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 05-MAY-2009, entry version 37. DE RecName: Full=5'-AMP-activated protein kinase subunit beta-2; DE Short=AMPK beta-2 chain; 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. 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). CC -!- FUNCTION: AMPK is responsible for the regulation of fatty acid CC synthesis by phosphorylation of acetyl-CoA carboxylase. Also CC regulates cholesterol synthesis via phosphorylation and CC inactivation of hydroxymethylglutaryl-CoA reductase and hormone- CC sensitive lipase. This is a regulatory subunit, may be a positive CC regulator of AMPK activity. It may also serve as an adapter CC molecule for the catalytic alpha-subunit (By similarity). CC -!- SUBUNIT: Heterotrimer of an alpha catalytic subunit, a beta and a CC gamma non-catalytic regulatory subunits (By similarity). CC -!- PTM: Phosphorylated when associated with the catalytic subunit (By CC similarity). 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 IPI; IPI00340519; -. DR RefSeq; NP_892042.2; -. DR UniGene; Mm.31175; -. DR SMR; Q6PAM0; 74-162. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR PhosphoSite; Q6PAM0; -. DR PRIDE; Q6PAM0; -. DR Ensembl; ENSMUSG00000038205; Mus musculus. DR GeneID; 108097; -. DR KEGG; mmu:108097; -. DR MGI; MGI:1336185; Prkab2. DR HOGENOM; Q6PAM0; -. DR HOVERGEN; Q6PAM0; -. DR OMA; Q6PAM0; VKPTQQA. DR NextBio; 360054; -. DR ArrayExpress; Q6PAM0; -. DR Bgee; Q6PAM0; -. DR GermOnline; ENSMUSG00000038205; Mus musculus. 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 GO; GO:0006950; P:response to stress; TAS:MGI. DR InterPro; IPR006828; AMPKBI. DR Pfam; PF04739; AMPKBI; 1. PE 2: Evidence at transcript level; KW Fatty acid biosynthesis; Lipid synthesis; Phosphoprotein. FT CHAIN 1 271 5'-AMP-activated protein kinase subunit FT beta-2. FT /FTId=PRO_0000204369. FT MOD_RES 107 107 Phosphoserine (By similarity). FT MOD_RES 182 182 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 //