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Q8BGM7

- AAKG3_MOUSE

UniProt

Q8BGM7 - AAKG3_MOUSE

Protein

5'-AMP-activated protein kinase subunit gamma-3

Gene

Prkag3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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 sitei225 – 2251AMP 1By similarity
    Binding sitei225 – 2251ATP 1By similarity
    Binding sitei306 – 3061AMP 2By similarity
    Binding sitei306 – 3061AMP 3By similarity
    Binding sitei306 – 3061ATP 2By similarity
    Binding sitei307 – 3071ATP 1By similarity
    Binding sitei307 – 3071ATP 2By similarity
    Binding sitei325 – 3251AMP 1By similarity
    Binding sitei325 – 3251ATP 1By similarity
    Binding sitei453 – 4531AMP 3By similarity
    Binding sitei454 – 4541AMP 1By similarity
    Binding sitei454 – 4541ATP 1By similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-KW
    2. glucose transport Source: MGI
    3. glycogen biosynthetic process Source: MGI

    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-3
    Short name:
    AMPK gamma3
    Short name:
    AMPK subunit gamma-3
    Gene namesi
    Name:Prkag3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1891343. Prkag3.

    Subcellular locationi

    GO - Cellular componenti

    1. AMP-activated protein kinase complex Source: Ensembl
    2. cytosol Source: Reactome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 4894895'-AMP-activated protein kinase subunit gamma-3PRO_0000204385Add
    BLAST

    Post-translational modificationi

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

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ8BGM7.
    PRIDEiQ8BGM7.

    PTM databases

    PhosphoSiteiQ8BGM7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8BGM7.
    BgeeiQ8BGM7.
    GenevestigatoriQ8BGM7.

    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

    STRINGi10090.ENSMUSP00000080342.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BGM7.
    SMRiQ8BGM7. Positions 181-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini197 – 25862CBS 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini280 – 34061CBS 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini355 – 41561CBS 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini427 – 48660CBS 4PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi293 – 31422AMPK 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.
    GeneTreeiENSGT00390000009849.
    HOGENOMiHOG000176880.
    HOVERGENiHBG050431.
    InParanoidiQ0VG42.
    KOiK07200.
    OMAiAKASRWT.
    OrthoDBiEOG74FF0W.
    PhylomeDBiQ8BGM7.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8BGM7-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEPELEHTLP GTLTWSHSGG PESQEMDFLE QGENSWPSPA VATSSERTCA    50
    IRGVKASRWT RQEAVEEAEP PGLGEGAQSR PAAESTRQEA TFPKATPLAQ 100
    AVPLAEAETS PTGWDLLLPD CAASAGGSST GDLELTIEFP APEAWDCELE 150
    GLGKDRPRPG PSPQAPLLGL SWDDELQKPG AQVYMHFMQE HTCYDAMATS 200
    SKLVIFDTTL EIKKAFFAMV ANGVRAAPLW DSKKQSFVGM LTITDFILVL 250
    HRYYRSPLVQ IYEIEEHKIE TWREIYLQGC FKPLVSISPN DSLFEAVYAL 300
    IKNRIHRLPV LDPVSGTVLY ILTHKRLLKF LHIFGALLPR PSFLCRTIQD 350
    LGIGTFRDLA VVLETAPVLT ALDIFVDRRV SALPVVNESG QVVGLYSRFD 400
    VIHLAAQQTY NHLDMSVGEA LRQRTLCLEG VLSCQPHESL GEVIDRIARE 450
    QVHRLVLVDE TQHLLGVVSL SDILQALVLS PAGIDALSA 489
    Length:489
    Mass (Da):53,849
    Last modified:March 1, 2003 - v1
    Checksum:i85C9F71D8BDBDA5D
    GO
    Isoform 2 (identifier: Q8BGM7-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         1-25: Missing.

