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Index > Protein center > PRKAG1(Gene name) > Human
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  • PRKAG1 (Gene name),
  • 5'-AMP-activated protein kinase subunit gamma-1 (Protein name ),  AAKG1_HUMAN from NCBI database.
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  • General Annotation
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  • Antigen Annotation
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  • 3D
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  • Predicted Eptitope
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  • Vaild Sequence
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  • Gene name:
    PRKAG1;
    Protein name:
    5'-AMP-activated protein kinase subunit gamma-1(AMPK gamma1;AMPK subunit gamma-1;AMPKg);
    Alternative:

    Organism:
    Human (Homo sapiens). 
    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:
    AMP/ATP-binding 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. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive.
    Subcellular Location:
    N/A
    Protein Attributes:
    Sequence length:
    331
    Sequence:
    50:
    METVISSDSS | PAVENEHPQE | TPESNNSVYT | SFMKSHRCYD | LIPTSSKLVV | 
    100:
    FDTSLQVKKA | FFALVTNGVR | AAPLWDSKKQ | SFVGMLTITD | FINILHRYYK | 
    150:
    SALVQIYELE | EHKIETWREV | YLQDSFKPLV | CISPNASLFD | AVSSLIRNKI | 
    200:
    HRLPVIDPES | GNTLYILTHK | RILKFLKLFI | TEFPKPEFMS | KSLEELQIGT | 
    250:
    YANIAMVRTT | TPVYVALGIF | VQHRVSALPV | VDEKGRVVDI | YSKFDVINLA | 
    300:
    AEKTYNNLDV | SVTKALQHRS | HYFEGVLKCY | LHETLETIIN | RLVEAEVHRL | 
    331:
    VVVDENDVVK | GIVSLSDILQ | ALVLTGGEKK | P
    3D Structure:
    N/A
    Predicted Eptitope:
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    EIAab Sequence  Vaild Sequence:
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    Related Databases
    UniGene:
    KEGG:
    String:
    MIM:
    SMR:
    Pfam:
    Uniprot:
     
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    Packing:
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    Polyclonal Antibody for Human AMPK gamma1
    Monoclonal Antibody for Human AMPK gamma1
    Monoclonal Antibody for Human AMPK gamma1
    Monoclonal Antibody for Human AMPK gamma1
    Monoclonal Antibody for Human AMPK gamma1
    Monoclonal Antibody for Human AMPK gamma1
    Protein for Human AMPK gamma1
    Protein for Human AMPK gamma1
    Protein for Human AMPK gamma1
    Protein for Human AMPK gamma1
    Protein for Human AMPK gamma1

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    References
    1. 1.
      "Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-activated protein kinase."
      Gao G. , Fernandez C.S. , Stapleton D. , Auster A.S. , Widmer J. , Dyck J.R.B. , Kemp B.E. , Witters L.A.
      J. Biol. Chem.271:8675-8681(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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);PARTIAL PROTEIN SEQUENCE
      tissue: Fetal liver.
    2. 2.
      "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N. , Chen X. , Rolfs A. , Halleck A. , Hines L. , Eisenstein S. , Koundinya M. , Raphael J. , Moreira D. , Kelley T. , LaBaer J. , Lin Y. , Phelan M. , Farmer A.
      Submitted (2003-05) to the EMBL/GenBank/DDBJ databases
      [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 [LARGE SCALE MRNA] (ISOFORM 1)
    3. 3.
      "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T. , Suzuki Y. , Nishikawa T. , Otsuki T. , Sugiyama T. , Irie R. , Wakamatsu A. , Hayashi K. , Sato H. , Nagai K. , Kimura K. , Makita H. , Sekine M. , Obayashi M. , Nishi T. , Shibahara T. , Tanaka T. , Ishii S. , more...
      Nat. Genet.36:40-45(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: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3)
      tissue: Glial tumor.
      tissue: Testis.
    4. 4.
      "The finished DNA sequence of human chromosome 12."
      Scherer S.E. , Muzny D.M. , Buhay C.J. , Chen R. , Cree A. , Ding Y. , Dugan-Rocha S. , Gill R. , Gunaratne P. , Harris R.A. , Hawes A.C. , Hernandez J. , Hodgson A.V. , Hume J. , Jackson A. , Khan Z.M. , Kovar-Smith C. , Lewis L.R. , more...
      Nature440:346-351(2006) [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 [LARGE SCALE GENOMIC DNA]
    5. 5.
      "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res.14:2121-2127(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: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
      tissue: Muscle.
    6. 6.
      "CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations."
      Scott J.W. , Hawley S.A. , Green K.A. , Anis M. , Stewart G. , Scullion G.A. , Norman D.G. , Hardie D.G.
      J. Clin. Invest.113:274-284(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: DOMAIN CBS;AMP-BINDING;ATP-BINDING
    7. 7.
      "Folliculin encoded by the BHD gene interacts with a binding protein, FNIP1, and AMPK, and is involved in AMPK and mTOR signaling."
      Baba M. , Hong S.-B. , Sharma N. , Warren M.B. , Nickerson M.L. , Iwamatsu A. , Esposito D. , Gillette W.K. , Hopkins R.F. III , Hartley J.L. , Furihata M. , Oishi S. , Zhen W. , Burke T.R. Jr. , Linehan W.M. , Schmidt L.S. , Zbar B.
      Proc. Natl. Acad. Sci. U.S.A.103:15552-15557(2006) [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: INTERACTION WITH FNIP1;IDENTIFICATION BY MASS SPECTROMETRY
    8. 8.
      "Regulation of AMP-activated protein kinase by a pseudosubstrate sequence on the gamma subunit."
      Scott J.W. , Ross F.A. , Liu J.K. , Hardie D.G.
      EMBO J.26:806-815(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: DOMAIN AMPK PSEUDOSUBSTRATE
    9. 9.
      "Identification and characterization of a novel folliculin-interacting protein FNIP2."
      Hasumi H. , Baba M. , Hong S.-B. , Hasumi Y. , Huang Y. , Yao M. , Valera V.A. , Linehan W.M. , Schmidt L.S.
      Gene415:60-67(2008) [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: INTERACTION WITH FNIP2
    10. 10.
      "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H. , Olsen J.V. , Bairlein M. , Gnad F. , Oppermann F.S. , Korner R. , Greff Z. , Keri G. , Stemmann O. , Mann M.
      Mol. Cell31:438-448(2008) [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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
      tissue: Cervix carcinoma.
    11. 11.
      "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 AND ULK2
    12. 12.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
    13. 13.
      "AMPK is a direct adenylate charge-regulated protein kinase."
      Oakhill J.S. , Steel R. , Chen Z.P. , Scott J.W. , Ling N. , Tam S. , Kemp B.E.
      Science332:1433-1435(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: INTERACTION WITH PRKAA1 AND PRKAB1;DOMAIN CBS;ADP-BINDING;MUTAGENESIS OF ASP-90; ASP-245 AND ASP-317;FUNCTION
    14. 14.
      "AMP-activated protein kinase in metabolic control and insulin signaling."
      Towler M.C. , Hardie D.G.
      Circ. Res.100:328-341(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: REVIEW ON FUNCTION
    15. 15.
      "AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy."
      Hardie D.G.
      Nat. Rev. Mol. Cell Biol.8:774-785(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: REVIEW ON FUNCTION
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