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O54950

- AAKG1_MOUSE

UniProt

O54950 - AAKG1_MOUSE

Protein

5'-AMP-activated protein kinase subunit gamma-1

Gene

Prkag1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (13 Sep 2005)
      Previous versions | rss
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    Functioni

    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 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei69 – 691AMP 1By similarity
    Binding sitei69 – 691ATP 1By similarity
    Binding sitei150 – 1501AMP 2By similarity
    Binding sitei150 – 1501AMP 3By similarity
    Binding sitei150 – 1501ATP 2By similarity
    Binding sitei151 – 1511ATP 1By similarity
    Binding sitei151 – 1511ATP 2By similarity
    Binding sitei169 – 1691AMP 1By similarity
    Binding sitei169 – 1691ATP 1By similarity
    Binding sitei297 – 2971AMP 3By similarity
    Binding sitei298 – 2981AMP 1By similarity
    Binding sitei298 – 2981ATP 1By similarity

    GO - Molecular functioni

    1. ADP binding Source: UniProtKB
    2. AMP-activated protein kinase activity Source: MGI
    3. AMP binding Source: UniProtKB
    4. ATP binding Source: UniProtKB

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-KW
    2. positive regulation of gene expression Source: Ensembl
    3. protein heterooligomerization Source: Ensembl
    4. regulation of catalytic activity Source: Ensembl

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_199054. Translocation of GLUT4 to the plasma membrane.
    REACT_205688. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
    REACT_220701. Regulation of AMPK activity via LKB1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    5'-AMP-activated protein kinase subunit gamma-1
    Short name:
    AMPK gamma1
    Short name:
    AMPK subunit gamma-1
    Short name:
    AMPKg
    Gene namesi
    Name:Prkag1
    Synonyms:Prkaac
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:108411. Prkag1.

    Subcellular locationi

    GO - Cellular componenti

    1. AMP-activated protein kinase complex Source: UniProtKB
    2. cytosol Source: Reactome
    3. nucleus Source: MGI

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3303305'-AMP-activated protein kinase subunit gamma-1PRO_0000204378Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei260 – 2601Phosphoserine; by ULK1By similarity
    Modified residuei262 – 2621Phosphothreonine; by ULK1By similarity
    Modified residuei269 – 2691Phosphoserine; by ULK1By similarity

    Post-translational modificationi

    Phosphorylated by ULK1 and ULK2; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1, ULK2 and AMPK.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO54950.
    PaxDbiO54950.
    PRIDEiO54950.

    PTM databases

    PhosphoSiteiO54950.

    Expressioni

    Gene expression databases

    BgeeiO54950.
    GenevestigatoriO54950.

    Interactioni

    Subunit structurei

    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 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi202364. 2 interactions.
    IntActiO54950. 3 interactions.
    MINTiMINT-4583597.

    Structurei

    3D structure databases

    ProteinModelPortaliO54950.
    SMRiO54950. Positions 26-324.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini42 – 10261CBS 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini124 – 18663CBS 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini197 – 25963CBS 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini271 – 32858CBS 4PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi137 – 15822AMPK pseudosubstrateAdd
    BLAST

    Domaini

    The AMPK pseudosubstrate motif resembles the sequence around sites phosphorylated on target proteins of AMPK, except the presence of a non-phosphorylatable residue in place of Ser. In the absence of AMP this pseudosubstrate sequence may bind to the active site groove on the alpha subunit (PRKAA1 or PRKAA2), preventing phosphorylation by the upstream activating kinase STK11/LKB1 By similarity.By similarity
    The CBS domains mediate binding to AMP, ADP and ATP. 2 sites bind either AMP or ATP, whereas a third site contains a tightly bound AMP that does not exchange. Under physiological conditions AMPK mainly exists in its inactive form in complex with ATP, which is much more abundant than AMP By similarity.By similarity

    Sequence similaritiesi

    Contains 4 CBS domains.PROSITE-ProRule annotation

    Keywords - Domaini

    CBS domain, Repeat

    Phylogenomic databases

    eggNOGiCOG0517.
    HOGENOMiHOG000176880.
    HOVERGENiHBG050431.
    InParanoidiO54950.
    KOiK07200.
    OMAiALGIFVE.
    OrthoDBiEOG74FF0W.
    PhylomeDBiO54950.
    TreeFamiTF313247.

    Family and domain databases

    InterProiIPR000644. CBS_dom.
    [Graphical view]
    PfamiPF00571. CBS. 4 hits.
    [Graphical view]
    SMARTiSM00116. CBS. 4 hits.
    [Graphical view]
    PROSITEiPS51371. CBS. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O54950-1 [UniParc]FASTAAdd to Basket

    « Hide

    MESVAAESSP ALENEHFQET PESNNSVYTS FMKSHRCYDL IPTSSKLVVF    50
    DTSLQVKKAF FALVTNGVRA APLWDSKKQS FVGMLTITDF INILHRYYKS 100
    ALVQIYELEE HKIETWREVY LQDSFKPLVC ISPNASLFDA VSSLIRNKIH 150
    RLPVIDPESG NTLYILTHKR ILKFLKLFIT EFPKPEFMSK SLQELQIGTY 200
    ANIAMVRTTT PVYVALGIFV QHRVSALPVV DEKGRVVDIY SKFDVINLAA 250
    EKTYNNLDVS VTKALQHRSH YFEGVLKCYL HETLETIINR LVEAEVHRLV 300
    VVDEHDVVKG IVSLSDILQA LVLTGGEKKP 330
    Length:330
    Mass (Da):37,520
    Last modified:September 13, 2005 - v2
    Checksum:i539F70EC8819C34D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti80 – 801S → C in AAB95475. (PubMed:11306812)Curated
    Sequence conflicti137 – 1371L → S in AAB95475. (PubMed:11306812)Curated
    Sequence conflicti180 – 1801T → I in AAB95475. (PubMed:11306812)Curated
    Sequence conflicti320 – 3201A → D in AAB95475. (PubMed:11306812)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF036535 mRNA. Translation: AAB95475.1.
    BC086660 mRNA. Translation: AAH86660.1.
    CCDSiCCDS49724.1.
    RefSeqiNP_058061.2. NM_016781.2.
    UniGeneiMm.6670.

    Genome annotation databases

    EnsembliENSMUST00000168846; ENSMUSP00000132499; ENSMUSG00000067713.
    GeneIDi19082.
    KEGGimmu:19082.
    UCSCiuc007xoa.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF036535 mRNA. Translation: AAB95475.1 .
    BC086660 mRNA. Translation: AAH86660.1 .
    CCDSi CCDS49724.1.
    RefSeqi NP_058061.2. NM_016781.2.
    UniGenei Mm.6670.

    3D structure databases

    ProteinModelPortali O54950.
    SMRi O54950. Positions 26-324.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202364. 2 interactions.
    IntActi O54950. 3 interactions.
    MINTi MINT-4583597.

    PTM databases

    PhosphoSitei O54950.

    Proteomic databases

    MaxQBi O54950.
    PaxDbi O54950.
    PRIDEi O54950.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000168846 ; ENSMUSP00000132499 ; ENSMUSG00000067713 .
    GeneIDi 19082.
    KEGGi mmu:19082.
    UCSCi uc007xoa.1. mouse.

    Organism-specific databases

    CTDi 5571.
    MGIi MGI:108411. Prkag1.

    Phylogenomic databases

    eggNOGi COG0517.
    HOGENOMi HOG000176880.
    HOVERGENi HBG050431.
    InParanoidi O54950.
    KOi K07200.
    OMAi ALGIFVE.
    OrthoDBi EOG74FF0W.
    PhylomeDBi O54950.
    TreeFami TF313247.

    Enzyme and pathway databases

    Reactomei REACT_199054. Translocation of GLUT4 to the plasma membrane.
    REACT_205688. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
    REACT_220701. Regulation of AMPK activity via LKB1.

    Miscellaneous databases

    NextBioi 295618.
    PROi O54950.
    SOURCEi Search...

    Gene expression databases

    Bgeei O54950.
    Genevestigatori O54950.

    Family and domain databases

    InterProi IPR000644. CBS_dom.
    [Graphical view ]
    Pfami PF00571. CBS. 4 hits.
    [Graphical view ]
    SMARTi SM00116. CBS. 4 hits.
    [Graphical view ]
    PROSITEi PS51371. CBS. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, organisation, chromosomal localization and expression analysis of the mouse Prkag1 gene."
      Shamsadin R., Jantsan K., Adham I.M., Engel W.
      Cytogenet. Cell Genet. 92:134-138(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Testis.
    2. "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]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
      Tissue: Eye.
    3. "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.
      Autophagy 7:696-706(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY ULK1 AND ULK2.

    Entry informationi

    Entry nameiAAKG1_MOUSE
    AccessioniPrimary (citable) accession number: O54950
    Secondary accession number(s): Q5PRE8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: September 13, 2005
    Last modified: October 1, 2014
    This is version 106 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3