AAKB2_MOUSE
ID AAKB2_MOUSE Reviewed; 271 AA.
AC Q6PAM0;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=5'-AMP-activated protein kinase subunit beta-2;
DE Short=AMPK subunit beta-2;
GN Name=Prkab2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [3]
RP PHOSPHORYLATION BY ULK1 AND ULK2.
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).
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). {ECO:0000250}.
CC -!- PTM: Phosphorylated when associated with the catalytic subunit (PRKAA1
CC or PRKAA2). Phosphorylated by ULK1 and ULK2; leading to negatively
CC regulate AMPK activity and suggesting the existence of a regulatory
CC feedback loop between ULK1, ULK2 and AMPK.
CC {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; BC060228; AAH60228.1; -; mRNA.
DR CCDS; CCDS17657.1; -.
DR RefSeq; NP_892042.2; NM_182997.2.
DR RefSeq; XP_006500903.1; XM_006500840.1.
DR RefSeq; XP_011238284.1; XM_011239982.2.
DR AlphaFoldDB; Q6PAM0; -.
DR BMRB; Q6PAM0; -.
DR SMR; Q6PAM0; -.
DR BioGRID; 223830; 1.
DR ComplexPortal; CPX-5851; AMPK complex, alpha2-beta2-gamma1 variant.
DR ComplexPortal; CPX-5853; AMPK complex, alpha1-beta2-gamma1 variant.
DR ComplexPortal; CPX-5854; AMPK complex, alpha2-beta2-gamma3 variant.
DR ComplexPortal; CPX-5855; AMPK complex, alpha1-beta2-gamma3 variant.
DR ComplexPortal; CPX-5859; AMPK complex, alpha2-beta2-gamma2 variant.
DR ComplexPortal; CPX-5860; AMPK complex, alpha1-beta2-gamma2 variant.
DR CORUM; Q6PAM0; -.
DR STRING; 10090.ENSMUSP00000036410; -.
DR BindingDB; Q6PAM0; -.
DR ChEMBL; CHEMBL3708161; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR iPTMnet; Q6PAM0; -.
DR PhosphoSitePlus; Q6PAM0; -.
DR jPOST; Q6PAM0; -.
DR MaxQB; Q6PAM0; -.
DR PaxDb; Q6PAM0; -.
DR PeptideAtlas; Q6PAM0; -.
DR PRIDE; Q6PAM0; -.
DR ProteomicsDB; 296464; -.
DR Antibodypedia; 33978; 321 antibodies from 33 providers.
DR DNASU; 108097; -.
DR Ensembl; ENSMUST00000045743; ENSMUSP00000036410; ENSMUSG00000038205.
DR GeneID; 108097; -.
DR KEGG; mmu:108097; -.
DR UCSC; uc008qpb.1; mouse.
DR CTD; 5565; -.
DR MGI; MGI:1336185; Prkab2.
DR VEuPathDB; HostDB:ENSMUSG00000038205; -.
DR eggNOG; KOG1616; Eukaryota.
DR GeneTree; ENSGT00940000159284; -.
DR HOGENOM; CLU_070949_2_0_1; -.
DR InParanoid; Q6PAM0; -.
DR OMA; PPHKPWE; -.
DR OrthoDB; 956412at2759; -.
DR PhylomeDB; Q6PAM0; -.
DR TreeFam; TF313827; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR Reactome; R-MMU-163680; AMPK inhibits chREBP transcriptional activation activity.
DR Reactome; R-MMU-200425; Carnitine metabolism.
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; 108097; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Prkab2; mouse.
DR PRO; PR:Q6PAM0; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q6PAM0; protein.
DR Bgee; ENSMUSG00000038205; Expressed in epithelium of lens and 222 other tissues.
DR ExpressionAtlas; Q6PAM0; baseline and differential.
DR Genevisible; Q6PAM0; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004679; F:AMP-activated protein kinase activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; 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:0120162; P:positive regulation of cold-induced thermogenesis; IGI:YuBioLab.
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:SF83; PTHR10343:SF83; 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; Phosphoprotein; Reference proteome.
FT CHAIN 1..271
FT /note="5'-AMP-activated protein kinase subunit beta-2"
FT /id="PRO_0000204369"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Phosphoserine; by ULK1"
FT /evidence="ECO:0000250|UniProtKB:Q9QZH4"
FT MOD_RES 39
FT /note="Phosphothreonine; by ULK1"
FT /evidence="ECO:0000250|UniProtKB:Q9QZH4"
FT MOD_RES 68
FT /note="Phosphoserine; by ULK1"
FT /evidence="ECO:0000250|UniProtKB:Q9QZH4"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43741"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 147
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43741"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43741"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43741"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZH4"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43741"
SQ SEQUENCE 271 AA; 30209 MW; 883B42716E996BE7 CRC64;
MGNTTSERVS GERHGAKAAR AEGGGHGPGK EHKIMVGSTD DPSVFSLPDS KLPGDKEFVP
WQQDLDDSVK PAQQARPTVI RWSEGGKEVF ISGSFNNWST KIPLIKSHND FVAILDLPEG
EHQYKFFVDG QWVHDPSEPV VTSQLGTINN LIHVKKSDFE VFDALKLDSM ESSETSCRDL
SSSPPGPYGQ EMYVFRSEER FKSPPILPPH LLQVILNKDT NISCDPALLP EPNHVMLNHL
YALSIKDSVM VLSATHRYKK KYVTTLLYKP I
