PRKAG2

PRKAG2
Identifiers
Aliases	PRKAG2, AAKG, AAKG2, CMH6, H91620p, WPWS, protein kinase AMP-activated non-catalytic subunit gamma 2
External IDs	OMIM: 602743; MGI: 1336153; HomoloGene: 136125; GeneCards: PRKAG2; OMA:PRKAG2 - orthologs
Gene location (Human)
Chr.	Chromosome 7 (human)
End	151,877,125 bp
Gene location (Mouse)
Chr.	Chromosome 5 (mouse)
End	25,305,640 bp
RNA expression pattern
	Top expressed in
	right auricle of heart; ; cardiac muscle tissue of right atrium; ; right coronary artery; ; left ventricle; ; left coronary artery; ; popliteal artery; ; tibial arteries; ; gastric mucosa; ; nucleus accumbens; ; apex of heart;
	Top expressed in
	seminiferous tubule; ; atrium; ; spermatid; ; dentate gyrus of hippocampal formation granule cell; ; tail of embryo; ; superior frontal gyrus; ; primary visual cortex; ; atrioventricular valve; ; spermatocyte; ; subiculum;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	nucleotide binding; ADP binding; AMP-activated protein kinase activity; protein kinase activator activity; phosphorylase kinase regulator activity; AMP binding; cAMP-dependent protein kinase regulator activity; cAMP-dependent protein kinase inhibitor activity; ATP binding; protein kinase binding; adenyl ribonucleotide binding;
Cellular component	cytosol; nucleoplasm; nucleotide-activated protein kinase complex; extracellular space;
Biological process	carnitine shuttle; intracellular signal transduction; sterol biosynthetic process; regulation of fatty acid oxidation; negative regulation of protein kinase activity; regulation of glucose import; lipid metabolism; regulation of fatty acid biosynthetic process; fatty acid metabolic process; regulation of glycolytic process; protein phosphorylation; fatty acid biosynthetic process; positive regulation of peptidyl-threonine phosphorylation; regulation of fatty acid metabolic process; ATP biosynthetic process; glycogen metabolic process; regulation of catalytic activity; macroautophagy; positive regulation of protein kinase activity; regulation of signal transduction by p53 class mediator; activation of protein kinase activity; negative regulation of protein serine/threonine kinase activity; regulation of macroautophagy; regulation of protein serine/threonine kinase activity;
	Sources:Amigo / QuickGO
Orthologs
	51422
	108099
	ENSG00000106617
	ENSMUSG00000028944
	Q9UGJ0
	Q91WG5
NM_001040633; NM_001304527; NM_001304531; NM_016203; NM_024429;
	NM_001363698
	NM_001170555; NM_001170556; NM_145401; NM_001310480
NP_001035723; NP_001291456; NP_001291460; NP_057287; NP_077747;
	NP_001350627
	NP_001164026; NP_001164027; NP_001297409; NP_663376
	Wikidata
View/Edit Human	View/Edit Mouse

5'-AMP-activated protein kinase subunit gamma-2 is an enzyme that in humans is encoded by the PRKAG2 gene.^[5]^[6]^[7]

Function

AMP-activated protein kinase (AMPK) is a heterotrimeric protein composed of a catalytic alpha subunit, a noncatalytic beta subunit, and a noncatalytic regulatory gamma subunit. Various forms of each of these subunits exist, encoded by different genes. AMPK is an important energy-sensing enzyme that monitors cellular energy status and functions by inactivating key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. This gene is a member of the AMPK gamma subunit family and encodes a protein with four CBS domains. Mutations in this gene have been associated with ventricular pre-excitation (Wolff–Parkinson–White syndrome), progressive conduction system disease and cardiac hypertrophy. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.^[7]

