Search by BoMiProt ID - Bomi3535


Primary Information

BoMiProt ID Bomi3535
Protein Name 5'-AMP-activated protein kinase subunit gamma-1
Organism Bos taurus
Uniprot IDP58108
Milk FractionExosomes
Ref Sequence ID NP_777011.2
Aminoacid Length 330
Molecular Weight 37497
FASTA Sequence Download
Gene Name PRKAG1
Gene ID 282324
Protein Existence Status Reviewed

Secondary Information

Presence in other biological fluids/tissue/cells baseline and differential
Protein Function 5'-AMP-activated protein kinase (AMPK) has been proposed to be a pivotal factor in cellular responses to both acute exercise and exercise training.
Biochemical Properties a serine/threonine protein kinase that is activated by various cellular stresses that increase AMP levels and decrease ATP levels.AMPK is a heterotrimeric complex consisting of a catalytic alpha subunit (e.g., PRKAA1), a noncatalytic beta subunit (e.g., PRKAB1), and a noncatalytic gamma subunit (e.g., PRKAG1). Structural and solution studies revealed that 2 sites on the gamma domain bind either AMP or magnesium ATP, whereas a third site contains a tightly bound AMP that does not exchange.The phosphate groups of AMP/ATP lie in a groove on the surface of the gamma domain, which is lined with basic residues, many of which are associated with disease-causing mutations.
PTMs Phosphorylation at Ser/Thr
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|P58108|AAKG1_BOVIN 5'-AMP-activated protein kinase subunit gamma-1 OS=Bos taurus OX=9913 GN=PRKAG1 PE=2 SV=2 MEAVPSSDSYPAVENEHLQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKA FFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREV YLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFI TEFPKPEFMSKSLEELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDI YSKFDVINLAAEKTYNNLDVS*261VT*263KALQHRS*270HYFEGVLKCYLHETLETIINRLVEAEVHRL VVVDENDVVKGIVSLSDILQALVLTGGEKP
Predicted Disorder Regions (1-25)
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs Phosphorylation leads to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1, ULK2 and AMPK.During AMP/ATP signaling whereby a phosphorylated residue from the alpha and/or beta subunits binds to the gamma subunit in the presence of AMP but not when ATP is bound.
Bibliography 1.Gao G, Fernandez CS, Stapleton D, Auster AS, Widmer J, Dyck JR, Kemp BE, Witters LA. Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-activated protein kinase. J Biol Chem. 1996 Apr 12;271(15):8675-81. doi: 10.1074/jbc.271.15.8675. PMID: 8621499. 2.Nielsen JN, Mustard KJ, Graham DA, Yu H, MacDonald CS, Pilegaard H, Goodyear LJ, Hardie DG, Richter EA, Wojtaszewski JF. 5'-AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle. J Appl Physiol (1985). 2003 Feb;94(2):631-41. doi: 10.1152/japplphysiol.00642.2002. Epub 2002 Oct 11. PMID: 12391032.