UniProt functional annotation for P06782



	UniProt functional annotation for P06782

UniProt code: P06782.

Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).

Taxonomy: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.

Function: Serine/threonine protein kinase essential for release from glucose repression (PubMed:3526554, PubMed:6366512, PubMed:3049551, PubMed:1944227, PubMed:8289797, PubMed:8628258, PubMed:25869125). Catalytic subunit of the AMP-activated protein kinase complex also known as the SNF1 kinase complex (Snf1c), a central regulator of cellular energy homeostasis, which, in response to a fall in intracellular ATP levels, activates energy-producing pathways and inhibits energy-consuming processes (PubMed:8289797, PubMed:26667037). The complex phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, leading to transcriptional activation through TBP recruitment to the promoters (PubMed:15719021). The complex also negatively regulates the HOG1 MAPK pathway in ER stress response including unfolded protein response (UPR) (PubMed:25730376, PubMed:26394309). Under nutrient/energy depletion, the complex phosphorylates and activates PAS kinase PSK1 which in turn activates PBS1, leading to the inhibition of the TORC1 signaling pathway (PubMed:25428989). SNF1 also interacts and phosphorylates adenylate cyclase CYR1 and negatively regulates the protein kinase A signaling pathway (PubMed:26309257). Also phosphorylates and regulates the transcriptional activator CAT8 (PubMed:15121831). {ECO:0000269|PubMed:15121831, ECO:0000269|PubMed:15719021, ECO:0000269|PubMed:1944227, ECO:0000269|PubMed:25428989, ECO:0000269|PubMed:25730376, ECO:0000269|PubMed:25869125, ECO:0000269|PubMed:26309257, ECO:0000269|PubMed:26394309, ECO:0000269|PubMed:26667037, ECO:0000269|PubMed:3049551, ECO:0000269|PubMed:3526554, ECO:0000269|PubMed:6366512, ECO:0000269|PubMed:8289797, ECO:0000269|PubMed:8628258}.

Catalytic activity: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:15719021, ECO:0000269|PubMed:2557546, ECO:0000269|PubMed:3526554};

Catalytic activity: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:15719021, ECO:0000269|PubMed:2557546, ECO:0000269|PubMed:3526554};

Activity regulation: The kinase activity is positively regulated by SNF4 via sequestration of the SNF1 auto-inhibitory domain (AID) (PubMed:2557546, PubMed:17851534). {ECO:0000269|PubMed:17851534, ECO:0000269|PubMed:2557546}.

Subunit: Component of the AMP-activated protein kinase complex also known as the SNF1 kinase complex (Snf1c), a heterotrimeric complex composed of an alpha subunit (SNF1), a regulatory subunit beta (GAL83 and substoichiometric alternate beta subunits SIP1 and SIP2), and a regulatory subunit gamma (SNF4) (PubMed:2557546, PubMed:2481228, PubMed:7813428, PubMed:9121458, PubMed:15719021, PubMed:17851534). Interacts with the transcriptional activator SIP4 (PubMed:8628258). Interacts with SAK1 (PubMed:12748292, PubMed:16847059). Interacts with CTK1 (PubMed:16182287): Interacts with adenylate cyclase CYR1 (PubMed:26309257). {ECO:0000269|PubMed:12748292, ECO:0000269|PubMed:15719021, ECO:0000269|PubMed:16182287, ECO:0000269|PubMed:16847059, ECO:0000269|PubMed:17851534, ECO:0000269|PubMed:2481228, ECO:0000269|PubMed:2557546, ECO:0000269|PubMed:26309257, ECO:0000269|PubMed:7813428, ECO:0000269|PubMed:8628258, ECO:0000269|PubMed:9121458}.

Subcellular location: Cytoplasm {ECO:0000269|PubMed:25869125}. Nucleus {ECO:0000269|PubMed:25869125}. Nucleus membrane {ECO:0000269|PubMed:17237508}; Peripheral membrane protein {ECO:0000269|PubMed:17237508}. Note=Nuclear translocation occurs under nitrogen and glucose starvation conditions (PubMed:25869125). {ECO:0000269|PubMed:25869125}.

Induction: Expression of the SNF1 gene itself is not glucose repressible (PubMed:6366513). {ECO:0000269|PubMed:6366513}.

Domain: The regulatory domain (RS) also called auto-inhibitory domain (AID) inhibits kinase activity of the protein kinase domain (KD) (PubMed:19474788, PubMed:20823513). The AID is sequestered by SNF4 within the AMP-activated protein kinase complex which might correspond to the activated SNF1 form (PubMed:17851534). {ECO:0000269|PubMed:17851534, ECO:0000269|PubMed:19474788, ECO:0000269|PubMed:20823513}.

Domain: The ubiquitin-associated domain (UBA) localized within the AID dampens kinase activation, probably by restraining SNF1-SNF4 associations (PubMed:25869125). Moreover, the UBA domain influences life span in a FKH1- and FKH2-dependent mechanism (PubMed:25869125). {ECO:0000269|PubMed:25869125}.

Ptm: Phosphorylation at Thr-210 in response to glucose limitation leads to activation of kinase activity (PubMed:11486005, PubMed:12748292). ADP, but not AMP, protects the enzyme from dephosphorylation at Thr-210 by GLC7 (PubMed:22019086). {ECO:0000269|PubMed:12748292, ECO:0000269|PubMed:22019086}.

Ptm: Sumoylation by the SUMO (E3) ligase MMS21 leads to inhibition by interaction of SUMO attached to Lys-549 with a SUMO-interacting sequence motif located near the active site of SNF1, and by targeting SNF1 for glucose-induced destruction via the SLX5-SLX8 (SUMO-directed) ubiquitin ligase (PubMed:24108357). {ECO:0000269|PubMed:24108357}.

Miscellaneous: Present with 589 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.

Similarity: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Taxonomy:		Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.



Function:		Serine/threonine protein kinase essential for release from glucose repression (PubMed:3526554, PubMed:6366512, PubMed:3049551, PubMed:1944227, PubMed:8289797, PubMed:8628258, PubMed:25869125). Catalytic subunit of the AMP-activated protein kinase complex also known as the SNF1 kinase complex (Snf1c), a central regulator of cellular energy homeostasis, which, in response to a fall in intracellular ATP levels, activates energy-producing pathways and inhibits energy-consuming processes (PubMed:8289797, PubMed:26667037). The complex phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, leading to transcriptional activation through TBP recruitment to the promoters (PubMed:15719021). The complex also negatively regulates the HOG1 MAPK pathway in ER stress response including unfolded protein response (UPR) (PubMed:25730376, PubMed:26394309). Under nutrient/energy depletion, the complex phosphorylates and activates PAS kinase PSK1 which in turn activates PBS1, leading to the inhibition of the TORC1 signaling pathway (PubMed:25428989). SNF1 also interacts and phosphorylates adenylate cyclase CYR1 and negatively regulates the protein kinase A signaling pathway (PubMed:26309257). Also phosphorylates and regulates the transcriptional activator CAT8 (PubMed:15121831). {ECO:0000269\|PubMed:15121831, ECO:0000269\|PubMed:15719021, ECO:0000269\|PubMed:1944227, ECO:0000269\|PubMed:25428989, ECO:0000269\|PubMed:25730376, ECO:0000269\|PubMed:25869125, ECO:0000269\|PubMed:26309257, ECO:0000269\|PubMed:26394309, ECO:0000269\|PubMed:26667037, ECO:0000269\|PubMed:3049551, ECO:0000269\|PubMed:3526554, ECO:0000269\|PubMed:6366512, ECO:0000269\|PubMed:8289797, ECO:0000269\|PubMed:8628258}.


