Q9UGJ0 (AAKG2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
5'-AMP-activated protein kinase subunit gamma-2
Short name=AMPK gamma2
Short name=AMPK subunit gamma-2

Alternative name(s):
H91620p

Gene names

Name:

PRKAG2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	569 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	AMP/ATP-binding 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. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive. Ref.8
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.
Tissue specificity	Isoform B is ubiquitously expressed except in liver and thymus. The highest level is detected in heart with abundant expression in placenta and testis.
Domain	The AMPK pseudosubstrate motif resembles the sequence around sites phosphorylated on target proteins of AMPK, except the presence of a non-phosphorylatable residue in place of Ser. In the absence of AMP this pseudosubstrate sequence may bind to the active site groove on the alpha subunit (PRKAA1 or PRKAA2), preventing phosphorylation by the upstream activating kinase STK11/LKB1. Ref.8 Ref.9 The CBS domains mediate binding to AMP, ADP and ATP. 2 sites bind either AMP or ATP, whereas a third site contains a tightly bound AMP that does not exchange. Under physiological conditions AMPK mainly exists in its inactive form in complex with ATP, which is much more abundant than AMP. Ref.8 Ref.9
Post-translational modification	Phosphorylated by ULK1; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1 and AMPK. Ref.12
Involvement in disease	Wolff-Parkinson-White syndrome (WPWS) [MIM:194200]: A supernormal conduction disorder characterized by the presence of one or several accessory atrioventricular connections, which can lead to episodes of sporadic tachycardia. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.15 Ref.17 Cardiomyopathy, familial hypertrophic 6 (CMH6) [MIM:600858]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. CMH6 patients present Wolff-Parkinson-White ventricular preexcitation, enlarged myocytes without myofiber disarray, and glycogen-containing cytosolic vacuoles within cardiomyocytes. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.20 Glycogen storage disease of heart lethal congenital (GSDH) [MIM:261740]: Rare disease which leads to death within a few weeks to a few months after birth, through heart failure and respiratory compromise. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21
Sequence similarities	Belongs to the 5'-AMP-activated protein kinase gamma subunit family. Contains 4 CBS domains.
Sequence caution	The sequence AAH20540.2 differs from that shown. Reason: Erroneous initiation. The sequence AAS02032.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAA84695.1 differs from that shown. Reason: Frameshift at positions 228 and 233. Frameshifts are upstream of the initiating Met of isoform B.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Cardiomyopathy Disease mutation Glycogen storage disease
Domain	CBS domain Repeat
Ligand	ATP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP biosynthetic process Traceable author statement Ref.16. Source: BHF-UCL carnitine shuttle Traceable author statement. Source: Reactome cell cycle arrest Traceable author statement. Source: Reactome cellular lipid metabolic process Traceable author statement. Source: Reactome cellular membrane organization Traceable author statement. Source: Reactome fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW glycogen metabolic process Inferred from mutant phenotype Ref.20Ref.21. Source: BHF-UCL insulin receptor signaling pathway Traceable author statement. Source: Reactome intracellular protein kinase cascade Inferred from mutant phenotype Ref.21. Source: BHF-UCL positive regulation of peptidyl-threonine phosphorylation Inferred from mutant phenotype Ref.21. Source: BHF-UCL regulation of fatty acid biosynthetic process Traceable author statement. Source: Reactome regulation of fatty acid oxidation Traceable author statement PubMed 9208914. Source: BHF-UCL regulation of glucose import Traceable author statement Ref.20. Source: BHF-UCL regulation of glycolysis Inferred from mutant phenotype Ref.21. Source: BHF-UCL sterol biosynthetic process Traceable author statement PubMed 9208914. Source: BHF-UCL
Cellular_component	AMP-activated protein kinase complex Inferred from direct assay Ref.21. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ADP binding Inferred from direct assay Ref.21. Source: BHF-UCL ATP binding Inferred from direct assay Ref.21. Source: BHF-UCL cAMP-dependent protein kinase inhibitor activity Inferred from direct assay Ref.9. Source: BHF-UCL cAMP-dependent protein kinase regulator activity Inferred from mutant phenotype Ref.21. Source: BHF-UCL phosphorylase kinase regulator activity Inferred from mutant phenotype Ref.21. Source: BHF-UCL protein kinase activator activity Inferred from mutant phenotype Ref.21. Source: BHF-UCL protein kinase binding Inferred from direct assay Ref.2. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: Q9UGJ0-1)

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 B (identifier: Q9UGJ0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-241: Missing.

