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P63027 (VAMP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vesicle-associated membrane protein 2

Short name=VAMP-2
Alternative name(s):
Synaptobrevin-2
Gene names
Name:VAMP2
Synonyms:SYB2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length116 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the targeting and/or fusion of transport vesicles to their target membrane.

Subunit structure

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.

Subcellular location

Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane; Single-pass type IV membrane protein. Cell junctionsynapsesynaptosome. Note: Neuronal synaptic vesicles.

Tissue specificity

Nervous system and skeletal muscle. Ref.7

Sequence similarities

Belongs to the synaptobrevin family.

Contains 1 v-SNARE coiled-coil homology domain.

Ontologies

Keywords
   Cellular componentCell junction
Cytoplasmic vesicle
Membrane
Synapse
Synaptosome
   DomainCoiled coil
Transmembrane
Transmembrane helix
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion-dependent exocytosis

Inferred from electronic annotation. Source: InterPro

cellular protein metabolic process

Traceable author statement. Source: Reactome

energy reserve metabolic process

Traceable author statement. Source: Reactome

glutamate secretion

Traceable author statement. Source: Reactome

membrane organization

Traceable author statement. Source: Reactome

neurotransmitter secretion

Traceable author statement. Source: Reactome

post-Golgi vesicle-mediated transport

Traceable author statement. Source: Reactome

regulation of exocytosis

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of insulin secretion

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

synaptic transmission

Traceable author statement. Source: Reactome

vesicle fusion

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentSNARE complex

Inferred from direct assay PubMed 19546860. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

clathrin-coated vesicle

Inferred from direct assay PubMed 19478182. Source: UniProtKB

clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane

Traceable author statement. Source: Reactome

clathrin-sculpted glutamate transport vesicle membrane

Traceable author statement. Source: Reactome

clathrin-sculpted monoamine transport vesicle membrane

Traceable author statement. Source: Reactome

endocytic vesicle membrane

Traceable author statement. Source: Reactome

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

membrane

Inferred from direct assay PubMed 22375059. Source: MGI

neuron projection

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Traceable author statement. Source: Reactome

secretory granule membrane

Traceable author statement. Source: Reactome

synaptic vesicle

Inferred from Biological aspect of Ancestor. Source: RefGenome

synaptic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionSNAP receptor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction PubMed 19478182PubMed 9920726. Source: UniProtKB

syntaxin binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 116115Vesicle-associated membrane protein 2
PRO_0000206723

Regions

Topological domain2 – 9493Cytoplasmic Potential
Transmembrane95 – 11420Helical; Anchor for type IV membrane protein; Potential
Topological domain115 – 1162Vesicular Potential
Domain31 – 9161v-SNARE coiled-coil homology

Amino acid modifications

Modified residue21N-acetylserine By similarity

Experimental info

Sequence conflict1161T → S in AAA60604. Ref.1
Sequence conflict1161T → S in CAA12385. Ref.2
Sequence conflict1161T → S in AAF15551. Ref.3

Secondary structure

...... 116
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P63027 [UniParc].

Last modified February 9, 2010. Version 3.
Checksum: 9CD679C4F6F1B5A8

FASTA11612,663
        10         20         30         40         50         60 
MSATAATAPP AAPAGEGGPP APPPNLTSNR RLQQTQAQVD EVVDIMRVNV DKVLERDQKL 

        70         80         90        100        110 
SELDDRADAL QAGASQFETS AAKLKRKYWW KNLKMMIILG VICAIILIII IVYFST 

« Hide

References

« Hide 'large scale' references
[1]"Structures and chromosomal localizations of two human genes encoding synaptobrevins 1 and 2."
Archer B.T. III, Oezcelik T., Jahn R., Francke U., Suedhof T.C.
J. Biol. Chem. 265:17267-17273(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Expression of VAMP genes in human neutrophils."
Nabokina S.M., Lazo P.A., Mollinedo F.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Peripheral blood.
[3]"Genomic structure of human SYB2 gene."
Taruscio D., Zoraqi K.G., Falbo V.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Blood.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cerebellum.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Neuroblastoma and Testis.
[7]"Insulin-responsive tissues contain the core complex protein SNAP-25 (synaptosomal-associated protein 25) A and B isoforms in addition to syntaxin 4 and synaptobrevins 1 and 2."
Jagadish M.N., Fernandez C.S., Hewish D.R., Macaulay S.L., Gough K.H., Grusovin J., Verkuylen A., Cosgrove L., Alafaci A., Frenkel M.J., Ward C.W.
Biochem. J. 317:945-954(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane."
Kutay U., Ahnert-Hilger G., Hartmann E., Wiedenmann B., Rapoport T.A.
EMBO J. 14:217-223(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY.
[9]"Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution."
Hanson M.A., Stevens R.C.
Nat. Struct. Biol. 7:687-692(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 34-89 IN COMPLEX WITH BOTB.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M36205 expand/collapse EMBL AC list , 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.
CCDSCCDS32561.1.
PIRB38315.
RefSeqNP_055047.2. NM_014232.2.
UniGeneHs.25348.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00069.
ProteinModelPortalP63027.
SMRP63027. Positions 30-116.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112711. 61 interactions.
DIPDIP-39072N.
IntActP63027. 7 interactions.
MINTMINT-4824900.
STRING9606.ENSP00000314214.

Chemistry

ChEMBLCHEMBL2364160.
DrugBankDB00042. Botulinum Toxin Type B.

Protein family/group databases

TCDB1.F.1.1.1. the synaptosomal vesicle fusion pore (svf-pore) family.

PTM databases

PhosphoSiteP63027.

Polymorphism databases

DMDM288558837.

Proteomic databases

MaxQBP63027.
PRIDEP63027.

Protocols and materials databases

DNASU6844.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000316509; ENSP00000314214; ENSG00000220205.
GeneID6844.
KEGGhsa:6844.
UCSCuc010cnt.1. human.

Organism-specific databases

CTD6844.
GeneCardsGC17M008062.
HGNCHGNC:12643. VAMP2.
MIM185881. gene.
neXtProtNX_P63027.
PharmGKBPA37267.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000042711.
HOVERGENHBG006675.
KOK13504.
OrthoDBEOG7MSMRJ.
PhylomeDBP63027.
TreeFamTF313666.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_11123. Membrane Trafficking.
REACT_116125. Disease.
REACT_13685. Neuronal System.
REACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP63027.
BgeeP63027.
CleanExHS_VAMP2.
GenevestigatorP63027.

Family and domain databases

InterProIPR001388. Synaptobrevin.
IPR016444. Synaptobrevin/VAMP_met/fun.
[Graphical view]
PfamPF00957. Synaptobrevin. 1 hit.
[Graphical view]
PIRSFPIRSF005409. Synaptobrevin_euk. 1 hit.
PRINTSPR00219. SYNAPTOBREVN.
PROSITEPS00417. SYNAPTOBREVIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSVAMP2. human.
EvolutionaryTraceP63027.
GeneWikiVAMP2.
GenomeRNAi6844.
NextBio26719.
PROP63027.
SOURCESearch...

Entry information

Entry nameVAMP2_HUMAN
AccessionPrimary (citable) accession number: P63027
Secondary accession number(s): P19065, Q9BUC2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: February 9, 2010
Last modified: July 9, 2014
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM