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Q9QZH4

- AAKB2_RAT

UniProt

Q9QZH4 - AAKB2_RAT

Protein

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

Gene

Prkab2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      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) By similarity.By similarity

    GO - Molecular functioni

    1. protein kinase binding Source: RGD

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB-KW
    2. protein phosphorylation Source: GOC

    Keywords - Biological processi

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

    Protein family/group databases

    CAZyiCBM48. Carbohydrate-Binding Module Family 48.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    5'-AMP-activated protein kinase subunit beta-2
    Short name:
    AMPK subunit beta-2
    Gene namesi
    Name:Prkab2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi620905. Prkab2.

    Subcellular locationi

    GO - Cellular componenti

    1. AMP-activated protein kinase complex Source: RGD
    2. apical plasma membrane Source: UniProtKB
    3. cAMP-dependent protein kinase complex Source: RGD
    4. cytoplasm Source: UniProtKB
    5. nucleoplasm Source: Reactome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2712715'-AMP-activated protein kinase subunit beta-2PRO_0000204370Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei38 – 381Phosphoserine; by ULK11 Publication
    Modified residuei39 – 391Phosphothreonine; by ULK11 Publication
    Modified residuei68 – 681Phosphoserine; by ULK11 Publication
    Modified residuei107 – 1071PhosphoserineBy similarity
    Modified residuei173 – 1731Phosphoserine; by ULK11 Publication
    Modified residuei183 – 1831Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated when associated with the catalytic subunit (PRKAA1 or PRKAA2). 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.2 Publications

    Keywords - PTMi

    Phosphoprotein

    PTM databases

    PhosphoSiteiQ9QZH4.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9QZH4.

    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).By similarity

    Structurei

    Secondary structure

    1
    271
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi73 – 753
    Beta strandi80 – 823
    Beta strandi89 – 935
    Helixi94 – 963
    Beta strandi111 – 1133
    Beta strandi119 – 1224
    Beta strandi124 – 1285
    Beta strandi131 – 1333
    Beta strandi136 – 1383
    Beta strandi140 – 1423
    Beta strandi152 – 1543
    Beta strandi157 – 1604

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LU3NMR-A67-163[»]
    2LU4NMR-A67-163[»]
    ProteinModelPortaliQ9QZH4.
    SMRiQ9QZH4. Positions 74-162, 189-271.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG238368.
    HOGENOMiHOG000230597.
    HOVERGENiHBG050430.
    InParanoidiQ9QZH4.
    KOiK07199.
    PhylomeDBiQ9QZH4.

    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.

    Q9QZH4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGNTTSERVS GERHGAKAAR AEGGGHGPGK EHKIMVGSTD DPSVFSLPDS    50
    KLPGDKEFVP WQQDLDDSVK PTQQARPTVI RWSEGGKEVF ISGSFNNWST 100
    KIPLIKSHND FVAILDLPEG EHQYKFFVDG QWVHDPSEPV VTSQLGTINN 150
    LIHVKKSDFE VFDALKLDSM ESSETSCRDL SSSPPGPYGQ EMYVFRSEER 200
    FKSPPILPPH LLQVILNKDT NISCDPALLP EPNHVMLNHL YALSTKDSVM 250
    VLSATHRYKK KYVTTLLYKP I 271
    Length:271
    Mass (Da):30,227
    Last modified:May 1, 2000 - v1
    Checksum:iD881451A03287BEA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF182717 mRNA. Translation: AAF01293.1.
    RefSeqiNP_072149.1. NM_022627.2.
    UniGeneiRn.207202.

    Genome annotation databases

    GeneIDi64562.
    KEGGirno:64562.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF182717 mRNA. Translation: AAF01293.1 .
    RefSeqi NP_072149.1. NM_022627.2.
    UniGenei Rn.207202.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LU3 NMR - A 67-163 [» ]
    2LU4 NMR - A 67-163 [» ]
    ProteinModelPortali Q9QZH4.
    SMRi Q9QZH4. Positions 74-162, 189-271.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM48. Carbohydrate-Binding Module Family 48.

    PTM databases

    PhosphoSitei Q9QZH4.

    Protocols and materials databases

    DNASUi 64562.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 64562.
    KEGGi rno:64562.

    Organism-specific databases

    CTDi 5565.
    RGDi 620905. Prkab2.

    Phylogenomic databases

    eggNOGi NOG238368.
    HOGENOMi HOG000230597.
    HOVERGENi HBG050430.
    InParanoidi Q9QZH4.
    KOi K07199.
    PhylomeDBi Q9QZH4.

    Miscellaneous databases

    NextBioi 613490.
    PROi Q9QZH4.

    Gene expression databases

    Genevestigatori Q9QZH4.

    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. "Expression of the AMP-activated protein kinase beta1 and beta2 subunits in skeletal muscle."
      Chen Z., Heierhorst J., Mann R.J., Mitchelhill K.I., Michell B.J., Witters L.A., Lynch G.S., Kemp B.E., Stapleton D.
      FEBS Lett. 460:343-348(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-183.
      Strain: Sprague-Dawley.
      Tissue: Skeletal muscle.
    2. "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, PHOSPHORYLATION AT SER-38; THR-39; SER-68 AND SER-173.

    Entry informationi

    Entry nameiAAKB2_RAT
    AccessioniPrimary (citable) accession number: Q9QZH4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 90 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3