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Vesicle-associated membrane protein 2 (VAMP-2) (Synaptobrevin-2)

 VAMP2_HUMAN             Reviewed;         116 AA.
P63027; P19065; Q9BUC2;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
09-FEB-2010, sequence version 3.
22-NOV-2017, entry version 137.
RecName: Full=Vesicle-associated membrane protein 2;
Short=VAMP-2;
AltName: Full=Synaptobrevin-2;
Name=VAMP2; Synonyms=SYB2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1976629;
Archer B.T. III, Oezcelik T., Jahn R., Francke U., Suedhof T.C.;
"Structures and chromosomal localizations of two human genes encoding
synaptobrevins 1 and 2.";
J. Biol. Chem. 265:17267-17273(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Peripheral blood;
Nabokina S.M., Lazo P.A., Mollinedo F.;
"Expression of VAMP genes in human neutrophils.";
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Blood;
Taruscio D., Zoraqi K.G., Falbo V.;
"Genomic structure of human SYB2 gene.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Neuroblastoma, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
TISSUE SPECIFICITY.
PubMed=8760387; DOI=10.1042/bj3170945;
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.;
"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.";
Biochem. J. 317:945-954(1996).
[8]
TOPOLOGY.
PubMed=7835332;
Kutay U., Ahnert-Hilger G., Hartmann E., Wiedenmann B., Rapoport T.A.;
"Transport route for synaptobrevin via a novel pathway of insertion
into the endoplasmic reticulum membrane.";
EMBO J. 14:217-223(1995).
[9]
INTERACTION WITH WDFY2; PRKCZ AND PRKCI, COMPLEX FORMATION WITH WDFY2
AND PRKCZ, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF
SER-28; SER-61; SER-75 AND SER-80.
PubMed=17313651; DOI=10.1111/j.1742-4658.2007.05702.x;
Fritzius T., Frey A.D., Schweneker M., Mayer D., Moelling K.;
"WD-repeat-propeller-FYVE protein, ProF, binds VAMP2 and protein
kinase Czeta.";
FEBS J. 274:1552-1566(2007).
[10]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 34-89 IN COMPLEX WITH BOTB.
PubMed=10932255; DOI=10.1038/77997;
Hanson M.A., Stevens R.C.;
"Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin
type B at 2.0 A resolution.";
Nat. Struct. Biol. 7:687-692(2000).
-!- FUNCTION: 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. {ECO:0000250|UniProtKB:P63045}.
-!- SUBUNIT: 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).
{ECO:0000250|UniProtKB:P63044, ECO:0000250|UniProtKB:P63045,
ECO:0000269|PubMed:10932255, ECO:0000269|PubMed:17313651}.
-!- INTERACTION:
D2KHQ9:- (xeno); NbExp=2; IntAct=EBI-520113, EBI-7604762;
Q57236:bont (xeno); NbExp=3; IntAct=EBI-520113, EBI-15790260;
A7GBG3:F (xeno); NbExp=2; IntAct=EBI-520113, EBI-7604673;
O55012:Picalm (xeno); NbExp=2; IntAct=EBI-520113, EBI-915601;
O94806:PRKD3; NbExp=7; IntAct=EBI-520113, EBI-1255366;
O95721:SNAP29; NbExp=5; IntAct=EBI-520113, EBI-490676;
Q12846:STX4; NbExp=5; IntAct=EBI-520113, EBI-744942;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
synaptic vesicle membrane; Single-pass type IV membrane protein.
Cell junction, synapse, synaptosome. Cell membrane
{ECO:0000250|UniProtKB:P63045}. Note=Neuronal synaptic vesicles.
Colocalizes with PRKCZ and WDFY2 in intracellular vesicles
(PubMed:17313651). {ECO:0000269|PubMed:17313651}.
-!- TISSUE SPECIFICITY: Nervous system and skeletal muscle.
{ECO:0000269|PubMed:8760387}.
-!- PTM: Phosphorylated by PRKCZ in vitro and this phosphorylation is
increased in the presence of WDFY2. {ECO:0000269|PubMed:17313651}.
-!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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EMBL; M36205; AAA60604.1; -; Genomic_DNA.
EMBL; M36201; AAA60604.1; JOINED; Genomic_DNA.
EMBL; M36202; AAA60604.1; JOINED; Genomic_DNA.
EMBL; M36203; AAA60604.1; JOINED; Genomic_DNA.
EMBL; M36204; AAA60604.1; JOINED; Genomic_DNA.
EMBL; AJ225044; CAA12385.1; -; mRNA.
EMBL; AF135372; AAF15551.1; -; Genomic_DNA.
EMBL; AK289555; BAF82244.1; -; mRNA.
EMBL; CH471108; EAW90087.1; -; Genomic_DNA.
EMBL; BC002737; AAH02737.3; -; mRNA.
EMBL; BC019608; AAH19608.1; -; mRNA.
EMBL; BC033870; AAH33870.1; -; mRNA.
CCDS; CCDS32561.1; -.
PIR; B38315; B38315.
RefSeq; NP_055047.2; NM_014232.2.
UniGene; Hs.25348; -.
PDB; 3FIE; X-ray; 2.10 A; C/D=22-57.
PDB; 3FII; X-ray; 2.17 A; B=27-57.
PDB; 3RK2; X-ray; 2.20 A; A/E=28-60.
PDB; 3RK3; X-ray; 3.50 A; A=28-60.
PDB; 3RL0; X-ray; 3.80 A; A/E/I/M/Q/U/Y/c=28-60.
PDBsum; 3FIE; -.
PDBsum; 3FII; -.
PDBsum; 3RK2; -.
PDBsum; 3RK3; -.
PDBsum; 3RL0; -.
DisProt; DP00069; -.
ProteinModelPortal; P63027; -.
SMR; P63027; -.
BioGrid; 112711; 78.
CORUM; P63027; -.
DIP; DIP-39072N; -.
IntAct; P63027; 22.
MINT; MINT-4824900; -.
STRING; 9606.ENSP00000314214; -.
ChEMBL; CHEMBL2364160; -.
DrugBank; DB00042; Botulinum Toxin Type B.
TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family.
iPTMnet; P63027; -.
PhosphoSitePlus; P63027; -.
SwissPalm; P63027; -.
BioMuta; VAMP2; -.
DMDM; 288558837; -.
EPD; P63027; -.
MaxQB; P63027; -.
PaxDb; P63027; -.
PeptideAtlas; P63027; -.
PRIDE; P63027; -.
TopDownProteomics; P63027; -.
DNASU; 6844; -.
Ensembl; ENST00000316509; ENSP00000314214; ENSG00000220205.
GeneID; 6844; -.
KEGG; hsa:6844; -.
UCSC; uc010cnt.2; human.
CTD; 6844; -.
DisGeNET; 6844; -.
EuPathDB; HostDB:ENSG00000220205.8; -.
GeneCards; VAMP2; -.
HGNC; HGNC:12643; VAMP2.
HPA; CAB078785; -.
MIM; 185881; gene.
neXtProt; NX_P63027; -.
OpenTargets; ENSG00000220205; -.
PharmGKB; PA37267; -.
eggNOG; KOG0860; Eukaryota.
eggNOG; COG5143; LUCA.
GeneTree; ENSGT00550000074449; -.
HOGENOM; HOG000042711; -.
HOVERGEN; HBG006675; -.
InParanoid; P63027; -.
KO; K13504; -.
PhylomeDB; P63027; -.
TreeFam; TF313666; -.
Reactome; R-HSA-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-HSA-181429; Serotonin Neurotransmitter Release Cycle.
Reactome; R-HSA-181430; Norepinephrine Neurotransmitter Release Cycle.
Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle.
Reactome; R-HSA-212676; Dopamine Neurotransmitter Release Cycle.
Reactome; R-HSA-264642; Acetylcholine Neurotransmitter Release Cycle.
Reactome; R-HSA-264876; Insulin processing.
Reactome; R-HSA-421837; Clathrin derived vesicle budding.
Reactome; R-HSA-422356; Regulation of insulin secretion.
Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
Reactome; R-HSA-449836; Other interleukin signaling.
Reactome; R-HSA-5250955; Toxicity of botulinum toxin type D (BoNT/D).
Reactome; R-HSA-5250958; Toxicity of botulinum toxin type B (BoNT/B).
Reactome; R-HSA-5250981; Toxicity of botulinum toxin type F (BoNT/F).
Reactome; R-HSA-5250982; Toxicity of tetanus toxin (TeNT).
Reactome; R-HSA-5250989; Toxicity of botulinum toxin type G (BoNT/G).
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
Reactome; R-HSA-888590; GABA synthesis, release, reuptake and degradation.
