CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022902
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 5'-AMP-activated protein kinase subunit gamma-2 
Protein Synonyms/Alias
 AMPK gamma2; AMPK subunit gamma-2; H91620p 
Gene Name
 PRKAG2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
9GSAVMDTKKKKDVSSacetylation[1]
475KVVDIYSKFDVINLAubiquitination[2]
Reference
 [1] 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]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
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 275 335 CBS 1.
 DOMAIN 357 415 CBS 2.
 DOMAIN 430 492 CBS 3.
 DOMAIN 504 562 CBS 4.
 MOTIF 370 391 AMPK pseudosubstrate.
 BINDING 302 302 AMP 1 (By similarity).
 BINDING 302 302 ATP 1 (By similarity).
 BINDING 383 383 AMP 2 (By similarity).
 BINDING 383 383 AMP 3 (By similarity).
 BINDING 383 383 ATP 2 (By similarity).
 BINDING 384 384 ATP 1 (By similarity).
 BINDING 384 384 ATP 2 (By similarity).
 BINDING 402 402 AMP 1 (By similarity).
 BINDING 402 402 ATP 1 (By similarity).
 BINDING 530 530 AMP 3 (By similarity).
 BINDING 531 531 AMP 1 (By similarity).
 BINDING 531 531 ATP 1 (By similarity).
 MOD_RES 65 65 Phosphoserine (By similarity).
 MOD_RES 71 71 Phosphoserine (By similarity).
 MOD_RES 73 73 Phosphoserine (By similarity).
 MOD_RES 90 90 Phosphoserine (By similarity).
 MOD_RES 138 138 Phosphoserine (By similarity).
 MOD_RES 161 161 Phosphoserine (By similarity).
 MOD_RES 162 162 Phosphoserine (By similarity).
 MOD_RES 196 196 Phosphoserine (By similarity).  
Keyword
 Alternative splicing; ATP-binding; Cardiomyopathy; CBS domain; Complete proteome; Disease mutation; Fatty acid biosynthesis; Fatty acid metabolism; Glycogen storage disease; Lipid biosynthesis; Lipid metabolism; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 569 AA 
Protein Sequence
MGSAVMDTKK KKDVSSPGGS GGKKNASQKR RSLRVHIPDL SSFAMPLLDG DLEGSGKHSS 60
RKVDSPFGPG SPSKGFFSRG PQPRPSSPMS APVRPKTSPG SPKTVFPFSY QESPPRSPRR 120
MSFSGIFRSS SKESSPNSNP ATSPGGIRFF SRSRKTSGLS SSPSTPTQVT KQHTFPLESY 180
KHEPERLENR IYASSSPPDT GQRFCPSSFQ SPTRPPLASP THYAPSKAAA LAAALGPAEA 240
GMLEKLEFED EAVEDSESGV YMRFMRSHKC YDIVPTSSKL VVFDTTLQVK KAFFALVANG 300
VRAAPLWESK KQSFVGMLTI TDFINILHRY YKSPMVQIYE LEEHKIETWR ELYLQETFKP 360
LVNISPDASL FDAVYSLIKN KIHRLPVIDP ISGNALYILT HKRILKFLQL FMSDMPKPAF 420
MKQNLDELGI GTYHNIAFIH PDTPIIKALN IFVERRISAL PVVDESGKVV DIYSKFDVIN 480
LAAEKTYNNL DITVTQALQH RSQYFEGVVK CNKLEILETI VDRIVRAEVH RLVVVNEADS 540
IVGIISLSDI LQALILTPAG AKQKETETE 569 
Gene Ontology
 GO:0031588; C:AMP-activated protein kinase complex; IDA:BHF-UCL.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0043531; F:ADP binding; IDA:BHF-UCL.
 GO:0005524; F:ATP binding; IDA:BHF-UCL.
 GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IDA:BHF-UCL.
 GO:0008603; F:cAMP-dependent protein kinase regulator activity; IMP:BHF-UCL.
 GO:0008607; F:phosphorylase kinase regulator activity; IMP:BHF-UCL.
 GO:0030295; F:protein kinase activator activity; IMP:BHF-UCL.
 GO:0019901; F:protein kinase binding; IDA:BHF-UCL.
 GO:0006754; P:ATP biosynthetic process; TAS:BHF-UCL.
 GO:0006853; P:carnitine shuttle; TAS:Reactome.
 GO:0007050; P:cell cycle arrest; TAS:Reactome.
 GO:0044255; P:cellular lipid metabolic process; TAS:Reactome.
 GO:0016044; P:cellular membrane organization; TAS:Reactome.
 GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
 GO:0005977; P:glycogen metabolic process; IMP:BHF-UCL.
 GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
 GO:0007243; P:intracellular protein kinase cascade; IMP:BHF-UCL.
 GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IMP:BHF-UCL.
 GO:0042304; P:regulation of fatty acid biosynthetic process; TAS:Reactome.
 GO:0046320; P:regulation of fatty acid oxidation; TAS:BHF-UCL.
 GO:0046324; P:regulation of glucose import; TAS:BHF-UCL.
 GO:0006110; P:regulation of glycolysis; IMP:BHF-UCL.
 GO:0016126; P:sterol biosynthetic process; TAS:BHF-UCL. 
Interpro
 IPR000644; Cysta_beta_synth_core. 
Pfam
 PF00571; CBS 
SMART
 SM00116; CBS 
PROSITE
 PS51371; CBS 
PRINTS