UniProt functional annotation for P12904



	UniProt functional annotation for P12904

UniProt code: P12904.

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

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

Function: Adenine nucleotides-binding subunit gamma of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer- term effects via phosphorylation of transcription regulators. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (SNF1) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. {ECO:0000269|PubMed:10099331, ECO:0000269|PubMed:10224244, ECO:0000269|PubMed:11486005, ECO:0000269|PubMed:12393914, ECO:0000269|PubMed:12960168, ECO:0000269|PubMed:1468623, ECO:0000269|PubMed:18474591, ECO:0000269|PubMed:2169717, ECO:0000269|PubMed:22019086, ECO:0000269|PubMed:2557546, ECO:0000269|PubMed:3049551, ECO:0000269|PubMed:3939253, ECO:0000269|PubMed:6392017, ECO:0000269|PubMed:7050076, ECO:0000269|PubMed:8224185, ECO:0000269|PubMed:8544831, ECO:0000269|PubMed:8985180, ECO:0000269|PubMed:9600950}.

Subunit: AMPK is a heterotrimer of an alpha catalytic subunit (SNF1), a beta (SIP1, SIP2 or GAL83) and a gamma non-catalytic subunits (SNF4). Note=Interaction between SNF1 and SNF4 is inhibited by high levels of glucose. {ECO:0000269|PubMed:12393914, ECO:0000269|PubMed:16847059, ECO:0000269|PubMed:17851534}.

Subcellular location: Nucleus {ECO:0000269|PubMed:17237508, ECO:0000269|PubMed:2481228, ECO:0000269|PubMed:3049255}. Cytoplasm {ECO:0000269|PubMed:17237508, ECO:0000269|PubMed:2481228}.

Domain: The 4 CBS domains mediate binding to nucleotides. Of the 4 potential nucleotide-binding sites, 2 are occupied, designated as sites 2 and 3 based on the CBS modules that provide the acidic residue for coordination with the 2'- and 3'-hydroxyl groups of the ribose of AMP. Site 3 can bind either AMP, ADP or ATP (AMP, ADP or ATP 2). Site 2 binds specifically ADP (ADP 1) and is likely to be responsible for protection of a conserved threonine in the activation loop of the alpha catalytic subunit through conformational changes induced by binding of ADP (PubMed:22019086). {ECO:0000269|PubMed:22019086}.

Disruption phenotype: Leads to a decrease in the length of G1 with respect to the wild-type strain along with a smaller difference in the cell cycle length of parent and daughter cells. {ECO:0000269|PubMed:9841784}.

Miscellaneous: Present with 11700 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.

Similarity: Belongs to the 5'-AMP-activated protein kinase gamma subunit family. {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:		Adenine nucleotides-binding subunit gamma of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer- term effects via phosphorylation of transcription regulators. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (SNF1) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. {ECO:0000269\|PubMed:10099331, ECO:0000269\|PubMed:10224244, ECO:0000269\|PubMed:11486005, ECO:0000269\|PubMed:12393914, ECO:0000269\|PubMed:12960168, ECO:0000269\|PubMed:1468623, ECO:0000269\|PubMed:18474591, ECO:0000269\|PubMed:2169717, ECO:0000269\|PubMed:22019086, ECO:0000269\|PubMed:2557546, ECO:0000269\|PubMed:3049551, ECO:0000269\|PubMed:3939253, ECO:0000269\|PubMed:6392017, ECO:0000269\|PubMed:7050076, ECO:0000269\|PubMed:8224185, ECO:0000269\|PubMed:8544831, ECO:0000269\|PubMed:8985180, ECO:0000269\|PubMed:9600950}.


Subunit:		AMPK is a heterotrimer of an alpha catalytic subunit (SNF1), a beta (SIP1, SIP2 or GAL83) and a gamma non-catalytic subunits (SNF4). Note=Interaction between SNF1 and SNF4 is inhibited by high levels of glucose. {ECO:0000269\|PubMed:12393914, ECO:0000269\|PubMed:16847059, ECO:0000269\|PubMed:17851534}.
Subcellular location:		Nucleus {ECO:0000269\|PubMed:17237508, ECO:0000269\|PubMed:2481228, ECO:0000269\|PubMed:3049255}. Cytoplasm {ECO:0000269\|PubMed:17237508, ECO:0000269\|PubMed:2481228}.
Domain:		The 4 CBS domains mediate binding to nucleotides. Of the 4 potential nucleotide-binding sites, 2 are occupied, designated as sites 2 and 3 based on the CBS modules that provide the acidic residue for coordination with the 2'- and 3'-hydroxyl groups of the ribose of AMP. Site 3 can bind either AMP, ADP or ATP (AMP, ADP or ATP 2). Site 2 binds specifically ADP (ADP 1) and is likely to be responsible for protection of a conserved threonine in the activation loop of the alpha catalytic subunit through conformational changes induced by binding of ADP (PubMed:22019086). {ECO:0000269\|PubMed:22019086}.
Disruption phenotype:		Leads to a decrease in the length of G1 with respect to the wild-type strain along with a smaller difference in the cell cycle length of parent and daughter cells. {ECO:0000269\|PubMed:9841784}.
Miscellaneous:		Present with 11700 molecules/cell in log phase SD medium. {ECO:0000269\|PubMed:14562106}.
Similarity:		Belongs to the 5'-AMP-activated protein kinase gamma subunit family. {ECO:0000305}.