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Q8BRK8

- AAPK2_MOUSE

UniProt

Q8BRK8 - AAPK2_MOUSE

Protein

5'-AMP-activated protein kinase catalytic subunit alpha-2

Gene

Prkaa2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    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/ULK1: 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 ATG1/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 SLC12A1.15 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.By similarity
    ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)] = ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate.
    ATP + [acetyl-CoA carboxylase] = ADP + [acetyl-CoA carboxylase] phosphate.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by phosphorylation on Thr-172. Binding of AMP to non-catalytic gamma subunit (PRKAG1, PRKAG2 or PRKAG3) results in allosteric activation, inducing phosphorylation on Thr-172. AMP-binding to gamma subunit also sustains activity by preventing dephosphorylation of Thr-172. ADP also stimulates Thr-172 phosphorylation, without stimulating already phosphorylated AMPK. ATP promotes dephosphorylation of Thr-172, rendering the enzyme inactive. Under physiological conditions AMPK mainly exists in its inactive form in complex with ATP, which is much more abundant than AMP. Selectively inhibited by compound C (6-[4-(2-Piperidin-1-yl-ethoxy)-phenyl)]-3-pyridin-4-yl-pyyrazolo[1,5-a] pyrimidine. Activated by resveratrol, a natural polyphenol present in red wine, and S17834, a synthetic polyphenol. Salicylate/aspirin directly activates kinase activity, primarily by inhibiting Thr-172 dephosphorylation.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei45 – 451ATP
    Active sitei139 – 1391Proton acceptorBy similarityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi22 – 309ATPBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. [acetyl-CoA carboxylase] kinase activity Source: UniProtKB-EC
    2. [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity Source: UniProtKB-EC
    3. AMP-activated protein kinase activity Source: UniProtKB
    4. ATP binding Source: UniProtKB-KW
    5. chromatin binding Source: UniProtKB
    6. histone serine kinase activity Source: UniProtKB
    7. metal ion binding Source: UniProtKB-KW
    8. protein binding Source: UniProtKB
    9. protein serine/threonine/tyrosine kinase activity Source: MGI
    10. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. autophagy Source: UniProtKB-KW
    2. cellular response to glucose starvation Source: UniProtKB
    3. cellular response to nutrient levels Source: UniProtKB
    4. cholesterol biosynthetic process Source: UniProtKB-KW
    5. fatty acid biosynthetic process Source: UniProtKB-KW
    6. fatty acid homeostasis Source: UniProtKB
    7. glucose homeostasis Source: UniProtKB
    8. histone-serine phosphorylation Source: GOC
    9. lipid biosynthetic process Source: UniProtKB
    10. negative regulation of apoptotic process Source: UniProtKB
    11. negative regulation of TOR signaling Source: UniProtKB
    12. positive regulation of autophagy Source: UniProtKB
    13. positive regulation of glycolytic process Source: UniProtKB
    14. regulation of circadian rhythm Source: UniProtKB
    15. regulation of energy homeostasis Source: UniProtKB
    16. regulation of transcription, DNA-templated Source: UniProtKB-KW
    17. response to stress Source: UniProtKB
    18. rhythmic process Source: UniProtKB-KW
    19. transcription, DNA-templated Source: UniProtKB-KW
    20. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Autophagy, Biological rhythms, Cholesterol biosynthesis, Cholesterol metabolism, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism, Transcription, Transcription regulation, Wnt signaling pathway

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-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 catalytic subunit alpha-2 (EC:2.7.11.1)
    Short name:
    AMPK subunit alpha-2
    Alternative name(s):
    Acetyl-CoA carboxylase kinase (EC:2.7.11.27)
    Short name:
    ACACA kinase
    Hydroxymethylglutaryl-CoA reductase kinase (EC:2.7.11.31)
    Short name:
    HMGCR kinase
    Gene namesi
    Name:Prkaa2Imported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1336173. Prkaa2.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus
    Note: In response to stress, recruited by p53/TP53 to specific promoters.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice develop obesity when animals are fed a high-fat diet, as a result of an enhanced lipid accumulation in pre-existing adipocytes but not in other tissues.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi45 – 451K → A: Loss of kinase activity. 1 Publication
    Mutagenesisi157 – 1571D → A: Loss of kinase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 5525525'-AMP-activated protein kinase catalytic subunit alpha-2PRO_0000262957Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei172 – 1721Phosphothreonine; by LKB1 and CaMKK23 Publications
    Modified residuei258 – 2581PhosphothreonineBy similarity
    Modified residuei377 – 3771Phosphoserine2 Publications
    Modified residuei491 – 4911PhosphoserineBy similarity

    Post-translational modificationi

    Ubiquitinated.By similarity
    Phosphorylated at Thr-172 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Also phosphorylated at Thr-172 by CAMKK2; triggered by a rise in intracellular calcium ions, without detectable changes in the AMP/ATP ratio. CAMKK1 can also phosphorylate Thr-172, but at much lower level. Dephosphorylated by protein phosphatase 2A and 2C (PP2A and PP2C). Phosphorylated by ULK1; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1 and AMPK. Dephosphorylated by PPM1A and PPM1B at Thr-172 (mediated by STK11/LKB1) By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8BRK8.
    PaxDbiQ8BRK8.
    PRIDEiQ8BRK8.

    PTM databases

    PhosphoSiteiQ8BRK8.

    Expressioni

    Gene expression databases

    BgeeiQ8BRK8.
    GenevestigatoriQ8BRK8.

    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

    BioGridi223817. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BRK8.
    SMRiQ8BRK8. Positions 7-551.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 268253Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni291 – 37686AISBy similarityAdd
    BLAST

    Domaini

    The AIS (autoinhibitory sequence) region shows some sequence similarity with the ubiquitin-associated domains and represses kinase activity.By similarity

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00740000115114.
    HOGENOMiHOG000233016.
    HOVERGENiHBG050432.
    InParanoidiB1ASQ8.
    KOiK07198.
    OMAiXGVILYA.
    OrthoDBiEOG7RRF6K.
    TreeFamiTF314032.

    Family and domain databases

    InterProiIPR028375. KA1/Ssp2_C.
    IPR011009. Kinase-like_dom.
    IPR028783. PRKAA2.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PANTHERiPTHR24343:SF82. PTHR24343:SF82. 1 hit.
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF103243. SSF103243. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8BRK8-1 [UniParc]FASTAAdd to Basket

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    MAEKQKHDGR VKIGHYVLGD TLGVGTFGKV KIGEHQLTGH KVAVKILNRQ    50
    KIRSLDVVGK IKREIQNLKL FRHPHIIKLY QVISTPTDFF MVMEYVSGGE 100
    LFDYICKHGR VEEVEARRLF QQILSAVDYC HRHMVVHRDL KPENVLLDAQ 150
    MNAKIADFGL SNMMSDGEFL RTSCGSPNYA APEVISGRLY AGPEVDIWSC 200
    GVILYALLCG TLPFDDEHVP TLFKKIRGGV FYIPDYLNRS VATLLMHMLQ 250
    VDPLKRATIK DIREHEWFKQ DLPSYLFPED PSYDANVIDD EAVKEVCEKF 300
    ECTESEVMNS LYSGDPQDQL AVAYHLIIDN RRIMNQASEF YLASSPPSGS 350
    FMDDSAMHIP PGLKPHPERM PPLIADSPKA RCPLDALNTT KPKSLAVKKA 400
    KWHLGIRSQS KACDIMAEVY RAMKQLGFEW KVVNAYHLRV RRKNPVTGNY 450
    VKMSLQLYLV DSRSYLLDFK SIDDEVVEQR SGSSTPQRSC SAAGLHRARS 500
    SFDSSTAENH SLSGSLTGSL TGSTLSSASP RLGSHTMDFF EMCASLITAL 550
    AR 552
    Length:552
    Mass (Da):62,022
    Last modified:July 27, 2011 - v3
    Checksum:i020B11E2685BFE39
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 151H → D in BAE22188. (PubMed:16141072)Curated
    Sequence conflicti289 – 2891D → V in BAC31746. (PubMed:16141072)Curated
    Sequence conflicti380 – 3801A → E in BAE22188. (PubMed:16141072)Curated
    Sequence conflicti502 – 5021F → Y in BAE22188. (PubMed:16141072)Curated
    Sequence conflicti506 – 5061T → K in BAE22188. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL627307, AL929466 Genomic DNA. Translation: CAM18832.1.
    AL929466, AL627307 Genomic DNA. Translation: CAM24127.1.
    BC138565 mRNA. Translation: AAI38566.1.
    BC138566 mRNA. Translation: AAI38567.1.
    AK044030 mRNA. Translation: BAC31746.1.
    AK134573 mRNA. Translation: BAE22188.1.
    CCDSiCCDS18416.1.
    RefSeqiNP_835279.2. NM_178143.2.
    UniGeneiMm.48638.

    Genome annotation databases

    EnsembliENSMUST00000030243; ENSMUSP00000030243; ENSMUSG00000028518.
    GeneIDi108079.
    KEGGimmu:108079.
    UCSCiuc008tyd.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL627307 , AL929466 Genomic DNA. Translation: CAM18832.1 .
    AL929466 , AL627307 Genomic DNA. Translation: CAM24127.1 .
    BC138565 mRNA. Translation: AAI38566.1 .
    BC138566 mRNA. Translation: AAI38567.1 .
    AK044030 mRNA. Translation: BAC31746.1 .
    AK134573 mRNA. Translation: BAE22188.1 .
    CCDSi CCDS18416.1.
    RefSeqi NP_835279.2. NM_178143.2.
    UniGenei Mm.48638.

    3D structure databases

    ProteinModelPortali Q8BRK8.
    SMRi Q8BRK8. Positions 7-551.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 223817. 1 interaction.

    Chemistry

    ChEMBLi CHEMBL1255154.

    PTM databases

    PhosphoSitei Q8BRK8.

    Proteomic databases

    MaxQBi Q8BRK8.
    PaxDbi Q8BRK8.
    PRIDEi Q8BRK8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030243 ; ENSMUSP00000030243 ; ENSMUSG00000028518 .
    GeneIDi 108079.
    KEGGi mmu:108079.
    UCSCi uc008tyd.2. mouse.

    Organism-specific databases

    CTDi 5563.
    MGIi MGI:1336173. Prkaa2.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000115114.
    HOGENOMi HOG000233016.
    HOVERGENi HBG050432.
    InParanoidi B1ASQ8.
    KOi K07198.
    OMAi XGVILYA.
    OrthoDBi EOG7RRF6K.
    TreeFami TF314032.

    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

    ChiTaRSi PRKAA2. mouse.
    NextBioi 360016.
    PROi Q8BRK8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8BRK8.
    Genevestigatori Q8BRK8.

    Family and domain databases

    InterProi IPR028375. KA1/Ssp2_C.
    IPR011009. Kinase-like_dom.
    IPR028783. PRKAA2.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    PANTHERi PTHR24343:SF82. PTHR24343:SF82. 1 hit.
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF103243. SSF103243. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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].
      Tissue: Brain.
    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] OF 15-552.
      Strain: C57BL/6JImported.
      Tissue: Brain cortexImported and Medulla oblongataImported.
    4. "Induced adiposity and adipocyte hypertrophy in mice lacking the AMP-activated protein kinase-alpha2 subunit."
      Villena J.A., Viollet B., Andreelli F., Kahn A., Vaulont S., Sul H.S.
      Diabetes 53:2242-2249(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    5. "The alpha2-5'AMP-activated protein kinase is a site 2 glycogen synthase kinase in skeletal muscle and is responsive to glucose loading."
      Jorgensen S.B., Nielsen J.N., Birk J.B., Olsen G.S., Viollet B., Andreelli F., Schjerling P., Vaulont S., Hardie D.G., Hansen B.F., Richter E.A., Wojtaszewski J.F.
      Diabetes 53:3074-3081(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF GYS1.
    6. "The Ca2+/calmodulin-dependent protein kinase kinases are AMP-activated protein kinase kinases."
      Hurley R.L., Anderson K.A., Franzone J.M., Kemp B.E., Means A.R., Witters L.A.
      J. Biol. Chem. 280:29060-29066(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-172, ENZYME REGULATION.
    7. Cited for: FUNCTION IN PHOSPHORYLATION OF CRTC2.
    8. "The kinase LKB1 mediates glucose homeostasis in liver and therapeutic effects of metformin."
      Shaw R.J., Lamia K.A., Vasquez D., Koo S.-H., Bardeesy N., Depinho R.A., Montminy M., Cantley L.C.
      Science 310:1642-1646(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CRTC2, PHOSPHORYLATION AT THR-172.
    9. Cited for: FUNCTION IN PHOSPHORYLATION OF TBC1D4.
    10. "Distinct signals regulate AS160 phosphorylation in response to insulin, AICAR, and contraction in mouse skeletal muscle."
      Kramer H.F., Witczak C.A., Fujii N., Jessen N., Taylor E.B., Arnolds D.E., Sakamoto K., Hirshman M.F., Goodyear L.J.
      Diabetes 55:2067-2076(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF TBC1D4.
    11. "AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1alpha."
      Jager S., Handschin C., St-Pierre J., Spiegelman B.M.
      Proc. Natl. Acad. Sci. U.S.A. 104:12017-12022(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF PPARGC1A.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    13. Cited for: FUNCTION IN PHOSPHORYLATION OF RPTOR.
    14. Cited for: FUNCTION IN PHOSPHORYLATION OF CRY1.
    15. "AMP-activated protein kinase (AMPK) cross-talks with canonical Wnt signaling via phosphorylation of beta-catenin at Ser 552."
      Zhao J., Yue W., Zhu M.J., Sreejayan N., Du M.
      Biochem. Biophys. Res. Commun. 395:146-151(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CTNNB1.
    16. "Signaling kinase AMPK activates stress-promoted transcription via histone H2B phosphorylation."
      Bungard D., Fuerth B.J., Zeng P.Y., Faubert B., Maas N.L., Viollet B., Carling D., Thompson C.B., Jones R.G., Berger S.L.
      Science 329:1201-1205(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF H2B, MUTAGENESIS OF ASP-157.
    17. "AMP-activated protein kinase regulates beta-catenin transcription via histone deacetylase 5."
      Zhao J.X., Yue W.F., Zhu M.J., Du M.
      J. Biol. Chem. 286:16426-16434(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HDAC5, MUTAGENESIS OF LYS-45.
    18. "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.
    19. "AMPK phosphorylates and inhibits SREBP activity to attenuate hepatic steatosis and atherosclerosis in diet-induced insulin-resistant mice."
      Li Y., Xu S., Mihaylova M.M., Zheng B., Hou X., Jiang B., Park O., Luo Z., Lefai E., Shyy J.Y., Gao B., Wierzbicki M., Verbeuren T.J., Shaw R.J., Cohen R.A., Zang M.
      Cell Metab. 13:376-388(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF SREBF1 AND SREBF2, ENZYME REGULATION.
    20. "AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1."
      Kim J., Kundu M., Viollet B., Guan K.L.
      Nat. Cell Biol. 13:132-141(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF ULK1.
    21. Cited for: FUNCTION IN PHOSPHORYLATION OF ULK1.
    22. Cited for: ENZYME REGULATION BY SALICYLATE.

    Entry informationi

    Entry nameiAAPK2_MOUSE
    AccessioniPrimary (citable) accession number: Q8BRK8
    Secondary accession number(s): B1ASQ8, Q3UYM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 106 of the entry and version 3 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3