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Q5EG47 (AAPK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5'-AMP-activated protein kinase catalytic subunit alpha-1

Short name=AMPK subunit alpha-1
EC=2.7.11.1
Alternative name(s):
Acetyl-CoA carboxylase kinase
Short name=ACACA kinase
EC=2.7.11.27
Hydroxymethylglutaryl-CoA reductase kinase
Short name=HMGCR kinase
EC=2.7.11.31
Tau-protein kinase PRKAA1
EC=2.7.11.26
Gene names
Name:Prkaa1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length559 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.6 Ref.7 Ref.8 Ref.9 Ref.12 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20

Catalytic activity

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.

Cofactor

Magnesium By similarity.

Enzyme regulation

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. Ref.3 Ref.5 Ref.18

Subunit structure

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.

Subcellular location

Cytoplasm By similarity. Nucleus. Note: In response to stress, recruited by p53/TP53 to specific promoters. Ref.14

Domain

The AIS (autoinhibitory sequence) region shows some sequence similarity with the ubiquitin-associated domains and represses kinase activity By similarity.

Post-translational modification

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. Ref.3 Ref.5 Ref.7 Ref.17

Ubiquitinated. Ref.11

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processAutophagy
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
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionChromatin regulator
Kinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

activation of MAPK activity

Inferred from electronic annotation. Source: InterPro

autophagy

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to ethanol

Inferred from electronic annotation. Source: Ensembl

cellular response to glucose starvation

Inferred from direct assay Ref.19. Source: UniProtKB

cellular response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

cellular response to nutrient levels

Inferred from direct assay Ref.19. Source: UniProtKB

cellular response to organonitrogen compound

Inferred from electronic annotation. Source: Ensembl

cholesterol biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

cold acclimation

Inferred from electronic annotation. Source: Ensembl

fatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

fatty acid homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

fatty acid oxidation

Inferred from mutant phenotype PubMed 12802337. Source: MGI

glucose homeostasis

Inferred from mutant phenotype Ref.7. Source: UniProtKB

glucose metabolic process

Inferred from mutant phenotype PubMed 12802337. Source: MGI

histone-serine phosphorylation

Inferred from direct assay Ref.16. Source: GOC

lipid biosynthetic process

Inferred from direct assay Ref.18. Source: UniProtKB

negative regulation of TOR signaling

Inferred from mutant phenotype Ref.12. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.12. Source: UniProtKB

negative regulation of glucose import in response to insulin stimulus

Inferred from electronic annotation. Source: Ensembl

negative regulation of lipid catabolic process

Inferred from direct assay Ref.4. Source: UniProtKB

positive regulation of autophagy

Inferred from mutant phenotype Ref.19. Source: UniProtKB

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

positive regulation of glycolytic process

Inferred from sequence or structural similarity. Source: UniProtKB

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of circadian rhythm

Inferred from mutant phenotype Ref.14. Source: UniProtKB

regulation of energy homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of vesicle-mediated transport

Inferred from electronic annotation. Source: Ensembl

response to UV

Inferred from mutant phenotype Ref.16. Source: UniProtKB

response to activity

Inferred from electronic annotation. Source: Ensembl

response to caffeine

Inferred from electronic annotation. Source: Ensembl

response to camptothecin

Inferred from mutant phenotype Ref.16. Source: UniProtKB

response to gamma radiation

Inferred from mutant phenotype Ref.16. Source: UniProtKB

response to hydrogen peroxide

Inferred from mutant phenotype Ref.16. Source: UniProtKB

rhythmic process

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentAMP-activated protein kinase complex

Inferred from sequence or structural similarity. Source: UniProtKB

apical plasma membrane

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 18381428. Source: MGI

nucleus

Inferred from direct assay Ref.14. Source: UniProtKB

   Molecular_functionAMP-activated protein kinase activity

Inferred from direct assay Ref.4Ref.12Ref.14Ref.19Ref.18. Source: UniProtKB

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

[acetyl-CoA carboxylase] kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

chromatin binding

Inferred from direct assay Ref.16. Source: UniProtKB

histone serine kinase activity

Inferred from direct assay Ref.16. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.4Ref.14Ref.19Ref.18. Source: UniProtKB

tau-protein kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5595595'-AMP-activated protein kinase catalytic subunit alpha-1
PRO_0000085590

Regions

Domain27 – 279253Protein kinase
Nucleotide binding33 – 419ATP By similarity
Region302 – 38180AIS By similarity

Sites

Active site1501Proton acceptor By similarity
Binding site561ATP By similarity

Amino acid modifications

Modified residue321Phosphothreonine By similarity
Modified residue1831Phosphothreonine; by LKB1 and CaMKK2 Ref.3 Ref.5 Ref.7
Modified residue3561Phosphoserine By similarity
Modified residue3601Phosphoserine; by ULK1 By similarity
Modified residue3681Phosphothreonine; by ULK1 By similarity
Modified residue3821Phosphothreonine By similarity
Modified residue3971Phosphoserine; by ULK1 By similarity
Modified residue4671Phosphoserine By similarity
Modified residue4861Phosphoserine; by ULK1 By similarity
Modified residue4881Phosphothreonine; by ULK1 By similarity
Modified residue4901Phosphothreonine By similarity
Modified residue4961Phosphoserine Ref.13

Experimental info

Mutagenesis1681D → A: Loss of kinase activity. Ref.4 Ref.19
Sequence conflict11 – 122Missing in AAW79567. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q5EG47 [UniParc].

Last modified July 28, 2009. Version 2.
Checksum: 08632503663D395B

FASTA55963,929
        10         20         30         40         50         60 
MRRLSSWRKM ATAEKQKHDG RVKIGHYILG DTLGVGTFGK VKVGKHELTG HKVAVKILNR 

        70         80         90        100        110        120 
QKIRSLDVVG KIRREIQNLK LFRHPHIIKL YQVISTPSDI FMVMEYVSGG ELFDYICKNG 

       130        140        150        160        170        180 
RLDEKESRRL FQQILSGVDY CHRHMVVHRD LKPENVLLDA HMNAKIADFG LSNMMSDGEF 

       190        200        210        220        230        240 
LRTSCGSPNY AAPEVISGRL YAGPEVDIWS SGVILYALLC GTLPFDDDHV PTLFKKICDG 

       250        260        270        280        290        300 
IFYTPQYLNP SVISLLKHML QVDPMKRAAI KDIREHEWFK QDLPKYLFPE DPSYSSTMID 

       310        320        330        340        350        360 
DEALKEVCEK FECSEEEVLS CLYNRNHQDP LAVAYHLIID NRRIMNEAKD FYLATSPPDS 

       370        380        390        400        410        420 
FLDDHHLTRP HPERVPFLVA ETPRARHTLD ELNPQKSKHQ GVRKAKWHLG IRSQSRPNDI 

       430        440        450        460        470        480 
MAEVCRAIKQ LDYEWKVVNP YYLRVRRKNP VTSTFSKMSL QLYQVDSRTY LLDFRSIDDE 

       490        500        510        520        530        540 
ITEAKSGTAT PQRSGSISNY RSCQRSDSDA EAQGKPSDVS LTSSVTSLDS SPVDVAPRPG 

       550 
SHTIEFFEMC ANLIKILAQ 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"The CREB coactivator TORC2 is a key regulator of fasting glucose metabolism."
Koo S.-H., Flechner L., Qi L., Zhang X., Screaton R.A., Jeffries S., Hedrick S., Xu W., Boussouar F., Brindle P., Takemori H., Montminy M.
Nature 437:1109-1111(2005) [PubMed] [Europe PMC] [Abstract]
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]"AMPK-mediated AS160 phosphorylation in skeletal muscle is dependent on AMPK catalytic and regulatory subunits."
Treebak J.T., Glund S., Deshmukh A., Klein D.K., Long Y.C., Jensen T.E., Jorgensen S.B., Viollet B., Andersson L., Neumann D., Wallimann T., Richter E.A., Chibalin A.V., Zierath J.R., Wojtaszewski J.F.
Diabetes 55:2051-2058(2006) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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]"AMPK phosphorylation of raptor mediates a metabolic checkpoint."
Gwinn D.M., Shackelford D.B., Egan D.F., Mihaylova M.M., Mery A., Vasquez D.S., Turk B.E., Shaw R.J.
Mol. Cell 30:214-226(2008) [PubMed] [Europe PMC] [Abstract]
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]"AMPK regulates the circadian clock by cryptochrome phosphorylation and degradation."
Lamia K.A., Sachdeva U.M., DiTacchio L., Williams E.C., Alvarez J.G., Egan D.F., Vasquez D.S., Juguilon H., Panda S., Shaw R.J., Thompson C.B., Evans R.M.
Science 326:437-440(2009) [PubMed] [Europe PMC] [Abstract]
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]"Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects energy sensing to mitophagy."
Egan D.F., Shackelford D.B., Mihaylova M.M., Gelino S., Kohnz R.A., Mair W., Vasquez D.S., Joshi A., Gwinn D.M., Taylor R., Asara J.M., Fitzpatrick J., Dillin A., Viollet B., Kundu M., Hansen M., Shaw R.J.
Science 331:456-461(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF ULK1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC131919 Genomic DNA. No translation available.
AC135079 Genomic DNA. No translation available.
AY885266 mRNA. Translation: AAW79567.1.
CCDSCCDS49574.1.
RefSeqNP_001013385.3. NM_001013367.3.
UniGeneMm.207004.

3D structure databases

ProteinModelPortalQ5EG47.
SMRQ5EG47. Positions 18-559.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid222923. 5 interactions.
IntActQ5EG47. 4 interactions.

Chemistry

ChEMBLCHEMBL1075161.

PTM databases

PhosphoSiteQ5EG47.

Proteomic databases

MaxQBQ5EG47.
PaxDbQ5EG47.
PRIDEQ5EG47.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000051186; ENSMUSP00000063166; ENSMUSG00000050697.
GeneID105787.
KEGGmmu:105787.
UCSCuc007vct.1. mouse.

Organism-specific databases

CTD5562.
MGIMGI:2145955. Prkaa1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000115114.
HOGENOMHOG000233016.
HOVERGENHBG050432.
InParanoidQ5EG47.
KOK07198.
OMAMKRATIR.
OrthoDBEOG7RRF6K.
PhylomeDBQ5EG47.
TreeFamTF314032.

Gene expression databases

ArrayExpressQ5EG47.
BgeeQ5EG47.
GenevestigatorQ5EG47.

Family and domain databases

InterProIPR028375. 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]
PANTHERPTHR24343:SF81. PTHR24343:SF81. 1 hit.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF103243. SSF103243. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio357894.
PROQ5EG47.
SOURCESearch...

Entry information

Entry nameAAPK1_MOUSE
AccessionPrimary (citable) accession number: Q5EG47
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: July 28, 2009
Last modified: July 9, 2014
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot