Q8BRK8 (AAPK2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
5'-AMP-activated protein kinase catalytic subunit alpha-2
Short name=AMPK subunit alpha-2
EC=2.7.11.1

Gene names

Name:

Prkaa2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	552 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 phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1. Ref.4 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. UniProtKB Q13131
Cofactor	Magnesium By similarity. UniProtKB Q13131
Enzyme regulation	Activated by phosphorylation on Thr-172. Binding of AMP to non-catalytic gamma subunit (PRKAG1, PRKAG2 or PRKAG3) results in allosteric activation, inducing phosphorylation on Thr-172. AMP-binding to gamma subunit also sustains activity by preventing dephosphorylation of Thr-172. ADP also stimulates Thr-172 phosphorylation, without stimulating already phosphorylated AMPK. ATP promotes dephosphorylation of Thr-172, rendering the enzyme inactive. Under physiological conditions AMPK mainly exists in its inactive form in complex with ATP, which is much more abundant than AMP. Selectively inhibited by compound C (6-[4-(2-Piperidin-1-yl-ethoxy)-phenyl)]-3-pyridin-4-yl-pyyrazolo[1,5-a] pyrimidine. Activated by resveratrol, a natural polyphenol present in red wine, and S17834, a synthetic polyphenol. Ref.6 Ref.19
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 By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus. Note: In response to stress, recruited by p53/TP53 to specific promoters.
Domain	The AIS (autoinhibitory sequence) region some sequence similarity with the ubiquitin-associated domains and represses kinase activity By similarity.
Post-translational modification	Ubiquitinated By similarity. Phosphorylated at Thr-172 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Also phosphorylated at Thr-172 by CAMKK2; triggered by a rise in intracellular calcium ions, without detectable changes in the AMP/ATP ratio. CAMKK1 can also phosphorylate Thr-172, but at much lower lvel. Dephosphorylated by protein phosphatase 2A and 2C (PP2A and PP2C). Phosphorylated by ULK1; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1 and AMPK. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21
Disruption phenotype	Mice develop obesity when animals are fed a high-fat diet, as a result of an enhanced lipid accumulation in pre-existing adipocytes but not in other tissues. Ref.4
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 Fatty acid biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis 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	Acetylation 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 glucose starvation Inferred from direct assay Ref.20. Source: UniProtKB cholesterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW fatty acid homeostasis Inferred from sequence or structural similarity. Source: UniProtKB glucose homeostasis Inferred