Complex.ID	Complex	BIOgrid	Subunit.number	species	MCS	Source.number	PMID-1	Description-1	PMID-2	Description-2	PMID-3	Description-3	PMID-4	Description-4	Name-1	Pubchme.CID-1	Molecular Formula-1	SMILES-1	Name-2	Pubchme.CID-2	Molecular Formula-2	SMILES-2	Entry.ID_subunit-1	Symbol_subunit-1	Uniprot_subunit-1	Organelle.location_subunit-1	Entry.ID_subunit-2	Symbol_subunit-2	Uniprot_subunit-2	Organelle.location_subunit-2	Entry.ID_subunit-3	Symbol_subunit-3	Uniprot_subunit-3	Organelle.location_subunit-3	Entry.ID_subunit-4	Symbol_subunit-4	Uniprot_subunit-4	Organelle.location_subunit-4	Entry.ID_subunit-5	Symbol_subunit-5	Uniprot_subunit-5	Organelle.location_subunit-5	Entry.ID_subunit-6	Symbol_subunit-6	Uniprot_subunit-6	Organelle.location_subunit-6	Entry.ID_subunit-7	Symbol_subunit-7	Uniprot_subunit-7	Organelle.location_subunit-7	Entry.ID_subunit-8	Symbol_subunit-8	Uniprot_subunit-8	Organelle.location_subunit-8
CMCS00001	VAPA_OSBPL1A	OSBPL1A_VAPA(LTP)	2	Human	ER-Autophagosome; Autophagosome-ER	1	27283760	ORP1L localizes to late autophagosomes and—under low-cholesterol conditions—contacts the ER protein VAP-A, forming ER-autophagosome contact sites, which prevent minus-end transport by the Rab7–RILP–dynein complex.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00001	OSBPL1A	Q9BXW6	Autophagosome	LMCS00002	VAPA	Q9P0L0	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00002	STARD11_MOSPD2	NA	2	Human	ER-GA; GA-ER	1	29858488	Consequently, MOSPD2 and these organelle‐bound proteins mediate the formation of contact sites between the ER and endosomes, mitochondria, or Golgi.; ll these proteins, by binding VAP proteins, are known to build contact sites between the ER and endosomes (STARD3, STARD3NL, ORP1L), mitochondria (PTPIP51), and Golgi (STARD11).	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00054	CERT1	Q9Y5P4	GA	LMCS00355	MOSPD2	Q8NHP6	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00003	OSBPL5_NPC1	OSBPL5_NPC1(LTP)	2	Human	ER-Endosome; Endosome-ER	1	21220512	Our results suggest that ORP5 may cooperate with NPC1 to deliver cholesterol from LE/LY to the ER.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00005	OSBPL5	Q9H0X9	ER	LMCS00004	NPC1	O15118	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00004	VAPA_OSBPL1A_sterol_PI(4)P_NPC1	VAPA_OSBPL1A(LTP)	5	Human	ER-Endosome; Endosome-ER	1	28564600	Cholesterol delivery to the ER required the sterol-, phosphatidylinositol 4-phosphate-, and vesicle-associated membrane protein-associated protein (VAP)-binding activities of ORP1L, as well as NPC1 expression.	NA	NA	NA	NA	NA	NA	sterol	1107	C17H28O	C1CC2CCC3C4CCC(CC4CCC3C2C1)O	PI(4)P	643965	C41H80O16P2	CCCCCCCCCCCCCCCC(=O)OCC(COP(=O)(O)OC1C(C(C(C(C1O)O)OP(=O)(O)O)O)O)OC(=O)CCCCCCCCCCCCCCC	LMCS00029	VAPA	Q9P0L0	ER	LMCS00026	OSBPL1A	Q9BXW6	Endosome	LMCS00004	NPC1	O15118	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00005	PTP1B_Prdx4_G-Csf3r	NA	3	Mouse	ER-Endosome; Endosome-ER	1	22045733	Using this technique, we could confirm the results obtained by confocal laser scanning microscopy (CLSM) showing colocalization of G-CSFR, Ptp1b and Prdx4.; Here, we show that the ER-resident antioxidant peroxiredoxin 4 (Prdx4) interacts with the cytoplasmic domain of the granulocyte colony-stimulating factor receptor (G-CSFR). This interaction occurs when the activated G-CSFR resides in early endosomes.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00006	Prdx4	O08807	ER	LMCS00007	Csf3r	P40223	Endosome	LMCS00274	Ptpn1	P35821	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00006	ZFYVE27_FYCO1_KIF5B_RAB7A_PI(3)P	ZFYVE27_RAB7A(HTP: 0.02); FYCO1_KIF5B(HTP: -); FYCO1_RAB7A(HTP: 0.00)	5	Human	ER-Endosome; Endosome-ER	1	25855459	Such fusion induces outgrowth of protrusions and neurites, which requires the abilities of protrudin and FYCO1 to interact with LEs and kinesin 1.Thus, protrudin-containing ER-LE contact sites are platforms for kinesin-1 loading onto LEs, and kinesin-1-mediated translocation of LEs to the plasma membrane, fuelled by repeated ER contacts, promotes protrusion and neurite outgrowth.	NA	NA	NA	NA	NA	NA	PI(3)P	643964	C41H80O16P2	CCCCCCCCCCCCCCCC(=O)OCC(COP(=O)(O)OC1C(C(C(C(C1O)OP(=O)(O)O)O)O)O)OC(=O)CCCCCCCCCCCCCCC	NA	NA	NA	NA	LMCS00032	ZFYVE27	Q5T4F4	ER	LMCS00009	FYCO1	Q9BQS8	Endosome	LMCS00065	KIF5B	P33176	Endosome	LMCS00039	RAB7A	P51149	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00007	S100A11_ANXA1	S100A11_ANXA1(LTP)	2	Human	ER-Endosome; Endosome-ER	1	27270042	Here we show that these contacts are tethered by annexin A1 and its Ca2+-dependent ligand, S100A11, and form a subpopulation of differentially regulated contact sites between the ER and endocytic organelles.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00010	S100A11	P31949	ER	LMCS00034	ANXA1	P04083	ER; Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00008	VAPA_VAPB_SNX2	VAPA_VAPB(LTP); VAPB_SNX2(HTP: 1.00)	3	Human	ER-Endosome; Endosome-ER	1	27419871	An interaction between VAP and the retromer subunit SNX2 tethers the ER to endosomes.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00029	VAPA	Q9P0L0	ER	LMCS00035	VAPB	O95292	ER	LMCS00011	SNX2	O60749	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00009	VAPA_VAPB_OSBP_PI(4)P	OSBP_VAPB(HTP: 1.00); VAPA_VAPB(LTP); OSBP_VAPA(LTP)	4	Human	ER-Endosome; Endosome-ER	1	27419871	Defects are mimicked by downregulation of OSBP, a VAP interactor and PI4P transporter that participates in VAP-dependent ER-endosomes tethers.	NA	NA	NA	NA	NA	NA	PI(4)P	643965	C41H80O16P2	CCCCCCCCCCCCCCCC(=O)OCC(COP(=O)(O)OC1C(C(C(C(C1O)O)OP(=O)(O)O)O)O)OC(=O)CCCCCCCCCCCCCCC	NA	NA	NA	NA	LMCS00029	VAPA	Q9P0L0	ER	LMCS00035	VAPB	O95292	ER	LMCS00012	OSBP	P22059	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00010	ZFYVE27_Fyco1_Kif5b_Rab7a_PI(3)P	NA	5	Rat	ER-Endosome; Endosome-ER	1	25855459	Here we show in human and rat cell lines that protrudin, an ER protein that promotes protrusion and neurite outgrowth, forms contact sites with late endosomes (LEs) via coincident detection of the small GTPase RAB7 and phosphatidylinositol 3-phosphate (PtdIns(3)P). These contact sites mediate transfer of the microtubule motor kinesin 1 from protrudin to the motor adaptor FYCO1 on LEs.	NA	NA	NA	NA	NA	NA	PI(3)P	643964	C41H80O16P2	CCCCCCCCCCCCCCCC(=O)OCC(COP(=O)(O)OC1C(C(C(C(C1O)OP(=O)(O)O)O)O)O)OC(=O)CCCCCCCCCCCCCCC	NA	NA	NA	NA	LMCS00211	Zfyve27	Q6P7B7	ER	LMCS00632	Fyco1	D3Z9D2	Endosome	LMCS00417	Kif5b	Q2PQA9	Endosome	LMCS00210	Rab7a	P09527	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00011	VAPA_VAPB_OSBPL1A	VAPA_VAPB(LTP); VAPB_OSBPL1A(LTP)	3	Human	ER-Endosome; Endosome-ER	1	27270042	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.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00029	VAPA	Q9P0L0	ER	LMCS00035	VAPB	O95292	ER	LMCS00026	OSBPL1A	Q9BXW6	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00012	Spast_Ist1	Ist1_Spast(HTP: 0.83)	2	Mouse	ER-Endosome; Endosome-ER	1	28389476	We found that interaction between the microtubule-severing enzyme spastin and the ESCRT protein IST1 at ER-endosome contacts drives endosomal tubule fission.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00018	Spast	Q9QYY8	ER	LMCS00017	Ist1	Q9CX00	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00013	MOSPD2_STARD3NL	STARD3NL_MOSPD2(HTP: 0.89)	2	Human	ER-Endosome; Endosome-ER	1	29858488	Consequently, MOSPD2 and these organelle‐bound proteins mediate the formation of contact sites between the ER and endosomes, mitochondria, or Golgi.; ll these proteins, by binding VAP proteins, are known to build contact sites between the ER and endosomes (STARD3, STARD3NL, ORP1L), mitochondria (PTPIP51), and Golgi (STARD11).	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00019	MOSPD2	Q8NHP6	ER	LMCS00031	STARD3NL	O95772	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00014	MOSPD2_STARD3	MOSPD2_STARD3(LTP)	2	Human	ER-Endosome; Endosome-ER	1	29858488	Consequently, MOSPD2 and these organelle‐bound proteins mediate the formation of contact sites between the ER and endosomes, mitochondria, or Golgi.; ll these proteins, by binding VAP proteins, are known to build contact sites between the ER and endosomes (STARD3, STARD3NL, ORP1L), mitochondria (PTPIP51), and Golgi (STARD11).	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00019	MOSPD2	Q8NHP6	ER	LMCS00030	STARD3	Q14849	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00015	MOSPD2_OSBPL1A	MOSPD2_OSBPL1A(LTP)	2	Human	ER-Endosome; Endosome-ER	1	29858488	Consequently, MOSPD2 and these organelle‐bound proteins mediate the formation of contact sites between the ER and endosomes, mitochondria, or Golgi.; ll these proteins, by binding VAP proteins, are known to build contact sites between the ER and endosomes (STARD3, STARD3NL, ORP1L), mitochondria (PTPIP51), and Golgi (STARD11).	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00019	MOSPD2	Q8NHP6	ER	LMCS00026	OSBPL1A	Q9BXW6	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00016	VPS13_SPO71	VPS13_SPO71(LTP)	2	Yeast	ER-Prospore membrane; Prospore membrane-ER	1	30018089	Our results suggest Spo71, an established Vps13 prospore membrane adaptor, contains a PxP motif that is necessary and sufficient for Vps13 binding, indicating that the mechanism for Vps13 binding is conserved between proteins.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00020	VPS13	Q07878	ER	LMCS00021	SPO71	Q03868	Prospore membrane	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00017	Pdzd8_Rab7a	NA	2	Mouse	ER-Endosome; Endosome-ER	1	31636202	PDZD8 mediates a Rab7-dependent interaction of the ER with late endosomes and lysosomes.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00022	Pdzd8	B9EJ80	ER	LMCS00040	Rab7a	P51150	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00018	PDZD8_RAB7A	RAB7A_PDZD8(LTP)	2	Human	ER-Endosome; Endosome-ER	1	31636202	PDZD8 mediates a Rab7-dependent interaction of the ER with late endosomes and lysosomes.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00023	PDZD8	Q8NEN9	ER	LMCS00039	RAB7A	P51149	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00019	Ano10_Rab7a	NA	2	Mouse	ER-Endosome; Endosome-ER	1	32620747	We find endoplasmic reticulum-localized TMEM16K acts at ER-endosome contact sites where it interacts with the endosomal protein Rab7.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00024	Ano10	Q8BH79	ER	LMCS00040	Rab7a	P51150	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00020	ANO10_RAB7A	NA	2	Human	ER-Endosome; Endosome-ER	1	32620747	We find endoplasmic reticulum-localized TMEM16K acts at ER-endosome contact sites where it interacts with the endosomal protein Rab7.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00025	ANO10	Q9NW15	ER	LMCS00039	RAB7A	P51149	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00021	PTPN1_Prdx4_CSF3R	NA	3	Human	ER-Endosome; Endosome-ER	1	22045733	Using this technique, we could confirm the results obtained by confocal laser scanning microscopy (CLSM) showing colocalization of G-CSFR, Ptp1b and Prdx4.; Here, we show that the ER-resident antioxidant peroxiredoxin 4 (Prdx4) interacts with the cytoplasmic domain of the granulocyte colony-stimulating factor receptor (G-CSFR). This interaction occurs when the activated G-CSFR resides in early endosomes.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00027	PTPN1	P18031	ER	LMCS00008	CSF3R	Q99062	Endosome	LMCS00272	PRDX4	Q13162	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00022	PTPN1_EGFR	PTPN1_EGFR(LTP)	2	Human	ER-Endosome; Endosome-ER	4	20118922	Membrane contacts between endosomes and ER provide sites for PTP1B-epidermal growth factor receptor(EGFR) interaction.	11872838	We investigated the in- teraction between PTP1B and two RTKs, the epidermal growth factor receptor (EGFR) and the platelet-derived growth factor receptor-b(PDGFR).	27270042	ER-MVB contacts additionally function in epidermal growth factor receptor (EGFR) tyrosine kinase downregulation by providing sites where the ER-localized phosphatase, PTP1B, interacts with endocytosed EGFR before the receptor is sorted onto intraluminal vesicles (ILVs).	36744428	In this study, we demonstrate that LRRK1 facilitates EGFR dephosphorylation by PTP1B (also known as PTPN1), an endoplasmic reticulum (ER)-localized protein tyrosine phosphatase, at the ER–endosome contact site, after which EGFR is sorted into the ILVs of endosomes.	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00027	PTPN1	P18031	ER	LMCS00033	EGFR	P00533	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00023	VAPA_VAPB_STARD3	VAPA_VAPB(LTP); VAPB_STARD3(LTP); VAPA_STARD3(LTP)	3	Human	ER-Endosome; Endosome-ER	2	24105263	STARD3 or STARD3NL and VAP form a novel molecular tether between late endosomes and the ER.	28377464	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.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00029	VAPA	Q9P0L0	ER	LMCS00035	VAPB	O95292	ER	LMCS00030	STARD3	Q14849	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00024	VAPA_VAPB_STARD3NL	VAPA_VAPB(LTP)	3	Human	ER-Endosome; Endosome-ER	1	24105263	STARD3 or STARD3NL and VAP form a novel molecular tether between late endosomes and the ER.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00029	VAPA	Q9P0L0	ER	LMCS00035	VAPB	O95292	ER	LMCS00031	STARD3NL	O95772	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00025	SPAST_IST1	SPAST_IST1(LTP)	2	Human	ER-Endosome; Endosome-ER	2	28389476	We found that interaction between the microtubule-severing enzyme spastin and the ESCRT protein IST1 at ER-endosome contacts drives endosomal tubule fission.	23897888	An ESCRT-spastin interaction promotes fission of recycling tubules from the endosome, Our results suggest that inclusion of IST1 into the ESCRT complex allows recruitment of spastin to promote fission of recycling tubules from the endosome.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00037	SPAST	Q9UBP0	ER	LMCS00036	IST1	P53990	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00026	VAPB_VAPA_VPS13C	VAPB_VPS13C(HTP: 0.90); VAPA_VPS13C(HTP: 1.00); VAPA_VAPB(LTP)	3	Human	ER-Endosome; Endosome-ER	1	30093493	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.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00035	VAPB	O95292	ER	LMCS00029	VAPA	Q9P0L0	ER	LMCS00038	VPS13C	Q709C8	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00027	VAPB_VAPA_OSBPL1A_RAB7A_RILP	VAPA_VAPB(LTP); VAPB_OSBPL1A(LTP); VAPA_OSBPL1A(LTP)	5	Human	ER-Endosome; Endosome-ER	1	19564404	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.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00029	VAPA	Q9P0L0	ER	LMCS00035	VAPB	O95292	ER	LMCS00026	OSBPL1A	Q9BXW6	Endosome	LMCS00039	RAB7A	P51149	Endosome	LMCS00013	RILP	Q96NA2	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00028	VAPB_CERT1_VAPA	VAPA_VAPB(LTP)	3	Human	ER-GA; GA-ER	1	16895911	CERT has a pleck-strin homology (PH) domain for Golgi targeting and a START domain catalyzing the intermembrane transfer of ceramide. The region between the two domains contains a short peptide motif designated FFAT, which is supposed to interact with the ER-resident proteins VAP-A and VAP-B.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00042	VAPB	O95292	ER	LMCS00054	CERT1	Q9Y5P4	GA	LMCS00057	VAPA	Q9P0L0	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00029	PI(4)P_ PLEKHA3_SACM1L_VAPA_VAPB	VAPA_PLEKHA3(HTP: -); VAPB_SACM1L(LTP); VAPA_VAPB(LTP); VAPA_SACM1L(LTP)	5	Human	ER-GA; GA-ER	1	30659099	The interaction of FAPP1, a TGN-associated protein, with two ER proteins (VAP and Sac1) prompted us to investigate whether FAPP1 localizes at ERTGoCS and whether the interaction of FAPP1 with Sac1 had any impact on the phosphatase activity of Sac1.; The activity of Sac1 across ER-TGN contact sites requires the four-phosphate-adaptor-protein-1.	