Catalytic activity:		Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269\|PubMed:15719021, ECO:0000269\|PubMed:2557546, ECO:0000269\|PubMed:3526554};
Catalytic activity:		Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269\|PubMed:15719021, ECO:0000269\|PubMed:2557546, ECO:0000269\|PubMed:3526554};
Activity regulation:		The kinase activity is positively regulated by SNF4 via sequestration of the SNF1 auto-inhibitory domain (AID) (PubMed:2557546, PubMed:17851534). {ECO:0000269\|PubMed:17851534, ECO:0000269\|PubMed:2557546}.
Subunit:		Component of the AMP-activated protein kinase complex also known as the SNF1 kinase complex (Snf1c), a heterotrimeric complex composed of an alpha subunit (SNF1), a regulatory subunit beta (GAL83 and substoichiometric alternate beta subunits SIP1 and SIP2), and a regulatory subunit gamma (SNF4) (PubMed:2557546, PubMed:2481228, PubMed:7813428, PubMed:9121458, PubMed:15719021, PubMed:17851534). Interacts with the transcriptional activator SIP4 (PubMed:8628258). Interacts with SAK1 (PubMed:12748292, PubMed:16847059). Interacts with CTK1 (PubMed:16182287): Interacts with adenylate cyclase CYR1 (PubMed:26309257). {ECO:0000269\|PubMed:12748292, ECO:0000269\|PubMed:15719021, ECO:0000269\|PubMed:16182287, ECO:0000269\|PubMed:16847059, ECO:0000269\|PubMed:17851534, ECO:0000269\|PubMed:2481228, ECO:0000269\|PubMed:2557546, ECO:0000269\|PubMed:26309257, ECO:0000269\|PubMed:7813428, ECO:0000269\|PubMed:8628258, ECO:0000269\|PubMed:9121458}.
Subcellular location:		Cytoplasm {ECO:0000269\|PubMed:25869125}. Nucleus {ECO:0000269\|PubMed:25869125}. Nucleus membrane {ECO:0000269\|PubMed:17237508}; Peripheral membrane protein {ECO:0000269\|PubMed:17237508}. Note=Nuclear translocation occurs under nitrogen and glucose starvation conditions (PubMed:25869125). {ECO:0000269\|PubMed:25869125}.
Induction:		Expression of the SNF1 gene itself is not glucose repressible (PubMed:6366513). {ECO:0000269\|PubMed:6366513}.
Domain:		The regulatory domain (RS) also called auto-inhibitory domain (AID) inhibits kinase activity of the protein kinase domain (KD) (PubMed:19474788, PubMed:20823513). The AID is sequestered by SNF4 within the AMP-activated protein kinase complex which might correspond to the activated SNF1 form (PubMed:17851534). {ECO:0000269\|PubMed:17851534, ECO:0000269\|PubMed:19474788, ECO:0000269\|PubMed:20823513}.
Domain:		The ubiquitin-associated domain (UBA) localized within the AID dampens kinase activation, probably by restraining SNF1-SNF4 associations (PubMed:25869125). Moreover, the UBA domain influences life span in a FKH1- and FKH2-dependent mechanism (PubMed:25869125). {ECO:0000269\|PubMed:25869125}.
Ptm:		Phosphorylation at Thr-210 in response to glucose limitation leads to activation of kinase activity (PubMed:11486005, PubMed:12748292). ADP, but not AMP, protects the enzyme from dephosphorylation at Thr-210 by GLC7 (PubMed:22019086). {ECO:0000269\|PubMed:12748292, ECO:0000269\|PubMed:22019086}.
Ptm:		Sumoylation by the SUMO (E3) ligase MMS21 leads to inhibition by interaction of SUMO attached to Lys-549 with a SUMO-interacting sequence motif located near the active site of SNF1, and by targeting SNF1 for glucose-induced destruction via the SLX5-SLX8 (SUMO-directed) ubiquitin ligase (PubMed:24108357). {ECO:0000269\|PubMed:24108357}.
Miscellaneous:		Present with 589 molecules/cell in log phase SD medium. {ECO:0000269\|PubMed:14562106}.
Similarity:		Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}.