MCS.ID	synonyms	gene.ID	gene.symbol	uniprot	species	MCS	location.literature.	cell.line.tissue	Experimental.Method	source.number	PMID-1	Description-1	Evidences-1	PMID-2	Description-2	Evidences-2	PMID-3	Description-3	Evidences-3	PMID-4	Description-4	Evidences-4	PMID-5	Description-5	Evidences-5	PMID-6	Description-6	Evidences-6	PMID-7	Description-7	Evidences-7	PMID-8	Description-8	Evidences-8	PMID-9	Description-9	Evidences-9	PMID-10	Description-10	Evidences-10	PMID-11	Description-11	Evidences-11	PMID-12	Description-12	Evidences-12
HMCS05733	CTR1; YPR124W; P9642.3	856241	CTR1	P49573	Yeast	ER-Vacuole; Vacuole-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05734	ERG2; YMR202W; YM8325.03	855242	ERG2	P32352	Yeast	ER-Vacuole; Vacuole-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05735	ERV14; YGL054C	852826	ERV14	P53173	Yeast	ER-Vacuole; Vacuole-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05736	GAA1; END2; YLR088W; L9449.4	850777	GAA1	P39012	Yeast	ER-Vacuole; Vacuole-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05737	KIP3; YGL216W	852655	KIP3	P53086	Yeast	ER-Vacuole; Vacuole-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05738	YMR147W; YM9375.17	855178	LDO45	P40218	Yeast	ER-Vacuole; Vacuole-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05739	NAT3; YPR131C	856249	NAT3	Q06504	Yeast	ER-Vacuole; Vacuole-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05740	NDC1; YML031W	854977	NDC1	P32500	Yeast	ER-Vacuole; Vacuole-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05741	NVJ1; VAB36; YHR195W	856602	NVJ1	P38881	Yeast	ER-Vacuole; Vacuole-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05742	SPC110; NUF1; XCM1; YDR356W; D9476.3	851957	SPC110	P32380	Yeast	ER-Vacuole; Vacuole-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05743	TAF9; TAF17; YMR236W; YM9959.18	855276	TAF9	Q05027	Yeast	ER-Vacuole; Vacuole-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05744	TUL1; YKL034W; YKL247	853832	TUL1	P36096	Yeast	ER-Vacuole; Vacuole-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05745	VPS15; GRD8; VAC4; VPL19; YBR097W; YBR0825	852394	VPS15	P22219	Yeast	ER-Vacuole; Vacuole-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05746	VPS3; VPT17; YDR495C; D9719.1	852106	VPS3	P23643	Yeast	ER-Vacuole; Vacuole-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05747	YNL034W; N2740	855697	YNL034W	P53963	Yeast	ER-Vacuole; Vacuole-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05748	YPQ1; YOL092W; O0929	854061	YPQ1	Q12010	Yeast	ER-Vacuole; Vacuole-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05749	ALG1; YBR110W; YBR0906	852407	ALG1	P16661	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05750	ALG11; YNL048W; N2510; YNL2510W	855679	ALG11	P53954	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05751	ALG14; YBR070C; YBR0711	852362	ALG14	P38242	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05752	ALG5; YPL227C; P1437	855874	ALG5	P40350	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05753	AXL1; YPR122W; P9642.4	856240	AXL1	P40851	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05754	BLS1; YLR408C	851124	BLS1	Q06071	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05755	CHO2; PEM1; YGR157W; G6673	853061	CHO2	P05374	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05756	CSF1; TWEEK; YLR087C	850776	CSF1	Q12150	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05757	CUE1; KIS4; YMR264W; YM8156.06	855306	CUE1	P38428	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05758	EIS1; YMR031C; YM9973.04C	855047	EIS1	Q05050	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05759	ERG2; YMR202W; YM8325.03	855242	ERG2	P32352	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05760	FLO1; FLO2; FLO4; FLO8; YAR050W	851289	FLO1	P32768	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05761	FMP27; HOB1; YLR454W	851175	FMP27	Q06179	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05762	GPR1; YDL035C	851527	GPR1	Q12361	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05763	HIM1; YDR317W	851915	HIM1	Q06674	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05764	IFA38; YBR159W; YBR1209	852456	IFA38	P38286	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05765	IRC23; YOR044W	854209	IRC23	Q08416	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05766	IZH4; YOL101C	854052	IZH4	Q99393	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05767	LAA1; YJL207C; HRD550; J0312	853223	LAA1	P39526	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05768	LSB3; YFR024C-A; YFR024C	850580	LSB3	P43603	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05769	MSC7; YHR039C	856434	MSC7	P38694	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05770	MTC1; YJL123C; J0718	853319	MTC1	P47018	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05771	MTQ1; YNL063W; N2420; YNL2420W	855662	MTQ1	P53944	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05772	MUM3; YOR298W	854473	MUM3	Q08750	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05773	MYO5; YMR109W; YM9718.08	855136	MYO5	Q04439	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05774	NBP1; YLR457C; L9122.6	851180	NBP1	P52919	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05775	NTE1; YML059C; YM9958.03C	854943	NTE1	Q04958	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05776	NUP170; NLE3; YBL079W; YBL0725	852199	NUP170	P38181	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05777	NUP82; YJL061W; HRB187; J1135	853385	NUP82	P40368	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05778	NUS1; YDL193W; D1239	851334	NUS1	Q12063	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05779	OST6; YML019W	854989	OST6	Q03723	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05780	YNL181W; N1640	855540	PBR1	P53878	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05781	PEP3; VAM8; VPS18; VPT18; YLR148W; L9634.2	850840	PEP3	P27801	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05782	PEX3; PAS3; YDR329C; D9798.15	851929	PEX3	P28795	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05783	PEX32; YBR168W; YBR1220	852466	PEX32	P38292	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05784	PGA2; YNL149C; N1774	855573	PGA2	P53903	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05785	PRK1; PAK1; YIL095W	854713	PRK1	P40494	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05786	RRT8; YOL048C	854109	RRT8	Q08219	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05787	SEC17; YBL050W; YBL0505; YBL0517	852230	SEC17	P32602	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05788	SNL1; YIL016W	854796	SNL1	P40548	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05789	SPS4; YOR313C; O6120	854490	SPS4	P09937	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05790	SRC1; HEH1; YML034W; YML033W	854974	SRC1	Q03707	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05791	STN1; YDR082W; D4456; YD8554.15	851655	STN1	P38960	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05792	TAZ1; YPR140W	856262	TAZ1	Q06510	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05793	TGL5; STC2; YOR081C; YOR29-32; YOR2964C	854248	TGL5	Q12043	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05794	TUL1; YKL034W; YKL247	853832	TUL1	P36096	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05795	UBX3; YDL091C	851467	UBX3	Q12229	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05796	VAC8; YEB3; YEL013W	856702	VAC8	P39968	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05797	VPS3; VPT17; YDR495C; D9719.1	852106	VPS3	P23643	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05798	YBR096W; YBR0824	852393	YBR096W	P38256	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05799	YET2; YMR040W; YM9532.05	855056	YET2	Q04210	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05800	YET3; YDL072C	851487	YET3	Q07451	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05801	YFR006W	850556	YFR006W	P43590	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05802	YJL028W; J1267	853425	YJL028W	P47062	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05803	YPQ1; YOL092W; O0929	854061	YPQ1	Q12010	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05804	YPR097W	856212	YPR097W	Q06839	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05805	HOB2; YPR117W	856233	YPR117W	Q06116	Yeast	ER-LD; LD-ER	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05806	ALG11; YNL048W; N2510; YNL2510W	855679	ALG11	P53954	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05807	ALG14; YBR070C; YBR0711	852362	ALG14	P38242	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05808	ALG5; YPL227C; P1437	855874	ALG5	P40350	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05809	BIK1; YCL029C; YCL29C	850328	BIK1	P11709	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05810	COA3; COX25; RRG10; YJL062W-A	853383	COA3	Q3E7B2	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05811	CSF1; TWEEK; YLR087C	850776	CSF1	Q12150	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05812	CSM4; YPL200W	855901	CSM4	Q08955	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05813	ERG2; YMR202W; YM8325.03	855242	ERG2	P32352	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05814	FMP27; HOB1; YLR454W	851175	FMP27	Q06179	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05815	HIM1; YDR317W	851915	HIM1	Q06674	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05816	IFA38; YBR159W; YBR1209	852456	IFA38	P38286	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05817	LYS14; YDR034C; YD9673.04C	851598	LYS14	P40971	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05818	MDM1; YML104C; YM8339.15C	854867	MDM1	Q01846	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05819	MUM3; YOR298W	854473	MUM3	Q08750	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05820	NDC1; YML031W	854977	NDC1	P32500	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05821	NEM1; YHR004C	856393	NEM1	P38757	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05822	NUP170; NLE3; YBL079W; YBL0725	852199	NUP170	P38181	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05823	NUP82; YJL061W; HRB187; J1135	853385	NUP82	P40368	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05824	NUS1; YDL193W; D1239	851334	NUS1	Q12063	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05825	YNL181W; N1640	855540	PBR1	P53878	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05826	PPX1; YHR201C	856608	PPX1	P38698	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05827	PRK1; PAK1; YIL095W	854713	PRK1	P40494	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05828	RNQ1; YCL028W; YCL181; YCL28W	850329	RNQ1	P25367	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05829	SPC25; YER018C	856738	SPC25	P40014	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05830	SPS4; YOR313C; O6120	854490	SPS4	P09937	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05831	STR3; YGL184C; G1601	852691	STR3	P53101	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05832	TAZ1; YPR140W	856262	TAZ1	Q06510	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05833	TUL1; YKL034W; YKL247	853832	TUL1	P36096	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05834	UBX3; YDL091C	851467	UBX3	Q12229	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05835	VAC8; YEB3; YEL013W	856702	VAC8	P39968	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05836	VHR1; YIL056W	854755	VHR1	P40522	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05837	YBR096W; YBR0824	852393	YBR096W	P38256	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05838	YET2; YMR040W; YM9532.05	855056	YET2	Q04210	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05839	YFR006W	850556	YFR006W	P43590	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05840	YJL118W; J0742	853323	YJL118W	P47022	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05841	YLR146W-A	3799977	YLR146W-A	Q2V2P1	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05842	HOB2; YPR117W	856233	YPR117W	Q06116	Yeast	LD-PM; PM-LD	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05843	ACM1; YPL267W	855861	ACM1	Q08981	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05844	ADY3; YDL239C	851359	ADY3	Q07732	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05845	AIM11; GEP8; YER093C-A	856829	AIM11	P87275	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05846	AIM39; YOL053W; O1269	854103	AIM39	Q08223	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05847	ANT1; YPR128C	856246	ANT1	Q06497	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05848	ASM4; NUP59; YDL088C; D2420	851470	ASM4	Q05166	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05849	ATG36; YJL185C; J0415	853254	ATG36	P46983	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05850	BNI1; PPF3; SHE5; YNL271C; N0646	855450	BNI1	P41832	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05851	BPH1; YCR032W; YCR32W; YCR591; YCR601	850398	BPH1	P25356	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05852	BUD31; CWC14; YCR063W; YCR63W; YCR903	850427	BUD31	P25337	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05853	CSM4; YPL200W	855901	CSM4	Q08955	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05854	CUE4; YML101C	854871	CUE4	Q04201	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05855	DJP1; ICS1; PAS22; YIR004W; YIB4W	854820	DJP1	P40564	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05856	DNM1; YLL001W; L1381	850686	DNM1	P54861	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05857	ECM19; YLR390W	851106	ECM19	Q06011	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05858	FMP27; HOB1; YLR454W	851175	FMP27	Q06179	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05859	FZO1; YBR179C; YBR1241	852477	FZO1	P38297	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05860	GIS1; YDR096W; YD8557.01	851670	GIS1	Q03833	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05861	IKI1; ELP5; HAP2; TOT5; YHR187W	856594	IKI1	P38874	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05862	INP1; YMR204C; YM8325.05C	855244	INP1	Q03694	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05863	YJR141W; J2166	853606	IPA1	P47172	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05864	IRC19; RRG4; YLL033W	850626	IRC19	Q07843	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05865	KIP1; CIN9; YBL063W; YBL0504; YBL0521	852216	KIP1	P28742	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05866	KIP3; YGL216W	852655	KIP3	P53086	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05867	LAM6; LTC1; YLR072W	850761	LAM6	Q08001	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05868	MCO6; YJL127C-B	1466466	MCO6	Q3E828	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05869	MDM1; YML104C; YM8339.15C	854867	MDM1	Q01846	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05870	MDV1; FIS2; GAG3; NET2; YJL112W; J0802	853332	MDV1	P47025	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05871	MGT1; YDL200C; D1204	851327	MGT1	P26188	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05872	YKL044W; YKL257	853822	MMO1	P36092	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05873	MPS3; NEP98; YJL019W; J1310; J1315; YJL018W	853434	MPS3	P47069	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05874	MRX11; YPL041C	856066	MRX11	Q03079	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05875	NAT2; YGR147C; G6630	853050	NAT2	P37293	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05876	NDC1; YML031W	854977	NDC1	P32500	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05877	NDL1; YLR254C	850956	NDL1	Q06568	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05878	NGL1; YOL042W	854115	NGL1	Q08213	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05879	NVJ1; VAB36; YHR195W	856602	NVJ1	P38881	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05880	OST4; YDL232W	851366	OST4	Q99380	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05881	PEX27; YOR193W	854368	PEX27	Q08580	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05882	PEX34; YCL056C; YCL433; YCL56C	850302	PEX34	P25584	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05883	YGR168C	853078	PEX35	P53293	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05884	PTC1; TPD1; YDL006W; D2925	851558	PTC1	P35182	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05885	RCF1; AIM31; YML030W	854978	RCF1	Q03713	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05886	RGR1; MED14; YLR071C	850760	RGR1	P19263	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05887	RPC10; RPB12; YHR143W-A; YHR143BW	856547	RPC10	P40422	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05888	RPL34A; YER056C-A; YER056BC	856784	RPL34A	P87262	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05889	RPL4B; RPL2B; YDR012W; YD8119.17	851575	RPL4B	P49626	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05890	SAN1; YDR143C; YD2943.02C	851721	SAN1	P22470	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05891	SHY1; YGR112W; G6150	853009	SHY1	P53266	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05892	SLO1; YER180C-A	856928	SLO1	Q3E784	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05893	STR3; YGL184C; G1601	852691	STR3	P53101	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05894	TAF12; TAF61; TAF68; YDR145W; YD8358.02	851723	TAF12	Q03761	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05895	TAF9; TAF17; YMR236W; YM9959.18	855276	TAF9	Q05027	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05896	YPR098C	856213	TMH18	Q06089	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05897	TOM5; MOM8A; YPR133W-A	856252	TOM5	P80967	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05898	TUL1; YKL034W; YKL247	853832	TUL1	P36096	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05899	UIP4; YPL186C	855916	UIP4	Q08926	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05900	VPS15; GRD8; VAC4; VPL19; YBR097W; YBR0825	852394	VPS15	P22219	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05901	YCL002C; YCL2C	850353	YCL002C	P25565	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05902	YIP3; PRA1; YNL044W; N2650	855683	YIP3	P53633	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05903	YNL034W; N2740	855697	YNL034W	P53963	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05904	PLS1; YNL097C-B; YNL097C-A	1466513	YNL097C-B	P0C271	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05905	YPT1; YP2; YFL038C	850505	YPT1	P01123	Yeast	MT-Peroxisome; Peroxisome-MT	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05906	ACM1; YPL267W	855861	ACM1	Q08981	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05907	AIM11; GEP8; YER093C-A	856829	AIM11	P87275	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05908	AIM39; YOL053W; O1269	854103	AIM39	Q08223	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05909	APM3; YKS6; YBR288C; YBR2035	852591	APM3	P38153	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05910	ATG11; CVT9; YPR049C; YP9499.07c	856162	ATG11	Q12527	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05911	BNI1; PPF3; SHE5; YNL271C; N0646	855450	BNI1	P41832	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05912	BUD31; CWC14; YCR063W; YCR63W; YCR903	850427	BUD31	P25337	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05913	DPL1; BST1; YDR294C; D9819.5	851888	DPL1	Q05567	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05914	ECM19; YLR390W	851106	ECM19	Q06011	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05915	GIS1; YDR096W; YD8557.01	851670	GIS1	Q03833	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05916	INP1; YMR204C; YM8325.05C	855244	INP1	Q03694	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05917	INP2; YMR163C; YM8520.12C	855198	INP2	Q03824	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05918	IRC19; RRG4; YLL033W	850626	IRC19	Q07843	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05919	KIP1; CIN9; YBL063W; YBL0504; YBL0521	852216	KIP1	P28742	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05920	MCM6; YGL201C	852673	MCM6	P53091	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05921	MGT1; YDL200C; D1204	851327	MGT1	P26188	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05922	YKL044W; YKL257	853822	MMO1	P36092	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05923	MRX11; YPL041C	856066	MRX11	Q03079	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05924	NAT2; YGR147C; G6630	853050	NAT2	P37293	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05925	NPY1; YGL067W	852813	NPY1	P53164	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05926	OST4; YDL232W	851366	OST4	Q99380	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05927	PEX13; PAS20; YLR191W; L9470.1	850888	PEX13	P80667	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05928	PEX14; YGL153W; G1870	852724	PEX14	P53112	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05929	PEX34; YCL056C; YCL433; YCL56C	850302	PEX34	P25584	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05930	PRK1; PAK1; YIL095W	854713	PRK1	P40494	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05931	PTC1; TPD1; YDL006W; D2925	851558	PTC1	P35182	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05932	RCF1; AIM31; YML030W	854978	RCF1	Q03713	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05933	RMD6; YEL072W	856637	RMD6	P39975	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05934	RPC10; RPB12; YHR143W-A; YHR143BW	856547	RPC10	P40422	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05935	RPL34A; YER056C-A; YER056BC	856784	RPL34A	P87262	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05936	RPL4B; RPL2B; YDR012W; YD8119.17	851575	RPL4B	P49626	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05937	SAN1; YDR143C; YD2943.02C	851721	SAN1	P22470	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05938	SHY1; YGR112W; G6150	853009	SHY1	P53266	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05939	SLO1; YER180C-A	856928	SLO1	Q3E784	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05940	SNF7; DID1; VPS32; YLR025W	850712	SNF7	P39929	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05941	SPC97; YHR172W	856577	SPC97	P38863	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05942	TAF12; TAF61; TAF68; YDR145W; YD8358.02	851723	TAF12	Q03761	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05943	TAF9; TAF17; YMR236W; YM9959.18	855276	TAF9	Q05027	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05944	TMA10; YLR327C; L8543.1	851037	TMA10	Q06177	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05945	TUL1; YKL034W; YKL247	853832	TUL1	P36096	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05946	VAC8; YEB3; YEL013W	856702	VAC8	P39968	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05947	VPS36; GRD12; VAC3; VPL11; YLR417W	851135	VPS36	Q06696	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05948	YCL002C; YCL2C	850353	YCL002C	P25565	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05949	YEH1; YLL012W; L1329	850648	YEH1	Q07804	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05950	YIP3; PRA1; YNL044W; N2650	855683	YIP3	P53633	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05951	ACM1; YPL267W	855861	ACM1	Q08981	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05952	ADY3; YDL239C	851359	ADY3	Q07732	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05953	AIM11; GEP8; YER093C-A	856829	AIM11	P87275	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05954	AIM39; YOL053W; O1269	854103	AIM39	Q08223	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05955	ARC35; YNR035C; N3296	855771	ARC35	P53731	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05956	BNI1; PPF3; SHE5; YNL271C; N0646	855450	BNI1	P41832	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05957	CIS1; YLR346C	851060	CIS1	Q06139	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05958	FZO1; YBR179C; YBR1241	852477	FZO1	P38297	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05959	GIS1; YDR096W; YD8557.01	851670	GIS1	Q03833	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05960	INA17; AIM43; FMP14; YPL099C	856005	INA17	Q02888	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05961	IRC19; RRG4; YLL033W	850626	IRC19	Q07843	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05962	KIP1; CIN9; YBL063W; YBL0504; YBL0521	852216	KIP1	P28742	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05963	LAM6; LTC1; YLR072W	850761	LAM6	Q08001	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05964	LSP1; YPL004C	856103	LSP1	Q12230	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05965	MCM6; YGL201C	852673	MCM6	P53091	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05966	MDM10; YAL010C; FUN37	851223	MDM10	P18409	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05967	MGT1; YDL200C; D1204	851327	MGT1	P26188	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05968	MSC7; YHR039C	856434	MSC7	P38694	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05969	MUM3; YOR298W	854473	MUM3	Q08750	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05970	NAT2; YGR147C; G6630	853050	NAT2	P37293	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05971	NDL1; YLR254C	850956	NDL1	Q06568	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05972	NGL1; YOL042W	854115	NGL1	Q08213	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05973	PEX14; YGL153W; G1870	852724	PEX14	P53112	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05974	PEX32; YBR168W; YBR1220	852466	PEX32	P38292	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05975	PRM9; YAR031W; FUN58	851282	PRM9	P39551	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05976	RCF1; AIM31; YML030W	854978	RCF1	Q03713	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05977	RPL34A; YER056C-A; YER056BC	856784	RPL34A	P87262	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05978	RPL4B; RPL2B; YDR012W; YD8119.17	851575	RPL4B	P49626	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05979	SHY1; YGR112W; G6150	853009	SHY1	P53266	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05980	SLO1; YER180C-A	856928	SLO1	Q3E784	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05981	SPS19; SPX19; YNL202W; N1362	855518	SPS19	P32573	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05982	STE23; YLR389C; L8084.12	851105	STE23	Q06010	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05983	TAF9; TAF17; YMR236W; YM9959.18	855276	TAF9	Q05027	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05984	TMA10; YLR327C; L8543.1	851037	TMA10	Q06177	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05985	YPR098C	856213	TMH18	Q06089	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05986	TRM2; NUC2; NUD1; RNC1; YKR056W	853930	TRM2	P33753	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05987	UIP4; YPL186C	855916	UIP4	Q08926	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
HMCS05988	PLS1; YNL097C-B; YNL097C-A	1466513	YNL097C-B	P0C271	Yeast	GA-Peroxisome; Peroxisome-GA	NA	Yeast strains	Mass-spectrometric techniques	1	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was detected by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00003	YMR124W; YM8564.06	855154	EPO1	P39523	Yeast	ER-PM; PM-ER	PM	Yeast strains	Low throughput experimental methods	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.	The protein was validated by affinity purification, mass spectrometry, confocal microscopy, photobleaching experiments, genetic interactions, in vitro binding and coimmunopurification experiments in yeast strains, and the ER-septin tethering at the yeast bud neck creates a diffusion barrier for ER proteins.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00020	VPS13; SOI1; VPT2; YME3; YLL040C	850619	VPS13	Q07878	Yeast	ER-Prospore membrane; Prospore membrane-ER	ER	Yeast strains	Low throughput experimental methods	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.	The protein was validated by fluorescence microscopy and coimmunoprecipitation in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00021	SPO71; YD8557.13c; YDR104C	851681	SPO71	Q03868	Yeast	ER-Prospore membrane; Prospore membrane-ER	Prospore membrane	Yeast strains	Low throughput experimental methods	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.	The protein was validated by fluorescence microscopy and coimmunoprecipitation in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00046	NVJ2; YPR091C	856207	NVJ2	Q06833	Yeast	ER-GA; GA-ER	ER	Yeast strains	Low throughput experimental methods	1	28011845	Nvj2p normally resides at contacts between the ER and other organelles, but during ER stress, it relocalizes to and increases ER-Golgi contacts.	The protein was validated by in vivo labeling, in vitro labeling, fluorescence microscopy and EM in yeast strains, and Nvj2-dependent ceramide transport to the medial-Golgi decreases ceramide levels, which helps prevent ceramide intoxication.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00067	SEI1; FLD1; YLR404W	851120	SEI1	Q06058	Yeast	ER-LD; LD-ER	ER; LD	Yeast strains	Low throughput experimental methods	1	29187528	In this study, we characterize the function of Ldo16 and Ldo45, two splicing isoforms of the same protein in budding yeast.We show that Ldo proteins interact with the seipin complex, which regulates contacts between LDs and the endoplasmic reticulum (ER). 	The protein was validated by immunoprecipitation experiments, fluorescence microscopy, LD isolation and protein mass spectrometry in yeast strains, which has the roles in controlling the LD proteome.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00079	NEM1; YHR004C	856393	NEM1	P38757	Yeast	ER-LD; LD-ER	ER; LD	Yeast strains	Low throughput experimental methods	2	21422231	Nem1p localizes next to lipid droplets on the ER. 	The protein was validated by fluorescence, electron microscopy, lipid analysis, cell lysis and organelle fractionation in yeast strains.	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was validated by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00080	ERG6; ISE1; LIS1; SED6; YML008C; YM9571.10C	855003	ERG6	P25087	Yeast	LD-Parasitophorous Vacuole; Parasitophorous Vacuole-LD	LD	Yeast strains	Low throughput experimental methods	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.	The protein was validated by protein complementation assay screen, lipid analysis by non-targeted gas chromatography-mass spectrometry and structured illumination microscopy in yeast strains, and the interactors reveal a role for lipid droplets in inclusion clearance.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00082	VPS13; SOI1; VPT2; YME3; YLL040C	850619	VPS13	Q07878	Yeast	ER-MT; MT-ER	MT	Yeast strains	Low throughput experimental methods	1	27280386	Together, these results suggest that Mcp1 must recruit Vps13 to mitochondrial membranes to compensate for ERMES defects.	The protein was validated by sporulation assays, western blot analysis, mitophagy assay and microscopy in yeast strains, and the complex compensates for ERMES defects.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00085	MCP1; YOR228C; YOR50-18	854403	MCP1	Q12106	Yeast	ER-MT; MT-ER	MT	Yeast strains	Low throughput experimental methods	1	27280386	Together, these results suggest that Mcp1 must recruit Vps13 to mitochondrial membranes to compensate for ERMES defects.	The protein was validated by sporulation assays, western blot analysis, mitophagy assay and microscopy in yeast strains, and the complex compensates for ERMES defects.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00089	NVJ2; YPR091C	856207	NVJ2	Q06833	Yeast	Nucleus-Vacuole; Vacuole-Nucleus	Nucleus	Yeast strains	Low throughput experimental methods	1	22250200	However, we found that Nvj2–GFP was also enriched on the nuclear membrane that is apposed to the vacuole, which suggests that it localizes to the NVJ.	The protein was validated by in fluorescence microscopy, liposome binding assay and membrane flotation in yeast strains, which plays roles in lipid metabolism.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00090	SVF1; SGI1; YDR346C	851947	SVF1	Q05515	Yeast	ER-GA; GA-ER	GA	Yeast strains	Low throughput experimental methods	1	36897280	 Here, we identified a role for yeast Svf1 in ceramide transport between the ER and the Golgi.	The protein was validated by in fluorescence microscopy in yeast strains, which is important to maintain flux of ceramides into complex SPs.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00109	NUM1; PAC12; YDR150W; YD8358.06	851727	NUM1	Q00402	Yeast	ER-MT-PM; PM-MT-ER	ER; MT	Yeast strains	Low throughput experimental methods	1	23341591	Thus, taken together, our findings identify Num1 as a key component of a mitochondria-ER-cortex anchor, which we termed MECA, that functions in parallel with mitochondrial dynamics to distribute and position the essential mitochondrial network.	The protein was validated by growth assays, yeast two-hybrid analysis, cytological analysis and proteomic analysis in yeast strains, which functions in parallel with mitochondrial dynamics to distribute and position the essential mitochondrial network.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00110	MDM36; YPR083W	856198	MDM36	Q06820	Yeast	ER-MT-PM; PM-MT-ER	MT	Yeast strains	Low throughput experimental methods	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.	The protein was validated by growth assays, yeast two-hybrid analysis, cytological analysis and proteomic analysis in yeast strains, which functions in parallel with mitochondrial dynamics to distribute and position the essential mitochondrial network.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00123	LAM5; LTC2; YFL042C	850501	LAM5	P43560	Yeast	ER-MT; MT-ER	ER	Yeast strains	Low throughput experimental methods	1	26001273	In contrast to these four peripheral proteins, both Lam5p and Lam6p showed complex intracellular targeting to multiple MCSs, including the NVJ and ER-mitochondrial contacts.	The protein was validated by bioinformatics and microscopy in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00127	GEM1; YAL048C	851249	GEM1	P39722	Yeast	ER-MT; MT-ER	MT	Yeast strains	Low throughput experimental methods	2	21825164	The core building block of ERMES is a heterotetrameric protein complex composed of Mmm1, an ER-resident integral membrane protein; Mdm12, a cytosolic protein; Mdm34, a putative OMM protein; and Mdm10, an integral B-barrel OMM protein.	The protein was validated by live microscopy and immunofluorescence in yeast strains, which regulates apoptosis at endoplasmic reticulum by modulating calcium release.	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. 	The protein was validated by pull-down, HPTLC and MS in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00128	MMR1; YLR190W	850887	MMR1	Q06324	Yeast	ER-MT; MT-ER	MT	Yeast strains	Low throughput experimental methods	1	22119524	These findings indicate that Mmr1p contributes to mitochondrial inheritance as a mediator of anchorage of mitochondria to cER sheets in the yeast bud tip, and that Ptc1p regulates Mmr1p phosphorylation, localization and function.	The protein was validated by fluorescence microscopy, SIM, electron microscopy and image analysis in yeast strains, which contributes to mitochondrial inheritance.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00135	LAM5; LTC2; YFL042C	850501	LAM5	P43560	Yeast	ER-GA; GA-ER	NA	Yeast strains	Low throughput experimental methods	1	29527758	Focusing in, we now suggest that Lam5 resides in contact sites between the endoplasmic reticulum and the late Golgi.	The protein was validated by high‐throughput microscopy and co‐immunoprecipitation in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00136	ARL1; ARF3; YBR164C; YBR1216	852462	ARL1	P38116	Yeast	ER-GA; GA-ER	NA	Yeast strains	Low throughput experimental methods	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.	The protein was validated by high‐throughput microscopy and co‐immunoprecipitation in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00139	SCS2; YER120W	856856	SCS2	P40075	Yeast	Nucleus-Vacuole; Vacuole-Nucleus	NA	Yeast strains	Low throughput experimental methods	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.	The protein was validated by cell imaging, in vitro binding assay and functionality of GFP-tagged Opi1p in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00143	TOM5; MOM8A; YPR133W-A	856252	TOM5	P80967	Yeast	ER-MT; MT-ER	MT	Yeast strains	Low throughput experimental methods	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.	The protein was validated by fluorescence microscopy, in vivo labeling, psd assay, EM and co-immunoprecipitation in yeast strains, and the EMC mediates lipid trafficking between the ER and mitochondria.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00144	TOM70; MAS70; OMP1; YNL121C; N1905	855602	TOM70	P07213	Yeast	ER-MT; MT-ER	MT	Yeast strains	Low throughput experimental methods	1	25987606	Ltc1 localized to ER-Mitochondrion and ER-vacuole contacts via the Mitochondrionl import receptors Tom70,71 and the vacuolar protein Vac8, respectively. 	The protein was validated by fluorescence microscopy, immunopurification and tandem mass spectrometry in yeast strains, and the EMC mediates lipid trafficking between the ER and mitochondria.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00145	TOM71; TOM72; YHR117W	856517	TOM71	P38825	Yeast	ER-MT; MT-ER	MT	Yeast strains	Low throughput experimental methods	1	25987606	Ltc1 localized to ER-Mitochondrion and ER-vacuole contacts via the Mitochondrionl import receptors Tom70,71 and the vacuolar protein Vac8, respectively. 	The protein was validated by fluorescence microscopy, immunopurification and tandem mass spectrometry in yeast strains, and the EMC mediates lipid trafficking between the ER and mitochondria.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00178	MDM34; MMM2; YGL219C	852654	MDM34	P53083	Yeast	ER-MT; MT-ER	MT	Yeast strains	Low throughput experimental methods	4	19556461	We identified the Mmm1,Mdm10,Mdm12,Mdm36 complex as a molecular tether between ER and Mitochondrion. 	The protein was validated by mutagenesis screen, microscopy, phospholipid analysis and protein analysis in yeast strains, and the tethering complex localized to discrete foci, suggesting that discrete sites of close apposition between ER and mitochondria facilitate interorganelle calcium and phospholipid exchange.	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. 	The protein was validated by pull-down, HPTLC and MS in yeast strains.	21825164	We identified the Mmm1,Mdm10,Mdm12,Mdm36 complex as a molecular tether between ER and Mitochondrion.	The protein was validated by live microscopy and immunofluorescence in yeast strains, which regulates apoptosis at endoplasmic reticulum by modulating calcium release.	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.	The protein was validated by in fluorescence microscopy, liposome binding assay and membrane flotation in optiprep gradients, which plays roles in lipid metabolism.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00179	MDM12; YOL009C	854153	MDM12	Q92328	Yeast	ER-MT; MT-ER	ER; MT	Yeast strains	Low throughput experimental methods	5	19556461	We identified the Mmm1,Mdm10,Mdm12,Mdm36 complex as a molecular tether between ER and Mitochondrion. 	The protein was validated by mutagenesis screen, microscopy, phospholipid analysis and protein analysis in yeast strains, and the tethering complex localized to discrete foci, suggesting that discrete sites of close apposition between ER and mitochondria facilitate interorganelle calcium and phospholipid exchange.	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. 	The protein was validated by pull-down, HPTLC and MS in yeast strains.	29279306	Structure-function insights into direct lipid transfer between membranes by Mmm1-Mdm12 of ERMES. 	The protein was validated by crystallization, data collection, lipid analyses and simulation methods in yeast strains, and the Mmm1–Mdm12 complex functions as a minimal unit that mediates lipid transfer between membranes.	21825164	We identified the Mmm1,Mdm10,Mdm12,Mdm36 complex as a molecular tether between ER and Mitochondrion.	The protein was validated by live microscopy and immunofluorescence in yeast strains, which regulates apoptosis at endoplasmic reticulum by modulating calcium release.	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.	The protein was validated by in fluorescence microscopy, liposome binding assay and membrane flotation in optiprep gradients, which plays roles in lipid metabolism.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00180	MDM10; YAL010C; FUN37	851223	MDM10	P18409	Yeast	ER-MT; MT-ER	MT	Yeast strains	Low throughput experimental methods	5	19556461	We identified the Mmm1,Mdm10,Mdm12,Mdm36 complex as a molecular tether between ER and Mitochondrion. 	The protein was validated by mutagenesis screen, microscopy, phospholipid analysis and protein analysis in yeast strains, and the tethering complex localized to discrete foci, suggesting that discrete sites of close apposition between ER and mitochondria facilitate interorganelle calcium and phospholipid exchange.	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. 	The protein was validated by pull-down, HPTLC and MS in yeast strains.	21825164	The core building block of ERMES is a heterotetrameric protein complex composed of Mmm1, an ER-resident integral membrane protein; Mdm12, a cytosolic protein; Mdm34, a putative OMM protein; and Mdm10, an integral B-barrel OMM protein.	The protein was validated by live microscopy and immunofluorescence in yeast strains, which regulates apoptosis at endoplasmic reticulum by modulating calcium release.	23781023	The yeast mitochondrial outer membrane (MOM) protein Mdm10 is involved in at least three different processes: (1) association of mitochondria with the endoplasmic reticulum and mitochondrial lipid homeostasis (2) membrane assembly of MOM proteins, and (3) inheritance and morphogenesis of mitochondria.	The protein was validated by biochemical methods, fluorescence microscopy and lipid component analysis in yeast strains, which plays a crucial role in ergosterol homeostasis of the organelle.	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.	The protein was validated by in fluorescence microscopy, liposome binding assay and membrane flotation in optiprep gradients.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00181	MMM1; YME6; YLL006W; L1357	850654	MMM1	P41800	Yeast	ER-MT; MT-ER	ER	Yeast strains	Low throughput experimental methods	5	19556461	We identified the Mmm1,Mdm10,Mdm12,Mdm36 complex as a molecular tether between ER and Mitochondrion. 	The protein was validated by mutagenesis screen, microscopy, phospholipid analysis and protein analysis in yeast strains, and the tethering complex localized to discrete foci, suggesting that discrete sites of close apposition between ER and mitochondria facilitate interorganelle calcium and phospholipid exchange.	29279306	Structure-function insights into direct lipid transfer between membranes by Mmm1-Mdm12 of ERMES. 	The protein was validated by crystallization, data collection, lipid analyses and simulation methods in yeast strains, and the Mmm1–Mdm12 complex functions as a minimal unit that mediates lipid transfer between membranes.	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. 	The protein was validated by pull-down, HPTLC and MS in yeast strains.	21825164	The core building block of ERMES is a heterotetrameric protein complex composed of Mmm1, an ER-resident integral membrane protein; Mdm12, a cytosolic protein; Mdm34, a putative OMM protein; and Mdm10, an integral B-barrel OMM protein.	The protein was validated by live microscopy and immunofluorescence in yeast strains, which regulates apoptosis at endoplasmic reticulum by modulating calcium release.	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.	The protein was validated by in fluorescence microscopy, liposome binding assay and membrane flotation in optiprep gradients, which plays roles in lipid metabolism.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00196	LAM6; LTC1; YLR072W	850761	LAM6	Q08001	Yeast	ER-MT; MT-ER	ER	Yeast strains	Low throughput experimental methods	2	26119743	Here, we show thatSaccharomyces cerevisiaeLam6 resides in several central contact sites: ERMES (ER Mitochondrion encounter structure), vCLAMP (vacuole and Mitochondrion patch), and NVJ (nuclear vacuolar junction). 	The protein was validated by manual fluorescence microscopy, EM and interaction proteomics in Yeast strains.	25987606	Ltc1 is an ER-localized sterol transporter and a component of ER–mitochondria and ER–vacuole contacts.	The protein was validated by fluorescence microscopy, immunopurification and tandem mass spectrometry in yeast strains, and the EMC mediates lipid trafficking between the ER and mitochondria, which is a sterol-dependent regulator of organelle and cellular homeostasis via its dual localization to ER–mitochondria and ER–vacuole contact sites.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00237	EMC1; YCL045C; YCL315; YCL45C	850312	EMC1	P25574	Yeast	ER-MT; MT-ER	ER	Yeast strains	Low throughput experimental methods	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.Together, our findings support that the EMC tethers ER to mitochondria, which is required for phospholipid synthesis and cell.	The protein was validated by fluorescence microscopy, in vivo labeling, psd assay, EM and co-immunoprecipitation in yeast strains, and the EMC mediates lipid trafficking between the ER and mitochondria.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00238	EMC2; YJR088C; J1875	853550	EMC2	P47133	Yeast	ER-MT; MT-ER	ER	Yeast strains	Low throughput experimental methods	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.Together, our findings support that the EMC tethers ER to mitochondria, which is required for phospholipid synthesis and cell.	The protein was validated by fluorescence microscopy, in vivo labeling, psd assay, EM and co-immunoprecipitation in yeast strains, and the EMC mediates lipid trafficking between the ER and mitochondria.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00239	EMC5; KRE27; YIL027C	854785	EMC5	P40540	Yeast	ER-MT; MT-ER	ER	Yeast strains	Low throughput experimental methods	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.Together, our findings support that the EMC tethers ER to mitochondria, which is required for phospholipid synthesis and cell.	The protein was validated by fluorescence microscopy, in vivo labeling, psd assay, EM and co-immunoprecipitation in yeast strains, and the EMC mediates lipid trafficking between the ER and mitochondria.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00240	PEX3; PAS3; YDR329C; D9798.15	851929	PEX3	P28795	Yeast	ER-Peroxisome; Peroxisome-ER	Peroxisome	Yeast strains	Low throughput experimental methods	1	23900285	Inp1p bridges the two compartments by acting as a molecular hinge between ER-bound Pex3p and peroxisomal Pex3p.	The protein was validated by confocal fluorescence microscopy in yeast strains, and the EMC mediates lipid trafficking between the ER and mitochondria, and the ER-peroxisome tether exerts peroxisome population control in yeast.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00241	INP1; YMR204C; YM8325.05C	855244	INP1	Q03694	Yeast	ER-Peroxisome; Peroxisome-ER	Peroxisome	Yeast strains	Low throughput experimental methods	1	23900285	Inp1p bridges the two compartments by acting as a molecular hinge between ER-bound Pex3p and peroxisomal Pex3p.	The protein was validated by confocal fluorescence microscopy in yeast strains, and the EMC mediates lipid trafficking between the ER and mitochondria, and the ER-peroxisome tether exerts peroxisome population control in yeast.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00250	PEX32	25774068	PEX32	A4GFD3	Yeast	ER-Peroxisome; Peroxisome-ER	Peroxisome	Yeast strains	Low throughput experimental methods	2	32665322	Pex24 and Pex32 are required to tether peroxisomes to the ER for organelle biogenesis, positioning and segregation in Yeast. 	The protein was validated by molecula, biochemical techniques, fluorescence microscopy, eluorescence microscopy and in silico analyses in yeast strains, and Pex24 and Pex32 are required to tether peroxisomes to the ER for organelle biogenesis, positioning and segregation in yeast.	35252206	In the yeast Hansenula polymorpha the peroxisomal membrane protein Pex11 and three endoplasmic reticulum localized proteins of the Pex23 family (Pex23, Pex24 and Pex32) are involved in the formation of peroxisome-ER contact sites.	The protein was validated by plasmids, molecular techniques and microscopy in yeast strains, which is involved in non-vesicular lipid transfer and important for expansion of the peroxisomal 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	NA	NA	NA	NA	NA	NA
LMCS00251	INP1	25773670	INP1	C0JW63	Yeast	ER-Peroxisome; Peroxisome-ER	Peroxisome	Yeast strains	Low throughput experimental methods	1	32665322	This indicates that Pex11 contributes to Pex32-dependent peroxisome-ER contact formation.	The protein was validated by molecula, biochemical techniques, fluorescence microscopy, eluorescence microscopy and in silico analyses in yeast strains, and 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	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00252	PEX24	25772954	PEX24	A4GFC9	Yeast	ER-Peroxisome; Peroxisome-ER	Peroxisome	Yeast strains	Low throughput experimental methods	2	32665322	Pex24 and Pex32 are required to tether peroxisomes to the ER for organelle biogenesis, positioning and segregation in Yeast. 	The protein was validated by molecula, biochemical techniques, fluorescence microscopy, eluorescence microscopy and in silico analyses in yeast strains, and Pex24 and Pex32 are required to tether peroxisomes to the ER for organelle biogenesis, positioning and segregation in yeast.	35252206	In the yeast Hansenula polymorpha the peroxisomal membrane protein Pex11 and three endoplasmic reticulum localized proteins of the Pex23 family (Pex23, Pex24 and Pex32) are involved in the formation of peroxisome-ER contact sites.	The protein was validated by plasmids, molecular techniques and microscopy in yeast strains, which is involved in non-vesicular lipid transfer and important for expansion of the peroxisomal 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	NA	NA	NA	NA	NA	NA
LMCS00264	SWH1; OSH1; YAR042W; YAR044W	851286	SWH1	P35845	Yeast	ER-PM; PM-ER	NA	Yeast strains	Low throughput experimental methods	1	21295699	Osh proteins regulate phosphoinositide metabolism at ER-plasma membrane contact sites.	The protein was validated by fluorescence microscopy, PI analysis, protein expression levels, protein-binding assays, Sac1 phosphatase assays, lipid-binding assays, NBD protein labeling and fluorescence spectroscopy in yeast strains, which regulates phosphoinositide metabolism at ER-Plasma membrane contact sites.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00265	IST2; YBR086C; YBR0809	852382	IST2	P38250	Yeast	ER-PM; PM-ER	NA	Yeast strains	Low throughput experimental methods	3	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.	The protein was validated by fluorescence microscopy, electron microscopy, phosphoinositide analysis, subcellular fractionation and β-Galactosidase assays in yeast strains, and the junctions are required for PI4P turnover at the PM.	32327560	Osh6 requires Ist2 for localization to ER–PM contacts and efficient phosphatidylserine transport in budding yeast.	The protein was validated by yeast two-hybrid assay, fluorescence microscopy, immunoprecipitation, western blot and mass spectrometry in yeast strains, which together mediate lipid transport at contact sites.	34259806	Ist2 recruits the lipid transporters Osh6/7 to ER–PM contacts to maintain phospholipid metabolism.	The protein was validated by confocal microscopy, protein interaction assay and SGA analysis in yeast strains, and the contacts maintain phospholipid metabolism.	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
LMCS00266	SCS2; YER120W	856856	SCS2	P40075	Yeast	ER-PM; PM-ER	ER	Yeast strains	Low throughput experimental methods	5	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.	The protein was validated by fluorescence microscopy, electron microscopy, phosphoinositide analysis, subcellular fractionation and β-Galactosidase assays in yeast strains, and the junctions are required for PI4P turnover at the PM.	23041194	Of the two proteins, Scs2 appeared to play a more prominent role in maintaining the ER-plasma membrane (PM) attachment.	The protein was validated by confocal microscopy, epifluorescence and differential interference images in yeast strains.	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.	The protein was validated by cell imaging, in vitro binding assay and functionality of GFP-tagged Opi1p in yeast strains.	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.	The protein was validated by affinity purification, mass spectrometry, confocal microscopy, photobleaching experiments, genetic interactions, in vitro binding and coimmunopurification experiments in yeast strains, and the ER-septin tethering at the yeast bud neck creates a diffusion barrier for ER proteins.	17984322	Scs2 interacts with an unidentifi ed bud tip component, suggesting that it bridges directly from the ER to the plasma membrane.	The protein was validated by light microscopy, electron microscopy, morphometry, quantitation of cER, swe1-myc protein levels and SGA analysis in yeast strains, which is required for cER inheritance.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00267	TCB2; YNL087W; N2250	855637	TCB2	P48231	Yeast	ER-PM; PM-ER	ER	Yeast strains	Low throughput experimental methods	2	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.	The protein was validated by fluorescence microscopy, electron microscopy, phosphoinositide analysis, subcellular fractionation and β-Galactosidase assays in yeast strains, and the junctions are required for PI4P turnover at the PM.	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.	The protein was validated by in fluorescence microscopy, liposome binding assay and membrane flotation in optiprep gradients, which plays roles in lipid metabolism.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00268	TCB3; YML072C	854903	TCB3	Q03640	Yeast	ER-PM; PM-ER	ER	Yeast strains	Low throughput experimental methods	2	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.	The protein was validated by fluorescence microscopy, electron microscopy, phosphoinositide analysis, subcellular fractionation and β-Galactosidase assays in yeast strains, and the junctions are required for PI4P turnover at the PM.	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.	The protein was validated by in fluorescence microscopy, liposome binding assay and membrane flotation in optiprep gradients, which plays roles in lipid metabolism.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00269	TCB1; YOR086C; YOR3141c	854253	TCB1	Q12466	Yeast	ER-PM; PM-ER	ER	Yeast strains	Low throughput experimental methods	2	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.	The protein was validated by fluorescence microscopy, electron microscopy, phosphoinositide analysis, subcellular fractionation and β-Galactosidase assays in yeast strains, and the junctions are required for PI4P turnover at the PM.	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.	The protein was validated by in fluorescence microscopy, liposome binding assay and membrane flotation in optiprep gradients, which plays roles in lipid metabolism.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00270	SCS22; YBL091C-A	852186	SCS22	Q6Q595	Yeast	ER-PM; PM-ER	ER	Yeast strains	Low throughput experimental methods	2	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.	The protein was validated by fluorescence microscopy, electron microscopy, phosphoinositide analysis, subcellular fractionation and β-Galactosidase assays in yeast strains, and the junctions are required for PI4P turnover at the PM.	23041194	Here, we identify the integral ER vesicle-associated membrane protein-associated proteins (VAPs), previously shown to control the composition of phosphoinositides at the ER-PM contact sites.; The VAP Proteins Scs2 and Scs22 Link the ER to the Lateral Cortex in S. pombe.	The protein was validated by confocal microscopy, epifluorescence and differential interference images in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00277	OSH3; YHR073W	856472	OSH3	P38713	Yeast	ER-PM; PM-ER	PM	Yeast strains	Low throughput experimental methods	2	21295699	Osh proteins regulate phosphoinositide metabolism at ER-plasma membrane contact sites.	The protein was validated by fluorescence microscopy, PI analysis, protein expression levels, protein-binding assays, Sac1 phosphatase assays, lipid-binding assays, NBD protein labeling and fluorescence spectroscopy in Yeast strains, which regulates phosphoinositide metabolism at ER-Plasma membrane contact sites.	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.	The protein was validated by cell imaging, in vitro binding assay and functionality of GFP-tagged Opi1p in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00278	OSH2; YDL019C; D2845	851543	OSH2	Q12451	Yeast	ER-PM; PM-ER	PM	Yeast strains	Low throughput experimental methods	2	21295699	Osh proteins regulate phosphoinositide metabolism at ER-plasma membrane contact sites.	The protein was validated by fluorescence microscopy, PI analysis, protein expression levels, protein-binding assays, Sac1 phosphatase assays, lipid-binding assays, NBD protein labeling and fluorescence spectroscopy in Yeast strains, which regulates phosphoinositide metabolism at ER-Plasma membrane contact sites.	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.	The protein was validated by cell imaging, in vitro binding assay and functionality of GFP-tagged Opi1p in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00284	YSP2; LAM2; LTC4; YDR326C	851926	YSP2	Q06681	Yeast	ER-PM; PM-ER	NA	Yeast strains	Low throughput experimental methods	2	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. 	The protein was validated by bioinformatics and microscopy in yeast strains, which has a role in ER-PM sterol transport.	28774891	Ltc3/4 define a new PM compartment at ER–PM contacts: The MCL.	The protein was validated by microscopy, image analysis, immunopurifications, proteomic analyses and western blotting in yeast strains, which coordinates cellular stress responses with sterol homeostasis.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00285	LAM4; LTC3; YHR080C	856480	LAM4	P38800	Yeast	ER-PM; PM-ER	ER	Yeast strains	Low throughput experimental methods	2	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. 	The protein was validated by bioinformatics and microscopy in yeast strains, which has a role in ER-PM sterol transport.	28774891	Ltc3/4 define a new PM compartment at ER–PM contacts: The MCL.	The protein was validated by microscopy, image analysis, immunopurifications, proteomic analyses and western blotting in yeast strains, which coordinates cellular stress responses with sterol homeostasis.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00287	MDM1; YML104C; YM8339.15C	854867	MDM1	Q01846	Yeast	ER-Vacuole; Vacuole-ER	NA	Yeast strains	Low throughput experimental methods	4	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.	The protein was validated by SGA methodology, Mup1-pHuorin screening, light microscopy, EM and yeast myriocin plating assays in yeast strains.	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. 	The protein was validated by lipid droplets, vacuole staining, microscopy, fluorescence image quantification, immuno‐precipitation and TLC quantification in yeast strains.	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was validated by co-localization imaging and organelle labelling in yeast strains.	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was validated by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00288	YDR179W-A; YD9395.13	851760	Nvj3	Q03983	Yeast	ER-Vacuole; Vacuole-ER	NA	Yeast strains	Low throughput experimental methods	3	26283797	Nvj3 Ydr179w-a is a second, novel ER-vacuole MCS protein.	The protein was validated by SGA methodology, Mup1-pHuorin screening, light microscopy, EM and yeast myriocin plating assays in yeast strains.	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. 	The protein was validated by lipid droplets, vacuole staining, microscopy, fluorescence image quantification, immuno‐precipitation and TLC quantification in yeast strains.	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was validated by co-localization imaging and organelle labelling in yeast strains.	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
LMCS00289	VAC8; YEB3; YEL013W	856702	VAC8	P39968	Yeast	ER-Vacuole; Vacuole-ER	Vacuole	Yeast strains	Low throughput experimental methods	2	25987606	Ltc1 localized to ER-Mitochondrion and ER-vacuole contacts via the Mitochondrionl import receptors Tom70,71 and the vacuolar protein Vac8, respectively. 	The protein was validated by fluorescence microscopy, immunopurification and tandem mass spectrometry in yeast strains, and the EMC mediates lipid trafficking between the ER and mitochondria.	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was validated by co-localization imaging and organelle labelling in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00290	LAM6; LTC1; YLR072W	850761	LAM6	Q08001	Yeast	ER-Vacuole; Vacuole-ER	ER	Yeast strains	Low throughput experimental methods	3	25987606	Ltc1 is an ER-localized sterol transporter and a component of ER-Mitochondrion and ER-vacuole contacts. 	The protein was validated by fluorescence microscopy, immunopurification and tandem mass spectrometry in yeast strains, and the EMC mediates lipid trafficking between the ER and mitochondria, which is a sterol-dependent regulator of organelle and cellular homeostasis via its dual localization to ER–mitochondria and ER–vacuole contact sites.	36354737	A total of 158 unique proteins were identified across all six contact sites.	The protein was validated by co-localization imaging and organelle labelling in yeast strains.	28774891	At ER–vacuole contacts, Ltc1 regulates TORC1 signaling via formation of sterol enriched vacuolar membrane domains	The protein was validated by microscopy, image analysis, immunopurifications, proteomic analyses and western blotting in yeast strains, which coordinates cellular stress responses with sterol homeostasis.	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
LMCS00292	SWH1; OSH1; YAR042W; YAR044W	851286	SWH1	P35845	Yeast	Nucleus-Vacuole; Vacuole-Nucleus	NA	Yeast strains	Low throughput experimental methods	3	11408574	Osh1p localizes to the NV junction.	The protein was validated by assay for osh1 growth phenotype and microscopy in yeast strains.	15367582	Here, we investigate the targeting of Osh1p to nucleus-vacuole (NV) junctions in Saccharomyces cerevisiae.	The protein was validated by immunoblot, cell imaging, confocal microscopy and immunoelectron microscopy in yeast strains, and the formation of nuclear PMN vesicles requires the overlapping activities of Osh1p and other Osh family members.	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.	The protein was validated by cell imaging, in vitro binding assay and functionality of GFP-tagged Opi1p in yeast strains.	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
LMCS00353	LAM6; LTC1; YLR072W	850761	LAM6	Q08001	Yeast	MT-Vacuole; Vacuole-MT		Yeast strains	Low throughput experimental methods	1	26119743	Here, we show thatSaccharomyces cerevisiaeLam6 resides in several central contact sites: ERMES (ER Mitochondrion encounter structure), vCLAMP (vacuole and Mitochondrion patch), and NVJ (nuclear vacuolar junction). 	The protein was validated by manual fluorescence microscopy, EM and interaction proteomics in Yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00354	MDM1; YML104C; YM8339.15C	854867	MDM1	Q01846	Yeast	ER-Endosome; Endosome-ER		Yeast strains	Low throughput experimental methods	1	26283797	Surprisingly, we demonstrate that Mdm1 is a novel interorganelle tethering protein that localizes to endoplasmic reticulum (ER)-vacuole/lysosome membrane contact sites (MCSs).	The protein was validated by SGA methodology, Mup1-pHuorin screening, light microscopy, EM and yeast myriocin plating assays in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00356	MDM34; MMM2; YGL219C	852654	MDM34	P53083	Yeast	MT-Peroxisome; Peroxisome-MT	MT	Yeast strains	Low throughput experimental methods	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.	The protein was validated by high-content fluorescence microscopy screen, confocal microscopy, staining, visualization of mitochondria, western blot, quantitative real-time PCR analyses and MYTH assay in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00357	PEX11; PMP24; PMP27; YOL147C; O0454	854018	PEX11	Q12462	Yeast	MT-Peroxisome; Peroxisome-MT	Peroxisome	Yeast strains	Low throughput experimental methods	2	25769804	Genome-wide localization study of yeast Pex11 identifies Peroxisome-Mitochondria interactions through the ERMES complex.	The protein was validated by high-content fluorescence microscopy screen, confocal microscopy, staining, visualization of mitochondria, western blot, quantitative real-time PCR analyses and MYTH assay in yeast strains, which is a protein with roles in metabolism and disease.	35252206	In the yeast Hansenula polymorpha the peroxisomal membrane protein Pex11 and three endoplasmic reticulum localized proteins of the Pex23 family (Pex23, Pex24 and Pex32) are involved in the formation of peroxisome-ER contact sites.	The protein was validated by plasmids, molecular techniques and microscopy in yeast strains, which is involved in non-vesicular lipid transfer and important for expansion of the peroxisomal 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	NA	NA	NA	NA	NA	NA
LMCS00360	PEX34; YCL056C; YCL433; YCL56C	850302	PEX34	P25584	Yeast	MT-Peroxisome; Peroxisome-MT	Peroxisome	Yeast strains	Low throughput experimental methods	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. 	The protein was validated by manual microscopy, split venus reporters and co-immunoprecipitation in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00361	FZO1; YBR179C; YBR1241	852477	FZO1	P38297	Yeast	MT-Peroxisome; Peroxisome-MT	MT	Yeast strains	Low throughput experimental methods	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. 	The protein was validated by manual microscopy, split venus reporters and co-immunoprecipitation in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00362	MFB1; YDR219C	851805	MFB1	Q04922	Yeast	MT-PM; PM-MT	MT	Yeast strains	Low throughput experimental methods	1	26839174	A role for Mfb1p in region-specific anchorage of high-functioning mitochondria and lifespan in Saccharomyces cerevisiae.	The protein was validated by microscopy, RLS analysis and long-term fluorescence microscopy in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00365	NUM1; PAC12; YDR150W; YD8358.06	851727	NUM1	Q00402	Yeast	MT-PM; PM-MT	NA	Yeast strains	Low throughput experimental methods	1	27241910	Num1 anchors mitochondria to the plasma membrane via two domains with different lipid binding specificities.	The protein was validated by imaging, image analysis, SEC-MALS, fluorescence microscopy and yeast two-hybrid analysis in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00366	MDM36; YPR083W	856198	MDM36	Q06820	Yeast	MT-PM; PM-MT	NA	Yeast strains	Low throughput experimental methods	1	27241910	Num1CC interacts directly with Mdm36 and phospholipid membranes.	The protein was validated by imaging, image analysis, SEC-MALS, fluorescence microscopy and yeast two-hybrid analysis in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00367	TOM40; ISP42; MOM38; YMR203W; YM8325.04	855243	TOM40	P23644	Yeast	MT-Vacuole; Vacuole-MT	MT	Yeast strains	Low throughput experimental methods	1	29870720	Vps39 interacts with tom40 to establish one of two functionally distinct vacuole-mitochondrion contact sites.	The protein was validated by fluorescence microscopy, growth tests, growth curves, survival curves, western blotting, SILAC labeling, GFP-trap pull down and mass spectrometry in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00368	VAM6; CVT4; VPL18; VPL22; VPS39; YDL077C	851482	VAM6	Q07468	Yeast	MT-Vacuole; Vacuole-MT	Vacuole	Yeast strains	Low throughput experimental methods	2	29870720	Vps39 interacts with tom40 to establish one of two functionally distinct vacuole-mitochondrion contact sites.	The protein was validated by fluorescence microscopy, growth tests, growth curves, survival curves, western blotting, SILAC labeling, GFP-trap pull down and mass spectrometry in yeast strains.	25026036	Using a high-content screen in yeast, we found a contact site, marked by Vam6/Vps39, between vacuoles (the yeast lysosomal compartment) and mitochondria, named vCLAMP (vacuole and mitochondria patch).	The protein was validated by SGA, high-content screening, manual fluorescence microscopy and electron microscopy in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00369	MCP1; YOR228C; YOR50-18	854403	MCP1	Q12106	Yeast	MT-Vacuole; Vacuole-MT	MT	Yeast strains	Low throughput experimental methods	2	29870720	And a second one by Vps13-Mcp1, which is redundant with ER-Mitochondrionl contacts formed by ERMES. 	The protein was validated by fluorescence microscopy, growth tests, growth curves, survival curves, western blotting, SILAC labeling, GFP-trap pull down and mass spectrometry in yeast strains.	28864540	Vps13-Mcp1 interact at vacuole–mitochondria interfaces and bypass ER–mitochondria contact sites.	The protein was validated by growth assayand microscopy, PK accessibility assay, GFP immunoprecipitation and fluorescence microscopy in yeast strains, which suppress all measured phenotypic consequences of ERMES deficiency.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00372	PDR16; SFH3; YNL231C; N1158	855490	PDR16	P53860	Yeast	LD-Parasitophorous Vacuole; Parasitophorous Vacuole-LD	LD	Yeast strains	Low throughput experimental methods	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.	The protein was validated by protein complementation assay screen, lipid analysis by non-targeted gas chromatography-mass spectrometry and structured illumination microscopy in yeast strains, which is crucial for efficient clearance of inclusion bodies.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00373	IML2; YJL082W; J1007	853363	IML2	P47031	Yeast	LD-Parasitophorous Vacuole; Parasitophorous Vacuole-LD	Parasitophorous Vacuole	Yeast strains	Low throughput experimental methods	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.	The protein was validated by protein complementation assay screen, lipid analysis by non-targeted gas chromatography-mass spectrometry and structured illumination microscopy in yeast strains, which is crucial for efficient clearance of inclusion bodies.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00374	PET10; YKR046C	853920	PET10	P36139	Yeast	LD-Parasitophorous Vacuole; Parasitophorous Vacuole-LD	LD	Yeast strains	Low throughput experimental methods	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.	The protein was validated by protein complementation assay screen, lipid analysis by non-targeted gas chromatography-mass spectrometry and structured illumination microscopy in yeast strains, and the interactors reveal a role for lipid droplets in inclusion clearance.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00375	VPS13; SOI1; VPT2; YME3; YLL040C	850619	VPS13	Q07878	Yeast	MT-Vacuole; Vacuole-MT	NA	Yeast strains	Low throughput experimental methods	3	29870720	And a second one by Vps13-Mcp1, which is redundant with ER-Mitochondrionl contacts formed by ERMES. 	The protein was validated by fluorescence microscopy, growth tests, growth curves, survival curves, western blotting, SILAC labeling, GFP-trap pull down and mass spectrometry in yeast strains.	28864540	Vps13-Mcp1 interact at vacuole–mitochondria interfaces and bypass ER–mitochondria contact sites.	The protein was validated by growth assayand microscopy, PK accessibility assay, GFP immunoprecipitation and fluorescence microscopy in yeast strains, which suppress all measured phenotypic consequences of ERMES deficiency.	26370498	Vps13 dynamically localizes to vacuole–mitochondria and to vacuole–nucleus contact sites depending on growth conditions.	The protein was validated by whole genome resequencing and microscopy in yeast strains, which suppress all measured phenotypic consequences of ERMES deficiency.	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
LMCS00376	YPT7; VAM4; YML001W; YM8270.02	855012	YPT7	P32939	Yeast	MT-Vacuole; Vacuole-MT	Vacuole	Yeast strains	Low throughput experimental methods	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.	The protein was validated by fluorescence microscopy, growth tests, growth curves, survival curves, western blotting, SILAC labeling, GFP-trap pull down and mass spectrometry in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00377	NVJ1; VAB36; YHR195W	856602	NVJ1	P38881	Yeast	Nucleus-Vacuole; Vacuole-Nucleus	Nucleus	Yeast strains	Low throughput experimental methods	1	10888680	Nucleus-vacuole junctions in Saccharomyces cerevisiae are formed through the direct interaction of Vac8p with Nvj1p.	The protein was validated by glutathione sepharose affinity chromatography, two-hybrid screen, analysis of API processing and microscopy in yeast strains, which are necessary components of a novel interorganelle junction apparatus.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00378	VAC8; YEB3; YEL013W	856702	VAC8	P39968	Yeast	Nucleus-Vacuole; Vacuole-Nucleus	Vacuole	Yeast strains	Low throughput experimental methods	2	10888680	Nucleus-vacuole junctions in Saccharomyces cerevisiae are formed through the direct interaction of Vac8p with Nvj1p.	The protein was validated by glutathione sepharose affinity chromatography, two-hybrid screen, analysis of API processing and microscopy in yeast strains, which are necessary components of a novel interorganelle junction apparatus.	26119743	This observation, coupled with the fact that one of the physical interactors of Lam6 was the NVJ contact site protein Vac8.	The protein was validated by manual fluorescence microscopy, EM and interaction proteomics in Yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00379	LAM6; LTC1; YLR072W	850761	LAM6	Q08001	Yeast	Nucleus-Vacuole; Vacuole-Nucleus	NA	Yeast strains	Low throughput experimental methods	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.	The protein was validated by manual fluorescence microscopy, EM and interaction proteomics in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00391	SIP3; LAM3; YNL257C; N0844	855464	SIP3	P38717	Yeast	ER-PM; PM-ER	ER	Yeast strains	Low throughput experimental methods	2	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.	The protein was validated by bioinformatics and microscopy in yeast strains, which has a role in ER-PM sterol transport.	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.	The protein was validated by microscopy, image analysis, immunopurifications, proteomic analyses and western blotting in yeast strains, which coordinates cellular stress responses with sterol homeostasis.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00396	OSH7; YHR001W	856389	OSH7	P38755	Yeast	ER-PM; PM-ER	ER	Yeast strains	Low throughput experimental methods	4	20008566	The ability of ORDs to interact with two membranes simultaneously could help promote the enrichment of Osh6p and Osh7p (and perhaps other ORPs) at MCSs. 	The protein was validated by fluorescence microscopy, tethering assays, transfer assays, Cryo-EM and analytical ultracentrifugation in yeast strains, which could sense and regulate the lipid composition of adjacent membranes.	23934110	Osh6 and Osh7 localize at membrane contact sites that bridge PS synthesis (the ER) with areas of PS accumulation and biological activity (the PM).	The protein was validated by HPTLC, LC/MS and fluorescence microscopy in yeast strains, which could sense and regulate the lipid composition of adjacent membranes.	32327560	Osh6 and Osh7 localize to ER–PM contact sites, although they lack membrane-targeting motifs.	The protein was validated by yeast two-hybrid assay, fluorescence microscopy, western blot and mass spectrometry in yeast strains.	34259806	Ist2 recruits the lipid transporters Osh6/7 to ER–PM contacts to maintain phospholipid metabolism.	The protein was validated by confocal microscopy, protein interaction assay and SGA analysis in yeast strains, and the contacts maintain phospholipid metabolism.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00397	OSH6; YKR003W; YK102	853872	OSH6	Q02201	Yeast	ER-PM; PM-ER	ER	Yeast strains	Low throughput experimental methods	4	20008566	The ability of ORDs to interact with two membranes simultaneously could help promote the enrichment of Osh6p and Osh7p (and perhaps other ORPs) at MCSs. 	The protein was validated by fluorescence microscopy, tethering assays, transfer assays, Cryo-EM and analytical ultracentrifugation in yeast strains, which could sense and regulate the lipid composition of adjacent membranes.	23934110	Osh6 and Osh7 localize at membrane contact sites that bridge PS synthesis (the ER) with areas of PS accumulation and biological activity (the PM).	The protein was validated by HPTLC, LC/MS and fluorescence microscopy in yeast strains, which could sense and regulate the lipid composition of adjacent membranes.	32327560	Osh6 requires Ist2 for localization to ER–PM contacts and efficient phosphatidylserine transport in budding yeast.	The protein was validated by yeast two-hybrid assay, fluorescence microscopy, immunoprecipitation, western blot and mass spectrometry in yeast strains, which together mediate lipid transport at contact sites.	34259806	Ist2 recruits the lipid transporters Osh6/7 to ER–PM contacts to maintain phospholipid metabolism.	The protein was validated by confocal microscopy, protein interaction assay and SGA analysis in yeast strains, and the contacts maintain phospholipid metabolism.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00400	LAM5; LTC2; YFL042C	850501	LAM5	P43560	Yeast	Nucleus-Vacuole; Vacuole-Nucleus	NA	Yeast strains	Low throughput experimental methods	1	26001273	In contrast to these four peripheral proteins, both Lam5p and Lam6p showed complex intracellular targeting to multiple MCSs, including the NVJ and ER-mitochondrial contacts.	The protein was validated by bioinformatics and microscopy in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00401	LAM1; YSP1; YHR155W	856560	LAM1	P38851	Yeast	ER-PM; PM-ER	ER	Yeast strains	Low throughput experimental methods	2	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.	The protein was validated by bioinformatics and microscopy in yeast strains, which has a role in ER-PM sterol transport.	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.	The protein was validated by microscopy, image analysis, immunopurifications, proteomic analyses and western blotting in yeast strains, which coordinates cellular stress responses with sterol homeostasis.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00408	DGR2; YKL121W; YKL525	853738	DGR2	P32330	Yeast	ER-PM; PM-ER	NA	Yeast strains	Low throughput experimental methods	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.	The protein was validated by microscopy, image analysis, immunopurifications, proteomic analyses and western blotting in yeast strains, which coordinates cellular stress responses with sterol homeostasis.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00409	YMR102C; YM6228.01C; YM6543.09C; YM9718.01C	855128	YMR102C	Q03177	Yeast	ER-PM; PM-ER	NA	Yeast strains	Low throughput experimental methods	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.	The protein was validated by microscopy, image analysis, immunopurifications, proteomic analyses and western blotting in yeast strains, which coordinates cellular stress responses with sterol homeostasis.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00410	LAM6; LTC1; YLR072W	850761	LAM6	Q08001	Yeast	ER-PM; PM-ER	ER	Yeast strains	Low throughput experimental methods	1	28774891	Ltc1 colocalizes with MCL proteins and partially colocalizes with Slm1.	The protein was validated by microscopy, image analysis, immunopurifications, proteomic analyses and western blotting in yeast strains, which coordinates cellular stress responses with sterol homeostasis.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00411	SLM1; LIT2; YIL105C	854701	SLM1	P40485	Yeast	ER-PM; PM-ER	NA	Yeast strains	Low throughput experimental methods	1	28774891	Ltc1 colocalizes with MCL proteins and partially colocalizes with Slm1.	The protein was validated by microscopy, image analysis, immunopurifications, proteomic analyses and western blotting in yeast strains, which coordinates cellular stress responses with sterol homeostasis.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00420	VPS13; SOI1; VPT2; YME3; YLL040C	850619	VPS13	Q07878	Yeast	ER-Peroxisome; Peroxisome-ER	NA	Yeast strains	Low throughput experimental methods	1	35252206	Here we identified VPS13 as a gene required for peroxisome biogenesis in H. polymorpha cells with disturbed peroxisome-ER contacts.	The protein was validated by plasmids, molecular techniques and microscopy in yeast strains, which is crucial for peroxisome formation in cells with reduced peroxisome-endoplasmic reticulum contact sites and plays a redundant function in lipid transfer from the ER to peroxisomes.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00424	VPS13; SOI1; VPT2; YME3; YLL040C	850619	VPS13	Q07878	Yeast	Nucleus-Vacuole; Vacuole-Nucleus	NA	Yeast strains	Low throughput experimental methods	3	26370498	Vps13 dynamically localizes to vacuole–mitochondria and to vacuole–nucleus contact sites depending on growth conditions.	The protein was validated by whole genome resequencing and microscopy in yeast strains, which suppress all measured phenotypic consequences of ERMES deficiency.	27280386	In different growth conditions, Vps13 localizes to endosome–mitochondrion contacts and to the nuclear–vacuole junctions, indicating that Vps13 may function at membrane contact sites.	The protein was validated by sporulation assays, western blot analysis, mitophagy assay and microscopy in yeast strains, which promotes mitochondrial function.	30018089	Vps13 and Ypt35 are interdependent for recruitment to the NVJ.	The protein was validated by fluorescence microscopy and coimmunoprecipitation in yeast strains.	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
LMCS00426	VPS13; SOI1; VPT2; YME3; YLL040C	850619	VPS13	Q07878	Yeast	MT-Endosome; Endosome-MT	NA	Yeast strains	Low throughput experimental methods	1	27280386	In different growth conditions, Vps13 localizes to endosome–mitochondrion contacts and to the nuclear–vacuole junctions, indicating that Vps13 may function at membrane contact sites.	The protein was validated by sporulation assays, western blot analysis, mitophagy assay and microscopy in yeast strains, which promotes mitochondrial function.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00450	FMP27; HOB1; YLR454W	851175	FMP27	Q06179	Yeast	ER-PM; PM-ER	ER	Yeast strains	Low throughput experimental methods	2	34415038	Taken together, these results demonstrate that Fmp27 localizes to ER-PM contact sites but does not appear to function as a tether.	The protein was validated by yeast imaging, yeast protease protection assay, electron microscopy, sequence alignments, conservation analysis, protein expression, purification, lipid blots and confocal microscopy in yeast strains.	35015055	Together, these findings indicate that Csf1, Fmp27, or Hob2 localizes to ER-PM and some ER-mitochondria contact sites. 	The protein was validated by microscopy of yeast, coimmunoprecipitation and qRT-PCR in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00452	FMP27; HOB1; YLR454W	851175	FMP27	Q06179	Yeast	ER-MT; MT-ER	NA	Yeast strains	Low throughput experimental methods	1	35015055	Together, these findings indicate that Csf1, Fmp27, or Hob2 localizes to ER-PM and some ER-mitochondria contact sites. 	The protein was validated by microscopy of yeast, coimmunoprecipitation and qRT-PCR in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00453	CSF1; TWEEK; YLR087C	850776	CSF1	Q12150	Yeast	ER-MT; MT-ER	NA	Yeast strains	Low throughput experimental methods	1	35015055	Together, these findings indicate that Csf1, Fmp27, or Hob2 localizes to ER-PM and some ER-mitochondria contact sites.	The protein was validated by microscopy of yeast, coimmunoprecipitation and qRT-PCR in yeast strains, which is necessary for efficient P-Etn incorporation into GPI anchors.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00454	HOB2; YPR117W	856233	Hob2	Q06116	Yeast	ER-MT; MT-ER	NA	Yeast strains	Low throughput experimental methods	1	35015055	Together, these findings indicate that Csf1, Fmp27, or Hob2 localizes to ER-PM and some ER-mitochondria contact sites.	The protein was validated by microscopy of yeast, coimmunoprecipitation and qRT-PCR in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00455	CSF1; TWEEK; YLR087C	850776	CSF1	Q12150	Yeast	ER-PM; PM-ER	NA	Yeast strains	Low throughput experimental methods	1	35015055	Csf1, Fmp27, and Hob2 localize to ER-PM and ER-mitochondria contact sites.	The protein was validated by microscopy of yeast, coimmunoprecipitation and qRT-PCR in yeast strains, which is necessary for efficient P-Etn incorporation into GPI anchors.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00456	HOB2; YPR117W	856233	Hob2	Q06116	Yeast	ER-PM; PM-ER	NA	Yeast strains	Low throughput experimental methods	2	35015055	Csf1, Fmp27, and Hob2 localize to ER-PM and ER-mitochondria contact sites.	The protein was validated by microscopy of yeast, coimmunoprecipitation and qRT-PCR in yeast strains.	34415038	The Hob proteins are novel and conserved lipid-binding proteins at ER–PM contact sites.	The protein was validated by yeast imaging, yeast protease protection assay, electron microscopy, sequence alignments, conservation analysis, protein expression, purification, lipid blots and confocal microscopy in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00461	PEX23	25770984	PEX23	A4GFC7	Yeast	ER-Peroxisome; Peroxisome-ER	ER	Yeast strains	Low throughput experimental methods	1	35252206	In the yeast Hansenula polymorpha the peroxisomal membrane protein Pex11 and three endoplasmic reticulum localized proteins of the Pex23 family (Pex23, Pex24 and Pex32) are involved in the formation of peroxisome-ER contact sites.	The protein was validated by plasmids, molecular techniques and microscopy in yeast strains, which is involved in non-vesicular lipid transfer and important for expansion of the peroxisomal 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	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00515	PEX3; PAS3; YDR329C; D9798.15	851929	PEX3	P28795	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	Peroxisome	Yeast strains	Low throughput experimental methods	1	23900285	Peroxisome development in yeast is associated with the formation of Pex3-dependent peroxisome-vacuole contact sites.	The protein was validated by biochemical techniques, fluorescence microscopy and EM in yeast strains, and this contact likely plays a role in membrane growth as it is formed solely at conditions of strong peroxisome expansion.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00516	PEX3; PAS3; YDR329C; D9798.15	851929	PEX3	P28795	Yeast	PM-Peroxisome; Peroxisome-PM	Peroxisome	Yeast strains	Low throughput experimental methods	1	32970792	The Pex3–Inp1 complex tethers yeast peroxisomes to the plasma membrane.	The protein was validated by cell lysis, immunoblotting, in vitro binding assays and in vitro competition assay in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00517	INP1; YMR204C; YM8325.05C	855244	INP1	Q03694	Yeast	PM-Peroxisome; Peroxisome-PM	PM	Yeast strains	Low throughput experimental methods	1	32970792	The Pex3–Inp1 complex tethers yeast peroxisomes to the plasma membrane.	The protein was validated by cell lysis, immunoblotting, in vitro binding assays and in vitro competition assay in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00526	YMR160W; YM8520.09	855195	Cvm1	Q03823	Yeast	MT-Vacuole; Vacuole-MT	NA	Yeast strains	Low throughput experimental methods	1	35766971	Taken together, our results show that Cvm1 is a novel tethering component of the vacuole–mitochondria contact site.	The protein was validated by low-throughput microscopy, growth tests, immuno-EM, SDS-PAGE and western blot in yeast strains, which is a component of multiple vacuolar contact sites required for sphingolipid homeostasis.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00527	YMR160W; YM8520.09	855195	Cvm1	Q03823	Yeast	Nucleus-Vacuole; Vacuole-Nucleus	NA	Yeast strains	Low throughput experimental methods	1	35766971	Furthermore, some Cvm1 accumulations colocalized with accumulations of Vac8 on the vacuolar membrane.; Cvm1 can thus be a part of the NVJ.	The protein was validated by low-throughput microscopy, growth tests, immuno-EM, SDS-PAGE and western blot in yeast strains, which is a component of multiple vacuolar contact sites required for sphingolipid homeostasis.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00528	ATG18; AUT10; CVT18; NMR1; SVP1; YFR021W	850577	ATG18	P43601	Yeast	ER-Phagophore; Phagophore-ER	NA	Yeast strains	Low throughput experimental methods	3	29848619	Assembly of the Atg9–Atg2–Atg18 complex is important to establish phagophore–endoplasmic reticulum (ER) contact sites.	The protein was validated by fluorescence microscopy, GUV assays, fluorescence and IET in yeast strains.	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.	The protein was validated by in silico analysis, in silico modeling, fluorescence microscopy, single-molecule fluorescence microscopy, co-immunoprecipitation experiments, western blotting and pho8delta60 assay in yeast strains, and Atg9 trimers via their transmembrane segments play a key role in phagophore expansion beyond Atg9ʹs role as a lipid scramblase.	30254161	The Atg2-Atg18 complex tethers pre-autophagosomal membranes to the endoplasmic reticulum for autophagosome formation.	The protein was validated by immunoblotting, immunoprecipitation, fluorescence microscopy, liposome flotation assay and liposome tethering assay in yeast strains, which initiates membrane expansion during autophagosome formation.	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
LMCS00529	ATG9; APG9; AUT9; CVT7; YDL149W; D1560	851406	ATG9	Q12142	Yeast	ER-Phagophore; Phagophore-ER	ER	Yeast strains	Low throughput experimental methods	2	29848619	Assembly of the Atg9–Atg2–Atg18 complex is important to establish phagophore–endoplasmic reticulum (ER) contact sites.	The protein was validated by fluorescence microscopy, GUV assays, fluorescence and IET in yeast strains.	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.	The protein was validated by in silico analysis, in silico modeling, fluorescence microscopy, single-molecule fluorescence microscopy, co-immunoprecipitation experiments, western blotting and pho8delta60 assay in yeast strains, and Atg9 trimers via their transmembrane segments play a key role in phagophore expansion beyond Atg9ʹs role as a lipid scramblase.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00530	ATG2; APG2; AUT8; SPO72; YNL242W; N1106	855479	ATG2	P53855	Yeast	ER-Phagophore; Phagophore-ER	ER	Yeast strains	Low throughput experimental methods	3	29848619	Assembly of the Atg9–Atg2–Atg18 complex is important to establish phagophore–endoplasmic reticulum (ER) contact sites.	The protein was validated by fluorescence microscopy, GUV assays, fluorescence and IET in yeast strains.	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.	The protein was validated by in silico analysis, in silico modeling, fluorescence microscopy, single-molecule fluorescence microscopy, co-immunoprecipitation experiments, western blotting and pho8delta60 assay in yeast strains, and Atg9 trimers via their transmembrane segments play a key role in phagophore expansion beyond Atg9ʹs role as a lipid scramblase.	30254161	The Atg2-Atg18 complex tethers pre-autophagosomal membranes to the endoplasmic reticulum for autophagosome formation.	The protein was validated by immunoblotting, immunoprecipitation, fluorescence microscopy, liposome flotation assay and liposome tethering assay in yeast strains, which initiates membrane expansion during autophagosome formation.	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
LMCS00547	YBR063C; YBR0610	852356	CNM1	P38083	Yeast	Nucleus-MT; MT-Nucleus	Nucleus	Yeast strains	Low throughput experimental methods	1	34694322	We show that Cnm1 mediates contact by interacting with Tom70 on mitochondria.	The protein was validated by manual fluorescence microscopy, library preparation, high-throughput screening, EM, western blot and coimmunoprecipitation in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00548	TOM70; MAS70; OMP1; YNL121C; N1905	855602	TOM70	P07213	Yeast	Nucleus-MT; MT-Nucleus	MT	Yeast strains	Low throughput experimental methods	1	34694322	We show that Cnm1 mediates contact by interacting with Tom70 on mitochondria.	The protein was validated by manual fluorescence microscopy, library preparation, high-throughput screening, EM, western blot and coimmunoprecipitation in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00552	YMR160W; YM8520.09	855195	Cvm1	Q03823	Yeast	Peroxisome-Vacuole; Vacuole-Peroxisome	NA	Yeast strains	Low throughput experimental methods	1	35766971	The localization of Cvm1 to the vacuole–peroxisome and vacuole–mitochondria contact sites.	The protein was validated by low-throughput microscopy, growth tests, immuno-EM, SDS-PAGE and western blot in yeast strains, which is a component of multiple vacuolar contact sites required for sphingolipid homeostasis.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00555	DIP2; UTP12; YLR129W; L3116; L9233.1	850820	DIP2	Q12220	Yeast	MT-Vacuole; Vacuole-MT	NA	Yeast strains	Low throughput experimental methods	1	35766356	DIP2 is associated with vacuoles through mitochondria–vacuole contact sites.	The protein was validated by thin-layer chromatography, mass spectrometry, live cell microscopy, western blot analysis and bioinformatics analysis in yeast strains, which is a unique regulator of diacylglycerol lipid homeostasis in eukaryotes.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00566	VAC8; YEB3; YEL013W	856702	VAC8	P39968	Yeast	LD-Vacuole; Vacuole-LD	Vacuole	Yeast strains	Low throughput experimental methods	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.	The protein was validated by immunoblot analysis, Quantitative Real-Time PCR, confocal fluorescence microscopy, transmission electron microscopy and immuno-electron microscopy in yeast strains, which can delivery of diverse cargo to the 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	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00567	YMR147W; YM9375.17	855178	LDO45	P40218	Yeast	LD-Vacuole; Vacuole-LD	LD	Yeast strains	Low throughput experimental methods	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.	The protein was validated by immunoblot analysis, Quantitative Real-Time PCR, confocal fluorescence microscopy, transmission electron microscopy and immuno-electron microscopy in yeast strains, and loss of vCLIP formation upon genetic ablation of the LDO proteins results in NVJ expansion and induction of PMN. 	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00568	OSW5; YMR148W; YM9375.18	855179	LDO16	P40219	Yeast	LD-Vacuole; Vacuole-LD	LD	Yeast strains	Low throughput experimental methods	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.	The protein was validated by immunoblot analysis, Quantitative Real-Time PCR, confocal fluorescence microscopy, transmission electron microscopy and immuno-electron microscopy in yeast strains, and loss of vCLIP formation upon genetic ablation of the LDO proteins results in NVJ expansion and induction of PMN. 	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA
LMCS00638	YPT35; YHR105W	856505	YPT35	P38815	Yeast	Nucleus-Vacuole; Vacuole-Nucleus	Vacuole	Yeast strains	Low throughput experimental methods	1	30018089	Vps13 and Ypt35 are interdependent for recruitment to the NVJ.	The protein was validated by fluorescence microscopy and coimmunoprecipitation in yeast strains.	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA	NA