MCS.ID	synonyms	gene.ID	gene.symbol	uniprot	species	MCS	location.literature.	cell.line.tissue	Experimental.Method	source.number	PMID-1	Description-1	Evidences-1	PMID-2	Description-2	Evidences-2	PMID-3	Description-3	Evidences-3	PMID-4	Description-4	Evidences-4	PMID-5	Description-5	Evidences-5	PMID-6	Description-6	Evidences-6	PMID-7	Description-7	Evidences-7	PMID-8	Description-8	Evidences-8	PMID-9	Description-9	Evidences-9	PMID-10	Description-10	Evidences-10	PMID-11	Description-11	Evidences-11	PMID-12	Description-12	Evidences-12
LMCS00371	hob; CG14967	38395	hob	Q9VZS7	Fruit fly	ER-PM; PM-ER	ER	Drosophila salivary glands	Low throughput experimental methods	1	34415038	The Hob proteins are novel and conserved lipid-binding proteins at ER–PM contact sites.	The protein was validated by yeast imaging, yeast protease protection assay, electron microscopy, sequence alignments, conservation analysis, protein expression, purification, lipid blots and confocal microscopy in drosophila salivary glands.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00521	Uvrag; CG6116	34735	Uvrag	Q9VK07	Fruit fly	ER-MT; MT-ER	NA	Drosophila S2 cells	Low throughput experimental methods	1	36323251	ER-mitochondrial contact protein Miga regulates autophagy through Atg14 and Uvrag.;In the present study, we found that the mitochondrial protein Miga forms complexes with Uvrag and Atg14 to regulate PI3P production and to stabilize Syx17 during autophagy.	The protein was validated by immunofluorescence, microscopy, TEM, co-immunoprecipitation, western blotting and real-time quantitative PCR in drosophila S2 cells, and Miga interacted with Uvrag to regulate PI3K activity.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00522	Atg6; CG5429	42850	Atg14	Q9VCE1	Fruit fly	ER-MT; MT-ER	NA	Drosophila S2 cells	Low throughput experimental methods	1	36323251	ER-mitochondrial contact protein Miga regulates autophagy through Atg14 and Uvrag.;In the present study, we found that the mitochondrial protein Miga forms complexes with Uvrag and Atg14 to regulate PI3P production and to stabilize Syx17 during autophagy.	The protein was validated by immunofluorescence, microscopy, TEM, co-immunoprecipitation, western blotting and real-time quantitative PCR in drosophila S2 cells, and Miga interacts with Atg14 to stabilize Syx17.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00523	Miga; CG12125	31775	Miga	Q9W3F7	Fruit fly	ER-MT; MT-ER	MT	Drosophila S2 cells	Low throughput experimental methods	1	36323251	ER-mitochondrial contact protein Miga regulates autophagy through Atg14 and Uvrag.;In the present study, we found that the mitochondrial protein Miga forms complexes with Uvrag and Atg14 to regulate PI3P production and to stabilize Syx17 during autophagy.	The protein was validated by immunofluorescence, microscopy, TEM, co-immunoprecipitation, western blotting and real-time quantitative PCR in drosophila S2 cells, which regulates fusion between autophagosomes and lysosomes.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00554	DIP2; CG7020	252479	DIP2	Q9W0S9	Fruit fly	MT-Vacuole; Vacuole-MT	NA	fly strains	Low throughput experimental methods	1	35766356	DIP2 is associated with vacuoles through mitochondria–vacuole contact sites.	The protein was validated by thin-layer chromatography, mass spectrometry, live cell microscopy, western blot analysis and bioinformatics analysis in fly strains, which is a unique regulator of diacylglycerol lipid homeostasis in eukaryotes.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00597	cert; BcDNA.GH07688; BcDNA:GH07688; CERT; Dcert; dcert; Dmel\CG7207; CG7207; Dmel_CG7207	38928	cert	Q9Y128	Fruit fly	ER-GA; GA-ER	NA	Fly strains	Low throughput experimental methods	1	37289040	Under fed conditions, PtdIns4P recruited its effectors Osbp and cert to the Golgi apparatus. The interaction between Osbp and ER protein VAP mediated ER-Golgi contact.	The protein was validated by immunofluorescence, filipin staining, transmission electron microscopy, quantitative RT-PCR and western blotting in fly strains, which is required for ER-Golgi contacts in fed cells.