UniProt Accession

 AAKG1_RAT; P80385; Q4QQW6 

Genbank Protein ID

 X95578; BC097940; U42413 

Genbank Nucleotide ID

 CAA64831.1; AAH97940.1; AAC52580.1 

Protein Name

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

Protein Synonyms/Alias

 AMPK gamma1; AMPK subunit gamma-1; AMPKg 

Gene Name

 Prkag1 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Rattus norvegicus (Rat) 

NCBI Taxa ID

 10116 

Lysine Modification

Position	Peptide	Type	References
169	TLYILTHKRILKFLK	acetylation	[1]
233	ALPVVDEKGRVVDIY	acetylation	[1]

Reference

 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 

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. 

Sequence Annotation

 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.
 BINDING 69 69 ATP 1.
 BINDING 150 150 AMP 2.
 BINDING 150 150 AMP 3.
 BINDING 150 150 ATP 2.
 BINDING 151 151 ATP 1.
 BINDING 151 151 ATP 2.
 BINDING 169 169 AMP 1.
 BINDING 169 169 ATP 1.
 BINDING 297 297 AMP 3.
 BINDING 298 298 AMP 1.
 BINDING 298 298 ATP 1.
 MOD_RES 260 260 Phosphoserine; by ULK1 (Probable).
 MOD_RES 262 262 Phosphothreonine; by ULK1 (Probable).
 MOD_RES 269 269 Phosphoserine; by ULK1.  

Keyword

 3D-structure; ATP-binding; CBS domain; Complete proteome; Direct protein sequencing; Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 330 AA 

Protein Sequence

Gene Ontology

 GO:0031588; C:AMP-activated protein kinase complex; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0043531; F:ADP binding; IDA:UniProtKB.
 GO:0016208; F:AMP binding; IDA:UniProtKB.
 GO:0004679; F:AMP-activated protein kinase activity; TAS:RGD.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
 GO:0051291; P:protein heterooligomerization; IDA:RGD.
 GO:0050790; P:regulation of catalytic activity; IDA:RGD. 

Interpro

 IPR000644; Cysta_beta_synth_core. 

Pfam

 PF00571; CBS 

SMART

 SM00116; CBS 

PROSITE

 PS51371; CBS 

PRINTS