PRKAG1

Protein-coding gene in the species Homo sapiens
PRKAG1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2UV4, 2UV5, 2UV6, 2UV7, 4CFE, 4CFF, 4RER, 4REW, 5EZV, 4ZHX

Identifiers
AliasesPRKAG1, AMPKG, protein kinase AMP-activated non-catalytic subunit gamma 1
External IDsOMIM: 602742; MGI: 108411; HomoloGene: 99712; GeneCards: PRKAG1; OMA:PRKAG1 - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for PRKAG1
Genomic location for PRKAG1
Band12q13.12Start49,002,274 bp[1]
End49,018,807 bp[1]
Gene location (Mouse)
Chromosome 15 (mouse)
Chr.Chromosome 15 (mouse)[2]
Chromosome 15 (mouse)
Genomic location for PRKAG1
Genomic location for PRKAG1
Band15 F1|15 54.73 cMStart98,710,678 bp[2]
End98,729,402 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • gastrocnemius muscle

  • islet of Langerhans

  • left ventricle

  • left adrenal gland

  • triceps brachii muscle

  • rectum

  • Achilles tendon

  • right coronary artery

  • body of pancreas

  • monocyte
Top expressed in
  • saccule

  • otic placode

  • right ventricle

  • molar

  • internal carotid artery

  • external carotid artery

  • lip

  • pyloric antrum

  • ciliary body

  • renal corpuscle
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • nucleotide binding
  • protein kinase activity
  • cAMP-dependent protein kinase activity
  • ADP binding
  • AMP-activated protein kinase activity
  • AMP binding
  • protein binding
  • cAMP-dependent protein kinase regulator activity
  • protein kinase binding
  • ATP binding
  • adenyl ribonucleotide binding
Cellular component
  • cytosol
  • membrane
  • nucleotide-activated protein kinase complex
  • extracellular exosome
  • nucleus
  • nucleoplasm
Biological process
  • lipid metabolism
  • fatty acid metabolic process
  • regulation of glycolytic process
  • protein phosphorylation
  • positive regulation of gene expression
  • fatty acid biosynthetic process
  • spermatogenesis
  • macroautophagy
  • signal transduction
  • positive regulation of protein kinase activity
  • regulation of signal transduction by p53 class mediator
  • regulation of macroautophagy
  • import into nucleus
  • regulation of protein serine/threonine kinase activity
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5571

19082

Ensembl

ENSG00000181929

ENSMUSG00000067713

UniProt

P54619

O54950

RefSeq (mRNA)

NM_001206709
NM_001206710
NM_002733
NM_212461

NM_016781

RefSeq (protein)

NP_001193638
NP_001193639
NP_002724

NP_058061

Location (UCSC)Chr 12: 49 – 49.02 MbChr 15: 98.71 – 98.73 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

5'-AMP-activated protein kinase subunit gamma-1 is an enzyme that in humans is encoded by the PRKAG1 gene.[5][6][7]

Function

The protein encoded by this gene is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. This subunit is one of the gamma regulatory subunits of AMPK. Alternatively spliced transcript variants encoding distinct isoforms have been observed.[7]

Interactions

PRKAG1 has been shown to interact with PRKAB2[8] and PRKAB1.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000181929 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000067713 – 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 (January 1996). "Mammalian AMP-activated protein kinase subfamily". The Journal of Biological Chemistry. 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 (April 1996). "Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-activated protein kinase". The Journal of Biological Chemistry. 271 (15): 8675–81. doi:10.1074/jbc.271.15.8675. PMID 8621499.
  7. ^ a b "Entrez Gene: PRKAG1 protein kinase, AMP-activated, gamma 1 non-catalytic subunit".
  8. ^ 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 (3): 659–69. doi:10.1042/0264-6021:3460659. PMC 1220898. PMID 10698692.

