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Q5EG47

- AAPK1_MOUSE

UniProt

Q5EG47 - AAPK1_MOUSE

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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

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 – 561ATP By similarity
Active sitei150 – 1501Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi33 – 419ATP By similarity

GO - Molecular functioni

  1. AMP-activated protein kinase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. [acetyl-CoA carboxylase] kinase activity Source: UniProtKB-EC
  4. [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity Source: UniProtKB-EC
  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. Wnt signaling pathway Source: UniProtKB-KW
  2. activation of MAPK activity Source: InterPro
  3. autophagy Source: UniProtKB-KW
  4. cellular response to ethanol Source: Ensembl
  5. cellular response to glucose starvation Source: UniProtKB
  6. cellular response to hydrogen peroxide Source: Ensembl
  7. cellular response to hypoxia Source: Ensembl
  8. cellular response to nutrient levels Source: UniProtKB
  9. cellular response to organonitrogen compound Source: Ensembl
  10. cholesterol biosynthetic process Source: UniProtKB-KW
  11. cold acclimation Source: Ensembl
  12. fatty acid biosynthetic process Source: UniProtKB-KW
  13. fatty acid homeostasis Source: UniProtKB
  14. fatty acid oxidation Source: MGI
  15. glucose homeostasis Source: UniProtKB
  16. glucose metabolic process Source: MGI
  17. histone-serine phosphorylation Source: GOC
  18. lipid biosynthetic process Source: UniProtKB
  19. negative regulation of TOR signaling Source: UniProtKB
  20. negative regulation of apoptotic process Source: UniProtKB
  21. negative regulation of glucose import in response to insulin stimulus Source: Ensembl
  22. negative regulation of lipid catabolic process Source: UniProtKB
  23. positive regulation of autophagy Source: UniProtKB
  24. positive regulation of cell proliferation Source: Ensembl
  25. positive regulation of gene expression Source: Ensembl
  26. positive regulation of glycolytic process Source: UniProtKB
  27. protein heterooligomerization Source: Ensembl
  28. regulation of circadian rhythm Source: UniProtKB
  29. regulation of energy homeostasis Source: UniProtKB
  30. regulation of transcription, DNA-templated Source: UniProtKB-KW
  31. regulation of vesicle-mediated transport Source: Ensembl
  32. response to UV Source: UniProtKB
  33. response to activity Source: Ensembl
  34. response to caffeine Source: Ensembl
  35. response to camptothecin Source: UniProtKB
  36. response to gamma radiation Source: UniProtKB
  37. response to hydrogen peroxide Source: UniProtKB
  38. rhythmic process Source: UniProtKB-KW
  39. transcription, DNA-templated 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_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
Note: In response to stress, recruited by p53/TP53 to specific promoters.1 Publication

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
Complete GO annotation...

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-1
PRO_0000085590Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321Phosphothreonine By similarity
Modified residuei183 – 1831Phosphothreonine; by LKB1 and CaMKK23 Publications
Modified residuei356 – 3561Phosphoserine By similarity
Modified residuei360 – 3601Phosphoserine; by ULK1 By similarity
Modified residuei368 – 3681Phosphothreonine; by ULK1 By similarity
Modified residuei382 – 3821Phosphothreonine By similarity
Modified residuei397 – 3971Phosphoserine; by ULK1 By similarity
Modified residuei467 – 4671Phosphoserine By similarity
Modified residuei486 – 4861Phosphoserine; by ULK1 By similarity
Modified residuei488 – 4881Phosphothreonine; by ULK1 By similarity
Modified residuei490 – 4901Phosphothreonine By similarity
Modified residuei496 – 4961Phosphoserine1 Publication

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.4 Publications
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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 279253Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni302 – 38180AIS By similarity
Add
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.
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

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 92 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

Similar proteinsi