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Index > Protein center > Prkaa2(Gene name) > Rat
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  • Prkaa2 (Gene name),
  • 5'-AMP-activated protein kinase catalytic subunit alpha-2 (Protein name ),  AAPK2_RAT from NCBI database.
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  • General Annotation
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  • Antigen Annotation
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  • Gene name:
    Prkaa2(Ampk;Ampk2);
    Protein name:
    5'-AMP-activated protein kinase catalytic subunit alpha-2(AMPK subunit alpha-2);
    Alternative:
    2.7.11.31;Hydroxymethylglutaryl-CoA reductase kinase(HMGCR kinase);2.7.11.27;Acetyl-CoA carboxylase kinase(ACACA kinase);
    Organism:
    Rat (Rattus norvegicus). 
    General Annotation
    Sub Unit:
    AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with FNIP1 and FNIP2.
    Function:
    Catalytic 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. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ULK1. AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1.
    Subcellular Location:
    Cytoplasm Nucleus In response to stress, recruited by p53/TP53 to specific promoters.
    Protein Attributes:
    Sequence length:
    552
    Sequence:
    50:
    MAEKQKHDGR | VKIGHYVLGD | TLGVGTFGKV | KIGEHQLTGH | KVAVKILNRQ | 
    100:
    KIRSLDVVGK | IKREIQNLKL | FRHPHIIKLY | QVISTPTDFF | MVMEYVSGGE | 
    150:
    LFDYICKHGR | VEEVEARRLF | QQILSAVDYC | HRHMVVHRDL | KPENVLLDAQ | 
    200:
    MNAKIADFGL | SNMMSDGEFL | RTSCGSPNYA | APEVISGRLY | AGPEVDIWSC | 
    250:
    GVILYALLCG | TLPFDDEHVP | TLFKKIRGGV | FYIPEYLNRS | IATLLMHMLQ | 
    300:
    VDPLKRATIK | DIREHEWFKQ | DLPSYLFPED | PSYDANVIDD | EAVKEVCEKF | 
    350:
    ECTESEVMNS | LYSGDPQDQL | AVAYHLIIDN | RRIMNQASEF | YLASSPPTGS | 
    400:
    FMDDMAMHIP | PGLKPHPERM | PPLIADSPKA | RCPLDALNTT | KPKSLAVKKA | 
    450:
    KWHLGIRSQS | KPYDIMAEVY | RAMKQLDFEW | KVVNAYHLRV | RRKNPVTGNY | 
    500:
    VKMSLQLYLV | DNRSYLLDFK | SIDDEVVEQR | SGSSTPQRSC | SAAGLHRPRS | 
    550:
    SVDSSTAENH | SLSGSLTGSL | TGSTLSSASP | RLGSHTMDFF | EMCASLITAL | 
    552:
    AR
    3D Structure:
    N/A
    Predicted Eptitope:
    Please Sign in.
    EIAab Sequence  Vaild Sequence:
    Please Sign in.
    Related Databases
    String:
    UniGene:
    SMR:
    Pfam:
    KEGG:
    Uniprot:
     
    FOR
    ELISA Kit for Rat AMPK subunit alpha-2
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    E10189h
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    ELISA Kit for Rat AMPK subunit alpha-2
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    E10189p
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    ELISA Kit for Rat AMPK subunit alpha-2
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    E10189m
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    ELISA Kit for Rat AMPK subunit alpha-2
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    E10189r
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    CLIA Kit for Rat AMPK subunit alpha-2
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    CLIA Kit for Rat AMPK subunit alpha-2
    Cat.:
    U10189h
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    Packing:
    96T
    CLIA Kit for Rat AMPK subunit alpha-2
    Cat.:
    U10189r
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    MSDS:
    Please sign in first.
    Packing:
    96T
    CLIA Kit for Rat AMPK subunit alpha-2
    Cat.:
    U10189m
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    MSDS:
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    Packing:
    96T
    Polyclonal Antibody for Rat AMPK subunit alpha-2
    Cat.:
    P10189Rb-h
    Price:
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    Packing:
    40ug/0.2ml
    Polyclonal Antibody for Rat AMPK subunit alpha-2
    Polyclonal Antibody for Rat AMPK subunit alpha-2
    Polyclonal Antibody for Rat AMPK subunit alpha-2
    Monoclonal Antibody for Rat AMPK subunit alpha-2
    Monoclonal Antibody for Rat AMPK subunit alpha-2
    Monoclonal Antibody for Rat AMPK subunit alpha-2
    Monoclonal Antibody for Rat AMPK subunit alpha-2
    Protein for Rat AMPK subunit alpha-2
    Protein for Rat AMPK subunit alpha-2
    Protein for Rat AMPK subunit alpha-2
    Protein for Rat AMPK subunit alpha-2

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    References
    1. 1.
      "Mammalian AMP-activated protein kinase is homologous to yeast and plant protein kinases involved in the regulation of carbon metabolism."
      Carling D. , Aguan K. , Woods A. , Verhoeven A.J.M. , Beri R.K. , Brennan C.H. , Sidebottom C. , Davison M.D. , Scott J.
      J. Biol. Chem.269:11442-11448(1994) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT);PARTIAL PROTEIN SEQUENCE
      tissue: Liver.
    2. 2.
      "Catalytic subunits of the porcine and rat 5'-AMP-activated protein kinase are members of the SNF1 protein kinase family."
      Gao G. , Widmer J. , Stapleton D. , Teh T. , Cox T. , Kemp B.E. , Witters L.A.
      Biochim. Biophys. Acta1266:73-82(1995) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG)
      strain: Sprague-Dawley.
      tissue: Liver.
    3. 3.
      "Regulation of HMG-CoA reductase: identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liver."
      Clarke P.R. , Hardie D.G.
