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Q9Y478

- AAKB1_HUMAN

UniProt

Q9Y478 - AAKB1_HUMAN

Protein

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

Gene

PRKAB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Non-catalytic 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. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein kinase activity Source: UniProtKB

    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. protein heterooligomerization Source: Ensembl
    7. protein phosphorylation Source: UniProtKB
    8. regulation of catalytic activity Source: Ensembl
    9. signal transduction Source: ProtInc

    Keywords - Biological processi

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

    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.
    SignaLinkiQ9Y478.

    Protein family/group databases

    CAZyiCBM48. Carbohydrate-Binding Module Family 48.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    5'-AMP-activated protein kinase subunit beta-1
    Short name:
    AMPK subunit beta-1
    Short name:
    AMPKb
    Gene namesi
    Name:PRKAB1
    Synonyms:AMPK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:9378. PRKAB1.

    Subcellular locationi

    GO - Cellular componenti

    1. AMP-activated protein kinase complex Source: Ensembl
    2. cytosol Source: Reactome
    3. nucleus Source: Ensembl

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21G → A: Abolishes myristoylation and AMP-enhanced phosphorylation of PRKAA1 or PRKAA2. 1 Publication

    Organism-specific databases

    PharmGKBiPA33746.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 2702695'-AMP-activated protein kinase subunit beta-1PRO_0000204363Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication
    Modified residuei4 – 41Phosphothreonine2 Publications
    Modified residuei5 – 51Phosphoserine2 Publications
    Modified residuei6 – 61Phosphoserine2 Publications
    Modified residuei19 – 191Phosphothreonine3 Publications
    Modified residuei24 – 241Phosphoserine; by autocatalysisBy similarity
    Modified residuei25 – 251Phosphoserine; by autocatalysisBy similarity
    Modified residuei40 – 401Phosphoserine4 Publications
    Modified residuei96 – 961Phosphoserine2 Publications
    Modified residuei101 – 1011PhosphoserineBy similarity
    Modified residuei108 – 1081Phosphoserine8 Publications
    Modified residuei148 – 1481Phosphothreonine2 Publications
    Modified residuei182 – 1821PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated when associated with the catalytic subunit (PRKAA1 or PRKAA2). Phosphorylated by ULK1; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1 and AMPK.8 Publications

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y478.
    PaxDbiQ9Y478.
    PRIDEiQ9Y478.

    PTM databases

    PhosphoSiteiQ9Y478.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y478.
    BgeeiQ9Y478.
    CleanExiHS_PRKAB1.
    GenevestigatoriQ9Y478.

    Organism-specific databases

    HPAiCAB005058.
    HPA004247.

    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
    CideaO703024EBI-719769,EBI-7927848From a different organism.
    GRB2P629932EBI-719769,EBI-401755
    PRKAA1Q131315EBI-719769,EBI-1181405
    PRKAG1P546194EBI-719769,EBI-1181439

    Protein-protein interaction databases

    BioGridi111551. 28 interactions.
    IntActiQ9Y478. 16 interactions.
    MINTiMINT-1400840.
    STRINGi9606.ENSP00000229328.

    Structurei

    Secondary structure

    1
    270
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi79 – 846
    Beta strandi91 – 955
    Turni96 – 1005
    Beta strandi112 – 1176
    Beta strandi120 – 12910
    Beta strandi132 – 1343
    Beta strandi141 – 1433
    Beta strandi145 – 1473
    Beta strandi149 – 1557
    Helixi157 – 1604
    Helixi162 – 17110
    Helixi208 – 2114
    Helixi214 – 2163
    Beta strandi238 – 2414
    Beta strandi248 – 25710
    Beta strandi260 – 26910

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4CFEX-ray3.02B/D1-270[»]
    4CFFX-ray3.92B/D1-270[»]
    ProteinModelPortaliQ9Y478.
    SMRiQ9Y478. Positions 77-270.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni68 – 16396Glycogen-binding domainBy similarityAdd
    BLAST

    Domaini

    The glycogen-binding domain may target AMPK to glycogen so that other factors like glycogen-bound debranching enzyme or protein phosphatases can directly affect AMPK activity.By similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG238368.
    HOGENOMiHOG000230597.
    HOVERGENiHBG050430.
    InParanoidiQ9Y478.
    KOiK07199.
    OMAiCKAEERF.
    OrthoDBiEOG7SXW3Z.
    PhylomeDBiQ9Y478.
    TreeFamiTF313827.

