Q5EG47 (AAPK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	559 AA.
Sequence status	Complete.
Protein existence	Evidence 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: 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 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.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19
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.17
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.13
Domain	The AIS (autoinhibitory sequence) region 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. Ref.3 Ref.5 Ref.7 Ref.16 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 process	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
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Chromatin regulator Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW autophagy Inferred from electronic annotation. Source: UniProtKB-KW cellular response to ethanol Inferred from electronic annotation. Source: Compara cellular response to glucose starvation Inferred from direct assay Ref.18. Source: UniProtKB cellular response to hydrogen peroxide Inferred from electronic annotation. Source: Compara cellular response to hypoxia Inferred from electronic annotation. Source: Compara cellular response to organic nitrogen Inferred from electronic annotation. Source: Compara cholesterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW cold acclimation Inferred from electronic annotation. Source: Compara 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 lipid biosynthetic process Inferred from direct assay Ref.17. Source: UniProtKB negative regulation of TOR signaling cascade 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: Compara negative regulation of lipid catabolic process Inferred from direct assay Ref.4. Source: UniProtKB positive regulation of autophagy Inferred from mutant phenotype Ref.18. Source: UniProtKB positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of glycolysis Inferred from sequence or structural similarity. Source: UniProtKB protein heterooligomerization Inferred from electronic annotation. Source: Compara regulation of circadian rhythm Inferred from mutant phenotype Ref.13. Source: UniProtKB regulation of energy homeostasis Inferred from sequence or structural similarity. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW regulation of vesicle-mediated transport Inferred from electronic annotation. Source: Compara response to activity Inferred from electronic annotation. Source: Compara response to caffeine Inferred from electronic annotation. Source: Compara rhythmic process Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	AMP-activated protein kinase complex Inferred from sequence or structural similarity. Source: UniProtKB apical plasma membrane Inferred from electronic annotation. Source: Compara cytoplasm Inferred from direct assay PubMed 18381428. Source: MGI nucleus Inferred from direct assay Ref.13. Source: UniProtKB
Molecular_function	AMP-activated protein kinase activity Inferred from direct assay Ref.4Ref.12Ref.13Ref.18Ref.17. Source: UniProtKB ATP binding Inferred from electronic annotation. Source: UniProtKB-KW [acetyl-CoA carboxylase] kinase activity Inferred from electronic annotation. Source: EC [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity Inferred from electronic annotation. Source: EC chromatin binding Inferred from direct assay Ref.15. Source: UniProtKB histone serine kinase activity Inferred from direct assay Ref.15. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW tau-protein kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 559	559	5'-AMP-activated protein kinase catalytic subunit alpha-1		PRO_0000085590
Regions
	Domain	27 – 279	253	Protein kinase
	Nucleotide binding	33 – 41	9	ATP By similarity
	Region	302 – 381	80	AIS By similarity
Sites
	Active site	150	1	Proton acceptor By similarity
	Binding site	56	1	ATP By similarity
Amino acid modifications
	Modified residue	32	1	Phosphothreonine By similarity
	Modified residue	183	1	Phosphothreonine; by LKB1 and CaMKK2 Ref.3 Ref.5 Ref.7
	Modified residue	184	1	Phosphoserine Ref.10
	Modified residue	356	1	Phosphoserine By similarity
	Modified residue	360	1	Phosphoserine; by ULK1 By similarity
	Modified residue	368	1	Phosphothreonine; by ULK1 By similarity
	Modified residue	382	1	Phosphothreonine By similarity
	Modified residue	397	1	Phosphoserine; by ULK1 By similarity
	Modified residue	467	1	Phosphoserine By similarity
	Modified residue	486	1	Phosphoserine; by ULK1 By similarity
	Modified residue	488	1	Phosphothreonine; by ULK1 By similarity
	Modified residue	490	1	Phosphothreonine By similarity
	Modified residue	496	1	Phosphoserine By similarity
	Modified residue	508	1	Phosphoserine Ref.10
Experimental info
	Mutagenesis	168	1	D → A: Loss of kinase activity. Ref.4 Ref.18
	Sequence conflict	11 – 12	2	Missing in AAW79567. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q5EG47 [UniParc]. Last modified July 28, 2009. Version 2. Checksum: 08632503663D395B	FASTA	559	63,929
	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

References

	« Hide 'large scale' referencesShow '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. , 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND SER-508, MASS SPECTROMETRY. 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]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
IPI	IPI00556823.
RefSeq	NP_001013385.3. NM_001013367.3.
UniGene	Mm.207004.
3D structure databases
ProteinModelPortal	Q5EG47.
SMR	Q5EG47. Positions 18-559.
ModBase	Search...
PTM databases
PhosphoSite	Q5EG47.
Proteomic databases
PaxDb	Q5EG47.
PRIDE	Q5EG47.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000051186; ENSMUSP00000063166; ENSMUSG00000050697.
GeneID	105787.
KEGG	mmu:105787.
UCSC	uc007vct.1. mouse.
Organism-specific databases
CTD	5562.
MGI	MGI:2145955. Prkaa1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00700000104077.
HOGENOM	HOG000233016.
HOVERGEN	HBG050432.
InParanoid	Q5EG47.
KO	K07198.
OMA	ACQRNDS.
OrthoDB	EOG4BK53H.
Gene expression databases
ArrayExpress	Q5EG47.
Bgee	Q5EG47.
Genevestigator	Q5EG47.
GermOnline	ENSMUSG00000050697. Mus musculus.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL1075161.
NextBio	357894.
SOURCE	Search...

Entry information

Entry name

AAPK1_MOUSE

Accession

Primary (citable) accession number: Q5EG47

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2005
Last sequence update:	July 28, 2009
Last modified:	April 3, 2013
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program