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Protein

Vesicle-associated membrane protein 2

Gene

VAMP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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

Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:G66-31833-MONOMER.
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-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

HGNCiHGNC:12643. VAMP2.

Subcellular locationi

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

GO - Cellular componenti

Complete GO annotation...

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
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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP63027.
MaxQBiP63027.
PaxDbiP63027.
PeptideAtlasiP63027.
PRIDEiP63027.
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.

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

WithEntry#Exp.IntActNotes
D2KHQ92EBI-520113,EBI-7604762From a different organism.
FA7GBG32EBI-520113,EBI-7604673From a different organism.
PicalmO550122EBI-520113,EBI-915601From a different organism.
PRKD3O948067EBI-520113,EBI-1255366
SNAP29O957215EBI-520113,EBI-490676
STX4Q128465EBI-520113,EBI-744942

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. 75 interactors.
DIPiDIP-39072N.
IntActiP63027. 17 interactors.
MINTiMINT-4824900.
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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FIEX-ray2.10C/D22-57[»]
3FIIX-ray2.17B27-57[»]
3RK2X-ray2.20A/E28-60[»]
3RK3X-ray3.50A28-60[»]
3RL0X-ray3.80A/E/I/M/Q/U/Y/c28-60[»]
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
Contains 1 v-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0860. Eukaryota.
COG5143. LUCA.
GeneTreeiENSGT00550000074449.
HOGENOMiHOG000042711.
HOVERGENiHBG006675.
InParanoidiP63027.
KOiK13504.
PhylomeDBiP63027.
TreeFamiTF313666.

Family and domain databases

Gene3Di1.10.3840.10. 1 hit.
InterProiIPR001388. Synaptobrevin.
IPR016444. Synaptobrevin/VAMP.
[Graphical view]
PfamiPF00957. Synaptobrevin. 1 hit.
[Graphical view]
PIRSFiPIRSF005409. Synaptobrevin_euk. 1 hit.
PRINTSiPR00219. SYNAPTOBREVN.
PROSITEiPS00417. SYNAPTOBREVIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FIEX-ray2.10C/D22-57[»]
3FIIX-ray2.17B27-57[»]
3RK2X-ray2.20A/E28-60[»]
3RK3X-ray3.50A28-60[»]
3RL0X-ray3.80A/E/I/M/Q/U/Y/c28-60[»]
DisProtiDP00069.
ProteinModelPortaliP63027.
SMRiP63027.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112711. 75 interactors.
DIPiDIP-39072N.
IntActiP63027. 17 interactors.
MINTiMINT-4824900.
STRINGi9606.ENSP00000314214.

Chemistry databases

ChEMBLiCHEMBL2364160.
DrugBankiDB00042. Botulinum Toxin Type B.

Protein family/group databases

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

PTM databases

iPTMnetiP63027.
PhosphoSitePlusiP63027.
SwissPalmiP63027.

Polymorphism and mutation databases

BioMutaiVAMP2.
DMDMi288558837.

Proteomic databases

EPDiP63027.
MaxQBiP63027.
PaxDbiP63027.
PeptideAtlasiP63027.
PRIDEiP63027.
TopDownProteomicsiP63027.

Protocols and materials databases

DNASUi6844.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6844.
DisGeNETi6844.
GeneCardsiVAMP2.
HGNCiHGNC:12643. VAMP2.
MIMi185881. gene.
neXtProtiNX_P63027.
OpenTargetsiENSG00000220205.
PharmGKBiPA37267.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0860. Eukaryota.
COG5143. LUCA.
GeneTreeiENSGT00550000074449.
HOGENOMiHOG000042711.
HOVERGENiHBG006675.
InParanoidiP63027.
KOiK13504.
PhylomeDBiP63027.
TreeFamiTF313666.

Enzyme and pathway databases

BioCyciZFISH:G66-31833-MONOMER.
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-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.

Miscellaneous databases

ChiTaRSiVAMP2. human.
EvolutionaryTraceiP63027.
GeneWikiiVAMP2.
GenomeRNAii6844.
PROiP63027.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000220205.
CleanExiHS_VAMP2.
ExpressionAtlasiP63027. baseline and differential.
GenevisibleiP63027. HS.

Family and domain databases

Gene3Di1.10.3840.10. 1 hit.
InterProiIPR001388. Synaptobrevin.
IPR016444. Synaptobrevin/VAMP.
[Graphical view]
PfamiPF00957. Synaptobrevin. 1 hit.
[Graphical view]
PIRSFiPIRSF005409. Synaptobrevin_euk. 1 hit.
PRINTSiPR00219. SYNAPTOBREVN.
PROSITEiPS00417. SYNAPTOBREVIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVAMP2_HUMAN
AccessioniPrimary (citable) accession number: P63027
Secondary accession number(s): P19065, Q9BUC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: February 9, 2010
Last modified: November 30, 2016
This is version 130 of the entry and version 3 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.