ChiTaRS; VAMP2; human.
EvolutionaryTrace; P63027; -.
GeneWiki; VAMP2; -.
GenomeRNAi; 6844; -.
PRO; PR:P63027; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000220205; -.
CleanEx; HS_VAMP2; -.
ExpressionAtlas; P63027; baseline and differential.
Genevisible; P63027; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
GO; GO:0030665; C:clathrin-coated vesicle membrane; TAS:Reactome.
GO; GO:0061202; C:clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane; TAS:Reactome.
GO; GO:0060203; C:clathrin-sculpted glutamate transport vesicle membrane; TAS:Reactome.
GO; GO:0070083; C:clathrin-sculpted monoamine transport vesicle membrane; TAS:Reactome.
GO; GO:0031410; C:cytoplasmic vesicle; ISS:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:ParkinsonsUK-UCL.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; ISS:ParkinsonsUK-UCL.
GO; GO:0044306; C:neuron projection terminus; ISS:ParkinsonsUK-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:ParkinsonsUK-UCL.
GO; GO:0005886; C:plasma membrane; ISS:ParkinsonsUK-UCL.
GO; GO:0030141; C:secretory granule; ISS:ParkinsonsUK-UCL.
GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
GO; GO:0045202; C:synapse; ISS:ParkinsonsUK-UCL.
GO; GO:0008021; C:synaptic vesicle; ISS:ParkinsonsUK-UCL.
GO; GO:0030672; C:synaptic vesicle membrane; ISS:ParkinsonsUK-UCL.
GO; GO:0070044; C:synaptobrevin 2-SNAP-25-syntaxin-1a complex; ISS:ParkinsonsUK-UCL.
GO; GO:0070032; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex; ISS:ParkinsonsUK-UCL.
GO; GO:0070033; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex; ISS:ParkinsonsUK-UCL.
GO; GO:0005802; C:trans-Golgi network; ISS:ParkinsonsUK-UCL.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0042589; C:zymogen granule membrane; ISS:ParkinsonsUK-UCL.
GO; GO:0048306; F:calcium-dependent protein binding; ISS:ParkinsonsUK-UCL.
GO; GO:0005516; F:calmodulin binding; ISS:ParkinsonsUK-UCL.
GO; GO:0005543; F:phospholipid binding; ISS:ParkinsonsUK-UCL.
GO; GO:0043621; F:protein self-association; TAS:ParkinsonsUK-UCL.
GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
GO; GO:0000149; F:SNARE binding; ISS:ParkinsonsUK-UCL.
GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB.
GO; GO:0017075; F:syntaxin-1 binding; ISS:ParkinsonsUK-UCL.
GO; GO:0017156; P:calcium ion regulated exocytosis; ISS:ParkinsonsUK-UCL.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:ParkinsonsUK-UCL.
GO; GO:0043308; P:eosinophil degranulation; IMP:UniProtKB.
GO; GO:0006887; P:exocytosis; TAS:ParkinsonsUK-UCL.
GO; GO:0014047; P:glutamate secretion; TAS:Reactome.
GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISS:ParkinsonsUK-UCL.
GO; GO:0060291; P:long-term synaptic potentiation; ISS:ParkinsonsUK-UCL.
GO; GO:0061025; P:membrane fusion; ISS:ParkinsonsUK-UCL.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0007269; P:neurotransmitter secretion; TAS:Reactome.
GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:ParkinsonsUK-UCL.
GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0006461; P:protein complex assembly; ISS:ParkinsonsUK-UCL.
GO; GO:0015031; P:protein transport; ISS:ParkinsonsUK-UCL.
GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; ISS:UniProtKB.
GO; GO:0017157; P:regulation of exocytosis; ISS:ParkinsonsUK-UCL.
GO; GO:0060627; P:regulation of vesicle-mediated transport; ISS:ParkinsonsUK-UCL.
GO; GO:0009749; P:response to glucose; ISS:ParkinsonsUK-UCL.
GO; GO:0016079; P:synaptic vesicle exocytosis; ISS:ParkinsonsUK-UCL.
GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
GO; GO:0016192; P:vesicle-mediated transport; ISS:ParkinsonsUK-UCL.
InterPro; IPR001388; Synaptobrevin.
InterPro; IPR016444; Synaptobrevin/VAMP.
InterPro; IPR028717; VAMP2.
PANTHER; PTHR21136:SF91; PTHR21136:SF91; 1.