NA	NA	NA	NA	NA	NA	PI(4)P	643965	C41H80O16P2	CCCCCCCCCCCCCCCC(=O)OCC(COP(=O)(O)OC1C(C(C(C(C1O)O)OP(=O)(O)O)O)O)OC(=O)CCCCCCCCCCCCCCC	NA	NA	NA	NA	LMCS00042	VAPB	O95292	ER	LMCS00057	VAPA	Q9P0L0	ER	LMCS00049	PLEKHA3	Q9HB20	GA	LMCS00050	SACM1L	Q9NTJ5	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00030	PI(4)P_VAPB_VAPA_OSBPL9_OSBP	OSBP_VAPB(HTP: 1.00); OSBP_VAPA(LTP); VAPA_VAPB(LTP); OSBPL9_VAPB(HTP: 6.69); OSBPL9_VAPA(HTP: 11.72)	5	Human	ER-GA; GA-ER	1	30659100	We have shown that OSBP1 and ORP9, while using the ERTGoCS for lipid exchange, can also act as tethers.The higher cellular levels of both OSBP1 and ORP9 and their higher affinity for VAPs and PI4P relative to other members of the family may explain why they can play a tethering role.	NA	NA	NA	NA	NA	NA	PI(4)P	643965	C41H80O16P2	CCCCCCCCCCCCCCCC(=O)OCC(COP(=O)(O)OC1C(C(C(C(C1O)O)OP(=O)(O)O)O)O)OC(=O)CCCCCCCCCCCCCCC	NA	NA	NA	NA	LMCS00042	VAPB	O95292	ER	LMCS00057	VAPA	Q9P0L0	ER	LMCS00059	OSBPL9	Q96SU4	GA	LMCS00056	OSBP	P22059	GA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00031	VAPA_VAPB_PI(4)P_OSBP	OSBP_VAPB(HTP: 1.00); VAPA_VAPB(LTP); OSBP_VAPA(LTP)	4	Human	ER-GA; GA-ER	2	30905771	OSBP contains an N-terminal pleckstrin homology (PH) domain, which interacts with the TGN or endosomal PI(4)P and a central FFAT (two phenylalanines in an acidic tract) motif, which interacts with the general ER receptor VAP-A or VAP-B.	25420878	This was observed in the absence of oxysterol treatment, suggesting that the endogenous sterol ligands of OSBP together with PI4P are sufficient to maintain part of the OSBP–VAP complexes at a Golgi (or ER–Golgi MCS) location.	NA	NA	NA	NA	PI(4)P	643965	C41H80O16P2	CCCCCCCCCCCCCCCC(=O)OCC(COP(=O)(O)OC1C(C(C(C(C1O)O)OP(=O)(O)O)O)O)OC(=O)CCCCCCCCCCCCCCC	NA	NA	NA	NA	LMCS00042	VAPB	O95292	ER	LMCS00057	VAPA	Q9P0L0	ER	LMCS00056	OSBP	P22059	GA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00032	VAPA_VAPB_PI(4)P_OSBP2	VAPA_OSBP2(HTP: 1.00); VAPA_VAPB(LTP); VAPB_OSBP2(HTP: 1.00)	4	Human	ER-GA; GA-ER	1	30905771	Although quite distant in sequence, the N terminus of OSBP-related protein-4 (ORP4) has similar effects. ; Ligand-dependent localization and function of ORP-VAP complexes at membrane contact sites.	NA	NA	NA	NA	NA	NA	PI(4)P	643965	C41H80O16P2	CCCCCCCCCCCCCCCC(=O)OCC(COP(=O)(O)OC1C(C(C(C(C1O)O)OP(=O)(O)O)O)O)OC(=O)CCCCCCCCCCCCCCC	NA	NA	NA	NA	LMCS00042	VAPB	O95292	ER	LMCS00057	VAPA	Q9P0L0	ER	LMCS00053	OSBP2	Q969R2	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00033	PI(4)P_ Plekha3_Sacm1l_Vapa_Vapb	NA	5	Mouse	ER-GA; GA-ER	1	30659099	The interaction of FAPP1, a TGN-associated protein, with two ER proteins (VAP and Sac1) prompted us to investigate whether FAPP1 localizes at ERTGoCS and whether the interaction of FAPP1 with Sac1 had any impact on the phosphatase activity of Sac1.; The activity of Sac1 across ER-TGN contact sites requires the four-phosphate-adaptor-protein-1.	NA	NA	NA	NA	NA	NA	PI(4)P	643965	C41H80O16P2	CCCCCCCCCCCCCCCC(=O)OCC(COP(=O)(O)OC1C(C(C(C(C1O)O)OP(=O)(O)O)O)O)OC(=O)CCCCCCCCCCCCCCC	NA	NA	NA	NA	LMCS00043	Vapb	Q9QY76	ER	LMCS00047	Sacm1l	Q9EP69	ER	LMCS00048	Plekha3	Q9ERS4	GA	LMCS00058	Vapa	Q9WV55	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00034	VAPA_PI(4)P_OSBP	OSBP_VAPA(LTP)	3	Human	ER-GA; GA-ER	1	24209621	Several proteins at endoplasmic reticulum (ER)-Golgi membrane contact sites contain a PH domain that interacts with the Golgi phosphoinositide PI(4)P, a FFAT motif that interacts with the ER protein VAP-A, and a lipid transfer domain.	NA	NA	NA	NA	NA	NA	PI(4)P	643965	C41H80O16P2	CCCCCCCCCCCCCCCC(=O)OCC(COP(=O)(O)OC1C(C(C(C(C1O)O)OP(=O)(O)O)O)O)OC(=O)CCCCCCCCCCCCCCC	NA	NA	NA	NA	LMCS00057	VAPA	Q9P0L0	ER	LMCS00056	OSBP	P22059	GA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00035	VAPA_OSBP	OSBP_VAPA(LTP)	2	Human	ER-GA; GA-ER	2	12023275	Vesicle-associated Membrane Protein-associated Protein-A (VAP-A) Interacts with the Oxysterol-binding Protein to Modify Export from the Endoplasmic Reticulum.	24209621	Several proteins at endoplasmic reticulum (ER)-Golgi membrane contact sites contain a PH domain that interacts with the Golgi phosphoinositide PI(4)P, a FFAT motif that interacts with the ER protein VAP-A, and a lipid transfer domain.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00057	VAPA	Q9P0L0	ER	LMCS00056	OSBP	P22059	GA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00036	VAPA_CERT1	NA	2	Human	ER-GA; GA-ER	1	16895911	Efficient trafficking of ceramide from the endoplasmic reticulum to the Golgi apparatus requires a VAMP-associated protein-interacting FFAT motif of CERT.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00057	VAPA	Q9P0L0	ER	LMCS00054	CERT1	Q9Y5P4	GA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00037	SLC27A1_DGAT2	DGAT2_SLC27A1(LTP)	2	Human	ER-LD; LD-ER	1	22927462	The FATP1-DGAT2 complex facilitates lipid droplet expansion at the ER-lipid droplet interface.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00060	SLC27A1	Q6PCB7	ER	LMCS00061	DGAT2	Q96PD7	LD	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00038	Rab18_Nbas_Rint1_Zw10_Stx18_Use1_Bnip1	NA	7	Mouse	ER-LD; LD-ER	1	29367353	Rab18 promotes lipid droplet (LD) growth by tethering the ER to LDs through SNARE and NRZ interactions.; LD-associated Rab18 bound specifically to the ER-associated NAG-RINT1-ZW10 (NRZ) tethering complex and their associated SNAREs (Syntaxin18, Use1, BNIP1), resulting in the recruitment of ER to LD and the formation of direct ER–LD contact.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00041	Nbas	E9Q411	NA	LMCS00051	Zw10	O54692	NA	LMCS00052	Bnip1	Q6QD59	NA	LMCS00055	Rint1	Q8BZ36	ER	LMCS00062	Rab18	P35293	LD	LMCS00063	Use1	Q9CQ56	ER	LMCS00064	Stx18	Q8VDS8	ER	NA	NA	NA	NA
CMCS00040	RAB18_NBAS_RINT1_ZW10_STX18_USE1_BNIP1	BNIP1_NBAS(HTP: 1.00); BNIP1_ZW10(HTP: 0.97); STX18_NBAS(HTP: 1.00); STX18_ZW10(LTP); STX18_BNIP1(HTP: 1.00); STX18_RINT1(LTP); USE1_STX18(HTP: 1.00); USE1_ZW10(HTP: 1.00); RINT1_BNIP1(HTP: 1.00); USE1_BNIP1(HTP: 1.00)	7	Human	ER-LD; LD-ER	1	29367353	Rab18 promotes lipid droplet (LD) growth by tethering the ER to LDs through SNARE and NRZ interactions.; LD-associated Rab18 bound specifically to the ER-associated NAG-RINT1-ZW10 (NRZ) tethering complex and their associated SNAREs (Syntaxin18, Use1, BNIP	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00068	NBAS	A2RRP1	NA	LMCS00069	ZW10	O43264	NA	LMCS00070	BNIP1	Q12981	NA	LMCS00071	RINT1	Q6NUQ1	ER	LMCS00072	RAB18	Q9NP72	LD	LMCS00073	USE1	Q9NZ43	ER	LMCS00074	STX18	Q9P2W9	ER	NA	NA	NA	NA
CMCS00041	VAPB_VAPA_VPS13C	VAPA_VPS13C(HTP: 1.00); VAPB_VPS13C(HTP: 0.90); VAPA_VAPB(LTP)	3	Human	ER-LD; LD-ER	1	30093493	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.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00075	VPS13C	Q709C8	ER	LMCS00091	VAPB	O95292	ER	LMCS00092	VAPA	Q9P0L0	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00042	SNX14_ACSL3	NA	2	Human	ER-LD; LD-ER	1	30765438	Multi-time point imaging reveals that Snx14 is recruited to ER microdomains containing the fatty acyl-CoA ligase ACSL3, where nascent LDs bud.We propose that Snx14 is a novel marker for ER-LD contacts and regulates FA-stimulated LD growth.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00076	ACSL3	O95573	LD	LMCS00077	SNX14	Q9Y5W7	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00043	BSCL2_LDAF1	LDAF1_BSCL2(HTP: 0.99)	2	Human	ER-LD; LD-ER	1	31708432	The ER protein seipin was shown to localize to ER-LD contacts soon after LDs form, but what determines the sites of initial LD biogenesis in the ER is unknown.Here we identify TMEM159, now re-named lipid droplet-assembly factor 1 (LDAF1), as an interaction partner of seipin.Together, LDAF1 and seipin form a 600kDa oligomeric complex that copurifies with TG.LDs form at LDAF1-seipin complexes, and re-localization of LDAF1 to the plasma membrane co-recruits seipin and redirects LD formation to these sites.Once LDs form, LDAF1 dissociates from seipin and moves to the LD surface.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00078	LDAF1	Q96B96	LD	LMCS00088	BSCL2	Q96G97	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00044	IML2_PDR16	NA	2	Yeast	LD-Parasitophorous Vacuole; Parasitophorous Vacuole-LD	1	26004510	Three of which are proteins that interact with Iml2: Pdr16, Erg6, and Pet10, suggesting that the interaction with these three proteins is somehow required for LD-mediated IB clearance.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00373	IML2	P47031	Parasitophorous Vacuole	LMCS00372	PDR16	P53860	LD	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00045	VAPB_VAPA_VPS13A	VAPA_VPS13A(HTP: 1.00); VAPB_VPS13A(HTP: 1.00); VAPA_VAPB(LTP)	3	Human	ER-LD; LD-ER	1	30093493	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.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00083	VPS13A	Q96RL7	ER	LMCS00091	VAPB	O95292	ER	LMCS00092	VAPA	Q9P0L0	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00046	VAPB_SNCA	SNCA_VAPB(HTP: -)	2	Human	ER-MT; MT-ER	1	28337542	alpha-Synuclein is a MAM protein and binds to VAPB but not PTPIP51 in immunoprecipitation assays.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00191	VAPB	O95292	ER	LMCS00152	SNCA	P37840	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
CMCS00047	STIM1_ESYT1	STIM1_ESYT1(HTP: 14.08)	2	Human	ER-PM; PM-ER	1	30850711	E-syt1 re-arranges STIM1 clusters to stabilize ring-shaped ER-PM contact sites and accelerate Ca2+ store replenishment.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00279	STIM1	Q13586	ER; PM	LMCS00512	ESYT1	Q9BSJ8	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00048	LAM5_ARL1	NA	2	Yeast	ER-GA; GA-ER	1	29527758	In support of this, we could experimentally confirm a specific interaction between Lam5 and the Golgi protein Arl1 by co‐immunoprecipitation (data not shown) supporting that Lam5 may be a specific ER/Golgi contact site protein.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00135	LAM5	P43560	NA	LMCS00136	ARL1	P38116	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
CMCS00049	IML2_ERG6	IML2_ERG6(HTP: -)	2	Yeast	LD-Parasitophorous Vacuole; Parasitophorous Vacuole-LD	1	26004510	Three of which are proteins that interact with Iml2: Pdr16, Erg6, and Pet10, suggesting that the interaction with these three proteins is somehow required for LD-mediated IB clearance.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00373	IML2	P47031	Parasitophorous Vacuole	LMCS00080	ERG6	P25087	LD	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00050	OSBPL5_NPC1	OSBPL5_NPC1(LTP)	2	Human	ER-LY; LY-ER	1	21220512	Our results suggest that ORP5 may cooperate with NPC1 to deliver cholesterol from LE/LY to the ER.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00093	OSBPL5	Q9H0X9	ER	LMCS00099	NPC1	O15118	LY	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00051	PTPIP51_MOSPD2	NA	2	Human	ER-MT; MT-ER	1	29858488	Consequently, MOSPD2 and these organelle‐bound proteins mediate the formation of contact sites between the ER and endosomes, mitochondria, or Golgi.; ll these proteins, by binding VAP proteins, are known to build contact sites between the ER and endosomes (STARD3, STARD3NL, ORP1L), mitochondria (PTPIP51), and Golgi (STARD11).	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00190	RMDN3	Q96TC7	MT	LMCS00094	MOSPD2	Q8NHP6	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00052	VAPB_VAPA_VPS13C	VAPB_VPS13C(HTP: 0.90); VAPA_VPS13C(HTP: 1.00); VAPA_VAPB(LTP)	3	Human	ER-LY; LY-ER	1	30093493	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.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00095	VPS13C	Q709C8	ER	LMCS00101	VAPB	O95292	ER	LMCS00102	VAPA	Q9P0L0	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00053	GRAMD1B_NPC1	NA	2	Human	ER-LY; LY-ER	1	31537798	We report a role for Niemann-Pick type C protein 1 (NPC1) in tethering ER-endocytic organelle MCS where it interacts with the ER-localised sterol transport protein Gramd1b to regulate cholesterol egress.We show that artificially tethering MCS rescues the cholesterol accumulation that characterises NPC1-deficient cells, consistent with direct lysosome to ER cholesterol transport across MCS.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00096	GRAMD1B	Q3KR37	ER	LMCS00099	NPC1	O15118	LY	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00054	VAPB_VAPA_OSBP	OSBP_VAPB(HTP: 1.00); OSBP_VAPA(LTP); VAPA_VAPB(LTP)	3	Human	ER-LY; LY-ER	1	31548609	We show that Oxysterol Binding Protein (OSBP) and its anchors at the endoplasmic reticulum (ER), VAPA or VAPB, deliver cholesterol across ER-lysosome contacts to activate mTORC1.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00101	VAPB	O95292	ER	LMCS00102	VAPA	Q9P0L0	ER	LMCS00097	OSBP	P22059	LY	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00055	VAPB_VAPA_OSBPL1A_RAB7A	RAB7A_OSBPL1A(HTP: 0.00); RAB7A_VAPB(HTP: 0.00); RAB7A_VAPA(HTP: 0.00); VAPB_OSBPL1A(LTP); VAPA_VAPB(LTP)	4	Human	ER-LY; LY-ER	1	34504082	Lysosomes are then recruited to the division site in a process mediated by the Rab7-ORP1L-VAPs interaction that establishs contact sites with the ER.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00100	OSBPL1A	Q9BXW6	NA	LMCS00101	VAPB	O95292	ER	LMCS00102	VAPA	Q9P0L0	ER	LMCS00104	RAB7A	P51149	LY	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00056	ganglioside GD3_AMBRA1_WIPI1_CANX	AMBRA1_WIPI1(LTP)	4	Human	ER-MT; MT-ER	1	27123544	All in all, these experiments suggested that, under autophagic stimulation, a molecular interaction between ganglioside GD3, AMBRA1 and WIPI1 with the MAM marker CANX clearly occurs.	NA	NA	NA	NA	NA	NA	Ganglioside GD3	20057323	C68H121N3O29	CCCCCCCCCCCCCCCC(=O)NC(COC1C(C(C(C(O1)CO)OC2C(C(C(C(O2)CO)O)OC3(CC(C(C(O3)C(C(CO)OC4(CC(C(C(O4)C(C(CO)O)O)NC(=O)C)O)C(=O)O)O)NC(=O)C)O)C(=O)O)O)O)O)C(C=CCCCCCCCCCCCCC)O	NA	NA	NA	NA	LMCS00147	AMBRA1	Q9C0C7	ER; MT	LMCS00148	WIPI1	Q5MNZ9	ER; MT	LMCS00199	CANX	P27824	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00057	Pdzd8_Rab7a	NA	2	Mouse	ER-LY; LY-ER	1	31636202	PDZD8 mediates a Rab7-dependent interaction of the ER with late endosomes and lysosomes.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00103	Pdzd8	B9EJ80	ER	LMCS00105	Rab7a	P51150	LY	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00058	PDZD8_RAB7A	RAB7A_PDZD8(HTP: 0.00)	2	Human	ER-LY; LY-ER	1	31636202	PDZD8 mediates a Rab7-dependent interaction of the ER with late endosomes and lysosomes.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00106	PDZD8	Q8NEN9	ER	LMCS00104	RAB7A	P51149	LY	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00059	PDIA3_CANX	CANX_PDIA3(LTP)	2	Human	ER-MT; MT-ER	1	23843619	The palmitoylation state of calnexin regulates its interaction with ERp57.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00114	PDIA3	P30101	ER	LMCS00199	CANX	P27824	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00060	Pdia3_Canx	NA	2	Mouse	ER-MT; MT-ER	1	23843619	We demonstrate that reversible palmitoylation assigns calnexin to the interaction with SERCA2b and a role in the regulation of Ca2+ transfer to mitochondria, whereas non-palmitoylated calnexin tends to interact with ERp57 to fulfill its role in protein folding and quality control.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00388	Pdia3	P27773	ER	LMCS00198	Canx	P35564	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00061	Canx_Atp2a2	NA	2	Mouse	ER-MT; MT-ER	1	23843619	Our results demonstrate that palmitoylated calnexin interacts with sarcoendoplasmic reticulum (SR) Ca2+ transport ATPase (SERCA) 2b and that this interaction determines ER Ca2+ content and the regulation of ER-mitochondria Ca2+ crosstalk.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00389	Atp2a2	O55143	ER	LMCS00198	Canx	P35564	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00062	CANX_ATP2A2	CANX_ATP2A2(HTP: 1.56)	2	Human	ER-MT; MT-ER	1	23843619	Our results demonstrate that palmitoylated calnexin interacts with sarcoendoplasmic reticulum (SR) Ca2+ transport ATPase (SERCA) 2b and that this interaction determines ER Ca2+ content and the regulation of ER-mitochondria Ca2+ crosstalk.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00115	ATP2A2	P16615	ER	LMCS00199	CANX	P27824	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00063	Orai1_Stim1_Unc93b1	Orai1_Stim1(LTP)	3	Mouse	ER-PM; PM-ER	1	35065962	At these ER–PM junctions, STIM1 can trap and gate Orai1 Ca2+ channels, eliciting an influx of Ca2+ from the extracellular milieu into the cytoplasm.; UNC93B1 deficiency might impair the traffic or activity of an adapter protein to reduce STIM1–Orai1 interactions but not STIM1 recruitment.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00098	CRCM1	Q8BWG9	NA	LMCS00086	Stim1	P70302	ER; PM	LMCS00636	Unc93b1	Q8VCW4	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00064	SCS2_EPO1	SCS2_EPO1(LTP)	2	Yeast	ER-PM; PM-ER	1	25083872	One protein identified encoded by the ORF YMR124W, localized to sites of polarized growth including the incipient bud site in G1, the tips of small and medium buds in S and G2, and the septum during cytokinesis. These localizations overlapped with many of the localizations of Scs2DTM-GFP. Ymr124w was an excellent candidate for polarizing Scs2 and we named it Epo1 for ER polarization.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00266	SCS2	P40075	ER	LMCS00003	EPO1	P39523	PM	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00065	Vdac1_Itpr3_Hspa9	NA	3	Rat	ER-MT; MT-ER	1	17178908	VDAC1, grp75, and IP3Rs are present in a macromolecular complex at the ER-mitochondria interface.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00121	Hspa9	P48721	MT	LMCS00122	Vdac1	Q9Z2L0	MT	LMCS00175	Itpr3	Q63269	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00066	GEM1_MMM1_MDM10_MDM12_MDM34	GEM1_MDM34(LTP); GEM1_MMM1(LTP); MMM1_MDM34(LTP); MDM12_GEM1(LTP); MDM12_MDM34(LTP); MDM12_MMM1(LTP); MDM10_MDM12(LTP); MDM10_MDM34(LTP); MDM10_GEM1(LTP)	5	Yeast	ER-MT; MT-ER	2	21825164	Here we purified ERMES complexes and identified the Ca2+-binding Miro GTPase Gem1 as an integral component of ERMES.	26056272	For contact sites with mitochondria, a multisubunit complex called the endoplasmic reticulum-mitochondrial encounter structure (ERMES) has been shown to provide a bridge to the ER in the Yeast Saccharomyces cerevisiae.The ERMES comprises the soluble protein Mdm12, the ER-resident membrane protein Mmm1, two outer mitochondrial membrane proteins, Mdm10 and Mdm34, and the mitochondrial regulatory Miro GTPase Gem1.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00127	GEM1	P39722	MT	LMCS00178	MDM34	P53083	MT	LMCS00181	MMM1	P41800	ER	LMCS00180	MDM10	P18409	MT	LMCS00179	MDM12	Q92328	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00067	PI(4,5)P2_NUM1_MDM36	NUM1_MDM36(LTP)	3	Yeast	ER-MT-PM; PM-MT-ER	1	23341591	Our data indicate that Num1, together with Mdm36, forms a physical tether that robustly anchors mitochondria to the cell cortex but plays no direct role in mitochondrial division.	NA	NA	NA	NA	NA	NA	PI(4,5)P2	125105	C9H21O17P3	C(C(COP(=O)(O)OC1C(C(C(C(C1O)OP(=O)(O)O)OP(=O)(O)O)O)O)O)O	NA	NA	NA	NA	LMCS00109	NUM1	Q00402	ER; MT	LMCS00110	MDM36	Q06820	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00068	ATG14_STX17	ATG14_STX17(LTP)	2	Human	ER-MT; MT-ER	1	23455425	The ER-resident SNARE protein syntaxin 17 (STX17) binds ATG14 and recruits it to the ER-mitochondria contact site.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00132	STX17	P56962	ER; MT	LMCS00133	ATG14	Q6ZNE5	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00069	Nlrp3_Pycard	Nlrp3_Pycard(LTP)	2	Mouse	ER-MT; MT-ER	1	23502856	We found that ASC on Mitochondrion mediated the signal from NLRP3 to caspase-1.These findings indicated that dynein-dependent transport of Mitochondrion along microtubules facilitated the approximation of ASC on Mitochondrion to NLRP3 on the endoplasmic reticulum in response to inducers of the NLRP3 inflammasome.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00134	Pycard	Q9EPB4	MT	LMCS00193	Nlrp3	Q8R4B8	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00070	NUM1_MDM36	NUM1_MDM36(LTP)	2	Yeast	MT-PM; PM-MT	1	27241910	Num1CC interacts directly with Mdm36 and phospholipid membranes.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00365	NUM1	Q00402	NA	LMCS00366	MDM36	Q06820	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
CMCS00071	VAPA_VAPB_CERT1	VAPA-VAPB(LTP)	3	Human	ER-Endosome; Endosome-ER	1	33124732	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.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00029	VAPA	Q9P0L0	ER	LMCS00035	VAPB	O95292	ER	LMCS00563	CERT1	Q9Y5P4	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00072	MOSPD2_CERT1	/	2	Human	ER-Endosome; Endosome-ER	1	33124732	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.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00019	MOSPD2	Q8NHP6	ER	LMCS00563	CERT1	Q9Y5P4	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00074	EMC5_EMC2_EMC1_TOM5	EMC5_EMC1(LTP); EMC5_EMC2(LTP); TOM5_EMC2(LTP); TOM5_EMC5(LTP); EMC1_EMC2(LTP); TOM5_EMC1(LTP)	4	Yeast	ER-MT; MT-ER	1	25313861	We find that all Emc proteins interact with the mitochondrial translocase of the outer membrane (TOM) complex protein Tom5 and this interaction is important for PS transfer and cell growth, suggesting that the EMC forms a tether by associating with the TOM complex.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00143	TOM5	P80967	MT	LMCS00237	EMC1	P25574	ER	LMCS00238	EMC2	P47133	ER	LMCS00239	EMC5	P40540	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00075	LAM6_TOM70	LAM6_TOM70(LTP)	2	Yeast	ER-MT; MT-ER	1	25987606	Ltc1 localized to ER-Mitochondrion and ER-vacuole contacts via the Mitochondrionl import receptors Tom70,71 and the vacuolar protein Vac8, respectively.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00144	TOM70	P07213	MT	LMCS00196	LAM6	Q08001	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00076	LAM6_TOM71	LAM6_TOM71(LTP)	2	Yeast	ER-MT; MT-ER	1	25987606	Ltc1 localized to ER-Mitochondrion and ER-vacuole contacts via the Mitochondrionl import receptors Tom70,71 and the vacuolar protein Vac8, respectively.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00145	TOM71	P38825	MT	LMCS00196	LAM6	Q08001	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00077	OSBPL5_OSBPL8_RMDN3	OSBPL5_OSBPL8(HTP: 1.00)	3	Human	ER-MT; MT-ER	1	27113756	In summary, we have demonstrated that the mammalian ORP5 and ORP8 proteins localize to ER-Mitochondrionl MCS, in addition to ER-PM contact sites.Their targeting to ER-Mitochondrion MCS and interaction with the Mitochondrionl PTPIP51 requires a functional lipid-binding or transfer ORD domain.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00146	OSBPL5	Q9H0X9	ER	LMCS00190	RMDN3	Q96TC7	MT	LMCS00197	OSBPL8	Q9BZF1	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00078	Sigmar1_Itpr3	NA	2	Mouse	ER-MT; MT-ER	1	27821430	All these data indicate that the Sig1R activation that regulates IP3R3‐mediated intracellular Ca2+ flux at the MAM is crucial to prevent MAM disruption in motor neurons both in vitro and in vivo.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00149	Sigmar1	O55242	ER; MT	LMCS00207	Itpr3	P70227	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00079	Sigmar1_Sel1l_Syvn1	NA	3	Mouse	ER-MT; MT-ER	1	32193362	Sel1L-Hrd1 ERAD regulates MAM and Mitochondrionl dynamics via SigmaR1.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00149	Sigmar1	O55242	ER	LMCS00167	Syvn1	Q9DBY1	ER	LMCS00168	Sel1l	Q9Z2G6	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00080	AHCYL1_BCL2L10	NA	2	Human	ER-MT; MT-ER	1	27995898	IRBIT controls apoptosis by interacting with the Bcl-2 homolog, Bcl2l10, and by promoting ER-mitochondria contact.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00150	BCL2L10	Q9HD36	ER; MT	LMCS00208	AHCYL1	O43865	ER; MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00081	Ahcyl1_Bcl2l10	NA	2	Mouse	ER-MT; MT-ER	1	27995898	IRBIT controls apoptosis by interacting with the Bcl-2 homolog, Bcl2l10, and by promoting ER-mitochondria contact.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00151	Bcl2l10	Q9Z0F3	ER; MT	LMCS00209	Ahcyl1	Q80SW1	ER; MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00082	Ern1_Marchf5	NA	2	Mouse	ER-MT; MT-ER	1	31368599	These results show that IRE1α and MITOL are enriched at the MAM.; IRE1α is a novel substrate for MITOL; Endogenous IRE1α was found to be co‐precipitated with endogenous MITOL.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00142	Ern1	Q9EQY0	ER	LMCS00192	Marchf5	Q3KNM2	ER; MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00083	TGM2_VDAC1_ITPR1_HSPA9	TGM2_HSPA9(LTP)	4	Human	ER-MT; MT-ER	1	30590033	GRP75 localizes in Mitochondrion-associated membranes (MAMs) and acts as a bridging molecule between the two organelles by assembling the IP3R-GRP75-VDAC complex, which is involved in the transport of Ca2+from the endoplasmic reticulum (ER) to Mitochondrion.TG2 interacts with GRP75 in mitochondria-associated membranes (MAMs).	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00157	TGM2	P21980	MT	LMCS00173	VDAC1	P21796	MT	LMCS00174	HSPA9	P38646	MT	LMCS00213	ITPR11	Q14643	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00084	Vapb_Rmdn3	NA	2	Rat	ER-MT; MT-ER	3	30841933	The VAPB-PTPIP51 endoplasmic reticulum-mitochondria tethering proteins are present in neuronal synapses and regulate synaptic activity.	28337542	However, many neuronal functions damaged in Parkinson’s disease are regulated by signalling between the endoplasmic reticulum (ER) and mitochondria. This signalling involves close physical associations between the two organelles that are mediated by binding of the integral ER protein vesicle-associated membrane protein-associated protein B (VAPB) to the outer mitochondrial membrane protein, protein tyrosine phosphatase-interacting protein 51 (PTPIP51). VAPB and PTPIP51 thus act as a scaffold to tether the two organelles.	35090998	Lanthanum decreased VAPB-PTPP51, BAP31-FIS1, and MFN2-MFN1 expression of mitochondria-associated membranes and induced abnormal autophagy in rat hippocampus.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00159	Rmdn3	Q66H15	MT	LMCS00160	Vapb	Q9Z269	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00085	Mfn2_Mfn1	NA	2	Rat	ER-MT; MT-ER	1	35090998	Lanthanum decreased VAPB-PTPP51, BAP31-FIS1, and MFN2-MFN1 expression of mitochondria-associated membranes and induced abnormal autophagy in rat hippocampus.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00427	Mfn2	Q8R500	MT	LMCS00428	Mfn1	Q8R4Z9	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00086	ERN1_MARCHF5	ERN1_MARCHF5(LTP)	2	Human	ER-MT; MT-ER	1	31368599	These results show that IRE1α and MITOL are enriched at the MAM.; IRE1α is a novel substrate for MITOL; Endogenous IRE1α was found to be co‐precipitated with endogenous MITOL.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00164	ERN1	O75460	ER	LMCS00225	MARCHF5	Q9NX47	ER; MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00087	PIGBOS_CLCC1	NA	2	Human	ER-MT; MT-ER	1	31653868	PIGBOS localizes to the mitochondrial outer membrane where it interacts with the ER protein CLCC1 at ER-mitochondria contact sites.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00165	PIGBOS	A0A0B4J2F0	MT	LMCS00166	CLCC1	Q96S66	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00088	Bcap31_Fis1	NA	2	Rat	ER-MT; MT-ER	1	35090998	Lanthanum decreased VAPB-PTPP51, BAP31-FIS1, and MFN2-MFN1 expression of mitochondria-associated membranes and induced abnormal autophagy in rat hippocampus.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00169	Fis1	P84817	MT	LMCS00170	Bcap31	Q6AY58	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00089	VDAC1_ITPR1_HSPA9	NA	3	Human	ER-MT; MT-ER	3	29367884	Following GRP75 silencing, we found that IP3R1-VDAC1 interaction sites, as indicated by the red punctae (Figure 1c), were reduced compared with control cells.	30590033	GRP75 localizes in mitochondria-associated membranes (MAMs) and acts as a bridging molecule between the two organelles by assembling the IP3R-GRP75-VDAC complex, which is involved in the transport of Ca2+ from the endoplasmic reticulum (ER) to mitochondria.	24947355	Mitochondria-associated endoplasmic reticulum (ER) membranes (MAMs) are functional domains between both organelles involved in Ca2+ exchange, through the voltage-dependent anion channel (VDAC)-1/glucose-regulated protein 75 (Grp75)/inositol 1,4,5-triphosphate receptor (IP3R)-1 complex, and regulating energy metabolism.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00173	VDAC1	P21796	MT	LMCS00174	HSPA9	P38646	MT	LMCS00213	ITPR11	Q14643	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00090	MFN1_MFN2	MFN1_MFN2(LTP)	2	Human	ER-MT; MT-ER	1	19052620	An in vitro assay as well as genetic and biochemical evidences support a model in which mitofusin 2 on the ER bridges the two organelles by engaging in homotypic and heterotypic complexes with mitofusin 1 or 2 on the surface of Mitochondrion.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00177	MFN1	Q8IWA4	MT	LMCS00176	MFN2	O95140	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00091	MFN2_MFN2	MFN2_MFN2(LTP)	2	Human	ER-MT; MT-ER	1	19052620	An in vitro assay as well as genetic and biochemical evidences support a model in which mitofusin 2 on the ER bridges the two organelles by engaging in homotypic and heterotypic complexes with mitofusin 1 or 2 on the surface of Mitochondrion.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00176	MFN2	O95140	MT	LMCS00176	MFN2	O95140	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00092	BCAP31_FIS1	BCAP31_FIS1(LTP)	2	Human	ER-MT; MT-ER	1	21183955	Fis1 and Bap31 bridge the Mitochondrion-ER interface to establish a platform for apoptosis induction.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00186	FIS1	Q9Y3D6	MT	LMCS00187	BCAP31	P51572	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00093	BCAP31_TOMM40_NDUFS4	BCAP31_TOMM40(LTP); BCAP31_NDUFS4(LTP)	3	Human	ER-MT; MT-ER	1	31206022	By performing database analyses and co-immunoprecipitation assays, I identified that mitochondrial proteins Tom40 and pre-NDUFS4/NDUFS4 are associating partners of BAP31 at the ER-mitochondria contact sites.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00187	BCAP31	P51572	ER	LMCS00223	TOM40	O96008	MT	LMCS00224	NDUFS4	O43181	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00094	ERP44_ITPR3	NA	2	Human	ER-MT; MT-ER	1	21854214	ERp44 distributes in ERGIC, ER, and MAM, in-teracting preferentially with reduced IP3R1 and inhibiting the channel activity.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00188	ERP44	Q9BS26	ER	LMCS00229	ITPR3	Q14573	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00095	VAPB_RMDN3	VAPB_RMDN3(LTP)	2	Human	ER-MT; MT-ER	3	22131369	Modulating PTPIP51 expression alters the association of VAPB with Mitochondrion.	