Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 153 (16 Oct 2019)
Sequence version 2 (23 Jan 2007)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Vesicle-associated membrane protein 2

Gene

Vamp2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Involved in the targeting and/or fusion of transport vesicles to their target membrane (Probable). Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 (PubMed:19690160).By similarity1 Publication1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei58 – 59(Microbial infection) Cleavage; by C.botulinum neurotoxin type F (BoNT/F, botF)1 Publication2
Sitei59 – 60(Microbial infection) Cleavage; by C.botulinum neurotoxin type D (BoNT/D, botD)1 Publication2
Sitei66 – 67(Microbial infection) Cleavage; by C.botulinum neurotoxin type X (BoNT/X)1 Publication2
Sitei76 – 77(Microbial infection) Cleavage; by C.botulinum neurotoxin type B (BoNT/B, botB)1 Publication2
Sitei76 – 77(Microbial infection) Cleavage; by C.tetani tetanus toxin (tetX)1 Publication2
Sitei81 – 82(Microbial infection) Cleavage; by C.botulinum neurotoxin type G (BoNT/G, botG)1 Publication2

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-181429 Serotonin Neurotransmitter Release Cycle
R-RNO-181430 Norepinephrine Neurotransmitter Release Cycle
R-RNO-210500 Glutamate Neurotransmitter Release Cycle
R-RNO-212676 Dopamine Neurotransmitter Release Cycle
R-RNO-264642 Acetylcholine Neurotransmitter Release Cycle
R-RNO-432720 Lysosome Vesicle Biogenesis
R-RNO-432722 Golgi Associated Vesicle Biogenesis
R-RNO-449836 Other interleukin signaling
R-RNO-8856825 Cargo recognition for clathrin-mediated endocytosis
R-RNO-8856828 Clathrin-mediated endocytosis
R-RNO-888590 GABA synthesis, release, reuptake and degradation
R-RNO-9609523 Insertion of tail-anchored proteins into the endoplasmic reticulum membrane

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Vesicle-associated membrane protein 2
Short name:
VAMP-2
Alternative name(s):
Synaptobrevin-2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Vamp2
Synonyms:Syb2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 10

Organism-specific databases

Rat genome database

More...
RGDi
3949 Vamp2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini2 – 94CytoplasmicSequence analysisAdd BLAST93
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei95 – 114Helical; Anchor for type IV membrane proteinSequence analysisAdd BLAST20
Topological domaini115 – 116VesicularSequence analysis2

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti

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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002067262 – 116Vesicle-associated membrane protein 2Add BLAST115

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by PRKCZ in vitro and this phosphorylation is increased in the presence of WDFY2.By similarity
(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type B (BoNT/B, botB) which hydrolyzes the 76-Gln-|-Phe-77 bond and inhibits neurotransmitter release (PubMed:1331807).1 Publication
(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type D (BoNT/D, botD) which hydrolyzes the 59-Lys-|-Leu-60 bond and inhibits neurotransmitter release (PubMed:8175689).1 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:8505288).1 Publication1 Publication
(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type G (BoNT/G, botG) which hydrolyzes the 81-Ala-|-Ala-82 bond and probably inhibits neurotransmitter release (PubMed:8505288).1 Publication
(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type X (BoNT/X) which hydrolyzes the 66-Arg-|-Ala-67 bond and probably inhibits neurotransmitter release (PubMed:28770820). It remains unknown whether BoNT/X is ever produced, or what organisms it targets.1 Publication
(Microbial infection) Targeted and hydrolyzed by C.tetani toxin (tetX) which hydrolyzes the 76-Gln-|-Phe-77 bond and inhibits neurotransmitter release (PubMed:1331807).1 Publication1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P63045

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P63045

PRoteomics IDEntifications database

More...
PRIDEi
P63045

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P63045

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P63045

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P63045

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P63045

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Nervous system specific. A higher level expression is seen in the brain as compared to the spinal cord (PubMed:2472388). Expressed in hippocampal neurons (PubMed:19196426).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000006989 Expressed in 10 organ(s), highest expression level in brain

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P63045 RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts (via N-terminus) with KCNB1 (via N-terminus and C-terminus); stimulates the channel inactivation rate of KCNB1 (PubMed:19690160). Part of the SNARE core complex containing SNAP25, VAMP2 and STX1A (PubMed:19196426). This complex binds to CPLX1.

Interacts with BVES and STX4.

Interacts with VAPA and VAPB.

Interacts with WDFY2, PRKCZ and PRKCI (By similarity).

Forms a complex with WDFY2 and PRKCZ (By similarity).

Interacts with SEPT8; the interaction inhibits interaction of VAMP2 with SYP (PubMed:19196426).

Interacts with SYP; the interaction is inhibited by interaction with SEPT8 (PubMed:19196426).

Interacts with PICALM (By similarity).

Interacts with alpha-synuclein/SNCA (By similarity).

Interacts with STX3 (By similarity).

By similarity2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
246926, 3 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P63045

Database of interacting proteins

More...
DIPi
DIP-35503N

Protein interaction database and analysis system

More...
IntActi
P63045, 23 interactors

Molecular INTeraction database

More...
MINTi
P63045

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000054114

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1116
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P63045

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P63045

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini31 – 91v-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd BLAST61

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni92 – 116Required for interaction with SEPT81 PublicationAdd BLAST25

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the synaptobrevin family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0860 Eukaryota
COG5143 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000158370

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000042711

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P63045

KEGG Orthology (KO)

More...
KOi
K13504

Identification of Orthologs from Complete Genome Data

More...
OMAi
MIIIMCA

Database of Orthologous Groups

More...
OrthoDBi
1606985at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P63045

Family and domain databases

Database of protein disorder

More...
DisProti
DP00622

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001388 Synaptobrevin
IPR016444 Synaptobrevin/VAMP
IPR042855 V_SNARE_CC
IPR028717 VAMP2

The PANTHER Classification System

More...
PANTHERi
PTHR45701 PTHR45701, 1 hit
PTHR45701:SF15 PTHR45701:SF15, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00957 Synaptobrevin, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF005409 Synaptobrevin_euk, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00219 SYNAPTOBREVN

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00417 SYNAPTOBREVIN, 1 hit
PS50892 V_SNARE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P63045-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSATAATVPP AAPAGEGGPP APPPNLTSNR RLQQTQAQVD EVVDIMRVNV
60 70 80 90 100
DKVLERDQKL SELDDRADAL QAGASQFETS AAKLKRKYWW KNLKMMIILG
110
VICAIILIII IVYFST
Length:116
Mass (Da):12,691
Last modified:January 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4A0D0D56B5409D0A
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M24105 mRNA Translation: AAA42321.1
BC074003 mRNA Translation: AAH74003.1

Protein sequence database of the Protein Information Resource

More...
PIRi
B34288

NCBI Reference Sequences

More...
RefSeqi
NP_036795.1, NM_012663.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000057295; ENSRNOP00000054114; ENSRNOG00000006989

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
24803

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:24803

UCSC genome browser

More...
UCSCi
RGD:3949 rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24105 mRNA Translation: AAA42321.1
BC074003 mRNA Translation: AAH74003.1
PIRiB34288
RefSeqiNP_036795.1, NM_012663.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KILX-ray2.30A28-92[»]
1N7SX-ray1.45A28-88[»]
1SFCX-ray2.40A/E/I1-96[»]
2BU0model-A25-88[»]
2KOGNMR-A1-116[»]
2N1TNMR-A25-93[»]
3HD7X-ray3.40A/E30-116[»]
3IPDX-ray4.80A/E30-116[»]
3J96electron microscopy7.60K28-89[»]
3J97electron microscopy7.80K28-89[»]
3J98electron microscopy8.40K28-89[»]
3J99electron microscopy8.20K28-89[»]
5CCGX-ray3.50A/G28-89[»]
5CCHX-ray3.60A28-89[»]
5CCIX-ray4.10A28-89[»]
5W5CX-ray1.85A28-66[»]
5W5DX-ray2.50A28-66[»]
6A30X-ray2.79P87-92[»]
6IP1electron microscopy3.90A1-94[»]
6MDMelectron microscopy4.40J1-89[»]
6MDNelectron microscopy4.40J1-72[»]
6MTIelectron microscopy10.40A/E/I/M/Q/U28-89[»]
SMRiP63045
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi246926, 3 interactors
CORUMiP63045
DIPiDIP-35503N
IntActiP63045, 23 interactors
MINTiP63045
STRINGi10116.ENSRNOP00000054114

PTM databases

iPTMnetiP63045
PhosphoSitePlusiP63045
SwissPalmiP63045

Proteomic databases

jPOSTiP63045
PaxDbiP63045
PRIDEiP63045

Genome annotation databases

EnsembliENSRNOT00000057295; ENSRNOP00000054114; ENSRNOG00000006989
GeneIDi24803
KEGGirno:24803
UCSCiRGD:3949 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6844
RGDi3949 Vamp2

Phylogenomic databases

eggNOGiKOG0860 Eukaryota
COG5143 LUCA
GeneTreeiENSGT00940000158370
HOGENOMiHOG000042711
InParanoidiP63045
KOiK13504
OMAiMIIIMCA
OrthoDBi1606985at2759
PhylomeDBiP63045

Enzyme and pathway databases

ReactomeiR-RNO-181429 Serotonin Neurotransmitter Release Cycle
R-RNO-181430 Norepinephrine Neurotransmitter Release Cycle
R-RNO-210500 Glutamate Neurotransmitter Release Cycle
R-RNO-212676 Dopamine Neurotransmitter Release Cycle
R-RNO-264642 Acetylcholine Neurotransmitter Release Cycle
R-RNO-432720 Lysosome Vesicle Biogenesis
R-RNO-432722 Golgi Associated Vesicle Biogenesis
R-RNO-449836 Other interleukin signaling
R-RNO-8856825 Cargo recognition for clathrin-mediated endocytosis
R-RNO-8856828 Clathrin-mediated endocytosis
R-RNO-888590 GABA synthesis, release, reuptake and degradation
R-RNO-9609523 Insertion of tail-anchored proteins into the endoplasmic reticulum membrane

Miscellaneous databases

EvolutionaryTraceiP63045
PMAP-CutDBiP63045

Protein Ontology

More...
PROi
PR:P63045

Gene expression databases

BgeeiENSRNOG00000006989 Expressed in 10 organ(s), highest expression level in brain
GenevisibleiP63045 RN

Family and domain databases

DisProtiDP00622
InterProiView protein in InterPro
IPR001388 Synaptobrevin
IPR016444 Synaptobrevin/VAMP
IPR042855 V_SNARE_CC
IPR028717 VAMP2
PANTHERiPTHR45701 PTHR45701, 1 hit
PTHR45701:SF15 PTHR45701:SF15, 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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiVAMP2_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P63045
Secondary accession number(s): Q64357
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: October 16, 2019
This is version 153 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again