Interactions

PRKAG2 has been shown to interact with PRKAB2^[8] and PRKAB1.^[8]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000106617 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000028944 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Stapleton D, Mitchelhill KI, Gao G, Widmer J, Michell BJ, Teh T, et al. (January 1996). "Mammalian AMP-activated protein kinase subfamily". The Journal of Biological Chemistry. 271 (2): 611–614. doi:10.1074/jbc.271.2.611. PMID 8557660.
^ Gao G, Fernandez CS, Stapleton D, Auster AS, Widmer J, Dyck JR, et al. (April 1996). "Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-activated protein kinase". The Journal of Biological Chemistry. 271 (15): 8675–8681. doi:10.1074/jbc.271.15.8675. PMID 8621499.
^ ^a ^b "Entrez Gene: PRKAG2 protein kinase, AMP-activated, gamma 2 non-catalytic subunit".
^ ^a ^b Cheung PC, Salt IP, Davies SP, Hardie DG, Carling D (March 2000). "Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding". The Biochemical Journal. 346 Pt 3 (Pt 3): 659–669. doi:10.1042/0264-6021:3460659. PMC 1220898. PMID 10698692.

Gollob MH, Green MS, Tang AS, Roberts R (May 2002). "PRKAG2 cardiac syndrome: familial ventricular preexcitation, conduction system disease, and cardiac hypertrophy". Current Opinion in Cardiology. 17 (3): 229–234. doi:10.1097/00001573-200205000-00004. PMID 12015471. S2CID 33599152.
Gollob MH (February 2003). "Glycogen storage disease as a unifying mechanism of disease in the PRKAG2 cardiac syndrome". Biochemical Society Transactions. 31 (Pt 1): 228–231. doi:10.1042/BST0310228. PMID 12546691.
Ofir M, Hochhauser E, Vidne BA, Freimark D, Arad M (October 2007). "[AMP-activated protein kinase: how a mistake in energy gauge causes glycogen storage]". Harefuah. 146 (10): 770–5, 813–4. PMID 17990392.
Hofmann B, Nishanian P, Baldwin RL, Insixiengmay P, Nel A, Fahey JL (December 1990). "HIV inhibits the early steps of lymphocyte activation, including initiation of inositol phospholipid metabolism". Journal of Immunology. 145 (11): 3699–3705. doi:10.4049/jimmunol.145.11.3699. PMID 1978848.
MacRae CA, Ghaisas N, Kass S, Donnelly S, Basson CT, Watkins HC, et al. (September 1995). "Familial Hypertrophic cardiomyopathy with Wolff-Parkinson-White syndrome maps to a locus on chromosome 7q3". The Journal of Clinical Investigation. 96 (3): 1216–1220. doi:10.1172/JCI118154. PMC 185741. PMID 7657794.
Hofmann B, Nishanian P, Nguyen T, Insixiengmay P, Fahey JL (July 1993). "Human immunodeficiency virus proteins induce the inhibitory cAMP/protein kinase A pathway in normal lymphocytes". Proceedings of the National Academy of Sciences of the United States of America. 90 (14): 6676–6680. Bibcode:1993PNAS...90.6676H. doi:10.1073/pnas.90.14.6676. PMC 46995. PMID 7688126.
Hofmann B, Nishanian P, Fan J, Nguyen T, Fahey JL (July 1994). "HIV Gag p17 protein impairs proliferation of normal lymphocytes in vitro". AIDS. 8 (7): 1016–1017. doi:10.1097/00002030-199407000-00025. PMID 7946090.
Swingler S, Gallay P, Camaur D, Song J, Abo A, Trono D (June 1997). "The Nef protein of human immunodeficiency virus type 1 enhances serine phosphorylation of the viral matrix". Journal of Virology. 71 (6): 4372–4377. doi:10.1128/JVI.71.6.4372-4377.1997. PMC 191654. PMID 9151826.
Stapleton D, Woollatt E, Mitchelhill KI, Nicholl JK, Fernandez CS, Michell BJ, et al. (June 1997). "AMP-activated protein kinase isoenzyme family: subunit structure and chromosomal location". FEBS Letters. 409 (3): 452–456. Bibcode:1997FEBSL.409..452S. doi:10.1016/S0014-5793(97)00569-3. PMID 9224708. S2CID 39329574.
Chen P, Mayne M, Power C, Nath A (September 1997). "The Tat protein of HIV-1 induces tumor necrosis factor-alpha production. Implications for HIV-1-associated neurological diseases". The Journal of Biological Chemistry. 272 (36): 22385–22388. doi:10.1074/jbc.272.36.22385. PMID 9278385.
Zidovetzki R, Wang JL, Chen P, Jeyaseelan R, Hofman F (July 1998). "Human immunodeficiency virus Tat protein induces interleukin 6 mRNA expression in human brain endothelial cells via protein kinase C- and cAMP-dependent protein kinase pathways". AIDS Research and Human Retroviruses. 14 (10): 825–833. doi:10.1089/aid.1998.14.825. PMID 9671211.
Mayne M, Bratanich AC, Chen P, Rana F, Nath A, Power C (1998). "HIV-1 tat molecular diversity and induction of TNF-alpha: implications for HIV-induced neurological disease". Neuroimmunomodulation. 5 (3–4): 184–192. doi:10.1159/000026336. PMID 9730685. S2CID 19529677.
Sanger Centre T, Washington University Genome Sequencing Cente T (November 1998). "Toward a complete human genome sequence". Genome Research. 8 (11): 1097–1108. doi:10.1101/gr.8.11.1097. PMID 9847074.
Cheung PC, Salt IP, Davies SP, Hardie DG, Carling D (March 2000). "Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding". The Biochemical Journal. 346 Pt 3 (Pt 3): 659–669. doi:10.1042/0264-6021:3460659. PMC 1220898. PMID 10698692.
Lang T, Yu L, Tu Q, Jiang J, Chen Z, Xin Y, et al. (December 2000). "Molecular cloning, genomic organization, and mapping of PRKAG2, a heart abundant gamma2 subunit of 5'-AMP-activated protein kinase, to human chromosome 7q36". Genomics. 70 (2): 258–263. doi:10.1006/geno.2000.6376. PMID 11112354.
Blair E, Redwood C, Ashrafian H, Oliveira M, Broxholme J, Kerr B, et al. (May 2001). "Mutations in the gamma(2) subunit of AMP-activated protein kinase cause familial hypertrophic cardiomyopathy: evidence for the central role of energy compromise in disease pathogenesis". Human Molecular Genetics. 10 (11): 1215–1220. doi:10.1093/hmg/10.11.1215. PMID 11371514.
Gollob MH, Green MS, Tang AS, Gollob T, Karibe A, Ali Hassan AS, et al. (June 2001). "Identification of a gene responsible for familial Wolff-Parkinson-White syndrome". The New England Journal of Medicine. 344 (24): 1823–1831. doi:10.1056/NEJM200106143442403. PMID 11407343.
Hamilton SR, Stapleton D, O'Donnell JB, Kung JT, Dalal SR, Kemp BE, et al. (July 2001). "An activating mutation in the gamma1 subunit of the AMP-activated protein kinase". FEBS Letters. 500 (3): 163–168. Bibcode:2001FEBSL.500..163H. doi:10.1016/S0014-5793(01)02602-3. PMID 11445078. S2CID 85248755.

External links

GeneReviews/NCBI/NIH/UW entry on Familial Hypertrophic Cardiomyopathy Overview

This article on a gene on human chromosome 7 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000106617 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000028944 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8557660-5] Stapleton D, Mitchelhill KI, Gao G, Widmer J, Michell BJ, Teh T, et al. (January 1996). "Mammalian AMP-activated protein kinase subfamily". The Journal of Biological Chemistry. 271 (2): 611–614. doi:10.1074/jbc.271.2.611. PMID 8557660.

[pmid8621499-6] Gao G, Fernandez CS, Stapleton D, Auster AS, Widmer J, Dyck JR, et al. (April 1996). "Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-activated protein kinase". The Journal of Biological Chemistry. 271 (15): 8675–8681. doi:10.1074/jbc.271.15.8675. PMID 8621499.

[entrez-7] "Entrez Gene: PRKAG2 protein kinase, AMP-activated, gamma 2 non-catalytic subunit".

[pmid10698692-8] Cheung PC, Salt IP, Davies SP, Hardie DG, Carling D (March 2000). "Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding". The Biochemical Journal. 346 Pt 3 (Pt 3): 659–669. doi:10.1042/0264-6021:3460659. PMC 1220898. PMID 10698692.

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v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Function

Interactions

References

Further reading

External links