Primary Information |
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BoMiProt ID | Bomi3535 |
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Protein Name | 5'-AMP-activated protein kinase subunit gamma-1 |
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Organism | Bos taurus |
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Uniprot ID | P58108 |
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Milk Fraction | Exosomes |
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Ref Sequence ID | NP_777011.2 |
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Aminoacid Length | 330 |
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Molecular Weight | 37497 |
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FASTA Sequence |
Download |
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Gene Name | PRKAG1 |
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Gene ID | 282324 |
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Protein Existence Status | Reviewed |
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Secondary Information |
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Presence in other biological fluids/tissue/cells | baseline and differential |
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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. |
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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. |
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PTMs | Phosphorylation at Ser/Thr |
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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
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Predicted Disorder Regions | (1-25) |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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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. |
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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. |