CPLM-008874

Genbank Nucleotide ID

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

Protein Synonyms/Alias

AMPK gamma1; AMPK subunit gamma-1; AMPKg

Homo sapiens (Human)

Position	Peptide	Type	References
34	SVYTSFMKSHRCYDL	ubiquitination	[1]
170	TLYILTHKRILKFLK	ubiquitination	[2, 3, 4]
174	LTHKRILKFLKLFIT	ubiquitination	[1]
234	ALPVVDEKGRVVDIY	ubiquitination	[1, 5, 6]
243	RVVDIYSKFDVINLA	ubiquitination	[1, 5, 6]
253	VINLAAEKTYNNLDV	ubiquitination	[6]
264	NLDVSVTKALQHRSH	acetylation	[7]
264	NLDVSVTKALQHRSH	ubiquitination	[1, 2, 6]
330	VLTGGEKKP******	ubiquitination	[1]

[1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[3] 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]
[4] 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]
[5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]

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.

DOMAIN 43 103 CBS 1.
DOMAIN 125 187 CBS 2.
DOMAIN 198 260 CBS 3.
DOMAIN 272 329 CBS 4.
MOTIF 138 159 AMPK pseudosubstrate.
BINDING 70 70 AMP 1 (By similarity).
BINDING 70 70 ATP 1 (By similarity).
BINDING 151 151 AMP 2 (By similarity).
BINDING 151 151 AMP 3 (By similarity).
BINDING 151 151 ATP 2 (By similarity).
BINDING 152 152 ATP 1 (By similarity).
BINDING 152 152 ATP 2 (By similarity).
BINDING 170 170 AMP 1 (By similarity).
BINDING 170 170 ATP 1 (By similarity).
BINDING 298 298 AMP 3 (By similarity).
BINDING 299 299 AMP 1 (By similarity).
BINDING 299 299 ATP 1 (By similarity).
MOD_RES 261 261 Phosphoserine; by ULK1 (By similarity).
MOD_RES 263 263 Phosphothreonine; by ULK1 (By
MOD_RES 270 270 Phosphoserine; by ULK1 (By similarity).

3D-structure; Alternative splicing; ATP-binding; CBS domain; Complete proteome; Direct protein sequencing; Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Nucleotide-binding; Phosphoprotein; Polymorphism; 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:0043531; F:ADP binding; ISS:UniProtKB.
GO:0016208; F:AMP binding; ISS:UniProtKB.
GO:0005524; F:ATP binding; ISS:UniProtKB.
GO:0004691; F:cAMP-dependent protein kinase activity; TAS:ProtInc.
GO:0008603; F:cAMP-dependent protein kinase regulator activity; TAS:BHF-UCL.
GO:0019901; F:protein kinase binding; IDA:BHF-UCL.
GO:0007050; P:cell cycle arrest; TAS:Reactome.
GO:0016044; P:cellular membrane organization; TAS:Reactome.
GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO:0045860; P:positive regulation of protein kinase activity; TAS:BHF-UCL.
GO:0006110; P:regulation of glycolysis; TAS:BHF-UCL.
GO:0007283; P:spermatogenesis; TAS:ProtInc.

IPR000644; Cysta_beta_synth_core.