Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9UGJ0

- AAKG2_HUMAN

UniProt

Q9UGJ0 - AAKG2_HUMAN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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

    ArrayExpressiQ9UGJ0.
    BgeeiQ9UGJ0.
    CleanExiHS_PRKAG2.
    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. 19 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.
    HOVERGENiHBG050431.
    InParanoidiQ9UGJ0.
    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

    MGSAVMDTKK KKDVSSPGGS GGKKNASQKR RSLRVHIPDL SSFAMPLLDG    50
    DLEGSGKHSS RKVDSPFGPG SPSKGFFSRG PQPRPSSPMS APVRPKTSPG 100
    SPKTVFPFSY QESPPRSPRR MSFSGIFRSS SKESSPNSNP ATSPGGIRFF 150
    SRSRKTSGLS SSPSTPTQVT KQHTFPLESY KHEPERLENR IYASSSPPDT 200
    GQRFCPSSFQ SPTRPPLASP THYAPSKAAA LAAALGPAEA GMLEKLEFED 250
    EAVEDSESGV YMRFMRSHKC YDIVPTSSKL VVFDTTLQVK KAFFALVANG 300
    VRAAPLWESK KQSFVGMLTI TDFINILHRY YKSPMVQIYE LEEHKIETWR 350
    ELYLQETFKP LVNISPDASL FDAVYSLIKN KIHRLPVIDP ISGNALYILT 400
    HKRILKFLQL FMSDMPKPAF MKQNLDELGI GTYHNIAFIH PDTPIIKALN 450
    IFVERRISAL PVVDESGKVV DIYSKFDVIN LAAEKTYNNL DITVTQALQH 500
    RSQYFEGVVK CNKLEILETI VDRIVRAEVH RLVVVNEADS IVGIISLSDI 550
    LQALILTPAG AKQKETETE 569
    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. 19 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.
    HOVERGENi HBG050431.
    InParanoidi Q9UGJ0.
    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

    ArrayExpressi Q9UGJ0.
    Bgeei Q9UGJ0.
    CleanExi HS_PRKAG2.
    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

    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 1, 2014
    This is version 135 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