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 19-MAR-2014, entry version 75. 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; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; 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 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). 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) (By similarity). 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 -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta CC subunit family. 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 RefSeq; NP_892042.2; NM_182997.2. DR RefSeq; XP_006500903.1; XM_006500840.1. DR UniGene; Mm.31175; -. DR ProteinModelPortal; Q6PAM0; -. DR SMR; Q6PAM0; 74-271. DR IntAct; Q6PAM0; 1. DR MINT; MINT-4086434; -. DR STRING; 10090.ENSMUSP00000036410; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR PhosphoSite; Q6PAM0; -. DR PaxDb; 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; NOG238368; -. DR GeneTree; ENSGT00390000001416; -. DR HOGENOM; HOG000230597; -. DR HOVERGEN; HBG050430; -. DR InParanoid; Q6PAM0; -. DR KO; K07199; -. DR OMA; SGIYHYK; -. DR TreeFam; TF313827; -. DR Reactome; REACT_147847; Translocation of Glut4 to the Plasma Membrane. DR ChiTaRS; PRKAB2; mouse. DR NextBio; 360054; -. DR PRO; PR:Q6PAM0; -. DR ArrayExpress; Q6PAM0; -. DR Bgee; Q6PAM0; -. DR Genevestigator; Q6PAM0; -. DR GO; GO:0031588; C:AMP-activated protein kinase complex; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0004679; F:AMP-activated protein kinase activity; TAS:MGI. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR006828; AMP_prot_kin_bsu_interact-dom. DR InterPro; IPR014756; Ig_E-set. DR Pfam; PF04739; AMPKBI; 1. DR SMART; SM01010; AMPKBI; 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 (By similarity). FT MOD_RES 39 39 Phosphothreonine; by ULK1 (By FT similarity). FT MOD_RES 68 68 Phosphoserine; by ULK1 (By similarity). FT MOD_RES 107 107 Phosphoserine (By similarity). FT MOD_RES 173 173 Phosphoserine (By similarity). FT MOD_RES 183 183 Phosphoserine (By similarity). 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 //