Isoform C (identifier: Q9UGJ0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 569	569	5'-AMP-activated protein kinase subunit gamma-2		PRO_0000204381
Regions
	Domain	275 – 335	61	CBS 1
	Domain	357 – 415	59	CBS 2
	Domain	430 – 492	63	CBS 3
	Domain	504 – 562	59	CBS 4
	Motif	370 – 391	22	AMPK pseudosubstrate
Sites
	Binding site	302	1	AMP 1 By similarity
	Binding site	302	1	ATP 1 By similarity
	Binding site	383	1	AMP 2 By similarity
	Binding site	383	1	AMP 3 By similarity
	Binding site	383	1	ATP 2 By similarity
	Binding site	384	1	ATP 1 By similarity
	Binding site	384	1	ATP 2 By similarity
	Binding site	402	1	AMP 1 By similarity
	Binding site	402	1	ATP 1 By similarity
	Binding site	530	1	AMP 3 By similarity
	Binding site	531	1	AMP 1 By similarity
	Binding site	531	1	ATP 1 By similarity
Amino acid modifications
	Modified residue	65	1	Phosphoserine By similarity
	Modified residue	71	1	Phosphoserine By similarity
	Modified residue	73	1	Phosphoserine By similarity
	Modified residue	90	1	Phosphoserine By similarity
	Modified residue	138	1	Phosphoserine By similarity
	Modified residue	161	1	Phosphoserine By similarity
	Modified residue	162	1	Phosphoserine By similarity
	Modified residue	196	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 241	241	Missing in isoform B.		VSP_000261
	Alternative sequence	1 – 44	44	Missing in isoform C.		VSP_015589
	Natural variant	6	1	M → L. Corresponds to variant rs3207363 [ dbSNP | Ensembl ].		VAR_048250
	Natural variant	302	1	R → Q in WPWS and CMH6; impaired AMP- and ATP-binding. Ref.8 Ref.17 Ref.20		VAR_013264
	Natural variant	350	1	R → RL in CMH6; severe. Ref.16		VAR_013265
	Natural variant	383	1	H → R in CMH6; severe; impaired AMP- and ATP-binding. Ref.8 Ref.16		VAR_013266
	Natural variant	400	1	T → N in CMH6; severe; impaired AMP- and ATP-binding. Ref.8 Ref.20 Corresponds to variant rs28938173 [ dbSNP | Ensembl ].		VAR_013267
	Natural variant	488	1	N → I in CMH6; severe. Ref.20		VAR_013268
	Natural variant	531	1	R → G in WPWS; absence of cardiac hypertrophy; onset in childhood; impaired AMP- and ATP-binding. Ref.8 Ref.15		VAR_032909
	Natural variant	531	1	R → Q in GSDH; reduction of binding affinities for AMP and ATP; loss of cooperative binding; enhanced basal activity; increased phosphorylation of the alpha-subunit. Ref.21		VAR_013269
Experimental info
	Mutagenesis	387	1	V → S: Induces phosphorylation by AMPK. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified May 1, 2000. Version 1. Checksum: F51C30668C294089	FASTA	569	63,066
	10 20 30 40 50 60 MGSAVMDTKK KKDVSSPGGS GGKKNASQKR RSLRVHIPDL SSFAMPLLDG DLEGSGKHSS 70 80 90 100 110 120 RKVDSPFGPG SPSKGFFSRG PQPRPSSPMS APVRPKTSPG SPKTVFPFSY QESPPRSPRR 130 140 150 160 170 180 MSFSGIFRSS SKESSPNSNP ATSPGGIRFF SRSRKTSGLS SSPSTPTQVT KQHTFPLESY 190 200 210 220 230 240 KHEPERLENR IYASSSPPDT GQRFCPSSFQ SPTRPPLASP THYAPSKAAA LAAALGPAEA 250 260 270 280 290 300 GMLEKLEFED EAVEDSESGV YMRFMRSHKC YDIVPTSSKL VVFDTTLQVK KAFFALVANG 310 320 330 340 350 360 VRAAPLWESK KQSFVGMLTI TDFINILHRY YKSPMVQIYE LEEHKIETWR ELYLQETFKP 370 380 390 400 410 420 LVNISPDASL FDAVYSLIKN KIHRLPVIDP ISGNALYILT HKRILKFLQL FMSDMPKPAF 430 440 450 460 470 480 MKQNLDELGI GTYHNIAFIH PDTPIIKALN IFVERRISAL PVVDESGKVV DIYSKFDVIN 490 500 510 520 530 540 LAAEKTYNNL DITVTQALQH RSQYFEGVVK CNKLEILETI VDRIVRAEVH RLVVVNEADS 550 560 IVGIISLSDI LQALILTPAG AKQKETETE
