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Q9UGJ0 (AAKG2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length569 AA.
Sequence statusComplete.
Protein existenceEvidence 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.13

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.16 Ref.18

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.17 Ref.21

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.22

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 processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCardiomyopathy
Disease mutation
Glycogen storage disease
   DomainCBS domain
Repeat
   LigandATP-binding
Nucleotide-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP biosynthetic process

Traceable author statement Ref.17. 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

energy reserve metabolic process

Traceable author statement. Source: Reactome

fatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

glycogen metabolic process

Inferred from mutant phenotype Ref.21Ref.22. Source: BHF-UCL

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

intracellular signal transduction

Inferred from mutant phenotype Ref.22. Source: BHF-UCL

membrane organization

Traceable author statement. Source: Reactome

negative regulation of protein kinase activity

Inferred from direct assay Ref.9. Source: BHF-UCL

negative regulation of protein serine/threonine kinase activity

Inferred from direct assay Ref.9. Source: GOC

positive regulation of peptidyl-threonine phosphorylation

Inferred from mutant phenotype Ref.22. Source: BHF-UCL

positive regulation of protein kinase activity

Inferred from mutant phenotype Ref.22. Source: BHF-UCL

regulation of fatty acid biosynthetic process

Traceable author statement. Source: Reactome

regulation of fatty acid metabolic process

Inferred from mutant phenotype Ref.22. Source: BHF-UCL

regulation of fatty acid oxidation

Traceable author statement PubMed 9208914. Source: BHF-UCL

regulation of glucose import

Traceable author statement Ref.21. Source: BHF-UCL

regulation of glycolysis

Inferred from mutant phenotype Ref.22. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

sterol biosynthetic process

Traceable author statement PubMed 9208914. Source: BHF-UCL

   Cellular_componentAMP-activated protein kinase complex

Inferred from direct assay Ref.22. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 22664934. Source: UniProt

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionADP binding

Inferred from direct assay Ref.22. Source: BHF-UCL

AMP binding

Inferred from electronic annotation. Source: Ensembl

ATP binding

Inferred from direct assay Ref.22. 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.22. Source: BHF-UCL

phosphorylase kinase regulator activity

Inferred from mutant phenotype Ref.22. Source: BHF-UCL

protein kinase activator activity

Inferred from mutant phenotype Ref.22. 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5695695'-AMP-activated protein kinase subunit gamma-2
PRO_0000204381

Regions

Domain275 – 33561CBS 1
Domain357 – 41559CBS 2
Domain430 – 49263CBS 3
Domain504 – 56259CBS 4
Motif370 – 39122AMPK pseudosubstrate

Sites

Binding site3021AMP 1 By similarity
Binding site3021ATP 1 By similarity
Binding site3831AMP 2 By similarity
Binding site3831AMP 3 By similarity
Binding site3831ATP 2 By similarity
Binding site3841ATP 1 By similarity
Binding site3841ATP 2 By similarity
Binding site4021AMP 1 By similarity
Binding site4021ATP 1 By similarity
Binding site5301AMP 3 By similarity
Binding site5311AMP 1 By similarity
Binding site5311ATP 1 By similarity

Amino acid modifications

Modified residue651Phosphoserine By similarity
Modified residue711Phosphoserine By similarity
Modified residue731Phosphoserine By similarity
Modified residue901Phosphoserine By similarity
Modified residue1381Phosphoserine By similarity
Modified residue1431Phosphoserine By similarity
Modified residue1611Phosphoserine By similarity
Modified residue1961Phosphoserine By similarity

Natural variations

Alternative sequence1 – 241241Missing in isoform B.
VSP_000261
Alternative sequence1 – 4444Missing in isoform C.
VSP_015589
Natural variant61M → L.
Corresponds to variant rs3207363 [ dbSNP | Ensembl ].
VAR_048250
Natural variant3021R → Q in WPWS and CMH6; impaired AMP- and ATP-binding. Ref.8 Ref.18 Ref.21
VAR_013264
Natural variant3501R → RL in CMH6; severe. Ref.17
VAR_013265
Natural variant3831H → R in CMH6; severe; impaired AMP- and ATP-binding. Ref.8 Ref.17
VAR_013266
Natural variant4001T → N in CMH6; severe; impaired AMP- and ATP-binding. Ref.8 Ref.21
Corresponds to variant rs28938173 [ dbSNP | Ensembl ].
VAR_013267
Natural variant4881N → I in CMH6; severe. Ref.21
VAR_013268
Natural variant5311R → G in WPWS; absence of cardiac hypertrophy; onset in childhood; impaired AMP- and ATP-binding. Ref.8 Ref.16
VAR_032909
Natural variant5311R → 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.22
VAR_013269

Experimental info

Mutagenesis3871V → S: Induces phosphorylation by AMPK. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: F51C30668C294089

FASTA56963,066
        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 

« Hide

Isoform B [UniParc].

Checksum: D8402E96E46DB5A5
Show »

FASTA32837,509
Isoform C [UniParc].

Checksum: 873DEE12F27F133D
Show »

FASTA52558,439

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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].
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[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. 345:552-552(2001)
[20]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)
[21]"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.
[22]"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

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.
RefSeqNP_001035723.1. NM_001040633.1.
NP_057287.2. NM_016203.3.
NP_077747.1. NM_024429.1.
UniGeneHs.647072.

3D structure databases

ProteinModelPortalQ9UGJ0.
SMRQ9UGJ0. Positions 256-557.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119531. 19 interactions.
IntActQ9UGJ0. 15 interactions.
MINTMINT-4831646.
STRING9606.ENSP00000287878.

Chemistry

BindingDBQ9UGJ0.
ChEMBLCHEMBL2096907.

PTM databases

PhosphoSiteQ9UGJ0.

Polymorphism databases

DMDM14285344.

Proteomic databases

PaxDbQ9UGJ0.
PRIDEQ9UGJ0.

Protocols and materials databases

DNASU51422.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000287878; ENSP00000287878; ENSG00000106617. [Q9UGJ0-1]
ENST00000392801; ENSP00000376549; ENSG00000106617. [Q9UGJ0-3]
ENST00000418337; ENSP00000387386; ENSG00000106617. [Q9UGJ0-2]
GeneID51422.
KEGGhsa:51422.
UCSCuc003wki.3. human. [Q9UGJ0-1]

Organism-specific databases

CTD51422.
GeneCardsGC07M151253.
HGNCHGNC:9386. PRKAG2.
HPACAB018641.
HPA004246.
MIM194200. phenotype.
261740. phenotype.
600858. phenotype.
602743. gene.
neXtProtNX_Q9UGJ0.
Orphanet155. Familial isolated hypertrophic cardiomyopathy.
907. Wolff-Parkinson-White syndrome.
PharmGKBPA33752.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0517.
HOVERGENHBG050431.
InParanoidQ9UGJ0.
KOK07200.
OMAXVQIYEL.
OrthoDBEOG74FF0W.
PhylomeDBQ9UGJ0.
TreeFamTF313247.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_11123. Membrane Trafficking.
SignaLinkQ9UGJ0.

Gene expression databases

ArrayExpressQ9UGJ0.
BgeeQ9UGJ0.
CleanExHS_PRKAG2.
GenevestigatorQ9UGJ0.

Family and domain databases

InterProIPR000644. CBS_dom.
[Graphical view]
PfamPF00571. CBS. 3 hits.
[Graphical view]
SMARTSM00116. CBS. 4 hits.
[Graphical view]
PROSITEPS51371. CBS. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRKAG2. human.
GeneWikiPRKAG2.
GenomeRNAi51422.
NextBio54969.
PROQ9UGJ0.
SOURCESearch...

Entry information

Entry nameAAKG2_HUMAN
AccessionPrimary (citable) accession number: Q9UGJ0
Secondary accession number(s): Q53Y07 expand/collapse secondary AC list , Q6NUI0, Q75MP4, Q9NUZ9, Q9UDN8, Q9ULX8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM