PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
28924045-8	2017	Moreover, the mitochondria-specific phospholipid, cardiolipin, was significantly reduced in both strains compromised for Opi1p-Scs2p interaction, indicating that this interaction is required for the transfer of phosphatidic acid from the ER to the mitochondria for cardiolipin synthesis.	Phospholipids	36-48	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	127-132
33917059-4	2021	In addition, we characterize through the hydrogen/deuterium (H/D) exchange assay the interface between Scs2 and Epo1.	Hydrogen	41-49	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	103-107
33917059-4	2021	In addition, we characterize through the hydrogen/deuterium (H/D) exchange assay the interface between Scs2 and Epo1.	Deuterium	50-59	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	103-107
33917059-4	2021	In addition, we characterize through the hydrogen/deuterium (H/D) exchange assay the interface between Scs2 and Epo1.	Deuterium	63-64	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	103-107
30084355-4	2018	Cells lacking Scs2/Scs22 performed spindle positioning via MT end capture-shrinkage mechanism, requiring dynein anchorage to an ER- and mitochondria-independent population of Num1, dynein motor activity, and CAP-Gly domain of dynactin Nip100/p150Glued subunit.	cap	208-211	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	14-18
30084355-4	2018	Cells lacking Scs2/Scs22 performed spindle positioning via MT end capture-shrinkage mechanism, requiring dynein anchorage to an ER- and mitochondria-independent population of Num1, dynein motor activity, and CAP-Gly domain of dynactin Nip100/p150Glued subunit.	Glycine	212-215	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	14-18
8537323-0	1995	Cloning and sequence of the SCS2 gene, which can suppress the defect of INO1 expression in an inositol auxotrophic mutant of Saccharomyces cerevisiae.	Inositol	94-102	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	28-32
8537323-4	1995	Among them, one gene, designated as SCS2, also suppressed the choline-sensitive dominant mutation, CSE1 [Hosaka, K. et al.	Choline	62-69	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	36-40
28924045-0	2017	Interaction between repressor Opi1p and ER membrane protein Scs2p facilitates transit of phosphatidic acid from the ER to mitochondria and is essential for INO1 gene expression in the presence of choline.	Phosphatidic Acids	89-106	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	60-65
28924045-0	2017	Interaction between repressor Opi1p and ER membrane protein Scs2p facilitates transit of phosphatidic acid from the ER to mitochondria and is essential for INO1 gene expression in the presence of choline.	Choline	196-203	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	60-65
28924045-2	2017	Inositol depletion favors Opi1p interaction with both Scs2p and phosphatidic acid at the endoplasmic reticulum (ER) membrane.	Inositol	0-8	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	54-59
28924045-8	2017	Moreover, the mitochondria-specific phospholipid, cardiolipin, was significantly reduced in both strains compromised for Opi1p-Scs2p interaction, indicating that this interaction is required for the transfer of phosphatidic acid from the ER to the mitochondria for cardiolipin synthesis.	Phosphatidic Acids	211-228	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	127-132
28924045-3	2017	Inositol supplementation, however, favors the translocation of Opi1p from the ER into the nucleus, where it interacts with the Ino2p-Ino4p complex, attenuating transcription of INO1 A strain devoid of Scs2p (scs2Delta) and a mutant, OPI1FFAT, lacking the ability to interact with Scs2p were utilized to examine the specific role(s) of the Opi1p-Scs2p interaction in the regulation of INO1 expression and overall lipid metabolism.	Inositol	0-8	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	201-206
28924045-3	2017	Inositol supplementation, however, favors the translocation of Opi1p from the ER into the nucleus, where it interacts with the Ino2p-Ino4p complex, attenuating transcription of INO1 A strain devoid of Scs2p (scs2Delta) and a mutant, OPI1FFAT, lacking the ability to interact with Scs2p were utilized to examine the specific role(s) of the Opi1p-Scs2p interaction in the regulation of INO1 expression and overall lipid metabolism.	Inositol	0-8	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	280-285
28924045-3	2017	Inositol supplementation, however, favors the translocation of Opi1p from the ER into the nucleus, where it interacts with the Ino2p-Ino4p complex, attenuating transcription of INO1 A strain devoid of Scs2p (scs2Delta) and a mutant, OPI1FFAT, lacking the ability to interact with Scs2p were utilized to examine the specific role(s) of the Opi1p-Scs2p interaction in the regulation of INO1 expression and overall lipid metabolism.	Inositol	0-8	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	280-285
29127205-1	2017	Phosphatidic acid (PA) and the conserved integral ER membrane protein Scs2p regulate localization of the transcriptional repressor Opi1p, which controls expression of phospholipid biosynthesis genes, but the mechanisms conducting Opi1p localization are not fully understood.	Phospholipids	167-179	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	70-75
26590299-0	2016	Induction of intranuclear membranes by overproduction of Opi1p and Scs2p, regulators for yeast phospholipid biosynthesis, suggests a mechanism for Opi1p nuclear translocation.	Phospholipids	95-107	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	67-72
28924045-4	2017	Loss of the Opi1p-Scs2p interaction reduced INO1 expression and conferred inositol auxotrophy.	Inositol	74-82	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	18-23
28924045-7	2017	However, in strains lacking the Opi1p-Scs2p interaction, Opi1p remained in the nucleus, preventing expression of INO1 These data support the conclusion that a specific pool of phosphatidic acid, associated with lipid droplet formation in the perinuclear ER, is responsible for the initial rapid exit of Opi1p from the nucleus to the ER and is required for INO1 expression in the presence of choline.	Phosphatidic Acids	176-193	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	38-43
26590299-9	2016	We hypothesize that Opi1p dissociates from Scs2p after targeting to the nuclear membrane, making it possible to be released from the membrane quickly when PA levels decrease.	Phosphatidic Acids	155-157	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	43-48
21372176-3	2011	Cells grown in the absence of inositol sequester Scs2p-Opi1p at the ER and derepress target genes including INO1.	Inositol	30-38	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	49-54
21372176-2	2011	A major phospholipid regulatory circuit in yeast is controlled by Scs2p, an ER membrane protein that binds the transcriptional repressor protein Opi1p.	Phospholipids	8-20	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	66-71
25461533-4	2014	Opi1p and Scs2p are phospholipid sensor proteins and they repress the expression of phospholipid genes.	Phospholipids	20-32	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	10-15
25461533-4	2014	Opi1p and Scs2p are phospholipid sensor proteins and they repress the expression of phospholipid genes.	Phospholipids	84-96	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	10-15
22025676-0	2012	Desumoylation of the endoplasmic reticulum membrane VAP family protein Scs2 by Ulp1 and SUMO regulation of the inositol synthesis pathway.	Inositol	111-119	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	71-75
22025676-4	2012	The protein was identified as Scs2, an endoplasmic reticulum (ER) membrane protein that regulates phosphatidylinositol synthesis and lipid trafficking.	Phosphatidylinositols	98-118	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	30-34
22025676-5	2012	Mutation of lysine 180 of Scs2 abolishes its sumoylation.	Lysine	12-18	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	26-30
22025676-6	2012	Notably, impairment of either cellular sumoylation or cellular desumoylation mechanisms inhibits cell growth in the absence of inositol and exacerbates the inositol auxotrophy caused by deletion of SCS2.	Inositol	156-164	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	198-202
21372176-6	2011	Yet complex binding to Scs2p-Opi1p was enhanced by inositol starvation, although the interaction between Scs2p and Opi1p was not influenced by YET1 or YET3 deletion.	Inositol	51-59	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	23-28
17963691-0	2007	The yeast VAP homolog Scs2p has a phosphoinositide-binding ability that is correlated with its activity.	Phosphatidylinositols	34-50	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	22-27
18685198-0	2008	Disruption of the SCS2 ortholog in the alkane-assimilating yeast Yarrowia lipolytica impairs its growth on n-decane, but does not impair inositol prototrophy.	Alkanes	39-45	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	18-22
18685198-0	2008	Disruption of the SCS2 ortholog in the alkane-assimilating yeast Yarrowia lipolytica impairs its growth on n-decane, but does not impair inositol prototrophy.	decane	107-115	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	18-22
18685198-1	2008	Disruption of an SCS2 ortholog impaired the growth of the alkane-assimilating yeast Yarrowia lipolytica on n-alkanes, particularly on n-decane, although the mRNA level of the ALK1 gene encoding a highly inducible cytochrome P450ALK was not much affected.	Alkanes	58-64	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	17-21
18685198-1	2008	Disruption of an SCS2 ortholog impaired the growth of the alkane-assimilating yeast Yarrowia lipolytica on n-alkanes, particularly on n-decane, although the mRNA level of the ALK1 gene encoding a highly inducible cytochrome P450ALK was not much affected.	n-alkanes	107-116	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	17-21
18685198-1	2008	Disruption of an SCS2 ortholog impaired the growth of the alkane-assimilating yeast Yarrowia lipolytica on n-alkanes, particularly on n-decane, although the mRNA level of the ALK1 gene encoding a highly inducible cytochrome P450ALK was not much affected.	decane	134-142	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	17-21
21144830-0	2011	Human VAPA and the yeast VAP Scs2p with an altered proline distribution can phenocopy amyotrophic lateral sclerosis-associated VAPB(P56S).	Proline	51-58	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	29-34
21144830-5	2011	This suggests that the appropriate distribution of three conserved prolines, not the existence of a particular proline, confers VAPA and Scs2p resistance to the Pro-56 mutation and, therefore, is critical for VAP activities.	Proline	67-75	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	137-142
21144830-5	2011	This suggests that the appropriate distribution of three conserved prolines, not the existence of a particular proline, confers VAPA and Scs2p resistance to the Pro-56 mutation and, therefore, is critical for VAP activities.	Proline	67-74	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	137-142
21144830-5	2011	This suggests that the appropriate distribution of three conserved prolines, not the existence of a particular proline, confers VAPA and Scs2p resistance to the Pro-56 mutation and, therefore, is critical for VAP activities.	Proline	161-164	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	137-142
17963691-1	2007	The yeast VAMP-associated protein (VAP) homolog Scs2p is an endoplasmic reticulum (ER)/nuclear membrane protein that binds to an FFAT (diphenylalanine in an acidic tract) motif found in various lipid-metabolic proteins, including Opi1p, a negative regulator of phospholipid biosynthesis.	diphenylalanine	135-150	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	48-53
17963691-1	2007	The yeast VAMP-associated protein (VAP) homolog Scs2p is an endoplasmic reticulum (ER)/nuclear membrane protein that binds to an FFAT (diphenylalanine in an acidic tract) motif found in various lipid-metabolic proteins, including Opi1p, a negative regulator of phospholipid biosynthesis.	Phospholipids	261-273	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	48-53
17963691-2	2007	Here, we show that Scs2p is a novel phosphoinositide-binding protein that can bind to phosphatidylinositol monophosphates and bisphosphates in vitro.	phosphatidylinositol monophosphates	86-121	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	19-24
17963691-2	2007	Here, we show that Scs2p is a novel phosphoinositide-binding protein that can bind to phosphatidylinositol monophosphates and bisphosphates in vitro.	bisphosphates	126-139	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	19-24
17963691-4	2007	When several lysine residues in the MSP domain were substituted for alanine, the resulting mutant Scs2 proteins lost the phosphoinositide-binding ability and failed to complement the inositol auxotrophy of an scs2 deletion strain.	Lysine	13-19	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	98-102
17963691-4	2007	When several lysine residues in the MSP domain were substituted for alanine, the resulting mutant Scs2 proteins lost the phosphoinositide-binding ability and failed to complement the inositol auxotrophy of an scs2 deletion strain.	Alanine	68-75	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	98-102
17963691-4	2007	When several lysine residues in the MSP domain were substituted for alanine, the resulting mutant Scs2 proteins lost the phosphoinositide-binding ability and failed to complement the inositol auxotrophy of an scs2 deletion strain.	Phosphatidylinositols	121-137	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	98-102
17963691-4	2007	When several lysine residues in the MSP domain were substituted for alanine, the resulting mutant Scs2 proteins lost the phosphoinositide-binding ability and failed to complement the inositol auxotrophy of an scs2 deletion strain.	Inositol	183-191	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	98-102
17963691-6	2007	These results suggest the possibility that Scs2p activity is regulated by phosphoinositides to coordinate phospholipid biosynthesis in response to changes in phospholipid composition.	Phosphatidylinositols	74-91	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	43-48
17963691-6	2007	These results suggest the possibility that Scs2p activity is regulated by phosphoinositides to coordinate phospholipid biosynthesis in response to changes in phospholipid composition.	Phospholipids	106-118	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	43-48
17963691-6	2007	These results suggest the possibility that Scs2p activity is regulated by phosphoinositides to coordinate phospholipid biosynthesis in response to changes in phospholipid composition.	Phospholipids	158-170	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	43-48
9537365-0	1998	The Saccharomyces cerevisiae SCS2 gene product, a homolog of a synaptobrevin-associated protein, is an integral membrane protein of the endoplasmic reticulum and is required for inositol metabolism.	Inositol	178-186	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	29-33
15668246-3	2005	Here we have studied the FFAT-VAP interaction in Saccharomyces cerevisiae, where the VAP homologue Scs2 regulates phospholipid metabolism via an interaction with the FFAT motif of Opi1.	Phospholipids	114-126	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	99-103
12761300-0	2003	Role of the yeast VAP homolog, Scs2p, in INO1 expression and phospholipid metabolism.	Phospholipids	61-73	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	31-36
12761300-3	2003	SCS2 encodes a type II membrane protein and its deletion leads to inositol auxotrophy at temperatures above 34 degrees C. We found that the expression of the INO1 gene was reduced in the scs2Delta strain even when the cells were cultured under derepressing conditions for INO1 expression.	Inositol	66-74	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	0-4
15341762-1	2004	Opi1p, a transcription regulator of phospholipid metabolism in budding yeast, is retained in the endoplasmic reticulum by association with Scs2p.	Phospholipids	36-48	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	139-144
12761300-6	2003	These results indicate that Scs2p can contribute to coordinated phospholipid metabolism including INO1 expression by regulating phosphatidylcholine synthesis through the CDP-choline pathway.	Phospholipids	64-76	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	28-33
12761300-6	2003	These results indicate that Scs2p can contribute to coordinated phospholipid metabolism including INO1 expression by regulating phosphatidylcholine synthesis through the CDP-choline pathway.	Phosphatidylcholines	128-147	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	28-33
12761300-6	2003	These results indicate that Scs2p can contribute to coordinated phospholipid metabolism including INO1 expression by regulating phosphatidylcholine synthesis through the CDP-choline pathway.	Cytidine Diphosphate	170-173	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	28-33
12761300-6	2003	These results indicate that Scs2p can contribute to coordinated phospholipid metabolism including INO1 expression by regulating phosphatidylcholine synthesis through the CDP-choline pathway.	Choline	140-147	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	28-33
12399377-3	2002	Elevated dosage of SCS2, previously implicated as a regulator of both inositol biosynthesis and telomeric silencing, suppressed the dominant-negative effect of a SIR2-143 mutation.	Inositol	70-78	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	19-23
11333225-0	2001	The Saccharomyces cerevisiae suppressor of choline sensitivity (SCS2) gene is a multicopy Suppressor of mec1 telomeric silencing defects.	Choline	43-50	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	64-68
11333225-4	2001	We identified SCS2 (suppressor of choline sensitivity), a gene previously isolated as a suppressor of defects in inositol synthesis.	Choline	34-41	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	14-18
11333225-4	2001	We identified SCS2 (suppressor of choline sensitivity), a gene previously isolated as a suppressor of defects in inositol synthesis.	Inositol	113-121	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	14-18
9537365-1	1998	The Saccharomyces cerevisiae SCS2 gene has been cloned as a suppressor of inositol auxotrophy of CSE1 and hac1/ire15 mutants (J. Nikawa, A. Murakami, E. Esumi, and K. Hosaka, J. Biochem.	Inositol	74-82	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	29-33
9537365-5	1998	The disruption of the SCS2 gene causes yeast cells to exhibit inositol auxotrophy at temperatures of above 34 degrees C. Genetic studies reveal that the overexpression of the INO1 gene rescues the inositol auxotrophy of the SCS2 disruption strain.	Inositol	62-70	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	22-26
9537365-5	1998	The disruption of the SCS2 gene causes yeast cells to exhibit inositol auxotrophy at temperatures of above 34 degrees C. Genetic studies reveal that the overexpression of the INO1 gene rescues the inositol auxotrophy of the SCS2 disruption strain.	Inositol	197-205	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	22-26
9537365-5	1998	The disruption of the SCS2 gene causes yeast cells to exhibit inositol auxotrophy at temperatures of above 34 degrees C. Genetic studies reveal that the overexpression of the INO1 gene rescues the inositol auxotrophy of the SCS2 disruption strain.	Inositol	197-205	phosphatidylinositol-binding protein SCS2	Saccharomyces cerevisiae S288C	224-228