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Q9UGJ0

- AAKG2_HUMAN

UniProt

Q9UGJ0 - AAKG2_HUMAN

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Protein

5'-AMP-activated protein kinase subunit gamma-2

Gene

PRKAG2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei302 – 3021AMP 1By similarity
Binding sitei302 – 3021ATP 1By similarity
Binding sitei383 – 3831AMP 2By similarity
Binding sitei383 – 3831AMP 3By similarity
Binding sitei383 – 3831ATP 2By similarity
Binding sitei384 – 3841ATP 1By similarity
Binding sitei384 – 3841ATP 2By similarity
Binding sitei402 – 4021AMP 1By similarity
Binding sitei402 – 4021ATP 1By similarity
Binding sitei530 – 5301AMP 3By similarity
Binding sitei531 – 5311AMP 1By similarity
Binding sitei531 – 5311ATP 1By similarity

GO - Molecular functioni

  1. ADP binding Source: BHF-UCL
  2. AMP binding Source: Ensembl
  3. ATP binding Source: BHF-UCL
  4. cAMP-dependent protein kinase inhibitor activity Source: BHF-UCL
  5. cAMP-dependent protein kinase regulator activity Source: BHF-UCL
  6. phosphorylase kinase regulator activity Source: BHF-UCL
  7. protein kinase activator activity Source: BHF-UCL
  8. protein kinase binding Source: BHF-UCL

GO - Biological processi

  1. ATP biosynthetic process Source: BHF-UCL
  2. carnitine shuttle Source: Reactome
  3. cell cycle arrest Source: Reactome
  4. cellular lipid metabolic process Source: Reactome
  5. energy reserve metabolic process Source: Reactome
  6. fatty acid biosynthetic process Source: UniProtKB-KW
  7. glycogen metabolic process Source: BHF-UCL
  8. insulin receptor signaling pathway Source: Reactome
  9. intracellular signal transduction Source: BHF-UCL
  10. membrane organization Source: Reactome
  11. negative regulation of protein kinase activity Source: BHF-UCL
  12. negative regulation of protein serine/threonine kinase activity Source: GOC
  13. positive regulation of peptidyl-threonine phosphorylation Source: BHF-UCL
  14. positive regulation of protein kinase activity Source: BHF-UCL
  15. regulation of fatty acid biosynthetic process Source: Reactome
  16. regulation of fatty acid metabolic process Source: BHF-UCL
  17. regulation of fatty acid oxidation Source: BHF-UCL
  18. regulation of glucose import Source: BHF-UCL
  19. regulation of glycolytic process Source: BHF-UCL
  20. small molecule metabolic process Source: Reactome
  21. sterol biosynthetic process Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_11082. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_1988. AMPK inhibits chREBP transcriptional activation activity.
REACT_200686. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_21285. Regulation of AMPK activity via LKB1.
REACT_21393. Regulation of Rheb GTPase activity by AMPK.
SignaLinkiQ9UGJ0.

Names & Taxonomyi

Protein namesi
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 namesi
Name:PRKAG2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:9386. PRKAG2.

Subcellular locationi

GO - Cellular componenti

  1. AMP-activated protein kinase complex Source: BHF-UCL
  2. cytosol Source: Reactome
  3. extracellular space Source: UniProt
  4. nucleoplasm Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti302 – 3021R → Q in WPWS and CMH6; impaired AMP- and ATP-binding. 2 Publications
VAR_013264
Natural varianti531 – 5311R → G in WPWS; absence of cardiac hypertrophy; onset in childhood; impaired AMP- and ATP-binding. 1 Publication
VAR_032909
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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti302 – 3021R → Q in WPWS and CMH6; impaired AMP- and ATP-binding. 2 Publications
VAR_013264
Natural varianti350 – 3501R → RL in CMH6; severe. 1 Publication
VAR_013265
Natural varianti383 – 3831H → R in CMH6; severe; impaired AMP- and ATP-binding. 1 Publication
VAR_013266
Natural varianti400 – 4001T → N in CMH6; severe; impaired AMP- and ATP-binding. 1 Publication
Corresponds to variant rs28938173 [ dbSNP | Ensembl ].
VAR_013267
Natural varianti488 – 4881N → I in CMH6; severe. 1 Publication
VAR_013268
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti531 – 5311R → Q in GSDH; reduction of binding affinities for AMP and ATP; loss of cooperative binding; enhanced basal activity; increased phosphorylation of the alpha-subunit. 1 Publication
VAR_013269

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi387 – 3871V → S: Induces phosphorylation by AMPK. 1 Publication

Keywords - Diseasei

Cardiomyopathy, Disease mutation, Glycogen storage disease

Organism-specific databases

MIMi194200. phenotype.
261740. phenotype.
600858. phenotype.
Orphaneti155. Familial isolated hypertrophic cardiomyopathy.
907. Wolff-Parkinson-White syndrome.
PharmGKBiPA33752.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5695695'-AMP-activated protein kinase subunit gamma-2PRO_0000204381Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei65 – 651PhosphoserineBy similarity
Modified residuei71 – 711PhosphoserineBy similarity
Modified residuei73 – 731PhosphoserineBy similarity
Modified residuei90 – 901PhosphoserineBy similarity
Modified residuei138 – 1381PhosphoserineBy similarity
Modified residuei143 – 1431PhosphoserineBy similarity
Modified residuei161 – 1611PhosphoserineBy similarity
Modified residuei196 – 1961PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by ULK1; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1 and AMPK.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UGJ0.
PaxDbiQ9UGJ0.
PRIDEiQ9UGJ0.

PTM databases

PhosphoSiteiQ9UGJ0.

Expressioni

Tissue specificityi

Isoform B is ubiquitously expressed except in liver and thymus. The highest level is detected in heart with abundant expression in placenta and testis.

Gene expression databases

BgeeiQ9UGJ0.
CleanExiHS_PRKAG2.
ExpressionAtlasiQ9UGJ0. baseline and differential.
GenevestigatoriQ9UGJ0.

Organism-specific databases

HPAiCAB018641.
HPA004246.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi119531. 21 interactions.
IntActiQ9UGJ0. 15 interactions.
MINTiMINT-4831646.
STRINGi9606.ENSP00000287878.

Structurei

3D structure databases

ProteinModelPortaliQ9UGJ0.
SMRiQ9UGJ0. Positions 260-557.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini275 – 33561CBS 1PROSITE-ProRule annotationAdd
BLAST
Domaini357 – 41559CBS 2PROSITE-ProRule annotationAdd
BLAST
Domaini430 – 49263CBS 3PROSITE-ProRule annotationAdd
BLAST
Domaini504 – 56259CBS 4PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi370 – 39122AMPK pseudosubstrateAdd
BLAST

Domaini

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.
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.

Sequence similaritiesi

Contains 4 CBS domains.PROSITE-ProRule annotation

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiCOG0517.
GeneTreeiENSGT00390000009849.
HOVERGENiHBG050431.
KOiK07200.
OMAiGAKQKEN.
OrthoDBiEOG74FF0W.
PhylomeDBiQ9UGJ0.
TreeFamiTF313247.

Family and domain databases

InterProiIPR000644. CBS_dom.
[Graphical view]
PfamiPF00571. CBS. 3 hits.
[Graphical view]
SMARTiSM00116. CBS. 4 hits.
[Graphical view]
PROSITEiPS51371. CBS. 4 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform A (identifier: Q9UGJ0-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGSAVMDTKK KKDVSSPGGS GGKKNASQKR RSLRVHIPDL SSFAMPLLDG
60 70 80 90 100
DLEGSGKHSS RKVDSPFGPG SPSKGFFSRG PQPRPSSPMS APVRPKTSPG
110 120 130 140 150
SPKTVFPFSY QESPPRSPRR MSFSGIFRSS SKESSPNSNP ATSPGGIRFF
160 170 180 190 200
SRSRKTSGLS SSPSTPTQVT KQHTFPLESY KHEPERLENR IYASSSPPDT
210 220 230 240 250
GQRFCPSSFQ SPTRPPLASP THYAPSKAAA LAAALGPAEA GMLEKLEFED
260 270 280 290 300
EAVEDSESGV YMRFMRSHKC YDIVPTSSKL VVFDTTLQVK KAFFALVANG
310 320 330 340 350
VRAAPLWESK KQSFVGMLTI TDFINILHRY YKSPMVQIYE LEEHKIETWR
360 370 380 390 400
ELYLQETFKP LVNISPDASL FDAVYSLIKN KIHRLPVIDP ISGNALYILT
410 420 430 440 450
HKRILKFLQL FMSDMPKPAF MKQNLDELGI GTYHNIAFIH PDTPIIKALN
460 470 480 490 500
IFVERRISAL PVVDESGKVV DIYSKFDVIN LAAEKTYNNL DITVTQALQH
510 520 530 540 550
RSQYFEGVVK CNKLEILETI VDRIVRAEVH RLVVVNEADS IVGIISLSDI
560
LQALILTPAG AKQKETETE
Length:569
Mass (Da):63,066
Last modified:May 1, 2000 - v1
Checksum:iF51C30668C294089
GO
Isoform B (identifier: Q9UGJ0-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:328
Mass (Da):37,509
Checksum:iD8402E96E46DB5A5
GO
Isoform C (identifier: Q9UGJ0-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:525
Mass (Da):58,439
Checksum:i873DEE12F27F133D
GO

Sequence cautioni

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.
The sequence AAH20540.2 differs from that shown. Reason: Erroneous initiation.
The sequence AAS02032.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61M → L.
Corresponds to variant rs3207363 [ dbSNP | Ensembl ].
VAR_048250
Natural varianti302 – 3021R → Q in WPWS and CMH6; impaired AMP- and ATP-binding. 2 Publications
VAR_013264
Natural varianti350 – 3501R → RL in CMH6; severe. 1 Publication
VAR_013265
Natural varianti383 – 3831H → R in CMH6; severe; impaired AMP- and ATP-binding. 1 Publication
VAR_013266
Natural varianti400 – 4001T → N in CMH6; severe; impaired AMP- and ATP-binding. 1 Publication
Corresponds to variant rs28938173 [ dbSNP | Ensembl ].
VAR_013267
Natural varianti488 – 4881N → I in CMH6; severe. 1 Publication
VAR_013268
Natural varianti531 – 5311R → G in WPWS; absence of cardiac hypertrophy; onset in childhood; impaired AMP- and ATP-binding. 1 Publication
VAR_032909
Natural varianti531 – 5311R → Q in GSDH; reduction of binding affinities for AMP and ATP; loss of cooperative binding; enhanced basal activity; increased phosphorylation of the alpha-subunit. 1 Publication
VAR_013269

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 241241Missing in isoform B. 5 PublicationsVSP_000261Add
BLAST
Alternative sequencei1 – 4444Missing in isoform C. 1 PublicationVSP_015589Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS43683.1. [Q9UGJ0-3]
CCDS47752.1. [Q9UGJ0-2]
CCDS5928.1. [Q9UGJ0-1]
RefSeqiNP_001035723.1. NM_001040633.1. [Q9UGJ0-3]
NP_057287.2. NM_016203.3. [Q9UGJ0-1]
NP_077747.1. NM_024429.1. [Q9UGJ0-2]
UniGeneiHs.647072.

Genome annotation databases

EnsembliENST00000287878; ENSP00000287878; ENSG00000106617. [Q9UGJ0-1]
ENST00000392801; ENSP00000376549; ENSG00000106617. [Q9UGJ0-3]
ENST00000418337; ENSP00000387386; ENSG00000106617. [Q9UGJ0-2]
GeneIDi51422.
KEGGihsa:51422.
UCSCiuc003wki.3. human. [Q9UGJ0-1]

Polymorphism databases

DMDMi14285344.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS43683.1. [Q9UGJ0-3 ]
CCDS47752.1. [Q9UGJ0-2 ]
CCDS5928.1. [Q9UGJ0-1 ]
RefSeqi NP_001035723.1. NM_001040633.1. [Q9UGJ0-3 ]
NP_057287.2. NM_016203.3. [Q9UGJ0-1 ]
NP_077747.1. NM_024429.1. [Q9UGJ0-2 ]
UniGenei Hs.647072.

3D structure databases

ProteinModelPortali Q9UGJ0.
SMRi Q9UGJ0. Positions 260-557.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119531. 21 interactions.
IntActi Q9UGJ0. 15 interactions.
MINTi MINT-4831646.
STRINGi 9606.ENSP00000287878.

Chemistry

BindingDBi Q9UGJ0.
ChEMBLi CHEMBL2096907.
DrugBanki DB00945. Acetylsalicylic acid.

PTM databases

PhosphoSitei Q9UGJ0.

Polymorphism databases

DMDMi 14285344.

Proteomic databases

MaxQBi Q9UGJ0.
PaxDbi Q9UGJ0.
PRIDEi Q9UGJ0.

Protocols and materials databases

DNASUi 51422.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000287878 ; ENSP00000287878 ; ENSG00000106617 . [Q9UGJ0-1 ]
ENST00000392801 ; ENSP00000376549 ; ENSG00000106617 . [Q9UGJ0-3 ]
ENST00000418337 ; ENSP00000387386 ; ENSG00000106617 . [Q9UGJ0-2 ]
GeneIDi 51422.
KEGGi hsa:51422.
UCSCi uc003wki.3. human. [Q9UGJ0-1 ]

Organism-specific databases

CTDi 51422.
GeneCardsi GC07M151253.
GeneReviewsi PRKAG2.
HGNCi HGNC:9386. PRKAG2.
HPAi CAB018641.
HPA004246.
MIMi 194200. phenotype.
261740. phenotype.
600858. phenotype.
602743. gene.
neXtProti NX_Q9UGJ0.
Orphaneti 155. Familial isolated hypertrophic cardiomyopathy.
907. Wolff-Parkinson-White syndrome.
PharmGKBi PA33752.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0517.
GeneTreei ENSGT00390000009849.
HOVERGENi HBG050431.
KOi K07200.
OMAi GAKQKEN.
OrthoDBi EOG74FF0W.
PhylomeDBi Q9UGJ0.
TreeFami TF313247.

Enzyme and pathway databases

Reactomei REACT_11082. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_1988. AMPK inhibits chREBP transcriptional activation activity.
REACT_200686. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_21285. Regulation of AMPK activity via LKB1.
REACT_21393. Regulation of Rheb GTPase activity by AMPK.
SignaLinki Q9UGJ0.

Miscellaneous databases

ChiTaRSi PRKAG2. human.
GeneWikii PRKAG2.
GenomeRNAii 51422.
NextBioi 54969.
PROi Q9UGJ0.
SOURCEi Search...

Gene expression databases

Bgeei Q9UGJ0.
CleanExi HS_PRKAG2.
ExpressionAtlasi Q9UGJ0. baseline and differential.
Genevestigatori Q9UGJ0.

Family and domain databases

InterProi IPR000644. CBS_dom.
[Graphical view ]
Pfami PF00571. CBS. 3 hits.
[Graphical view ]
SMARTi SM00116. CBS. 4 hits.
[Graphical view ]
PROSITEi PS51371. CBS. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. "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. 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. Cited for: VARIANT WPWS GLN-302.
  19. "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.
  20. "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.

Entry informationi

Entry nameiAAKG2_HUMAN
AccessioniPrimary (citable) accession number: Q9UGJ0
Secondary accession number(s): Q53Y07
, Q6NUI0, Q75MP4, Q9NUZ9, Q9UDN8, Q9ULX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3