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Q15836 (VAMP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 3

Short name=VAMP-3
Alternative name(s):
Cellubrevin
Short name=CEB
Synaptobrevin-3
Gene names
Name:VAMP3
Synonyms:SYB3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length100 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. Ref.6

Subunit structure

Interacts with BVES (via the C-terminus cytoplasmic tail) By similarity. Interacts with BCAP31; involved in VAMP3 export from the endoplasmic reticulum By similarity.

Subcellular location

Membrane; Single-pass type IV membrane protein Probable. Cell junctionsynapsesynaptosome By similarity.

Sequence similarities

Belongs to the synaptobrevin family.

Contains 1 v-SNARE coiled-coil homology domain.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell junction
Membrane
Synapse
Synaptosome
   DomainCoiled coil
Transmembrane
Transmembrane helix
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi to plasma membrane protein transport

Inferred from electronic annotation. Source: Ensembl

calcium ion-dependent exocytosis

Inferred from electronic annotation. Source: Ensembl

exocytosis

Traceable author statement Ref.1. Source: ProtInc

membrane fusion

Traceable author statement Ref.1. Source: ProtInc

neurotransmitter secretion

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of receptor recycling

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex assembly

Traceable author statement Ref.1. Source: ProtInc

retrograde transport, endosome to Golgi

Inferred from direct assay Ref.6. Source: UniProtKB

substrate adhesion-dependent cell spreading

Inferred from sequence or structural similarity. Source: UniProtKB

vesicle docking involved in exocytosis

Traceable author statement Ref.1. Source: ProtInc

vesicle fusion

Inferred from Biological aspect of Ancestor. Source: RefGenome

vesicle-mediated transport

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentSNARE complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

apical plasma membrane

Inferred from electronic annotation. Source: Ensembl

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

clathrin-coated vesicle

Inferred from direct assay PubMed 19478182. Source: UniProtKB

clathrin-coated vesicle membrane

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Traceable author statement Ref.1. Source: ProtInc

neuron projection

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

recycling endosome

Inferred from direct assay PubMed 19061864. Source: MGI

secretory granule

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionSNAP receptor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

SNARE binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PicalmO550122EBI-722343,EBI-915601From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.8
Chain2 – 10099Vesicle-associated membrane protein 3
PRO_0000206728

Regions

Topological domain2 – 7776Cytoplasmic Potential
Transmembrane78 – 9821Helical; Anchor for type IV membrane protein; Potential
Topological domain99 – 1002Vesicular Potential
Domain14 – 7461v-SNARE coiled-coil homology

Amino acid modifications

Modified residue21N-acetylserine Ref.8

Experimental info

Sequence conflict771K → E in AAH05941. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q15836 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 347E9163157AFF42

FASTA10011,309
        10         20         30         40         50         60 
MSTGPTAATG SNRRLQQTQN QVDEVVDIMR VNVDKVLERD QKLSELDDRA DALQAGASQF 

        70         80         90        100 
ETSAAKLKRK YWWKNCKMWA IGITVLVIFI IIIIVWVVSS 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a cellubrevin/vesicle associated membrane protein 3 homologue in human platelets."
Bernstein A.M., Whiteheart S.W.
Blood 93:571-579(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Kidney and Urinary bladder.
[5]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-14.
Tissue: Platelet.
[6]"A syntaxin 10-SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells."
Ganley I.G., Espinosa E., Pfeffer S.R.
J. Cell Biol. 180:159-172(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U64520 mRNA. Translation: AAB05814.1.
BT007327 mRNA. Translation: AAP35991.1.
Z98884 Genomic DNA. Translation: CAB63146.1.
BC003570 mRNA. Translation: AAH03570.1.
BC005941 mRNA. Translation: AAH05941.1.
BC007050 mRNA. Translation: AAH07050.1.
RefSeqNP_004772.1. NM_004781.3.
UniGeneHs.66708.

3D structure databases

ProteinModelPortalQ15836.
SMRQ15836. Positions 11-75.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114747. 17 interactions.
IntActQ15836. 11 interactions.
STRING9606.ENSP00000054666.

PTM databases

PhosphoSiteQ15836.

Polymorphism databases

DMDM2501082.

Proteomic databases

PaxDbQ15836.
PRIDEQ15836.

Protocols and materials databases

DNASU9341.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000054666; ENSP00000054666; ENSG00000049245.
GeneID9341.
KEGGhsa:9341.
UCSCuc001aol.3. human.

Organism-specific databases

CTD9341.
GeneCardsGC01P007765.
HGNCHGNC:12644. VAMP3.
MIM603657. gene.
neXtProtNX_Q15836.
PharmGKBPA37268.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG266115.
HOGENOMHOG000042711.
HOVERGENHBG006675.
InParanoidQ15836.
KOK13505.
OMAFTHACAF.
OrthoDBEOG7MSMRJ.
PhylomeDBQ15836.
TreeFamTF313666.

Gene expression databases

ArrayExpressQ15836.
BgeeQ15836.
CleanExHS_VAMP3.
GenevestigatorQ15836.

Family and domain databases

InterProIPR001388. Synaptobrevin.
IPR016444. Synaptobrevin/VAMP_met/fun.
IPR028706. VAMP3.
[Graphical view]
PANTHERPTHR21136:SF37. PTHR21136:SF37. 1 hit.
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

ChiTaRSVAMP3. human.
GeneWikiVAMP3.
GenomeRNAi9341.
NextBio34987.
PMAP-CutDBQ15836.
PROQ15836.
SOURCESearch...

Entry information

Entry nameVAMP3_HUMAN
AccessionPrimary (citable) accession number: Q15836
Secondary accession number(s): Q9BRV4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 131 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

MIM cross-references

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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM