AAKB1_MOUSE
ID AAKB1_MOUSE Reviewed; 270 AA.
AC Q9R078; Q91YN6;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=5'-AMP-activated protein kinase subunit beta-1;
DE Short=AMPK subunit beta-1;
DE Short=AMPKb;
GN Name=Prkab1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1;
RA Valentijn L.J., Hoff E.I., Baas F.;
RT "5'-AMP-activated protein kinase subunit beta interacts with the p42
RT subunit of translation initiation factor eIF3.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-108 AND SER-182, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP PHOSPHORYLATION BY ULK1.
RX PubMed=21460634; DOI=10.4161/auto.7.7.15451;
RA Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M.,
RA Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.;
RT "Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory
RT feedback loop.";
RL Autophagy 7:696-706(2011).
RN [7]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-201, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP PHOSPHORYLATION AT SER-108.
RX PubMed=26359501; DOI=10.1074/jbc.m115.678433;
RA Cattin M.E., Wang J., Weldrick J.J., Roeske C.L., Mak E., Thorn S.L.,
RA DaSilva J.N., Wang Y., Lusis A.J., Burgon P.G.;
RT "Deletion of MLIP (muscle-enriched A-type lamin-interacting protein) leads
RT to cardiac hyperactivation of Akt/mammalian target of rapamycin (mTOR) and
RT impaired cardiac adaptation.";
RL J. Biol. Chem. 290:26699-26714(2015).
CC -!- FUNCTION: Non-catalytic subunit of AMP-activated protein kinase (AMPK),
CC an energy sensor protein kinase that plays a key role in regulating
CC cellular energy metabolism. In response to reduction of intracellular
CC ATP levels, AMPK activates energy-producing pathways and inhibits
CC energy-consuming processes: inhibits protein, carbohydrate and lipid
CC biosynthesis, as well as cell growth and proliferation. AMPK acts via
CC direct phosphorylation of metabolic enzymes, and by longer-term effects
CC via phosphorylation of transcription regulators. Also acts as a
CC regulator of cellular polarity by remodeling the actin cytoskeleton;
CC probably by indirectly activating myosin. Beta non-catalytic subunit
CC acts as a scaffold on which the AMPK complex assembles, via its C-
CC terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits
CC (PRKAG1, PRKAG2 or PRKAG3) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1
CC or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic
CC subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with FNIP1 and FNIP2 (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The glycogen-binding domain may target AMPK to glycogen so that
CC other factors like glycogen-bound debranching enzyme or protein
CC phosphatases can directly affect AMPK activity. {ECO:0000250}.
CC -!- PTM: Phosphorylated when associated with the catalytic subunit (PRKAA1
CC or PRKAA2). Phosphorylated by ULK1; leading to negatively regulate AMPK
CC activity and suggesting the existence of a regulatory feedback loop
CC between ULK1 and AMPK. {ECO:0000269|PubMed:21460634}.
CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC family. {ECO:0000305}.
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DR EMBL; AF108215; AAF14222.1; -; mRNA.
DR EMBL; BC016398; AAH16398.1; -; mRNA.
DR CCDS; CCDS19598.1; -.
DR RefSeq; NP_114075.1; NM_031869.2.
DR RefSeq; XP_006530264.1; XM_006530201.1.
DR AlphaFoldDB; Q9R078; -.
DR SMR; Q9R078; -.
DR BioGRID; 202363; 4.
DR ComplexPortal; CPX-5698; AMPK complex, alpha1-beta1-gamma1 variant.
DR ComplexPortal; CPX-5849; AMPK complex, alpha1-beta1-gamma2 variant.
DR ComplexPortal; CPX-5852; AMPK complex, alpha2-beta1-gamma1 variant.
DR ComplexPortal; CPX-5856; AMPK complex, alpha1-beta1-gamma3 variant.
DR ComplexPortal; CPX-5857; AMPK complex, alpha2-beta1-gamma3 variant.
DR ComplexPortal; CPX-5858; AMPK complex, alpha2-beta1-gamma2 variant.
DR CORUM; Q9R078; -.
DR IntAct; Q9R078; 7.
DR MINT; Q9R078; -.
DR STRING; 10090.ENSMUSP00000031486; -.
DR BindingDB; Q9R078; -.
DR ChEMBL; CHEMBL4524004; -.
DR CarbonylDB; Q9R078; -.
DR iPTMnet; Q9R078; -.
DR PhosphoSitePlus; Q9R078; -.
DR EPD; Q9R078; -.
DR jPOST; Q9R078; -.
DR MaxQB; Q9R078; -.
DR PaxDb; Q9R078; -.
DR PRIDE; Q9R078; -.
DR ProteomicsDB; 285894; -.
DR Antibodypedia; 1328; 846 antibodies from 42 providers.
DR DNASU; 19079; -.
DR Ensembl; ENSMUST00000031486; ENSMUSP00000031486; ENSMUSG00000029513.
DR Ensembl; ENSMUST00000111999; ENSMUSP00000107630; ENSMUSG00000029513.
DR GeneID; 19079; -.
DR KEGG; mmu:19079; -.
DR UCSC; uc008zew.1; mouse.
DR CTD; 5564; -.
DR MGI; MGI:1336167; Prkab1.
DR VEuPathDB; HostDB:ENSMUSG00000029513; -.
DR eggNOG; KOG1616; Eukaryota.
DR GeneTree; ENSGT00940000155307; -.
DR HOGENOM; CLU_070949_2_0_1; -.
DR InParanoid; Q9R078; -.
DR OMA; NDRAPTQ; -.
DR OrthoDB; 956412at2759; -.
DR PhylomeDB; Q9R078; -.
DR TreeFam; TF313827; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR Reactome; R-MMU-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR BioGRID-ORCS; 19079; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Prkab1; mouse.
DR PRO; PR:Q9R078; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9R078; protein.
DR Bgee; ENSMUSG00000029513; Expressed in granulocyte and 264 other tissues.
DR ExpressionAtlas; Q9R078; baseline and differential.
DR Genevisible; Q9R078; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0004679; F:AMP-activated protein kinase activity; TAS:MGI.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0031669; P:cellular response to nutrient levels; ISO:MGI.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035878; P:nail development; IMP:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IGI:YuBioLab.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR032640; AMPK1_CBM.
DR InterPro; IPR039160; AMPKB.
DR InterPro; IPR006828; ASC_dom.
DR InterPro; IPR037256; ASC_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR10343:SF89; PTHR10343:SF89; 1.
DR Pfam; PF16561; AMPK1_CBM; 1.
DR Pfam; PF04739; AMPKBI; 1.
DR SMART; SM01010; AMPKBI; 1.
DR SUPFAM; SSF160219; SSF160219; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Lipoprotein; Myristate; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y478"
FT CHAIN 2..270
FT /note="5'-AMP-activated protein kinase subunit beta-1"
FT /id="PRO_0000204364"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..163
FT /note="Glycogen-binding domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 11..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y478"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y478"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y478"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y478"
FT MOD_RES 24
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P80386"
FT MOD_RES 25
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P80386"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y478"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P80386"
FT MOD_RES 108
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:26359501,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 148
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y478"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 201
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 270 AA; 30308 MW; 6B520A95A0A844E5 CRC64;
MGNTSSERAA LERQAGHKTP RRDSSGGAKD GDRPKILMDS PEDADIFHSE EIKAPEKEEF
LAWQHDLEAN DKAPAQARPT VFRWTGGGKE VYLSGSFNNW SKLPLTRSQN NFVAILDLPE
GEHQYKFFVD GQWTHDPSEP IVTSQLGTVN NIIQVKKTDF EVFDALMVDS QKCSDVSELS
SSPPGPYHQE PYMSKPEERF KAPPILPPHL LQVILNKDTG ISCDPALLPE PNHVMLNHLY
ALSIKDGVMV LSATHRYKKK YVTTLLYKPI