Further reading

  • 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): 3699–705. doi:10.4049/jimmunol.145.11.3699. PMID 1978848. S2CID 39230415.
  • Beebe SJ, Oyen O, Sandberg M, Frøysa A, Hansson V, Jahnsen T (March 1990). "Molecular cloning of a tissue-specific protein kinase (C gamma) from human testis--representing a third isoform for the catalytic subunit of cAMP-dependent protein kinase". Molecular Endocrinology. 4 (3): 465–75. doi:10.1210/mend-4-3-465. PMID 2342480.
  • 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): 6676–80. 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): 1016–7. doi:10.1097/00002030-199407000-00025. PMID 7946090.
  • Woods A, Cheung PC, Smith FC, Davison MD, Scott J, Beri RK, Carling D (April 1996). "Characterization of AMP-activated protein kinase beta and gamma subunits. Assembly of the heterotrimeric complex in vitro". The Journal of Biological Chemistry. 271 (17): 10282–90. doi:10.1074/jbc.271.48.30517. PMID 8626596.
  • Dyck JR, Gao G, Widmer J, Stapleton D, Fernandez CS, Kemp BE, Witters LA (July 1996). "Regulation of 5'-AMP-activated protein kinase activity by the noncatalytic beta and gamma subunits". The Journal of Biological Chemistry. 271 (30): 17798–803. doi:10.1074/jbc.271.30.17798. PMID 8663446.
  • Bonaldo MF, Lennon G, Soares MB (September 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • 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): 4372–7. 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, Witters LA, Power DA, Sutherland GR, Kemp BE (June 1997). "AMP-activated protein kinase isoenzyme family: subunit structure and chromosomal location". FEBS Letters. 409 (3): 452–6. 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): 22385–8. doi:10.1074/jbc.272.36.22385. PMID 9278385.
  • Reinton N, Haugen TB, Orstavik S, Skålhegg BS, Hansson V, Jahnsen T, Taskén K (April 1998). "The gene encoding the C gamma catalytic subunit of cAMP-dependent protein kinase is a transcribed retroposon". Genomics. 49 (2): 290–7. doi:10.1006/geno.1998.5240. PMID 9598317.
  • 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): 825–33. 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): 184–92. doi:10.1159/000026336. PMID 9730685. S2CID 19529677.
  • 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 (3): 659–69. doi:10.1042/0264-6021:3460659. PMC 1220898. PMID 10698692.
  • Hamilton SR, Stapleton D, O'Donnell JB, Kung JT, Dalal SR, Kemp BE, Witters LA (July 2001). "An activating mutation in the gamma1 subunit of the AMP-activated protein kinase". FEBS Letters. 500 (3): 163–8. doi:10.1016/S0014-5793(01)02602-3. PMID 11445078. S2CID 85248755.
  • Minokoshi Y, Alquier T, Furukawa N, Kim YB, Lee A, Xue B, Mu J, Foufelle F, Ferré P, Birnbaum MJ, Stuck BJ, Kahn BB (April 2004). "AMP-kinase regulates food intake by responding to hormonal and nutrient signals in the hypothalamus". Nature. 428 (6982): 569–74. Bibcode:2004Natur.428..569M. doi:10.1038/nature02440. PMID 15058305. S2CID 4302317.

External links

  • PDBe-KB provides an overview of all the structure information available in the PDB for Human 5'-AMP-activated protein kinase subunit gamma-1 (PRKAG1)
  • v
  • t
  • e
  • 2uv4: CRYSTAL STRUCTURE OF A CBS DOMAIN PAIR FROM THE REGULATORY GAMMA1 SUBUNIT OF HUMAN AMPK IN COMPLEX WITH AMP
    2uv4: CRYSTAL STRUCTURE OF A CBS DOMAIN PAIR FROM THE REGULATORY GAMMA1 SUBUNIT OF HUMAN AMPK IN COMPLEX WITH AMP
  • 2uv5: CRYSTAL STRUCTURE OF A CBS DOMAIN PAIR FROM THE REGULATORY GAMMA1 SUBUNIT OF HUMAN AMPK IN COMPLEX WITH AMP
    2uv5: CRYSTAL STRUCTURE OF A CBS DOMAIN PAIR FROM THE REGULATORY GAMMA1 SUBUNIT OF HUMAN AMPK IN COMPLEX WITH AMP
  • 2uv6: CRYSTAL STRUCTURE OF A CBS DOMAIN PAIR FROM THE REGULATORY GAMMA1 SUBUNIT OF HUMAN AMPK IN COMPLEX WITH AMP
    2uv6: CRYSTAL STRUCTURE OF A CBS DOMAIN PAIR FROM THE REGULATORY GAMMA1 SUBUNIT OF HUMAN AMPK IN COMPLEX WITH AMP
  • 2uv7: CRYSTAL STRUCTURE OF A CBS DOMAIN PAIR FROM THE REGULATORY GAMMA1 SUBUNIT OF HUMAN AMPK IN COMPLEX WITH AMP
    2uv7: CRYSTAL STRUCTURE OF A CBS DOMAIN PAIR FROM THE REGULATORY GAMMA1 SUBUNIT OF HUMAN AMPK IN COMPLEX WITH AMP
  • v
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  • e
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)
  • -
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)
  • -
Tropomyosin kinase (EC 2.7.11.28)
  • -
Low-density-lipoprotein receptor kinase (EC 2.7.11.29)
  • -
Receptor protein serine/threonine kinase (EC 2.7.11.30)
MAP2K
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