P63027 (VAMP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vesicle-associated membrane protein 2
Short name=VAMP-2

Alternative name(s):
Synaptobrevin-2

Gene names

Name:	VAMP2
Synonyms:	SYB2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	116 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 vesicle › secretory vesicle › synaptic vesicle membrane; Single-pass type IV membrane protein. Cell junction › synapse › synaptosome. 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 component	Cell junction Cytoplasmic vesicle Membrane Synapse Synaptosome
Domain	Coiled coil Transmembrane Transmembrane helix
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular membrane organization Traceable author statement. Source: Reactome energy reserve metabolic process Traceable author statement. Source: Reactome glutamate secretion Traceable author statement. Source: Reactome neurotransmitter secretion Traceable author statement. Source: Reactome post-Golgi vesicle-mediated transport Traceable author statement. Source: Reactome regulation of insulin secretion Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	SNARE complex Inferred from direct assay PubMed 19546860. Source: UniProtKB cell junction Inferred from electronic annotation. Source: UniProtKB-KW 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 to plasma membrane Traceable author statement Ref.1. Source: ProtInc neuron projection Inferred from electronic annotation. Source: UniProtKB-SubCell secretory granule membrane Traceable author statement. Source: Reactome synaptic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Picalm	O55012	2	EBI-520113,EBI-915601	From a different organism.
PRKD3	O94806	7	EBI-520113,EBI-1255366

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 116

115

Vesicle-associated membrane protein 2

PRO_0000206723

Regions

Topological domain

2 – 94

93

Cytoplasmic Potential

Transmembrane

95 – 114

20

Helical; Anchor for type IV membrane protein; Potential

Topological domain

115 – 116

2

Vesicular Potential

Domain

31 – 91

61

v-SNARE coiled-coil homology

Amino acid modifications

Modified residue

2

1

N-acetylserine By similarity

Modified residue

75

1

Phosphoserine By similarity

Experimental info

Sequence conflict

116

1

T → S in AAA60604. Ref.1

Sequence conflict

116

1

T → S in CAA12385. Ref.2

Sequence conflict

116

1

T → S in AAF15551. Ref.3

Secondary structure

1

.

.

.

.

.

.

116

Helix Strand Turn

Details...

Beta strand

34 – 36

3

Turn

47 – 49

3

Helix

50 – 53

4

Sequences

	Sequence		Length	Mass (Da)
	P63027 [UniParc]. Last modified February 9, 2010. Version 3. Checksum: 9CD679C4F6F1B5A8	FASTA	116	12,663
	10 20 30 40 50 60 MSATAATAPP AAPAGEGGPP APPPNLTSNR RLQQTQAQVD EVVDIMRVNV DKVLERDQKL 70 80 90 100 110 SELDDRADAL QAGASQFETS AAKLKRKYWW KNLKMMIILG VICAIILIII IVYFST

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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].
[10]	"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 , 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.

IPI

IPI00553138.

PIR

B38315.

RefSeq

NP_055047.2. NM_014232.2.

UniGene

Hs.25348.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FIE	X-ray	2.10	C/D	22-57	[»]
3FII	X-ray	2.17	B	27-57	[»]
3RK2	X-ray	2.20	A/E	28-60	[»]
3RK3	X-ray	3.50	A	28-60	[»]
3RL0	X-ray	3.80	A/E/I/M/Q/U/Y/c	28-60	[»]

DisProt

DP00069.

ProteinModelPortal

P63027.

SMR

P63027. Positions 30-116.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-39072N.

IntAct

P63027. 5 interactions.

STRING

9606.ENSP00000314214.

Protein family/group databases

TCDB

1.F.1.1.1. synaptosomal vesicle fusion pore (SVF-Pore) family.

PTM databases

PhosphoSite

P63027.

Polymorphism databases

DMDM

288558837.

Proteomic databases

PRIDE

P63027.

Protocols and materials databases

DNASU

6844.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000316509; ENSP00000314214; ENSG00000220205.

GeneID

6844.

KEGG

hsa:6844.

UCSC

uc010cnt.1. human.

Organism-specific databases

CTD

6844.

GeneCards

GC17M008054.

HGNC

HGNC:12643. VAMP2.

MIM

185881. gene.

neXtProt

NX_P63027.

PharmGKB

PA37267.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HOG000042711.

HOVERGEN

HBG006675.

KO

K13504.

OrthoDB

EOG43JC6B.

Enzyme and pathway databases

Pathway_Interaction_DB

botulinumtoxinpathway. Effects of Botulinum toxin.
insulin_glucose_pathway. Insulin-mediated glucose transport.

Reactome

REACT_111217. Metabolism.
REACT_11123. Membrane Trafficking.
REACT_116125. Disease.
REACT_13685. Neuronal System.

Gene expression databases

ArrayExpress

P63027.

Bgee

P63027.

CleanEx

HS_VAMP2.

Genevestigator

P63027.

GermOnline

ENSG00000179036. Homo sapiens.

Family and domain databases

InterPro

IPR001388. Synaptobrevin.
IPR016444. Synaptobrevin_met/fun.
[Graphical view]

Pfam

PF00957. Synaptobrevin. 1 hit.
[Graphical view]

PIRSF

PIRSF005409. Synaptobrevin_euk. 1 hit.

PRINTS

PR00219. SYNAPTOBREVN.

PROSITE

PS00417. SYNAPTOBREVIN. 1 hit.
PS50892. V_SNARE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

VAMP2. human.

DrugBank

DB00042. Botulinum Toxin Type B.

EvolutionaryTrace

P63027.

GenomeRNAi

6844.

NextBio

26719.

SOURCE

Search...

Entry information

Entry name

VAMP2_HUMAN

Accession

Primary (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:	April 3, 2013
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.