Overview
| Uniprot ID | P54619 |
|---|
| Protein Name | 5'-AMP-activated protein kinase subunit gamma-1 |
|---|
| Gene Name | PRKAG1 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 170 |
TLYILTHKRILKFLK |
| 264 |
NLDVSVTKALQHRSH |
Function
AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism (PubMed:21680840, PubMed:24563466). 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 (PubMed:21680840, PubMed:24563466). AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators (PubMed:21680840, PubMed:24563466). Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin (PubMed:21680840, PubMed:24563466). 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 (PubMed:21680840, PubMed:24563466). ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit (PubMed:21680840, PubMed:24563466). ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive (PubMed:21680840, PubMed:24563466)
Protein Sequence
10
METVISSDSS
20
PAVENEHPQE
30
TPESNNSVYT
40
SFMKSHRCYD
50
LIPTSSKLVV
60
FDTSLQVKKA
70
FFALVTNGVR
80
AAPLWDSKKQ
90
SFVGMLTITD
100
FINILHRYYK
110
SALVQIYELE
120
EHKIETWREV
130
YLQDSFKPLV
140
CISPNASLFD
150
AVSSLIRNKI
160
HRLPVIDPES
170
GNTLYILTHK
180
RILKFLKLFI
190
TEFPKPEFMS
200
KSLEELQIGT
210
YANIAMVRTT
220
TPVYVALGIF
230
VQHRVSALPV
240
VDEKGRVVDI
250
YSKFDVINLA
260
AEKTYNNLDV
270
SVTKALQHRS
280
HYFEGVLKCY
290
LHETLETIIN
300
RLVEAEVHRL
310
VVVDENDVVK
320
GIVSLSDILQ
330
ALVLTGGEKK
P
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0016020 |
membrane |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005788 |
endoplasmic reticulum lumen |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0031588 |
nucleotide-activated protein kinase complex |
| Cellular Component |
GO:0005634 |
nucleus |
| Molecular Function |
GO:0043531 |
ADP binding |
| Molecular Function |
GO:0016208 |
AMP binding |
| Molecular Function |
GO:0004679 |
AMP-activated protein kinase activity |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0004691 |
cAMP-dependent protein kinase activity |
| Molecular Function |
GO:0008603 |
cAMP-dependent protein kinase regulator activity |
| Molecular Function |
GO:0019901 |
protein kinase binding |
| Molecular Function |
GO:0019887 |
protein kinase regulator activity |
| Molecular Function |
GO:0044877 |
protein-containing complex binding |
| Biological Process |
GO:0042149 |
cellular response to glucose starvation |
| Biological Process |
GO:0031669 |
cellular response to nutrient levels |
| Biological Process |
GO:0006633 |
fatty acid biosynthetic process |
| Biological Process |
GO:0045722 |
positive regulation of gluconeogenesis |
| Biological Process |
GO:0006468 |
protein phosphorylation |
| Biological Process |
GO:0051726 |
regulation of cell cycle |
| Biological Process |
GO:0006110 |
regulation of glycolytic process |
| Biological Process |
GO:0007165 |
signal transduction |
| Biological Process |
GO:0007283 |
spermatogenesis |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.