PRKAG2

Protein-coding gene in the species Homo sapiens
PRKAG2
Identifiers
AliasesPRKAG2, AAKG, AAKG2, CMH6, H91620p, WPWS, protein kinase AMP-activated non-catalytic subunit gamma 2
External IDsOMIM: 602743 MGI: 1336153 HomoloGene: 136125 GeneCards: PRKAG2
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)[1]
Chromosome 7 (human)
Genomic location for PRKAG2
Genomic location for PRKAG2
Band7q36.1Start151,556,124 bp[1]
End151,877,125 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for PRKAG2
Genomic location for PRKAG2
Band5|5 A3Start25,067,742 bp[2]
End25,305,640 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right coronary artery

  • left ventricle

  • left coronary artery

  • popliteal artery

  • gastric mucosa

  • nucleus accumbens

  • monocyte

  • caudate nucleus

  • right lobe of liver

  • putamen
Top expressed in
  • seminiferous tubule

  • atrium

  • spermatid

  • superior frontal gyrus

  • atrioventricular valve

  • spermatocyte

  • subiculum

  • olfactory tubercle

  • cerebellar cortex

  • endocardial cushion
More reference expression data
BioGPS
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
SpeciesHumanMouse
Entrez

51422

108099

Ensembl

ENSG00000106617

ENSMUSG00000028944

UniProt

Q9UGJ0

Q91WG5

RefSeq (mRNA)
NM_001040633
NM_001304527
NM_001304531
NM_016203
NM_024429

NM_001363698

NM_001170555
NM_001170556
NM_145401
NM_001310480

RefSeq (protein)
NP_001035723
NP_001291456
NP_001291460
NP_057287
NP_077747

NP_001350627

NP_001164026
NP_001164027
NP_001297409
NP_663376

Location (UCSC)Chr 7: 151.56 – 151.88 MbChr 5: 25.07 – 25.31 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000106617 – Ensembl, May 2017
  2. ^ a b c 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.
  5. ^ Stapleton D, Mitchelhill KI, Gao G, Widmer J, Michell BJ, Teh T, House CM, Fernandez CS, Cox T, Witters LA, Kemp BE (February 1996). "Mammalian AMP-activated protein kinase subfamily". J Biol Chem. 271 (2): 611–4. doi:10.1074/jbc.271.2.611. PMID 8557660.
  6. ^ Gao G, Fernandez CS, Stapleton D, Auster AS, Widmer J, Dyck JR, Kemp BE, Witters LA (June 1996). "Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-activated protein kinase". J Biol Chem. 271 (15): 8675–81. doi:10.1074/jbc.271.15.8675. PMID 8621499.
  7. ^ a b "Entrez Gene: PRKAG2 protein kinase, AMP-activated, gamma 2 non-catalytic subunit".
  8. ^ a b Cheung PC, Salt I P, Davies S P, Hardie D G, Carling D (March 2000). "Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding". Biochem. J. 346 Pt 3 (3). ENGLAND: 659–69. doi:10.1042/0264-6021:3460659. ISSN 0264-6021. PMC 1220898. PMID 10698692.

Further reading

  • Gollob MH, Green MS, Tang AS, Roberts R (2002). "PRKAG2 cardiac syndrome: familial ventricular preexcitation, conduction system disease, and cardiac hypertrophy". Curr. Opin. Cardiol. 17 (3): 229–34. doi:10.1097/00001573-200205000-00004. PMID 12015471. S2CID 33599152.
  • Gollob MH (2003). "Glycogen storage disease as a unifying mechanism of disease in the PRKAG2 cardiac syndrome". Biochem. Soc. Trans. 31 (Pt 1): 228–31. doi:10.1042/BST0310228. PMID 12546691.
  • Ofir M, Hochhauser E, Vidne BA, et al. (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, et al. (1991). "HIV inhibits the early steps of lymphocyte activation, including initiation of inositol phospholipid metabolism". J. Immunol. 145 (11): 3699–705. doi:10.4049/jimmunol.145.11.3699. PMID 1978848.
  • MacRae CA, Ghaisas N, Kass S, et al. (1995). "Familial Hypertrophic cardiomyopathy with Wolff-Parkinson-White syndrome maps to a locus on chromosome 7q3" (PDF). J. Clin. Invest. 96 (3): 1216–20. doi:10.1172/JCI118154. PMC 185741. PMID 7657794.
  • Hofmann B, Nishanian P, Nguyen T, et al. (1993). "Human immunodeficiency virus proteins induce the inhibitory cAMP/protein kinase A pathway in normal lymphocytes". Proc. Natl. Acad. Sci. U.S.A. 90 (14): 6676–80. Bibcode:1993PNAS...90.6676H. doi:10.1073/pnas.90.14.6676. PMC 46995. PMID 7688126.
  • Hofmann B, Nishanian P, Fan J, et al. (1994). "HIV Gag p17 protein impairs proliferation of normal lymphocytes in vitro". AIDS. 8 (7): 1016–7. doi:10.1097/00002030-199407000-00025. PMID 7946090.
  • Swingler S, Gallay P, Camaur D, et al. (1997). "The Nef protein of human immunodeficiency virus type 1 enhances serine phosphorylation of the viral matrix". J. Virol. 71 (6): 4372–7. doi:10.1128/JVI.71.6.4372-4377.1997. PMC 191654. PMID 9151826.
  • Stapleton D, Woollatt E, Mitchelhill KI, et al. (1997). "AMP-activated protein kinase isoenzyme family: subunit structure and chromosomal location". FEBS Lett. 409 (3): 452–6. doi:10.1016/S0014-5793(97)00569-3. PMID 9224708. S2CID 39329574.
  • Chen P, Mayne M, Power C, Nath A (1997). "The Tat protein of HIV-1 induces tumor necrosis factor-alpha production. Implications for HIV-1-associated neurological diseases". J. Biol. Chem. 272 (36): 22385–8. doi:10.1074/jbc.272.36.22385. PMID 9278385.
  • Zidovetzki R, Wang JL, Chen P, et al. (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 Res. Hum. Retroviruses. 14 (10): 825–33. doi:10.1089/aid.1998.14.825. PMID 9671211.
  • Mayne M, Bratanich AC, Chen P, et al. (1998). "HIV-1 tat molecular diversity and induction of TNF-alpha: implications for HIV-induced neurological disease". Neuroimmunomodulation. 5 (3–4): 184–92. doi:10.1159/000026336. PMID 9730685. S2CID 19529677.
  • Sanger Centre T, Washington University Genome Sequencing Cente T (1999). "Toward a complete human genome sequence". Genome Res. 8 (11): 1097–108. doi:10.1101/gr.8.11.1097. PMID 9847074.
  • Cheung PC, Salt IP, Davies SP, et al. (2000). "Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding". Biochem. J. 346 Pt 3 (3): 659–69. doi:10.1042/0264-6021:3460659. PMC 1220898. PMID 10698692.
  • Lang T, Yu L, Tu Q, et al. (2001). "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): 258–63. doi:10.1006/geno.2000.6376. PMID 11112354.
  • Blair E, Redwood C, Ashrafian H, et al. (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". Hum. Mol. Genet. 10 (11): 1215–20. doi:10.1093/hmg/10.11.1215. PMID 11371514.
  • Gollob MH, Green MS, Tang AS, et al. (2001). "Identification of a gene responsible for familial Wolff-Parkinson-White syndrome". N. Engl. J. Med. 344 (24): 1823–31. doi:10.1056/NEJM200106143442403. PMID 11407343.
  • Hamilton SR, Stapleton D, O'Donnell JB, et al. (2001). "An activating mutation in the gamma1 subunit of the AMP-activated protein kinase". FEBS Lett. 500 (3): 163–8. doi:10.1016/S0014-5793(01)02602-3. PMID 11445078. S2CID 85248755.

External links

  • GeneReviews/NCBI/NIH/UW entry on Familial Hypertrophic Cardiomyopathy Overview
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Non-specific serine/threonine protein kinases (EC 2.7.11.1)
Pyruvate dehydrogenase kinase (EC 2.7.11.2)
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)
Myosin-heavy-chain kinase (EC 2.7.11.7)
Fas-activated serine/threonine kinase (EC 2.7.11.8)
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)
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IκB kinase (EC 2.7.11.10)
cAMP-dependent protein kinase (EC 2.7.11.11)
cGMP-dependent protein kinase (EC 2.7.11.12)
Protein kinase C (EC 2.7.11.13)
Rhodopsin kinase (EC 2.7.11.14)
Beta adrenergic receptor kinase (EC 2.7.11.15)
G-protein coupled receptor kinases (EC 2.7.11.16)
Ca2+/calmodulin-dependent (EC 2.7.11.17)
Myosin light-chain kinase (EC 2.7.11.18)
Phosphorylase kinase (EC 2.7.11.19)
Elongation factor 2 kinase (EC 2.7.11.20)
Polo kinase (EC 2.7.11.21)
Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)
Polo kinase (EC 2.7.11.21)
Cyclin-dependent kinase (EC 2.7.11.22)
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)
Mitogen-activated protein kinase (EC 2.7.11.24)
MAP3K (EC 2.7.11.25)
Tau-protein kinase (EC 2.7.11.26)
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)
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Tropomyosin kinase (EC 2.7.11.28)
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Low-density-lipoprotein receptor kinase (EC 2.7.11.29)
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Receptor protein serine/threonine kinase (EC 2.7.11.30)
MAP2K
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