    Show »
    Length:464
    Mass (Da):51,117
    Checksum:iCEC324A5855C3F2E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti390 – 3901G → GS in AAP22981. (PubMed:14970697)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2525Missing in isoform 2. 2 PublicationsVSP_015588Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF525500 mRNA. Translation: AAN47137.1.
    AF525501 mRNA. Translation: AAN47138.1.
    AY263402 Genomic DNA. Translation: AAP22981.1.
    AK036585 mRNA. Translation: BAC29492.1.
    BC116749 mRNA. Translation: AAI16750.1.
    BC116777 mRNA. Translation: AAI16778.1.
    CCDSiCCDS15055.1. [Q8BGM7-1]
    RefSeqiNP_714966.1. NM_153744.3. [Q8BGM7-1]
    XP_006496051.1. XM_006495988.1. [Q8BGM7-1]
    XP_006496052.1. XM_006495989.1. [Q8BGM7-1]
    UniGeneiMm.166501.
    Mm.453463.

    Genome annotation databases

    EnsembliENSMUST00000081636; ENSMUSP00000080342; ENSMUSG00000006542. [Q8BGM7-1]
    ENSMUST00000113672; ENSMUSP00000109302; ENSMUSG00000006542. [Q8BGM7-2]
    ENSMUST00000160732; ENSMUSP00000125344; ENSMUSG00000006542. [Q8BGM7-1]
    GeneIDi241113.
    KEGGimmu:241113.
    UCSCiuc007bnb.2. mouse. [Q8BGM7-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF525500 mRNA. Translation: AAN47137.1 .
    AF525501 mRNA. Translation: AAN47138.1 .
    AY263402 Genomic DNA. Translation: AAP22981.1 .
    AK036585 mRNA. Translation: BAC29492.1 .
    BC116749 mRNA. Translation: AAI16750.1 .
    BC116777 mRNA. Translation: AAI16778.1 .
    CCDSi CCDS15055.1. [Q8BGM7-1 ]
    RefSeqi NP_714966.1. NM_153744.3. [Q8BGM7-1 ]
    XP_006496051.1. XM_006495988.1. [Q8BGM7-1 ]
    XP_006496052.1. XM_006495989.1. [Q8BGM7-1 ]
    UniGenei Mm.166501.
    Mm.453463.

    3D structure databases

    ProteinModelPortali Q8BGM7.
    SMRi Q8BGM7. Positions 181-480.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000080342.

    PTM databases

    PhosphoSitei Q8BGM7.

    Proteomic databases

    PaxDbi Q8BGM7.
    PRIDEi Q8BGM7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000081636 ; ENSMUSP00000080342 ; ENSMUSG00000006542 . [Q8BGM7-1 ]
    ENSMUST00000113672 ; ENSMUSP00000109302 ; ENSMUSG00000006542 . [Q8BGM7-2 ]
    ENSMUST00000160732 ; ENSMUSP00000125344 ; ENSMUSG00000006542 . [Q8BGM7-1 ]
    GeneIDi 241113.
    KEGGi mmu:241113.
    UCSCi uc007bnb.2. mouse. [Q8BGM7-1 ]

    Organism-specific databases

    CTDi 53632.
    MGIi MGI:1891343. Prkag3.

    Phylogenomic databases

    eggNOGi COG0517.
    GeneTreei ENSGT00390000009849.
    HOGENOMi HOG000176880.
    HOVERGENi HBG050431.
    InParanoidi Q0VG42.
    KOi K07200.
    OMAi AKASRWT.
    OrthoDBi EOG74FF0W.
    PhylomeDBi Q8BGM7.
    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 384884.
    PROi Q8BGM7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BGM7.
    Bgeei Q8BGM7.
    Genevestigatori Q8BGM7.

    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 and characterization of mouse 5'-AMP-activated protein kinase gamma3 subunit."
      Yu H., Fujii N., Hirshman M.F., Pomerleau J.M., Goodyear L.J.
      Am. J. Physiol. 286:C283-C292(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Strain: BALB/c.
      Tissue: Skeletal muscle.
    2. "Comparative sequence analysis of the PRKAG3 region between human and pig: evolution of repetitive sequences and potential new exons."
      Amarger V., Erlandsson R., Pielberg G., Jeon J.-T., Andersson L.
      Cytogenet. Genome Res. 102:163-172(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Bone.
    4. "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] (ISOFORM 2).
      Tissue: Brain.
    5. "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.

    Entry informationi

    Entry nameiAAKG3_MOUSE
    AccessioniPrimary (citable) accession number: Q8BGM7
    Secondary accession number(s): Q0VG42, Q80WK8, Q8CJ41
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2005
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 83 of the entry and version 1 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