGNCiHGNC:12643 VAMP2
MIMi185881 gene
neXtProtiNX_P63027

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 94CytoplasmicSequence analysisAdd BLAST93
Transmembranei95 – 114Helical; Anchor for type IV membrane proteinSequence analysisAdd BLAST20
Topological domaini115 – 116VesicularSequence analysis2

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasmic vesicle, Membrane, Synapse, Synaptosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi28S → A: Significant loss of phosphorylation; when associated with A-61, A-75 and A-80. 1 Publication1
Mutagenesisi41E → A: 70% reduction in cleavage by C.botulinum neurotoxin type F (BoNT/F, botF). 1 Publication1
Mutagenesisi50V → D: 65% reduction in cleavage by BoNT/F. 1 Publication1
Mutagenesisi53 – 54VL → DD: 98% reduction in cleavage by BoNT/F. 1 Publication2
Mutagenesisi53V → A: Wild-type cleavage by BoNT/F. 1 Publication1
Mutagenesisi53V → D: 90% reduction in cleavage by BoNT/F. 1 Publication1
Mutagenesisi61S → A: Significant loss of phosphorylation; when associated with A-28, A-75 and A-80. 1 Publication1
Mutagenesisi75S → A: Significant loss of phosphorylation; when associated with A-28, A-61 and A-80. 1 Publication1
Mutagenesisi80S → A: Significant loss of phosphorylation; when associated with A-28, A-61 and A-75. 1 Publication1

Organism-specific databases

DisGeNETi6844
OpenTargetsiENSG00000220205
PharmGKBiPA37267

Chemistry databases

ChEMBLiCHEMBL2364160
DrugBankiDB00042 Botulinum Toxin Type B

Polymorphism and mutation databases

BioMutaiVAMP2
DMDMi288558837

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002067232 – 116Vesicle-associated membrane protein 2Add BLAST115

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1

Post-translational modificationi

Phosphorylated by PRKCZ in vitro and this phosphorylation is increased in the presence of WDFY2.1 Publication
(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type B (BoNT/B, botB) which hydrolyzes the 76-Gln-|-Phe-77 bond and probably inhibits neurotransmitter release (PubMed:7803399).1 Publication1 Publication
(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type D (BoNT/D, botD) which probably hydrolyzes the 59-Lys-|-Leu-60 bond and inhibits neurotransmitter release (PubMed:22289120). Note that humans are not known to be infected by C.botulinum type D.Curated1 Publication
(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type F (BoNT/F, botF) which hydrolyzes the 58-Gln-|-Lys-59 bond and probably inhibits neurotransmitter release (PubMed:19543288).2 Publications
(Microbial infection) Targeted and hydrolyzed by C.tetani tetanus toxin (tetX) which hydrolyzes the 76-Gln-|-Phe-77 bond and probably inhibits neurotransmitter release (PubMed:7803399).1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP63027
MaxQBiP63027
PaxDbiP63027
PeptideAtlasiP63027
PRIDEiP63027
ProteomicsDBi57471
TopDownProteomicsiP63027

PTM databases

iPTMnetiP63027
PhosphoSitePlusiP63027
SwissPalmiP63027

Expressioni

Tissue specificityi

Nervous system and skeletal muscle.1 Publication

Gene expression databases

BgeeiENSG00000220205
CleanExiHS_VAMP2
ExpressionAtlasiP63027 baseline and differential
GenevisibleiP63027 HS

Organism-specific databases

HPAiCAB078785

Interactioni

Subunit structurei

Interacts (via N-terminus) with KCNB1 (via N-terminus and C-terminus); stimulates the channel inactivation rate of KCNB1 (By similarity). Part of the SNARE core complex containing SNAP25, VAMP2 and STX1A. This complex binds to CPLX1. Interacts with BVES and STX4 (By similarity). Interacts with VAPA and VAPB. Interacts with WDFY2, PRKCZ and PRKCI (PubMed:17313651). Forms a complex with WDFY2 and PRKCZ (PubMed:17313651).By similarity2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • calcium-dependent protein binding Source: ParkinsonsUK-UCL
  • calmodulin binding Source: ParkinsonsUK-UCL
  • protein self-association Source: ParkinsonsUK-UCL
  • SNAP receptor activity Source: GO_Central
  • SNARE binding Source: ParkinsonsUK-UCL
  • syntaxin-1 binding Source: ParkinsonsUK-UCL
  • syntaxin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112711, 79 interactors
CORUMiP63027
DIPiDIP-39072N
IntActiP63027, 31 interactors
MINTiP63027
STRINGi9606.ENSP00000314214

Structurei

Secondary structure

1116
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 36Combined sources3
Turni47 – 49Combined sources3
Helixi50 – 53Combined sources4

3D structure databases

DisProtiDP00069
ProteinModelPortaliP63027
SMRiP63027
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63027

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 91v-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd BLAST61

Sequence similaritiesi

Belongs to the synaptobrevin family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0860 Eukaryota
COG5143 LUCA
GeneTreeiENSGT00550000074449
HOGENOMiHOG000042711
HOVERGENiHBG006675
InParanoidiP63027
KOiK13504
PhylomeDBiP63027
TreeFamiTF313666

Family and domain databases

InterProiView protein in InterPro
IPR001388 Synaptobrevin
IPR016444 Synaptobrevin/VAMP
IPR028717 VAMP2
PANTHERiPTHR21136:SF91 PTHR21136:SF91, 1 hit
PfamiView protein in Pfam
PF00957 Synaptobrevin, 1 hit
PIRSFiPIRSF005409 Synaptobrevin_euk, 1 hit
PRINTSiPR00219 SYNAPTOBREVN
PROSITEiView protein in PROSITE
PS00417 SYNAPTOBREVIN, 1 hit
PS50892 V_SNARE, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P63027-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSATAATAPP AAPAGEGGPP APPPNLTSNR RLQQTQAQVD EVVDIMRVNV
60 70 80 90 100
DKVLERDQKL SELDDRADAL QAGASQFETS AAKLKRKYWW KNLKMMIILG
110
VICAIILIII IVYFST
Length:116
Mass (Da):12,663
Last modified:February 9, 2010 - v3
Checksum:i9CD679C4F6F1B5A8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti116T → S in AAA60604 (PubMed:1976629).Curated1
Sequence conflicti116T → S in CAA12385 (Ref. 2) Curated1
Sequence conflicti116T → S in AAF15551 (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36205
, M36201, M36202, M36203, M36204 Genomic DNA Translation: AAA60604.1
AJ225044 mRNA Translation: CAA12385.1
AF135372 Genomic DNA Translation: AAF15551.1
AK289555 mRNA Translation: BAF82244.1
CH471108 Genomic DNA Translation: EAW90087.1
BC002737 mRNA Translation: AAH02737.3
BC019608 mRNA Translation: AAH19608.1
BC033870 mRNA Translation: AAH33870.1
CCDSiCCDS32561.1
PIRiB38315
RefSeqiNP_055047.2, NM_014232.2
UniGeneiHs.25348

Genome annotation databases

EnsembliENST00000316509; ENSP00000314214; ENSG00000220205
GeneIDi6844
KEGGihsa:6844
UCSCiuc010cnt.2 human

Similar proteinsi

Entry informationi

Entry nameiVAMP2_HUMAN
AccessioniPrimary (citable) accession number: P63027
Secondary accession number(s): P19065, Q9BUC2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: February 9, 2010
Last modified: July 18, 2018
This is version 142 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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