CPLM-000835

Genbank Nucleotide ID

5'-AMP-activated protein kinase subunit gamma-1

Protein Synonyms/Alias

AMPK gamma1; AMPK subunit gamma-1; AMPKg

Mus musculus (Mouse)

Position	Peptide	Type	References
263	NLDVSVTKALQHRSH	ubiquitination	[1, 2, 3]

[1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
[2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]

Functional Description

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. 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 (By similarity).

DOMAIN 42 102 CBS 1.
DOMAIN 124 186 CBS 2.
DOMAIN 197 259 CBS 3.
DOMAIN 271 328 CBS 4.
MOTIF 137 158 AMPK pseudosubstrate.
BINDING 69 69 AMP 1 (By similarity).
BINDING 69 69 ATP 1 (By similarity).
BINDING 150 150 AMP 2 (By similarity).
BINDING 150 150 AMP 3 (By similarity).
BINDING 150 150 ATP 2 (By similarity).
BINDING 151 151 ATP 1 (By similarity).
BINDING 151 151 ATP 2 (By similarity).
BINDING 169 169 AMP 1 (By similarity).
BINDING 169 169 ATP 1 (By similarity).
BINDING 297 297 AMP 3 (By similarity).
BINDING 298 298 AMP 1 (By similarity).
BINDING 298 298 ATP 1 (By similarity).
MOD_RES 260 260 Phosphoserine; by ULK1 (By similarity).
MOD_RES 262 262 Phosphothreonine; by ULK1 (By
MOD_RES 269 269 Phosphoserine; by ULK1 (By similarity).

ATP-binding; CBS domain; Complete proteome; Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0031588; C:AMP-activated protein kinase complex; ISS:UniProtKB.
GO:0005829; C:cytosol; TAS:Reactome.
GO:0005634; C:nucleus; IDA:MGI.
GO:0043531; F:ADP binding; ISS:UniProtKB.
GO:0016208; F:AMP binding; ISS:UniProtKB.
GO:0004679; F:AMP-activated protein kinase activity; TAS:MGI.
GO:0005524; F:ATP binding; ISS:UniProtKB.
GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO:0051291; P:protein heterooligomerization; IEA:Compara.
GO:0050790; P:regulation of catalytic activity; IEA:Compara.

IPR000644; Cysta_beta_synth_core.