PRKAA2: Difference between revisions

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{{Infobox_gene}}
| update_page = yes
'''5'-AMP-activated protein kinase catalytic subunit alpha-2''' is an [[enzyme]] that in humans is encoded by the ''PRKAA2'' [[gene]].<ref name="pmid7959015">{{cite journal | vauthors = Aguan K, Scott J, See CG, Sarkar NH | title = Characterization and chromosomal localization of the human homologue of a rat AMP-activated protein kinase-encoding gene: a major regulator of lipid metabolism in mammals | journal = Gene | volume = 149 | issue = 2 | pages = 345–50 | date = Dec 1994 | pmid = 7959015 | pmc =  | doi = 10.1016/0378-1119(94)90174-0 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PRKAA2 protein kinase, AMP-activated, alpha 2 catalytic subunit| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5563| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_PRKAA2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2h6d.
| PDB = {{PDB2|2h6d}}
| Name = Protein kinase, AMP-activated, alpha 2 catalytic subunit
| HGNCid = 9377
| Symbol = PRKAA2
| AltSymbols =; AMPK; AMPK2; PRKAA
| OMIM = 600497
| ECnumber = 
| Homologene = 4551
| MGIid = 1336173
| GeneAtlas_image1 = PBB_GE_PRKAA2_207709_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006633 |text = fatty acid biosynthetic process}} {{GNF_GO|id=GO:0006695 |text = cholesterol biosynthetic process}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5563
    | Hs_Ensembl = ENSG00000162409
    | Hs_RefseqProtein = NP_006243
    | Hs_RefseqmRNA = NM_006252
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 56883583
    | Hs_GenLoc_end = 56953596
    | Hs_Uniprot = P54646
    | Mm_EntrezGene = 108079
    | Mm_Ensembl = ENSMUSG00000028518
    | Mm_RefseqmRNA = NM_178143
    | Mm_RefseqProtein = NP_835279
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 104532922
    | Mm_GenLoc_end = 104607801
    | Mm_Uniprot = Q8BRK8
  }}
}}
'''Protein kinase, AMP-activated, alpha 2 catalytic subunit''', also known as '''PRKAA2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRKAA2 protein kinase, AMP-activated, alpha 2 catalytic subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5563| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein encoded by this gene is a catalytic 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. Studies of the mouse counterpart suggest that this catalytic subunit may control whole-body insulin sensitivity and is necessary for maintaining myocardial energy homeostasis during ischemia.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a catalytic 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. Studies of the mouse counterpart suggest that this catalytic subunit may control whole-body insulin sensitivity and is necessary for maintaining myocardial energy homeostasis during ischemia.<ref name="entrez">{{cite web | title = Entrez Gene: PRKAA2 protein kinase, AMP-activated, alpha 2 catalytic subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5563| accessdate = }}</ref>
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Hardie DG, MacKintosh RW | title = AMP-activated protein kinase--an archetypal protein kinase cascade? | journal = BioEssays | volume = 14 | issue = 10 | pages = 699–704 | year = 1995 | pmid = 1365882 | doi = 10.1002/bies.950141011 }}
| citations =
* {{cite journal | vauthors = Hardie DG | title = Regulation of fatty acid and cholesterol metabolism by the AMP-activated protein kinase | journal = Biochim. Biophys. Acta | volume = 1123 | issue = 3 | pages = 231–8 | year = 1992 | pmid = 1536860 | doi = 10.1016/0005-2760(92)90001-c }}
*{{cite journal | author=Hardie DG, MacKintosh RW |title=AMP-activated protein kinase--an archetypal protein kinase cascade? |journal=Bioessays |volume=14 |issue= 10 |pages= 699-704 |year= 1995 |pmid= 1365882 |doi= 10.1002/bies.950141011 }}
* {{cite journal | vauthors = Carling D | title = The AMP-activated protein kinase cascade--a unifying system for energy control | journal = Trends Biochem. Sci. | volume = 29 | issue = 1 | pages = 18–24 | year = 2004 | pmid = 14729328 | doi = 10.1016/j.tibs.2003.11.005 }}
*{{cite journal | author=Hardie DG |title=Regulation of fatty acid and cholesterol metabolism by the AMP-activated protein kinase. |journal=Biochim. Biophys. Acta |volume=1123 |issue= 3 |pages= 231-8 |year= 1992 |pmid= 1536860 |doi= }}
* {{cite journal | vauthors = Beri RK, Marley AE, See CG, Sopwith WF, Aguan K, Carling D, Scott J, Carey F | title = Molecular cloning, expression and chromosomal localisation of human AMP-activated protein kinase | journal = FEBS Lett. | volume = 356 | issue = 1 | pages = 117–21 | year = 1995 | pmid = 7988703 | doi = 10.1016/0014-5793(94)01247-4 }}
*{{cite journal | author=Carling D |title=The AMP-activated protein kinase cascade--a unifying system for energy control. |journal=Trends Biochem. Sci. |volume=29 |issue= 1 |pages= 18-24 |year= 2004 |pmid= 14729328 |doi= }}
* {{cite journal | vauthors = Bonaldo MF, Lennon G, Soares MB | title = Normalization and subtraction: two approaches to facilitate gene discovery | journal = Genome Res. | volume = 6 | issue = 9 | pages = 791–806 | year = 1997 | pmid = 8889548 | doi = 10.1101/gr.6.9.791 }}
*{{cite journal  | author=Aguan K, Scott J, See CG, Sarkar NH |title=Characterization and chromosomal localization of the human homologue of a rat AMP-activated protein kinase-encoding gene: a major regulator of lipid metabolism in mammals. |journal=Gene |volume=149 |issue= 2 |pages= 345-50 |year= 1994 |pmid= 7959015 |doi=  }}
* {{cite journal | vauthors = Vavvas D, Apazidis A, Saha AK, Gamble J, Patel A, Kemp BE, Witters LA, Ruderman NB | title = Contraction-induced changes in acetyl-CoA carboxylase and 5'-AMP-activated kinase in skeletal muscle | journal = J. Biol. Chem. | volume = 272 | issue = 20 | pages = 13255–61 | year = 1997 | pmid = 9148944 | doi = 10.1074/jbc.272.20.13255 }}
*{{cite journal | author=Beri RK, Marley AE, See CG, ''et al.'' |title=Molecular cloning, expression and chromosomal localisation of human AMP-activated protein kinase. |journal=FEBS Lett. |volume=356 |issue= 1 |pages= 117-21 |year= 1995 |pmid= 7988703 |doi= }}
* {{cite journal | vauthors = Stapleton D, Woollatt E, Mitchelhill KI, Nicholl JK, Fernandez CS, Michell BJ, Witters LA, Power DA, Sutherland GR, Kemp BE | title = AMP-activated protein kinase isoenzyme family: subunit structure and chromosomal location | journal = FEBS Lett. | volume = 409 | issue = 3 | pages = 452–6 | year = 1997 | pmid = 9224708 | doi = 10.1016/S0014-5793(97)00569-3 }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
* {{cite journal | vauthors = Stein SC, Woods A, Jones NA, Davison MD, Carling D | title = The regulation of AMP-activated protein kinase by phosphorylation | journal = Biochem. J. | volume = 345 | issue = 3 | pages = 437–43 | year = 2000 | pmid = 10642499 | pmc = 1220775 | doi = 10.1042/0264-6021:3450437 }}
*{{cite journal | author=Vavvas D, Apazidis A, Saha AK, ''et al.'' |title=Contraction-induced changes in acetyl-CoA carboxylase and 5'-AMP-activated kinase in skeletal muscle. |journal=J. Biol. Chem. |volume=272 |issue= 20 |pages= 13255-61 |year= 1997 |pmid= 9148944 |doi= }}
* {{cite journal | vauthors = da Silva Xavier G, Leclerc I, Salt IP, Doiron B, Hardie DG, Kahn A, Rutter GA | title = Role of AMP-activated protein kinase in the regulation by glucose of islet beta cell gene expression | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 97 | issue = 8 | pages = 4023–8 | year = 2000 | pmid = 10760274 | pmc = 18135 | doi = 10.1073/pnas.97.8.4023 }}
*{{cite journal | author=Stapleton D, Woollatt E, Mitchelhill KI, ''et al.'' |title=AMP-activated protein kinase isoenzyme family: subunit structure and chromosomal location. |journal=FEBS Lett. |volume=409 |issue= 3 |pages= 452-6 |year= 1997 |pmid= 9224708 |doi= }}
* {{cite journal | vauthors = Mu J, Brozinick JT, Valladares O, Bucan M, Birnbaum MJ | title = A role for AMP-activated protein kinase in contraction- and hypoxia-regulated glucose transport in skeletal muscle | journal = Mol. Cell | volume = 7 | issue = 5 | pages = 1085–94 | year = 2001 | pmid = 11389854 | doi = 10.1016/S1097-2765(01)00251-9 }}
*{{cite journal | author=Stein SC, Woods A, Jones NA, ''et al.'' |title=The regulation of AMP-activated protein kinase by phosphorylation. |journal=Biochem. J. |volume=345 Pt 3 |issue= |pages= 437-43 |year= 2000 |pmid= 10642499 |doi= }}
* {{cite journal | vauthors = Minokoshi Y, Kim YB, Peroni OD, Fryer LG, Müller C, Carling D, Kahn BB | title = Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase | journal = Nature | volume = 415 | issue = 6869 | pages = 339–43 | year = 2002 | pmid = 11797013 | doi = 10.1038/415339a }}
*{{cite journal | author=da Silva Xavier G, Leclerc I, Salt IP, ''et al.'' |title=Role of AMP-activated protein kinase in the regulation by glucose of islet beta cell gene expression. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 8 |pages= 4023-8 |year= 2000 |pmid= 10760274 |doi= }}
* {{cite journal | vauthors = Dubbelhuis PF, Meijer AJ | title = Hepatic amino acid-dependent signaling is under the control of AMP-dependent protein kinase | journal = FEBS Lett. | volume = 521 | issue = 1–3 | pages = 39–42 | year = 2002 | pmid = 12067722 | doi = 10.1016/S0014-5793(02)02815-6 }}
*{{cite journal | author=Mu J, Brozinick JT, Valladares O, ''et al.'' |title=A role for AMP-activated protein kinase in contraction- and hypoxia-regulated glucose transport in skeletal muscle. |journal=Mol. Cell |volume=7 |issue= 5 |pages= 1085-94 |year= 2001 |pmid= 11389854 |doi= }}
* {{cite journal | vauthors = Esumi H, Izuishi K, Kato K, Hashimoto K, Kurashima Y, Kishimoto A, Ogura T, Ozawa T | title = Hypoxia and nitric oxide treatment confer tolerance to glucose starvation in a 5'-AMP-activated protein kinase-dependent manner | journal = J. Biol. Chem. | volume = 277 | issue = 36 | pages = 32791–8 | year = 2002 | pmid = 12091379 | doi = 10.1074/jbc.M112270200 }}
*{{cite journal | author=Minokoshi Y, Kim YB, Peroni OD, ''et al.'' |title=Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase. |journal=Nature |volume=415 |issue= 6869 |pages= 339-43 |year= 2002 |pmid= 11797013 |doi= 10.1038/415339a }}
* {{cite journal | vauthors = Nielsen JN, Mustard KJ, Graham DA, Yu H, MacDonald CS, Pilegaard H, Goodyear LJ, Hardie DG, Richter EA, Wojtaszewski JF | title = 5'-AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle | journal = J. Appl. Physiol. | volume = 94 | issue = 2 | pages = 631–41 | year = 2003 | pmid = 12391032 | doi = 10.1152/japplphysiol.00642.2002 }}
*{{cite journal | author=Dubbelhuis PF, Meijer AJ |title=Hepatic amino acid-dependent signaling is under the control of AMP-dependent protein kinase. |journal=FEBS Lett. |volume=521 |issue= 1-3 |pages= 39-42 |year= 2002 |pmid= 12067722 |doi= }}
* {{cite journal | vauthors = Wojtaszewski JF, Mourtzakis M, Hillig T, Saltin B, Pilegaard H | title = Dissociation of AMPK activity and ACCbeta phosphorylation in human muscle during prolonged exercise | journal = Biochem. Biophys. Res. Commun. | volume = 298 | issue = 3 | pages = 309–16 | year = 2002 | pmid = 12413941 | doi = 10.1016/S0006-291X(02)02465-8 }}
*{{cite journal | author=Esumi H, Izuishi K, Kato K, ''et al.'' |title=Hypoxia and nitric oxide treatment confer tolerance to glucose starvation in a 5'-AMP-activated protein kinase-dependent manner. |journal=J. Biol. Chem. |volume=277 |issue= 36 |pages= 32791-8 |year= 2002 |pmid= 12091379 |doi= 10.1074/jbc.M112270200 }}
* {{cite journal | vauthors = Hallows KR, McCane JE, Kemp BE, Witters LA, Foskett JK | title = Regulation of channel gating by AMP-activated protein kinase modulates cystic fibrosis transmembrane conductance regulator activity in lung submucosal cells | journal = J. Biol. Chem. | volume = 278 | issue = 2 | pages = 998–1004 | year = 2003 | pmid = 12427743 | doi = 10.1074/jbc.M210621200 }}
*{{cite journal | author=Nielsen JN, Mustard KJ, Graham DA, ''et al.'' |title=5'-AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle. |journal=J. Appl. Physiol. |volume=94 |issue= 2 |pages= 631-41 |year= 2003 |pmid= 12391032 |doi= 10.1152/japplphysiol.00642.2002 }}
* {{cite journal | vauthors = Zong H, Ren JM, Young LH, Pypaert M, Mu J, Birnbaum MJ, Shulman GI | title = AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 99 | issue = 25 | pages = 15983–7 | year = 2003 | pmid = 12444247 | pmc = 138551 | doi = 10.1073/pnas.252625599 }}
*{{cite journal | author=Wojtaszewski JF, Mourtzakis M, Hillig T, ''et al.'' |title=Dissociation of AMPK activity and ACCbeta phosphorylation in human muscle during prolonged exercise. |journal=Biochem. Biophys. Res. Commun. |volume=298 |issue= 3 |pages= 309-16 |year= 2002 |pmid= 12413941 |doi= }}
*{{cite journal | author=Hallows KR, McCane JE, Kemp BE, ''et al.'' |title=Regulation of channel gating by AMP-activated protein kinase modulates cystic fibrosis transmembrane conductance regulator activity in lung submucosal cells. |journal=J. Biol. Chem. |volume=278 |issue= 2 |pages= 998-1004 |year= 2003 |pmid= 12427743 |doi= 10.1074/jbc.M210621200 }}
*{{cite journal | author=Zong H, Ren JM, Young LH, ''et al.'' |title=AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 25 |pages= 15983-7 |year= 2003 |pmid= 12444247 |doi= 10.1073/pnas.252625599 }}
}}
{{refend}}
{{refend}}


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Revision as of 18:40, 7 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

5'-AMP-activated protein kinase catalytic subunit alpha-2 is an enzyme that in humans is encoded by the PRKAA2 gene.[1][2]

Function

The protein encoded by this gene is a catalytic 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. Studies of the mouse counterpart suggest that this catalytic subunit may control whole-body insulin sensitivity and is necessary for maintaining myocardial energy homeostasis during ischemia.[2]

References

  1. ↑ Aguan K, Scott J, See CG, Sarkar NH (Dec 1994). "Characterization and chromosomal localization of the human homologue of a rat AMP-activated protein kinase-encoding gene: a major regulator of lipid metabolism in mammals". Gene. 149 (2): 345–50. doi:10.1016/0378-1119(94)90174-0. PMID 7959015.
  2. ↑ 2.0 2.1 "Entrez Gene: PRKAA2 protein kinase, AMP-activated, alpha 2 catalytic subunit".

Further reading


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