Phosphatidylinositol transfer protein; has a potential role in regulating lipid and fatty acid metabolism under heme-depleted conditions; interacts specifically with thioredoxin peroxidase; may have a role in oxidative stress resistance; protein abundance increases in response to DNA replication stress; Belongs to the PITP family.

SEC14 cytosolic factor; Phosphatidylinositol/phosphatidylcholine transfer protein; involved in regulating PtdIns, PtdCho, and ceramide metabolism, products of which regulate intracellular transport and UPR; has a role in localization of lipid raft proteins; functionally homologous to mammalian PITPs; SEC14 has a paralog, YKL091C, that arose from the whole genome duplication.

Phosphatidylinositol transfer protein; has a potential role in regulating lipid and fatty acid metabolism under heme-depleted conditions; interacts specifically with thioredoxin peroxidase; may have a role in oxidative stress resistance; protein abundance increases in response to DNA replication stress; Belongs to the PITP family.

Non-classical phosphatidylinositol transfer protein (PITP); exhibits PI- but not PC-transfer activity; localizes to the peripheral endoplasmic reticulum, cytosol and microsomes; similar to Sec14p; partially relocalizes to the plasma membrane upon DNA replication stress.

Non-essential protein of unknown function; promoter contains a consensus binding sequence for factor Abf1p.

Inhibitory regulator protein IRA2; GTPase-activating protein; negatively regulates RAS by converting it from the GTP- to the GDP-bound inactive form, required for reducing cAMP levels under nutrient limiting conditions; IRA2 has a paralog, IRA1, that arose from the whole genome duplication; defects in human homolog NF1 are associated with neurofibromatosis.

Inhibitory regulator protein IRA1; GTPase-activating protein; negatively regulates RAS by converting it from GTP- to the GDP-bound inactive form, required for reducing cAMP levels under nutrient limiting conditions, mediates membrane association of adenylate cyclase; mutations cause catalase T deficiency, defective glycogen synthesis and defective trehalose accumulation; IRA1 has a paralog, IRA2, that arose from the whole genome duplication; defects in human homolog NF1 are associated with neurofibromatosis.

Inhibitory regulator protein IRA2; GTPase-activating protein; negatively regulates RAS by converting it from the GTP- to the GDP-bound inactive form, required for reducing cAMP levels under nutrient limiting conditions; IRA2 has a paralog, IRA1, that arose from the whole genome duplication; defects in human homolog NF1 are associated with neurofibromatosis.

Inhibitory regulator protein IRA2; GTPase-activating protein; negatively regulates RAS by converting it from the GTP- to the GDP-bound inactive form, required for reducing cAMP levels under nutrient limiting conditions; IRA2 has a paralog, IRA1, that arose from the whole genome duplication; defects in human homolog NF1 are associated with neurofibromatosis.

Non-essential protein of unknown function; promoter contains a consensus binding sequence for factor Abf1p.

Inhibitory regulator protein IRA2; GTPase-activating protein; negatively regulates RAS by converting it from the GTP- to the GDP-bound inactive form, required for reducing cAMP levels under nutrient limiting conditions; IRA2 has a paralog, IRA1, that arose from the whole genome duplication; defects in human homolog NF1 are associated with neurofibromatosis.

Inhibitory regulator protein IRA1; GTPase-activating protein; negatively regulates RAS by converting it from GTP- to the GDP-bound inactive form, required for reducing cAMP levels under nutrient limiting conditions, mediates membrane association of adenylate cyclase; mutations cause catalase T deficiency, defective glycogen synthesis and defective trehalose accumulation; IRA1 has a paralog, IRA2, that arose from the whole genome duplication; defects in human homolog NF1 are associated with neurofibromatosis.

Phosphatidylinositol transfer protein (PITP); controlled by the multiple drug resistance regulator Pdr1p; localizes to lipid particles and microsomes; controls levels of various lipids, may regulate lipid synthesis; homologous to Pdr17p; protein abundance increases in response to DNA replication stress.

SEC14 cytosolic factor; Phosphatidylinositol/phosphatidylcholine transfer protein; involved in regulating PtdIns, PtdCho, and ceramide metabolism, products of which regulate intracellular transport and UPR; has a role in localization of lipid raft proteins; functionally homologous to mammalian PITPs; SEC14 has a paralog, YKL091C, that arose from the whole genome duplication.

Phosphatidylinositol transfer protein (PITP); controlled by the multiple drug resistance regulator Pdr1p; localizes to lipid particles and microsomes; controls levels of various lipids, may regulate lipid synthesis; homologous to Pdr17p; protein abundance increases in response to DNA replication stress.

Non-classical phosphatidylinositol transfer protein (PITP); exhibits PI- but not PC-transfer activity; localizes to the peripheral endoplasmic reticulum, cytosol and microsomes; similar to Sec14p; partially relocalizes to the plasma membrane upon DNA replication stress.

Phosphatidylinositol transfer protein (PITP); downregulates Plb1p-mediated turnover of phosphatidylcholine; forms a complex with Psd2p which appears essential for maintenance of vacuolar PE levels; found in the cytosol and microsomes; homologous to Pdr16p; deletion affects phospholipid composition.

SEC14 cytosolic factor; Phosphatidylinositol/phosphatidylcholine transfer protein; involved in regulating PtdIns, PtdCho, and ceramide metabolism, products of which regulate intracellular transport and UPR; has a role in localization of lipid raft proteins; functionally homologous to mammalian PITPs; SEC14 has a paralog, YKL091C, that arose from the whole genome duplication.

Phosphatidylinositol transfer protein (PITP); downregulates Plb1p-mediated turnover of phosphatidylcholine; forms a complex with Psd2p which appears essential for maintenance of vacuolar PE levels; found in the cytosol and microsomes; homologous to Pdr16p; deletion affects phospholipid composition.

Non-classical phosphatidylinositol transfer protein (PITP); exhibits PI- but not PC-transfer activity; localizes to the peripheral endoplasmic reticulum, cytosol and microsomes; similar to Sec14p; partially relocalizes to the plasma membrane upon DNA replication stress.

SEC14 cytosolic factor; Phosphatidylinositol/phosphatidylcholine transfer protein; involved in regulating PtdIns, PtdCho, and ceramide metabolism, products of which regulate intracellular transport and UPR; has a role in localization of lipid raft proteins; functionally homologous to mammalian PITPs; SEC14 has a paralog, YKL091C, that arose from the whole genome duplication.

Phosphatidylinositol transfer protein; has a potential role in regulating lipid and fatty acid metabolism under heme-depleted conditions; interacts specifically with thioredoxin peroxidase; may have a role in oxidative stress resistance; protein abundance increases in response to DNA replication stress; Belongs to the PITP family.

SEC14 cytosolic factor; Phosphatidylinositol/phosphatidylcholine transfer protein; involved in regulating PtdIns, PtdCho, and ceramide metabolism, products of which regulate intracellular transport and UPR; has a role in localization of lipid raft proteins; functionally homologous to mammalian PITPs; SEC14 has a paralog, YKL091C, that arose from the whole genome duplication.

Phosphatidylinositol transfer protein (PITP); controlled by the multiple drug resistance regulator Pdr1p; localizes to lipid particles and microsomes; controls levels of various lipids, may regulate lipid synthesis; homologous to Pdr17p; protein abundance increases in response to DNA replication stress.

SEC14 cytosolic factor; Phosphatidylinositol/phosphatidylcholine transfer protein; involved in regulating PtdIns, PtdCho, and ceramide metabolism, products of which regulate intracellular transport and UPR; has a role in localization of lipid raft proteins; functionally homologous to mammalian PITPs; SEC14 has a paralog, YKL091C, that arose from the whole genome duplication.

Phosphatidylinositol transfer protein (PITP); downregulates Plb1p-mediated turnover of phosphatidylcholine; forms a complex with Psd2p which appears essential for maintenance of vacuolar PE levels; found in the cytosol and microsomes; homologous to Pdr16p; deletion affects phospholipid composition.

SEC14 cytosolic factor; Phosphatidylinositol/phosphatidylcholine transfer protein; involved in regulating PtdIns, PtdCho, and ceramide metabolism, products of which regulate intracellular transport and UPR; has a role in localization of lipid raft proteins; functionally homologous to mammalian PITPs; SEC14 has a paralog, YKL091C, that arose from the whole genome duplication.

Non-classical phosphatidylinositol transfer protein (PITP); exhibits PI- but not PC-transfer activity; localizes to the peripheral endoplasmic reticulum, cytosol and microsomes; similar to Sec14p; partially relocalizes to the plasma membrane upon DNA replication stress.

SEC14 cytosolic factor; Phosphatidylinositol/phosphatidylcholine transfer protein; involved in regulating PtdIns, PtdCho, and ceramide metabolism, products of which regulate intracellular transport and UPR; has a role in localization of lipid raft proteins; functionally homologous to mammalian PITPs; SEC14 has a paralog, YKL091C, that arose from the whole genome duplication.

CRAL-TRIO domain-containing protein YKL091C; Putative phosphatidylinositol/phosphatidylcholine transfer protein; possibly involved in lipid metabolism; localizes to the nucleus; contains a CRAL/TRIO domain and binds several lipids in a large-scale study; YKL091C has a paralog, SEC14, that arose from the whole genome duplication.

Non-classical phosphatidylinositol transfer protein (PITP); exhibits PI- but not PC-transfer activity; localizes to the peripheral endoplasmic reticulum, cytosol and microsomes; similar to Sec14p; partially relocalizes to the plasma membrane upon DNA replication stress.

Phosphatidylinositol transfer protein; has a potential role in regulating lipid and fatty acid metabolism under heme-depleted conditions; interacts specifically with thioredoxin peroxidase; may have a role in oxidative stress resistance; protein abundance increases in response to DNA replication stress; Belongs to the PITP family.

Non-classical phosphatidylinositol transfer protein (PITP); exhibits PI- but not PC-transfer activity; localizes to the peripheral endoplasmic reticulum, cytosol and microsomes; similar to Sec14p; partially relocalizes to the plasma membrane upon DNA replication stress.

Phosphatidylinositol transfer protein (PITP); controlled by the multiple drug resistance regulator Pdr1p; localizes to lipid particles and microsomes; controls levels of various lipids, may regulate lipid synthesis; homologous to Pdr17p; protein abundance increases in response to DNA replication stress.

Non-classical phosphatidylinositol transfer protein (PITP); exhibits PI- but not PC-transfer activity; localizes to the peripheral endoplasmic reticulum, cytosol and microsomes; similar to Sec14p; partially relocalizes to the plasma membrane upon DNA replication stress.

Phosphatidylinositol transfer protein (PITP); downregulates Plb1p-mediated turnover of phosphatidylcholine; forms a complex with Psd2p which appears essential for maintenance of vacuolar PE levels; found in the cytosol and microsomes; homologous to Pdr16p; deletion affects phospholipid composition.

Non-classical phosphatidylinositol transfer protein (PITP); exhibits PI- but not PC-transfer activity; localizes to the peripheral endoplasmic reticulum, cytosol and microsomes; similar to Sec14p; partially relocalizes to the plasma membrane upon DNA replication stress.

SEC14 cytosolic factor; Phosphatidylinositol/phosphatidylcholine transfer protein; involved in regulating PtdIns, PtdCho, and ceramide metabolism, products of which regulate intracellular transport and UPR; has a role in localization of lipid raft proteins; functionally homologous to mammalian PITPs; SEC14 has a paralog, YKL091C, that arose from the whole genome duplication.

Non-classical phosphatidylinositol transfer protein (PITP); exhibits PI- but not PC-transfer activity; localizes to the peripheral endoplasmic reticulum, cytosol and microsomes; similar to Sec14p; partially relocalizes to the plasma membrane upon DNA replication stress.

CRAL-TRIO domain-containing protein YKL091C; Putative phosphatidylinositol/phosphatidylcholine transfer protein; possibly involved in lipid metabolism; localizes to the nucleus; contains a CRAL/TRIO domain and binds several lipids in a large-scale study; YKL091C has a paralog, SEC14, that arose from the whole genome duplication.