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 27-MAR-2024, entry version 141. 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, RC Pancreas, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 2. 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 GlyGen; Q6PAM0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q6PAM0; -. DR PhosphoSitePlus; Q6PAM0; -. DR SwissPalm; Q6PAM0; -. DR jPOST; Q6PAM0; -. DR MaxQB; Q6PAM0; -. DR PaxDb; 10090-ENSMUSP00000036410; -. DR PeptideAtlas; Q6PAM0; -. DR ProteomicsDB; 296464; -. DR Pumba; Q6PAM0; -. DR Antibodypedia; 33978; 347 antibodies from 33 providers. DR DNASU; 108097; -. DR Ensembl; ENSMUST00000045743.13; ENSMUSP00000036410.7; ENSMUSG00000038205.13. DR GeneID; 108097; -. DR KEGG; mmu:108097; -. DR UCSC; uc008qpb.1; mouse. DR AGR; MGI:1336185; -. 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; IPPHKPW; -. DR OrthoDB; 120305at2759; -. 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 82 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 225 other cell types or tissues. DR ExpressionAtlas; Q6PAM0; baseline and differential. 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; TAS: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:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd02859; E_set_AMPKbeta_like_N; 1. DR Gene3D; 6.20.250.60; -; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR032640; AMPK1_CBM. 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; 5'-AMP-ACTIVATED PROTEIN KINASE , BETA SUBUNIT; 1. DR PANTHER; PTHR10343:SF92; 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-2; 1. DR Pfam; PF16561; AMPK1_CBM; 1. DR Pfam; PF04739; AMPKBI; 1. DR SMART; SM01010; AMPKBI; 1. DR SUPFAM; SSF160219; AMPKBI-like; 1. DR SUPFAM; SSF81296; E set domains; 1. DR Genevisible; Q6PAM0; MM. 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 //