from mutant phenotype Ref.8. Source: UniProtKB negative regulation of TOR signaling cascade Inferred from mutant phenotype Ref.13. Source: UniProtKB negative regulation of apoptotic process Inferred from mutant phenotype Ref.13. Source: UniProtKB positive regulation of autophagy Inferred from mutant phenotype Ref.20. Source: UniProtKB positive regulation of glycolysis Inferred from sequence or structural similarity. Source: UniProtKB 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-dependent Inferred from electronic annotation. Source: UniProtKB-KW rhythmic process Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	AMP-activated protein kinase activity Inferred from direct assay Ref.13Ref.14Ref.20Ref.19. Source: UniProtKB ATP binding Inferred from electronic annotation. Source: UniProtKB-KW 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 552	552	5'-AMP-activated protein kinase catalytic subunit alpha-2		PRO_0000262957
Regions
	Domain	16 – 268	253	Protein kinase
	Nucleotide binding	22 – 30	9	ATP By similarity UniProtKB P28523
	Region	291 – 376	86	AIS By similarity
Sites
	Active site	139	1	Proton acceptor By similarity UniProtKB P28523
	Binding site	45	1	ATP UniProtKB P28523
Amino acid modifications
	Modified residue	69	1	N6-acetyllysine By similarity
	Modified residue	172	1	Phosphothreonine; by LKB1 and CaMKK2 Ref.6 Ref.8 UniProtKB Q13131
	Modified residue	173	1	Phosphoserine Ref.11
	Modified residue	176	1	Phosphoserine By similarity
	Modified residue	377	1	Phosphoserine By similarity
	Modified residue	500	1	Phosphoserine Ref.11
Experimental info
	Mutagenesis	45	1	K → A: Loss of kinase activity. Ref.17
	Mutagenesis	157	1	D → A: Loss of kinase activity. Ref.16
	Sequence conflict	15	1	H → D in BAE22188. Ref.3
	Sequence conflict	289	1	D → V in BAC31746. Ref.3
	Sequence conflict	380	1	A → E in BAE22188. Ref.3
	Sequence conflict	502	1	F → Y in BAE22188. Ref.3
	Sequence conflict	506	1	T → K in BAE22188. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q8BRK8 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 020B11E2685BFE39	FASTA	552	62,022
	10 20 30 40 50 60 MAEKQKHDGR VKIGHYVLGD TLGVGTFGKV KIGEHQLTGH KVAVKILNRQ KIRSLDVVGK 70 80 90 100 110 120 IKREIQNLKL FRHPHIIKLY QVISTPTDFF MVMEYVSGGE LFDYICKHGR VEEVEARRLF 130 140 150 160 170 180 QQILSAVDYC HRHMVVHRDL KPENVLLDAQ MNAKIADFGL SNMMSDGEFL RTSCGSPNYA 190 200 210 220 230 240 APEVISGRLY AGPEVDIWSC GVILYALLCG TLPFDDEHVP TLFKKIRGGV FYIPDYLNRS 250 260 270 280 290 300 VATLLMHMLQ VDPLKRATIK DIREHEWFKQ DLPSYLFPED PSYDANVIDD EAVKEVCEKF 310 320 330 340 350 360 ECTESEVMNS LYSGDPQDQL AVAYHLIIDN RRIMNQASEF YLASSPPSGS FMDDSAMHIP 370 380 390 400 410 420 PGLKPHPERM PPLIADSPKA RCPLDALNTT KPKSLAVKKA KWHLGIRSQS KACDIMAEVY 430 440 450 460 470 480 RAMKQLGFEW KVVNAYHLRV RRKNPVTGNY VKMSLQLYLV DSRSYLLDFK SIDDEVVEQR 490 500 510 520 530 540 SGSSTPQRSC SAAGLHRARS SFDSSTAENH SLSGSLTGSL TGSTLSSASP RLGSHTMDFF 550 EMCASLITAL AR

