CPLM-008430

Genbank Nucleotide ID

Vesicle-associated membrane protein 7

Protein Synonyms/Alias

VAMP-7; Synaptobrevin-like protein 1; Tetanus-insensitive VAMP; Ti-VAMP

Homo sapiens (Human)

Position	Peptide	Type	References
125	SENKGLDKVMETQAQ	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
137	QAQVDELKGIMVRNI	ubiquitination	[2, 3, 4, 5, 7, 8, 9]
160	RLELLIDKTENLVDS	ubiquitination	[2, 4, 5, 8, 9, 10]
172	VDSSVTFKTTSRNLA	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 10]

[1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[8] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[9] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[10] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]

Functional Description

Involved in the targeting and/or fusion of transport vesicles to their target membrane during transport of proteins from the early endosome to the lysosome. Required for heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion. Required for calcium regulated lysosomal exocytosis. Involved in the export of chylomicrons from the endoplasmic reticulum to the cis Golgi. Required for exocytosis of mediators during eosinophil and neutrophil degranulation, and target cell killing by natural killer cells. Required for focal exocytosis of late endocytic vesicles during phagosome formation.

DOMAIN 7 110 Longin.
DOMAIN 125 185 v-SNARE coiled-coil homology.
MOD_RES 2 2 N-acetylalanine; partial.

3D-structure; Acetylation; Alternative splicing; Cell junction; Coiled coil; Complete proteome; Cytoplasmic vesicle; Direct protein sequencing; Endoplasmic reticulum; Endosome; Exocytosis; Golgi apparatus; Lysosome; Membrane; Protein transport; Reference proteome; Signal-anchor; Synapse; Synaptosome; Transmembrane; Transmembrane helix; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0045177; C:apical part of cell; IEA:Compara.
GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
GO:0005794; C:Golgi apparatus; IDA:HPA.
GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
GO:0031902; C:late endosome membrane; ISS:UniProtKB.
GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
GO:0043005; C:neuron projection; ISS:UniProtKB.
GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
GO:0005886; C:plasma membrane; TAS:Reactome.
GO:0031201; C:SNARE complex; ISS:UniProtKB.
GO:0045202; C:synapse; IEA:UniProtKB-KW.
GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
GO:0017156; P:calcium ion-dependent exocytosis; ISS:UniProtKB.
GO:0008333; P:endosome to lysosome transport; IDA:UniProtKB.
GO:0043308; P:eosinophil degranulation; ISS:UniProtKB.
GO:0006888; P:ER to Golgi vesicle-mediated transport; ISS:UniProtKB.
GO:0043001; P:Golgi to plasma membrane protein transport; IEA:Compara.
GO:0043312; P:neutrophil degranulation; ISS:UniProtKB.
GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome.
GO:1900483; P:regulation of protein targeting to vacuolar membrane; IEA:Compara.
GO:0034197; P:triglyceride transport; IEA:Compara.
GO:0006906; P:vesicle fusion; IDA:UniProtKB.
GO:0048280; P:vesicle fusion with Golgi apparatus; IEA:Compara.

IPR011012; Longin-like_dom.
IPR010908; Longin_dom.
IPR001388; Synaptobrevin.

PF13774; Longin
PF00957; Synaptobrevin

PS50859; LONGIN
PS00417; SYNAPTOBREVIN
PS50892; V_SNARE

PR00219; SYNAPTOBREVN.