      EMBO J.9:2439-2446(1990) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: CATALYTIC ACTIVITY;FUNCTION IN PHOSPHORYLATION OF HMGCR
    4. 4.
      "Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase."
      Hawley S.A. , Davison M. , Woods A. , Davies S.P. , Beri R.K. , Carling D. , Hardie D.G.
      J. Biol. Chem.271:27879-27887(1996) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION AT THR-172;ENZYME REGULATION
    5. 5.
      "Phosphorylation of rat muscle acetyl-CoA carboxylase by AMP-activated protein kinase and protein kinase A."
      Winder W.W. , Wilson H.A. , Hardie D.G. , Rasmussen B.B. , Hutber C.A. , Call G.B. , Clayton R.D. , Conley L.M. , Yoon S. , Zhou B.
      J. Appl. Physiol.82:219-225(1997) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: CATALYTIC ACTIVITY;FUNCTION IN PHOSPHORYLATION OF ACACA AND ACACB
    6. 6.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN PHOSPHORYLATION OF NOS3
    7. 7.
      "Phosphorylation and activation of heart PFK-2 by AMPK has a role in the stimulation of glycolysis during ischaemia."
      Marsin A.S. , Bertrand L. , Rider M.H. , Deprez J. , Beauloye C. , Vincent M.F. , Van den Berghe G. , Carling D. , Hue L.
      Curr. Biol.10:1247-1255(2000) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN PHOSPHORYLATION OF PFKFB2
    8. 8.
      "5'-AMP-activated protein kinase phosphorylates IRS-1 on Ser-789 in mouse C2C12 myotubes in response to 5-aminoimidazole-4-carboxamide riboside."
      Jakobsen S.N. , Hardie D.G. , Morrice N. , Tornqvist H.E.
      J. Biol. Chem.276:46912-46916(2001) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN PHOSPHORYLATION OF IRS1
    9. 9.
      "Mechanism for fatty acid 'sparing' effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase."
      Kawaguchi T. , Osatomi K. , Yamashita H. , Kabashima T. , Uyeda K.
      J. Biol. Chem.277:3829-3835(2002) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN PHOSPHORYLATION OF MLXIPL
    10. 10.
      "The stimulation of glycolysis by hypoxia in activated monocytes is mediated by AMP-activated protein kinase and inducible 6-phosphofructo-2-kinase."
      Marsin A.S. , Bouzin C. , Bertrand L. , Hue L.
      J. Biol. Chem.277:30778-30783(2002) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN PHOSPHORYLATION OF PFKFB3
    11. 11.
      "LKB1 is the upstream kinase in the AMP-activated protein kinase cascade."
      Woods A. , Johnstone S.R. , Dickerson K. , Leiper F.C. , Fryer L.G. , Neumann D. , Schlattner U. , Wallimann T. , Carlson M. , Carling D.
      Curr. Biol.13:2004-2008(2003) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION AT THR-172;ENZYME REGULATION
    12. 12.
      "Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade."
      Hawley S.A. , Boudeau J. , Reid J.L. , Mustard K.J. , Udd L. , Makela T.P. , Alessi D.R. , Hardie D.G.
      J. Biol.2:28.1-28.16(2003) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;ENZYME REGULATION;PHOSPHORYLATION AT THR-172
    13. 13.
      "AMP-activated protein kinase regulates HNF4alpha transcriptional activity by inhibiting dimer formation and decreasing protein stability."
      Hong Y.H. , Varanasi U.S. , Yang W. , Leff T.
      J. Biol. Chem.278:27495-27501(2003) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN PHOSPHORYLATION OF HNF4A
    14. 14.
      "Identification of phosphorylation sites in AMP-activated protein kinase (AMPK) for upstream AMPK kinases and study of their roles by site-directed mutagenesis."
      Woods A. , Vertommen D. , Neumann D. , Turk R. , Bayliss J. , Schlattner U. , Wallimann T. , Carling D. , Rider M.H.
      J. Biol. Chem.278:28434-28442(2003) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION AT THR-258 AND SER-491;IDENTIFICATION BY MASS SPECTROMETRY
    15. 15.
      "Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398."
      Browne G.J. , Finn S.G. , Proud C.G.
      J. Biol. Chem.279:12220-12231(2004) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN PHOSPHORYLATION OF EEF2K
    16. 16.
      "Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase."
      Hawley S.A. , Pan D.A. , Mustard K.J. , Ross L. , Bain J. , Edelman A.M. , Frenguelli B.G. , Hardie D.G.
      Cell Metab.2:9-19(2005) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION AT THR-172;ENZYME REGULATION
    17. 17.
      "Ca2+/calmodulin-dependent protein kinase kinase-beta acts upstream of AMP-activated protein kinase in mammalian cells."
      Woods A. , Dickerson K. , Heath R. , Hong S.-P. , Momcilovic M. , Johnstone S.R. , Carlson M. , Carling D.
      Cell Metab.2:21-33(2005) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION AT THR-172;ENZYME REGULATION
    18. 18.
      "Regulation of the renal-specific Na+-K+-2Cl- co-transporter NKCC2 by AMP-activated protein kinase (AMPK)."
      Fraser S.A. , Gimenez I. , Cook N. , Jennings I. , Katerelos M. , Katsis F. , Levidiotis V. , Kemp B.E. , Power D.A.
      Biochem. J.405:85-93(2007) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN PHOSPHORYLATION OF SLC12A1
    19. 19.
      "Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop."
      Loffler A.S. , Alers S. , Dieterle A.M. , Keppeler H. , Franz-Wachtel M. , Kundu M. , Campbell D.G. , Wesselborg S. , Alessi D.R. , Stork B.
      Autophagy7:696-706(2011) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION BY ULK1
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