ID AAKB2_MOUSE STANDARD; PRT; 271 AA. AC Q6PAM0; DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 07-FEB-2006, entry version 11. DE 5'-AMP-activated protein kinase subunit beta-2 (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 MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). 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 MGI; MGI:1336185; Prkab2. DR GO; GO:0004679; F:AMP-activated protein kinase activity; TAS. DR GO; GO:0006950; P:response to stress; TAS. DR InterPro; IPR006828; AMPKBI. DR Pfam; PF04739; AMPKBI; 1. KW Fatty acid biosynthesis; Lipid synthesis; Phosphorylation. FT CHAIN 1 271 5'-AMP-activated protein kinase subunit FT beta-2. FT /FTId=PRO_0000204369. 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 //