SequenceDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRI LKFLKLFITEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFV QHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHR S
AMP activated protein kinase noncatalytic gamma 1 subunit
AMPK gamma 1 chain
AMPK subunit gamma-1
Protein kinase AMP activated gamma 1 non catalytic subunit
protein kinase, AMP-activated, noncatalytic gamma-1
FunctionAMP/ATP-binding subunit 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. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. 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 (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.
Sequence similaritiesBelongs to the 5'-AMP-activated protein kinase gamma subunit family. Contains 4 CBS domains.
DomainThe AMPK pseudosubstrate motif resembles the sequence around sites phosphorylated on target proteins of AMPK, except the presence of a non-phosphorylatable residue in place of Ser. In the absence of AMP this pseudosubstrate sequence may bind to the active site groove on the alpha subunit (PRKAA1 or PRKAA2), preventing phosphorylation by the upstream activating kinase STK11/LKB1. The CBS domains mediate binding to AMP, ADP and ATP. 2 sites bind either AMP or ATP, whereas a third site contains a tightly bound AMP that does not exchange. Under physiological conditions AMPK mainly exists in its inactive form in complex with ATP, which is much more abundant than AMP.
Post-translational modificationsPhosphorylated by ULK1 and ULK2; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1, ULK2 and AMPK.
SDS-PAGE - AMPK gamma 1 protein (Tagged-His Tag) (ab91948)
The image shows an electrophoretic assay performed using an Agilent 5100 ALP. In some images coloured control bands can be seen at 15 kDa (green) and/or 240 kDa (purple). The protein-specific band is blue.
References for Human AMPK gamma 1 protein fragment (ab91948)
has not yet been referenced specifically in any publications.
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