PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
10509015-1	1999	The HOM3 gene of Saccharomyces cerevisiae encodes aspartate kinase, which catalyses the first step in the branched pathway leading to the synthesis of threonine and methionine from aspartate.	Threonine	151-160	aspartate kinase	Saccharomyces cerevisiae S288C	4-8
15927871-5	2005	Sn2+ -induced reversion of the yeast his1-798, his1-208 and lys1-1 mutant alleles, in diploid and haploid cells, respectively, and putative frameshift mutagenesis (reversion of the hom3-10 allele) was observed.	Tin(2+)	0-4	aspartate kinase	Saccharomyces cerevisiae S288C	181-188
15358146-0	2004	Characterization of the aspartate kinase from Saccharomyces cerevisiae and of its interaction with threonine.	Threonine	99-108	aspartate kinase	Saccharomyces cerevisiae S288C	24-40
15358146-1	2004	Aspartate kinase (AK) from Saccharomyces cerevisiae has been characterized to elucidate its quaternary structure and the effect of the allosteric inhibitor threonine on the enzyme conformation.	Threonine	156-165	aspartate kinase	Saccharomyces cerevisiae S288C	0-16
15358146-1	2004	Aspartate kinase (AK) from Saccharomyces cerevisiae has been characterized to elucidate its quaternary structure and the effect of the allosteric inhibitor threonine on the enzyme conformation.	Threonine	156-165	aspartate kinase	Saccharomyces cerevisiae S288C	18-20
15358146-4	2004	Threonine caused a decrease in the apparent molecular mass of AK as evidenced by size-exclusion chromatography (from 345 to 280 kDa) and blue native gel electrophoresis (from 346 to 297 kDa); no other molecular species were detected.	Threonine	0-9	aspartate kinase	Saccharomyces cerevisiae S288C	62-64
15358146-7	2004	These results indicate that the allosteric transition elicited by binding of threonine to yeast AK involves a large conformational change of the protein that isomerizes from a relaxed active conformation to a more compact inactive one of smaller molecular dimensions.	Threonine	77-86	aspartate kinase	Saccharomyces cerevisiae S288C	96-98
12602885-6	2003	Correspondingly, cDNA expression in an AK-deficient hom3 yeast mutant resulted in threonine and methionine prototrophy and a threonine-sensitive AK activity was observed in cell-free extracts.	Threonine	82-91	aspartate kinase	Saccharomyces cerevisiae S288C	52-56
12602885-6	2003	Correspondingly, cDNA expression in an AK-deficient hom3 yeast mutant resulted in threonine and methionine prototrophy and a threonine-sensitive AK activity was observed in cell-free extracts.	Methionine	96-106	aspartate kinase	Saccharomyces cerevisiae S288C	52-56
12602885-6	2003	Correspondingly, cDNA expression in an AK-deficient hom3 yeast mutant resulted in threonine and methionine prototrophy and a threonine-sensitive AK activity was observed in cell-free extracts.	Threonine	125-134	aspartate kinase	Saccharomyces cerevisiae S288C	52-56
15645479-1	2005	In Saccharomyces cerevisiae, aspartate kinase (the HOM3 product) regulates the metabolic flux through the threonine biosynthetic pathway through feedback inhibition by the end product.	Threonine	106-115	aspartate kinase	Saccharomyces cerevisiae S288C	51-55
15645479-2	2005	In order to obtain a strain able to produce threonine in a controlled way, we have isolated a mutant allele (HOM3-ts31d) that gives rise to a deregulated aspartate kinase.	Threonine	44-53	aspartate kinase	Saccharomyces cerevisiae S288C	109-113
15645479-4	2005	The HOM3-ts31d allele carries a mutation that leads to a Ser399 --> Phe substitution in the postulated regulatory region of the enzyme.	Phenylalanine	71-74	aspartate kinase	Saccharomyces cerevisiae S288C	4-8
10862883-4	2000	The results show that the amplification of the clustered genes affects threonine and homoserine accumulation only when it includes the HOM3 gene, or when combined with a HOM3-R2 mutation.	Threonine	71-80	aspartate kinase	Saccharomyces cerevisiae S288C	135-139
10862883-4	2000	The results show that the amplification of the clustered genes affects threonine and homoserine accumulation only when it includes the HOM3 gene, or when combined with a HOM3-R2 mutation.	Threonine	71-80	aspartate kinase	Saccharomyces cerevisiae S288C	170-174
10862883-4	2000	The results show that the amplification of the clustered genes affects threonine and homoserine accumulation only when it includes the HOM3 gene, or when combined with a HOM3-R2 mutation.	Homoserine	85-95	aspartate kinase	Saccharomyces cerevisiae S288C	135-139
10862883-4	2000	The results show that the amplification of the clustered genes affects threonine and homoserine accumulation only when it includes the HOM3 gene, or when combined with a HOM3-R2 mutation.	Homoserine	85-95	aspartate kinase	Saccharomyces cerevisiae S288C	170-174
10509015-1	1999	The HOM3 gene of Saccharomyces cerevisiae encodes aspartate kinase, which catalyses the first step in the branched pathway leading to the synthesis of threonine and methionine from aspartate.	Methionine	165-175	aspartate kinase	Saccharomyces cerevisiae S288C	4-8
10509015-1	1999	The HOM3 gene of Saccharomyces cerevisiae encodes aspartate kinase, which catalyses the first step in the branched pathway leading to the synthesis of threonine and methionine from aspartate.	Aspartic Acid	50-59	aspartate kinase	Saccharomyces cerevisiae S288C	4-8
10509015-3	1999	We have isolated and characterized three HOM3 mutants that show growth inhibition by threonine due to a severe, threonine-induced reduction of the carbon flow into the aspartate pathway, leading to methionine limitation.	Threonine	85-94	aspartate kinase	Saccharomyces cerevisiae S288C	41-45
10509015-3	1999	We have isolated and characterized three HOM3 mutants that show growth inhibition by threonine due to a severe, threonine-induced reduction of the carbon flow into the aspartate pathway, leading to methionine limitation.	Threonine	112-121	aspartate kinase	Saccharomyces cerevisiae S288C	41-45
10509015-3	1999	We have isolated and characterized three HOM3 mutants that show growth inhibition by threonine due to a severe, threonine-induced reduction of the carbon flow into the aspartate pathway, leading to methionine limitation.	Carbon	147-153	aspartate kinase	Saccharomyces cerevisiae S288C	41-45
10509015-3	1999	We have isolated and characterized three HOM3 mutants that show growth inhibition by threonine due to a severe, threonine-induced reduction of the carbon flow into the aspartate pathway, leading to methionine limitation.	Aspartic Acid	168-177	aspartate kinase	Saccharomyces cerevisiae S288C	41-45
10509015-3	1999	We have isolated and characterized three HOM3 mutants that show growth inhibition by threonine due to a severe, threonine-induced reduction of the carbon flow into the aspartate pathway, leading to methionine limitation.	Methionine	198-208	aspartate kinase	Saccharomyces cerevisiae S288C	41-45
10509015-9	1999	Mutagenesis of a HOM3 region centred in the KFGG-coding triplets generated alleles that determine threonine sensitivity or auxotrophy for threonine and methionine, but not a phenotype associated with a feedback-resistant aspartate kinase, indicating that this region is not involved in the allosteric response of the enzyme.	Threonine	98-107	aspartate kinase	Saccharomyces cerevisiae S288C	17-21
10509015-9	1999	Mutagenesis of a HOM3 region centred in the KFGG-coding triplets generated alleles that determine threonine sensitivity or auxotrophy for threonine and methionine, but not a phenotype associated with a feedback-resistant aspartate kinase, indicating that this region is not involved in the allosteric response of the enzyme.	Threonine	138-147	aspartate kinase	Saccharomyces cerevisiae S288C	17-21
10509015-9	1999	Mutagenesis of a HOM3 region centred in the KFGG-coding triplets generated alleles that determine threonine sensitivity or auxotrophy for threonine and methionine, but not a phenotype associated with a feedback-resistant aspartate kinase, indicating that this region is not involved in the allosteric response of the enzyme.	Methionine	152-162	aspartate kinase	Saccharomyces cerevisiae S288C	17-21
9870705-6	1998	Furthermore we compared sequence spectra of reversions of the +1 hom3-10 frameshift allele and found a strong preference for -1 deletions in mononucleotide repeats in selection-induced and replication-dependent revertants, indicating slippage errors during DNA repair synthesis as well as during DNA replication.	mononucleotide	141-155	aspartate kinase	Saccharomyces cerevisiae S288C	65-69
9872767-0	1999	Threonine overproduction in yeast strains carrying the HOM3-R2 mutant allele under the control of different inducible promoters.	Threonine	0-9	aspartate kinase	Saccharomyces cerevisiae S288C	55-59
9872767-1	1999	The HOM3 gene of Saccharomyces cerevisiae codes for aspartate kinase, which plays a crucial role in the regulation of the metabolic flux that leads to threonine biosynthesis.	Threonine	151-160	aspartate kinase	Saccharomyces cerevisiae S288C	4-8
9872767-2	1999	With the aim of obtaining yeast strains able to overproduce threonine in a controlled way, we have placed the HOM3-R2 mutant allele, which causes expression of a feedback-insensitive enzyme, under the control of four distinctive regulatable yeast promoters, namely, PGAL1, PCHA1, PCYC1-HSE2, and PGPH1.	Threonine	60-69	aspartate kinase	Saccharomyces cerevisiae S288C	110-114
28335772-10	2017	Removing feedback inhibition of aspartate kinase HOM3, an enzyme involved in threonine biosynthesis in yeast, elevated (S)-2-aminobutyric acid biosynthesis to above 0.49 mg/L in cultures not receiving additional L-threonine.	Threonine	77-86	aspartate kinase	Saccharomyces cerevisiae S288C	49-53
1622238-4	1992	Genetic and biochemical studies have revealed that the threonine overproduction is, in all cases studied, associated with the presence in the strain of a HOM3 allele coding for a mutant aspartate kinase that is totally or partially insensitive to feedback inhibition by threonine.	Threonine	55-64	aspartate kinase	Saccharomyces cerevisiae S288C	154-158
1622238-4	1992	Genetic and biochemical studies have revealed that the threonine overproduction is, in all cases studied, associated with the presence in the strain of a HOM3 allele coding for a mutant aspartate kinase that is totally or partially insensitive to feedback inhibition by threonine.	Threonine	270-279	aspartate kinase	Saccharomyces cerevisiae S288C	154-158
1789001-2	1991	Four major responses were evident: strong repression by methionine of MET3, MET5 and MET14, as previously described for MET3, MET2 and MET25; weak repression by methionine of MET6; weak stimulation by methionine but no response to threonine was seen for THR1, HOM2 and HOM3; no response to any of the signals tested, for HOM6 and MES1.	Methionine	56-66	aspartate kinase	Saccharomyces cerevisiae S288C	269-273
1789001-4	1991	The stimulation of transcription by methionine for HOM2, HOM3 and THR1 is mediated by the GCN4 gene product and hence these genes are under the general amino acid control.	Methionine	36-46	aspartate kinase	Saccharomyces cerevisiae S288C	57-61
34849833-5	2021	One mutant, designated gal four throttle 1 (gft1) was identified as a recessive allele of hom3, encoding aspartokinase, and mutations in hom3 caused effects typical of inhibition of TORC1, including rapamycin sensitivity and enhanced nuclear localization of the TORC1-responsive transcription factor Gat1.	Sirolimus	199-208	aspartate kinase	Saccharomyces cerevisiae S288C	137-141
2892836-3	1988	Mutations in HOM3 result in a requirement for threonine and methionine (or homoserine) for growth and a lack of detectable aspartokinase activity.	Threonine	46-55	aspartate kinase	Saccharomyces cerevisiae S288C	13-17
2892836-3	1988	Mutations in HOM3 result in a requirement for threonine and methionine (or homoserine) for growth and a lack of detectable aspartokinase activity.	Methionine	60-70	aspartate kinase	Saccharomyces cerevisiae S288C	13-17
2892836-3	1988	Mutations in HOM3 result in a requirement for threonine and methionine (or homoserine) for growth and a lack of detectable aspartokinase activity.	Homoserine	75-85	aspartate kinase	Saccharomyces cerevisiae S288C	13-17
6821505-1	1982	Three threonine-overproducing mutants were obtained as prototrophic revertants of a hom3 mutant strain of Saccharomyces cerevisiae.	Threonine	6-15	aspartate kinase	Saccharomyces cerevisiae S288C	84-88
6821505-2	1982	The gene HOM3 codes for aspartokinase (aspartate kinase; EC 2.7.2.4), the first enzyme of the threonine-methionine biosynthetic route, which is subjected to feedback inhibition by threonine.	Threonine	94-103	aspartate kinase	Saccharomyces cerevisiae S288C	9-13
6821505-2	1982	The gene HOM3 codes for aspartokinase (aspartate kinase; EC 2.7.2.4), the first enzyme of the threonine-methionine biosynthetic route, which is subjected to feedback inhibition by threonine.	Methionine	104-114	aspartate kinase	Saccharomyces cerevisiae S288C	9-13
6821505-2	1982	The gene HOM3 codes for aspartokinase (aspartate kinase; EC 2.7.2.4), the first enzyme of the threonine-methionine biosynthetic route, which is subjected to feedback inhibition by threonine.	Threonine	180-189	aspartate kinase	Saccharomyces cerevisiae S288C	9-13
30003101-6	2018	In fact, deleting HOM3 in the first step, preventing the pathway to reach the HOM6 step, rescues the sensitivity of the hom6 strain to doxorubicin.	Doxorubicin	135-146	aspartate kinase	Saccharomyces cerevisiae S288C	18-22
18626862-3	1996	The results show that only the amplification of the HOM3 alleles leads to threonine and, in some instances, to homoserine overproduction.	Threonine	74-83	aspartate kinase	Saccharomyces cerevisiae S288C	52-56
18626862-3	1996	The results show that only the amplification of the HOM3 alleles leads to threonine and, in some instances, to homoserine overproduction.	Homoserine	111-121	aspartate kinase	Saccharomyces cerevisiae S288C	52-56
785224-3	1976	In the first group borrelidin resistance is coupled to the gene HOM3 coding for aspartokinase, in the second group to the gene LEU1.	borrelidin	19-29	aspartate kinase	Saccharomyces cerevisiae S288C	64-68
28335772-10	2017	Removing feedback inhibition of aspartate kinase HOM3, an enzyme involved in threonine biosynthesis in yeast, elevated (S)-2-aminobutyric acid biosynthesis to above 0.49 mg/L in cultures not receiving additional L-threonine.	Threonine	212-223	aspartate kinase	Saccharomyces cerevisiae S288C	49-53
28335772-10	2017	Removing feedback inhibition of aspartate kinase HOM3, an enzyme involved in threonine biosynthesis in yeast, elevated (S)-2-aminobutyric acid biosynthesis to above 0.49 mg/L in cultures not receiving additional L-threonine.	alpha-aminobutyric acid	119-142	aspartate kinase	Saccharomyces cerevisiae S288C	49-53
22615397-5	2012	Our method successfully identified specific disruption of the Hom3:Fpr1 interaction by the immunosuppressant FK506, illustrating the assay"s capacity to identify chemical inhibitors of protein-protein interactions.	Tacrolimus	109-114	aspartate kinase	Saccharomyces cerevisiae S288C	62-66
21279647-8	2011	A dominant-negative version of DPBF4 fused to the SRDX repressor domain of SUPERMAN could counteract the repression and stimulate AK expression under low sugar and darkness in planta.	Sugars	154-159	aspartate kinase	Saccharomyces cerevisiae S288C	130-132
21279647-1	2011	Initial steps of aspartate-derived biosynthesis pathway (Asp pathway) producing Lys, Thr, Met and Ile are catalyzed by bifunctional (AK/HSD) and monofunctional (AK-lys) aspartate kinase (AK) enzymes.	Aspartic Acid	17-26	aspartate kinase	Saccharomyces cerevisiae S288C	133-135
20305003-6	2010	In both species, serum sensitivity was suppressed by the addition of threonine, a feedback inhibitor of Hom3p.	Threonine	69-78	aspartate kinase	Saccharomyces cerevisiae S288C	104-109
21279647-1	2011	Initial steps of aspartate-derived biosynthesis pathway (Asp pathway) producing Lys, Thr, Met and Ile are catalyzed by bifunctional (AK/HSD) and monofunctional (AK-lys) aspartate kinase (AK) enzymes.	Aspartic Acid	17-26	aspartate kinase	Saccharomyces cerevisiae S288C	161-163
21279647-1	2011	Initial steps of aspartate-derived biosynthesis pathway (Asp pathway) producing Lys, Thr, Met and Ile are catalyzed by bifunctional (AK/HSD) and monofunctional (AK-lys) aspartate kinase (AK) enzymes.	Aspartic Acid	17-26	aspartate kinase	Saccharomyces cerevisiae S288C	169-185
21279647-1	2011	Initial steps of aspartate-derived biosynthesis pathway (Asp pathway) producing Lys, Thr, Met and Ile are catalyzed by bifunctional (AK/HSD) and monofunctional (AK-lys) aspartate kinase (AK) enzymes.	Aspartic Acid	17-26	aspartate kinase	Saccharomyces cerevisiae S288C	161-163
21279647-1	2011	Initial steps of aspartate-derived biosynthesis pathway (Asp pathway) producing Lys, Thr, Met and Ile are catalyzed by bifunctional (AK/HSD) and monofunctional (AK-lys) aspartate kinase (AK) enzymes.	Aspartic Acid	57-60	aspartate kinase	Saccharomyces cerevisiae S288C	133-135
21279647-1	2011	Initial steps of aspartate-derived biosynthesis pathway (Asp pathway) producing Lys, Thr, Met and Ile are catalyzed by bifunctional (AK/HSD) and monofunctional (AK-lys) aspartate kinase (AK) enzymes.	Aspartic Acid	57-60	aspartate kinase	Saccharomyces cerevisiae S288C	161-163
21279647-1	2011	Initial steps of aspartate-derived biosynthesis pathway (Asp pathway) producing Lys, Thr, Met and Ile are catalyzed by bifunctional (AK/HSD) and monofunctional (AK-lys) aspartate kinase (AK) enzymes.	Aspartic Acid	57-60	aspartate kinase	Saccharomyces cerevisiae S288C	169-185
21279647-1	2011	Initial steps of aspartate-derived biosynthesis pathway (Asp pathway) producing Lys, Thr, Met and Ile are catalyzed by bifunctional (AK/HSD) and monofunctional (AK-lys) aspartate kinase (AK) enzymes.	Aspartic Acid	57-60	aspartate kinase	Saccharomyces cerevisiae S288C	161-163
21279647-1	2011	Initial steps of aspartate-derived biosynthesis pathway (Asp pathway) producing Lys, Thr, Met and Ile are catalyzed by bifunctional (AK/HSD) and monofunctional (AK-lys) aspartate kinase (AK) enzymes.	Lysine	80-83	aspartate kinase	Saccharomyces cerevisiae S288C	133-135
21279647-1	2011	Initial steps of aspartate-derived biosynthesis pathway (Asp pathway) producing Lys, Thr, Met and Ile are catalyzed by bifunctional (AK/HSD) and monofunctional (AK-lys) aspartate kinase (AK) enzymes.	Lysine	80-83	aspartate kinase	Saccharomyces cerevisiae S288C	161-163
21279647-1	2011	Initial steps of aspartate-derived biosynthesis pathway (Asp pathway) producing Lys, Thr, Met and Ile are catalyzed by bifunctional (AK/HSD) and monofunctional (AK-lys) aspartate kinase (AK) enzymes.	Lysine	80-83	aspartate kinase	Saccharomyces cerevisiae S288C	169-185
21279647-1	2011	Initial steps of aspartate-derived biosynthesis pathway (Asp pathway) producing Lys, Thr, Met and Ile are catalyzed by bifunctional (AK/HSD) and monofunctional (AK-lys) aspartate kinase (AK) enzymes.	Lysine	80-83	aspartate kinase	Saccharomyces cerevisiae S288C	161-163
21279647-1	2011	Initial steps of aspartate-derived biosynthesis pathway (Asp pathway) producing Lys, Thr, Met and Ile are catalyzed by bifunctional (AK/HSD) and monofunctional (AK-lys) aspartate kinase (AK) enzymes.	Threonine	85-88	aspartate kinase	Saccharomyces cerevisiae S288C	133-135
21279647-1	2011	Initial steps of aspartate-derived biosynthesis pathway (Asp pathway) producing Lys, Thr, Met and Ile are catalyzed by bifunctional (AK/HSD) and monofunctional (AK-lys) aspartate kinase (AK) enzymes.	Threonine	85-88	aspartate kinase	Saccharomyces cerevisiae S288C	161-163
21279647-1	2011	Initial steps of aspartate-derived biosynthesis pathway (Asp pathway) producing Lys, Thr, Met and Ile are catalyzed by bifunctional (AK/HSD) and monofunctional (AK-lys) aspartate kinase (AK) enzymes.	Threonine	85-88	aspartate kinase	Saccharomyces cerevisiae S288C	169-185
21279647-1	2011	Initial steps of aspartate-derived biosynthesis pathway (Asp pathway) producing Lys, Thr, Met and Ile are catalyzed by bifunctional (AK/HSD) and monofunctional (AK-lys) aspartate kinase (AK) enzymes.	Threonine	85-88	aspartate kinase	Saccharomyces cerevisiae S288C	161-163
21279647-1	2011	Initial steps of aspartate-derived biosynthesis pathway (Asp pathway) producing Lys, Thr, Met and Ile are catalyzed by bifunctional (AK/HSD) and monofunctional (AK-lys) aspartate kinase (AK) enzymes.	Isoleucine	98-101	aspartate kinase	Saccharomyces cerevisiae S288C	133-135
21279647-1	2011	Initial steps of aspartate-derived biosynthesis pathway (Asp pathway) producing Lys, Thr, Met and Ile are catalyzed by bifunctional (AK/HSD) and monofunctional (AK-lys) aspartate kinase (AK) enzymes.	Isoleucine	98-101	aspartate kinase	Saccharomyces cerevisiae S288C	161-163
21279647-1	2011	Initial steps of aspartate-derived biosynthesis pathway (Asp pathway) producing Lys, Thr, Met and Ile are catalyzed by bifunctional (AK/HSD) and monofunctional (AK-lys) aspartate kinase (AK) enzymes.	Isoleucine	98-101	aspartate kinase	Saccharomyces cerevisiae S288C	169-185
21279647-1	2011	Initial steps of aspartate-derived biosynthesis pathway (Asp pathway) producing Lys, Thr, Met and Ile are catalyzed by bifunctional (AK/HSD) and monofunctional (AK-lys) aspartate kinase (AK) enzymes.	Isoleucine	98-101	aspartate kinase	Saccharomyces cerevisiae S288C	161-163
21279647-2	2011	Here, we show that transcription of all AK genes is negatively regulated under darkness and low sugar conditions.	Sugars	96-101	aspartate kinase	Saccharomyces cerevisiae S288C	40-42
21279647-4	2011	Elevated transcript levels of DPBF4 and ABI5 under darkness and low sugar conditions coincide with the repression of AK gene expression.	Sugars	68-73	aspartate kinase	Saccharomyces cerevisiae S288C	117-119
20305003-7	2010	Because mutation of the HOM3 and HOM6 genes, required for the production of the toxic pathway intermediate homoserine, also suppressed serum sensitivity, we hypothesize that serum sensitivity is a consequence of homoserine accumulation.	Homoserine	107-117	aspartate kinase	Saccharomyces cerevisiae S288C	24-28
20305003-7	2010	Because mutation of the HOM3 and HOM6 genes, required for the production of the toxic pathway intermediate homoserine, also suppressed serum sensitivity, we hypothesize that serum sensitivity is a consequence of homoserine accumulation.	Homoserine	212-222	aspartate kinase	Saccharomyces cerevisiae S288C	24-28
17606896-2	2007	This analysis in Saccharomyces cerevisiae revealed genetic modules involved in tricarboxylic acid cycle regulation (RTG1, RTG2, RTG3), threonine biosynthesis (HOM3, HOM2, HOM6, THR1, THR4), amino acid permease trafficking (LST4, LST7), and threonine catabolism (GLY1).	Tricarboxylic Acids	79-97	aspartate kinase	Saccharomyces cerevisiae S288C	159-163