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Q8BRK8

- AAPK2_MOUSE

UniProt

Q8BRK8 - AAPK2_MOUSE

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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

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.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 – 451ATPBy similarity
Active sitei139 – 1391Proton acceptor By similarityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi22 – 309ATP By similarityBy similarity

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
Complete GO annotation...

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:Prkaa2
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
Complete GO annotation...

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 CaMKK2By similarity2 Publications
Modified residuei258 – 2581Phosphothreonine By similarity
Modified residuei377 – 3771Phosphoserine1 Publication
Modified residuei491 – 4911Phosphoserine By 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.3 Publications

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.

Protein-protein interaction databases

BioGridi223817. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ8BRK8.
SMRiQ8BRK8. Positions 7-551.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 268253Protein kinaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni291 – 37686AIS By 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

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

« Hide

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151H → D in BAE22188. 1 Publication
Sequence conflicti289 – 2891D → V in BAC31746. 1 Publication
Sequence conflicti380 – 3801A → E in BAE22188. 1 Publication
Sequence conflicti502 – 5021F → Y in BAE22188. 1 Publication
Sequence conflicti506 – 5061T → K in BAE22188. 1 Publication

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

« Hide 'large scale' publications
  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/6J.
    Tissue: Brain cortex and Medulla oblongata.
  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: September 3, 2014
This is version 105 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

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