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Basic Information:

Symbol	VAPB
Synonyms	UNQ484/PRO983
Protein Name	Vesicle-associated membrane protein-associated protein B/C (VAMP-B/VAMP-C) (VAMP-associated protein B/C) (VAP-B/VAP-C)
Species	Human
Entrez ID	9217
Uniprot ID	O95292
Membrane Contact Site	ER-Endosome; Endosome-ER
Location (from literature)	ER
Cell line/Tissue	HeLa cells; COS-7 cells; MelJuSo cells; HEK293T cells
Experimental Method	Low throughput experimental methods
Protein Sequence
More related results

Complex Information:

Complex ID	Subunit of complex	Subcellular location	Species	More
CMCS00008	VAPA; VAPB; SNX2	ER-Endosome; Endosome-ER	Human	more
CMCS00009	VAPA; VAPB; OSBP; PI(4)P	ER-Endosome; Endosome-ER	Human	more
CMCS00011	VAPA; VAPB; OSBPL1A	ER-Endosome; Endosome-ER	Human	more
CMCS00023	VAPA; VAPB; STARD3	ER-Endosome; Endosome-ER	Human	more
CMCS00024	VAPA; VAPB; STARD3NL	ER-Endosome; Endosome-ER	Human	more
CMCS00026	VAPB; VAPA; VPS13C	ER-Endosome; Endosome-ER	Human	more
CMCS00027	VAPB; VAPA; OSBPL1A; RAB7A; RILP	ER-Endosome; Endosome-ER	Human	more
CMCS00167	OSBPL10; OSBPL9; VAPA; VAPB; PI(4)P	ER-Endosome; Endosome-ER	Human	more
CMCS00071	VAPA; VAPB; CERT1	ER-Endosome; Endosome-ER	Human	more

Expression Overview of VAPB:

Homology Information of VAPB:

Uniprot ID	O95292
EggNOG	KOG0439
HOGENOM	CLU_032848_0_1_1
OrthoDB	122649at2759
TreeFam	TF317024
GeneTree	ENSGT00940000155769

References:

Pubmed ID	27419871
DOI	10.1016/j.cell.2016.06.037
Description	Endosome-ER Contacts Control Actin Nucleation and Retromer Function through VAP-Dependent Regulation of PI4P.
Description of experimental evidence	The protein was validated by TALENs, fluorescence microscopy, western blotting and phosphoinositide analysis in HeLa cells, COS-7 cells, and these results reveal a role of PI5P in retromer-/WASH-dependent budding from endosomes.
More related results

Pubmed ID	24105263
DOI	10.1242/jcs.139295
Description	STARD3 or STARD3NL and VAP form a novel molecular tether between late endosomes and the ER.The ER interaction partners of STARD3 and STARD3NL in LE-ER MCS are VAP-A and VAP-B.
Description of experimental evidence	The protein was validated by immunoprecipitation, electron microscopy, immunofluorescence, in situ proximity ligation assay, mSDS-PAGE and western blot analysis in HeLa cells.
More related results

Pubmed ID	28377464
DOI	10.15252/embj.201695917
Description	Corroborating this, in vitro reconstitution assays indicated that STARD3 and its ER-anchored partner, Vesicle-associated membrane protein-associated protein (VAP), assemble into a machine that allows a highly efficient transport of cholesterol within membrane contacts.
Description of experimental evidence	The protein was validated by immunofluorescence, colocalization analysis, filipin staining, GFP-D4, filipin co-staining, flotation experiments, electron microscopy and stereology in Hela cells, and the complex allows a highly efficient transport of cholesterol within membrane contacts.
More related results

Pubmed ID	27270042
DOI	10.1016/j.devcel.2016.05.005
Description	This sterol traffic depends on interaction between ER-localized VAP and endosomal oxysterol-binding protein ORP1L, and is required for the formation of ILVs within the MVB and thus for the spatial regulation of EGFR signaling.
Description of experimental evidence	The protein was validated by electron microscopy, florescence Imaging, western blotting, immunoprecipitation, and quantitative RT-PCR in HeLa cells, which has important role in the sterol traffic.
More related results

Pubmed ID	19564404
DOI	10.1083/jcb.200811005
Description	We show that cholesterol in LEs is sensed by ORP1L, which transmits this information to the Rab7–RILP–p150Glued complex through the formation of ER–LE membrane contact sites (MCSs). At these sites, the ER protein VAP enters the Rab7–RILP complex to control p150Glued binding and positioning of LEs.
Description of experimental evidence	The protein was validated by microscopy, FLIM, Immuno-EM and filipin stainings in MelJuSo cells, and these data explain how the ER and cholesterol control the association of LEs with motor proteins and their positioning in cells.
More related results

Pubmed ID	34817532
DOI	10.1083/jcb.202103141
Description	ORP10 localizes in a PI4P-dependent manner at ER–endosome membrane contact sites tethered by ORP9 and VAP, where it mediates countertransport of PI4P and PS.
Description of experimental evidence	The protein was validated by immunofluorescence microscopy, live-cell imaging, image analysis, coimmunoprecipitation and LC-MS/MS in HeLa cells, HEK293T cells and COS-7 cells.
More related results

Pubmed ID	30093493
DOI	10.1083/jcb.201807019
Description	An FFAT motif, a short amino acid sequence known to interact with the ER VAMP-associated protein (VAP), is present in the Vps13α region of both proteins as previously noted.; These findings not only confirm the role of the FFAT motif in anchoring these proteins to the ER but also indicate that binding sites for mitochondria (in VPS13A), late endosomes/lysosomes (in VPS13C), and lipid droplets (both proteins) are localized in the C-terminal regions of the two proteins.
Description of experimental evidence	The protein was validated by bioinformatic analysis, mass spectrometry, FRET assays, correlative fluorescence, EM microscopy, Image processing, analysis and statistics in HeLa cells and COS-7 cells which has the lipid transport roles.
More related results

Pubmed ID	33124732
DOI	10.15252/embj.2019104369
Description	The endoplasmic reticulum possesses three major receptors, VAP‐A, VAP‐B, and MOSPD2, which interact with proteins at the surface of other organelles to build contacts; onventional FFATs (illustrated here with STARD11/CERT) which allow the formation of a stable complex between VAPs/MOSPD2 and thus the formation of MCSs.
Description of experimental evidence	The protein was validated by pull‐down assays, immunoprecipitation,SDS–PAGE, western blot, CIP treatment, coomassie blue staining, mass spectrometry analysis, immunofluorescence and colocalization analysis in HeLa cells.
More related results