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P54645

- AAPK1_RAT

UniProt

P54645 - AAPK1_RAT

Protein

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

Gene

Prkaa1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (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.5 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: RGD
    5. chromatin binding Source: UniProtKB
    6. eukaryotic elongation factor-2 kinase activator activity Source: UniProtKB
    7. histone serine kinase activity Source: UniProtKB
    8. kinase binding Source: RGD
    9. metal ion binding Source: UniProtKB-KW
    10. protein binding Source: UniProtKB
    11. protein C-terminus binding Source: RGD
    12. protein serine/threonine kinase activity Source: RGD
    13. 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: RGD
    4. cellular response to glucose starvation Source: UniProtKB
    5. cellular response to hydrogen peroxide Source: RGD
    6. cellular response to hypoxia Source: RGD
    7. cellular response to nutrient levels Source: UniProtKB
    8. cellular response to organonitrogen compound Source: RGD
    9. cholesterol biosynthetic process Source: UniProtKB-KW
    10. cold acclimation Source: RGD
    11. fatty acid biosynthetic process Source: UniProtKB-KW
    12. fatty acid homeostasis Source: UniProtKB
    13. fatty acid oxidation Source: Ensembl
    14. glucose homeostasis Source: UniProtKB
    15. glucose metabolic process Source: Ensembl
    16. lipid biosynthetic process Source: UniProtKB
    17. negative regulation of apoptotic process Source: UniProtKB
    18. negative regulation of glucose import in response to insulin stimulus Source: RGD
    19. negative regulation of lipid catabolic process Source: UniProtKB
    20. negative regulation of TOR signaling Source: UniProtKB
    21. negative regulation of translation Source: UniProtKB
    22. positive regulation of autophagy Source: UniProtKB
    23. positive regulation of cell proliferation Source: RGD
    24. positive regulation of fatty acid oxidation Source: UniProtKB
    25. positive regulation of gene expression Source: Ensembl
    26. positive regulation of gluconeogenesis Source: UniProtKB
    27. positive regulation of glucose import Source: UniProtKB
    28. positive regulation of glycolytic process Source: UniProtKB
    29. protein heterooligomerization Source: RGD
    30. protein phosphorylation Source: UniProtKB
    31. regulation of circadian rhythm Source: UniProtKB
    32. regulation of energy homeostasis Source: UniProtKB
    33. regulation of transcription, DNA-templated Source: UniProtKB-KW
    34. regulation of vesicle-mediated transport Source: RGD
    35. response to activity Source: RGD
    36. response to caffeine Source: RGD
    37. response to gamma radiation Source: UniProtKB
    38. rhythmic process Source: UniProtKB-KW
    39. transcription, DNA-templated Source: UniProtKB-KW
    40. 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

    BRENDAi2.7.11.1. 5301.

    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
    Synonyms:Ampk1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 2

    Organism-specific databases

    RGDi3387. Prkaa1.

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi183 – 1831T → E: Hinders activation. 2 Publications
    Mutagenesisi269 – 2691T → A: Hinders activation. 2 Publications
    Mutagenesisi269 – 2691T → D: Retains activation ability. 2 Publications
    Mutagenesisi386 – 3916RHTLDE → AHALAA: Allosterically activated by AMP but is not protected against dephosphorylation by AMP or ADP. 1 Publication
    Mutagenesisi496 – 4961S → A: Hinders activation. 2 Publications
    Mutagenesisi496 – 4961S → D: Retains activation ability. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 5595595'-AMP-activated protein kinase catalytic subunit alpha-1PRO_0000085593Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei32 – 321PhosphothreonineBy similarity
    Modified residuei183 – 1831Phosphothreonine; by LKB1 and CaMKK26 Publications
    Modified residuei269 – 2691Phosphothreonine2 Publications
    Modified residuei356 – 3561PhosphoserineBy similarity
    Modified residuei360 – 3601Phosphoserine; by ULK11 Publication
    Modified residuei368 – 3681Phosphothreonine; by ULK11 Publication
    Modified residuei382 – 3821PhosphothreonineBy similarity
    Modified residuei397 – 3971Phosphoserine; by ULK11 Publication
    Modified residuei467 – 4671PhosphoserineBy similarity
    Modified residuei486 – 4861Phosphoserine; by ULK11 Publication
    Modified residuei488 – 4881Phosphothreonine; by ULK11 Publication
    Modified residuei490 – 4901PhosphothreonineBy similarity
    Modified residuei496 – 4961Phosphoserine2 Publications

    Post-translational modificationi

    Ubiquitinated.By similarity
    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. There is some ambiguity for some phosphosites: Ser-360/Thr-368 and Ser-486/Thr-488. Dephosphorylated by PPM1A and PPM1B By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP54645.

    PTM databases

    PhosphoSiteiP54645.

    Expressioni

    Tissue specificityi

    Low expression in kidney, liver, lung, heart and brain.

    Gene expression databases

    GenevestigatoriP54645.

    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 FNIP2.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FlcnQ76JQ22EBI-7596967,EBI-7596839

    Protein-protein interaction databases

    BioGridi249325. 1 interaction.
    DIPiDIP-57168N.
    IntActiP54645. 1 interaction.
    MINTiMINT-4566241.
    STRINGi10116.ENSRNOP00000017626.

    Structurei

    Secondary structure

    1
    559
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi27 – 348
    Beta strandi37 – 393
    Beta strandi41 – 466
    Turni47 – 493
    Beta strandi52 – 598
    Helixi60 – 634
    Turni64 – 674
    Helixi69 – 8012
    Beta strandi90 – 956
    Beta strandi97 – 1059
    Turni112 – 1176
    Beta strandi118 – 1214
    Helixi124 – 14320
    Beta strandi155 – 1584
    Beta strandi164 – 1663
    Beta strandi188 – 1903
    Helixi193 – 1964
    Helixi204 – 22017
    Helixi230 – 2389
    Helixi250 – 25910
    Turni264 – 2663
    Helixi270 – 2745
    Helixi277 – 2804
    Beta strandi287 – 2893
    Helixi301 – 31111
    Helixi315 – 3239
    Helixi330 – 34718
    Helixi349 – 3513
    Helixi372 – 3743
    Helixi376 – 3816
    Beta strandi407 – 4137
    Helixi417 – 43014
    Beta strandi434 – 4396
    Beta strandi442 – 4487
    Turni450 – 4523
    Beta strandi455 – 46410
    Beta strandi466 – 4683
    Beta strandi470 – 4778
    Helixi542 – 55514

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2V8QX-ray2.10A407-559[»]
    2V92X-ray2.40A407-559[»]
    2V9JX-ray2.53A407-559[»]
    2Y8LX-ray2.50A407-555[»]
    2Y8QX-ray2.80A407-555[»]
    2YA3X-ray2.51A407-555[»]
    4CFHX-ray3.24A13-481[»]
    C535-559[»]
    4EAIX-ray2.28A405-479[»]
    A540-559[»]
    4EAJX-ray2.61A405-479[»]
    A540-559[»]
    4EAKX-ray2.50A405-479[»]
    A540-559[»]
    4EALX-ray2.51A405-479[»]
    A540-559[»]
    4F2LX-ray1.50A295-347[»]
    ProteinModelPortaliP54645.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54645.

    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.
    InParanoidiP54645.
    KOiK07198.
    OMAiMKRATIR.
    OrthoDBiEOG7RRF6K.
    PhylomeDBiP54645.
    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.

    P54645-1 [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 QVDPMKRATI 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 EAQGKPSEVS LTSSVTSLDS SPVDVAPRPG SHTIEFFEMC 550
    ANLIKILAQ 559
    Length:559
    Mass (Da):63,973
    Last modified:July 28, 2009 - v2
    Checksum:iA869C340A85785ED
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 142Missing in AAC52355. (PubMed:8557660)Curated
    Sequence conflicti473 – 4731D → L AA sequence (PubMed:8557660)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH474048 Genomic DNA. No translation available.
    U40819 mRNA. Translation: AAC52355.1.
    RefSeqiNP_062015.2. NM_019142.2.
    UniGeneiRn.87789.

    Genome annotation databases

    EnsembliENSRNOT00000017626; ENSRNOP00000017626; ENSRNOG00000012799.
    GeneIDi65248.
    KEGGirno:65248.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CH474048 Genomic DNA. No translation available.
    U40819 mRNA. Translation: AAC52355.1 .
    RefSeqi NP_062015.2. NM_019142.2.
    UniGenei Rn.87789.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2V8Q X-ray 2.10 A 407-559 [» ]
    2V92 X-ray 2.40 A 407-559 [» ]
    2V9J X-ray 2.53 A 407-559 [» ]
    2Y8L X-ray 2.50 A 407-555 [» ]
    2Y8Q X-ray 2.80 A 407-555 [» ]
    2YA3 X-ray 2.51 A 407-555 [» ]
    4CFH X-ray 3.24 A 13-481 [» ]
    C 535-559 [» ]
    4EAI X-ray 2.28 A 405-479 [» ]
    A 540-559 [» ]
    4EAJ X-ray 2.61 A 405-479 [» ]
    A 540-559 [» ]
    4EAK X-ray 2.50 A 405-479 [» ]
    A 540-559 [» ]
    4EAL X-ray 2.51 A 405-479 [» ]
    A 540-559 [» ]
    4F2L X-ray 1.50 A 295-347 [» ]
    ProteinModelPortali P54645.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 249325. 1 interaction.
    DIPi DIP-57168N.
    IntActi P54645. 1 interaction.
    MINTi MINT-4566241.
    STRINGi 10116.ENSRNOP00000017626.

    Chemistry

    BindingDBi P54645.
    ChEMBLi CHEMBL4533.

    PTM databases

    PhosphoSitei P54645.

    Proteomic databases

    PRIDEi P54645.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000017626 ; ENSRNOP00000017626 ; ENSRNOG00000012799 .
    GeneIDi 65248.
    KEGGi rno:65248.

    Organism-specific databases

    CTDi 5562.
    RGDi 3387. Prkaa1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000115114.
    HOGENOMi HOG000233016.
    HOVERGENi HBG050432.
    InParanoidi P54645.
    KOi K07198.
    OMAi MKRATIR.
    OrthoDBi EOG7RRF6K.
    PhylomeDBi P54645.
    TreeFami TF314032.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 5301.

    Miscellaneous databases

    EvolutionaryTracei P54645.
    NextBioi 614203.
    PROi P54645.

    Gene expression databases

    Genevestigatori P54645.

    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. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-559, PROTEIN SEQUENCE OF 24-40; 90-115; 129-140; 150-160; 166-182; 236-257; 272-276; 286-305; 326-341; 350-367; 375-384; 409-426; 437-446; 458-475 AND 507-517.
      Strain: Sprague-Dawley.
      Tissue: Hypothalamus and Liver.
    3. "Regulation of HMG-CoA reductase: identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liver."
      Clarke P.R., Hardie D.G.
      EMBO J. 9:2439-2446(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION IN PHOSPHORYLATION OF HMGCR.
    4. "Mammalian 5'-AMP-activated protein kinase non-catalytic subunits are homologs of proteins that interact with yeast Snf1 protein kinase."
      Stapleton D., Gao G., Michell B.J., Widmer J., Mitchelhill K.I., Teh T., House C.M., Witters L.A., Kemp B.E.
      J. Biol. Chem. 269:29343-29346(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE AMPK COMPLEX.
      Strain: Sprague-Dawley.
      Tissue: Hypothalamus and Liver.
    5. "Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase."
      Hawley S.A., Davison M., Woods A., Davies S.P., Beri R.K., Carling D., Hardie D.G.
      J. Biol. Chem. 271:27879-27887(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-183, ENZYME REGULATION.
    6. "Phosphorylation of rat muscle acetyl-CoA carboxylase by AMP-activated protein kinase and protein kinase A."
      Winder W.W., Wilson H.A., Hardie D.G., Rasmussen B.B., Hutber C.A., Call G.B., Clayton R.D., Conley L.M., Yoon S., Zhou B.
      J. Appl. Physiol. 82:219-225(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION IN PHOSPHORYLATION OF ACACA AND ACACB.
    7. Cited for: FUNCTION IN PHOSPHORYLATION OF NOS3.
    8. "Phosphorylation and activation of heart PFK-2 by AMPK has a role in the stimulation of glycolysis during ischaemia."
      Marsin A.S., Bertrand L., Rider M.H., Deprez J., Beauloye C., Vincent M.F., Van den Berghe G., Carling D., Hue L.
      Curr. Biol. 10:1247-1255(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF PFKFB2.
    9. "5'-AMP-activated protein kinase phosphorylates IRS-1 on Ser-789 in mouse C2C12 myotubes in response to 5-aminoimidazole-4-carboxamide riboside."
      Jakobsen S.N., Hardie D.G., Morrice N., Tornqvist H.E.
      J. Biol. Chem. 276:46912-46916(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF IRS1.
    10. "Mechanism for fatty acid 'sparing' effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase."
      Kawaguchi T., Osatomi K., Yamashita H., Kabashima T., Uyeda K.
      J. Biol. Chem. 277:3829-3835(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF MLXIPL.
    11. "The stimulation of glycolysis by hypoxia in activated monocytes is mediated by AMP-activated protein kinase and inducible 6-phosphofructo-2-kinase."
      Marsin A.S., Bouzin C., Bertrand L., Hue L.
      J. Biol. Chem. 277:30778-30783(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF PFKFB3.
    12. Cited for: PHOSPHORYLATION AT THR-183, ENZYME REGULATION.
    13. "Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade."
      Hawley S.A., Boudeau J., Reid J.L., Mustard K.J., Udd L., Makela T.P., Alessi D.R., Hardie D.G.
      J. Biol. 2:28.1-28.16(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-183.
    14. "AMP-activated protein kinase regulates HNF4alpha transcriptional activity by inhibiting dimer formation and decreasing protein stability."
      Hong Y.H., Varanasi U.S., Yang W., Leff T.
      J. Biol. Chem. 278:27495-27501(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HNF4A.
    15. "Identification of phosphorylation sites in AMP-activated protein kinase (AMPK) for upstream AMPK kinases and study of their roles by site-directed mutagenesis."
      Woods A., Vertommen D., Neumann D., Turk R., Bayliss J., Schlattner U., Wallimann T., Carling D., Rider M.H.
      J. Biol. Chem. 278:28434-28442(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-269 AND SER-496, MUTAGENESIS OF THR-183; THR-269 AND SER-496, IDENTIFICATION BY MASS SPECTROMETRY.
    16. "Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398."
      Browne G.J., Finn S.G., Proud C.G.
      J. Biol. Chem. 279:12220-12231(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF EEF2K.
    17. "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: PHOSPHORYLATION AT THR-183, ENZYME REGULATION.
    18. "Ca2+/calmodulin-dependent protein kinase kinase-beta acts upstream of AMP-activated protein kinase in mammalian cells."
      Woods A., Dickerson K., Heath R., Hong S.-P., Momcilovic M., Johnstone S.R., Carlson M., Carling D.
      Cell Metab. 2:21-33(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-183, ENZYME REGULATION.
    19. "Regulation of the renal-specific Na+-K+-2Cl- co-transporter NKCC2 by AMP-activated protein kinase (AMPK)."
      Fraser S.A., Gimenez I., Cook N., Jennings I., Katerelos M., Katsis F., Levidiotis V., Kemp B.E., Power D.A.
      Biochem. J. 405:85-93(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF SLC12A1.
    20. "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 ULK, PHOSPHORYLATION AT SER-360; THR-368; SER-397; SER-486 AND THR-488.
    21. "AMP-activated protein kinase (AMPK) is a tau kinase, activated in response to amyloid beta-peptide exposure."
      Thornton C., Bright N.J., Sastre M., Muckett P.J., Carling D.
      Biochem. J. 434:503-512(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF MAPT.
    22. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 405-557 IN COMPLEX WITH PRKAB2 AND PRKAG1.
    23. Cited for: X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 13-559 IN COMPLEX WITH PRKAB2 AND PRKAG1, MUTAGENESIS OF 386-ARG--GLU-391.

    Entry informationi

    Entry nameiAAPK1_RAT
    AccessioniPrimary (citable) accession number: P54645
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 139 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3