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P54619

- AAKG1_HUMAN

UniProt

P54619 - AAKG1_HUMAN

Protein

5'-AMP-activated protein kinase subunit gamma-1

Gene

PRKAG1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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 sitei70 – 701AMP 1By similarity
    Binding sitei70 – 701ATP 1By similarity
    Binding sitei151 – 1511AMP 2By similarity
    Binding sitei151 – 1511AMP 3By similarity
    Binding sitei151 – 1511ATP 2By similarity
    Binding sitei152 – 1521ATP 1By similarity
    Binding sitei152 – 1521ATP 2By similarity
    Binding sitei170 – 1701AMP 1By similarity
    Binding sitei170 – 1701ATP 1By similarity
    Binding sitei298 – 2981AMP 3By similarity
    Binding sitei299 – 2991AMP 1By similarity
    Binding sitei299 – 2991ATP 1By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell cycle arrest Source: Reactome
    2. fatty acid biosynthetic process Source: UniProtKB-KW
    3. insulin receptor signaling pathway Source: Reactome
    4. membrane organization Source: Reactome
    5. positive regulation of gene expression Source: UniProtKB
    6. positive regulation of protein kinase activity Source: BHF-UCL
    7. protein heterooligomerization Source: Ensembl
    8. protein phosphorylation Source: UniProtKB
    9. regulation of glycolytic process Source: BHF-UCL
    10. signal transduction Source: ProtInc
    11. spermatogenesis Source: ProtInc

    Keywords - Biological processi

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

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
    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.
    SignaLinkiP54619.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    5'-AMP-activated protein kinase subunit gamma-1
    Short name:
    AMPK gamma1
    Short name:
    AMPK subunit gamma-1
    Short name:
    AMPKg
    Gene namesi
    Name:PRKAG1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:9385. PRKAG1.

    Subcellular locationi

    GO - Cellular componenti

    1. AMP-activated protein kinase complex Source: UniProtKB
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB
    5. nucleus Source: Ensembl

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi90 – 901D → A: Reduced AMP-activation of phosphorylation of PRKAA1 or PRKAA2. Reduced ADP activation of phosphorylation of PRKAA1 or PRKAA2. 1 Publication
    Mutagenesisi245 – 2451D → A: Reduced AMP-activation of phosphorylation of PRKAA1 or PRKAA2. Reduced ADP activation of phosphorylation of PRKAA1 or PRKAA2. 1 Publication
    Mutagenesisi317 – 3171D → A: Reduced AMP-activation of phosphorylation of PRKAA1 or PRKAA2. Does not affect ADP activation of phosphorylation of PRKAA1 or PRKAA2. 1 Publication

    Organism-specific databases

    PharmGKBiPA33751.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3313315'-AMP-activated protein kinase subunit gamma-1PRO_0000204377Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei261 – 2611Phosphoserine; by ULK1By similarity
    Modified residuei263 – 2631Phosphothreonine; by ULK1By similarity
    Modified residuei270 – 2701Phosphoserine; by ULK1By similarity

    Post-translational modificationi

    Phosphorylated by ULK1 and ULK2; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1, ULK2 and AMPK.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP54619.
    PaxDbiP54619.
    PRIDEiP54619.

    PTM databases

    PhosphoSiteiP54619.

    Expressioni

    Gene expression databases

    ArrayExpressiP54619.
    BgeeiP54619.
    CleanExiHS_PRKAG1.
    GenevestigatoriP54619.

    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 FNIP2.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRKAB1Q9Y4784EBI-1181439,EBI-719769
    PRKAB2O437413EBI-1181439,EBI-1053424

    Protein-protein interaction databases

    BioGridi111558. 20 interactions.
    IntActiP54619. 19 interactions.
    MINTiMINT-4649712.
    STRINGi9606.ENSP00000323867.

    Structurei

    Secondary structure

    1
    331
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi28 – 336
    Helixi38 – 414
    Beta strandi44 – 529
    Helixi57 – 6610
    Beta strandi72 – 765
    Turni77 – 804
    Beta strandi81 – 866
    Helixi88 – 9710
    Beta strandi102 – 1043
    Helixi107 – 1115
    Helixi114 – 1207
    Helixi138 – 14710
    Beta strandi151 – 1566
    Turni158 – 1603
    Beta strandi163 – 1686
    Helixi169 – 1779
    Turni178 – 1825
    Helixi186 – 1894
    Helixi193 – 1964
    Helixi213 – 22311
    Beta strandi226 – 2316
    Beta strandi235 – 2428
    Helixi243 – 2519
    Helixi262 – 2676
    Helixi271 – 2744
    Beta strandi277 – 2793
    Helixi285 – 29511
    Beta strandi298 – 3036
    Beta strandi307 – 3148
    Helixi315 – 3228

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2UV4X-ray1.33A182-325[»]
    2UV5X-ray1.69A182-325[»]
    2UV6X-ray2.00A182-325[»]
    2UV7X-ray2.00A182-325[»]
    4CFEX-ray3.02E/F1-331[»]
    4CFFX-ray3.92E/F1-331[»]
    ProteinModelPortaliP54619.
    SMRiP54619. Positions 27-325.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54619.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini43 – 10361CBS 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini125 – 18763CBS 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini198 – 26063CBS 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini272 – 32958CBS 4PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi138 – 15922AMPK 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.
    InParanoidiP54619.
    KOiK07200.
    OMAiKGGAYDE.
    PhylomeDBiP54619.
    TreeFamiTF313247.

    Family and domain databases

    InterProiIPR000644. CBS_dom.
    [Graphical view]
    PfamiPF00571. CBS. 4 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 1 (identifier: P54619-1) [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

    METVISSDSS PAVENEHPQE TPESNNSVYT SFMKSHRCYD LIPTSSKLVV    50
    FDTSLQVKKA FFALVTNGVR AAPLWDSKKQ SFVGMLTITD FINILHRYYK 100
    SALVQIYELE EHKIETWREV YLQDSFKPLV CISPNASLFD AVSSLIRNKI 150
    HRLPVIDPES GNTLYILTHK RILKFLKLFI TEFPKPEFMS KSLEELQIGT 200
    YANIAMVRTT TPVYVALGIF VQHRVSALPV VDEKGRVVDI YSKFDVINLA 250
    AEKTYNNLDV SVTKALQHRS HYFEGVLKCY LHETLETIIN RLVEAEVHRL 300
    VVVDENDVVK GIVSLSDILQ ALVLTGGEKK P 331
    Length:331
    Mass (Da):37,579
    Last modified:October 1, 1996 - v1
    Checksum:i0F22B9CA1DBD87AE
    GO
    Isoform 2 (identifier: P54619-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-32: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:299
    Mass (Da):34,084
    Checksum:iA9BA11BA1205419E
    GO
    Isoform 3 (identifier: P54619-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         83-83: V → VVLRALSCPL

    Note: No experimental confirmation available. May be due to competing acceptor splice site.

    Show »
    Length:340
    Mass (Da):38,533
    Checksum:iBCDF1B75723C4321
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti89 – 891T → S.
    Corresponds to variant rs1126930 [ dbSNP | Ensembl ].
    VAR_033453
    Natural varianti329 – 3291K → N.
    Corresponds to variant rs34210356 [ dbSNP | Ensembl ].
    VAR_033454

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3232Missing in isoform 2. 1 PublicationVSP_046711Add
    BLAST
    Alternative sequencei83 – 831V → VVLRALSCPL in isoform 3. 1 PublicationVSP_046712

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U42412 mRNA. Translation: AAC50495.1.
    BT007345 mRNA. Translation: AAP36009.1.
    AK097606 mRNA. Translation: BAC05117.1.
    AK293332 mRNA. Translation: BAG56848.1.
    AC011603 Genomic DNA. No translation available.
    BC000358 mRNA. Translation: AAH00358.1.
    CCDSiCCDS55824.1. [P54619-2]
    CCDS55825.1. [P54619-3]
    CCDS8777.1. [P54619-1]
    RefSeqiNP_001193638.1. NM_001206709.1. [P54619-3]
    NP_001193639.1. NM_001206710.1. [P54619-2]
    NP_002724.1. NM_002733.4. [P54619-1]
    XP_006719562.1. XM_006719499.1. [P54619-2]
    UniGeneiHs.530862.

    Genome annotation databases

    EnsembliENST00000316299; ENSP00000323867; ENSG00000181929. [P54619-3]
    ENST00000548065; ENSP00000447433; ENSG00000181929. [P54619-1]
    ENST00000552212; ENSP00000448972; ENSG00000181929. [P54619-2]
    GeneIDi5571.
    KEGGihsa:5571.
    UCSCiuc001rsy.3. human. [P54619-1]
    uc001rsz.3. human.

    Polymorphism databases

    DMDMi1703037.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U42412 mRNA. Translation: AAC50495.1 .
    BT007345 mRNA. Translation: AAP36009.1 .
    AK097606 mRNA. Translation: BAC05117.1 .
    AK293332 mRNA. Translation: BAG56848.1 .
    AC011603 Genomic DNA. No translation available.
    BC000358 mRNA. Translation: AAH00358.1 .
    CCDSi CCDS55824.1. [P54619-2 ]
    CCDS55825.1. [P54619-3 ]
    CCDS8777.1. [P54619-1 ]
    RefSeqi NP_001193638.1. NM_001206709.1. [P54619-3 ]
    NP_001193639.1. NM_001206710.1. [P54619-2 ]
    NP_002724.1. NM_002733.4. [P54619-1 ]
    XP_006719562.1. XM_006719499.1. [P54619-2 ]
    UniGenei Hs.530862.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2UV4 X-ray 1.33 A 182-325 [» ]
    2UV5 X-ray 1.69 A 182-325 [» ]
    2UV6 X-ray 2.00 A 182-325 [» ]
    2UV7 X-ray 2.00 A 182-325 [» ]
    4CFE X-ray 3.02 E/F 1-331 [» ]
    4CFF X-ray 3.92 E/F 1-331 [» ]
    ProteinModelPortali P54619.
    SMRi P54619. Positions 27-325.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111558. 20 interactions.
    IntActi P54619. 19 interactions.
    MINTi MINT-4649712.
    STRINGi 9606.ENSP00000323867.

    Chemistry

    BindingDBi P54619.
    ChEMBLi CHEMBL2096907.
    DrugBanki DB00945. Acetylsalicylic acid.

    PTM databases

    PhosphoSitei P54619.

    Polymorphism databases

    DMDMi 1703037.

    Proteomic databases

    MaxQBi P54619.
    PaxDbi P54619.
    PRIDEi P54619.

    Protocols and materials databases

    DNASUi 5571.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000316299 ; ENSP00000323867 ; ENSG00000181929 . [P54619-3 ]
    ENST00000548065 ; ENSP00000447433 ; ENSG00000181929 . [P54619-1 ]
    ENST00000552212 ; ENSP00000448972 ; ENSG00000181929 . [P54619-2 ]
    GeneIDi 5571.
    KEGGi hsa:5571.
    UCSCi uc001rsy.3. human. [P54619-1 ]
    uc001rsz.3. human.

    Organism-specific databases

    CTDi 5571.
    GeneCardsi GC12M049396.
    HGNCi HGNC:9385. PRKAG1.
    MIMi 602742. gene.
    neXtProti NX_P54619.
    PharmGKBi PA33751.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0517.
    HOVERGENi HBG050431.
    InParanoidi P54619.
    KOi K07200.
    OMAi KGGAYDE.
    PhylomeDBi P54619.
    TreeFami TF313247.

    Enzyme and pathway databases

    Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.
    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 P54619.

    Miscellaneous databases

    ChiTaRSi PRKAG1. human.
    EvolutionaryTracei P54619.
    GeneWikii PRKAG1.
    GenomeRNAii 5571.
    NextBioi 21596.
    PROi P54619.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54619.
    Bgeei P54619.
    CleanExi HS_PRKAG1.
    Genevestigatori P54619.

    Family and domain databases

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

    Publicationsi

    1. "Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-activated protein kinase."
      Gao G., Fernandez C.S., Stapleton D., Auster A.S., Widmer J., Dyck J.R.B., Kemp B.E., Witters L.A.
      J. Biol. Chem. 271:8675-8681(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
      Tissue: Fetal liver.
    2. "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 1).
    3. "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] (ISOFORMS 2 AND 3).
      Tissue: Glial tumor and Testis.
    4. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Muscle.
    6. "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.
    7. Cited for: INTERACTION WITH FNIP1, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "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.
    9. "Identification and characterization of a novel folliculin-interacting protein FNIP2."
      Hasumi H., Baba M., Hong S.-B., Hasumi Y., Huang Y., Yao M., Valera V.A., Linehan W.M., Schmidt L.S.
      Gene 415:60-67(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FNIP2.
    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. "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 AND ULK2.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "AMPK is a direct adenylate charge-regulated protein kinase."
      Oakhill J.S., Steel R., Chen Z.P., Scott J.W., Ling N., Tam S., Kemp B.E.
      Science 332:1433-1435(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRKAA1 AND PRKAB1, DOMAIN CBS, ADP-BINDING, MUTAGENESIS OF ASP-90; ASP-245 AND ASP-317, FUNCTION.
    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.

    Entry informationi

    Entry nameiAAKG1_HUMAN
    AccessioniPrimary (citable) accession number: P54619
    Secondary accession number(s): B4DDT7, Q8N7V9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 132 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3