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: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-552. Strain: C57BL/6J. Tissue: Brain cortex and Medulla oblongata.
[4]	"Induced adiposity and adipocyte hypertrophy in mice lacking the AMP-activated protein kinase-alpha2 subunit." Villena J.A., Viollet B., Andreelli F., Kahn A., Vaulont S., Sul H.S. Diabetes 53:2242-2249(2004) [PubMed: 15331533] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[5]	"The alpha2-5'AMP-activated protein kinase is a site 2 glycogen synthase kinase in skeletal muscle and is responsive to glucose loading." Jorgensen S.B., Nielsen J.N., Birk J.B., Olsen G.S., Viollet B., Andreelli F., Schjerling P., Vaulont S., Hardie D.G., Hansen B.F., Richter E.A., Wojtaszewski J.F. Diabetes 53:3074-3081(2004) [PubMed: 15561936] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF GYS1.
[6]	"The Ca2+/calmodulin-dependent protein kinase kinases are AMP-activated protein kinase kinases." Hurley R.L., Anderson K.A., Franzone J.M., Kemp B.E., Means A.R., Witters L.A. J. Biol. Chem. 280:29060-29066(2005) [PubMed: 15980064] [Abstract] Cited for: PHOSPHORYLATION AT THR-172, ENZYME REGULATION.
[7]	"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: 16148943] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CRTC2.
[8]	"The kinase LKB1 mediates glucose homeostasis in liver and therapeutic effects of metformin." Shaw R.J., Lamia K.A., Vasquez D., Koo S.-H., Bardeesy N., Depinho R.A., Montminy M., Cantley L.C. Science 310:1642-1646(2005) [PubMed: 16308421] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CRTC2, PHOSPHORYLATION AT THR-172.
[9]	"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: 16804075] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF TBC1D4.
[10]	"Distinct signals regulate AS160 phosphorylation in response to insulin, AICAR, and contraction in mouse skeletal muscle." Kramer H.F., Witczak C.A., Fujii N., Jessen N., Taylor E.B., Arnolds D.E., Sakamoto K., Hirshman M.F., Goodyear L.J. Diabetes 55:2067-2076(2006) [PubMed: 16804077] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF TBC1D4.
[11]	"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: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-500, MASS SPECTROMETRY. Tissue: Liver.
[12]	"AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1alpha." Jager S., Handschin C., St-Pierre J., Spiegelman B.M. Proc. Natl. Acad. Sci. U.S.A. 104:12017-12022(2007) [PubMed: 17609368] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PPARGC1A.
[13]	"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: 18439900] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF RPTOR.
[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: 19833968] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CRY1.
[15]	"AMP-activated protein kinase (AMPK) cross-talks with canonical Wnt signaling via phosphorylation of beta-catenin at Ser 552." Zhao J., Yue W., Zhu M.J., Sreejayan N., Du M. Biochem. Biophys. Res. Commun. 395:146-151(2010) [PubMed: 20361929] [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: 20647423] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF H2B, MUTAGENESIS OF ASP-157.
[17]	"AMP-activated protein kinase regulates beta-catenin transcription via histone deacetylase 5." Zhao J.X., Yue W.F., Zhu M.J., Du M. J. Biol. Chem. 286:16426-16434(2011) [PubMed: 21454484] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF HDAC5, MUTAGENESIS OF LYS-45.
[18]	"Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop." Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M., Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B. Autophagy 7:696-706(2011) [PubMed: 21460634] [Abstract] Cited for: PHOSPHORYLATION BY ULK1.
[19]	"AMPK phosphorylates and inhibits SREBP activity to attenuate hepatic steatosis and atherosclerosis in diet-induced insulin-resistant mice." Li Y., Xu S., Mihaylova M.M., Zheng B., Hou X., Jiang B., Park O., Luo Z., Lefai E., Shyy J.Y., Gao B., Wierzbicki M., Verbeuren T.J., Shaw R.J., Cohen R.A., Zang M. Cell Metab. 13:376-388(2011) [PubMed: 21459323] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF SREBF1 AND SREBF2, ENZYME REGULATION.
[20]	"AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1." Kim J., Kundu M., Viollet B., Guan K.L. Nat. Cell Biol. 13:132-141(2011) [PubMed: 21258367] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF ULK1.
[21]	"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: 21205641] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF ULK1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL627307, AL929466 Genomic DNA. Translation: CAM18832.1. AL929466, AL627307 Genomic DNA. Translation: CAM24127.1. BC138565 mRNA. Translation: AAI38566.1. BC138566 mRNA. Translation: AAI38567.1. AK044030 mRNA. Translation: BAC31746.1. AK134573 mRNA. Translation: BAE22188.1.
IPI	IPI00123445.
RefSeq	NP_835279.2. NM_178143.2.
UniGene	Mm.48638.
3D structure databases
HSSP	HSSP built from PDB template 2EUE based on UniProtKB P06782.
ProteinModelPortal	Q8BRK8.
SMR	Q8BRK8. Positions 7-551.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8BRK8.
PTM databases
PhosphoSite	Q8BRK8.
Proteomic databases
PRIDE	Q8BRK8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000030243; ENSMUSP00000030243; ENSMUSG00000028518.
GeneID	108079.
KEGG	mmu:108079.
Organism-specific databases
CTD	5563.
MGI	MGI:1336173. Prkaa2.
Phylogenomic databases
eggNOG	roNOG12508.
GeneTree	ENSGT00600000084026.
HOGENOM	HBG755340.
HOVERGEN	HBG050432.
InParanoid	Q8BRK8.
OrthoDB	EOG4XSKPM.
PhylomeDB	Q8BRK8.
Gene expression databases
ArrayExpress	Q8BRK8.
Bgee	Q8BRK8.
Genevestigator	Q8BRK8.
GermOnline	ENSMUSG00000028518. Mus musculus.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K07198.
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
NextBio	360016.
SOURCE	Search...

Entry information

Entry name

AAPK2_MOUSE

Accession

Primary (citable) accession number: Q8BRK8
Secondary accession number(s): B1ASQ8, Q3UYM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	July 27, 2011
Last modified:	December 14, 2011
This is version 77 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program