ID AAKG2_MOUSE Reviewed; 566 AA. AC Q91WG5; Q6V7V5; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 01-SEP-2009, entry version 48. DE RecName: Full=5'-AMP-activated protein kinase subunit gamma-2; DE Short=AMPK gamma-2 chain; DE Short=AMPK gamma2; GN Name=Prkag2; 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 [MRNA] (ISOFORM B). RC STRAIN=C57BL/6J; RA Zhou G., Jiang D., Zhang Y.; RT "Cloning of mouse protein kinase, AMP-activated, gamma 2 non-catalytic RT subunit."; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RC STRAIN=FVB/N; TISSUE=Kidney; 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 [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND MASS RP SPECTROMETRY. RC TISSUE=Brain cortex; RX PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200; RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., RA Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; RT "Qualitative and quantitative analyses of protein phosphorylation in RT naive and stimulated mouse synaptosomal preparations."; RL Mol. Cell. Proteomics 6:283-293(2007). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-71; SER-73; RP SER-90; SER-138; SER-158; SER-161 AND SER-162, AND MASS SPECTROMETRY. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). 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 (By similarity). CC -!- SUBUNIT: Heterotrimer of an alpha catalytic subunit, a beta and a CC gamma non-catalytic regulatory subunits (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=Q91WG5-1; Sequence=Displayed; CC Name=B; CC IsoId=Q91WG5-2; Sequence=VSP_015586; CC -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By CC similarity). CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase gamma CC subunit family. CC -!- SIMILARITY: Contains 4 CBS domains. 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; AY348864; AAQ55224.1; -; mRNA. DR EMBL; BC015283; AAH15283.1; -; mRNA. DR IPI; IPI00128126; -. DR IPI; IPI00649331; -. DR RefSeq; NP_663376.1; -. DR UniGene; Mm.33649; -. DR UniGene; Mm.442668; -. DR STRING; Q91WG5; -. DR PhosphoSite; Q91WG5; -. DR PRIDE; Q91WG5; -. DR Ensembl; ENSMUST00000030784; ENSMUSP00000030784; ENSMUSG00000028944; Mus musculus. DR GeneID; 108099; -. DR KEGG; mmu:108099; -. DR UCSC; uc008wsm.1; mouse. DR CTD; 108099; -. DR MGI; MGI:1336153; Prkag2. DR HOGENOM; Q91WG5; -. DR HOVERGEN; Q91WG5; -. DR NextBio; 360062; -. DR ArrayExpress; Q91WG5; -. DR Bgee; Q91WG5; -. DR GermOnline; ENSMUSG00000028944; 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; IPR000644; Cysta_beta_synth_core. DR Pfam; PF00571; CBS; 2. DR SMART; SM00116; CBS; 4. DR PROSITE; PS51371; CBS; 4. PE 1: Evidence at protein level; KW Alternative splicing; CBS domain; Fatty acid biosynthesis; KW Lipid synthesis; Phosphoprotein; Repeat. FT CHAIN 1 566 5'-AMP-activated protein kinase subunit FT gamma-2. FT /FTId=PRO_0000204382. FT DOMAIN 272 332 CBS 1. FT DOMAIN 354 412 CBS 2. FT DOMAIN 427 489 CBS 3. FT DOMAIN 501 559 CBS 4. FT MOD_RES 65 65 Phosphoserine. FT MOD_RES 71 71 Phosphoserine. FT MOD_RES 73 73 Phosphoserine. FT MOD_RES 90 90 Phosphoserine. FT MOD_RES 138 138 Phosphoserine. FT MOD_RES 143 143 Phosphoserine (By similarity). FT MOD_RES 157 157 Phosphoserine (By similarity). FT MOD_RES 158 158 Phosphoserine. FT MOD_RES 161 161 Phosphoserine. FT MOD_RES 162 162 Phosphoserine. FT MOD_RES 167 167 Phosphothreonine (By similarity). FT MOD_RES 196 196 Phosphoserine. FT VAR_SEQ 1 240 Missing (in isoform B). FT /FTId=VSP_015586. FT CONFLICT 257 257 F -> V (in Ref. 1; AAQ55224). FT CONFLICT 516 516 T -> N (in Ref. 1; AAQ55224). SQ SEQUENCE 566 AA; 62997 MW; 754DE4D696102C7D CRC64; MGSAAMDTKK KKEVSSPGGS SGKKNPSLKR RSLRVHIPDL SSFAMPLLDG DVENSEKHSS RKVDSPFSSG SPSRGLFSRG PQPRPSSPVS APVRPKTSPG SPKTVFPFSY QESPPRSPRR MSFSGIFRSS SKESSPNSNP STSPGGIRFF SRSRKTSSVS SSPSTPTQVT KQHPFPLESY KQEPERPESR IYASSSPPDT GQRFCLAFQS PARPPLASPT YHAPLRTAVL AAAPGPAEAG MLEKLEFQEE EDSESGFYMR FMRSHKCYDI VPTSSKLVVF DTTLQVKKAF FALVANGVRA APLWESKKQS FVGMLTITDF INILHRYYKS PMVQIYELEE HKIETWRELY LQETFKPLVN ISPDASLFDA VYSLIKNKIH RLPVIDPISG NALYILTHKR ILKFLQLFMS DMPKPAFMKQ NLDELGIGTY HNIAFIHPDT PIIKALNIFV ERRISALPVV DESGKVVDIY SKFDVINLAA EKTYNNLDIT VTQALQHRSQ YFEGVVKCSK LETLETIVDR IVRAEVHRLV VVNEADSIVG IISLSDILQA LILTPAGAKQ KETETE //