Pfam; PF00957; Synaptobrevin; 1.
PIRSF; PIRSF005409; Synaptobrevin_euk; 1.
PRINTS; PR00219; SYNAPTOBREVN.
PROSITE; PS00417; SYNAPTOBREVIN; 1.
PROSITE; PS50892; V_SNARE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell junction; Cell membrane; Coiled coil;
Complete proteome; Cytoplasmic vesicle; Membrane; Phosphoprotein;
Reference proteome; Synapse; Synaptosome; Transmembrane;
Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P63026}.
CHAIN 2 116 Vesicle-associated membrane protein 2.
/FTId=PRO_0000206723.
TOPO_DOM 2 94 Cytoplasmic. {ECO:0000255}.
TRANSMEM 95 114 Helical; Anchor for type IV membrane
protein. {ECO:0000255}.
TOPO_DOM 115 116 Vesicular. {ECO:0000255}.
DOMAIN 31 91 v-SNARE coiled-coil homology.
{ECO:0000255|PROSITE-ProRule:PRU00290}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P63026}.
MUTAGEN 28 28 S->A: Significant loss of
phosphorylation; when associated with A-
61, A-75 and A-80.
{ECO:0000269|PubMed:17313651}.
MUTAGEN 61 61 S->A: Significant loss of
phosphorylation; when associated with A-
28, A-75 and A-80.
{ECO:0000269|PubMed:17313651}.
MUTAGEN 75 75 S->A: Significant loss of
phosphorylation; when associated with A-
28, A-61 and A-80.
{ECO:0000269|PubMed:17313651}.
MUTAGEN 80 80 S->A: Significant loss of
phosphorylation; when associated with A-
28, A-61 and A-75.
{ECO:0000269|PubMed:17313651}.
CONFLICT 116 116 T -> S (in Ref. 1; AAA60604, 2; CAA12385
and 3; AAF15551). {ECO:0000305}.
STRAND 34 36 {ECO:0000244|PDB:3FIE}.
TURN 47 49 {ECO:0000244|PDB:3FIE}.
HELIX 50 53 {ECO:0000244|PDB:3FIE}.
SEQUENCE 116 AA; 12663 MW; 9CD679C4F6F1B5A8 CRC64;
MSATAATAPP AAPAGEGGPP APPPNLTSNR RLQQTQAQVD EVVDIMRVNV DKVLERDQKL
SELDDRADAL QAGASQFETS AAKLKRKYWW KNLKMMIILG VICAIILIII IVYFST


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EIAAB45607 Mouse,Mus musculus,Sybl1,Synaptobrevin-like protein 1,Vamp7,VAMP-7,Vesicle-associated membrane protein 7
EIAAB45598 CEB,Cellubrevin,Homo sapiens,Human,SYB3,Synaptobrevin-3,VAMP3,VAMP-3,Vesicle-associated membrane protein 3
EIAAB45620 33 kDa VAMP-associated protein,Homo sapiens,Human,VAMP-A,VAMP-associated protein A,VAP33,VAP-33,VAPA,VAP-A,Vesicle-associated membrane protein-associated protein A
EIAAB45622 33 kDa VAMP-associated protein,Rat,Rattus norvegicus,VAMP-A,VAMP-associated protein A,Vap33,VAP-33,Vapa,VAP-A,Vesicle-associated membrane protein-associated protein A
EIAAB45621 33 kDa VAMP-associated protein,Mouse,Mus musculus,VAMP-A,VAMP-associated protein A,Vap33,VAP-33,Vapa,VAP-A,Vesicle-associated membrane protein-associated protein A
EIAAB45627 Mouse,Mus musculus,VAMP-associated protein 33b,VAMP-associated protein B,VAMP-B,Vapb,VAP-B,Vesicle-associated membrane protein-associated protein B
EIAAB45626 Homo sapiens,Human,UNQ484_PRO983,VAMP-associated protein B_C,VAMP-B_VAMP-C,VAPB,VAP-B_VAP-C,Vesicle-associated membrane protein-associated protein B_C
EIAAB45628 Bos taurus,Bovine,VAMP-associated protein B,VAMP-B,VAPB,VAP-B,Vesicle-associated membrane protein-associated protein B
EIAAB45625 Rat,Rattus norvegicus,VAMP-associated protein B,VAMP-B,Vapb,VAP-B,Vesicle-associated membrane protein-associated protein B


 

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