Reviewed, UniProtKB/Swiss-Prot Q13131 (AAPK1_HUMAN)

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

Gene names

Name:	PRKAA1
Synonyms:	AMPK1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	559 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase. It also regulates cholesterol synthesis via phosphorylation and inactivation of hormone-sensitive lipase and hydroxymethylglutaryl-CoA reductase. Appears to act as a metabolic stress-sensing protein kinase switching off biosynthetic pathways when cellular ATP levels are depleted and when 5'-AMP rises in response to fuel limitation and/or hypoxia. This is a catalytic subunit. Ref.8 Ref.9
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Enzyme regulation	Binding of AMP results in allosteric activation, inducing phosphorylation on Thr-183 by STK11 in complex with STE20-related adapter-alpha (STRAD alpha) pseudo kinase and CAB39. Also activated by phosphorylation by CAMKK2 triggered by a rise in intracellular calcium ions, without detectable changes in the AMP/ATP ratio. Ref.8 Ref.9
Subunit structure	Heterotrimer of an alpha catalytic subunit, a beta and a gamma non-catalytic subunits. Interacts with FNIP1 and FNIP2. Ref.14 Ref.15
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily. Contains 1 protein kinase domain.
Sequence caution	The sequence AAH48980.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Cholesterol biosynthesis Fatty acid biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	activation of MAPK activity Non-traceable author statement. Source: UniProtKB cholesterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of glucosylceramide biosynthetic process Non-traceable author statement. Source: UniProtKB positive regulation of anti-apoptosis Non-traceable author statement. Source: UniProtKB positive regulation of cholesterol biosynthetic process Ref.7 Non-traceable author statement. Source: UniProtKB regulation of fatty acid oxidation Inferred from Experiment. Source: Reactome response to hypoxia Ref.7 Non-traceable author statement. Source: UniProtKB
Cellular component	intracellular Ref.7 Inferred by curator. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cAMP-dependent protein kinase activity Ref.7 Non-traceable author statement. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.15 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABI1	Q8IZP0	1	EBI-1181405,EBI-375446
CPE	P16870	1	EBI-1181405,EBI-711320
Ppard	P35396	1	EBI-1181405,EBI-1809541	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13131-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q13131-2)

The sequence of this isoform differs from the canonical sequence as follows:
     121-121: R → RKSDVPGVVKTGSTKE

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_0000085589
Regions
	Domain	27 – 279	253	Protein kinase
	Nucleotide binding	33 – 41	9	ATP 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
	Modified residue	183	1	Phosphothreonine; by STK11 By similarity
	Modified residue	184	1	Phosphoserine
	Modified residue	187	1	Phosphoserine
	Modified residue	269	1	Phosphothreonine By similarity
	Modified residue	355	1	Phosphothreonine
	Modified residue	356	1	Phosphoserine Ref.16 Ref.17
	Modified residue	382	1	Phosphothreonine Ref.17 Ref.13 Ref.20
	Modified residue	397	1	Phosphoserine
	Modified residue	441	1	Phosphotyrosine
	Modified residue	442	1	Phosphotyrosine Ref.11
	Modified residue	467	1	Phosphoserine
	Modified residue	476	1	Phosphoserine
	Modified residue	486	1	Phosphoserine Ref.16 Ref.17
	Modified residue	488	1	Phosphothreonine
	Modified residue	490	1	Phosphothreonine Ref.16 Ref.17 Ref.20
	Modified residue	496	1	Phosphoserine Ref.16 Ref.17 Ref.10 Ref.12
	Modified residue	502	1	Phosphoserine
	Modified residue	506	1	Phosphoserine
	Modified residue	508	1	Phosphoserine Ref.16
	Modified residue	516	1	Phosphoserine
	Modified residue	520	1	Phosphoserine
	Modified residue	522	1	Phosphothreonine
	Modified residue	523	1	Phosphoserine Ref.16
	Modified residue	524	1	Phosphoserine
	Modified residue	527	1	Phosphoserine Ref.16
Natural variations
	Alternative sequence	121	1	R → RKSDVPGVVKTGSTKE in isoform 2.		VSP_035431
	Natural variant	10	1	M → L: dbSNP rs17855679. Ref.2		VAR_058401
	Natural variant	16	1	Q → R in a breast cancer sample; somatic mutation. Ref.21		VAR_035622
Experimental info
	Sequence conflict	5	1	S → C in BAG35788. Ref.4
	Sequence conflict	9	1	K → S in AAD43027. Ref.5
	Sequence conflict	37	1	T → A in AAA64850. Ref.6
	Sequence conflict	202	1	A → V in AAA64850. Ref.6
	Sequence conflict	208	1	I → L in AAA64850. Ref.6
	Sequence conflict	269	1	T → S in BAA36547. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 28, 2009. Version 4. Checksum: ABAE71FBF912947A	FASTA	559	64,009
	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 QVDPMKRATI 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 VTSTYSKMSL QLYQVDSRTY LLDFRSIDDE 490 500 510 520 530 540 ITEAKSGTAT PQRSGSVSNY RSCQRSDSDA EAQGKSSEVS LTSSVTSLDS SPVDLTPRPG 550 SHTIEFFEMC ANLIKILAQ
	Isoform 2. Checksum: 8EA8B85393F48DAA	FASTA	574	65,523
	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 RKSDVPGVVK TGSTKELDEK ESRRLFQQIL SGVDYCHRHM VVHRDLKPEN VLLDAHMNAK 190 200 210 220 230 240 IADFGLSNMM SDGEFLRTSC GSPNYAAPEV ISGRLYAGPE VDIWSSGVIL YALLCGTLPF 250 260 270 280 290 300 DDDHVPTLFK KICDGIFYTP QYLNPSVISL LKHMLQVDPM KRATIKDIRE HEWFKQDLPK 310 320 330 340 350 360 YLFPEDPSYS STMIDDEALK EVCEKFECSE EEVLSCLYNR NHQDPLAVAY HLIIDNRRIM 370 380 390 400 410 420 NEAKDFYLAT SPPDSFLDDH HLTRPHPERV PFLVAETPRA RHTLDELNPQ KSKHQGVRKA 430 440 450 460 470 480 KWHLGIRSQS RPNDIMAEVC RAIKQLDYEW KVVNPYYLRV RRKNPVTSTY SKMSLQLYQV 490 500 510 520 530 540 DSRTYLLDFR SIDDEITEAK SGTATPQRSG SVSNYRSCQR SDSDAEAQGK SSEVSLTSSV 550 560 570 TSLDSSPVDL TPRPGSHTIE FFEMCANLIK ILAQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed: 15372022] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORMS 1 AND 2), VARIANT LEU-10. Tissue: Brain and Testis.
[3]	"Nucleotide sequence of cDNA for human AMP-activated protein kinase alpha-1." Yano K. Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-559 (ISOFORM 1). Tissue: Mammary gland.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-559 (ISOFORM 1). Tissue: Trachea.
[5]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-559 (ISOFORM 1). Tissue: Umbilical cord blood.
[6]	Taboada E.N., Hickey D.A. Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 36-209 (ISOFORM 1). Tissue: Intestine.
[7]	"Mammalian AMP-activated protein kinase subfamily." Stapleton D., Mitchelhill K.I., Gao G., Widmer J., Michell B.J., Teh T., House C.M., Fernandez C.S., Cox T., Witters L.A., Kemp B.E. J. Biol. Chem. 271:611-614(1996) [PubMed: 8557660] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 303-559 (ISOFORMS 1/2). Tissue: Liver.
[8]	"LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1." Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A., Boudeau J., Hawley S.A., Udd L., Maekelae T.P., Hardie D.G., Alessi D.R. EMBO J. 23:833-843(2004) [PubMed: 14976552] [Abstract] Cited for: FUNCTION, ENZYME REGULATION.
[9]	"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: 16054095] [Abstract] Cited for: FUNCTION, ENZYME REGULATION.
[10]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496, MASS SPECTROMETRY.
[11]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-442, MASS SPECTROMETRY.
[12]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496, MASS SPECTROMETRY. Tissue: Platelet.
[13]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-382, MASS SPECTROMETRY.
[14]	"Folliculin encoded by the BHD gene interacts with a binding protein, FNIP1, and AMPK, and is involved in AMPK and mTOR signaling." Baba M., Hong S.-B., Sharma N., Warren M.B., Nickerson M.L., Iwamatsu A., Esposito D., Gillette W.K., Hopkins R.F. III, Hartley J.L., Furihata M., Oishi S., Zhen W., Burke T.R. Jr., Linehan W.M., Schmidt L.S., Zbar B. Proc. Natl. Acad. Sci. U.S.A. 103:15552-15557(2006) [PubMed: 17028174] [Abstract] Cited for: INTERACTION WITH FNIP1.
[15]	"Identification and characterization of a novel folliculin-interacting protein FNIP2." Hasumi H., Baba M., Hong S.-B., Hasumi Y., Huang Y., Yao M., Valera V.A., Linehan W.M., Schmidt L.S. Gene 415:60-67(2008) [PubMed: 18403135] [Abstract] Cited for: INTERACTION WITH FNIP2.
[16]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; SER-486; THR-490; SER-496; SER-508; SER-523 AND SER-527, MASS SPECTROMETRY.
[17]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; THR-382; SER-486; THR-490 AND SER-496, MASS SPECTROMETRY.
[18]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[19]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32; THR-183; SER-184; SER-187; THR-355; SER-356; SER-397; TYR-441; SER-467; SER-476; SER-486; THR-488; THR-490; SER-496; SER-502; SER-506; SER-508; SER-516; SER-520; THR-522; SER-523; SER-524 AND SER-527, MASS SPECTROMETRY.
[20]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-382 AND THR-490, MASS SPECTROMETRY. Tissue: T-cell.
[21]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-16.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC008810 Genomic DNA. No translation available. BC048980 mRNA. Translation: AAH48980.1. AB022017 mRNA. Translation: BAA36547.1. Different initiation. AK312947 mRNA. Translation: BAG35788.1. Different initiation. BC037303 mRNA. Translation: AAH37303.1. Different initiation. AF100763 mRNA. Translation: AAD43027.1. Different initiation. U22456 mRNA. Translation: AAA64850.1. Different initiation. Y12856 mRNA. Translation: CAA73361.1. Different initiation.
IPI	IPI00410287. IPI00792482.
PIR	G01743.
RefSeq	NP_006242.5. NP_996790.3.
UniGene	Hs.43322
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-39973N.
IntAct	Q13131. 46 interactions.
STRING	Q13131.
PTM databases
PhosphoSite	Q13131.
Proteomic databases
PRIDE	Q13131.
Genome annotation databases
Ensembl	ENST00000397128; ENSP00000380317; ENSG00000132356; Homo sapiens. [Genome view]
GeneID	5562.
KEGG	hsa:5562.
Organism-specific databases
CTD	5562.
GeneCards	GC05M040795.
H-InvDB	HIX0004832.
HGNC	HGNC:9376. PRKAA1.
HPA	CAB005050.
MIM	602739. gene.
PharmGKB	PA33744.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16386.
HOVERGEN	Q13131.
OMA	QGVRRAK.
OrthoDB	EOG90ZTGR.
PhylomeDB	Q13131.
Enzyme and pathway databases
BRENDA	2.7.11.1. 247.
Reactome	REACT_1505. Integration of energy metabolism.
Gene expression databases
ArrayExpress	Q13131.
Bgee	Q13131.
CleanEx	HS_PRKAA1.
Genevestigator	Q13131.
GermOnline	ENSG00000132356. Homo sapiens.
Family and domain databases
InterPro	IPR020636. Ca/CaM-dep_prot_kinase-like. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR015741. Prot_kinase_Snf1-like_AMPK. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. [Graphical view]
PANTHER	PTHR22982:SF61. AMPK. 1 hit. PTHR22982. Ca/CaM-dep_prot_kinase-like. 1 hit.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00131. Adenosine monophosphate. DB00171. Adenosine triphosphate. DB00914. Phenformin.
SOURCE	Search...

Entry information

Entry name

AAPK1_HUMAN

Accession

Primary (citable) accession number: Q13131
Secondary accession number(s): A8MTQ6 , B2R7E1, O00286, Q5D0E1, Q86VS1, Q9UNQ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 28, 2009
Last modified:	February 9, 2010
This is version 108 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.