PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
19033468-7	2008	We report here that the Ubr1 N-recognin, which conditionally targets Cup9 for degradation, is phosphorylated in vivo at multiple sites, including Ser(300) and Tyr(277).	Serine	146-149	Cup9p	Saccharomyces cerevisiae S288C	69-73
10850718-8	2000	We show that the degradation of Cup9 is allosterically activated by dipeptides with destabilizing N-terminal residues.	Dipeptides	68-78	Cup9p	Saccharomyces cerevisiae S288C	32-36
10850718-9	2000	In the resulting positive feedback circuit, imported dipeptides bind to Ubr1 and accelerate the Ubr1-dependent degradation of Cup9, thereby de-repressing the expression of Ptr2 and increasing the cell"s capacity to import peptides.	Dipeptides	53-63	Cup9p	Saccharomyces cerevisiae S288C	126-130
9427760-9	1998	An earlier study identified Cup9p as a protein required for an aspect of resistance to copper toxicity in S.cerevisiae.	Copper	87-93	Cup9p	Saccharomyces cerevisiae S288C	28-33
7969120-2	1994	Using an ethyl methanesulfonate mutant of a yeast strain in which CUP1 and ACE1 were deleted, we isolated a gene, designated CUP9, which permits yeast cells to grow at high concentrations of environmental copper, most notably when lactate is the sole carbon source.	Ethyl Methanesulfonate	9-31	Cup9p	Saccharomyces cerevisiae S288C	125-129
7969120-2	1994	Using an ethyl methanesulfonate mutant of a yeast strain in which CUP1 and ACE1 were deleted, we isolated a gene, designated CUP9, which permits yeast cells to grow at high concentrations of environmental copper, most notably when lactate is the sole carbon source.	Copper	205-211	Cup9p	Saccharomyces cerevisiae S288C	125-129
7969120-2	1994	Using an ethyl methanesulfonate mutant of a yeast strain in which CUP1 and ACE1 were deleted, we isolated a gene, designated CUP9, which permits yeast cells to grow at high concentrations of environmental copper, most notably when lactate is the sole carbon source.	Lactic Acid	231-238	Cup9p	Saccharomyces cerevisiae S288C	125-129
7969120-2	1994	Using an ethyl methanesulfonate mutant of a yeast strain in which CUP1 and ACE1 were deleted, we isolated a gene, designated CUP9, which permits yeast cells to grow at high concentrations of environmental copper, most notably when lactate is the sole carbon source.	Carbon	251-257	Cup9p	Saccharomyces cerevisiae S288C	125-129
7969120-3	1994	Disruption of CUP9, which is located on chromosome XVI, caused a loss of copper resistance in strains which possessed CUP1 and ACE1, as well as in the cup1 ace1 deletion strain.	Copper	73-79	Cup9p	Saccharomyces cerevisiae S288C	14-18
7969120-5	1994	CUP9 mRNA levels were, however, down regulated by copper when yeast cells were grown with glucose but not with lactate or glycerol-ethanol as the sole carbon source.	Copper	50-56	Cup9p	Saccharomyces cerevisiae S288C	0-4
7969120-5	1994	CUP9 mRNA levels were, however, down regulated by copper when yeast cells were grown with glucose but not with lactate or glycerol-ethanol as the sole carbon source.	Glucose	90-97	Cup9p	Saccharomyces cerevisiae S288C	0-4
7969120-5	1994	CUP9 mRNA levels were, however, down regulated by copper when yeast cells were grown with glucose but not with lactate or glycerol-ethanol as the sole carbon source.	Lactic Acid	111-118	Cup9p	Saccharomyces cerevisiae S288C	0-4
7969120-5	1994	CUP9 mRNA levels were, however, down regulated by copper when yeast cells were grown with glucose but not with lactate or glycerol-ethanol as the sole carbon source.	Carbon	151-157	Cup9p	Saccharomyces cerevisiae S288C	0-4
7969120-7	1994	The DNA sequence of CUP9 predicts an open reading frame of 306 amino acids in which a 55-amino-acid sequence showed 47% identity with the homeobox domain of the human proto-oncogene PBX1, suggesting that CUP9 is a DNA-binding protein which regulates the expression of important copper homeostatic genes.	Copper	278-284	Cup9p	Saccharomyces cerevisiae S288C	20-24
7969120-7	1994	The DNA sequence of CUP9 predicts an open reading frame of 306 amino acids in which a 55-amino-acid sequence showed 47% identity with the homeobox domain of the human proto-oncogene PBX1, suggesting that CUP9 is a DNA-binding protein which regulates the expression of important copper homeostatic genes.	Copper	278-284	Cup9p	Saccharomyces cerevisiae S288C	204-208
33989396-5	2021	However, a screen of mutants defective in transcription factor genes revealed that Cup9 is required for normal caspofungin tolerance under hyphal and not yeast growth conditions.	Caspofungin	111-122	Cup9p	Saccharomyces cerevisiae S288C	83-87
33989396-6	2021	In a hyphal-defective efg1Delta/Delta background, Cup9 is still required for normal caspofungin tolerance.	Caspofungin	84-95	Cup9p	Saccharomyces cerevisiae S288C	50-54
33989396-11	2021	Five Cup9-activated surface-protein genes have roles in cell wall integrity, based on mutant analysis published previously (PGA31, IFF11) or shown here (ORF19.3499, ORF19.851 or PGA28), and therefore may explain the hypersensitivity of the cup9Delta/Delta mutant to caspofungin.	Caspofungin	266-277	Cup9p	Saccharomyces cerevisiae S288C	5-9
33989396-12	2021	Our findings define Cup9 as a new determinant of caspofungin susceptibility.	Caspofungin	49-60	Cup9p	Saccharomyces cerevisiae S288C	20-24
19033468-7	2008	We report here that the Ubr1 N-recognin, which conditionally targets Cup9 for degradation, is phosphorylated in vivo at multiple sites, including Ser(300) and Tyr(277).	Tyrosine	159-162	Cup9p	Saccharomyces cerevisiae S288C	69-73
18708352-6	2008	These dipeptides bind to UBR1, the ubiquitin ligase of the N-end rule pathway, and allosterically accelerate the UBR1-dependent degradation of CUP9, a transcriptional repressor of PTR2.	Dipeptides	6-16	Cup9p	Saccharomyces cerevisiae S288C	143-147
18566452-10	2008	We show that the previously demonstrated in vivo dependence of CUP9 ubiquitylation on the binding of cognate dipeptides to the type-1/2 sites of UBR1 can be reconstituted in a completely defined in vitro system.	Dipeptides	109-119	Cup9p	Saccharomyces cerevisiae S288C	63-67
18566452-11	2008	We also found that purified UBR1 and CUP9 interact nonspecifically and that specific binding (which involves, in particular, the binding by cognate dipeptides to the UBR1 type-1/2 sites) can be restored either by a chaperone such as EF1A or through macromolecular crowding.	Dipeptides	148-158	Cup9p	Saccharomyces cerevisiae S288C	37-41
18162538-8	2008	We show that hemin does not directly occlude the substrate-binding sites of UBR1 but blocks the activation of its CUP9-binding site by dipeptides.	Hemin	13-18	Cup9p	Saccharomyces cerevisiae S288C	114-118
18162538-8	2008	We show that hemin does not directly occlude the substrate-binding sites of UBR1 but blocks the activation of its CUP9-binding site by dipeptides.	Dipeptides	135-145	Cup9p	Saccharomyces cerevisiae S288C	114-118
12391316-5	2002	Previous work demonstrated that dipeptides with destabilizing N-terminal residues allosterically activate UBR1, leading to accelerated in vivo degradation of CUP9 and the induction of PTR2 expression.	Dipeptides	32-42	Cup9p	Saccharomyces cerevisiae S288C	158-162
12391316-8	2002	This dissociation, which allows the interaction between UBR1 and CUP9, is strongly increased only if both type 1- and type 2-binding sites of UBR1 are occupied by dipeptides.	Dipeptides	163-173	Cup9p	Saccharomyces cerevisiae S288C	65-69