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 28-FEB-2018, entry version 111. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND IDENTIFICATION RP BY 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 RT 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 RT regulatory feedback loop."; RL Autophagy 7:696-706(2011). CC -!- FUNCTION: Non-catalytic subunit of AMP-activated protein kinase CC (AMPK), an energy sensor protein kinase that plays a key role in CC regulating cellular energy metabolism. In response to reduction of CC intracellular ATP levels, AMPK activates energy-producing pathways CC and inhibits energy-consuming processes: inhibits protein, CC carbohydrate and lipid biosynthesis, as well as cell growth and CC proliferation. AMPK acts via direct phosphorylation of metabolic CC enzymes, and by longer-term effects via phosphorylation of CC transcription regulators. Also acts as a regulator of cellular CC polarity by remodeling the actin cytoskeleton; probably by CC indirectly activating myosin. Beta non-catalytic subunit acts as a CC scaffold on which the AMPK complex assembles, via its C-terminus CC that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, CC PRKAG2 or PRKAG3) (By similarity). {ECO:0000250}. CC -!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit CC (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non- CC catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). {ECO:0000250}. CC -!- PTM: Phosphorylated when associated with the catalytic subunit CC (PRKAA1 or PRKAA2). Phosphorylated by ULK1 and ULK2; leading to CC negatively regulate AMPK activity and suggesting the existence of CC a regulatory feedback loop between ULK1, ULK2 and AMPK. CC {ECO:0000269|PubMed:21460634}. CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta CC subunit 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 UniGene; Mm.31175; -. DR ProteinModelPortal; Q6PAM0; -. DR SMR; Q6PAM0; -. DR CORUM; Q6PAM0; -. DR IntAct; Q6PAM0; 1. DR MINT; Q6PAM0; -. DR STRING; 10090.ENSMUSP00000036410; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR iPTMnet; Q6PAM0; -. DR PhosphoSitePlus; Q6PAM0; -. DR MaxQB; Q6PAM0; -. DR PaxDb; Q6PAM0; -. DR PeptideAtlas; Q6PAM0; -. DR PRIDE; Q6PAM0; -. 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 eggNOG; KOG1616; Eukaryota. DR eggNOG; ENOG410XRB3; LUCA. DR GeneTree; ENSGT00390000001416; -. DR HOGENOM; HOG000230597; -. DR HOVERGEN; HBG050430; -. DR InParanoid; Q6PAM0; -. DR KO; K07199; -. DR OMA; QMGTINN; -. DR OrthoDB; EOG091G0DZR; -. 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; Import of palmitoyl-CoA into the mitochondrial matrix. 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 ChiTaRS; Prkab2; mouse. DR PRO; PR:Q6PAM0; -. DR Proteomes; UP000000589; Chromosome 3. DR Bgee; ENSMUSG00000038205; -. DR ExpressionAtlas; Q6PAM0; baseline and differential. DR Genevisible; Q6PAM0; MM. 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:0004679; F:AMP-activated protein kinase activity; TAS:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 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 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 Complete proteome; Fatty acid biosynthesis; Fatty acid metabolism; KW Lipid biosynthesis; Lipid metabolism; Phosphoprotein; KW Reference proteome. FT CHAIN 1 271 5'-AMP-activated protein kinase subunit FT beta-2. FT /FTId=PRO_0000204369. FT MOD_RES 38 38 Phosphoserine; by ULK1. FT {ECO:0000250|UniProtKB:O43741}. FT MOD_RES 39 39 Phosphothreonine; by ULK1. FT {ECO:0000250|UniProtKB:O43741}. FT MOD_RES 68 68 Phosphoserine; by ULK1. FT {ECO:0000250|UniProtKB:Q9QZH4}. FT MOD_RES 94 94 Phosphoserine. FT {ECO:0000250|UniProtKB:O43741}. FT MOD_RES 107 107 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 147 147 Phosphothreonine. FT {ECO:0000250|UniProtKB:O43741}. FT MOD_RES 157 157 Phosphoserine. FT {ECO:0000250|UniProtKB:O43741}. FT MOD_RES 169 169 Phosphoserine. FT {ECO:0000250|UniProtKB:O43741}. FT MOD_RES 173 173 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9QZH4}. FT MOD_RES 183 183 Phosphoserine. FT {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 //