    Family and domain databases

    InterProiIPR006828. AMP_prot_kin_bsu_interact-dom.
    IPR014756. Ig_E-set.
    [Graphical view]
    PfamiPF04739. AMPKBI. 1 hit.
    [Graphical view]
    SMARTiSM01010. AMPKBI. 1 hit.
    [Graphical view]
    SUPFAMiSSF81296. SSF81296. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9Y478-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGNTSSERAA LERHGGHKTP RRDSSGGTKD GDRPKILMDS PEDADLFHSE    50
    EIKAPEKEEF LAWQHDLEVN DKAPAQARPT VFRWTGGGKE VYLSGSFNNW 100
    SKLPLTRSHN NFVAILDLPE GEHQYKFFVD GQWTHDPSEP IVTSQLGTVN 150
    NIIQVKKTDF EVFDALMVDS QKCSDVSELS SSPPGPYHQE PYVCKPEERF 200
    RAPPILPPHL LQVILNKDTG ISCDPALLPE PNHVMLNHLY ALSIKDGVMV 250
    LSATHRYKKK YVTTLLYKPI 270
    Length:270
    Mass (Da):30,382
    Last modified:January 23, 2007 - v4
    Checksum:iF0BCAA94D5BC15FC
    GO

    Sequence cautioni

    The sequence AAC98897.1 differs from that shown. Reason: Frameshift at position 245.
    The sequence AAB71326.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101A → G in CAA73146. (PubMed:9224708)Curated
    Sequence conflicti10 – 101A → G in AAC98897. 1 PublicationCurated
    Sequence conflicti15 – 151G → A in CAA12024. 1 PublicationCurated
    Sequence conflicti20 – 201P → A in CAA73146. (PubMed:9224708)Curated
    Sequence conflicti20 – 201P → A in AAC98897. 1 PublicationCurated
    Sequence conflicti22 – 221R → K in AAD09237. 1 PublicationCurated
    Sequence conflicti22 – 221R → K in AAD00625. 1 PublicationCurated
    Sequence conflicti56 – 561E → Y in AAD09237. 1 PublicationCurated
    Sequence conflicti56 – 561E → Y in AAD00625. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ224515 mRNA. Translation: CAA12024.1.
    Y12556 mRNA. Translation: CAA73146.1.
    U83994 mRNA. Translation: AAD09237.1.
    U87276
    , U87271, U87272, U87273, U87274, U87275 Genomic DNA. Translation: AAD00625.1.
    AF022116 mRNA. Translation: AAC98897.1. Frameshift.
    AC002563 Genomic DNA. Translation: AAB71326.1. Sequence problems.
    BC001007 mRNA. Translation: AAH01007.1.
    BC001056 mRNA. Translation: AAH01056.1.
    BC001823 mRNA. Translation: AAH01823.1.
    BC017671 mRNA. Translation: AAH17671.1.
    CCDSiCCDS9191.1.
    PIRiT09514.
    RefSeqiNP_006244.2. NM_006253.4.
    XP_005253966.1. XM_005253909.1.
    UniGeneiHs.741184.

    Genome annotation databases

    EnsembliENST00000229328; ENSP00000229328; ENSG00000111725.
    ENST00000541640; ENSP00000441369; ENSG00000111725.
    GeneIDi5564.
    KEGGihsa:5564.
    UCSCiuc001txg.3. human.

    Polymorphism databases

    DMDMi14194425.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ224515 mRNA. Translation: CAA12024.1 .
    Y12556 mRNA. Translation: CAA73146.1 .
    U83994 mRNA. Translation: AAD09237.1 .
    U87276
    , U87271 , U87272 , U87273 , U87274 , U87275 Genomic DNA. Translation: AAD00625.1 .
    AF022116 mRNA. Translation: AAC98897.1 . Frameshift.
    AC002563 Genomic DNA. Translation: AAB71326.1 . Sequence problems.
    BC001007 mRNA. Translation: AAH01007.1 .
    BC001056 mRNA. Translation: AAH01056.1 .
    BC001823 mRNA. Translation: AAH01823.1 .
    BC017671 mRNA. Translation: AAH17671.1 .
    CCDSi CCDS9191.1.
    PIRi T09514.
    RefSeqi NP_006244.2. NM_006253.4.
    XP_005253966.1. XM_005253909.1.
    UniGenei Hs.741184.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4CFE X-ray 3.02 B/D 1-270 [» ]
    4CFF X-ray 3.92 B/D 1-270 [» ]
    ProteinModelPortali Q9Y478.
    SMRi Q9Y478. Positions 77-270.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111551. 28 interactions.
    IntActi Q9Y478. 16 interactions.
    MINTi MINT-1400840.
    STRINGi 9606.ENSP00000229328.

    Chemistry

    BindingDBi Q9Y478.
    ChEMBLi CHEMBL2111345.
    DrugBanki DB00945. Acetylsalicylic acid.
    DB00131. Adenosine monophosphate.
    DB00331. Metformin.

    Protein family/group databases

    CAZyi CBM48. Carbohydrate-Binding Module Family 48.

    PTM databases

    PhosphoSitei Q9Y478.

    Polymorphism databases

    DMDMi 14194425.

    Proteomic databases

    MaxQBi Q9Y478.
    PaxDbi Q9Y478.
    PRIDEi Q9Y478.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000229328 ; ENSP00000229328 ; ENSG00000111725 .
    ENST00000541640 ; ENSP00000441369 ; ENSG00000111725 .
    GeneIDi 5564.
    KEGGi hsa:5564.
    UCSCi uc001txg.3. human.

    Organism-specific databases

    CTDi 5564.
    GeneCardsi GC12P120105.
    HGNCi HGNC:9378. PRKAB1.
    HPAi CAB005058.
    HPA004247.
    MIMi 602740. gene.
    neXtProti NX_Q9Y478.
    PharmGKBi PA33746.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG238368.
    HOGENOMi HOG000230597.
    HOVERGENi HBG050430.
    InParanoidi Q9Y478.
    KOi K07199.
    OMAi CKAEERF.
    OrthoDBi EOG7SXW3Z.
    PhylomeDBi Q9Y478.
    TreeFami TF313827.

    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 Q9Y478.

    Miscellaneous databases

    GeneWikii PRKAB1.
    GenomeRNAii 5564.
    NextBioi 21556.
    PROi Q9Y478.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y478.
    Bgeei Q9Y478.
    CleanExi HS_PRKAB1.
    Genevestigatori Q9Y478.

    Family and domain databases

    InterProi IPR006828. AMP_prot_kin_bsu_interact-dom.
    IPR014756. Ig_E-set.
    [Graphical view ]
    Pfami PF04739. AMPKBI. 1 hit.
    [Graphical view ]
    SMARTi SM01010. AMPKBI. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81296. SSF81296. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Non-catalytic beta and gamma subunits isoforms of the AMP-activated protein kinase."
      Carling D.
      Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "AMP-activated protein kinase isoenzyme family: subunit structure and chromosomal location."
      Stapleton D., Woollatt E., Mitchelhill K., Nicholl J.K., Fernandez C.S., Michell B.J., Witters L.A., Power D.A., Sutherland G.R., Kemp B.E.
      FEBS Lett. 409:452-456(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    3. "Transcription map of the 5cM region surrounding the hepatocyte nuclear factor-1a/MODY3 gene on chromosome 12."
      Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V., Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M., Lathrop M., Cox R.D., Bell G.I.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    4. "Cloning and expression of the complete mRNA coding human AMP-activated protein kinase."
      Wang X., Yu L., Tu Q.
      Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "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].
    6. "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].
      Tissue: Lung and Muscle.
    7. Cited for: INTERACTION WITH FNIP1.
    8. "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.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4; SER-5; SER-6 AND SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-40 AND SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-40; SER-108 AND THR-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 AND SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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 PRKAG1, MUTAGENESIS OF GLY-2, MYRISTOYLATION AT GLY-2.
    19. "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.
    20. "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 nameiAAKB1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y478
    Secondary accession number(s): Q9UBV0
    , Q9UE20, Q9UEX2, Q9Y6V8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 142 of the entry and version 4 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, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3