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Q5EG47

- AAPK1_MOUSE

UniProt

Q5EG47 - AAPK1_MOUSE

Protein

5'-AMP-activated protein kinase catalytic subunit alpha-1

Gene

Prkaa1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 2 (28 Jul 2009)
      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 has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1.12 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.
    ATP + [tau protein] = ADP + [tau protein] phosphate.
    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-183. Binding of AMP to non-catalytic gamma subunit (PRKAG1, PRKAG2 or PRKAG3) results in allosteric activation, inducing phosphorylation on Thr-183. AMP-binding to gamma subunit also sustains activity by preventing dephosphorylation of Thr-183. ADP also stimulates Thr-183 phosphorylation, without stimulating already phosphorylated AMPK. ATP promotes dephosphorylation of Thr-183, 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.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei56 – 561ATPPROSITE-ProRule annotation
    Active sitei150 – 1501Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi33 – 419ATPPROSITE-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. tau-protein kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. activation of MAPK activity Source: InterPro
    2. autophagy Source: UniProtKB-KW
    3. cellular response to ethanol Source: Ensembl
    4. cellular response to glucose starvation Source: UniProtKB
    5. cellular response to hydrogen peroxide Source: Ensembl
    6. cellular response to hypoxia Source: Ensembl
    7. cellular response to nutrient levels Source: UniProtKB
    8. cellular response to organonitrogen compound Source: Ensembl
    9. cholesterol biosynthetic process Source: UniProtKB-KW
    10. cold acclimation Source: Ensembl
    11. fatty acid biosynthetic process Source: UniProtKB-KW
    12. fatty acid homeostasis Source: UniProtKB
    13. fatty acid oxidation Source: MGI
    14. glucose homeostasis Source: UniProtKB
    15. glucose metabolic process Source: MGI
    16. histone-serine phosphorylation Source: GOC
    17. lipid biosynthetic process Source: UniProtKB
    18. negative regulation of apoptotic process Source: UniProtKB
    19. negative regulation of glucose import in response to insulin stimulus Source: Ensembl
    20. negative regulation of lipid catabolic process Source: UniProtKB
    21. negative regulation of TOR signaling Source: UniProtKB
    22. positive regulation of autophagy Source: UniProtKB
    23. positive regulation of cell proliferation Source: Ensembl
    24. positive regulation of gene expression Source: Ensembl
    25. positive regulation of glycolytic process Source: UniProtKB
    26. protein heterooligomerization Source: Ensembl
    27. regulation of circadian rhythm Source: UniProtKB
    28. regulation of energy homeostasis Source: UniProtKB
    29. regulation of transcription, DNA-templated Source: UniProtKB-KW
    30. regulation of vesicle-mediated transport Source: Ensembl
    31. response to activity Source: Ensembl
    32. response to caffeine Source: Ensembl
    33. response to camptothecin Source: UniProtKB
    34. response to gamma radiation Source: UniProtKB
    35. response to hydrogen peroxide Source: UniProtKB
    36. response to UV Source: UniProtKB
    37. rhythmic process Source: UniProtKB-KW
    38. transcription, DNA-templated Source: UniProtKB-KW
    39. 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_220701. Regulation of AMPK activity via LKB1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    5'-AMP-activated protein kinase catalytic subunit alpha-1 (EC:2.7.11.1)
    Short name:
    AMPK subunit alpha-1
    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
    Tau-protein kinase PRKAA1 (EC:2.7.11.26)
    Gene namesi
    Name:Prkaa1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:2145955. Prkaa1.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus 1 Publication
    Note: In response to stress, recruited by p53/TP53 to specific promoters.

    GO - Cellular componenti

    1. AMP-activated protein kinase complex Source: UniProtKB
    2. apical plasma membrane Source: Ensembl
    3. cytoplasm Source: MGI
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi168 – 1681D → A: Loss of kinase activity. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 5595595'-AMP-activated protein kinase catalytic subunit alpha-1PRO_0000085590Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei32 – 321PhosphothreonineBy similarity
    Modified residuei183 – 1831Phosphothreonine; by LKB1 and CaMKK24 Publications
    Modified residuei356 – 3561PhosphoserineBy similarity
    Modified residuei360 – 3601Phosphoserine; by ULK1By similarity
    Modified residuei368 – 3681Phosphothreonine; by ULK1By similarity
    Modified residuei382 – 3821PhosphothreonineBy similarity
    Modified residuei397 – 3971Phosphoserine; by ULK1By similarity
    Modified residuei467 – 4671PhosphoserineBy similarity
    Modified residuei486 – 4861Phosphoserine; by ULK1By similarity
    Modified residuei488 – 4881Phosphothreonine; by ULK1By similarity
    Modified residuei490 – 4901PhosphothreonineBy similarity
    Modified residuei496 – 4961Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated at Thr-183 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Also phosphorylated at Thr-183 by CAMKK2; triggered by a rise in intracellular calcium ions, without detectable changes in the AMP/ATP ratio. CAMKK1 can also phosphorylate Thr-183, but at a much lower level. Dephosphorylated by protein phosphatase 2A and 2C (PP2A and PP2C). 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. Dephosphorylated by PPM1A and PPM1B By similarity.By similarity
    Ubiquitinated.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ5EG47.
    PaxDbiQ5EG47.
    PRIDEiQ5EG47.

    PTM databases

    PhosphoSiteiQ5EG47.

    Expressioni

    Gene expression databases

    ArrayExpressiQ5EG47.
    BgeeiQ5EG47.
    GenevestigatoriQ5EG47.

    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.

    Protein-protein interaction databases

    BioGridi222923. 5 interactions.
    IntActiQ5EG47. 4 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5EG47.
    SMRiQ5EG47. Positions 18-559.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 279253Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni302 – 38180AISBy 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.
    InParanoidiQ5EG47.
    KOiK07198.
    OMAiMKRATIR.
    OrthoDBiEOG7RRF6K.
    PhylomeDBiQ5EG47.
    TreeFamiTF314032.

    Family and domain databases

    InterProiIPR028375. KA1/Ssp2_C.
    IPR011009. Kinase-like_dom.
    IPR028797. PRKAA1.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PANTHERiPTHR24343:SF81. PTHR24343:SF81. 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.

    Q5EG47-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRRLSSWRKM ATAEKQKHDG RVKIGHYILG DTLGVGTFGK VKVGKHELTG    50
    HKVAVKILNR QKIRSLDVVG KIRREIQNLK LFRHPHIIKL YQVISTPSDI 100
    FMVMEYVSGG ELFDYICKNG RLDEKESRRL FQQILSGVDY CHRHMVVHRD 150
    LKPENVLLDA HMNAKIADFG LSNMMSDGEF LRTSCGSPNY AAPEVISGRL 200
    YAGPEVDIWS SGVILYALLC GTLPFDDDHV PTLFKKICDG IFYTPQYLNP 250
    SVISLLKHML QVDPMKRAAI KDIREHEWFK QDLPKYLFPE DPSYSSTMID 300
    DEALKEVCEK FECSEEEVLS CLYNRNHQDP LAVAYHLIID NRRIMNEAKD 350
    FYLATSPPDS FLDDHHLTRP HPERVPFLVA ETPRARHTLD ELNPQKSKHQ 400
    GVRKAKWHLG IRSQSRPNDI MAEVCRAIKQ LDYEWKVVNP YYLRVRRKNP 450
    VTSTFSKMSL QLYQVDSRTY LLDFRSIDDE ITEAKSGTAT PQRSGSISNY 500
    RSCQRSDSDA EAQGKPSDVS LTSSVTSLDS SPVDVAPRPG SHTIEFFEMC 550
    ANLIKILAQ 559
    Length:559
    Mass (Da):63,929
    Last modified:July 28, 2009 - v2
    Checksum:i08632503663D395B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 122Missing in AAW79567. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC131919 Genomic DNA. No translation available.
    AC135079 Genomic DNA. No translation available.
    AY885266 mRNA. Translation: AAW79567.1.
    CCDSiCCDS49574.1.
    RefSeqiNP_001013385.3. NM_001013367.3.
    UniGeneiMm.207004.

    Genome annotation databases

    EnsembliENSMUST00000051186; ENSMUSP00000063166; ENSMUSG00000050697.
    GeneIDi105787.
    KEGGimmu:105787.
    UCSCiuc007vct.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC131919 Genomic DNA. No translation available.
    AC135079 Genomic DNA. No translation available.
    AY885266 mRNA. Translation: AAW79567.1 .
    CCDSi CCDS49574.1.
    RefSeqi NP_001013385.3. NM_001013367.3.
    UniGenei Mm.207004.

    3D structure databases

    ProteinModelPortali Q5EG47.
    SMRi Q5EG47. Positions 18-559.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 222923. 5 interactions.
    IntActi Q5EG47. 4 interactions.

    Chemistry

    ChEMBLi CHEMBL1075161.

    PTM databases

    PhosphoSitei Q5EG47.

    Proteomic databases

    MaxQBi Q5EG47.
    PaxDbi Q5EG47.
    PRIDEi Q5EG47.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000051186 ; ENSMUSP00000063166 ; ENSMUSG00000050697 .
    GeneIDi 105787.
    KEGGi mmu:105787.
    UCSCi uc007vct.1. mouse.

    Organism-specific databases

    CTDi 5562.
    MGIi MGI:2145955. Prkaa1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000115114.
    HOGENOMi HOG000233016.
    HOVERGENi HBG050432.
    InParanoidi Q5EG47.
    KOi K07198.
    OMAi MKRATIR.
    OrthoDBi EOG7RRF6K.
    PhylomeDBi Q5EG47.
    TreeFami TF314032.

    Enzyme and pathway databases

    Reactomei REACT_220701. Regulation of AMPK activity via LKB1.

    Miscellaneous databases

    NextBioi 357894.
    PROi Q5EG47.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5EG47.
    Bgeei Q5EG47.
    Genevestigatori Q5EG47.

    Family and domain databases

    InterProi IPR028375. KA1/Ssp2_C.
    IPR011009. Kinase-like_dom.
    IPR028797. PRKAA1.
    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:SF81. PTHR24343:SF81. 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. Xie X., Chen Y.
      Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-559.
      Strain: C57BL/6N.
      Tissue: Muscle.
    3. "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]
      Cited for: ENZYME REGULATION, PHOSPHORYLATION AT THR-183.
    4. "Anti-lipolytic action of AMP-activated protein kinase in rodent adipocytes."
      Daval M., Diot-Dupuy F., Bazin R., Hainault I., Viollet B., Vaulont S., Hajduch E., Ferre P., Foufelle F.
      J. Biol. Chem. 280:25250-25257(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF LIPE, MUTAGENESIS OF ASP-168.
    5. "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-183, ENZYME REGULATION.
    6. Cited for: FUNCTION IN PHOSPHORYLATION OF CRTC2.
    7. "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-183.
    8. Cited for: FUNCTION IN PHOSPHORYLATION OF TBC1D4.
    9. "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.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    11. "Control of AMPK-related kinases by USP9X and atypical Lys(29)/Lys(33)-linked polyubiquitin chains."
      Al-Hakim A.K., Zagorska A., Chapman L., Deak M., Peggie M., Alessi D.R.
      Biochem. J. 411:249-260(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    12. Cited for: FUNCTION IN PHOSPHORYLATION OF RPTOR.
    13. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: FUNCTION IN PHOSPHORYLATION OF CRY1, SUBCELLULAR LOCATION.
    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.
    17. "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.
    18. "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.
    19. "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, MUTAGENESIS OF ASP-168.
    20. Cited for: FUNCTION IN PHOSPHORYLATION OF ULK1.

    Entry informationi

    Entry nameiAAPK1_MOUSE
    AccessioniPrimary (citable) accession number: Q5EG47
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2005
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 93 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. 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