	Isoform B [UniParc]. Checksum: D8402E96E46DB5A5	FASTA	328	37,509
	10 20 30 40 50 60 MLEKLEFEDE AVEDSESGVY MRFMRSHKCY DIVPTSSKLV VFDTTLQVKK AFFALVANGV 70 80 90 100 110 120 RAAPLWESKK QSFVGMLTIT DFINILHRYY KSPMVQIYEL EEHKIETWRE LYLQETFKPL 130 140 150 160 170 180 VNISPDASLF DAVYSLIKNK IHRLPVIDPI SGNALYILTH KRILKFLQLF MSDMPKPAFM 190 200 210 220 230 240 KQNLDELGIG TYHNIAFIHP DTPIIKALNI FVERRISALP VVDESGKVVD IYSKFDVINL 250 260 270 280 290 300 AAEKTYNNLD ITVTQALQHR SQYFEGVVKC NKLEILETIV DRIVRAEVHR LVVVNEADSI 310 320 VGIISLSDIL QALILTPAGA KQKETETE
	Isoform C [UniParc]. Checksum: 873DEE12F27F133D	FASTA	525	58,439
	10 20 30 40 50 60 MPLLDGDLEG SGKHSSRKVD SPFGPGSPSK GFFSRGPQPR PSSPMSAPVR PKTSPGSPKT 70 80 90 100 110 120 VFPFSYQESP PRSPRRMSFS GIFRSSSKES SPNSNPATSP GGIRFFSRSR KTSGLSSSPS 130 140 150 160 170 180 TPTQVTKQHT FPLESYKHEP ERLENRIYAS SSPPDTGQRF CPSSFQSPTR PPLASPTHYA 190 200 210 220 230 240 PSKAAALAAA LGPAEAGMLE KLEFEDEAVE DSESGVYMRF MRSHKCYDIV PTSSKLVVFD 250 260 270 280 290 300 TTLQVKKAFF ALVANGVRAA PLWESKKQSF VGMLTITDFI NILHRYYKSP MVQIYELEEH 310 320 330 340 350 360 KIETWRELYL QETFKPLVNI SPDASLFDAV YSLIKNKIHR LPVIDPISGN ALYILTHKRI 370 380 390 400 410 420 LKFLQLFMSD MPKPAFMKQN LDELGIGTYH NIAFIHPDTP IIKALNIFVE RRISALPVVD 430 440 450 460 470 480 ESGKVVDIYS KFDVINLAAE KTYNNLDITV TQALQHRSQY FEGVVKCNKL EILETIVDRI 490 500 510 520 VRAEVHRLVV VNEADSIVGI ISLSDILQAL ILTPAGAKQK ETETE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human homolog of AMPK gamma-1 chain." Hattori A., Seki N., Hayashi A., Kozuma S., Muramatsu M., Saito T. Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
[2]	"Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding." Cheung P.C.F., Salt I.P., Davies S.P., Hardie D.G., Carling D. Biochem. J. 346:659-669(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[3]	"Molecular cloning, genomic organization, and mapping of PRKAG2, a heart abundant gamma-2 subunit of 5'-AMP-activated protein kinase, to human chromosome 7q36." Lang T.M., Yu L., Qiang T., Jiang J.M., Chen Z., Xin Y.R., Liu G.Y., Zhao S. Genomics 70:258-263(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). Tissue: Placenta.
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
[6]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND C). Tissue: Brain and Liver.
[8]	"CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations." Scott J.W., Hawley S.A., Green K.A., Anis M., Stewart G., Scullion G.A., Norman D.G., Hardie D.G. J. Clin. Invest. 113:274-284(2004) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN CBS, AMP-BINDING, ATP-BINDING, CHARACTERIZATION OF VARIANTS WPWS GLN-302; ARG-383 AND ASN-400, CHARACTERIZATION OF VARIANT WPWS GLY-531, FUNCTION.
[9]	"Regulation of AMP-activated protein kinase by a pseudosubstrate sequence on the gamma subunit." Scott J.W., Ross F.A., Liu J.K., Hardie D.G. EMBO J. 26:806-815(2007) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN AMPK PSEUDOSUBSTRATE, MUTAGENESIS OF VAL-387.
[10]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[11]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"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.
[13]	"AMP-activated protein kinase in metabolic control and insulin signaling." Towler M.C., Hardie D.G. Circ. Res. 100:328-341(2007) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[14]	"AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy." Hardie D.G. Nat. Rev. Mol. Cell Biol. 8:774-785(2007) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[15]	"Novel PRKAG2 mutation responsible for the genetic syndrome of ventricular preexcitation and conduction system disease with childhood onset and absence of cardiac hypertrophy." Gollob M.H., Seger J.J., Gollob T.N., Tapscott T., Gonzales O., Bachinski L., Roberts R. Circulation 104:3030-3033(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT WPWS GLY-531.
[16]	"Mutations in the gamma(2) subunit of AMP-activated protein kinase cause familial hypertrophic cardiomyopathy: evidence for the central role of energy compromise in disease pathogenesis." Blair E., Redwood C., Ashrafian H., Oliveira M., Broxholme J., Kerr B., Salmon A., Oestman-Smith I., Watkins H. Hum. Mol. Genet. 10:1215-1220(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CMH6 LEU-350 INS AND ARG-383.
[17]	"Identification of a gene responsible for familial Wolff-Parkinson-White syndrome." Gollob M.H., Green M.S., Tang A.S.-L., Gollob T., Karibe A., Al Sayegh A.H., Ahmad F., Lozado R., Shah G., Fananapazir L., Bachinski L.L., Roberts R. N. Engl. J. Med. 344:1823-1831(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT WPWS GLN-302.
[18]	Erratum Gollob M.H., Green M.S., Tang A.S.-L., Gollob T., Karibe A., Al Sayegh A.H., Ahmad F., Lozado R., Shah G., Fananapazir L., Bachinski L.L., Roberts R. N. Engl. J. Med. 345:552-552(2001)
[19]	Erratum Gollob M.H., Green M.S., Tang A.S.-L., Gollob T., Karibe A., Al Sayegh A.H., Ahmad F., Lozado R., Shah G., Fananapazir L., Bachinski L.L., Roberts R. N. Engl. J. Med. 346:300-300(2002)
[20]	"Constitutively active AMP kinase mutations cause glycogen storage disease mimicking hypertrophic cardiomyopathy." Arad M., Benson D.W., Perez-Atayde A.R., McKenna W.J., Sparks E.A., Kanter R.J., McGarry K., Seidman J.G., Seidman C.E. J. Clin. Invest. 109:357-362(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CMH6 GLN-302; ASN-400 AND ILE-488.
[21]	"Fatal congenital heart glycogenosis caused by a recurrent activating R531Q mutation in the gamma 2-subunit of AMP-activated protein kinase (PRKAG2), not by phosphorylase kinase deficiency." Burwinkel B., Scott J.W., Buehrer C., van Landeghem F.K.H., Cox G.F., Wilson C.J., Grahame Hardie D., Kilimann M.W. Am. J. Hum. Genet. 76:1034-1049(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSDH GLN-531, CHARACTERIZATION OF VARIANT GSDH GLN-531.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB025580 mRNA. Translation: BAA84695.1. Frameshift. AJ249976 mRNA. Translation: CAB65116.1. AF087875 mRNA. Translation: AAK00413.1. AK001887 mRNA. Translation: BAA91962.1. BT007127 mRNA. Translation: AAP35791.1. AC006358 Genomic DNA. Translation: AAS02032.1. Sequence problems. AC006966 Genomic DNA. Translation: AAF03528.2. AC093583 Genomic DNA. No translation available. BC020540 mRNA. Translation: AAH20540.2. Different initiation. BC068598 mRNA. Translation: AAH68598.1.
IPI	IPI00005367. IPI00219377. IPI00646448.
RefSeq	NP_001035723.1. NM_001040633.1. NP_057287.2. NM_016203.3. NP_077747.1. NM_024429.1.
UniGene	Hs.647072.
3D structure databases
ProteinModelPortal	Q9UGJ0.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UGJ0. 15 interactions.
MINT	MINT-4831646.
STRING	9606.ENSP00000287878.
PTM databases
PhosphoSite	Q9UGJ0.
Polymorphism databases
DMDM	14285344.
Proteomic databases
PaxDb	Q9UGJ0.
PRIDE	Q9UGJ0.
Protocols and materials databases
DNASU	51422.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000287878; ENSP00000287878; ENSG00000106617. ENST00000392801; ENSP00000376549; ENSG00000106617. ENST00000418337; ENSP00000387386; ENSG00000106617.
GeneID	51422.
KEGG	hsa:51422.
UCSC	uc003wki.3. human.
Organism-specific databases
CTD	51422.
GeneCards	GC07M151253.
HGNC	HGNC:9386. PRKAG2.
HPA	CAB018641. HPA004246.
MIM	194200. phenotype. 261740. phenotype. 600858. phenotype. 602743. gene.
neXtProt	NX_Q9UGJ0.
Orphanet	155. Familial isolated hypertrophic cardiomyopathy. 907. Wolff-Parkinson-White syndrome.
PharmGKB	PA33752.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0517.
HOVERGEN	HBG050431.
InParanoid	Q9UGJ0.
KO	K07200.
OMA	FSRGPQH.
OrthoDB	EOG45DWPQ.
PhylomeDB	Q9UGJ0.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_11123. Membrane Trafficking. REACT_11163. Activated AMPK stimulates fatty-acid oxidation in muscle.
SignaLink	Q9UGJ0.
Gene expression databases
ArrayExpress	Q9UGJ0.
Bgee	Q9UGJ0.
CleanEx	HS_PRKAG2.
Genevestigator	Q9UGJ0.
GermOnline	ENSG00000106617. Homo sapiens.
Family and domain databases
InterPro	IPR000644. Cysta_beta_synth_core. [Graphical view]
Pfam	PF00571. CBS. 3 hits. [Graphical view]
SMART	SM00116. CBS. 4 hits. [Graphical view]
PROSITE	PS51371. CBS. 4 hits. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9UGJ0.
ChEMBL	CHEMBL2453.
ChiTaRS	PRKAG2. human.
GenomeRNAi	51422.
NextBio	54969.
SOURCE	Search...

Entry information

Entry name

AAKG2_HUMAN

Accession

Primary (citable) accession number: Q9UGJ0
Secondary accession number(s): Q53Y07 , Q6NUI0, Q75MP4, Q9NUZ9, Q9UDN8, Q9ULX8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	May 1, 2000
Last modified:	May 29, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.