28132811	Finally, we demonstrate that the mechanism by which the VAPB-PTPIP51 tethers regulate autophagy involves their role in mediating delivery of Ca2+ to Mitochondrion from ER stores.	28337542	alpha-Synuclein is a MAM protein and binds to VAPB but not PTPIP51 in immunoprecipitation assays.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00190	RMDN3	Q96TC7	MT	LMCS00191	VAPB	O95292	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00096	VPS13A_VAPB_VAPA	VAPA_VPS13A(HTP: 1.00); VAPB_VPS13A(HTP: 1.00); VAPA_VAPB(LTP)	3	Human	ER-MT; MT-ER	2	30093493	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.	30741634	VPS13A interacts with the ER residing protein VAP-A via its FFAT domain.Interaction with Mitochondrion is mediated via its C-terminal domain.In VPS13A-depleted cells, ER-Mitochondrion contact sites are decreased, Mitochondrion are fragmented and mitophagy is decreased.; Our results showed that VPS13A also interacts with VAP-B in a FFAT dependent manner, consistent with the fact that VAP-A and VAP-B functions are often redundant.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00219	VPS13A	Q96RL7	MT	LMCS00191	VAPB	O95292	ER	LMCS00220	VAPA	Q9P0L0	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00097	Esyt1_Synj2bp	NA	2	Mouse	ER-MT; MT-ER	1	https://doi.org/10.1101/2022.11.14.516495	The deletion of ESYT1 or SYNJ2BP reduced the number and length of MERCs, indicating that the ESYT1-SYN2JBP complex plays a role in tethering ER and mitochondria.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00595	Esyt1	Q3U7R1	ER	LMCS00138	Synj2bp	Q9D6K5	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00098	VAPB_VAPA_OSBPL2	VAPA_OSBPL2(HTP: 1.00); VAPA_VAPB(LTP); VAPB_OSBPL2(HTP: 1.00)	3	Human	ER-LD; LD-ER	1	25420878	We provide evidence that complexes of human ORP2 and VAPs at ER–lipid droplet interfaces regulate the hydrolysis of triglycerides and lipid droplet turnover.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00091	VAPB	O95292	ER	LMCS00092	VAPA	Q9P0L0	ER	LMCS00028	OSBPL2	Q9H1P3	LD	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00099	Fundc1_Canx	NA	2	Mouse	ER-MT; MT-ER	1	27145933	Here, we describe a new pathway mediating Mitochondrionl fission and subsequent mitophagy under hypoxic conditions.FUNDC1 accumulates at the MAM by associating with the ER membrane protein calnexin.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00198	Canx	P35564	ER	LMCS00202	Fundc1	Q9DB70	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00100	FUNDC1_CANX	NA	2	Human	ER-MT; MT-ER	2	27145933	FUNDC1 accumulates at the MAM by associating with the ER membrane protein calnexin.	27314574	We have shown that the outer Mitochondrionl membrane protein FUNDC1 is a novel Mitochondrionl-associated membrane (MAM) protein, enriched at the MAM by interacting with the ER resident protein CANX (calnexin) under hypoxia.As mitophagy proceeds, it dissociates from CANX and preferably recruits DNM1L.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00199	CANX	P27824	ER	LMCS00201	FUNDC1	Q8IVP5	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00101	FUNDC1_DNM1L	NA	2	Human	ER-MT; MT-ER	2	27145933	Triple-color imaging further demonstrated that FUNDC1 and DRP1 puncta are closely associated with lacunae formed by ER lattices in hypoxic conditions.	27314574	We have shown that the outer Mitochondrionl membrane protein FUNDC1 is a novel Mitochondrionl-associated membrane (MAM) protein, enriched at the MAM by interacting with the ER resident protein CANX (calnexin) under hypoxia.As mitophagy proceeds, it dissociates from CANX and preferably recruits DNM1L.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00200	DNM1L	O00429	ER	LMCS00201	FUNDC1	Q8IVP5	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00102	Fundc1_Dnm1l	NA	2	Mouse	ER-MT; MT-ER	1	27145933	We found that DRP1 is also enriched in the MAM fraction in hypoxic cells and localizes with FUNDC1 in the MAM as evidenced by double immunogold EM. Triple‐color imaging further demonstrated that FUNDC1 and DRP1 puncta are closely associated with lacunae formed by ER lattices in hypoxic conditions.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00203	Dnm1l	Q8K1M6	ER	LMCS00202	Fundc1	Q9DB70	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00103	Fundc1_Itpr2	NA	2	Mouse	ER-MT; MT-ER	1	28942427	In cardiomyocytes, FUNDC1 binds to IP3R2 to form MAMs, which modulates Ca2+ release from ER into mitochondria and cytosols.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00212	Itpr2	Q9Z329	MT	LMCS00202	Fundc1	Q9DB70	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00104	Mfn1_Mfn2	Mfn1_Mfn2(LTP)	2	Mouse	ER-MT; MT-ER	2	27647893	Structurally, homo- or heterotypic in transinteraction between the ER-Mfn2 and Mitochondrionl Mfn2 or Mfn1 are supported by Mfn2’s role in Mitochondrionl tethering and fusion.	19052620	An in vitro assay as well as genetic and biochemical evidences support a model in which mitofusin 2 on the ER bridges the two organelles by engaging in homotypic and heterotypic complexes with mitofusin 1 or 2 on the surface of Mitochondrion.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00206	Mfn1	Q811U4	MT	LMCS00205	Mfn2	Q80U63	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00105	Mfn2_Mfn2	NA	2	Mouse	ER-MT; MT-ER	2	27647893	Structurally, homo- or heterotypic in transinteraction between the ER-Mfn2 and Mitochondrionl Mfn2 or Mfn1 are supported by Mfn2’s role in Mitochondrionl tethering and fusion.	19052620	Mitofusin 2 tethers endoplasmic reticulum to Mitochondrion Mitofusin 2 ablation increases endoplasmic reticulum-Mitochondrion coupling.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00205	Mfn2	Q80U63	MT	LMCS00205	Mfn2	Q80U63	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00106	Pml_Itpr3_Akt1_Ppp2r2b	Akt1_Ppp2r2b(LTP)	4	Mouse	ER-MT; MT-ER	1	21030605	We found that Pml, IP3R3, Akt, and PP2a colocalize in high molecular weight complexes, supporting their possible interaction in the native state.; We show that extranuclear Pml was specifically enriched at the endoplasmic reticulum (ER) and at the mitochondria-associated membranes, signaling domains involved in ER-to-mitochondria calcium ion (Ca2+) transport and in induction of apoptosis.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00207	Itpr3	P70227	ER	LMCS00385	pml	Q60953	ER	LMCS00386	Akt1	P31750	NA	LMCS00387	Ppp2r2b	Q6ZWR4	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00107	Itpr3_Hspa9_Vdac1_Park7	Itpr3_Hspa9(LTP); Park7_Itpr3(LTP); Park7_Hspa9(LTP); Park7_Vdac1(LTP)	4	Mouse	ER-MT; MT-ER	1	31767755	DJ-1 regulates the integrity and function of ER-mitochondria association through interaction with IP3R3-GRP75-VDAC1.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00207	Itpr3	P70227	ER	LMCS00216	Hspa9	P38647	MT	LMCS00230	Vdac1	Q60932	MT	LMCS00231	Park7	Q99LX0	ER; MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00108	VDAC1_GSK3B	NA	2	Human	ER-MT; MT-ER	1	29523440	Rapid activation of Akt by mTORC2 led to inhibition of Gsk-3b at mitochondria-ER junctions, enabling recruitment of hexokinase I (HK-I) to the mitochondrial channel, VDAC.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00214	GSK3B	P49841	ER	LMCS00173	VDAC1	P21796	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00109	VAPA_VPS13A	VAPA_VPS13A(HTP: 1.00)	2	Human	ER-MT; MT-ER	1	30741634	VPS13A interacts with the ER residing protein VAP-A via its FFAT domain.Interaction with Mitochondrion is mediated via its C-terminal domain.In VPS13A-depleted cells, ER-Mitochondrion contact sites are decreased, Mitochondrion are fragmented and mitophagy is decreased.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00220	VAPA	Q9P0L0	ER	LMCS00219	VPS13A	Q96RL7	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00110	INF2_SPIRE1	NA	2	Human	ER-MT; MT-ER	1	26305500	We propose Spire1C cooperates with INF2 to regulate actin assembly at ER-mitochondrial contacts.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00221	SPIRE1	Q08AE8	MT	LMCS00222	INF2	Q27J81	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00111	SEC22B_STIM1	SEC22B_STIM1(HTP: 105.00)	2	Human	ER-PM; PM-ER	1	37794132	Total internal reflection microscopy (TIRF) analysis allowed simultaneous imaging of Sec22b and STIM1 recruitment to ER-PM MCS, visible as puncta at the PM plane, during the activation of store-operated Ca2+ entry (SOCE) .	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00254	SEC22B	O75396	ER	LMCS00279	STIM1	Q13586	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00112	MMM1_MDM12	MMM1_MDM12(LTP)	2	Yeast	ER-MT; MT-ER	1	29279306	Structure-function insights into direct lipid transfer between membranes by Mmm1-Mdm12 of ERMES.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00181	MMM1	P41800	ER	LMCS00179	MDM12	Q92328	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
CMCS00113	ITPR3_HSPA9_VDAC1	ITPR3_VDAC1(LTP); ITPR3_HSPA9(LTP)	3	Human	ER-MT; MT-ER	2	17178908	VDAC1, grp75, and IP3Rs are present in a macromolecular complex at the ER-mitochondria interface.	29367884	In fact, we showed that GRP75 knockdown and pharmacological inhibition reduced the number of interaction sites between IP3R1 and VDAC1, thus reduced ER-mitochondrial coupling.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00173	VDAC1	P21796	MT	LMCS00174	HSPA9	P38646	MT	LMCS00229	ITPR3	Q14573	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00114	SIGMAR1_ITPR3	SIGMAR1_ITPR3(LTP)	2	Human	ER-MT; MT-ER	1	27821430	All these data indicate that the Sig1R activation that regulates IP3R3‐mediated intracellular Ca2+ flux at the MAM is crucial to prevent MAM disruption in motor neurons both in vitro and in vivo.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00229	ITPR3	Q14573	NA	LMCS00233	SIGMAR1	Q99720	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00115	PEX3_INP1	PEX3_INP1(LTP)	2	Yeast	ER-Peroxisome; Peroxisome-ER	1	23900285	Inp1p bridges the two compartments by acting as a molecular hinge between ER-bound Pex3p and peroxisomal Pex3p.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00240	PEX3	P28795	ER; Peroxisome	LMCS00241	INP1	Q03694	Peroxisome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00116	VAPB_VAPA_ACBD5	VAPA_ACBD5(HTP: 7.17); VAPB_ACBD5(HTP: 22.05); VAPA_VAPB(LTP)	3	Human	ER-Peroxisome; Peroxisome-ER	1	28108526	VAPs and ACBD5 tether peroxisomes to the ER for peroxisome maintenance and lipid homeostasis.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00242	ACBD5	Q5T8D3	Peroxisome	LMCS00243	VAPA	Q9P0L0	ER	LMCS00255	VAPB	O95292	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00117	VAPB_ACBD4	VAPB_ACBD4(HTP: 1.00)	2	Human	ER-Peroxisome; Peroxisome-ER	1	28463579	Here, we characterize acyl-CoA binding domain protein 4 (ACBD4) as a tail-anchored peroxisomal membrane protein which interacts with the ER protein, vesicle-associated membrane protein-associated protein-B (VAPB) to promote peroxisome-ER associations.	NA	NA	NA	NA	NA	NA	PI(4,5)P2	125105	C9H21O17P3	C(C(COP(=O)(O)OC1C(C(C(C(C1O)OP(=O)(O)O)OP(=O)(O)O)O)O)O)O	NA	NA	NA	NA	LMCS00244	ACBD4	Q8NC06	Peroxisome	LMCS00255	VAPB	O95292	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00118	PI(4,5)P2_ESYT2_ESYT1_ESYT3	ESYT1_ESYT2(LTP)	4	Human	ER-Peroxisome; Peroxisome-ER	1	31144242	Depletion of peroxisomal PI(4,5)P2 or E-Syts hampers peroxisome-ER membrane contact formation and blocks cholesterol transport from one organelle to another, resulting in cholesterol accumulation in lysosomes.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00245	ESYT2	A0FGR8	ER	LMCS00246	ESYT3	A0FGR9	ER	LMCS00247	ESYT1	Q9BSJ8	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00119	ABCD3_ATF6	NA	2	Human	ER-Peroxisome; Peroxisome-ER	1	31149896	Ceapins induce the neomorphic association of ER and peroxisomes by directly tethering the cytosolic domain of ATF6a to ABCD3’s transmembrane regions without inhibiting or depending on ABCD3 transporter activity.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00248	ATF6	P18850	ER	LMCS00249	ABCD3	P28288	Peroxisome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00120	PEX24_PEX32_INP1	NA	3	Yeast	ER-Peroxisome; Peroxisome-ER	1	32665322	This indicates that Pex11 contributes to Pex32-dependent peroxisome-ER contact formation.Pex24 and Pex32 are required to tether peroxisomes to the ER for organelle biogenesis, positioning and segregation in Yeast.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00250	PEX32	A4GFD3	ER	LMCS00251	INP1	C0JW63	Peroxisome	LMCS00252	PEX24	A4GFC9	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00121	Jph1_Jph2_Jph3	NA	3	Mouse	ER-PM; PM-ER	1	10949023	Junctional complexes between the plasma membrane (PM) and endoplasmic or sarcoplasmic reticulum (ER or SR) are a common feature of all excitable cell types and mediate cross-talk between cell surface and intracellular ion channels.We have identified the junctophilins (JPs), a novel conserved family of proteins that are components of the junctional complexes.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00257	Jph2	Q9ET78	ER	LMCS00258	Jph1	Q9ET80	ER	LMCS00256	Jph3	Q9ET77	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00122	ORAI1_STIM1_TRPC1	STIM1_ORAI1(LTP); STIM1_TRPC1(LTP)	3	Human	ER-PM; PM-ER	1	18644792	Orai1 Mediates the Interaction between STIM1 and hTRPC1 and Regulates the Mode of Activation of hTRPC1-forming Ca2+ Channels.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00260	ORAI1	Q96D31	PM	LMCS00261	TRPC1	P48995	PM	LMCS00279	STIM1	Q13586	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00123	OSBPL2_OSBPL1A_VAPA_VAPB	VAPA_OSBPL2(HTP: 1.00); VAPB_OSBPL1A(LTP); VAPB_OSBPL2(HTP: 1.00); VAPA_VAPB(LTP); VAPA_OSBPL1A(LTP)	4	Human	ER-PM; PM-ER	1	21062391	The results provide the first evidence for a role of mammalian ORPs in sterol transport from the PM to the ER and LDs, and uncover a role for VAPs in maintaining ORP levels.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00262	OSBPL1A	Q9BXW6	NA	LMCS00263	OSBPL1A	Q9H1P3	PM	LMCS00281	VAPA	Q9P0L0	ER	LMCS00280	VAPB	O95292	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00124	SCS2_SCS22_IST2_TCB3_TCB1_TCB2	IST2_SCS2(LTP); IST2_TCB3(LTP); IST2_TCB1(LTP); IST2_TCB3(LTP); TCB1_TCB2(LTP); TCB1_TCB3(LTP); TCB2_TCB3(LTP)	6	Yeast	ER-PM; PM-ER	1	23237950	We have identified Ist2 (related to the mammalian TMEM16 family of ion channels) and the tricalbins (C2 domain-containing proteins similar to the extended synaptotagmin-like proteins E-Syt1/2/3) as ER tether proteins that function with the VAP orthologs Scs2 and Scs22 to establish junctions between the ER and PM.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00265	IST2	P38250	ER	LMCS00266	SCS2	P40075	ER	LMCS00267	TCB2	P48231	ER; PM	LMCS00268	TCB3	Q03640	ER; PM	LMCS00269	TCB1	Q12466	ER; PM	LMCS00270	SCS22	Q6Q595	ER	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00125	VAPB_PITPNM1	VAPB_PITPNM1(HTP: 1.00)	2	Human	ER-PM; PM-ER	1	26028218	These results confirmed that Nir2 was an ER-associated peripheral protein in the quiescent state but after PLC activation it also formed contacts with the PM.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00271	PITPNM1	O00562	PM	LMCS00280	VAPB	O95292	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00126	ORAI1_TRPC1	NA	2	Human	ER-PM; PM-ER	1	19249086	These studies establish a molecular mechanism for store-operated Ca2+ entry in which the direct binding of STIM1 to Orai1 drives the accumulation and the activation of CRAC channels at ER-PM junctions.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00260	ORAI1	Q96D31	NA	LMCS00279	STIM1	Q13586	ER; PM	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00127	GRAMD2A_STIM1	NA	2	Human	ER-PM; PM-ER	1	29469807	They localize to ER-PM contact sites  GRAMD2a pre-marks a subset of ER-PM contacts used for STIM1 recruitment.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00275	GRAMD2A	Q8IUY3	ER	LMCS00279	STIM1	Q13586	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00128	GRAMD2A_ESYT2_ESYT3	NA	3	Human	ER-PM; PM-ER	1	29469807	GRAMD2a, but not GRAMD1a, co-localizes with the E-Syt2/3 tethers at ER-PM contacts in a PIP lipid-dependent manner.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00275	GRAMD2A	Q8IUY3	ER	LMCS00282	ESYT2	A0FGR8	ER	LMCS00283	ESYT3	A0FGR9	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00129	YSP2_LAM4_LAM1_SIP3	YSP2_LAM4(LTP)	4	Yeast	ER-PM; PM-ER	1	26001273	StART-like domains from Ysp2p and its paralog Lam4p specifically bind sterols, and Ysp2p, Lam4p and their homologs Ysp1p and Sip3p target punctate ER-PM contact sites distinct from those occupied by known ER-PM tethers.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00284	YSP2	Q06681	NA	LMCS00285	LAM4	P38800	ER	LMCS00391	SIP3	P38717	ER	LMCS00401	LAM1	P38851	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00130	YSP2_LAM4_LAM1_SIP4_DGR2_YMR102C_LAM6_SLM1	YSP2_LAM4(LTP)	8	Yeast	ER-PM; PM-ER	1	28774891	Thus, together with proteomic data, cytological data support the existence of a novel distinct domain of the PM, which we term the MCL, comprised of the paralogous protein pairs of Ltc3/4, Lam1/Sip3, and Dgr2/Ymr102c.; Ltc1 colocalizes with MCL proteins and partially colocalizes with Slm1.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00284	YSP2	Q06681	NA	LMCS00285	LAM4	P38800	ER	LMCS00391	SIP3	P38717	ER	LMCS00401	LAM1	P38851	ER	LMCS00408	DGR2	P32330	NA	LMCS00409	YMR102C	Q03177	NA	LMCS00410	LAM6	Q08001	ER	LMCS00411	SLM1	P40485	NA
CMCS00131	Nvj3_MDM1	Nvj3_MDM1(LTP)	2	Yeast	ER-Vacuole; Vacuole-ER	2	26283797	We also show that Mdm1 and its paralogue Ydr179w-a (named Nvj3 in this study) localize to ER-vacuole MCSs independently of established tether Nvj1.	29146766	Here, we show that yeast ER–vacuole contact sites (NVJs) serve as sites for generating LDs in response to nutritional stress, and identify the ER–vacuole tether Mdm1 as a protein that demarcates sites of NVJ‐associated LD budding.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00287	MDM1	Q01846	ER	LMCS00288	Nvj3	Q03983	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00132	LAM6_VAC8	LAM6_VAC8(LTP)	2	Yeast	ER-Vacuole; Vacuole-ER	1	25987606	Ltc1 localized to ER-Mitochondrion and ER-vacuole contacts via the Mitochondrionl import receptors Tom70,71 and the vacuolar protein Vac8, respectively.	NA	NA	NA	NA	NA	NA	PI(3)P	643964	C41H80O16P2	CCCCCCCCCCCCCCCC(=O)OCC(COP(=O)(O)OC1C(C(C(C(C1O)OP(=O)(O)O)O)O)O)OC(=O)CCCCCCCCCCCCCCC	NA	NA	NA	NA	LMCS00289	VAC8	P39968	Vacuole	LMCS00290	LAM6	Q08001	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00133	VAPA_VAPB_PI(3)P_ULK1_WIPI2_RB1CC1	RB1CC1_ULK1(LTP); RB1CC1_VAPB(LTP); RB1CC1_VAPA(LTP); VAPA_VAPB(LTP)	6	Human	IM-ER; ER-IM	1	29628370	APs directly interact with FIP200 and ULK1 through their conserved FFAT motifs and stabilize the ULK1, FIP200 complex at the autophagosome formation sites on the ER.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00293	RB1CC1	Q8TDY2	NA	LMCS00295	ULK1	O75385	NA	LMCS00296	VAPB	O95292	ER	LMCS00297	VAPA	Q9P0L0	ER	LMCS00294	WIPI2	Q9Y4P8	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00134	OSH2_SCS2	OSH2_SCS2(LTP)	2	Yeast	ER-PM; PM-ER	1	12727870	For Osh2p and Osh3p, a second site is distributed uniformly around the entire cell periphery, possibly associated with the plasma membrane (data not shown). Thus, the interaction with Scs2p appears to restrict Osh proteins to regions of the ER adjacent to the other sites they target.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00278	OSH2	Q12451	PM	LMCS00266	SCS2	P40075	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00135	OSH3_SCS2	OSH3_SCS2(LTP)	2	Yeast	ER-PM; PM-ER	1	12727870	For Osh2p and Osh3p, a second site is distributed uniformly around the entire cell periphery, possibly associated with the plasma membrane (data not shown). Thus, the interaction with Scs2p appears to restrict Osh proteins to regions of the ER adjacent to the other sites they target.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00277	OSH3	P38713	PM	LMCS00266	SCS2	P40075	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00139	MTOR_RPTOR_MLST8_RHEB	NA	4	Human	LY-GA; GA-LY	1	29222112	Rheb localized on the Golgi membrane activates lysosome-localized mTORC1 at the Golgi-lysosome contact site.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00321	MTOR	P42345	LY	LMCS00323	RPTOR	Q8N122	LY	LMCS00319	MLST8	Q9BVC4	LY	LMCS00320	RHEB	Q15382	GA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00140	Mtor_Rptor_Mlst8_Rheb	NA	4	Mouse	LY-GA; GA-LY	1	29222112	Rheb localized on the Golgi membrane activates lysosome-localized mTORC1 at the Golgi-lysosome contact site.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00318	Mtor	Q9JLN9	LY	LMCS00317	Rptor	Q8K4Q0	LY	LMCS00316	Mlst8	Q9DCJ1	LY	LMCS00322	Rheb	Q921J2	GA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00141	PLIN2_Hspa8	NA	2	Mouse	LY-LD; LD-LY	1	26902588	This motif is recognized by HSPA8 Hsc70 (heat shock 70 kDa protein 8) that targets the protein to lysosomes.At the lysosome, the substrate proteins bind to the CMA receptor, LAMP2A (lysosome-associated membrane protein 2A),which then organizes into a multimeric complex for translocation of the substrate into the lumen.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00324	Hspa8	P63017	NA	LMCS00326	PLIN2	P43883	LD	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00142	PI(4,5)P2_SYT7	NA	2	Human	LY-Peroxisome	1	25860611	We further demonstrated that peroxisome forms transient lysosome-peroxisome membrane contact (LPMC) withlysosomethrough the binding of peroxisomal lipid PI(4,5)P2by lysosomal proteinSynaptotagminVII (Syt7).	NA	NA	NA	NA	NA	NA	PI(4,5)P2	125105	C9H21O17P3	C(C(COP(=O)(O)OC1C(C(C(C(C1O)OP(=O)(O)O)OP(=O)(O)O)O)O)O)O	NA	NA	NA	NA	LMCS00327	SYT7	O43581	LY	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
CMCS00143	PI(4,5)P2_Syt7	NA	2	Mouse	LY-Peroxisome	1	25860611	We further demonstrated that peroxisome forms transient lysosome-peroxisome membrane contact (LPMC) withlysosomethrough the binding of peroxisomal lipid PI(4,5)P2by lysosomal proteinSynaptotagminVII (Syt7).	NA	NA	NA	NA	NA	NA	PI(4,5)P2	125105	C9H21O17P3	C(C(COP(=O)(O)OC1C(C(C(C(C1O)OP(=O)(O)O)OP(=O)(O)O)O)O)O)O	NA	NA	NA	NA	LMCS00329	Syt7	Q9R0N7	LY	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
CMCS00145	ALS2_RAB5A	NA	2	Human	MT-Endosome; Endosome-MT	1	29469808	These findings define a novel pathway whereby Alsin catalyzes the assembly of the Rab5 endocytic machinery on Mitochondrion.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00336	RAB5A	P20339	Endosome; MT	LMCS00337	ALS2	Q96Q42	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00146	Mfn2_Plin1	NA	2	Mouse	MT-LD; LD-MT	1	28348166	Importantly, Mfn2 directly interacts with perilipin 1, facilitating the interaction between the mitochondria and the lipid droplet in response to adrenergic stimulation.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00341	Mfn2	Q80U63	MT	LMCS00342	Plin1	Q8CGN5	LD	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00147	Acsl1_Snap23_Vamp4	NA	3	Mouse	MT-LD; LD-MT	1	30190326	Thus, the interaction of SNAP23 and VAMP4 with ACSL1 during glucose deprivation, a condition that primes the cell to oxidize more FA, is consistent with tethering of LDs to the OMM during FA oxidation.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00343	Acsl1	P41216	MT	LMCS00348	Snap23	O09044	MT	LMCS00325	Vamp4	O70480	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00148	TBC1D15_RAB7A	TBC1D15_RAB7A(HTP: 0.61)	2	Human	MT-LY; LY-MT	1	29364868	Contact formation was promoted by active GTP-bound lysosomal RAB7, and contact untethering was mediated by recruitment of the RAB7 GTPase-activating protein TBC1D15 to mitochondria by FIS1 to drive RAB7 GTP hydrolysis and thereby release contacts.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00349	RAB7A	P51149	LY	LMCS00350	TBC1D15	Q8TC07	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00149	ESYT1_SYNJ2BP	ESYT1_SYNJ2BP(LTP)	2	Human	ER-MT; MT-ER	1	https://doi.org/10.1101/2022.11.14.516495	The deletion of ESYT1 or SYNJ2BP reduced the number and length of MERCs, indicating that the ESYT1-SYN2JBP complex plays a role in tethering ER and mitochondria.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00594	ESYT1	Q9BSJ8	ER	LMCS00335	SYNJ2BP	P57105	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00150	PEX11_MDM34	PEX11_MDM34(LTP)	2	Yeast	MT-Peroxisome; Peroxisome-MT	1	25769804	Moreover, we found that Pex11 and Mdm34 physically interact and that Pex11 plays a role in establishing the contact sites between peroxisomes and mitochondria through the ERMES complex.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00356	MDM34	P53083	MT	LMCS00357	PEX11	Q12462	Peroxisome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00151	FZO1_PEX34	NA	2	Yeast	MT-Peroxisome; Peroxisome-MT	1	29720625	We then focus on a little-studied yet highly disease-relevant contact, the Peroxisome-Mitochondria (PerMit) proximity, and uncover and characterize two tether proteins: Fzo1 and Pex34.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00360	PEX34	P25584	Peroxisome	LMCS00361	FZO1	P38297	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00152	SWH1_SCS2	SWH1_SCS2(LTP)	2	Yeast	Nucleus-Vacuole; Vacuole-Nucleus	1	12727870	This implies that the interaction with Scs2p is integrated with other targeting signals. For Osh1p, the other targeting determinant is the ankyrin repeat region targeting the NVJ.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00292	SWH1	P35845	NA	LMCS00139	SCS2	P40075	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
CMCS00153	Sec22b_Stim1	NA	2	Mouse	ER-PM; PM-ER	1	37794132	Total internal reflection microscopy (TIRF) analysis allowed simultaneous imaging of Sec22b and STIM1 recruitment to ER-PM MCS, visible as puncta at the PM plane, during the activation of store-operated Ca2+ entry (SOCE) .	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00081	Sec22b	O75396	ER	LMCS00086	Stim1	P70302	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00154	TOM40_VAM6_YPT7	VAM6_YPT7(LTP); VAM6_TOM40(LTP)	3	Yeast	MT-Vacuole; Vacuole-MT	1	29870720	Unexpectedly, our mutant analysis revealed the existence of two functionally independent vacuole-mitochondria MCSs: one formed by the Ypt7-Vps39-Tom40 tether and a second one by Vps13-Mcp1, which is redundant with ER-mitochondrial contacts formed by ERMES.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00367	TOM40	P23644	MT	LMCS00368	VAM6	Q07468	Vacuole	LMCS00376	YPT7	P32939	Vacuole	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00155	MCP1_VPS13	MCP1_VPS13(LTP)	2	Yeast	MT-Vacuole; Vacuole-MT	2	29870720	And a second one by Vps13-Mcp1, which is redundant with ER-Mitochondrionl contacts formed by ERMES.	28864540	Vps13-Mcp1 interact at vacuole-mitochondria interfaces and bypass ER-mitochondria contact sites.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00369	MCP1	Q12106	MT	LMCS00375	VPS13	Q07878	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00156	NVJ1_VAC8	NVJ1_VAC8(LTP)	2	Yeast	Nucleus-Vacuole; Vacuole-Nucleus	1	10888680	Nucleus-vacuole junctions in Saccharomyces cerevisiae are formed through the direct interaction of Vac8p with Nvj1p.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00377	NVJ1	P38881	Nucleus	LMCS00378	VAC8	P39968	Vacuole	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00157	LAM6_VAC8	LAM6_VAC8(LTP)	2	Yeast	Nucleus-Vacuole; Vacuole-Nucleus	1	26119743	We assayed whether Lam6 localized to ERMES-mediated contact sites. ; This observation, coupled with the fact that one of the physical interactors of Lam6 was the NVJ contact site protein Vac8.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00378	VAC8	P39968	Vacuole	LMCS00379	LAM6	Q08001	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
CMCS00158	SPAST_ABCD1_IST1_CHMP1B	IST1_CHMP1B(LTP); SPAST_IST1(HTP: -); SPAST_CHMP1B(LTP)	4	Human	Peroxisome-LD; LD-Peroxisome	1	31227594	Model of M1 Spastin in conjunction with ABCD1, IST1, and CHMP1B regulating LD–peroxisome contact formation and LD-to-peroxisome FA trafficking.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00380	IST1	P53990	LD	LMCS00381	CHMP1B	Q7LBR1	LD	LMCS00382	ABCD1	P33897	Peroxisome	LMCS00383	SPAST	Q9UBP0	LD	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00159	STIM_SARAF	NA	2	Human	ER-PM; PM-ER	1	22464749	SARAF Translocates to ER-PM Regions in a STIM1-Dependent Manner after Store Depletion.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00279	STIM1	Q13586	ER	LMCS00394	SARAF	Q96BY9	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00160	NET3C_PVA11	NA	2	Arabidopsis thaliana	ER-PM; PM-ER	2	24909329	The Plant Cytoskeleton, NET3C, and VAP27 Mediate the Link between the Plasma Membrane and Endoplasmic Reticulum.	27159525	The endoplasmic reticulum (ER) is connected to the plasma membrane (PM) through the plant-specific NETWORKED protein, NET3C, and phylogenetically conserved vesicle-associated membrane protein-associated proteins (VAPs).	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00398	NET3C	O82259	ER	LMCS00399	PVA11	Q8VZ95	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00161	Tgm2_Vdac1_Itpr1_Hspa9	Itpr1_Hspa9(LTP); Tgm2_Hspa9(LTP)	4	Mouse	ER-MT; MT-ER	1	30590033	GRP75 localizes in Mitochondrion-associated membranes (MAMs) and acts as a bridging molecule between the two organelles by assembling the IP3R-GRP75-VDAC complex, which is involved in the transport of Ca2+from the endoplasmic reticulum (ER) to Mitochondrion.TG2 interacts with GRP75 in mitochondria-associated membranes (MAMs).	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00216	Hspa9	P38647	MT	LMCS00230	Vdac1	Q60932	MT	LMCS00215	Tgm2	P21981	MT	LMCS00218	Itpr1	P11881	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00162	PPM1L_ABCD3	NA	2	Human	ER-GA; GA-ER	1	22796112	Acyl-CoA binding domain containing 3 (ACBD3) recruits the protein phosphatase PPM1L to ER-Golgi membrane contact sites.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00045	PPM1L	Q5SGD2	ER	LMCS00044	ABCD3	P28288	GA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00163	TRPC3_STIM1_PI(4,5)P2	NA	3	Human	ER-PM; PM-ER	1	35416932	TRPC3 channel gating by lipids requires localization at the ER-PM junctions defined by STIM1.; Notably, the activation and regulation of TRPC3 by PI(4,5)P2 require recruitment of TRPC3 to the ER/PM junctions at a PI(4,5)P2-rich domain.	NA	NA	NA	NA	NA	NA	PI(4,5)P2	125105	C9H21O17P3	C(C(COP(=O)(O)OC1C(C(C(C(C1O)OP(=O)(O)O)OP(=O)(O)O)O)O)O)O	NA	NA	NA	NA	LMCS00479	TRPC3	Q13507	PM	LMCS00279	STIM1	Q13586	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00164	SPTLC2_SPTLC1	SPTLC2_SPTLC1(HTP: -)	2	Human	ER-MT; MT-ER	1	34785538	This study demonstrates that the SPTLC1 and SPTLC2 subunits can interact in cis on the ER and in trans across membranes to form a functional SPT complex, the latter suggesting that de novo sphingolipid synthesis occurs at ER–mitochondria contact sites.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00482	SPTLC2	O15270	ER; MT	LMCS00481	SPTLC1	O15269	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00165	Sptlc2_Sptlc1	NA	2	Mouse	ER-MT; MT-ER	1	34785538	We demonstrate that mitochondrial SPTLC2 interacts and forms a complex in trans with the ER-localized SPT subunit SPTLC1.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00451	Sptlc2	P97363	ER; MT	LMCS00484	Sptlc1	O35704	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00166	At1g07985_sldp1_sldp2	NA	3	Arabidopsis thaliana	LD-PM; PM-LD	1	35348751	Here, we identified and characterized three proteins of Arabidopsis thaliana that form a lipid droplet (LD)–plasma membrane (PM) tethering complex in plant cells, namely LD-localized SEED LD PROTEIN (SLDP) 1 and SLDP2 and PM-localized LD-PLASMA MEMBRANE ADAPTOR (LIPA).	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00614	sldp1	F4I9U3	LD	LMCS00615	sldp2	A0A178UK34	LD	LMCS00460	At1g07985	Q3EDG6	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00167	OSBPL10_OSBPL9_VAPA_VAPB_PI(4)P	VAPB_OSBPL10(HTP: 1.00); OSBPL9_OSBPL10(HTP: 10.79); OSBPL9_VAPB(HTP: 6.69); VAPA_OSBPL10(HTP: 1.00); OSBPL9_VAPA(HTP: 11.72); SPAST_CHMP1B(LTP); VAPA_VAPB(LTP)	5	Human	ER-Endosome; Endosome-ER	1	34817532	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.	NA	NA	NA	NA	NA	NA	PI(4)P	643965	C41H80O16P2	CCCCCCCCCCCCCCCC(=O)OCC(COP(=O)(O)OC1C(C(C(C(C1O)O)OP(=O)(O)O)O)O)OC(=O)CCCCCCCCCCCCCCC	NA	NA	NA	NA	LMCS00465	OSBPL10	Q9BXB5	Endosome	LMCS00425	OSBPL9	Q96SU4	Endosome	LMCS00029	VAPA	Q9P0L0	ER	LMCS00035	VAPB	O95292	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00168	RFFL_PRKN	RFFL_PRKN(LTP)	2	Human	MT-Endosome; Endosome-MT	1	35373701	Endosomal-associated RFFL facilitates mitochondrial clearance by enhancing PRKN (parkin) recruitment to mitochondria.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00466	RFFL	Q8WZ73	Endosome	LMCS00467	PRKN	O60260	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00169	TMED9_PREB	NA	2	Human	ER-GA; GA-ER	1	34561617	A new type of ERGIC-ERES membrane contact mediated by TMED9 and SEC12 is required for autophagosome biogenesis.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00468	TMED9	Q9BVK6	ER	LMCS00469	PREB	Q9HCU5	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
CMCS00170	Sec22b_Stim1	NA	2	Mouse	ER-Phg; Phg-ER	1	37794132	By overexpressing and knocking down Sec22b in the presence and absence of STIM1, we show that Sec22b is present at and regulates ER-phagosome MCS independently of STIM proteins.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00472	Sec22b	O08547	ER	LMCS00475	Stim1	P70302	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
CMCS00171	Sec22b_Osbpl8	NA	2	Mouse	ER-Phg; Phg-ER	1	37794132	Moreover, Sec22b co-precipitated and was co-recruited to phagosomes with the PS,PI(4)P lipid exchange protein ORP8.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00472	Sec22b	O08547	ER	LMCS00477	Osbpl8	B9EJ86	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
CMCS00172	SEC22B_STIM1	SEC22B_STIM1(HTP: 105.00)	2	Human	ER-Phg; Phg-ER	1	37794132	We thus investigated whether a connection between Sec22b and STIM1 might exist either at the PM or phagosomes.; whereas overexpression of Sec22b had a dramatic effect on STIM1 recruitment that surprisingly did not translate to changes in cytosolic signals.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00473	SEC22B	O75396	ER	LMCS00474	STIM1	Q13586	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
CMCS00173	SEC22B_OSBPL8	NA	2	Human	ER-Phg; Phg-ER	1	37794132	Moreover, Sec22b co-precipitated and was co-recruited to phagosomes with the PS,PI(4)P lipid exchange protein ORP8.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00473	SEC22B	O75396	ER	LMCS00476	OSBPL8	Q9BZF1	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
CMCS00174	Vapb_Snca	NA	2	Rat	ER-MT; MT-ER	1	28337542	alpha-Synuclein is a MAM protein and binds to VAPB but not PTPIP51 in immunoprecipitation assays.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00160	Vapb	Q9Z269	ER	LMCS00130	Snca	P37377	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
CMCS00175	Vdac1_Itpr1_Hspa9	NA	3	Mouse	ER-MT; MT-ER	2	30590033	GRP75 localizes in Mitochondrion-associated membranes (MAMs) and acts as a bridging molecule between the two organelles by assembling the IP3R-GRP75-VDAC complex, which is involved in the transport of Ca2+from the endoplasmic reticulum (ER) to Mitochondrion.TG2 interacts with GRP75 in mitochondria-associated membranes (MAMs).	24947355	Mitochondria-associated endoplasmic reticulum (ER) membranes (MAMs) are functional domains between both organelles involved in Ca2+ exchange, through the voltage-dependent anion channel (VDAC)-1/glucose-regulated protein 75 (Grp75)/inositol 1,4,5-triphosphate receptor (IP3R)-1 complex, and regulating energy metabolism.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00216	Hspa9	P38647	MT	LMCS00230	Vdac1	Q60932	MT	LMCS00218	Itpr1	P11881	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00176	Pigbos1_Clcc1	NA	2	Rat	ER-MT; MT-ER	1	31653868	This result demonstrated that the PIGBOS-CLCC1 interaction can be regulated by modulation of ER-mitochondria contacts, and further bolstered the model of CLCC1 and PIGBOS interacting at ER-mitochondria contact sites.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00111	Pigbos1	C0HLN0	MT	LMCS00112	Clcc1	Q9WU61	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00177	Vdac1_Gsk3b	NA	2	Mouse	ER-MT; MT-ER	1	29523440	Rapid activation of Akt by mTORC2 led to inhibition of Gsk-3b at mitochondria-ER junctions, enabling recruitment of hexokinase I (HK-I) to the mitochondrial channel, VDAC.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00189	Gsk3b	Q9WV60	ER	LMCS00230	Vdac1	Q60932	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00178	ITPR3_HSPA9_VDAC1_PARK7	ITPR3_VDAC1(LTP); ITPR3_HSPA9(LTP); PARK7_ITPR3(LTP); PARK7_HSPA9(LTP); PARK7_VDAC1(LTP)	4	Human	ER-MT; MT-ER	1	31767755	DJ-1 regulates the integrity and function of ER-mitochondria association through interaction with IP3R3-GRP75-VDAC1.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00229	ITPR3	Q14573	ER	LMCS00174	HSPA9	P38646	MT	LMCS00173	VDAC1	P21796	MT	LMCS00407	PARK7	Q99497	MT; ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00179	VAPB_VAPA_MIGA2	VAPA_MIGA2(HTP: 1.00); VAPA_VAPB(LTP); VAPB_MIGA2(HTP: 1.00)	3	Human	ER-MT; MT-ER	1	31628041	MIGA2 binds to LDs and VAP proteins in the ER.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00191	VAPB	O95292	ER	LMCS00220	VAPA	Q9P0L0	ER	LMCS00344	MIGA2	Q7L4E1	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00180	Vapb_Vapa_Miga2	NA	3	Mouse	ER-MT; MT-ER	1	31628041	MIGA2 binds to LDs and VAP proteins in the ER.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00414	Vapb	Q9QY76	ER	LMCS00415	Vapa	Q9WV55	ER	LMCS00413	Miga2	Q8BK03	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00181	TCB1_TCB2_TCB3	TCB1_TCB2(LTP); TCB1_TCB3(LTP); TCB2_TCB3(LTP)	3	Yeast	ER-PM; PM-ER	1	22250200	In yeast, seven proteins contain SMP domains: Mmm1p, Mdm12p and Mdm34p in the ERMES complex; Tcb1p, Tcb2p and Tcb3p called tricalbins; and the protein encoded by the uncharacterized gene YPR091C, which we here name Nvj2p.; The tricalbins localize to ER–PM contacts.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00269	TCB1	Q12466	ER; PM	LMCS00267	TCB2	P48231	ER; PM	LMCS00268	TCB3	Q03640	ER; PM	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00182	IML2_PET10	IML2_PET10(LTP)	2	Yeast	LD-Parasitophorous Vacuole; Parasitophorous Vacuole-LD	1	26004510	To verify this interaction, we performed a pull-down of Iml2 and could detect an interaction with Pet10 specifically under stress conditions when Iml2 becomes an IB resident.; Since Iml2 binds LD proteins only under conditions where it is localized exclusively to IBs, this necessitates that LDs and IBs lie in close proximity during misfolding stress.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00373	IML2	P47031	Parasitophorous Vacuole	LMCS00374	PET10	P36139	LD	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00183	PDZD8_RAB7A_ZFYVE27	PDZD8_RAB7A(HTP: 0.00); RAB7A_ZFYVE27(HTP: 0.02)	3	Human	ER-Endosome; Endosome-ER	1	32686675	Our results identify the ER membrane proteins, PDZD8 and Protrudin, together with the late endosomal protein Rab7, as components of an ER-late endosome MCS in mammalian cells.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00023	PDZD8	Q8NEN9	ER	LMCS00039	RAB7A	P51149	Endosome	LMCS00032	ZFYVE27	Q5T4F4	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00184	MCP1_VPS13	MCP1_VPS13(LTP)	2	Yeast	ER-MT; MT-ER	1	27280386	Together, these results suggest that Mcp1 must recruit Vps13 to mitochondrial membranes to compensate for ERMES defects.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00085	MCP1	Q12106	MT	LMCS00082	VPS13	Q07878	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00185	TRPC1_STIM1	TRPC1_STIM1(LTP)	2	Human	ER-PM; PM-ER	1	18430726	Store depletion induces STIM1 to aggregate and relocate into clusters at ER-plasma membrane junctions. Lipid raft-associated STIM1 interacts with TRPC1.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00261	TRPC1	P48995	PM	LMCS00279	STIM1	Q13586	ER; PM	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00186	Tdrkh_Atp5f1a	NA	2	Mouse	ER-MT; MT-ER	1	29785746	In addition, immunofluorescence further revealed that TDRKH co-localizes with mitochondrial marker protein ATP5A in mouse testes, which providing the possibility for its location in MAM.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00445	Tdrkh	Q80VL1	MT	LMCS00156	Atp5f1a	Q03265	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00187	SYNJ2BP_RRBP1	SYNJ2BP_RRBP1(HTP: 1.00)	2	Human	ER-MT; MT-ER	1	28441135	Follow-up experiments showed that overexpression of SYNJ2BP in HEK 293T cells leads to a dramatic increase in mitochondrial contacts specifically with rough ER membrane, mediated by SYNJ2BP’s binding partner on the ER membrane, RRBP1.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00335	SYNJ2BP	P57105	NA	LMCS00273	RRBP1	Q9P2E9	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
CMCS00188	Vps13D_RHOT2_RHOT1_VAPA_VAPB	RHOT2_RHOT1(HTP: 1.00); RHOT2_VPS13D(HTP: 1.00); VAPA_VAPB(LTP); RHOT2_VAPA(HTP: 0.98); RHOT2_VAPB(HTP: 0.99)	5	Human	ER-MT; MT-ER	1	33891013	The interaction of VPS13D with the ER is mediated by VAP, and its interaction with either mitochondria or peroxisomes is mediated by Miro; VPS13D binds the ER protein VAP via an unconventional FFAT motif.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00486	VPS13D	Q5THJ4	NA	LMCS00228	RHOT2	Q8IXI1	MT	LMCS00232	RHOT1	Q8IXI2	MT	LMCS00191	VAPB	O95292	ER	LMCS00220	VAPA	Q9P0L0	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00189	Vps13d_Rhot2_Rhot1_Vapa_Vapb	NA	5	Mouse	ER-MT; MT-ER	1	33891013	The interaction of VPS13D with the ER is mediated by VAP, and its interaction with either mitochondria or peroxisomes is mediated by Miro.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00488	Vps13d	B1ART2	NA	LMCS00226	Rhot2	Q8JZN7	MT	LMCS00227	Rhot1	Q8BG51	MT	LMCS00414	Vapb	Q9QY76	ER	LMCS00415	Vapa	Q9WV55	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00190	Vps13D_RHOT2_RHOT1_VAPA_VAPB	RHOT2_RHOT1(HTP: 1.00); RHOT2_VPS13D(HTP: 1.00); VAPA_VAPB(LTP); RHOT2_VAPA(HTP: 0.98); RHOT2_VAPB(HTP: 0.99)	5	Human	ER-Peroxisome; Peroxisome-ER	1	33891013	The interaction of VPS13D with the ER is mediated by VAP, and its interaction with either mitochondria or peroxisomes is mediated by Miro.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00487	VPS13D	Q5THJ4	NA	LMCS00492	RHOT2	Q8IXI1	Peroxisome	LMCS00493	RHOT1	Q8IXI2	Peroxisome	LMCS00255	VAPB	O95292	ER	LMCS00243	VAPA	Q9P0L0	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00191	Vps13d_Rhot2_Rhot1_Vapa_Vapb	NA	5	Mouse	ER-Peroxisome; Peroxisome-ER	1	33891013	The interaction of VPS13D with the ER is mediated by VAP, and its interaction with either mitochondria or peroxisomes is mediated by Miro.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00489	Vps13d	B1ART2	NA	LMCS00490	Rhot2	Q8JZN7	Peroxisome	LMCS00491	Rhot1	Q8BG51	Peroxisome	LMCS00494	Vapb	Q9QY76	ER	LMCS00495	Vapa	Q9WV55	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00192	OSBPL3_VAPA_VAPB_RRAS	VAPB_OSBPL3(HTP: 1.00); VAPA_OSBPL3(HTP: 1.00); VAPA_VAPB(LTP)	4	Human	ER-PM; PM-ER	1	25447204	ORP3 is an R-Ras interacting oxysterol-binding protein homolog that regulates cell adhesion and is overexpressed in several cancers.; Furthermore, we present evidence that ORP3-VAPA complexes stimulate R-Ras signaling.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00496	OSBPL3	Q9H4L5	ER	LMCS00280	VAPB	O95292	ER	LMCS00281	VAPA	Q9P0L0	ER	LMCS00253	RRAS	P10301	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00193	Kcnb1_Vapa_Vapb	Kcnb1_Vapa(LTP); Kcnb1_Vapb(LTP)	3	Mouse	ER-PM; PM-ER	1	30012696	Multiplex immunolabeling revealed colocalization of Kv2.1 and Kv2.2 with endogenous VAPs at ER-PM junctions in brain neurons from male and female mice in situ and in cultured rat hippocampal neurons, and KO of VAPA in mammalian cells reduces Kv2.1 clustering.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00497	Kcnb1	Q03717	PM	LMCS00504	Vapa	Q9WV55	ER	LMCS00503	Vapb	Q9QY76	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00194	Kcnb2_Vapa_Vapb	NA	3	Mouse	ER-PM; PM-ER	1	30012696	Multiplex immunolabeling revealed colocalization of Kv2.1 and Kv2.2 with endogenous VAPs at ER-PM junctions in brain neurons from male and female mice in situ and in cultured rat hippocampal neurons, and KO of VAPA in mammalian cells reduces Kv2.1 clustering.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00498	Kcnb2	A6H8H5	PM	LMCS00504	Vapa	Q9WV55	ER	LMCS00503	Vapb	Q9QY76	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00195	Kcnb1_Vapa_Vapb	Kcnb1_Vapa(LTP)	3	Rat	ER-PM; PM-ER	2	30012696	Multiplex immunolabeling revealed colocalization of Kv2.1 and Kv2.2 with endogenous VAPs at ER-PM junctions in brain neurons from male and female mice in situ and in cultured rat hippocampal neurons, and KO of VAPA in mammalian cells reduces Kv2.1 clustering.	29941597	Kv2 potassium channels form endoplasmic reticulum/plasma membrane junctions via interaction with VAPA and VAPB.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00499	Kcnb1	P15387	PM	LMCS00506	Vapb	Q9Z269	ER	LMCS00505	Vapa	Q9Z270	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00196	Kcnb2_Vapa_Vapb	Kcnb2_Vapb(LTP)	3	Rat	ER-PM; PM-ER	2	30012696	Multiplex immunolabeling revealed colocalization of Kv2.1 and Kv2.2 with endogenous VAPs at ER-PM junctions in brain neurons from male and female mice in situ and in cultured rat hippocampal neurons, and KO of VAPA in mammalian cells reduces Kv2.1 clustering.	29941597	Kv2 potassium channels form endoplasmic reticulum/plasma membrane junctions via interaction with VAPA and VAPB.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00500	Kcnb2	Q63099	PM	LMCS00506	Vapb	Q9Z269	ER	LMCS00505	Vapa	Q9Z270	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00197	Kcnb1_VAPA_VAPB	VAPA_VAPB(LTP); KCNB1_VAPA(LTP); KCNB1_VAPB(LTP)	3	Human	ER-PM; PM-ER	2	30012696	These data together demonstrate that the Kv2 PRC domain is both necessary and sufficient for the unique ability of Kv2.1 (and Kv2.2) to recruit endogenous VAPA to ER-PM junctions in HEK293T cells.	29941597	Kv2 potassium channels form endoplasmic reticulum/plasma membrane junctions via interaction with VAPA and VAPB.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00501	KCNB1	Q14721	PM	LMCS00281	VAPA	Q9P0L0	ER	LMCS00280	VAPB	O95292	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00198	Kcnb2_VAPA_VAPB	VAPA_VAPB(LTP)	3	Human	ER-PM; PM-ER	2	30012696	These data together demonstrate that the Kv2 PRC domain is both necessary and sufficient for the unique ability of Kv2.1 (and Kv2.2) to recruit endogenous VAPA to ER-PM junctions in HEK293T cells.	29941597	Kv2 potassium channels form endoplasmic reticulum/plasma membrane junctions via interaction with VAPA and VAPB.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00502	KCNB2	Q92953	PM	LMCS00281	VAPA	Q9P0L0	ER	LMCS00280	VAPB	O95292	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00199	VAPA_OSBPL9	VAPA_OSBPL9(HTP: 11.72)	2	Human	ER-GA; GA-ER	1	15212954	Similar to OSBP, ORP9L localization to the Golgi apparatus and interaction with VAP-A on the ER suggest that it cycles or partitions between these organelles.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00057	VAPA	Q9P0L0	ER	LMCS00059	OSBPL9	Q96SU4	GA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00200	IncV_VAPA_VAPB	VAPA_VAPB(LTP)	3	Human; Chlamydia	ER-Parasitophorous vacuole; Parasitophorous vacuole-ER	1	29078338	We propose a model in which IncV acts as one of the primary tethers that contribute to the formation of ER-inclusion MCS.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00507	IncV	V8TPH4	Parasitophorous vacuole	LMCS00508	VAPA	Q9P0L0	ER	LMCS00509	VAPB	O95292	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00201	ESYT2_ESYT1_ESYT3	ESYT1_ESYT2(LTP)	3	Human	ER-PM; PM-ER	1	25787254	Because E-Syt1 interacts with both E-Syt2 and E-Syt3, E-Syt1 acts as a Ca2+-dependent regulator of E-Syt–mediated ER–PM tethering.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00282	ESYT2	A0FGR8	ER	LMCS00283	ESYT3	A0FGR9	ER	LMCS00512	ESYT1	Q9BSJ8	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00202	PI(4,5)P2_ESYT2_ESYT1_ESYT3	ESYT1_ESYT2(LTP)	4	Human	ER-PM; PM-ER	1	23791178	E-Syts tether the ER to the PM via C2 domain-PI(4,5)P2 interactions.	NA	NA	NA	NA	NA	NA	PI(4,5)P2	125105	C9H21O17P3	C(C(COP(=O)(O)OC1C(C(C(C(C1O)OP(=O)(O)O)OP(=O)(O)O)O)O)O)O	NA	NA	NA	NA	LMCS00282	ESYT2	A0FGR8	ER	LMCS00283	ESYT3	A0FGR9	ER	LMCS00512	ESYT1	Q9BSJ8	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00203	MMM1_MDM10_MDM12_MDM34	MMM1_MDM34(LTP); MDM12_GEM1(LTP); MDM12_MDM34(LTP); MDM12_MMM1(LTP); MDM10_MDM12(LTP); MDM10_MDM34(LTP); 	4	Yeast	ER-MT; MT-ER	2	19556461	We identified the Mmm1,Mdm10,Mdm12,Mdm36 complex as a molecular tether between ER and Mitochondrion.	22250200	A complex named the ER–mitochondrion encounter structure (ERMES) facilitates contacts between the ER and mitochondria.This complex consists of four proteins: Mdm10p and Mdm34p in the mitochondrial outer membrane, Mmm1p in the ER and the soluble protein Mdm12p.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00178	MDM34	P53083	MT	LMCS00181	MMM1	P41800	ER	LMCS00180	MDM10	P18409	MT	LMCS00179	MDM12	Q92328	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00204	VAPA_CERT1	NA	2	Human	ER-MVB; MVB-ER	1	35421371	VAP-A-CERT linkages at ER membrane contact sites drive biogenesis of RNA-containing Evs.; Ceramide transporter CERT localizes to MVBs and controls biogenesis of RNA-containing Evs.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00513	VAPA	Q9P0L0	ER	LMCS00514	CERT1	Q9Y5P4	MVB	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00205	PEX3_INP1	PEX3_INP1(LTP)	2	Yeast	PM-Peroxisome; Peroxisome-PM	1	32970792	The Pex3–Inp1 complex tethers yeast peroxisomes to the plasma membrane.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00516	PEX3	P28795	Peroxisome	LMCS00517	INP1	Q03694	PM	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00206	EHD1_ETMP1	NA	2	Entamoeba histolytica	Endosome-Mitosome; Mitosome-Endosome	1	35404118	We posit lipid and ion transport, mitosome fission, and quality control as potential processes that are mediated by the ETMP1-EHD1-tethered mitosome-endosome contact site in E. histolytica.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00518	EHD1	C4M131	Endosome	LMCS00519	ETMP1	C4LZN1	Mitosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00207	ATG18_ATG9_ATG2	ATG9_ATG18(LTP); ATG2_ATG18(LTP); ATG2_ATG9(LTP)	3	Yeast	ER-Phagophore; Phagophore-ER	2	29848619	Assembly of the Atg9–Atg2–Atg18 complex is important to establish phagophore–endoplasmic reticulum (ER) contact sites.	36354155	Sequential binding of yeast Atg2 and Atg18 to Atg9, the only conserved transmembrane protein in autophagy, at the extremities of the phagophore mediates the establishment of membrane contact sites between the phagophore and the endoplasmic reticulum.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00528	ATG18	P43601	NA	LMCS00529	ATG9	Q12142	ER	LMCS00530	ATG2	P53855	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00208	ORP2A_PVA11	ORP2A_PVA11(HTP: -)	2	Arabidopsis thaliana	ER-PM; PM-ER	1	36252028	Under normal conditions, ORP2A locates to EPCSs and interacts with VAP27-1.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00531	ORP2A	Q940Y1	ER	LMCS00399	PVA11	Q8VZ95	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00209	ORP2A_PVA11_ATG8E	ORP2A_PVA11(HTP: -)	3	Arabidopsis thaliana	ER-Autophagosome; Autophagosome-ER	1	36252028	However, upon autophagic induction, ORP2A interacts with VAP27-1 and ATG8e as a complex to bridge the EACSs.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00532	ORP2A	Q940Y1	ER	LMCS00533	PVA11	Q8VZ95	ER	LMCS00534	ATG8E	Q8S926	Autophagosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00210	PI(3)P_Uvrag_Atg14_Miga	NA	4	Fruit fly	ER-MT; MT-ER	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.	NA	NA	NA	NA	NA	NA	PI(3)P	643964	C41H80O16P2	CCCCCCCCCCCCCCCC(=O)OCC(COP(=O)(O)OC1C(C(C(C(C1O)OP(=O)(O)O)O)O)O)OC(=O)CCCCCCCCCCCCCCC	NA	NA	NA	NA	LMCS00521	Uvrag	Q9VK07	NA	LMCS00522	Atg14	Q9VCE1	NA	LMCS00523	Miga	Q9W3F7	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00211	TRB2_TRB1_PVA11	TRB2_TRB1(LTP)	3	Arabidopsis thaliana	ER-MT; MT-ER	1	36163196	ER-mitochondrial contact sites (EMCSs) are important for mitochondrial function. Here, we have identified a EMCS complex, comprising a family of uncharacterised mitochondrial outer membrane proteins, TRB1, TRB2, and the ER protein, VAP27-1.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00535	TRB2	Q9FJW5	ER; MT	LMCS00536	TRB1	Q8VWK4	MT	LMCS00291	PVA11	Q8VZ95	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00212	PI(4)P_Osbpl6	NA	2	Mouse	ER-PM; PM-ER	1	35518199	The present data clearly demonstrate ORP6 localizing to ER-PM contact sites by binding to PM PI4P through the PH domain.	NA	NA	NA	NA	NA	NA	PI(4)P	643965	C41H80O16P2	CCCCCCCCCCCCCCCC(=O)OCC(COP(=O)(O)OC1C(C(C(C(C1O)O)OP(=O)(O)O)O)O)OC(=O)CCCCCCCCCCCCCCC	NA	NA	NA	NA	LMCS00537	Osbpl6	Q8BXR9	ER	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
CMCS00213	CIDEC_PLIN1	NA	2	Human	LD-LD	1	23481402	Fsp27 accumulates at the LDCS when two LDs attach each other, creating a pore that specifically allows bidirectional lipid exchange.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00541	CIDEC	Q96AQ7	LD	LMCS00539	PLIN1	O60240	LD	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00214	Cidec_Plin1	NA	2	Mouse	LD-LD	1	23481402	Fsp27 accumulates at the LDCS when two LDs attach each other, creating a pore that specifically allows bidirectional lipid exchange.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00542	Cidec	P56198	LD	LMCS00540	Plin1	Q8CGN5	LD	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00215	CNM1_TOM70	CNM1_TOM70(LTP)	2	Yeast	Nucleus-MT; MT-Nucleus	1	34694322	We show that Cnm1 mediates contact by interacting with Tom70 on mitochondria.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00547	CNM1	P38083	Nucleus	LMCS00548	TOM70	P07213	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00216	CTL0402_STIM1	NA	2	Human; Chlamydia	ER-Parasitophorous vacuole; Parasitophorous vacuole-ER	1	36853051	Here, we show that the C. trachomatis inclusion membrane protein IncS (CTL0402) specifically recruits STIM1 to ER-inclusion MCS via direct interaction with a cytosolic domain of STIM1.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00551	CTL0402	A0A0H3MGT3	Parasitophorous vacuole	LMCS00550	STIM1	Q13586	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00217	CTL0402_Stim1	NA	2	Mouse; Chlamydia	ER-Parasitophorous vacuole; Parasitophorous vacuole-ER	1	36853051	Here, we show that the C. trachomatis inclusion membrane protein IncS (CTL0402) specifically recruits STIM1 to ER-inclusion MCS via direct interaction with a cytosolic domain of STIM1.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00551	CTL0402	A0A0H3MGT3	Parasitophorous vacuole	LMCS00549	Stim1	P70302	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00218	ACBD5_VAPB_GSK3B	ACBD5_VAPB(HTP: 22.05)	3	Human	ER-Peroxisome; Peroxisome-ER	1	35019937	Finally, we show that GSK3β can associate with the ACBD5–VAPB complex to regulate peroxisome–ER contacts by phosphorylating serine-269.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00242	ACBD5	Q5T8D3	Peroxisome	LMCS00255	VAPB	O95292	ER	LMCS00559	GSK3B	P49841	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00219	IMC10_LMF1	NA	2	Toxoplasma gondii	MT-Pellicle; Pellicle-MT	1	36314270	IMC10 and LMF1 mediate mitochondrial morphology through mitochondrion–pellicle contact sites in Toxoplasma gondii.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00560	IMC10	S7WH01	Pellicle	LMCS00561	LMF1	A0A125YTR6	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00220	IncV_VAPA_VAPB_CSNK2A1_CSNK2A2_ CSNK2B	CSNK2A1_ CSNK2B(LTP); CSNK2A2_ CSNK2B(LTP); VAPA_VAPB(LTP)	6	Human; Chlamydia	ER-Parasitophorous vacuole; Parasitophorous vacuole-ER	1	35838228	IncV/CK2/VAP interplay in ER-Inclusion MCS formation.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00563	IncV	V8TPH4	Parasitophorous vacuole	LMCS00564	VAPA	Q9P0L0	ER	LMCS00565	VAPB	O95292	ER	LMCS00562	CSNK2A1	P68400	Parasitophorous vacuole	LMCS00571	CSNK2A2	P19784	Parasitophorous vacuole	LMCS00654	CSNK2B	P67870	Parasitophorous vacuole	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00221	VAC8_LDO45_LDO16	NA	3	Yeast	LD-Vacuole; Vacuole-LD	1	10.1101/2023.04.21.537797	LDO proteins and Vac8 form a vacuole-lipid droplet contact site required for lipophagy in response to starvation	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00566	VAC8	P39968	Vacuole	LMCS00567	LDO45	P40218	LD	LMCS00568	LDO16	P40219	LD	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00222	LONP1_FUNDC1_ULK1	NA	3	Human	ER-MT; MT-ER	1	36927870	Accordingly, our findings highlight a novel mechanism responsible for mitophagy initiation under hypoxia by chaperone Lon in mitochondria through the interaction with FUNDC1-ULK1 complex at the EMC site.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00432	LONP1	P36776	MT	LMCS00201	FUNDC1	Q8IVP5	MT	LMCS00569	ULK1	O75385	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00223	Vapb_Miga2	NA	2	Mouse	ER-MT; MT-ER	1	35764626	These structures reveal that the MIGA2 LD targeting domain has a large internal hydrophobic pocket that accommodates phospholipids and that two phosphorylations of the FFAT motif are required for tight interaction of MIGA2 with VAPB, which enhances the rate of lipid transport.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00414	Vapb	Q9QY76	ER	LMCS00413	Miga2	Q8BK03	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00224	Plin2_Tp53	NA	2	Mouse	MT-LD; LD-MT	1	37055989	This study aimed to assess the molecular machinery of mitochondria and LDs contacts involved in hepatic lipotoxicity and uncover the critical role of mito-p53-PLIN2 interaction in AFB1 exposure-induced lipid metabolic disorders.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00572	Plin2	P43883	MT	LMCS00575	Tp53	P02340	LD	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00225	PLIN2_TP53	NA	2	Human	MT-LD; LD-MT	1	37055989	This study aimed to assess the molecular machinery of mitochondria and LDs contacts involved in hepatic lipotoxicity and uncover the critical role of mito-p53-PLIN2 interaction in AFB1 exposure-induced lipid metabolic disorders.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00573	PLIN2	Q99541	MT	LMCS00574	TP53	P04637	LD	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00226	PVA12_PVA11_MSL10	NA	3	Arabidopsis thaliana	ER-PM; PM-ER	1	https://doi.org/10.7936/2hqh-f829	I propose a model wherein MSL10’s direct interaction with VAP27s creates EPCSs which has implications for MSL10 function.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00577	PVA12	Q9SHC8	ER	LMCS00399	PVA11	Q8VZ95	ER	LMCS00576	MSL10	Q9LYG9	PM	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00227	Nrg2_Vapa_Vapb	NA	3	Mouse	ER-PM; PM-ER	1	36769244	Importantly, we demonstrate that proNRG2 promotes the formation of ER-PM junctions by directly binding the ER-resident membrane tether VAP, like Kv2.1.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00504	Vapa	Q9WV55	ER	LMCS00503	Vapb	Q9QY76	ER	LMCS00579	Nrg2	P56974	PM	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00228	Nrg2_Vapa_Vapb	NA	3	Rat	ER-PM; PM-ER	1	36769244	Importantly, we demonstrate that proNRG2 promotes the formation of ER-PM junctions by directly binding the ER-resident membrane tether VAP, like Kv2.1.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00506	Vapb	Q9Z269	ER	LMCS00505	Vapa	Q9Z270	ER	LMCS00578	Nrg2	O35569	PM	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00229	NRG2_VAPA_VAPB	VAPA_VAPB(LTP)	3	Human	ER-PM; PM-ER	1	36769244	Importantly, we demonstrate that proNRG2 promotes the formation of ER-PM junctions by directly binding the ER-resident membrane tether VAP, like Kv2.1.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00281	VAPA	Q9P0L0	ER	LMCS00280	VAPB	O95292	ER	LMCS00580	NRG2	O14511	PM	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00230	OSBPL5_OSBPL8_MIB1_APOO	OSBPL5_OSBPL8(HTP: 1.00)	4	Human	ER-MT; MT-ER	1	36130504	ORP5/8 and MIB/MICOS link ER-mitochondria and intra-mitochondrial contacts for non-vesicular transport of phosphatidylserine.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00146	OSBPL5	Q9H0X9	ER	LMCS00197	OSBPL8	Q9BZF1	ER	LMCS00581	MIB1	Q86YT6	MT	LMCS00582	APOO	Q9BUR5	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00231	OSBPL9_OSBPL10	OSBPL9_OSBPL10(HTP: 10.79)	2	Human	ER-GA; GA-ER	1	36853333	ORP9 and ORP10 form a heterocomplex to transfer phosphatidylinositol 4-phosphate at ER-TGN contact sites.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00059	OSBPL9	Q96SU4	NA	LMCS00583	OSBPL10	Q9BXB5	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
CMCS00232	VCP_FAF2	VCP_FAF2(LTP)	2	Human	ER-MT; MT-ER	1	36746962	The p97-UBXD8 complex regulates ER-Mitochondria contact sites by altering membrane lipid saturation and composition.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00584	VCP	P55072	NA	LMCS00585	FAF2	Q96CS3	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00233	Vcp_Faf2	NA	2	Human	ER-MT; MT-ER	1	36746962	The p97-UBXD8 complex regulates ER-Mitochondria contact sites by altering membrane lipid saturation and composition.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00586	Vcp	Q01853	NA	LMCS00587	Faf2	Q3TDN2	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00234	PLIN5_SLC27A4	NA	2	Human	MT-LD; LD-MT	1	37290445	We focused on perilipin 5 (PLIN5), an LD protein that tethers mitochondria, to probe the function and regulation of LD-mitochondria contacts.; We focused on perilipin 5 (PLIN5), an LD protein that tethers mitochondria, to probe the function and regulation of LD-mitochondria contacts.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00084	PLIN5	Q00G26	LD	LMCS00590	SLC27A4	Q6P1M0	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00235	Plin5_Slc27a4	NA	2	Mouse	MT-LD; LD-MT	1	37290445	We focused on perilipin 5 (PLIN5), an LD protein that tethers mitochondria, to probe the function and regulation of LD-mitochondria contacts.; We focused on perilipin 5 (PLIN5), an LD protein that tethers mitochondria, to probe the function and regulation of LD-mitochondria contacts.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00347	Plin5	Q8BVZ1	LD	LMCS00591	Slc27a4	Q91VE0	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00236	EIF2AK3_ESYT1	NA	2	Human	ER-MT; MT-ER	1	36821088	PERK recruits E-Syt1 at ER-mitochondria contacts for mitochondrial lipid transport and respiration.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00592	EIF2AK3	Q9NZJ5	ER	LMCS00594	ESYT1	Q9BSJ8	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00237	Eif2ak3_Esyt1	NA	2	Mouse	ER-MT; MT-ER	1	36821088	PERK recruits E-Syt1 at ER-mitochondria contacts for mitochondrial lipid transport and respiration.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00593	Eif2ak3	Q9Z2B5	ER	LMCS00595	Esyt1	Q3U7R1	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00238	ORAI1_STIM1_PI(4)P	STIM1_ORAI1(LTP)	3	Human	ER-PM; PM-ER	1	25517631	These findings identify a role for tethered ER/PM microdomains in regulating Ca2+ influx and directing STIM1-Orai1 conformational changes, and report on a new mode of regulation by PI(4,5)P2.	NA	NA	NA	NA	NA	NA	PI(4)P	643965	C41H80O16P2	CCCCCCCCCCCCCCCC(=O)OCC(COP(=O)(O)OC1C(C(C(C(C1O)O)OP(=O)(O)O)O)O)OC(=O)CCCCCCCCCCCCCCC	NA	NA	NA	NA	LMCS00260	ORAI1	Q96D31	PM	LMCS00279	STIM1	Q13586	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00239	cert_Osbp_vap_PI(4)P	NA	4	Fruit fly	ER-GA; GA-ER	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.	NA	NA	NA	NA	NA	NA	PI(4)P	643965	C41H80O16P2	CCCCCCCCCCCCCCCC(=O)OCC(COP(=O)(O)OC1C(C(C(C(C1O)O)OP(=O)(O)O)O)O)OC(=O)CCCCCCCCCCCCCCC	NA	NA	NA	NA	LMCS00597	cert	Q9Y128	NA	LMCS00599	Osbp	Q9VC05	NA	LMCS00601	vap	Q8IR23	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00240	cert_Osbp_vap_PI(4)P	NA	4	Fruit fly	ER-Autolysosome; Autolysosome-ER	1	37289040	Osbp and cert proteins were recruited by the autolysosomal PtdIns4P and established contacts between ER and autolysosomes.	NA	NA	NA	NA	NA	NA	PI(4)P	643965	C41H80O16P2	CCCCCCCCCCCCCCCC(=O)OCC(COP(=O)(O)OC1C(C(C(C(C1O)O)OP(=O)(O)O)O)O)OC(=O)CCCCCCCCCCCCCCC	NA	NA	NA	NA	LMCS00598	cert	Q9Y128	NA	LMCS00600	Osbp	Q9VC05	NA	LMCS00602	vap	Q8IR23	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00241	rdgB_dVAP-A	NA	2	Fruit fly	ER-PM; PM-ER	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.	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.	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.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00605	rdgB	P43125	NA	LMCS00606	dVAP-A	Q9W4N8	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00243	MpPHOT_MpRTN1	NA	2	Marchantia polymorpha	ER-PM; PM-ER	1	35476214	A model for collaborative organelle repositioning by phot and RTN in Marchantia polymorpha.In wild-type (WT) cells, Mpphot on the plasma membrane (PM) and MpRTN1 in the ER membrane interact at ER-PM contact sites.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00607	MpPHOT	A0A077KFI9	PM	LMCS00608	MpRTN1	A0A2R6X5G0	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00244	LIP1_sldp1	NA	2	Arabidopsis thaliana	LD-PM; PM-LD	1	10.1101/2022.01.13.476213	SLDP and LIPA mediate lipid droplet-plasma membrane tethering in Arabidopsis thaliana.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00613	LIP1	Q9ZWT1	PM	LMCS00614	sldp1	F4I9U3	LD	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00245	LIP1_sldp2	NA	2	Arabidopsis thaliana	LD-PM; PM-LD	1	10.1101/2022.01.13.476213	SLDP and LIPA mediate lipid droplet-plasma membrane tethering in Arabidopsis thaliana.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00613	LIP1	Q9ZWT1	PM	LMCS00615	sldp2	A0A178UK34	LD	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00246	SYTL2_RAB27A_PI(4,5)P2	SYTL2_RAB27A(LTP)	3	Human	PM-WP body; WP body-PM	1	35660980	Rab27a recruits Slp2-a to WPB via its SHD.; As a consequence, Slp2-a would be enriched at that part of the WPB which is closest to the PM and permits interactions with PM PI(4,5)P2.	NA	NA	NA	NA	NA	NA	PI(4,5)P2	125105	C9H21O17P3	C(C(COP(=O)(O)OC1C(C(C(C(C1O)OP(=O)(O)O)OP(=O)(O)O)O)O)O)O	NA	NA	NA	NA	LMCS00616	SYTL2	Q9HCH5	PM; WP body	LMCS00617	RAB27A	P51159	WP body	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00247	SNX5_VPS13A	NA	2	Human	ER-Endosome; Endosome-ER	1	36977596	We have identified the sorting nexin SNX5 as an interactor of VPS13A that mediates its association with endosomal subdomains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00618	SNX5	Q9Y5X3	Endosome	LMCS00619	VPS13A	Q96RL7	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00248	TEX2_PP4P1	NA	2	Human	ER-LY; LY-ER	1	36705603	Together, our data identify Tex2 as a tubular ER protein that resides at TMEM55-dependent ER–LE/lys MCSs required for lysosomal functions.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00623	TEX2	Q8IWB9	ER	LMCS00624	PP4P1	Q86T03	LY	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00249	TEX2_PP4P1	NA	2	Human	ER-Endosome; Endosome-ER	1	36705603	Together, our data identify Tex2 as a tubular ER protein that resides at TMEM55-dependent ER–LE/lys MCSs required for lysosomal functions.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00625	TEX2	Q8IWB9	ER	LMCS00626	PP4P1	Q86T03	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00250	TMED10_TMED2	TMED10_TMED2(HTP: 1.00)	2	Human	ER-MT; MT-ER	1	36174556	ER-Golgi-localized proteins TMED2 and TMED10 control the formation of plasma membrane lipid nanodomains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00627	TMED10	P49755	ER	LMCS00628	TMED2	Q15363	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00251	SACM1L_VAPA_TMED10_TMED2_OSBP_ARF1_PPM1L_CERT1	SACM1L_VAPA(HTP: -); TMED10_VAPA; TMED10_TMED2(HTP: 1.00)	8	Human	ER-GA; GA-ER	1	36174556	MCSs between the ER and the Golgi are well known to have two classes of complexes: one involved in cholesterol transfer, containing VAPA, SAC1, OSBP, and ARF1; and another involved in ceramide transfer, containing VAPA, PPM1L, and CERT. The above analysis shows not only that TMED2/10 are present in both these complexes and required for their existence but also that these two complexes actually can form supercomplexes, mediating the transfer of both cholesterol and ceramide, again in a TMED2/10-dependent manner.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00050	SACM1L	Q9NTJ5	ER	LMCS00057	VAPA	Q9P0L0	ER	LMCS00627	TMED10	P49755	GA	LMCS00628	TMED2	Q15363	GA	LMCS00629	OSBP	P22059	GA	LMCS00630	ARF1	P84077	GA	LMCS00631	PPM1L	Q5SGD2	ER	LMCS00054	CERT1	Q9Y5P4	GA
CMCS00252	STIM1_VAPB_PI(4,5)P2	STIM1_VAPB(HTP: 28.35)	3	Human	ER-PM; PM-ER	1	35416932	Accordingly, we identified an FFAT site at the TRPC3 N-terminal loop within the linker helices that envelope the C-terminus pole helix. The FFAT site interacts with the ER-resident VAPB to recruit TRPC3 to the ER/PM junctions and control its receptor-mediated activation.	NA	NA	NA	NA	NA	NA	PI(4,5)P2	125105	C9H21O17P3	C(C(COP(=O)(O)OC1C(C(C(C(C1O)OP(=O)(O)O)OP(=O)(O)O)O)O)O)O	NA	NA	NA	NA	LMCS00279	STIM1	Q13586	ER; PM	LMCS00280	VAPB	O95292	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00253	ATG18_ATG2	ATG18_ATG2(LTP)	2	Yeast	ER-Phagophore; Phagophore-ER	1	30254161	The Atg2-Atg18 complex tethers pre-autophagosomal membranes to the endoplasmic reticulum for autophagosome formation.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00528	ATG18	P43601	NA	LMCS00530	ATG2	P53855	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00254	VPS13_YPT35	VPS13_YPT35(LTP)	2	Yeast	Nucleus-Vacuole; Vacuole-Nucleus	1	30018089	Vps13 and Ypt35 are interdependent for recruitment to the NVJ.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00424	VPS13	Q07878	NA	LMCS00638	YPT35	P38815	Vacuole	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00255	TOMM40_TOMM70_ATG2A	TOMM40_TOMM70(LTP)	3	Human	ER-MT; MT-ER	1	31412244	TOM40/70 complex recruits Atg2A to MAM.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00223	TOMM40	O96008	MT	LMCS00642	TOMM70	O94826	MT	LMCS00641	ATG2A	Q2TAZ0	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00256	ATG2A_ATG9A	NA	2	Human	ER-Vesicle; Vesicle-ER	1	31412244	In addition, Atg2A interacts with Atg9A by a region within its N terminus.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00643	ATG2A	Q2TAZ0	ER	LMCS00644	ATG9A	Q7Z3C6	Vesicle	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00257	PITPNM1_VAPB	PITPNM1_VAPB(HTP: 1.00)	2	Human	ER-GA; GA-ER	2	15545272	The Inte+raction of VAP-B with Nir2 Affects the ER Structure-The VAP-B protein was previously localized to the ER and to pre-Golgi intermediates by biochemical and immunocytochemical methods.We have previously shown that Nir2 mainly localizes in the Golgi apparatus, but it is also found in the ER in interphase cells.	18614794	Our results show that the coordinated function of Nir2, OSBP, and CERT, at the ER–Golgi MCSs requires the VAP proteins, and it is critical for maintaining the structural and functional identity of the Golgi complex.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00645	PITPNM1	O00562	NA	LMCS00042	VAPB	O95292	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00258	PITPNM1_CERT1_OSBP_PI(4)P	NA	4	Human	ER-GA; GA-ER	1	18614794	Our results show that the coordinated function of Nir2, OSBP, and CERT, at the ER–Golgi MCSs requires the VAP proteins, and it is critical for maintaining the structural and functional identity of the Golgi complex.	NA	NA	NA	NA	NA	NA	PI(4)P	643965	C41H80O16P2	CCCCCCCCCCCCCCCC(=O)OCC(COP(=O)(O)OC1C(C(C(C(C1O)O)OP(=O)(O)O)O)O)OC(=O)CCCCCCCCCCCCCCC	NA	NA	NA	NA	LMCS00042	VAPB	O95292	ER	LMCS00054	CERT1	Q9Y5P4	NA	LMCS00056	OSBP	P22059	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00259	RELCH_OSBP_RAB11A	RAB11A_RELCH(HTP: 146.83)	3	Human	GA-Endosome; Endosome-GA	1	29514919	The novel protein RELCH/KIAA1468 as a Rab11-binding protein and show that RELCH/KIAA1468 and Rab11 regulate OSBP-dependent nonvesicular cholesterol transport from recycling endosomes to the trans-Golgi network.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00646	RELCH	Q9P260	Endosome	LMCS00647	OSBP	P22059	GA	LMCS00648	RAB11A	P62491	Endosome	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00260	VAPB_ OSBP_VAPA_OSBPL2_PI(4)P	OSBP_VAPB(HTP: 1.00); VAPB_OSBPL2(HTP: 1.00); VAPA_OSBPL2(HTP: 1.00); VAPA_VAPB(LTP); OSBP_VAPA(LTP)	5	Human	ER-GA; GA-ER	1	29930082	In addition, we show that the OSBP, lipid and VAP binding activities of ORP4L control its association at the ER–Golgi interface where it influences PI(4)P content and structure of the TGN and proximal Golgi compartments.	NA	NA	NA	NA	NA	NA	PI(4)P	643965	C41H80O16P2	CCCCCCCCCCCCCCCC(=O)OCC(COP(=O)(O)OC1C(C(C(C(C1O)O)OP(=O)(O)O)O)O)OC(=O)CCCCCCCCCCCCCCC	NA	NA	NA	NA	LMCS00042	VAPB	O95292	ER	LMCS00056	OSBP	P22059	ER; GA	LMCS00057	VAPA	Q9P0L0	ER	LMCS00649	OSBPL2	Q9H1P3	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00261	OSBPL5_OSBPL8_PI(4)P	OSBPL5_OSBPL8(HTP: 1.00)	3	Human	ER-PM; PM-ER	3	26206935	We found that two similar ER integral membrane proteins, oxysterol-binding protein (OSBP)–related protein 5 (ORP5) and ORP8, tethered the ER to the plasma membrane (PM) via the interaction of their pleckstrin homology domains with phosphatidylinositol 4-phosphate (PI4P) in this membrane.	28970484	ORP5 and ORP8 are reported to localize to endoplasmic reticulum–plasma membrane junctions via binding to phosphatidylinositol-4-phosphate (PtdIns(4)P), and act as a PtdIns(4)P/phosphatidylserine counter exchanger between the endoplasmic reticulum and plasma membrane.	29472386	PI(4,5)P2 controls plasma membrane PI4P and PS levels via ORP5/8 recruitment to ER–PM contact sites.	NA	NA	PI(4)P	643965	C41H80O16P2	CCCCCCCCCCCCCCCC(=O)OCC(COP(=O)(O)OC1C(C(C(C(C1O)O)OP(=O)(O)O)O)O)OC(=O)CCCCCCCCCCCCCCC	NA	NA	NA	NA	LMCS00652	OSBPL5	Q9H0X9	ER	LMCS00653	OSBPL8	Q9BZF1	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00262	IST2_OSH6	IST2_OSH6(LTP)	2	Yeast	ER-PM; PM-ER	2	32327560	Osh6 requires Ist2 for localization to ER–PM contacts and efficient phosphatidylserine transport in budding yeast.	34259806	Ist2 recruits the lipid transporters Osh6/7 to ER–PM contacts to maintain phospholipid metabolism.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00265	IST2	P38250	ER	LMCS00397	OSH6	Q02201	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00263	IST2_OSH7	IST2_OSH7(LTP)	2	Yeast	ER-PM; PM-ER	1	34259806	Ist2 recruits the lipid transporters Osh6/7 to ER–PM contacts to maintain phospholipid metabolism.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00265	IST2	P38250	ER	LMCS00396	OSH7	P38755	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00264	Dnm1l_C1qtnf1	NA	2	Mouse	ER-MT; MT-ER	1	34837016	ER-associated CTRP1 regulates mitochondrial fission via interaction with DRP1.; We herein showed that ablation of CTRP1 suppresses the recruitment of DRP1 to mitochondria and provided evidence suggesting that the ER-mitochondrion interaction is required for the proper regulation of mitochondrial morphology.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00203	Dnm1l	Q8K1M6	MT	LMCS00656	C1qtnf1	Q9QXP7	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00265	ORAI1_STIM1_UNC93B1	ORAI1_STIM1(LTP); ORAI1_UNC93B1(HTP: 0.59)	3	Human	ER-PM; PM-ER	1	35065962	At these ER–PM junctions, STIM1 can trap and gate Orai1 Ca2+ channels, eliciting an influx of Ca2+ from the extracellular milieu into the cytoplasm.; UNC93B1 deficiency might impair the traffic or activity of an adapter protein to reduce STIM1–Orai1 interactions but not STIM1 recruitment.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00260	ORAI1	Q96D31	NA	LMCS00279	STIM1	Q13586	ER; PM	LMCS00635	UNC93B1	Q9H1C4	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00266	Itpr3_Hspa9_Vdac1_Pdk4	NA	4	Mouse	ER-MT; MT-ER	1	30523025	Here, we demonstrate that PDK4 interacts with and stabilizes the IP3R1-GRP75-VDAC1 complex at the MAM interface.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00216	Hspa9	P38647	MT	LMCS00230	Vdac1	Q60932	MT	LMCS00218	Itpr1	P11881	ER	LMCS00155	Pdk4	O70571	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00267	Bid_PACS2	NA	2	Human	ER-MT; MT-ER	1	15692567	Our demonstration that apoptotic inducers promote PACS-2 to bind and translocate full-length Bid to mitochondria.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00658	Bid	P70444	NA	LMCS00116	PACS2	Q86VP3	ER; MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00268	ERO1A_EIF2AK3	NA	2	Mouse	ER-MT; MT-ER	1	36586409	The PERK-Ero1a complex increases mitochondria-ER contacts during early ER stress.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00183	ERO1A	Q96HE7	ER	LMCS00592	EIF2AK3	Q9NZJ5	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00269	Ero1a_Eif2ak3	NA	2	Human	ER-MT; MT-ER	1	36586409	The PERK-Ero1a complex increases mitochondria-ER contacts during early ER stress.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00556	Ero1a	Q8R180	ER	LMCS00593	Eif2ak3	Q9Z2B5	ER	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
CMCS00270	RMDN3_MARCHF5	MARCHF5_RMDN3(LTP)	2	Human	ER-MT; MT-ER	1	34964862	We found that MITOL interacts with and ubiquitinates RMDN3.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	LMCS00190	RMDN3	Q96TC7	MT	LMCS00225	MARCHF5	Q9NX47	MT	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA