Glucokinase-1; Glucokinase; catalyzes the phosphorylation of glucose at C6 in the first irreversible step of glucose metabolism; one of three glucose phosphorylating enzymes; expression regulated by non-fermentable carbon sources; GLK1 has a paralog, EMI2, that arose from the whole genome duplication; Belongs to the hexokinase family.

ATP-dependent molecular chaperone HSP82; Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication.

Glucokinase-1; Glucokinase; catalyzes the phosphorylation of glucose at C6 in the first irreversible step of glucose metabolism; one of three glucose phosphorylating enzymes; expression regulated by non-fermentable carbon sources; GLK1 has a paralog, EMI2, that arose from the whole genome duplication; Belongs to the hexokinase family.

Mitochondrial porin (voltage-dependent anion channel); outer membrane protein required for maintenance of mitochondrial osmotic stability and mitochondrial membrane permeability; couples the glutathione pools of the intermembrane space (IMS) and the cytosol; interacts with Om45 and Om14 in the outer membrane; phosphorylated; protein abundance increases in response to DNA replication stress.

ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication.

ATP-dependent molecular chaperone HSP82; Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication.

ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication.

Mitochondrial porin (voltage-dependent anion channel); outer membrane protein required for maintenance of mitochondrial osmotic stability and mitochondrial membrane permeability; couples the glutathione pools of the intermembrane space (IMS) and the cytosol; interacts with Om45 and Om14 in the outer membrane; phosphorylated; protein abundance increases in response to DNA replication stress.

ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication.

Vesicular-fusion protein SEC18; AAA ATPase and SNARE disassembly chaperone; required for vesicular transport between ER and Golgi, the 'priming' step in homotypic vacuole fusion, autophagy, and protein secretion; releases Sec17p from SNAP complexes; has similarity to mammalian N-ethylmaleimide-sensitive factor (NSF).

ATP-dependent molecular chaperone HSP82; Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication.

Glucokinase-1; Glucokinase; catalyzes the phosphorylation of glucose at C6 in the first irreversible step of glucose metabolism; one of three glucose phosphorylating enzymes; expression regulated by non-fermentable carbon sources; GLK1 has a paralog, EMI2, that arose from the whole genome duplication; Belongs to the hexokinase family.

ATP-dependent molecular chaperone HSP82; Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication.

ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication.

ATP-dependent molecular chaperone HSP82; Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication.

Mitochondrial porin (voltage-dependent anion channel); outer membrane protein required for maintenance of mitochondrial osmotic stability and mitochondrial membrane permeability; couples the glutathione pools of the intermembrane space (IMS) and the cytosol; interacts with Om45 and Om14 in the outer membrane; phosphorylated; protein abundance increases in response to DNA replication stress.

ATP-dependent molecular chaperone HSP82; Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication.

Vesicular-fusion protein SEC18; AAA ATPase and SNARE disassembly chaperone; required for vesicular transport between ER and Golgi, the 'priming' step in homotypic vacuole fusion, autophagy, and protein secretion; releases Sec17p from SNAP complexes; has similarity to mammalian N-ethylmaleimide-sensitive factor (NSF).

Repressible vacuolar alkaline phosphatase; regulated by levels of Pi and by Pho4p, Pho9p, Pho80p, Pho81p and Pho85p; dephosphorylates phosphotyrosyl peptides; contributes to NAD+ metabolism by producing nicotinamide riboside from NMN.

Endopolyphosphatase; Dual endo- and exopolyphosphatase with a role in phosphate metabolism; acts as both an endopolyphosphatase cleaving long chains of polyphosphate distributively to generate shorter polymer chains and as an exopolyphosphatase catalyzing the hydrolysis of terminal phosphate from polyphosphate; localizes to the vacuole, nucleus and cytosol; functions as a homodimer; relocalizes from vacuole to cytoplasm upon DNA replication stress.

Repressible vacuolar alkaline phosphatase; regulated by levels of Pi and by Pho4p, Pho9p, Pho80p, Pho81p and Pho85p; dephosphorylates phosphotyrosyl peptides; contributes to NAD+ metabolism by producing nicotinamide riboside from NMN.

Vesicular-fusion protein SEC18; AAA ATPase and SNARE disassembly chaperone; required for vesicular transport between ER and Golgi, the 'priming' step in homotypic vacuole fusion, autophagy, and protein secretion; releases Sec17p from SNAP complexes; has similarity to mammalian N-ethylmaleimide-sensitive factor (NSF).

Repressible vacuolar alkaline phosphatase; regulated by levels of Pi and by Pho4p, Pho9p, Pho80p, Pho81p and Pho85p; dephosphorylates phosphotyrosyl peptides; contributes to NAD+ metabolism by producing nicotinamide riboside from NMN.

Regulatory subunit of the vacuolar transporter chaperone (VTC) complex; VTC complex is involved in membrane trafficking, vacuolar polyphosphate accumulation, microautophagy and non-autophagic vacuolar fusion; also has mRNA binding activity; protein abundance increases in response to DNA replication stress.

Repressible vacuolar alkaline phosphatase; regulated by levels of Pi and by Pho4p, Pho9p, Pho80p, Pho81p and Pho85p; dephosphorylates phosphotyrosyl peptides; contributes to NAD+ metabolism by producing nicotinamide riboside from NMN.

Regulatory subunit of the vacuolar transporter chaperone (VTC) complex; involved in membrane trafficking, vacuolar polyphosphate accumulation, microautophagy and non-autophagic vacuolar fusion; VTC3 has a paralog, VTC2, that arose from the whole genome duplication; Belongs to the VTC2/3 family.

Repressible vacuolar alkaline phosphatase; regulated by levels of Pi and by Pho4p, Pho9p, Pho80p, Pho81p and Pho85p; dephosphorylates phosphotyrosyl peptides; contributes to NAD+ metabolism by producing nicotinamide riboside from NMN.

Vacuolar transporter chaperone 4; Vacuolar membrane polyphosphate polymerase; subunit of the vacuolar transporter chaperone (VTC) complex involved in synthesis and transfer of polyP to the vacuole; regulates membrane trafficking; role in non-autophagic vacuolar fusion; protein abundance increases in response to DNA replication stress.

Repressible vacuolar alkaline phosphatase; regulated by levels of Pi and by Pho4p, Pho9p, Pho80p, Pho81p and Pho85p; dephosphorylates phosphotyrosyl peptides; contributes to NAD+ metabolism by producing nicotinamide riboside from NMN.

Putative metallophosphoesterase YNL217W; Putative protein of unknown function; weak sequence similarity to bis (5'-nucleotidyl)-tetraphosphatases; (GFP)-fusion protein localizes to the vacuole; null mutant is highly sensitive to azaserine and resistant to sodium-O-vandate.

Mitochondrial porin (voltage-dependent anion channel); outer membrane protein required for maintenance of mitochondrial osmotic stability and mitochondrial membrane permeability; couples the glutathione pools of the intermembrane space (IMS) and the cytosol; interacts with Om45 and Om14 in the outer membrane; phosphorylated; protein abundance increases in response to DNA replication stress.

Glucokinase-1; Glucokinase; catalyzes the phosphorylation of glucose at C6 in the first irreversible step of glucose metabolism; one of three glucose phosphorylating enzymes; expression regulated by non-fermentable carbon sources; GLK1 has a paralog, EMI2, that arose from the whole genome duplication; Belongs to the hexokinase family.

Mitochondrial porin (voltage-dependent anion channel); outer membrane protein required for maintenance of mitochondrial osmotic stability and mitochondrial membrane permeability; couples the glutathione pools of the intermembrane space (IMS) and the cytosol; interacts with Om45 and Om14 in the outer membrane; phosphorylated; protein abundance increases in response to DNA replication stress.

ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication.

Mitochondrial porin (voltage-dependent anion channel); outer membrane protein required for maintenance of mitochondrial osmotic stability and mitochondrial membrane permeability; couples the glutathione pools of the intermembrane space (IMS) and the cytosol; interacts with Om45 and Om14 in the outer membrane; phosphorylated; protein abundance increases in response to DNA replication stress.

ATP-dependent molecular chaperone HSP82; Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication.

Endopolyphosphatase; Dual endo- and exopolyphosphatase with a role in phosphate metabolism; acts as both an endopolyphosphatase cleaving long chains of polyphosphate distributively to generate shorter polymer chains and as an exopolyphosphatase catalyzing the hydrolysis of terminal phosphate from polyphosphate; localizes to the vacuole, nucleus and cytosol; functions as a homodimer; relocalizes from vacuole to cytoplasm upon DNA replication stress.

Repressible vacuolar alkaline phosphatase; regulated by levels of Pi and by Pho4p, Pho9p, Pho80p, Pho81p and Pho85p; dephosphorylates phosphotyrosyl peptides; contributes to NAD+ metabolism by producing nicotinamide riboside from NMN.

Endopolyphosphatase; Dual endo- and exopolyphosphatase with a role in phosphate metabolism; acts as both an endopolyphosphatase cleaving long chains of polyphosphate distributively to generate shorter polymer chains and as an exopolyphosphatase catalyzing the hydrolysis of terminal phosphate from polyphosphate; localizes to the vacuole, nucleus and cytosol; functions as a homodimer; relocalizes from vacuole to cytoplasm upon DNA replication stress.

Exopolyphosphatase; hydrolyzes inorganic polyphosphate (poly P) into Pi residues; located in the cytosol, plasma membrane, and mitochondrial matrix; Belongs to the PPase class C family.