Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Vesicle-associated membrane protein 7  

UniProtKB / Swiss-Prot ID :  VAMP7_HUMAN

Gene Name (Synonyms) : 
VAMP7, SYBL1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasmic vesicle, secretory vesicle membrane; Single-pass type IV membrane protein (By similarity). Golgi apparatus, trans-Golgi network membrane; Single-pass type IV membrane protein (By similarity). Late endosome membrane; Single- pass type IV membr 

Protein Function :  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. 

Transmembrane Topology (topPTM) : VAMP7_HUMAN 

Protein Sequence MAILFAVVARGTTILAKHAWCGGNFLEVTEQILAKIPSENNKLTYSHGNYLFHYICQDRIVYLCITDDDF...
Predicted Secondary Structure  -
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine; partial.---MAILFA
---
13.75UniProtKB
Link
12PhosphothreonineVARGTTILA
12.71HPRD
Link
13PhosphothreonineARGTTILAK
19.47HPRD
Link
125Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KGLDKVMET
48.82Phosphositeplus
Link
137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VDELKGIMV
44.32Phosphositeplus
Link
160Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LLIDKTENL
51.23Phosphositeplus
Link
167PhosphoserineNLVDSSVTF
21.16HPRD
Link
168PhosphoserineLVDSSVTFK
22.25HPRD
Link
168PhosphoserineLVDSSVTFK
22.25Phosphositeplus
Link
168PhosphoserineLVDSSVTFK
22.25SysPTM
Link
168Phosphoserine.LVDSSVTFK
22.25UniProtKB
Link
172Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SVTFKTTSR
41.34Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
STX1A_HUMANin vitro
in vivo
HPRD:02084HPRD12853575
STX4_HUMANin vivoHPRD:02084HPRD14993220
DNJC5_HUMANin vitroHPRD:02084HPRD15610015
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures