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P54645

- AAPK1_RAT

UniProt

P54645 - AAPK1_RAT

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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

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 C-terminus binding Source: RGD
  11. protein serine/threonine kinase activity Source: RGD
  12. 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 camptothecin Source: Ensembl
  38. response to gamma radiation Source: UniProtKB
  39. response to UV Source: Ensembl
  40. rhythmic process Source: UniProtKB-KW
  41. transcription, DNA-templated Source: UniProtKB-KW
  42. 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

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

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

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 CaMKK25 Publications
Modified residuei269 – 2691Phosphothreonine1 Publication
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 – 4961Phosphoserine1 Publication

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 – 348Combined sources
Beta strandi37 – 393Combined sources
Beta strandi41 – 466Combined sources
Turni47 – 493Combined sources
Beta strandi52 – 598Combined sources
Helixi60 – 634Combined sources
Turni64 – 674Combined sources
Helixi69 – 8012Combined sources
Beta strandi90 – 956Combined sources
Beta strandi97 – 1059Combined sources
Turni112 – 1176Combined sources
Beta strandi118 – 1214Combined sources
Helixi124 – 14320Combined sources
Beta strandi155 – 1584Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi188 – 1903Combined sources
Helixi193 – 1964Combined sources
Helixi204 – 22017Combined sources
Helixi230 – 2389Combined sources
Helixi250 – 25910Combined sources
Turni264 – 2663Combined sources
Helixi270 – 2745Combined sources
Helixi277 – 2804Combined sources
Beta strandi287 – 2893Combined sources
Helixi301 – 31111Combined sources
Helixi315 – 3239Combined sources
Helixi330 – 34718Combined sources
Helixi349 – 3513Combined sources
Helixi372 – 3743Combined sources
Helixi376 – 3816Combined sources
Beta strandi407 – 4137Combined sources
Helixi417 – 43014Combined sources
Beta strandi434 – 4396Combined sources
Beta strandi442 – 4487Combined sources
Turni450 – 4523Combined sources
Beta strandi455 – 46410Combined sources
Beta strandi466 – 4683Combined sources
Beta strandi470 – 4778Combined sources
Helixi542 – 55514Combined sources

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[»]
4QFGX-ray3.46A11-480[»]
A536-559[»]
4QFRX-ray3.34A11-480[»]
A536-559[»]
4QFSX-ray3.55A11-479[»]
A536-559[»]
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.
GeneTreeiENSGT00760000118892.
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.
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

        10         20         30         40         50
MRRLSSWRKM ATAEKQKHDG RVKIGHYILG DTLGVGTFGK VKVGKHELTG
60 70 80 90 100
HKVAVKILNR QKIRSLDVVG KIRREIQNLK LFRHPHIIKL YQVISTPSDI
110 120 130 140 150
FMVMEYVSGG ELFDYICKNG RLDEKESRRL FQQILSGVDY CHRHMVVHRD
160 170 180 190 200
LKPENVLLDA HMNAKIADFG LSNMMSDGEF LRTSCGSPNY AAPEVISGRL
210 220 230 240 250
YAGPEVDIWS SGVILYALLC GTLPFDDDHV PTLFKKICDG IFYTPQYLNP
260 270 280 290 300
SVISLLKHML QVDPMKRATI KDIREHEWFK QDLPKYLFPE DPSYSSTMID
310 320 330 340 350
DEALKEVCEK FECSEEEVLS CLYNRNHQDP LAVAYHLIID NRRIMNEAKD
360 370 380 390 400
FYLATSPPDS FLDDHHLTRP HPERVPFLVA ETPRARHTLD ELNPQKSKHQ
410 420 430 440 450
GVRKAKWHLG IRSQSRPNDI MAEVCRAIKQ LDYEWKVVNP YYLRVRRKNP
460 470 480 490 500
VTSTFSKMSL QLYQVDSRTY LLDFRSIDDE ITEAKSGTAT PQRSGSISNY
510 520 530 540 550
RSCQRSDSDA EAQGKPSEVS LTSSVTSLDS SPVDVAPRPG SHTIEFFEMC

ANLIKILAQ
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 [» ]
4QFG X-ray 3.46 A 11-480 [» ]
A 536-559 [» ]
4QFR X-ray 3.34 A 11-480 [» ]
A 536-559 [» ]
4QFS X-ray 3.55 A 11-479 [» ]
A 536-559 [» ]
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 ENSGT00760000118892.
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.
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. 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 29, 2014
This is version 140 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