PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
18953022-3	2009	In this report, we demonstrate that in Saccharomyces cerevisiae the transcription of COX15 is regulated by Hap1, a transcription factor whose activity is positively controlled by intracellular heme concentration.	Heme	193-197	Hap1p	Saccharomyces cerevisiae S288C	107-111
19175415-4	2009	The gene expressions of both the important transcription factors Hap1 and Rox1, involved in oxygen sensing, were mainly increased in the first 3 h, while YAP1 expression, which is involved in the oxidative stress response, increased drastically only in the first 45 min.	Oxygen	92-98	Hap1p	Saccharomyces cerevisiae S288C	65-69
15654089-0	2005	The heme activator protein Hap1 represses transcription by a heme-independent mechanism in Saccharomyces cerevisiae.	Heme	4-8	Hap1p	Saccharomyces cerevisiae S288C	27-31
19519523-0	2009	A unique mechanism of chaperone action: heme regulation of Hap1 activity involves separate control of repression and activation.	Heme	40-44	Hap1p	Saccharomyces cerevisiae S288C	59-63
19519523-3	2009	The yeast heme activator protein Hap1 promotes transcription of many genes in response to heme.	Heme	10-14	Hap1p	Saccharomyces cerevisiae S288C	33-37
19519523-5	2009	The mechanism by which molecular chaperones promote heme regulation of Hap1 activity is distinct from the mechanism by which molecular chaperones promote steroid signaling.	Heme	52-56	Hap1p	Saccharomyces cerevisiae S288C	71-75
19519523-6	2009	Hsp70 and Hsp90 molecular chaperones act separately to promote Hap1 repression in heme-deficient cells and heme activation of Hap1 in heme-sufficient cells.	Heme	82-86	Hap1p	Saccharomyces cerevisiae S288C	63-67
19519523-6	2009	Hsp70 and Hsp90 molecular chaperones act separately to promote Hap1 repression in heme-deficient cells and heme activation of Hap1 in heme-sufficient cells.	Heme	107-111	Hap1p	Saccharomyces cerevisiae S288C	126-130
19519523-6	2009	Hsp70 and Hsp90 molecular chaperones act separately to promote Hap1 repression in heme-deficient cells and heme activation of Hap1 in heme-sufficient cells.	Heme	107-111	Hap1p	Saccharomyces cerevisiae S288C	126-130
19519523-7	2009	Likewise, distinct Hap1 elements or domains act to mediate Hap1 repression and heme activation separately.	Heme	79-83	Hap1p	Saccharomyces cerevisiae S288C	19-23
19519523-8	2009	In this review, we summarize the current knowledge about the molecular mechanism governing heme regulation of Hap1 activity, and we compare this mechanism to the molecular mechanism by which Hsp90 and Hsp70 molecular chaperones promote the regulation of glucocorticoid receptor, the most extensively studied substrate of Hsp90 and Hsp70 molecular chaperones.	Heme	91-95	Hap1p	Saccharomyces cerevisiae S288C	110-114
19008939-6	2008	We used a new machine learning algorithm called MEDUSA to uncover detailed information about the oxygen regulatory network using genome-wide expression changes in response to perturbations in the levels of oxygen, heme, Hap1, and Co2+.	Oxygen	97-103	Hap1p	Saccharomyces cerevisiae S288C	220-224
19008939-9	2008	This network includes both known oxygen and heme regulators, such as Hap1, Mga2, Hap4, and Upc2, as well as many new candidate regulators.	Oxygen	33-39	Hap1p	Saccharomyces cerevisiae S288C	69-73
17785431-0	2007	Heme levels switch the function of Hap1 of Saccharomyces cerevisiae between transcriptional activator and transcriptional repressor.	Heme	0-4	Hap1p	Saccharomyces cerevisiae S288C	35-39
17785431-4	2007	The repressive activity of Hap1 controls several genes, including three ERG genes required for ergosterol biosynthesis.	Ergosterol	95-105	Hap1p	Saccharomyces cerevisiae S288C	27-31
17785431-7	2007	The switch of Hap1 from acting as a hypoxic repressor to an aerobic activator is determined by heme, which is synthesized only in the presence of oxygen.	Heme	95-99	Hap1p	Saccharomyces cerevisiae S288C	14-18
17785431-7	2007	The switch of Hap1 from acting as a hypoxic repressor to an aerobic activator is determined by heme, which is synthesized only in the presence of oxygen.	Oxygen	146-152	Hap1p	Saccharomyces cerevisiae S288C	14-18
16963631-6	2006	Our analyses revealed extensive networks of genes subject to combinatorial regulation by both heme-dependent (e.g., Hap1, Hap2/3/4/5, Rox1, Mot3, and Upc2) and heme-independent (e.g., Yap1, Skn7, and Puf3) factors under these conditions.	Heme	94-98	Hap1p	Saccharomyces cerevisiae S288C	116-120
16963631-6	2006	Our analyses revealed extensive networks of genes subject to combinatorial regulation by both heme-dependent (e.g., Hap1, Hap2/3/4/5, Rox1, Mot3, and Upc2) and heme-independent (e.g., Yap1, Skn7, and Puf3) factors under these conditions.	Heme	160-164	Hap1p	Saccharomyces cerevisiae S288C	116-120
18806211-0	2008	Oxygen-dependent transcriptional regulator Hap1p limits glucose uptake by repressing the expression of the major glucose transporter gene RAG1 in Kluyveromyces lactis.	Oxygen	0-6	Hap1p	Saccharomyces cerevisiae S288C	43-48
18806211-0	2008	Oxygen-dependent transcriptional regulator Hap1p limits glucose uptake by repressing the expression of the major glucose transporter gene RAG1 in Kluyveromyces lactis.	Glucose	56-63	Hap1p	Saccharomyces cerevisiae S288C	43-48
18806211-1	2008	The HAP1 (CYP1) gene product of Saccharomyces cerevisiae is known to regulate the transcription of many genes in response to oxygen availability.	Oxygen	125-131	Hap1p	Saccharomyces cerevisiae S288C	4-8
18806211-1	2008	The HAP1 (CYP1) gene product of Saccharomyces cerevisiae is known to regulate the transcription of many genes in response to oxygen availability.	Oxygen	125-131	Hap1p	Saccharomyces cerevisiae S288C	10-14
18806211-3	2008	It is suspected that a difference in the interaction of Hap1p with its target genes may explain some of the species-related variation in oxygen responses.	Oxygen	137-143	Hap1p	Saccharomyces cerevisiae S288C	56-61
15870279-5	2005	By approximately 0.2 generation of anaerobiosis in both media, more chronic, heme-dependent effects were observed, including the down-regulation of Hap1-regulated networks, derepression of Rox1-regulated networks, and activation of Upc2-regulated ones.	Heme	77-81	Hap1p	Saccharomyces cerevisiae S288C	148-152
15654089-1	2005	The yeast heme activator protein Hap1 binds to DNA and activates transcription of genes encoding functions required for respiration and for controlling oxidative damage, in response to heme.	Heme	10-14	Hap1p	Saccharomyces cerevisiae S288C	33-37
15654089-3	2005	The regulation of Hap1 transcription-activating activity is controlled by two classes of Hap1 elements, repression modules (RPM1-3) and heme-responsive motifs (HRM1-7).	Heme	136-140	Hap1p	Saccharomyces cerevisiae S288C	18-22
15654089-9	2005	These results show that Hap1 binds to its own promoter and represses transcription in a heme-independent but Hsp70-dependent manner.	Heme	88-92	Hap1p	Saccharomyces cerevisiae S288C	24-28
12614847-5	2003	As an intracellular oxygen sensor, heme stimulated TSA2 transcription by activating Hap1p.	Oxygen	20-26	Hap1p	Saccharomyces cerevisiae S288C	84-89
16233684-0	2004	A hap1 mutation in a laboratory strain of Saccharomyces cerevisiae results in decreased expression of ergosterol-related genes and cellular ergosterol content compared to sake yeast.	Ergosterol	102-112	Hap1p	Saccharomyces cerevisiae S288C	2-6
16233684-0	2004	A hap1 mutation in a laboratory strain of Saccharomyces cerevisiae results in decreased expression of ergosterol-related genes and cellular ergosterol content compared to sake yeast.	Ergosterol	140-150	Hap1p	Saccharomyces cerevisiae S288C	2-6
16233684-6	2004	These results suggest that the differences in the expression levels of ergosterol-related genes and ergosterol content between strains K7 and X2180 were largely caused by the hap1 mutation in strain X2180.	Ergosterol	71-81	Hap1p	Saccharomyces cerevisiae S288C	175-179
16233684-6	2004	These results suggest that the differences in the expression levels of ergosterol-related genes and ergosterol content between strains K7 and X2180 were largely caused by the hap1 mutation in strain X2180.	Ergosterol	100-110	Hap1p	Saccharomyces cerevisiae S288C	175-179
14530431-5	2003	Repressor synthesis is triggered by heme, which de-represses a mechanism controlling expression of both MOT3 and ROX1 in anaerobic cells; it includes Hap1, Tup1, Ssn6 and a fourth unidentified factor.	Heme	36-40	Hap1p	Saccharomyces cerevisiae S288C	150-154
15102838-0	2004	A novel mode of chaperone action: heme activation of Hap1 by enhanced association of Hsp90 with the repressed Hsp70-Hap1 complex.	Heme	34-38	Hap1p	Saccharomyces cerevisiae S288C	53-57
15102838-0	2004	A novel mode of chaperone action: heme activation of Hap1 by enhanced association of Hsp90 with the repressed Hsp70-Hap1 complex.	Heme	34-38	Hap1p	Saccharomyces cerevisiae S288C	116-120
15102838-2	2004	The yeast heme-responsive transcriptional activator Hap1 is a native substrate of both Hsp90 and Hsp70.	Heme	10-14	Hap1p	Saccharomyces cerevisiae S288C	52-56
15102838-3	2004	Hsp90 and Hsp70 are critical for the precise regulation of Hap1 activity by heme.	Heme	76-80	Hap1p	Saccharomyces cerevisiae S288C	59-63
15102838-6	2004	Heme enhances the interaction between Hap1 and Hsp90.	Heme	0-4	Hap1p	Saccharomyces cerevisiae S288C	38-42
15102838-7	2004	In vivo, defective Ssa, Ydj1, or Sro9 function causes Hap1 derepression in the absence of heme, whereas defective Hsp90 function causes reduced Hap1 activity at high heme concentrations.	Heme	166-170	Hap1p	Saccharomyces cerevisiae S288C	144-148
14512429-1	2003	Multiple oxygen-responsive steps in the heme biosynthetic pathway affect Hap1 activity.	Oxygen	9-15	Hap1p	Saccharomyces cerevisiae S288C	73-77
14512429-1	2003	Multiple oxygen-responsive steps in the heme biosynthetic pathway affect Hap1 activity.	Heme	40-44	Hap1p	Saccharomyces cerevisiae S288C	73-77
14512429-6	2003	We found that Hap1 activity is controlled in vivo by heme and not by its precursors and that heme activates Hap1 even in anoxic cells.	Heme	53-57	Hap1p	Saccharomyces cerevisiae S288C	14-18
14512429-6	2003	We found that Hap1 activity is controlled in vivo by heme and not by its precursors and that heme activates Hap1 even in anoxic cells.	Heme	93-97	Hap1p	Saccharomyces cerevisiae S288C	108-112
14512429-7	2003	We also found that Hap1 activity exhibits the same oxygen dose-response curves as Hap1-dependent aerobic genes and that these dose-response curves have a sharp break at approximately 1 microM O2.	Oxygen	51-57	Hap1p	Saccharomyces cerevisiae S288C	19-23
14512429-8	2003	The results show that the intracellular signaling heme level, reflected as Hap1 activity, is closely correlated with oxygen concentration.	Heme	50-54	Hap1p	Saccharomyces cerevisiae S288C	75-79
14512429-8	2003	The results show that the intracellular signaling heme level, reflected as Hap1 activity, is closely correlated with oxygen concentration.	Oxygen	117-123	Hap1p	Saccharomyces cerevisiae S288C	75-79
12614847-5	2003	As an intracellular oxygen sensor, heme stimulated TSA2 transcription by activating Hap1p.	Heme	35-39	Hap1p	Saccharomyces cerevisiae S288C	84-89
12614847-6	2003	The induction of TSA2 by H(2)O(2) is also mediated in part through Hap1p.	Hydrogen Peroxide	25-33	Hap1p	Saccharomyces cerevisiae S288C	67-72
12112237-3	2002	The Hap1 transcription factor senses cellular heme status and increases expression of aerobic genes in response to oxygen.	Oxygen	115-121	Hap1p	Saccharomyces cerevisiae S288C	4-8
11827753-5	2002	Deletion of HAP1 or inhibition of heme synthesis abolished induction of mTPx I by H(2)O(2) on cells which were grown in media containing glucose, indicating that Hap1p is involved in the regulation of this process.	Heme	34-38	Hap1p	Saccharomyces cerevisiae S288C	162-167
11751848-0	2002	The molecular chaperone Hsp90 mediates heme activation of the yeast transcriptional activator Hap1.	Heme	39-43	Hap1p	Saccharomyces cerevisiae S288C	94-98
11751848-3	2002	Hap1 transcriptional activity is precisely and stringently controlled by heme.	Heme	73-77	Hap1p	Saccharomyces cerevisiae S288C	0-4
11751848-4	2002	Previous biochemical studies suggest that in the absence of heme, Hap1 is bound to Hsp90 and other proteins, forming a higher order complex termed HMC (high molecular weight complex), and is repressed.	Heme	60-64	Hap1p	Saccharomyces cerevisiae S288C	66-70
11751848-5	2002	Heme promotes the disruption of the HMC and activates Hap1, permitting Hap1 to bind to DNA with high affinity and to stimulate transcription.	Heme	0-4	Hap1p	Saccharomyces cerevisiae S288C	54-58
11751848-5	2002	Heme promotes the disruption of the HMC and activates Hap1, permitting Hap1 to bind to DNA with high affinity and to stimulate transcription.	Heme	0-4	Hap1p	Saccharomyces cerevisiae S288C	71-75
11751848-6	2002	By lowering the expression levels of wild-type Hsp90, using a highly specific Hsp90 inhibitor, and by examining the effects of various Hsp90 mutants on Hap1, we show that Hsp90 is critical for Hap1 activation by heme.	Heme	212-216	Hap1p	Saccharomyces cerevisiae S288C	193-197
11751848-9	2002	Additionally, we found that a heme-independent Hap1 mutant still depends on Hsp90 for high activity.	Heme	30-34	Hap1p	Saccharomyces cerevisiae S288C	47-51
12112237-2	2002	Under aerobic conditions oxygen control of gene expression is exerted through the activator Hap1 and the repressor Rox1.	Oxygen	25-31	Hap1p	Saccharomyces cerevisiae S288C	92-96
12112237-3	2002	The Hap1 transcription factor senses cellular heme status and increases expression of aerobic genes in response to oxygen.	Heme	46-50	Hap1p	Saccharomyces cerevisiae S288C	4-8
11827753-5	2002	Deletion of HAP1 or inhibition of heme synthesis abolished induction of mTPx I by H(2)O(2) on cells which were grown in media containing glucose, indicating that Hap1p is involved in the regulation of this process.	Glucose	137-144	Hap1p	Saccharomyces cerevisiae S288C	12-16
11827753-5	2002	Deletion of HAP1 or inhibition of heme synthesis abolished induction of mTPx I by H(2)O(2) on cells which were grown in media containing glucose, indicating that Hap1p is involved in the regulation of this process.	Glucose	137-144	Hap1p	Saccharomyces cerevisiae S288C	162-167
11827753-7	2002	Finally, mTPx I also induced by t-butyl hydroperoxide in a Hap1p-independent manner.	tert-Butylhydroperoxide	32-53	Hap1p	Saccharomyces cerevisiae S288C	59-64
11689685-0	2001	The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme.	Heme	65-69	Hap1p	Saccharomyces cerevisiae S288C	88-92
11689685-1	2001	In Saccharomyces cerevisiae, heme directly mediates the effects of oxygen on transcription through the heme activator protein Hap1.	Heme	29-33	Hap1p	Saccharomyces cerevisiae S288C	126-130
11689685-1	2001	In Saccharomyces cerevisiae, heme directly mediates the effects of oxygen on transcription through the heme activator protein Hap1.	Oxygen	67-73	Hap1p	Saccharomyces cerevisiae S288C	126-130
11081979-1	2000	Hap1 and Rox1 are transcriptional regulators that bind regulatory sites in the promoters of oxygen-regulated genes in Saccharomyces cerevisiae.	Oxygen	92-98	Hap1p	Saccharomyces cerevisiae S288C	0-4
11689685-7	2001	Our results suggest that Ssa-Ydj1 and Sro9 act together to mediate Hap1 repression in the absence of heme and that molecular chaperones promote heme regulation of Hap1 by a mechanism distinct from the mechanism of steroid signaling.	Heme	144-148	Hap1p	Saccharomyces cerevisiae S288C	163-167
11489845-10	2001	ARE2 requires the HAP1 transcription factor for optimal expression, and both ARE genes are derepressed in a rox1 (repressor of oxygen) mutant genetic background.	Oxygen	127-133	Hap1p	Saccharomyces cerevisiae S288C	18-22
10873649-0	2000	Functional analysis of heme regulatory elements of the transcriptional activator Hap1.	Heme	23-27	Hap1p	Saccharomyces cerevisiae S288C	81-85
10972830-4	2000	We found that Hap1p activity, known to be oxygen dependent, is effected by DNA-protein interaction with two binding sites present in the CYB2 promoter.	Oxygen	42-48	Hap1p	Saccharomyces cerevisiae S288C	14-19
10873649-4	2000	We examined the effects of these HRMs and repeats on heme regulation of Hap1 activity by deletion analysis and by Ala substitutions of key residues.	Heme	53-57	Hap1p	Saccharomyces cerevisiae S288C	72-76
10873649-5	2000	We found that the effect of mutation or deletion of one HRM or 17-amino-acid repeat on Hap1 heme responsiveness is different from the effect of mutation or deletion of another HRM or repeat.	17-amino-acid	63-76	Hap1p	Saccharomyces cerevisiae S288C	87-91
10873649-5	2000	We found that the effect of mutation or deletion of one HRM or 17-amino-acid repeat on Hap1 heme responsiveness is different from the effect of mutation or deletion of another HRM or repeat.	Heme	92-96	Hap1p	Saccharomyces cerevisiae S288C	87-91
10873649-6	2000	Our data suggest that HRM7 plays a dominant role in mediating heme activation of Hap1 in heme-sufficient cells while HRM1-6 may scavenge heme and cause a low level of Hap1 activation in heme-deficient cells.	Heme	62-66	Hap1p	Saccharomyces cerevisiae S288C	81-85
10873649-6	2000	Our data suggest that HRM7 plays a dominant role in mediating heme activation of Hap1 in heme-sufficient cells while HRM1-6 may scavenge heme and cause a low level of Hap1 activation in heme-deficient cells.	Heme	89-93	Hap1p	Saccharomyces cerevisiae S288C	81-85
10873649-6	2000	Our data suggest that HRM7 plays a dominant role in mediating heme activation of Hap1 in heme-sufficient cells while HRM1-6 may scavenge heme and cause a low level of Hap1 activation in heme-deficient cells.	Heme	89-93	Hap1p	Saccharomyces cerevisiae S288C	81-85
10873649-6	2000	Our data suggest that HRM7 plays a dominant role in mediating heme activation of Hap1 in heme-sufficient cells while HRM1-6 may scavenge heme and cause a low level of Hap1 activation in heme-deficient cells.	Heme	89-93	Hap1p	Saccharomyces cerevisiae S288C	81-85
10617612-1	2000	The heme activator protein Hap1 is a member of the yeast Gal4 family, which consists of transcription factors with a conserved Zn(2)Cys(6) cluster that recognizes a CGG triplet.	Zinc	127-129	Hap1p	Saccharomyces cerevisiae S288C	27-31
10617612-1	2000	The heme activator protein Hap1 is a member of the yeast Gal4 family, which consists of transcription factors with a conserved Zn(2)Cys(6) cluster that recognizes a CGG triplet.	Cysteine	132-135	Hap1p	Saccharomyces cerevisiae S288C	27-31
10628845-3	1999	We therefore examined the role of the heme-dependent transcriptional activator Hap1p and the carbon source-dependent Hap2/3/4/5 complex.	Heme	38-42	Hap1p	Saccharomyces cerevisiae S288C	79-84
10628845-4	1999	We found that the Hap2/3/4/5 complex and Hap1p have additive effects on the activation of DLD1 transcription: the Hap2/3/4/5 complex is necessary for DLD1 derepression following a shift from fermentable to non-fermentable carbon sources, while the Hap1p effect was independent of the carbon sources tested.	Carbon	222-228	Hap1p	Saccharomyces cerevisiae S288C	41-46
10628845-4	1999	We found that the Hap2/3/4/5 complex and Hap1p have additive effects on the activation of DLD1 transcription: the Hap2/3/4/5 complex is necessary for DLD1 derepression following a shift from fermentable to non-fermentable carbon sources, while the Hap1p effect was independent of the carbon sources tested.	Carbon	222-228	Hap1p	Saccharomyces cerevisiae S288C	248-253
10628845-4	1999	We found that the Hap2/3/4/5 complex and Hap1p have additive effects on the activation of DLD1 transcription: the Hap2/3/4/5 complex is necessary for DLD1 derepression following a shift from fermentable to non-fermentable carbon sources, while the Hap1p effect was independent of the carbon sources tested.	Carbon	284-290	Hap1p	Saccharomyces cerevisiae S288C	41-46
10628845-4	1999	We found that the Hap2/3/4/5 complex and Hap1p have additive effects on the activation of DLD1 transcription: the Hap2/3/4/5 complex is necessary for DLD1 derepression following a shift from fermentable to non-fermentable carbon sources, while the Hap1p effect was independent of the carbon sources tested.	Carbon	284-290	Hap1p	Saccharomyces cerevisiae S288C	248-253
11212295-0	1999	Molecular mechanism of heme signaling in yeast: the transcriptional activator Hap1 serves as the key mediator.	Heme	23-27	Hap1p	Saccharomyces cerevisiae S288C	78-82
11212295-3	1999	In yeast, oxygen sensing and heme signaling are primarily mediated by the heme activator protein Hap1, which, in response to heme, activates the transcription of genes required for respiration and for controlling oxidative damage.	Oxygen	10-16	Hap1p	Saccharomyces cerevisiae S288C	97-101
11212295-3	1999	In yeast, oxygen sensing and heme signaling are primarily mediated by the heme activator protein Hap1, which, in response to heme, activates the transcription of genes required for respiration and for controlling oxidative damage.	Heme	29-33	Hap1p	Saccharomyces cerevisiae S288C	97-101
11212295-3	1999	In yeast, oxygen sensing and heme signaling are primarily mediated by the heme activator protein Hap1, which, in response to heme, activates the transcription of genes required for respiration and for controlling oxidative damage.	Heme	74-78	Hap1p	Saccharomyces cerevisiae S288C	97-101
11212295-5	1999	In this review, we summarize recent knowledge about (i) how heme synthesis may be controlled by oxygen tension, (ii) how heme precisely and stringently controls Hap1 activity and (iii) whether other transcriptional activators can also mediate heme action.	Heme	121-125	Hap1p	Saccharomyces cerevisiae S288C	161-165
11212295-5	1999	In this review, we summarize recent knowledge about (i) how heme synthesis may be controlled by oxygen tension, (ii) how heme precisely and stringently controls Hap1 activity and (iii) whether other transcriptional activators can also mediate heme action.	Heme	121-125	Hap1p	Saccharomyces cerevisiae S288C	161-165
10541856-1	1999	The HAP1 gene encodes a complex transcriptional regulator of many genes involved in electron-transfer reactions and is essential in anaerobic or heme-depleted conditions.	Heme	145-149	Hap1p	Saccharomyces cerevisiae S288C	4-8
10541856-3	1999	This mutant allele acts as a HAP1 null allele in terms of cytochrome c expression and CYC1 UAS1-dependent transcription, but is able to sustain limited growth in heme-depleted conditions.	Heme	162-166	Hap1p	Saccharomyces cerevisiae S288C	29-33
9886287-5	1999	Unexpectedly, the single amino acid substitution in HAP1-18 nucleates a significantly altered hydrogen bond interface between the protein and DNA resulting in DNA conformational changes and an ordering of one N-terminal arm of the protein dimer along the DNA minor groove.	Hydrogen	94-102	Hap1p	Saccharomyces cerevisiae S288C	52-56
10428861-0	1999	The yeast heme-responsive transcriptional activator Hap1 is a preexisting dimer in the absence of heme.	Heme	10-14	Hap1p	Saccharomyces cerevisiae S288C	52-56
10428861-0	1999	The yeast heme-responsive transcriptional activator Hap1 is a preexisting dimer in the absence of heme.	Heme	98-102	Hap1p	Saccharomyces cerevisiae S288C	52-56
10428861-2	1999	Heme disrupts this complex and permits Hap1 to bind to DNA with high affinity, thereby activating transcription.	Heme	0-4	Hap1p	Saccharomyces cerevisiae S288C	39-43
10428861-3	1999	Heme regulation of Hap1 activity is analogous to the regulation of steroid receptors by steroids, which involves molecular chaperones.	Heme	0-4	Hap1p	Saccharomyces cerevisiae S288C	19-23
10428861-3	1999	Heme regulation of Hap1 activity is analogous to the regulation of steroid receptors by steroids, which involves molecular chaperones.	Steroids	88-96	Hap1p	Saccharomyces cerevisiae S288C	19-23
10428861-5	1999	Furthermore, previous studies indicate that dimerization might be important for heme activation of Hap1.	Heme	80-84	Hap1p	Saccharomyces cerevisiae S288C	99-103
9632766-0	1998	Molecular mechanism governing heme signaling in yeast: a higher-order complex mediates heme regulation of the transcriptional activator HAP1.	Heme	30-34	Hap1p	Saccharomyces cerevisiae S288C	136-140
9632766-0	1998	Molecular mechanism governing heme signaling in yeast: a higher-order complex mediates heme regulation of the transcriptional activator HAP1.	Heme	87-91	Hap1p	Saccharomyces cerevisiae S288C	136-140
9632766-2	1998	To gain insights into molecular mechanisms of heme signaling and oxygen sensing in eukaryotes, we investigated the yeast heme-responsive transcriptional activator HAP1.	Heme	46-50	Hap1p	Saccharomyces cerevisiae S288C	163-167
9632766-2	1998	To gain insights into molecular mechanisms of heme signaling and oxygen sensing in eukaryotes, we investigated the yeast heme-responsive transcriptional activator HAP1.	Oxygen	65-71	Hap1p	Saccharomyces cerevisiae S288C	163-167
9632766-2	1998	To gain insights into molecular mechanisms of heme signaling and oxygen sensing in eukaryotes, we investigated the yeast heme-responsive transcriptional activator HAP1.	Heme	121-125	Hap1p	Saccharomyces cerevisiae S288C	163-167
9632766-3	1998	HAP1 activity is regulated precisely and tightly by heme.	Heme	52-56	Hap1p	Saccharomyces cerevisiae S288C	0-4
9632766-6	1998	The formation of this complex is directly correlated with HAP1 repression in the absence of heme, and mutational or heme disruption of the complex correlates with HAP1 activation, suggesting that this complex is responsible for heme regulation of HAP1 activity.	Heme	92-96	Hap1p	Saccharomyces cerevisiae S288C	58-62
9632766-6	1998	The formation of this complex is directly correlated with HAP1 repression in the absence of heme, and mutational or heme disruption of the complex correlates with HAP1 activation, suggesting that this complex is responsible for heme regulation of HAP1 activity.	Heme	116-120	Hap1p	Saccharomyces cerevisiae S288C	58-62
9632766-6	1998	The formation of this complex is directly correlated with HAP1 repression in the absence of heme, and mutational or heme disruption of the complex correlates with HAP1 activation, suggesting that this complex is responsible for heme regulation of HAP1 activity.	Heme	116-120	Hap1p	Saccharomyces cerevisiae S288C	163-167
9632766-6	1998	The formation of this complex is directly correlated with HAP1 repression in the absence of heme, and mutational or heme disruption of the complex correlates with HAP1 activation, suggesting that this complex is responsible for heme regulation of HAP1 activity.	Heme	116-120	Hap1p	Saccharomyces cerevisiae S288C	163-167
9632766-6	1998	The formation of this complex is directly correlated with HAP1 repression in the absence of heme, and mutational or heme disruption of the complex correlates with HAP1 activation, suggesting that this complex is responsible for heme regulation of HAP1 activity.	Heme	116-120	Hap1p	Saccharomyces cerevisiae S288C	58-62
9632766-6	1998	The formation of this complex is directly correlated with HAP1 repression in the absence of heme, and mutational or heme disruption of the complex correlates with HAP1 activation, suggesting that this complex is responsible for heme regulation of HAP1 activity.	Heme	116-120	Hap1p	Saccharomyces cerevisiae S288C	163-167
9632766-6	1998	The formation of this complex is directly correlated with HAP1 repression in the absence of heme, and mutational or heme disruption of the complex correlates with HAP1 activation, suggesting that this complex is responsible for heme regulation of HAP1 activity.	Heme	116-120	Hap1p	Saccharomyces cerevisiae S288C	163-167
9632766-7	1998	Further, we determined HAP1 domains required for heme regulation: three domains-the dimerization domain, the heme domain, and the HRM7 (heme-responsive motif 7) domain-cooperate to form the higher-order complex and mediate heme regulation.	Heme	49-53	Hap1p	Saccharomyces cerevisiae S288C	23-27
9632766-7	1998	Further, we determined HAP1 domains required for heme regulation: three domains-the dimerization domain, the heme domain, and the HRM7 (heme-responsive motif 7) domain-cooperate to form the higher-order complex and mediate heme regulation.	Heme	109-113	Hap1p	Saccharomyces cerevisiae S288C	23-27
9632766-7	1998	Further, we determined HAP1 domains required for heme regulation: three domains-the dimerization domain, the heme domain, and the HRM7 (heme-responsive motif 7) domain-cooperate to form the higher-order complex and mediate heme regulation.	Heme	109-113	Hap1p	Saccharomyces cerevisiae S288C	23-27
9632766-7	1998	Further, we determined HAP1 domains required for heme regulation: three domains-the dimerization domain, the heme domain, and the HRM7 (heme-responsive motif 7) domain-cooperate to form the higher-order complex and mediate heme regulation.	Heme	109-113	Hap1p	Saccharomyces cerevisiae S288C	23-27
9632766-8	1998	Strikingly, we uncovered a novel function for the HAP1 dimerization domain: it not only allows dimerization but also provides critical functions in heme regulation and transcriptional activation.	Heme	148-152	Hap1p	Saccharomyces cerevisiae S288C	50-54
9632766-9	1998	Our studies provide significant insights into the molecular events leading to heme activation of HAP1 and may shed light on molecular mechanisms of various heme-controlled biological processes in diverse organisms.	Heme	78-82	Hap1p	Saccharomyces cerevisiae S288C	97-101
9632766-9	1998	Our studies provide significant insights into the molecular events leading to heme activation of HAP1 and may shed light on molecular mechanisms of various heme-controlled biological processes in diverse organisms.	Heme	156-160	Hap1p	Saccharomyces cerevisiae S288C	97-101
9504906-2	1998	Analysis of intragenic revertants shows that this function depends on the amino acid preceding the first cysteine residue of the DNA-binding domain of Hap1p.	Cysteine	105-113	Hap1p	Saccharomyces cerevisiae S288C	151-156
9224603-0	1997	NMR analysis of CYP1(HAP1) DNA binding domain-CYC1 upstream activation sequence interactions: recognition of a CGG trinucleotide and of an additional thymine 5 bp downstream by the zinc cluster and the N-terminal extremity of the protein.	cgg trinucleotide	111-128	Hap1p	Saccharomyces cerevisiae S288C	16-20
9224603-0	1997	NMR analysis of CYP1(HAP1) DNA binding domain-CYC1 upstream activation sequence interactions: recognition of a CGG trinucleotide and of an additional thymine 5 bp downstream by the zinc cluster and the N-terminal extremity of the protein.	cgg trinucleotide	111-128	Hap1p	Saccharomyces cerevisiae S288C	21-25
9224603-0	1997	NMR analysis of CYP1(HAP1) DNA binding domain-CYC1 upstream activation sequence interactions: recognition of a CGG trinucleotide and of an additional thymine 5 bp downstream by the zinc cluster and the N-terminal extremity of the protein.	Thymine	150-157	Hap1p	Saccharomyces cerevisiae S288C	16-20
9224603-0	1997	NMR analysis of CYP1(HAP1) DNA binding domain-CYC1 upstream activation sequence interactions: recognition of a CGG trinucleotide and of an additional thymine 5 bp downstream by the zinc cluster and the N-terminal extremity of the protein.	Thymine	150-157	Hap1p	Saccharomyces cerevisiae S288C	21-25
7835342-2	1995	Interestingly, heme also potentiates binding of the yeast transcriptional activator HAP1 to DNA and inhibits mitochondrial import of the mammalian delta-aminolevulinate synthase (ALAS) and the catalytic activity of the reticulocyte kinase, HRI.	Heme	15-19	Hap1p	Saccharomyces cerevisiae S288C	84-88
9108135-5	1997	Finally, Hap1p, a heme-binding, DNA-binding transcription activator, is required for full SOD2 expression during growth on glucose.	Heme	18-22	Hap1p	Saccharomyces cerevisiae S288C	9-14
9108135-5	1997	Finally, Hap1p, a heme-binding, DNA-binding transcription activator, is required for full SOD2 expression during growth on glucose.	Glucose	123-130	Hap1p	Saccharomyces cerevisiae S288C	9-14
9108135-7	1997	Interestingly, the DNA sequences necessary for repression in the absence of heme overlap those that mediate Hap1p activation.	Heme	76-80	Hap1p	Saccharomyces cerevisiae S288C	108-113
9027731-5	1997	Under aerobic conditions, heme accumulates and serves as an effector for the transcriptional activator Hap1.	Heme	26-30	Hap1p	Saccharomyces cerevisiae S288C	103-107
9027731-7	1997	Under hypoxic conditions, heme levels fall, and a heme-deficient Hap1 complex represses ROX1 expression.	Heme	26-30	Hap1p	Saccharomyces cerevisiae S288C	65-69
9037103-5	1997	Mutagenesis of the perfect consensus for HAP2/3/4 complex binding at position -542 resulted in considerable reduction of UBI4 promoter derepression with respiratory adaptation in HAP wild-type cells and abolished the reduced UBI4-LacZ derepression normally seen when aerobic cultures of the hap1 mutant are transferred from glucose to lactate.	Glucose	324-331	Hap1p	Saccharomyces cerevisiae S288C	291-295
9037103-5	1997	Mutagenesis of the perfect consensus for HAP2/3/4 complex binding at position -542 resulted in considerable reduction of UBI4 promoter derepression with respiratory adaptation in HAP wild-type cells and abolished the reduced UBI4-LacZ derepression normally seen when aerobic cultures of the hap1 mutant are transferred from glucose to lactate.	Lactic Acid	335-342	Hap1p	Saccharomyces cerevisiae S288C	291-295
9003293-6	1996	Interestingly, we find that in the presence of the CYP3-5 mutation, which disrupts this potential UAS1, the CYP-UAS" complex is importantly diminished and the transcription of CYP3 is insensitive to the wild-type CYP1-activating protein.	Phenindione	98-101	Hap1p	Saccharomyces cerevisiae S288C	213-217
8683583-0	1996	1H, 15N resonance assignment and three-dimensional structure of CYP1 (HAP1) DNA-binding domain.	Hydrogen	0-2	Hap1p	Saccharomyces cerevisiae S288C	70-74
8683583-0	1996	1H, 15N resonance assignment and three-dimensional structure of CYP1 (HAP1) DNA-binding domain.	15n	4-7	Hap1p	Saccharomyces cerevisiae S288C	64-68
8683583-0	1996	1H, 15N resonance assignment and three-dimensional structure of CYP1 (HAP1) DNA-binding domain.	15n	4-7	Hap1p	Saccharomyces cerevisiae S288C	70-74
7768429-5	1995	Also, we found that, as reported previously, Hap1 is partially responsible for heme-induction of ROX1, but, in addition, it also may play a role in ROX1 repression in the absence of heme.	Heme	79-83	Hap1p	Saccharomyces cerevisiae S288C	45-49
7768429-5	1995	Also, we found that, as reported previously, Hap1 is partially responsible for heme-induction of ROX1, but, in addition, it also may play a role in ROX1 repression in the absence of heme.	Heme	182-186	Hap1p	Saccharomyces cerevisiae S288C	45-49
8710512-2	1996	Among them are the heme-dependent protein, Hap1p, and the multiprotein complex, Hap2/3/4/5, which mediate transcriptional induction under aerobic conditions and after exhaustion of glucose, respectively.	Glucose	181-188	Hap1p	Saccharomyces cerevisiae S288C	43-48
8593679-5	1995	Both Rox1p and Cyp1p partially repressed HEM13 in aerobic heme-sufficient cells, probably in an independent manner.	Heme	58-62	Hap1p	Saccharomyces cerevisiae S288C	15-20
7651346-0	1995	Multiple domains mediate heme control of the yeast activator HAP1.	Heme	25-29	Hap1p	Saccharomyces cerevisiae S288C	61-65
7651346-1	1995	The activity of the yeast activator HAP1 in vivo requires heme.	Heme	58-62	Hap1p	Saccharomyces cerevisiae S288C	36-40
7651346-2	1995	A heme responsive domain of HAP1 was identified previously.	Heme	2-6	Hap1p	Saccharomyces cerevisiae S288C	28-32
7651346-5	1995	These mutants define a second region of HAP1, close to the activation domain, which also controls its response to heme.	Heme	114-118	Hap1p	Saccharomyces cerevisiae S288C	40-44
8182072-1	1994	The activity of the yeast transcription activator HAP1 is controlled by heme.	Heme	72-76	Hap1p	Saccharomyces cerevisiae S288C	50-54
7957173-3	1994	We show that this CYP1(49-126) peptide requires zinc or cadmium in the growth medium in order to maintain a stable structure.	Cadmium	56-63	Hap1p	Saccharomyces cerevisiae S288C	18-22
7957173-5	1994	We demonstrate that the purified CYP1(49-126) fragment contains two zinc ions/fragment or two cadmium ions/fragment, which are necessary for DNA binding.	Cadmium	94-101	Hap1p	Saccharomyces cerevisiae S288C	33-37
7957173-6	1994	113Cd one-dimensional NMR data suggest that CYP1(HAP1) has a tetrahedral coordination, and that it forms a zinc-cluster complex like GAL4.	Cadmium, isotope of mass 113	0-5	Hap1p	Saccharomyces cerevisiae S288C	44-48
7957173-6	1994	113Cd one-dimensional NMR data suggest that CYP1(HAP1) has a tetrahedral coordination, and that it forms a zinc-cluster complex like GAL4.	Cadmium, isotope of mass 113	0-5	Hap1p	Saccharomyces cerevisiae S288C	49-53
7958882-6	1994	Dimethylsulfate protection patterns on six of these sites show protections and enhancements that also lie in a directly repeated orientation, suggesting that the two HAP1 DNA recognition domains of a HAP1 homodimer are oriented in a directly repeated configuration on the DNA.	dimethyl sulfate	0-15	Hap1p	Saccharomyces cerevisiae S288C	166-170
7958882-6	1994	Dimethylsulfate protection patterns on six of these sites show protections and enhancements that also lie in a directly repeated orientation, suggesting that the two HAP1 DNA recognition domains of a HAP1 homodimer are oriented in a directly repeated configuration on the DNA.	dimethyl sulfate	0-15	Hap1p	Saccharomyces cerevisiae S288C	200-204
8182072-3	1994	In this report, we show that HAP1 is sequestered in a high molecular weight complex in the absence of heme.	Heme	102-106	Hap1p	Saccharomyces cerevisiae S288C	29-33
8182072-4	1994	Titration of the high molecular weight complex by addition of a non-DNA-binding form of HAP1 allows the protein to form dimeric complexes in the absence of heme in vitro and acquires partial transcriptional activity in vivo.	Heme	156-160	Hap1p	Saccharomyces cerevisiae S288C	88-92
8182072-5	1994	The results indicate that one or more cellular factor(s) complexes with HAP1 and represses its activity in the absence of heme.	Heme	122-126	Hap1p	Saccharomyces cerevisiae S288C	72-76
8182072-6	1994	Deletion of the heme domain prevents sequestration of HAP1 in the high molecular weight complex.	Heme	16-20	Hap1p	Saccharomyces cerevisiae S288C	54-58
8182072-7	1994	We discuss these findings in a model that postulates that the heme domain of HAP1 can interact with other cellular factors to regulate HAP1.	Heme	62-66	Hap1p	Saccharomyces cerevisiae S288C	77-81
8182072-7	1994	We discuss these findings in a model that postulates that the heme domain of HAP1 can interact with other cellular factors to regulate HAP1.	Heme	62-66	Hap1p	Saccharomyces cerevisiae S288C	135-139
8005436-1	1994	The activity of the yeast transcriptional activator HAP1 is controlled by heme and the heme effect is mediated through the heme domain of HAP1.	Heme	74-78	Hap1p	Saccharomyces cerevisiae S288C	52-56
8005436-1	1994	The activity of the yeast transcriptional activator HAP1 is controlled by heme and the heme effect is mediated through the heme domain of HAP1.	Heme	87-91	Hap1p	Saccharomyces cerevisiae S288C	52-56
8005436-1	1994	The activity of the yeast transcriptional activator HAP1 is controlled by heme and the heme effect is mediated through the heme domain of HAP1.	Heme	87-91	Hap1p	Saccharomyces cerevisiae S288C	138-142
8005436-1	1994	The activity of the yeast transcriptional activator HAP1 is controlled by heme and the heme effect is mediated through the heme domain of HAP1.	Heme	87-91	Hap1p	Saccharomyces cerevisiae S288C	52-56
8005436-1	1994	The activity of the yeast transcriptional activator HAP1 is controlled by heme and the heme effect is mediated through the heme domain of HAP1.	Heme	87-91	Hap1p	Saccharomyces cerevisiae S288C	138-142
8005436-4	1994	The results suggest that TUP1/SSN6 have a positive effect on the activity of HAP1 and this effect is mediated through the heme domain.	Heme	122-126	Hap1p	Saccharomyces cerevisiae S288C	77-81
8005437-4	1994	HAP1 encodes an activator protein whose DNA binding activity is stimulated by heme, and is required for the transcription of CYC1, ROX1 and a number of other heme-dependent genes.	Heme	78-82	Hap1p	Saccharomyces cerevisiae S288C	0-4
8005437-4	1994	HAP1 encodes an activator protein whose DNA binding activity is stimulated by heme, and is required for the transcription of CYC1, ROX1 and a number of other heme-dependent genes.	Heme	158-162	Hap1p	Saccharomyces cerevisiae S288C	0-4
8005437-9	1994	The mutation associated with this novel allele of HAP1 was localized to a glycine to aspartate change in amino acid 235 of HAP1, between the DNA binding and heme responsive domains.	Heme	157-161	Hap1p	Saccharomyces cerevisiae S288C	50-54
8005437-9	1994	The mutation associated with this novel allele of HAP1 was localized to a glycine to aspartate change in amino acid 235 of HAP1, between the DNA binding and heme responsive domains.	Heme	157-161	Hap1p	Saccharomyces cerevisiae S288C	123-127
8464899-0	1993	Antibody-promoted dimerization bypasses the regulation of DNA binding by the heme domain of the yeast transcriptional activator HAP1.	Heme	77-81	Hap1p	Saccharomyces cerevisiae S288C	128-132
8152420-0	1994	Functional analysis of the zinc cluster domain of the CYP1 (HAP1) complex regulator in heme-sufficient and heme-deficient yeast cells.	Heme	87-91	Hap1p	Saccharomyces cerevisiae S288C	54-58
8152420-0	1994	Functional analysis of the zinc cluster domain of the CYP1 (HAP1) complex regulator in heme-sufficient and heme-deficient yeast cells.	Heme	87-91	Hap1p	Saccharomyces cerevisiae S288C	60-64
8152420-1	1994	CYP1 determines the expression of several genes whose transcription is heme-dependent in yeast.	Heme	71-75	Hap1p	Saccharomyces cerevisiae S288C	0-4
8152420-6	1994	We show that CYP1 does belong to the zinc cluster regulatory family since a sixth essential cysteine residue is indeed present, albeit at a modified position when compared to the consensus sequence.	Cysteine	92-100	Hap1p	Saccharomyces cerevisiae S288C	13-17
8464899-1	1993	The yeast transcriptional activator HAP1 contains a DNA-binding domain homologous to the zinc finger of GAL4 and an adjacent regulatory domain that blocks DNA binding in the absence of the inducer heme.	Heme	197-201	Hap1p	Saccharomyces cerevisiae S288C	36-40
8464899-5	1993	Interestingly, the antibody will also promote DNA binding of a larger HAP1 fragment containing the DNA-binding and the heme-regulatory domains.	Heme	119-123	Hap1p	Saccharomyces cerevisiae S288C	70-74
8464899-6	1993	This suggests that the regulatory domain acts by preventing dimerization of HAP1 in the absence of heme.	Heme	99-103	Hap1p	Saccharomyces cerevisiae S288C	76-80
8464899-7	1993	Consistent with this view is an in vivo assay that also reveals that heme promotes HAP1 dimerization in yeast cells.	Heme	69-73	Hap1p	Saccharomyces cerevisiae S288C	83-87
1715975-0	1991	CYP1 (HAP1) is a determinant effector of alternative expression of heme-dependent transcribed genes in yeast [corrected].	Heme	67-71	Hap1p	Saccharomyces cerevisiae S288C	0-4
1588959-4	1992	The transcriptional activator HAP1 is demonstrated to be required for the full-level expression of HEM13 in the absence of heme.	Heme	123-127	Hap1p	Saccharomyces cerevisiae S288C	30-34
1588959-5	1992	It is also shown that the repression of HEM13 transcription caused by heme involves the HAP1 and ROX1 gene products; a mutation in either gene results in derepression of HEM13 expression.	Heme	70-74	Hap1p	Saccharomyces cerevisiae S288C	88-92
1588959-6	1992	The heme-dependent expression of ROX1 was found to require functional HAP1, leading one to propose that repression of HEM13 results from a pathway involving HAP1-mediated regulation of ROX1 transcription in response to heme levels followed by ROX1-mediated repression of HEM13 transcription.	Heme	4-8	Hap1p	Saccharomyces cerevisiae S288C	70-74
1588959-6	1992	The heme-dependent expression of ROX1 was found to require functional HAP1, leading one to propose that repression of HEM13 results from a pathway involving HAP1-mediated regulation of ROX1 transcription in response to heme levels followed by ROX1-mediated repression of HEM13 transcription.	Heme	4-8	Hap1p	Saccharomyces cerevisiae S288C	157-161
1588959-6	1992	The heme-dependent expression of ROX1 was found to require functional HAP1, leading one to propose that repression of HEM13 results from a pathway involving HAP1-mediated regulation of ROX1 transcription in response to heme levels followed by ROX1-mediated repression of HEM13 transcription.	Heme	219-223	Hap1p	Saccharomyces cerevisiae S288C	70-74
1588959-6	1992	The heme-dependent expression of ROX1 was found to require functional HAP1, leading one to propose that repression of HEM13 results from a pathway involving HAP1-mediated regulation of ROX1 transcription in response to heme levels followed by ROX1-mediated repression of HEM13 transcription.	Heme	219-223	Hap1p	Saccharomyces cerevisiae S288C	157-161
1588959-8	1992	The ability of ROX1 encoded by the galactose-inducible ROX1 construct to function in the absence of HAP1 indicates that the only role of HAP1 in repression of HEM13 is to activate ROX1 transcription.	Galactose	35-44	Hap1p	Saccharomyces cerevisiae S288C	137-141
1316998-5	1992	These analyses showed that, in the presence of glucose, transcription of CYT1 is positively controlled by oxygen, presumably through the haem signal, and mediated by the HAP1-encoded transactivator.	Glucose	47-54	Hap1p	Saccharomyces cerevisiae S288C	170-174
8458333-0	1993	Evidence for an interaction between the CYP1(HAP1) activator and a cellular factor during heme-dependent transcriptional regulation in the yeast Saccharomyces cerevisiae.	Heme	90-94	Hap1p	Saccharomyces cerevisiae S288C	40-44
8458333-0	1993	Evidence for an interaction between the CYP1(HAP1) activator and a cellular factor during heme-dependent transcriptional regulation in the yeast Saccharomyces cerevisiae.	Heme	90-94	Hap1p	Saccharomyces cerevisiae S288C	45-49
8458333-1	1993	Previously, it was shown that the CYP1(HAP1) gene product mediates the transcription of several oxygen-regulated genes through a metabolic co-effector, heme, in the yeast Saccharomyces cerevisiae.	Oxygen	96-102	Hap1p	Saccharomyces cerevisiae S288C	34-38
8458333-1	1993	Previously, it was shown that the CYP1(HAP1) gene product mediates the transcription of several oxygen-regulated genes through a metabolic co-effector, heme, in the yeast Saccharomyces cerevisiae.	Oxygen	96-102	Hap1p	Saccharomyces cerevisiae S288C	39-43
8458333-1	1993	Previously, it was shown that the CYP1(HAP1) gene product mediates the transcription of several oxygen-regulated genes through a metabolic co-effector, heme, in the yeast Saccharomyces cerevisiae.	Heme	152-156	Hap1p	Saccharomyces cerevisiae S288C	34-38
8458333-1	1993	Previously, it was shown that the CYP1(HAP1) gene product mediates the transcription of several oxygen-regulated genes through a metabolic co-effector, heme, in the yeast Saccharomyces cerevisiae.	Heme	152-156	Hap1p	Saccharomyces cerevisiae S288C	39-43
8458333-4	1993	Band-shift experiments show that the CYP1(HAP1) protein is able to interact specifically with its target sequences in vitro without addition of hemin, and forms a large complex with one or several unidentified factors denoted as X.	Hemin	144-149	Hap1p	Saccharomyces cerevisiae S288C	37-41
8458333-4	1993	Band-shift experiments show that the CYP1(HAP1) protein is able to interact specifically with its target sequences in vitro without addition of hemin, and forms a large complex with one or several unidentified factors denoted as X.	Hemin	144-149	Hap1p	Saccharomyces cerevisiae S288C	42-46
8458333-6	1993	The internal deletion of the seven repeated amino acid sequences containing the KCPVDH motif in the CYP1(HAP1) protein modifies the heme responsiveness phenomenon observed in vitro in the band-shift experiments and in vivo in the transcription of the CYB2, CYC1, CYP3(CYC7) and ERG11 genes.	Heme	132-136	Hap1p	Saccharomyces cerevisiae S288C	100-104
8458333-6	1993	The internal deletion of the seven repeated amino acid sequences containing the KCPVDH motif in the CYP1(HAP1) protein modifies the heme responsiveness phenomenon observed in vitro in the band-shift experiments and in vivo in the transcription of the CYB2, CYC1, CYP3(CYC7) and ERG11 genes.	Heme	132-136	Hap1p	Saccharomyces cerevisiae S288C	105-109
8458333-7	1993	On the basis of these data, we propose a new model for heme-induced activation of the CYP1 protein.	Heme	55-59	Hap1p	Saccharomyces cerevisiae S288C	86-90
1564443-7	1992	Resistance to peroxide was also inducible in an isogenic petite and an isogenic strain with a mutation in the HAP1 gene, indicating that the adaptive response does not require functional mitochondria.	Peroxides	14-22	Hap1p	Saccharomyces cerevisiae S288C	110-114
1715975-0	1991	CYP1 (HAP1) is a determinant effector of alternative expression of heme-dependent transcribed genes in yeast [corrected].	Heme	67-71	Hap1p	Saccharomyces cerevisiae S288C	6-10
1715975-1	1991	The CYP1 (HAP1) gene of Saccharomyces cerevisiae is known to activate a number of target genes in response to the presence of heme.	Heme	126-130	Hap1p	Saccharomyces cerevisiae S288C	4-8
1715975-1	1991	The CYP1 (HAP1) gene of Saccharomyces cerevisiae is known to activate a number of target genes in response to the presence of heme.	Heme	126-130	Hap1p	Saccharomyces cerevisiae S288C	10-14
1715975-7	1991	Opposite effects of CYP1 are observed in aerobic, heme-sufficient cells.	Heme	50-54	Hap1p	Saccharomyces cerevisiae S288C	20-24
1715975-8	1991	We concluded that: (i) CYP1 is an efficient activator especially in heme-depleted cells; (ii) CYP1 exerts both positive and negative regulatory effects; (iii) the nature of the regulatory function of CYP1 depends on the target gene; and (iv) for a given gene, the presence or absence of heme or oxygen reverses the sense of CYP1-dependent regulation.	Heme	68-72	Hap1p	Saccharomyces cerevisiae S288C	23-27
1715975-8	1991	We concluded that: (i) CYP1 is an efficient activator especially in heme-depleted cells; (ii) CYP1 exerts both positive and negative regulatory effects; (iii) the nature of the regulatory function of CYP1 depends on the target gene; and (iv) for a given gene, the presence or absence of heme or oxygen reverses the sense of CYP1-dependent regulation.	Heme	287-291	Hap1p	Saccharomyces cerevisiae S288C	23-27
1715975-8	1991	We concluded that: (i) CYP1 is an efficient activator especially in heme-depleted cells; (ii) CYP1 exerts both positive and negative regulatory effects; (iii) the nature of the regulatory function of CYP1 depends on the target gene; and (iv) for a given gene, the presence or absence of heme or oxygen reverses the sense of CYP1-dependent regulation.	Heme	287-291	Hap1p	Saccharomyces cerevisiae S288C	94-98
1715975-8	1991	We concluded that: (i) CYP1 is an efficient activator especially in heme-depleted cells; (ii) CYP1 exerts both positive and negative regulatory effects; (iii) the nature of the regulatory function of CYP1 depends on the target gene; and (iv) for a given gene, the presence or absence of heme or oxygen reverses the sense of CYP1-dependent regulation.	Heme	287-291	Hap1p	Saccharomyces cerevisiae S288C	94-98
1715975-8	1991	We concluded that: (i) CYP1 is an efficient activator especially in heme-depleted cells; (ii) CYP1 exerts both positive and negative regulatory effects; (iii) the nature of the regulatory function of CYP1 depends on the target gene; and (iv) for a given gene, the presence or absence of heme or oxygen reverses the sense of CYP1-dependent regulation.	Heme	287-291	Hap1p	Saccharomyces cerevisiae S288C	94-98
1715975-8	1991	We concluded that: (i) CYP1 is an efficient activator especially in heme-depleted cells; (ii) CYP1 exerts both positive and negative regulatory effects; (iii) the nature of the regulatory function of CYP1 depends on the target gene; and (iv) for a given gene, the presence or absence of heme or oxygen reverses the sense of CYP1-dependent regulation.	Oxygen	295-301	Hap1p	Saccharomyces cerevisiae S288C	23-27
1715975-8	1991	We concluded that: (i) CYP1 is an efficient activator especially in heme-depleted cells; (ii) CYP1 exerts both positive and negative regulatory effects; (iii) the nature of the regulatory function of CYP1 depends on the target gene; and (iv) for a given gene, the presence or absence of heme or oxygen reverses the sense of CYP1-dependent regulation.	Oxygen	295-301	Hap1p	Saccharomyces cerevisiae S288C	94-98
1715975-8	1991	We concluded that: (i) CYP1 is an efficient activator especially in heme-depleted cells; (ii) CYP1 exerts both positive and negative regulatory effects; (iii) the nature of the regulatory function of CYP1 depends on the target gene; and (iv) for a given gene, the presence or absence of heme or oxygen reverses the sense of CYP1-dependent regulation.	Oxygen	295-301	Hap1p	Saccharomyces cerevisiae S288C	94-98
1715975-8	1991	We concluded that: (i) CYP1 is an efficient activator especially in heme-depleted cells; (ii) CYP1 exerts both positive and negative regulatory effects; (iii) the nature of the regulatory function of CYP1 depends on the target gene; and (iv) for a given gene, the presence or absence of heme or oxygen reverses the sense of CYP1-dependent regulation.	Oxygen	295-301	Hap1p	Saccharomyces cerevisiae S288C	94-98
2046677-3	1991	Furthermore, we have shown that the CYB2 promoter contains one cis negative regulatory region and two heme-dependent positive regions, one of which is controlled by the transcriptional regulator CYP1 (HAP1) which is involved in the modulation of the expression of several oxygen-regulated genes.	Heme	102-106	Hap1p	Saccharomyces cerevisiae S288C	195-199
2046677-3	1991	Furthermore, we have shown that the CYB2 promoter contains one cis negative regulatory region and two heme-dependent positive regions, one of which is controlled by the transcriptional regulator CYP1 (HAP1) which is involved in the modulation of the expression of several oxygen-regulated genes.	Heme	102-106	Hap1p	Saccharomyces cerevisiae S288C	201-205
2182199-5	1990	In contrast, hap1 caused a decrease in all cytochromes and an accumulation of a pigment, probably Zn porphyrin.	zn porphyrin	98-110	Hap1p	Saccharomyces cerevisiae S288C	13-17
2046677-3	1991	Furthermore, we have shown that the CYB2 promoter contains one cis negative regulatory region and two heme-dependent positive regions, one of which is controlled by the transcriptional regulator CYP1 (HAP1) which is involved in the modulation of the expression of several oxygen-regulated genes.	Oxygen	272-278	Hap1p	Saccharomyces cerevisiae S288C	195-199
2046677-3	1991	Furthermore, we have shown that the CYB2 promoter contains one cis negative regulatory region and two heme-dependent positive regions, one of which is controlled by the transcriptional regulator CYP1 (HAP1) which is involved in the modulation of the expression of several oxygen-regulated genes.	Oxygen	272-278	Hap1p	Saccharomyces cerevisiae S288C	201-205
2182199-10	1990	Results are consistent with generalized control of mitochondrial replication directed by the HAP1-HAP2 system and heme-directed control of formation of all apocytochromes mediated by HAP1.	Heme	114-118	Hap1p	Saccharomyces cerevisiae S288C	183-187
2182199-8	1990	The hap1 mutant grew at near-normal rates on glycerol, whereas hap2 and hap3 mutants grew very slowly.	Glycerol	45-53	Hap1p	Saccharomyces cerevisiae S288C	4-8
2509943-11	1989	We thus conclude that HAP1-18 is a better activator of transcription than the wild-type protein when bound to the UAS of CYC7.	Phenindione	114-117	Hap1p	Saccharomyces cerevisiae S288C	22-29
2685574-4	1989	The effect of heme on HMG1 expression was mediated by the HAP1 transcriptional regulator and was independent of HAP2.	Heme	14-18	Hap1p	Saccharomyces cerevisiae S288C	58-62
2540169-4	1989	By quantitating COX6 RNA levels and assaying beta-galactosidase activity in yeast cells carrying COX6-lacZ fusion genes, we have found that COX6 is regulated positively by heme and HAP2, but is unaffected by HAP1.	Heme	172-176	Hap1p	Saccharomyces cerevisiae S288C	208-212
2851658-0	1988	CYP1 (HAP1) regulator of oxygen-dependent gene expression in yeast.	Oxygen	25-31	Hap1p	Saccharomyces cerevisiae S288C	0-4
2851658-0	1988	CYP1 (HAP1) regulator of oxygen-dependent gene expression in yeast.	Oxygen	25-31	Hap1p	Saccharomyces cerevisiae S288C	6-10
2851659-0	1988	CYP1 (HAP1) regulator of oxygen-dependent gene expression in yeast.	Oxygen	25-31	Hap1p	Saccharomyces cerevisiae S288C	0-4
2851659-0	1988	CYP1 (HAP1) regulator of oxygen-dependent gene expression in yeast.	Oxygen	25-31	Hap1p	Saccharomyces cerevisiae S288C	6-10
2844525-1	1988	Control of expression of the Saccharomyces cerevisiae CTT1 (catalase T) gene by the HAP1 (CYP1) gene, a mediator of heme control of mitochondrial cytochromes, was studied.	Heme	116-120	Hap1p	Saccharomyces cerevisiae S288C	84-88
2841577-2	1988	Oxygen regulation is mediated by the expression of the CYP1 gene, and the CYP1 protein interacts with both CYC1 upstream activation sequence 1 (UAS1) and CYC7 UASo.	Oxygen	0-6	Hap1p	Saccharomyces cerevisiae S288C	55-59
2841577-2	1988	Oxygen regulation is mediated by the expression of the CYP1 gene, and the CYP1 protein interacts with both CYC1 upstream activation sequence 1 (UAS1) and CYC7 UASo.	Oxygen	0-6	Hap1p	Saccharomyces cerevisiae S288C	74-78
2841577-5	1988	Directed mutagenesis changing these GC residues to CG residues in CYC7 led to CYC1-like expression of CYC7 both in a CYP1 wild-type strain and in a strain carrying the semidominant mutation CYP1-16 which reverses the oxygen-dependent expression of the two genes.	gallocatechol	36-38	Hap1p	Saccharomyces cerevisiae S288C	117-121
2841577-5	1988	Directed mutagenesis changing these GC residues to CG residues in CYC7 led to CYC1-like expression of CYC7 both in a CYP1 wild-type strain and in a strain carrying the semidominant mutation CYP1-16 which reverses the oxygen-dependent expression of the two genes.	gallocatechol	36-38	Hap1p	Saccharomyces cerevisiae S288C	190-194
2841577-5	1988	Directed mutagenesis changing these GC residues to CG residues in CYC7 led to CYC1-like expression of CYC7 both in a CYP1 wild-type strain and in a strain carrying the semidominant mutation CYP1-16 which reverses the oxygen-dependent expression of the two genes.	cysteinylglycine	51-53	Hap1p	Saccharomyces cerevisiae S288C	117-121
2841577-5	1988	Directed mutagenesis changing these GC residues to CG residues in CYC7 led to CYC1-like expression of CYC7 both in a CYP1 wild-type strain and in a strain carrying the semidominant mutation CYP1-16 which reverses the oxygen-dependent expression of the two genes.	cysteinylglycine	51-53	Hap1p	Saccharomyces cerevisiae S288C	190-194
2841577-5	1988	Directed mutagenesis changing these GC residues to CG residues in CYC7 led to CYC1-like expression of CYC7 both in a CYP1 wild-type strain and in a strain carrying the semidominant mutation CYP1-16 which reverses the oxygen-dependent expression of the two genes.	Oxygen	217-223	Hap1p	Saccharomyces cerevisiae S288C	190-194
2844525-1	1988	Control of expression of the Saccharomyces cerevisiae CTT1 (catalase T) gene by the HAP1 (CYP1) gene, a mediator of heme control of mitochondrial cytochromes, was studied.	Heme	116-120	Hap1p	Saccharomyces cerevisiae S288C	90-94
2844525-3	1988	As demonstrated by a gel retardation assay, the HAP1 protein binds to a heme control region of the CTT1 gene.	Heme	72-76	Hap1p	Saccharomyces cerevisiae S288C	48-52
2844525-10	1988	Heme acts as a metabolic signal in this coordination, which is mediated by the HAP1 protein.	Heme	0-4	Hap1p	Saccharomyces cerevisiae S288C	79-83
3037351-6	1987	The weak oxygen regulation in wild-type cells and the enhanced induction in CYP1-16 mutants were found to be mediated through the positive site.	Oxygen	9-15	Hap1p	Saccharomyces cerevisiae S288C	76-80
2823123-3	1987	Deletion analysis showed that induction by heme depends upon sequences between -250 and -228 (from the coding sequence) and upon the HAP1 activator gene, previously shown to be required for CYC1 expression (L. Guarente et al., Cell 36:503-511, 1984).	Heme	43-47	Hap1p	Saccharomyces cerevisiae S288C	133-137
3030565-1	1987	We show that the HAP1 protein binds in vitro to the upstream activation site (UAS) of the yeast CYC7 gene.	Phenindione	78-81	Hap1p	Saccharomyces cerevisiae S288C	17-21
3030567-3	1987	The binding of HAP1 in vitro, like the activity of UAS1 in vivo, is stimulated by heme.	Heme	82-86	Hap1p	Saccharomyces cerevisiae S288C	15-19
6319028-7	1984	Second, trans-acting regulatory mutations, hap1-1 and hap2-1, selectively abolish the activity of UAS1 or UAS2.	uas1	98-102	Hap1p	Saccharomyces cerevisiae S288C	43-49
2987643-2	1985	When introduced in yeast cells this hybrid gene is expressed and regulated like the production of iso2-cytochrome c: it is under the control of the general catabolic repression and of the unlinked trans-acting CYP1 gene whose CYP1-18 allele causes an overproduction of iso2-cytochrome c. The expression of hybrid genes whose upstream region has been progressively shortened or altered by internal deletions was studied either in wild-type CYP1+ cells or in cells carrying the CYP1-18 allele grown either on glucose or on glycerol.	Glucose	507-514	Hap1p	Saccharomyces cerevisiae S288C	210-214
2987643-2	1985	When introduced in yeast cells this hybrid gene is expressed and regulated like the production of iso2-cytochrome c: it is under the control of the general catabolic repression and of the unlinked trans-acting CYP1 gene whose CYP1-18 allele causes an overproduction of iso2-cytochrome c. The expression of hybrid genes whose upstream region has been progressively shortened or altered by internal deletions was studied either in wild-type CYP1+ cells or in cells carrying the CYP1-18 allele grown either on glucose or on glycerol.	Glucose	507-514	Hap1p	Saccharomyces cerevisiae S288C	226-230
2987643-2	1985	When introduced in yeast cells this hybrid gene is expressed and regulated like the production of iso2-cytochrome c: it is under the control of the general catabolic repression and of the unlinked trans-acting CYP1 gene whose CYP1-18 allele causes an overproduction of iso2-cytochrome c. The expression of hybrid genes whose upstream region has been progressively shortened or altered by internal deletions was studied either in wild-type CYP1+ cells or in cells carrying the CYP1-18 allele grown either on glucose or on glycerol.	Glucose	507-514	Hap1p	Saccharomyces cerevisiae S288C	226-230
2987643-2	1985	When introduced in yeast cells this hybrid gene is expressed and regulated like the production of iso2-cytochrome c: it is under the control of the general catabolic repression and of the unlinked trans-acting CYP1 gene whose CYP1-18 allele causes an overproduction of iso2-cytochrome c. The expression of hybrid genes whose upstream region has been progressively shortened or altered by internal deletions was studied either in wild-type CYP1+ cells or in cells carrying the CYP1-18 allele grown either on glucose or on glycerol.	Glucose	507-514	Hap1p	Saccharomyces cerevisiae S288C	226-230
2987643-2	1985	When introduced in yeast cells this hybrid gene is expressed and regulated like the production of iso2-cytochrome c: it is under the control of the general catabolic repression and of the unlinked trans-acting CYP1 gene whose CYP1-18 allele causes an overproduction of iso2-cytochrome c. The expression of hybrid genes whose upstream region has been progressively shortened or altered by internal deletions was studied either in wild-type CYP1+ cells or in cells carrying the CYP1-18 allele grown either on glucose or on glycerol.	Glycerol	521-529	Hap1p	Saccharomyces cerevisiae S288C	210-214
2987643-2	1985	When introduced in yeast cells this hybrid gene is expressed and regulated like the production of iso2-cytochrome c: it is under the control of the general catabolic repression and of the unlinked trans-acting CYP1 gene whose CYP1-18 allele causes an overproduction of iso2-cytochrome c. The expression of hybrid genes whose upstream region has been progressively shortened or altered by internal deletions was studied either in wild-type CYP1+ cells or in cells carrying the CYP1-18 allele grown either on glucose or on glycerol.	Glycerol	521-529	Hap1p	Saccharomyces cerevisiae S288C	226-230
2987643-2	1985	When introduced in yeast cells this hybrid gene is expressed and regulated like the production of iso2-cytochrome c: it is under the control of the general catabolic repression and of the unlinked trans-acting CYP1 gene whose CYP1-18 allele causes an overproduction of iso2-cytochrome c. The expression of hybrid genes whose upstream region has been progressively shortened or altered by internal deletions was studied either in wild-type CYP1+ cells or in cells carrying the CYP1-18 allele grown either on glucose or on glycerol.	Glycerol	521-529	Hap1p	Saccharomyces cerevisiae S288C	226-230
2987643-2	1985	When introduced in yeast cells this hybrid gene is expressed and regulated like the production of iso2-cytochrome c: it is under the control of the general catabolic repression and of the unlinked trans-acting CYP1 gene whose CYP1-18 allele causes an overproduction of iso2-cytochrome c. The expression of hybrid genes whose upstream region has been progressively shortened or altered by internal deletions was studied either in wild-type CYP1+ cells or in cells carrying the CYP1-18 allele grown either on glucose or on glycerol.	Glycerol	521-529	Hap1p	Saccharomyces cerevisiae S288C	226-230
2993801-6	1985	To clone the CYP1 gene, we took advantage of the iso 2-cytochrome c overproducer phenotype of the mutated allele CYP1-18, which confers a Lactate+ phenotype on an iso 1-cytochrome c-deficient strain.	Lactic Acid	138-145	Hap1p	Saccharomyces cerevisiae S288C	13-17
2993801-6	1985	To clone the CYP1 gene, we took advantage of the iso 2-cytochrome c overproducer phenotype of the mutated allele CYP1-18, which confers a Lactate+ phenotype on an iso 1-cytochrome c-deficient strain.	Lactic Acid	138-145	Hap1p	Saccharomyces cerevisiae S288C	113-117
6319028-7	1984	Second, trans-acting regulatory mutations, hap1-1 and hap2-1, selectively abolish the activity of UAS1 or UAS2.	uas2	106-110	Hap1p	Saccharomyces cerevisiae S288C	43-49
6319028-8	1984	HAP1 appears to encode a protein that mediates catabolite repression of UAS1 by responding to intracellular heme levels.	Heme	108-112	Hap1p	Saccharomyces cerevisiae S288C	0-4
28830930-6	2017	We found that heme induces transcription of HAP4, the transcriptional activation subunit of the Hap2/3/4/5p complex, required for growth on nonfermentable carbon sources, in a Hap1p- and Hap2/3/4/5p-dependent manner.	Heme	14-18	Hap1p	Saccharomyces cerevisiae S288C	176-181
29649251-9	2018	We also show that Hap1p-dependent cross protection relies on novel regulation of cytosolic catalase T (Ctt1p) during ethanol stress in a wild oak strain.	Ethanol	117-124	Hap1p	Saccharomyces cerevisiae S288C	18-23
28830930-8	2017	Increased heme synthesis, even under conditions of glucose repression, activated Hap1p and the Hap2/3/4/5p complex and induced transcription of HAP4 and genes required for the tricarboxylic acid (TCA) cycle, electron transport chain, and oxidative phosphorylation, leading to a switch from fermentation to respiration.	Heme	10-14	Hap1p	Saccharomyces cerevisiae S288C	81-86
21610214-3	2011	In addition, Tpa1 represses, by an unknown mechanism, genes regulated by Hap1, a transcription factor involved in the response to levels of heme and O(2).	Heme	140-144	Hap1p	Saccharomyces cerevisiae S288C	73-77
27247412-6	2016	We also find that the glycolytic enzyme glyceraldehyde phosphate dehydrogenase constitutes a major cellular heme buffer, and is responsible for maintaining the activity of the heme-dependent nuclear transcription factor heme activator protein (Hap1p).	Heme	108-112	Hap1p	Saccharomyces cerevisiae S288C	244-249
25082441-7	2015	In this study, we propose a strategy for further engineering S. cerevisiae by altering the oxygen sensing pathway by deleting the transcription factor HAP1, which resulted in an increase of the final recombinant active hemoglobin titer exceeding 7% of the total cellular protein.	Oxygen	91-97	Hap1p	Saccharomyces cerevisiae S288C	151-155
24911589-10	2014	Results demonstrated that the initial velocity pattern of this enzyme for the resorufin derivatives is different from the one described for most vertebrate CYP1As.	resorufin	78-87	Hap1p	Saccharomyces cerevisiae S288C	156-160
22703342-9	2013	Exposure to menadione and H2O2 enhanced both, Hap1-independent expression of ROX1 and Rox1 steady-state levels without affecting Ord1.	Vitamin K 3	12-21	Hap1p	Saccharomyces cerevisiae S288C	46-50
22703342-9	2013	Exposure to menadione and H2O2 enhanced both, Hap1-independent expression of ROX1 and Rox1 steady-state levels without affecting Ord1.	Hydrogen Peroxide	26-30	Hap1p	Saccharomyces cerevisiae S288C	46-50
29468124-5	2016	We demonstrate how Hap1p can activate a set of oxidative stress response genes and meanwhile contribute to increase the metabolic rate of the yeast strains, therefore mitigating the negative effect of the ROS accumulation associated to protein folding and hence increasing the production capacity during batch fermentations.	ros	205-208	Hap1p	Saccharomyces cerevisiae S288C	19-24
26231923-6	2015	RESULTS: CYP1s expressed in yeast dealkylated ethoxy-, methoxy-, pentoxy- and benzoxy-resorufin (EROD, MROD, PROD, BROD).	ethoxy-, methoxy-, pentoxy- and benzoxy-resorufin	46-95	Hap1p	Saccharomyces cerevisiae S288C	9-13
22703342-14	2013	CONCLUSION: ROS induce expression of hypoxic COX5b and CYC7 genes through an Ord1- and Hap1-independent mechanism that promotes the release of Rox1 from or limits the access of Rox1 to its hypoxic gene promoter targets.	Reactive Oxygen Species	12-15	Hap1p	Saccharomyces cerevisiae S288C	87-91
20630870-10	2010	In parallel, we show that Tpa1 represses the expression of genes regulated by Hap1, a transcription factor involved in the response to levels of heme and oxygen.	Heme	145-149	Hap1p	Saccharomyces cerevisiae S288C	78-82
20630870-10	2010	In parallel, we show that Tpa1 represses the expression of genes regulated by Hap1, a transcription factor involved in the response to levels of heme and oxygen.	Oxygen	154-160	Hap1p	Saccharomyces cerevisiae S288C	78-82
20008079-6	2010	As another example, decreased mRNA levels of the cytochrome c-encoding CYC1 gene under iron-limiting conditions involve heme-dependent transcriptional regulation via the Hap1 transcription factor.	Iron	87-91	Hap1p	Saccharomyces cerevisiae S288C	170-174
20008079-6	2010	As another example, decreased mRNA levels of the cytochrome c-encoding CYC1 gene under iron-limiting conditions involve heme-dependent transcriptional regulation via the Hap1 transcription factor.	Heme	120-124	Hap1p	Saccharomyces cerevisiae S288C	170-174