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00598	cert; BcDNA.GH07688; BcDNA:GH07688; CERT; Dcert; dcert; Dmel\CG7207; CG7207; Dmel_CG7207	38928	cert	Q9Y128	Fruit fly	ER-Autolysosome; Autolysosome-ER	NA	Fly strains	Low throughput experimental methods	1	37289040	Osbp and cert proteins were recruited by the autolysosomal PtdIns4P and established contacts between ER and autolysosomes.	The protein was validated by immunofluorescence, filipin staining, transmission electron microscopy, quantitative RT-PCR and western blotting in fly strains, which is required for the reduction of PtdIns4P on autolysosomes.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00599	Osbp; Dmel\CG6708; OSBP; osbp; OSBP-Dm; CG6708; Dmel_CG6708	42985	Osbp	Q9VC05	Fruit fly	ER-GA; GA-ER	NA	Fly strains	Low throughput experimental methods	1	37289040	Under fed conditions, PtdIns4P recruited its effectors Osbp and cert to the Golgi apparatus. The interaction between Osbp and ER protein VAP mediated ER-Golgi contact.	The protein was validated by immunofluorescence, filipin staining, transmission electron microscopy, quantitative RT-PCR and western blotting in fly strains, which is required for ER-Golgi contacts in fed cells.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00600	Osbp; Dmel\CG6708; OSBP; osbp; OSBP-Dm; CG6708; Dmel_CG6708	42985	Osbp	Q9VC05	Fruit fly	ER-Autolysosome; Autolysosome-ER	NA	Fly strains	Low throughput experimental methods	1	37289040	Osbp and cert proteins were recruited by the autolysosomal PtdIns4P and established contacts between ER and autolysosomes.	The protein was validated by immunofluorescence, filipin staining, transmission electron microscopy, quantitative RT-PCR and western blotting in fly strains, which is required for the reduction of PtdIns4P on autolysosomes.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00601	vap; D-RasGAP; Dmel\CG9209; FBpp0073946; p120; RasGAP; p120RasGAP; RAS-GAP; RasGAP; RasGap; rasGap; RasGAP/Vap; vap-RA; CG9209; Dmel_CG9209	32569	vap	Q8IR23	Fruit fly	ER-GA; GA-ER	ER	Fly strains	Low throughput experimental methods	1	37289040	Under fed conditions, PtdIns4P recruited its effectors Osbp and cert to the Golgi apparatus. The interaction between Osbp and ER protein VAP mediated ER-Golgi contact.	The protein was validated by immunofluorescence, filipin staining, transmission electron microscopy, quantitative RT-PCR and western blotting in fly strains, which is required for ER-Golgi contacts in fed cells.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00602	vap; D-RasGAP; Dmel\CG9209; FBpp0073946; p120; RasGAP; p120RasGAP; RAS-GAP; RasGAP; RasGap; rasGap; RasGAP/Vap; vap-RA; CG9209; Dmel_CG9209	32569	vap	Q8IR23	Fruit fly	ER-Autolysosome; Autolysosome-ER	ER	Fly strains	Low throughput experimental methods	1	37289040	Under fed conditions, PtdIns5P recruited its effectors Osbp and cert to the Golgi apparatus. The interaction between Osbp and ER protein VAP mediated ER-Golgi contact.; A same set of molecular machinery was used by two distinct organelle contacts under different nutrition statuses.	The protein was validated by immunofluorescence, filipin staining, transmission electron microscopy, quantitative RT-PCR and western blotting in fly strains, which is required for the reduction of PtdIns4P on autolysosomes.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00603	Sac1; Sacm1l; CG9128	38137	Sac1	Q9W0I6	Fruit fly	ER-GA; GA-ER	ER	Fly strains	Low throughput experimental methods	1	37289040	PtdIns4P was transported from the Golgi apparatus to ER and hydrolyzed by Sac1, which triggered the cholesterol or other lipid transfer between two organelles mediated by Osbp and cert.	The protein was validated by immunofluorescence, filipin staining, transmission electron microscopy, quantitative RT-PCR and western blotting in fly strains, which is required for ER-Golgi contacts in fed cells.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00604	Sac1; Sacm1l; CG9128	38137	Sac1	Q9W0I6	Fruit fly	ER-Autolysosome; Autolysosome-ER	ER	Fly strains	Low throughput experimental methods	1	37289040	PtdIns4P was transported from the Golgi apparatus to ER and hydrolyzed by Sac1, which triggered the cholesterol or other lipid transfer between two organelles mediated by Osbp and cert.; A same set of molecular machinery was used by two distinct organelle contacts under different nutrition statuses.	The protein was validated by immunofluorescence, filipin staining, transmission electron microscopy, quantitative RT-PCR and western blotting in fly strains, which is required for the reduction of PtdIns4P on autolysosomes.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00605	rdgB; CG11111	32340	rdgB	P43125	Fruit fly	ER-PM; PM-ER	NA	S2R+ Cells; Drosophila; fruit fly	Low throughput experimental methods	3	36803287	Overall our model explains the topology of the RDGB-VAP complex at this ER-PM contact site and paves the way for analysis of lipid transfer function in this setting.	The protein was validated by immunofluorescence, co-immunoprecipitation, immunocytochemsitry and electron microscopic determination in S2R+ Cells and drosophila.	33597200	Previously, the interaction between the FFAT motif of RDGB and the integral ER protein dVAP-A was shown to be essential for accurate localization to ER–PM MCS. Here, we report that the FFAT/dVAP-A interaction alone is insufficient to localize RDGB accurately; this also requires the function of the C-terminal domains, DDHD and LNS2.	The protein was validated by western blotting, immunostaining and coimmunoprecipitation in S2R+ Cells and fruit fly.	29180517	dVAP-A is enriched at the SMC and is essential for localization of RDGBα.; In Drosophila photoreceptors, endogenous RDGBα is constitutively localized to the SMC, an ER–PM contact site.	The protein was validated by western blotting, electron microscopy and immunohistochemistry in fruit fly.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00606	Vap33; anon-EST:Liang-2.42; anon-WO03040301.124; BcDNA:GM03307; clone 2.42; Dmel\CG5014; DVAP; dVAP; dvap; DVAP-33A; dVAP-A; DVAP33A; dVAP33A; dvap33a; l(1)G0231; VAP; VAP-33; VAP-33-1; Vap-33-1; Vap-33A; vap-33A; VAP33; Vap33-1; vap33-1; VAP33-A; VAP33A; VAPB; CG5014; Dmel_CG5014	31349	dVAP-A	Q9W4N8	Fruit fly	ER-PM; PM-ER	ER	S2R+ Cells; Drosophila; fruit fly	Low throughput experimental methods	3	36803287	Overall our model explains the topology of the RDGB-VAP complex at this ER-PM contact site and paves the way for analysis of lipid transfer function in this setting.	The protein was validated by immunofluorescence, co-immunoprecipitation, immunocytochemsitry and electron microscopic determination in S2R+ Cells and drosophila.	33597200	Previously, the interaction between the FFAT motif of RDGB and the integral ER protein dVAP-A was shown to be essential for accurate localization to ER–PM MCS. Here, we report that the FFAT/dVAP-A interaction alone is insufficient to localize RDGB accurately; this also requires the function of the C-terminal domains, DDHD and LNS2.	The protein was validated by western blotting, immunostaining and coimmunoprecipitation in S2R+ Cells and fruit fly.	29180517	dVAP-A is enriched at the SMC and is essential for localization of RDGBα.; In Drosophila photoreceptors, endogenous RDGBα is constitutively localized to the SMC, an ER–PM contact site.	The protein was validated by western blotting, electron microscopy and immunohistochemistry in fruit fly.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00639	Vps13; CG2093	35693	Vps13	A1Z713	Fruit fly	ER-PM; PM-ER	NA	Fly strains	Low throughput experimental methods	1	32994170	Ultrastructural analysis uncovered the presence of an underlying Vps13-dependent membranous structure in close association with the plasma membrane.	The protein was validated by CRISPR/Cas9, qPCR, microscopy and western blot analysis in fly strains, which is required for timely removal of nurse cell corpses.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA