Protein phosphatase; involved in downregulation of the unfolded protein response (UPR), at least in part through dephosphorylation of Ire1p; dosage-dependent positive regulator of the G1/S phase transition through control of the timing of START; physically interacts with, dephosphorylates and destabilizes Sic1p; SWAT-GFP and mCherry fusion proteins localize to the vacuole.

Serine/threonine-protein phosphatase PP1-2; Type 1 S/T protein phosphatase (PP1) catalytic subunit; involved in glycogen metabolism, sporulation and mitotic progression; interacts with multiple regulatory subunits; regulates actomyosin ring formation; subunit of CPF; recruited to mating projections by Afr1p interaction; regulates nucleocytoplasmic shuttling of Hxk2p; import into the nucleus is inhibited during spindle assembly checkpoint arrest; involved in dephosphorylating Rps6a/b and Bnr1p.

Protein phosphatase; involved in downregulation of the unfolded protein response (UPR), at least in part through dephosphorylation of Ire1p; dosage-dependent positive regulator of the G1/S phase transition through control of the timing of START; physically interacts with, dephosphorylates and destabilizes Sic1p; SWAT-GFP and mCherry fusion proteins localize to the vacuole.

Protein ROD1; Alpha-arrestin involved in ubiquitin-dependent endocytosis; activating dephosphorylation relays glucose signaling to transporter endocytosis; calcineurin dephosphorylation is required for Rsp5p-dependent internalization of agonist-occupied Ste2p, as part of signal desensitization; recruits Rsp5p to Ste2p via its 2 PPXY motifs; protein abundance increases in response to DNA replication stress; ROD1 has a paralog, ROG3, that arose from the whole genome duplication.

Serine/threonine-protein kinase ELM1; Serine/threonine protein kinase; regulates the orientation checkpoint, the morphogenesis checkpoint and the metabolic switch from fermentative to oxidative metabolism by phosphorylating the activation loop of Kin4p, Hsl1p and Snf4p respectively; cooperates with Hsl7p in recruiting Hsl1p to the septin ring, a prerequisite for subsequent recruitment, phosphorylation, and degradation of Swe1p; forms part of the bud neck ring; regulates cytokinesis.

One of three possible beta-subunits of the Snf1 kinase complex; allows nuclear localization of the Snf1 kinase complex in the presence of a nonfermentable carbon source; necessary and sufficient for phosphorylation of the Mig2p transcription factor in response to alkaline stress; functionally redundant with SIP1 and SIP2 for the phosphorylation of Mig1p in response to glucose deprivation; contains a glycogen-binding domain.

Serine/threonine-protein kinase ELM1; Serine/threonine protein kinase; regulates the orientation checkpoint, the morphogenesis checkpoint and the metabolic switch from fermentative to oxidative metabolism by phosphorylating the activation loop of Kin4p, Hsl1p and Snf4p respectively; cooperates with Hsl7p in recruiting Hsl1p to the septin ring, a prerequisite for subsequent recruitment, phosphorylation, and degradation of Swe1p; forms part of the bud neck ring; regulates cytokinesis.

Serine/threonine-protein phosphatase PP1-2; Type 1 S/T protein phosphatase (PP1) catalytic subunit; involved in glycogen metabolism, sporulation and mitotic progression; interacts with multiple regulatory subunits; regulates actomyosin ring formation; subunit of CPF; recruited to mating projections by Afr1p interaction; regulates nucleocytoplasmic shuttling of Hxk2p; import into the nucleus is inhibited during spindle assembly checkpoint arrest; involved in dephosphorylating Rps6a/b and Bnr1p.

Serine/threonine-protein kinase ELM1; Serine/threonine protein kinase; regulates the orientation checkpoint, the morphogenesis checkpoint and the metabolic switch from fermentative to oxidative metabolism by phosphorylating the activation loop of Kin4p, Hsl1p and Snf4p respectively; cooperates with Hsl7p in recruiting Hsl1p to the septin ring, a prerequisite for subsequent recruitment, phosphorylation, and degradation of Swe1p; forms part of the bud neck ring; regulates cytokinesis.

Upstream serine/threonine kinase for the SNF1 complex; plays a role in pseudohyphal groth; partially redundant with Elm1p and Tos3p; members of this family have functional orthology with LKB1, a mammalian kinase associated with Peutz-Jeghers cancer-susceptibility syndrome; SAK1 has a paralog, TOS3, that arose from the whole genome duplication.

Serine/threonine-protein kinase ELM1; Serine/threonine protein kinase; regulates the orientation checkpoint, the morphogenesis checkpoint and the metabolic switch from fermentative to oxidative metabolism by phosphorylating the activation loop of Kin4p, Hsl1p and Snf4p respectively; cooperates with Hsl7p in recruiting Hsl1p to the septin ring, a prerequisite for subsequent recruitment, phosphorylation, and degradation of Swe1p; forms part of the bud neck ring; regulates cytokinesis.

Alternate beta-subunit of the Snf1p kinase complex; may confer substrate specificity; vacuolar protein containing KIS (Kinase-Interacting Sequence) and ASC (Association with Snf1 kinase Complex) domains involved in protein interactions.

Serine/threonine-protein kinase ELM1; Serine/threonine protein kinase; regulates the orientation checkpoint, the morphogenesis checkpoint and the metabolic switch from fermentative to oxidative metabolism by phosphorylating the activation loop of Kin4p, Hsl1p and Snf4p respectively; cooperates with Hsl7p in recruiting Hsl1p to the septin ring, a prerequisite for subsequent recruitment, phosphorylation, and degradation of Swe1p; forms part of the bud neck ring; regulates cytokinesis.

One of three beta subunits of the Snf1 kinase complex; involved in the response to glucose starvation; null mutants exhibit accelerated aging; N-myristoylprotein localized to the cytoplasm and the plasma membrane; SIP2 has a paralog, GAL83, that arose from the whole genome duplication.

Serine/threonine-protein kinase ELM1; Serine/threonine protein kinase; regulates the orientation checkpoint, the morphogenesis checkpoint and the metabolic switch from fermentative to oxidative metabolism by phosphorylating the activation loop of Kin4p, Hsl1p and Snf4p respectively; cooperates with Hsl7p in recruiting Hsl1p to the septin ring, a prerequisite for subsequent recruitment, phosphorylation, and degradation of Swe1p; forms part of the bud neck ring; regulates cytokinesis.

AMP-activated S/T protein kinase; forms a complex with Snf4p and members of the Sip1p/Sip2p/Gal83p family; required for transcription of glucose-repressed genes, thermotolerance, sporulation, and peroxisome biogenesis; regulates nucleocytoplasmic shuttling of Hxk2p; regulates filamentous growth and acts as a non-canonical GEF, activating Arf3p during invasive growth; SUMOylation by Mms21p inhibits its function and targets Snf1p for destruction via the Slx5-Slx8 Ub ligase.

Serine/threonine-protein kinase ELM1; Serine/threonine protein kinase; regulates the orientation checkpoint, the morphogenesis checkpoint and the metabolic switch from fermentative to oxidative metabolism by phosphorylating the activation loop of Kin4p, Hsl1p and Snf4p respectively; cooperates with Hsl7p in recruiting Hsl1p to the septin ring, a prerequisite for subsequent recruitment, phosphorylation, and degradation of Swe1p; forms part of the bud neck ring; regulates cytokinesis.

Activating gamma subunit of the AMP-activated Snf1p kinase complex; additional subunits of the complex are Snf1p and a Sip1p/Sip2p/Gal83p family member; activates glucose-repressed genes, represses glucose-induced genes; role in sporulation, and peroxisome biogenesis; protein abundance increases in response to DNA replication stress.

Serine/threonine-protein kinase ELM1; Serine/threonine protein kinase; regulates the orientation checkpoint, the morphogenesis checkpoint and the metabolic switch from fermentative to oxidative metabolism by phosphorylating the activation loop of Kin4p, Hsl1p and Snf4p respectively; cooperates with Hsl7p in recruiting Hsl1p to the septin ring, a prerequisite for subsequent recruitment, phosphorylation, and degradation of Swe1p; forms part of the bud neck ring; regulates cytokinesis.

Serine/threonine-protein kinase TOS3; Protein kinase; related to and functionally redundant with Elm1p and Sak1p for the phosphorylation and activation of Snf1p; functionally orthologous to LKB1, a mammalian kinase associated with Peutz-Jeghers cancer-susceptibility syndrome; TOS3 has a paralog, SAK1, that arose from the whole genome duplication.

One of three possible beta-subunits of the Snf1 kinase complex; allows nuclear localization of the Snf1 kinase complex in the presence of a nonfermentable carbon source; necessary and sufficient for phosphorylation of the Mig2p transcription factor in response to alkaline stress; functionally redundant with SIP1 and SIP2 for the phosphorylation of Mig1p in response to glucose deprivation; contains a glycogen-binding domain.

Serine/threonine-protein kinase ELM1; Serine/threonine protein kinase; regulates the orientation checkpoint, the morphogenesis checkpoint and the metabolic switch from fermentative to oxidative metabolism by phosphorylating the activation loop of Kin4p, Hsl1p and Snf4p respectively; cooperates with Hsl7p in recruiting Hsl1p to the septin ring, a prerequisite for subsequent recruitment, phosphorylation, and degradation of Swe1p; forms part of the bud neck ring; regulates cytokinesis.

One of three possible beta-subunits of the Snf1 kinase complex; allows nuclear localization of the Snf1 kinase complex in the presence of a nonfermentable carbon source; necessary and sufficient for phosphorylation of the Mig2p transcription factor in response to alkaline stress; functionally redundant with SIP1 and SIP2 for the phosphorylation of Mig1p in response to glucose deprivation; contains a glycogen-binding domain.

Serine/threonine-protein phosphatase PP1-2; Type 1 S/T protein phosphatase (PP1) catalytic subunit; involved in glycogen metabolism, sporulation and mitotic progression; interacts with multiple regulatory subunits; regulates actomyosin ring formation; subunit of CPF; recruited to mating projections by Afr1p interaction; regulates nucleocytoplasmic shuttling of Hxk2p; import into the nucleus is inhibited during spindle assembly checkpoint arrest; involved in dephosphorylating Rps6a/b and Bnr1p.

One of three possible beta-subunits of the Snf1 kinase complex; allows nuclear localization of the Snf1 kinase complex in the presence of a nonfermentable carbon source; necessary and sufficient for phosphorylation of the Mig2p transcription factor in response to alkaline stress; functionally redundant with SIP1 and SIP2 for the phosphorylation of Mig1p in response to glucose deprivation; contains a glycogen-binding domain.

Upstream serine/threonine kinase for the SNF1 complex; plays a role in pseudohyphal groth; partially redundant with Elm1p and Tos3p; members of this family have functional orthology with LKB1, a mammalian kinase associated with Peutz-Jeghers cancer-susceptibility syndrome; SAK1 has a paralog, TOS3, that arose from the whole genome duplication.

One of three possible beta-subunits of the Snf1 kinase complex; allows nuclear localization of the Snf1 kinase complex in the presence of a nonfermentable carbon source; necessary and sufficient for phosphorylation of the Mig2p transcription factor in response to alkaline stress; functionally redundant with SIP1 and SIP2 for the phosphorylation of Mig1p in response to glucose deprivation; contains a glycogen-binding domain.

Alternate beta-subunit of the Snf1p kinase complex; may confer substrate specificity; vacuolar protein containing KIS (Kinase-Interacting Sequence) and ASC (Association with Snf1 kinase Complex) domains involved in protein interactions.

One of three possible beta-subunits of the Snf1 kinase complex; allows nuclear localization of the Snf1 kinase complex in the presence of a nonfermentable carbon source; necessary and sufficient for phosphorylation of the Mig2p transcription factor in response to alkaline stress; functionally redundant with SIP1 and SIP2 for the phosphorylation of Mig1p in response to glucose deprivation; contains a glycogen-binding domain.

One of three beta subunits of the Snf1 kinase complex; involved in the response to glucose starvation; null mutants exhibit accelerated aging; N-myristoylprotein localized to the cytoplasm and the plasma membrane; SIP2 has a paralog, GAL83, that arose from the whole genome duplication.

One of three possible beta-subunits of the Snf1 kinase complex; allows nuclear localization of the Snf1 kinase complex in the presence of a nonfermentable carbon source; necessary and sufficient for phosphorylation of the Mig2p transcription factor in response to alkaline stress; functionally redundant with SIP1 and SIP2 for the phosphorylation of Mig1p in response to glucose deprivation; contains a glycogen-binding domain.

AMP-activated S/T protein kinase; forms a complex with Snf4p and members of the Sip1p/Sip2p/Gal83p family; required for transcription of glucose-repressed genes, thermotolerance, sporulation, and peroxisome biogenesis; regulates nucleocytoplasmic shuttling of Hxk2p; regulates filamentous growth and acts as a non-canonical GEF, activating Arf3p during invasive growth; SUMOylation by Mms21p inhibits its function and targets Snf1p for destruction via the Slx5-Slx8 Ub ligase.

One of three possible beta-subunits of the Snf1 kinase complex; allows nuclear localization of the Snf1 kinase complex in the presence of a nonfermentable carbon source; necessary and sufficient for phosphorylation of the Mig2p transcription factor in response to alkaline stress; functionally redundant with SIP1 and SIP2 for the phosphorylation of Mig1p in response to glucose deprivation; contains a glycogen-binding domain.

Activating gamma subunit of the AMP-activated Snf1p kinase complex; additional subunits of the complex are Snf1p and a Sip1p/Sip2p/Gal83p family member; activates glucose-repressed genes, represses glucose-induced genes; role in sporulation, and peroxisome biogenesis; protein abundance increases in response to DNA replication stress.

One of three possible beta-subunits of the Snf1 kinase complex; allows nuclear localization of the Snf1 kinase complex in the presence of a nonfermentable carbon source; necessary and sufficient for phosphorylation of the Mig2p transcription factor in response to alkaline stress; functionally redundant with SIP1 and SIP2 for the phosphorylation of Mig1p in response to glucose deprivation; contains a glycogen-binding domain.

Serine/threonine-protein kinase TOS3; Protein kinase; related to and functionally redundant with Elm1p and Sak1p for the phosphorylation and activation of Snf1p; functionally orthologous to LKB1, a mammalian kinase associated with Peutz-Jeghers cancer-susceptibility syndrome; TOS3 has a paralog, SAK1, that arose from the whole genome duplication.

Serine/threonine-protein phosphatase PP1-2; Type 1 S/T protein phosphatase (PP1) catalytic subunit; involved in glycogen metabolism, sporulation and mitotic progression; interacts with multiple regulatory subunits; regulates actomyosin ring formation; subunit of CPF; recruited to mating projections by Afr1p interaction; regulates nucleocytoplasmic shuttling of Hxk2p; import into the nucleus is inhibited during spindle assembly checkpoint arrest; involved in dephosphorylating Rps6a/b and Bnr1p.

Protein phosphatase; involved in downregulation of the unfolded protein response (UPR), at least in part through dephosphorylation of Ire1p; dosage-dependent positive regulator of the G1/S phase transition through control of the timing of START; physically interacts with, dephosphorylates and destabilizes Sic1p; SWAT-GFP and mCherry fusion proteins localize to the vacuole.

Serine/threonine-protein phosphatase PP1-2; Type 1 S/T protein phosphatase (PP1) catalytic subunit; involved in glycogen metabolism, sporulation and mitotic progression; interacts with multiple regulatory subunits; regulates actomyosin ring formation; subunit of CPF; recruited to mating projections by Afr1p interaction; regulates nucleocytoplasmic shuttling of Hxk2p; import into the nucleus is inhibited during spindle assembly checkpoint arrest; involved in dephosphorylating Rps6a/b and Bnr1p.

Serine/threonine-protein kinase ELM1; Serine/threonine protein kinase; regulates the orientation checkpoint, the morphogenesis checkpoint and the metabolic switch from fermentative to oxidative metabolism by phosphorylating the activation loop of Kin4p, Hsl1p and Snf4p respectively; cooperates with Hsl7p in recruiting Hsl1p to the septin ring, a prerequisite for subsequent recruitment, phosphorylation, and degradation of Swe1p; forms part of the bud neck ring; regulates cytokinesis.