Mitochondrial distribution and morphology protein 12; Mitochondrial outer membrane protein, ERMES complex subunit; required for transmission of mitochondria to daughter cells; required for mitophagy; may influence import and assembly of outer membrane beta-barrel proteins; ERMES complex is often co-localized with peroxisomes and with concentrated areas of pyruvate dehydrogenase; Belongs to the MDM12 family.

Mitochondrial distribution and morphology protein 34; Mitochondrial component of the ERMES complex; links the ER to mitochondria and may promote inter-organellar calcium and phospholipid exchange as well as coordinating mitochondrial DNA replication and growth; required for mitophagy; ERMES complex is often co-localized with peroxisomes and with concentrated areas of pyruvate dehydrogenase.

Mitochondrial distribution and morphology protein 12; Mitochondrial outer membrane protein, ERMES complex subunit; required for transmission of mitochondria to daughter cells; required for mitophagy; may influence import and assembly of outer membrane beta-barrel proteins; ERMES complex is often co-localized with peroxisomes and with concentrated areas of pyruvate dehydrogenase; Belongs to the MDM12 family.

Uncharacterized PH domain-containing protein YPR091C; Lipid-binding ER protein, enriched at nucleus-vacuolar junctions (NVJ); may be involved in sterol metabolism or signaling at the NVJ; contains a synaptotagmin-like-mitochondrial-lipid binding protein (SMP) domain; binds phosphatidylinositols and other lipids in a large-scale study; may interact with ribosomes, based on co-purification experiments.

Mitochondrial distribution and morphology protein 34; Mitochondrial component of the ERMES complex; links the ER to mitochondria and may promote inter-organellar calcium and phospholipid exchange as well as coordinating mitochondrial DNA replication and growth; required for mitophagy; ERMES complex is often co-localized with peroxisomes and with concentrated areas of pyruvate dehydrogenase.

Mitochondrial distribution and morphology protein 12; Mitochondrial outer membrane protein, ERMES complex subunit; required for transmission of mitochondria to daughter cells; required for mitophagy; may influence import and assembly of outer membrane beta-barrel proteins; ERMES complex is often co-localized with peroxisomes and with concentrated areas of pyruvate dehydrogenase; Belongs to the MDM12 family.

Mitochondrial distribution and morphology protein 34; Mitochondrial component of the ERMES complex; links the ER to mitochondria and may promote inter-organellar calcium and phospholipid exchange as well as coordinating mitochondrial DNA replication and growth; required for mitophagy; ERMES complex is often co-localized with peroxisomes and with concentrated areas of pyruvate dehydrogenase.

Uncharacterized PH domain-containing protein YPR091C; Lipid-binding ER protein, enriched at nucleus-vacuolar junctions (NVJ); may be involved in sterol metabolism or signaling at the NVJ; contains a synaptotagmin-like-mitochondrial-lipid binding protein (SMP) domain; binds phosphatidylinositols and other lipids in a large-scale study; may interact with ribosomes, based on co-purification experiments.

Uncharacterized PH domain-containing protein YPR091C; Lipid-binding ER protein, enriched at nucleus-vacuolar junctions (NVJ); may be involved in sterol metabolism or signaling at the NVJ; contains a synaptotagmin-like-mitochondrial-lipid binding protein (SMP) domain; binds phosphatidylinositols and other lipids in a large-scale study; may interact with ribosomes, based on co-purification experiments.

Mitochondrial distribution and morphology protein 12; Mitochondrial outer membrane protein, ERMES complex subunit; required for transmission of mitochondria to daughter cells; required for mitophagy; may influence import and assembly of outer membrane beta-barrel proteins; ERMES complex is often co-localized with peroxisomes and with concentrated areas of pyruvate dehydrogenase; Belongs to the MDM12 family.

Uncharacterized PH domain-containing protein YPR091C; Lipid-binding ER protein, enriched at nucleus-vacuolar junctions (NVJ); may be involved in sterol metabolism or signaling at the NVJ; contains a synaptotagmin-like-mitochondrial-lipid binding protein (SMP) domain; binds phosphatidylinositols and other lipids in a large-scale study; may interact with ribosomes, based on co-purification experiments.

Mitochondrial distribution and morphology protein 34; Mitochondrial component of the ERMES complex; links the ER to mitochondria and may promote inter-organellar calcium and phospholipid exchange as well as coordinating mitochondrial DNA replication and growth; required for mitophagy; ERMES complex is often co-localized with peroxisomes and with concentrated areas of pyruvate dehydrogenase.

Uncharacterized PH domain-containing protein YPR091C; Lipid-binding ER protein, enriched at nucleus-vacuolar junctions (NVJ); may be involved in sterol metabolism or signaling at the NVJ; contains a synaptotagmin-like-mitochondrial-lipid binding protein (SMP) domain; binds phosphatidylinositols and other lipids in a large-scale study; may interact with ribosomes, based on co-purification experiments.

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.

Uncharacterized PH domain-containing protein YPR091C; Lipid-binding ER protein, enriched at nucleus-vacuolar junctions (NVJ); may be involved in sterol metabolism or signaling at the NVJ; contains a synaptotagmin-like-mitochondrial-lipid binding protein (SMP) domain; binds phosphatidylinositols and other lipids in a large-scale study; may interact with ribosomes, based on co-purification experiments.

Tricalbin-1; Lipid-binding ER protein involved in ER-plasma membrane tethering; one of 6 proteins (Ist2p, Scs2p, Scs22p, Tcb1p, Tcb2p, Tcb3p) that connect ER to plasma membrane and regulate PI4P levels by controlling access of Sac1p phosphatase to its substrate PI4P in PM; contains 3 calcium and lipid binding domains; non-tagged protein also localizes to mitochondria; C-termini of Tcb1p, Tcb2p and Tcb3p interact; TCB1 has a paralog, TCB2, that arose from the whole genome duplication; Belongs to the tricalbin family.

Uncharacterized PH domain-containing protein YPR091C; Lipid-binding ER protein, enriched at nucleus-vacuolar junctions (NVJ); may be involved in sterol metabolism or signaling at the NVJ; contains a synaptotagmin-like-mitochondrial-lipid binding protein (SMP) domain; binds phosphatidylinositols and other lipids in a large-scale study; may interact with ribosomes, based on co-purification experiments.

Tricalbin-2; ER protein involved in ER-plasma membrane tethering; one of 6 proteins (Ist2p, Scs2p, Scs22p, Tcb1p, Tcb2p, Tcb3p) that connect ER to plasma membrane (PM) and regulate PM phosphatidylinositol-4-phosphate (PI4P) levels by controlling access of Sac1p phosphatase to its substrate PI4P in the PM; contains 3 calcium and lipid binding domains; mRNA is targeted to bud; TCB2 has a paralog, TCB1, that arose from the whole genome duplication.

Uncharacterized PH domain-containing protein YPR091C; Lipid-binding ER protein, enriched at nucleus-vacuolar junctions (NVJ); may be involved in sterol metabolism or signaling at the NVJ; contains a synaptotagmin-like-mitochondrial-lipid binding protein (SMP) domain; binds phosphatidylinositols and other lipids in a large-scale study; may interact with ribosomes, based on co-purification experiments.

Tricalbin-3; Cortical ER protein involved in ER-plasma membrane tethering; one of 6 proteins (Ist2p, Scs2p, Scs22p, Tcb1p, Tcb2p, Tcb3p) that connect ER to the plasma membrane (PM) and regulate PM phosphatidylinositol-4-phosphate (PI4P) levels by controlling access of Sac1p phosphatase to its substrate PI4P in the PM; localized to the bud via specific mRNA transport; non-tagged protein detected in a phosphorylated state in mitochondria; C-termini of Tcb1p, Tcb2p and Tcb3p interact; Belongs to the tricalbin family.

Member of an oxysterol-binding protein family; this family has seven members in S. cerevisiae; family members have overlapping, redundant functions in sterol metabolism and collectively perform a function essential for viability; contains FFAT motif; interacts with ER anchor Scs2p at patches at the plasma membrane; regulated by sterol binding; Belongs to the OSBP 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.

Member of an oxysterol-binding protein family; this family has seven members in S. cerevisiae; family members have overlapping, redundant functions in sterol metabolism and collectively perform a function essential for viability; contains FFAT motif; interacts with ER anchor Scs2p at patches at the plasma membrane; regulated by sterol binding; Belongs to the OSBP 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.

Member of an oxysterol-binding protein family; this family has seven members in S. cerevisiae; family members have overlapping, redundant functions in sterol metabolism and collectively perform a function essential for viability; contains FFAT motif; interacts with ER anchor Scs2p at patches at the plasma membrane; regulated by sterol binding; Belongs to the OSBP family.

Tricalbin-1; Lipid-binding ER protein involved in ER-plasma membrane tethering; one of 6 proteins (Ist2p, Scs2p, Scs22p, Tcb1p, Tcb2p, Tcb3p) that connect ER to plasma membrane and regulate PI4P levels by controlling access of Sac1p phosphatase to its substrate PI4P in PM; contains 3 calcium and lipid binding domains; non-tagged protein also localizes to mitochondria; C-termini of Tcb1p, Tcb2p and Tcb3p interact; TCB1 has a paralog, TCB2, that arose from the whole genome duplication; Belongs to the tricalbin family.

Member of an oxysterol-binding protein family; this family has seven members in S. cerevisiae; family members have overlapping, redundant functions in sterol metabolism and collectively perform a function essential for viability; contains FFAT motif; interacts with ER anchor Scs2p at patches at the plasma membrane; regulated by sterol binding; Belongs to the OSBP family.

Tricalbin-2; ER protein involved in ER-plasma membrane tethering; one of 6 proteins (Ist2p, Scs2p, Scs22p, Tcb1p, Tcb2p, Tcb3p) that connect ER to plasma membrane (PM) and regulate PM phosphatidylinositol-4-phosphate (PI4P) levels by controlling access of Sac1p phosphatase to its substrate PI4P in the PM; contains 3 calcium and lipid binding domains; mRNA is targeted to bud; TCB2 has a paralog, TCB1, that arose from the whole genome duplication.

Member of an oxysterol-binding protein family; this family has seven members in S. cerevisiae; family members have overlapping, redundant functions in sterol metabolism and collectively perform a function essential for viability; contains FFAT motif; interacts with ER anchor Scs2p at patches at the plasma membrane; regulated by sterol binding; Belongs to the OSBP family.

Tricalbin-3; Cortical ER protein involved in ER-plasma membrane tethering; one of 6 proteins (Ist2p, Scs2p, Scs22p, Tcb1p, Tcb2p, Tcb3p) that connect ER to the plasma membrane (PM) and regulate PM phosphatidylinositol-4-phosphate (PI4P) levels by controlling access of Sac1p phosphatase to its substrate PI4P in the PM; localized to the bud via specific mRNA transport; non-tagged protein detected in a phosphorylated state in mitochondria; C-termini of Tcb1p, Tcb2p and Tcb3p interact; Belongs to the tricalbin family.

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.

Member of an oxysterol-binding protein family; this family has seven members in S. cerevisiae; family members have overlapping, redundant functions in sterol metabolism and collectively perform a function essential for viability; contains FFAT motif; interacts with ER anchor Scs2p at patches at the plasma membrane; regulated by sterol binding; Belongs to the OSBP family.