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P63044 (VAMP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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. Ref.1

Subunit structure

Part of the SNARE core complex containing SNAP25, VAMP2 and STX1A. This complex binds to CPLX1. Interacts with VAPA and VAPB By similarity. Interacts with BVES and STX4. Ref.4 Ref.7

Subcellular location

Cytoplasmic vesicle › secretory vesicle › synaptic vesicle membrane; Single-pass type IV membrane protein. Cell junction › synapse › synaptosome. Note: Neuronal synaptic vesicles.

Sequence similarities

Belongs to the synaptobrevin family.

Contains 1 v-SNARE coiled-coil homology domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Cdc42P607662EBI-521920,EBI-81763

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 116115Vesicle-associated membrane protein 2
PRO_0000206725

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
Modified residue751Phosphoserine Ref.6

Sequences

Sequence LengthMass (Da)Tools
P63044 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 4A0D0D56B5409D0A

FASTA11612,691
        10         20         30         40         50         60 
MSATAATVPP AAPAGEGGPP APPPNLTSNR RLQQTQAQVD EVVDIMRVNV DKVLERDQKL 

        70         80         90        100        110 
SELDDRADAL QAGASQFETS AAKLKRKYWW KNLKMMIILG VICAIILIII IVYFST

« Hide

References

« Hide 'large scale' references
[1]"Vesicle-associated membrane protein 2 plays a specific role in the insulin-dependent trafficking of the facilitative glucose transporter GLUT4 in 3T3-L1 adipocytes."
Martin L.B., Shewan A., Millar C.A., Gould G.W., James D.E.
J. Biol. Chem. 273:1444-1452(1998) [PubMed: 9430681] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Brain.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"Doc2beta is a novel Munc18c-interacting partner and positive effector of syntaxin 4-mediated exocytosis."
Ke B., Oh E., Thurmond D.C.
J. Biol. Chem. 282:21786-21797(2007) [PubMed: 17548353] [Abstract]
Cited for: INTERACTION WITH STX4.
[5]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 31-47 AND 60-83, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[6]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, MASS SPECTROMETRY.
Tissue: Brain cortex.
[7]"Identification of a novel Bves function: regulation of vesicular transport."
Hager H.A., Roberts R.J., Cross E.E., Proux-Gillardeaux V., Bader D.M.
EMBO J. 29:532-545(2010) [PubMed: 20057356] [Abstract]
Cited for: INTERACTION WITH BVES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U60150 mRNA. Translation: AAB03463.1.
AK090178 mRNA. Translation: BAC41125.1.
BC055105 mRNA. Translation: AAH55105.1.
IPIIPI00229703.
RefSeqNP_033523.1. NM_009497.3.
UniGeneMm.28643.

3D structure databases

ProteinModelPortalP63044.
SMRP63044. Positions 30-116.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29065N.
IntActP63044. 7 interactions.
MINTMINT-2411573.
STRINGP63044.

PTM databases

PhosphoSiteP63044.

Proteomic databases

PRIDEP63044.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021273; ENSMUSP00000021273; ENSMUSG00000020894.
GeneID22318.
KEGGmmu:22318.

Organism-specific databases

CTD6844.
MGIMGI:1313277. Vamp2.

Phylogenomic databases

HOVERGENHBG006675.
OMAMSAPEGS.
OrthoDBEOG43JC6B.
PhylomeDBP63044.

Enzyme and pathway databases

ReactomeREACT_112621. Metabolism.

Gene expression databases

ArrayExpressP63044.
BgeeP63044.
CleanExMM_VAMP2.
GenevestigatorP63044.
GermOnlineENSMUSG00000020894. Mus musculus.

Family and domain databases

InterProIPR001388. Synaptobrevin.
IPR016444. Synaptobrevin_met/fun.
[Graphical view]
KOK13504.
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

NextBio302529.
SOURCESearch...

Entry information

Entry nameVAMP2_MOUSE
AccessionPrimary (citable) accession number: P63044
Secondary accession number(s): Q64357
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: November 16, 2011
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents