AAKB2_HUMAN
ID AAKB2_HUMAN Reviewed; 272 AA.
AC O43741; A8K9V5; B4DH06; Q5VXY0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=5'-AMP-activated protein kinase subunit beta-2;
DE Short=AMPK subunit beta-2;
GN Name=PRKAB2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9575201; DOI=10.1074/jbc.273.20.12443;
RA Thornton C., Snowden M.A., Carling D.;
RT "Identification of a novel AMP-activated protein kinase beta subunit
RT isoform that is highly expressed in skeletal muscle.";
RL J. Biol. Chem. 273:12443-12450(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12490143; DOI=10.1006/mcpr.2002.0439;
RA Prochazka M., Farook V.S., Ossowski V., Wolford J.K., Bogardus C.;
RT "Variant screening of PRKAB2, a type 2 diabetes mellitus susceptibility
RT candidate gene on 1q in Pima Indians.";
RL Mol. Cell. Probes 16:421-427(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-184, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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 regulatory
RT feedback loop.";
RL Autophagy 7:696-706(2011).
RN [15]
RP REVIEW ON FUNCTION.
RX PubMed=17307971; DOI=10.1161/01.res.0000256090.42690.05;
RA Towler M.C., Hardie D.G.;
RT "AMP-activated protein kinase in metabolic control and insulin signaling.";
RL Circ. Res. 100:328-341(2007).
RN [16]
RP REVIEW ON FUNCTION.
RX PubMed=17712357; DOI=10.1038/nrm2249;
RA Hardie D.G.;
RT "AMP-activated/SNF1 protein kinases: conserved guardians of cellular
RT energy.";
RL Nat. Rev. Mol. Cell Biol. 8:774-785(2007).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-108; THR-148; SER-158
RP AND SER-170, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 187-272 IN COMPLEX WITH PRKAA1 AND
RP PRKAG1.
RX PubMed=17851531; DOI=10.1038/nature06161;
RA Xiao B., Heath R., Saiu P., Leiper F.C., Leone P., Jing C., Walker P.A.,
RA Haire L., Eccleston J.F., Davis C.T., Martin S.R., Carling D.,
RA Gamblin S.J.;
RT "Structural basis for AMP binding to mammalian AMP-activated protein
RT kinase.";
RL Nature 449:496-500(2007).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 187-272 IN COMPLEX WITH PRKAA1
RP AND PRKAG1, AND MUTAGENESIS OF HIS-235.
RX PubMed=21399626; DOI=10.1038/nature09932;
RA Xiao B., Sanders M.J., Underwood E., Heath R., Mayer F.V., Carmena D.,
RA Jing C., Walker P.A., Eccleston J.F., Haire L.F., Saiu P., Howell S.A.,
RA Aasland R., Martin S.R., Carling D., Gamblin S.J.;
RT "Structure of mammalian AMPK and its regulation by ADP.";
RL Nature 472:230-233(2011).
CC -!- FUNCTION: Non-catalytic subunit of AMP-activated protein kinase (AMPK),
CC an energy sensor protein kinase that plays a key role in regulating
CC cellular energy metabolism. In response to reduction of intracellular
CC ATP levels, AMPK activates energy-producing pathways and inhibits
CC energy-consuming processes: inhibits protein, carbohydrate and lipid
CC biosynthesis, as well as cell growth and proliferation. AMPK acts via
CC direct phosphorylation of metabolic enzymes, and by longer-term effects
CC via phosphorylation of transcription regulators. Also acts as a
CC regulator of cellular polarity by remodeling the actin cytoskeleton;
CC probably by indirectly activating myosin. Beta non-catalytic subunit
CC acts as a scaffold on which the AMPK complex assembles, via its C-
CC terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits
CC (PRKAG1, PRKAG2 or PRKAG3).
CC -!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1
CC or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic
CC subunits (PRKAG1, PRKAG2 or PRKAG3). {ECO:0000269|PubMed:17851531,
CC ECO:0000269|PubMed:21399626}.
CC -!- INTERACTION:
CC O43741; Q8NFV4-4: ABHD11; NbExp=3; IntAct=EBI-1053424, EBI-12318443;
CC O43741; Q6UY14-3: ADAMTSL4; NbExp=4; IntAct=EBI-1053424, EBI-10173507;
CC O43741; Q9NYG5-2: ANAPC11; NbExp=3; IntAct=EBI-1053424, EBI-12224467;
CC O43741; Q03989: ARID5A; NbExp=3; IntAct=EBI-1053424, EBI-948603;
CC O43741; Q9H7T9: AUNIP; NbExp=3; IntAct=EBI-1053424, EBI-10693257;
CC O43741; P01185: AVP; NbExp=3; IntAct=EBI-1053424, EBI-6858021;
CC O43741; Q8N9N5: BANP; NbExp=3; IntAct=EBI-1053424, EBI-744695;
CC O43741; Q8N9N5-2: BANP; NbExp=5; IntAct=EBI-1053424, EBI-11524452;
CC O43741; Q7L4P6: BEND5; NbExp=4; IntAct=EBI-1053424, EBI-724373;
CC O43741; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-1053424, EBI-11519926;
CC O43741; Q9H2G9: BLZF1; NbExp=9; IntAct=EBI-1053424, EBI-2548012;
CC O43741; Q9H5F2: C11orf1; NbExp=3; IntAct=EBI-1053424, EBI-718615;
CC O43741; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-1053424, EBI-11976299;
CC O43741; Q9NWW7: C2orf42; NbExp=3; IntAct=EBI-1053424, EBI-2812028;
CC O43741; Q3SXR2: C3orf36; NbExp=3; IntAct=EBI-1053424, EBI-18036948;
CC O43741; P42575: CASP2; NbExp=3; IntAct=EBI-1053424, EBI-520342;
CC O43741; Q9BUN5-3: CCDC28B; NbExp=5; IntAct=EBI-1053424, EBI-12920646;
CC O43741; O60729: CDC14B; NbExp=3; IntAct=EBI-1053424, EBI-970231;
CC O43741; O14627: CDX4; NbExp=5; IntAct=EBI-1053424, EBI-10181162;
CC O43741; P27918: CFP; NbExp=3; IntAct=EBI-1053424, EBI-9038570;
CC O43741; Q96BA8: CREB3L1; NbExp=4; IntAct=EBI-1053424, EBI-6942903;
CC O43741; O43186: CRX; NbExp=9; IntAct=EBI-1053424, EBI-748171;
CC O43741; A8MQ03: CYSRT1; NbExp=4; IntAct=EBI-1053424, EBI-3867333;
CC O43741; P14920: DAO; NbExp=6; IntAct=EBI-1053424, EBI-3908043;
CC O43741; O95865: DDAH2; NbExp=3; IntAct=EBI-1053424, EBI-749139;
CC O43741; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-1053424, EBI-742054;
CC O43741; G5E9A7: DMWD; NbExp=3; IntAct=EBI-1053424, EBI-10976677;
CC O43741; Q7L591-3: DOK3; NbExp=3; IntAct=EBI-1053424, EBI-10694655;
CC O43741; O00472: ELL2; NbExp=3; IntAct=EBI-1053424, EBI-395274;
CC O43741; Q9NQ30: ESM1; NbExp=3; IntAct=EBI-1053424, EBI-12260294;
CC O43741; P22607: FGFR3; NbExp=3; IntAct=EBI-1053424, EBI-348399;
CC O43741; P21333-2: FLNA; NbExp=3; IntAct=EBI-1053424, EBI-9641086;
CC O43741; P15976: GATA1; NbExp=3; IntAct=EBI-1053424, EBI-3909284;
CC O43741; P15976-2: GATA1; NbExp=6; IntAct=EBI-1053424, EBI-9090198;
CC O43741; Q8WXI9: GATAD2B; NbExp=4; IntAct=EBI-1053424, EBI-923440;
CC O43741; Q5JQS6: GCSAML; NbExp=3; IntAct=EBI-1053424, EBI-17857617;
CC O43741; Q7L5D6: GET4; NbExp=8; IntAct=EBI-1053424, EBI-711823;
CC O43741; Q08379: GOLGA2; NbExp=10; IntAct=EBI-1053424, EBI-618309;
CC O43741; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-1053424, EBI-5916454;
CC O43741; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-1053424, EBI-739467;
CC O43741; Q8TC17: GRAPL; NbExp=3; IntAct=EBI-1053424, EBI-18300553;
CC O43741; Q14957: GRIN2C; NbExp=3; IntAct=EBI-1053424, EBI-8285963;
CC O43741; P28799: GRN; NbExp=4; IntAct=EBI-1053424, EBI-747754;
CC O43741; O15499: GSC2; NbExp=3; IntAct=EBI-1053424, EBI-19954058;
CC O43741; P06396: GSN; NbExp=3; IntAct=EBI-1053424, EBI-351506;
CC O43741; P04792: HSPB1; NbExp=3; IntAct=EBI-1053424, EBI-352682;
CC O43741; Q8IYA8: IHO1; NbExp=6; IntAct=EBI-1053424, EBI-8638439;
CC O43741; Q13422: IKZF1; NbExp=3; IntAct=EBI-1053424, EBI-745305;
CC O43741; Q9UKT9: IKZF3; NbExp=11; IntAct=EBI-1053424, EBI-747204;
CC O43741; Q9NZH6: IL37; NbExp=5; IntAct=EBI-1053424, EBI-3862125;
CC O43741; Q5VVH5: IRAK1BP1; NbExp=3; IntAct=EBI-1053424, EBI-9658404;
CC O43741; Q9H079: KATNBL1; NbExp=3; IntAct=EBI-1053424, EBI-715394;
CC O43741; Q7Z7F0-4: KHDC4; NbExp=3; IntAct=EBI-1053424, EBI-9089060;
CC O43741; O60333-2: KIF1B; NbExp=3; IntAct=EBI-1053424, EBI-10975473;
CC O43741; Q9UIH9: KLF15; NbExp=9; IntAct=EBI-1053424, EBI-2796400;
CC O43741; Q5JUW0-3: KRBOX4; NbExp=3; IntAct=EBI-1053424, EBI-12893625;
CC O43741; Q15323: KRT31; NbExp=3; IntAct=EBI-1053424, EBI-948001;
CC O43741; Q6A162: KRT40; NbExp=6; IntAct=EBI-1053424, EBI-10171697;
CC O43741; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-1053424, EBI-11959885;
CC O43741; Q8IUG1: KRTAP1-3; NbExp=5; IntAct=EBI-1053424, EBI-11749135;
CC O43741; P60412: KRTAP10-11; NbExp=3; IntAct=EBI-1053424, EBI-10217483;
CC O43741; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-1053424, EBI-10172150;
CC O43741; P60409: KRTAP10-7; NbExp=8; IntAct=EBI-1053424, EBI-10172290;
CC O43741; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-1053424, EBI-10171774;
CC O43741; P60411: KRTAP10-9; NbExp=6; IntAct=EBI-1053424, EBI-10172052;
CC O43741; Q9BYP8: KRTAP17-1; NbExp=3; IntAct=EBI-1053424, EBI-11988175;
CC O43741; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-1053424, EBI-14065470;
CC O43741; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-1053424, EBI-3957694;
CC O43741; Q9BQ66: KRTAP4-12; NbExp=3; IntAct=EBI-1053424, EBI-739863;
CC O43741; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-1053424, EBI-10172511;
CC O43741; Q9BYR2: KRTAP4-5; NbExp=3; IntAct=EBI-1053424, EBI-11993254;
CC O43741; P26371: KRTAP5-9; NbExp=6; IntAct=EBI-1053424, EBI-3958099;
CC O43741; Q9BYQ4: KRTAP9-2; NbExp=8; IntAct=EBI-1053424, EBI-1044640;
CC O43741; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-1053424, EBI-1043191;
CC O43741; Q9BYQ2: KRTAP9-4; NbExp=3; IntAct=EBI-1053424, EBI-10185730;
CC O43741; Q9BYQ0: KRTAP9-8; NbExp=8; IntAct=EBI-1053424, EBI-11958364;
CC O43741; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-1053424, EBI-12039345;
CC O43741; Q5T3J3: LRIF1; NbExp=3; IntAct=EBI-1053424, EBI-473196;
CC O43741; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-1053424, EBI-1216080;
CC O43741; Q9BRK4: LZTS2; NbExp=4; IntAct=EBI-1053424, EBI-741037;
CC O43741; Q9Y5V3: MAGED1; NbExp=4; IntAct=EBI-1053424, EBI-716006;
CC O43741; Q3KP22-3: MAJIN; NbExp=3; IntAct=EBI-1053424, EBI-18015780;
CC O43741; P31153: MAT2A; NbExp=3; IntAct=EBI-1053424, EBI-1050743;
CC O43741; Q99750: MDFI; NbExp=12; IntAct=EBI-1053424, EBI-724076;
CC O43741; P50222: MEOX2; NbExp=3; IntAct=EBI-1053424, EBI-748397;
CC O43741; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-1053424, EBI-8487781;
CC O43741; Q6PF18: MORN3; NbExp=3; IntAct=EBI-1053424, EBI-9675802;
CC O43741; Q15742: NAB2; NbExp=3; IntAct=EBI-1053424, EBI-8641936;
CC O43741; P0CG21: NHLRC4; NbExp=3; IntAct=EBI-1053424, EBI-12868744;
CC O43741; Q8TDS5: OXER1; NbExp=3; IntAct=EBI-1053424, EBI-12813389;
CC O43741; P18545: PDE6G; NbExp=3; IntAct=EBI-1053424, EBI-2622029;
CC O43741; Q13956: PDE6H; NbExp=3; IntAct=EBI-1053424, EBI-10231995;
CC O43741; Q99471: PFDN5; NbExp=3; IntAct=EBI-1053424, EBI-357275;
CC O43741; O75928: PIAS2; NbExp=3; IntAct=EBI-1053424, EBI-348555;
CC O43741; Q6ZR37: PLEKHG7; NbExp=3; IntAct=EBI-1053424, EBI-12891828;
CC O43741; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-1053424, EBI-1105153;
CC O43741; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-1053424, EBI-710402;
CC O43741; Q9GZV8: PRDM14; NbExp=4; IntAct=EBI-1053424, EBI-3957793;
CC O43741; Q13131: PRKAA1; NbExp=16; IntAct=EBI-1053424, EBI-1181405;
CC O43741; P54646: PRKAA2; NbExp=14; IntAct=EBI-1053424, EBI-1383852;
CC O43741; P54619: PRKAG1; NbExp=17; IntAct=EBI-1053424, EBI-1181439;
CC O43741; Q9UGI9: PRKAG3; NbExp=5; IntAct=EBI-1053424, EBI-7428853;
CC O43741; O00231: PSMD11; NbExp=3; IntAct=EBI-1053424, EBI-357816;
CC O43741; P61289: PSME3; NbExp=9; IntAct=EBI-1053424, EBI-355546;
CC O43741; P11217: PYGM; NbExp=7; IntAct=EBI-1053424, EBI-357469;
CC O43741; Q96PU8: QKI; NbExp=3; IntAct=EBI-1053424, EBI-945792;
CC O43741; Q96QF0-7: RAB3IP; NbExp=3; IntAct=EBI-1053424, EBI-11984839;
CC O43741; Q5RL73: RBM48; NbExp=3; IntAct=EBI-1053424, EBI-473821;
CC O43741; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-1053424, EBI-740343;
CC O43741; Q04864-2: REL; NbExp=4; IntAct=EBI-1053424, EBI-10829018;
CC O43741; Q8TAI7: RHEBL1; NbExp=7; IntAct=EBI-1053424, EBI-746555;
CC O43741; Q9UFD9: RIMBP3; NbExp=4; IntAct=EBI-1053424, EBI-10182375;
CC O43741; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-1053424, EBI-396669;
CC O43741; Q01974: ROR2; NbExp=3; IntAct=EBI-1053424, EBI-6422642;
CC O43741; Q9UNE2: RPH3AL; NbExp=3; IntAct=EBI-1053424, EBI-2855824;
CC O43741; Q9UPU9-3: SAMD4A; NbExp=3; IntAct=EBI-1053424, EBI-11986417;
CC O43741; Q14140: SERTAD2; NbExp=3; IntAct=EBI-1053424, EBI-2822051;
CC O43741; Q12824-2: SMARCB1; NbExp=3; IntAct=EBI-1053424, EBI-358436;
CC O43741; Q53HV7-2: SMUG1; NbExp=3; IntAct=EBI-1053424, EBI-12275818;
CC O43741; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1053424, EBI-5235340;
CC O43741; O43609: SPRY1; NbExp=3; IntAct=EBI-1053424, EBI-3866665;
CC O43741; O43597: SPRY2; NbExp=4; IntAct=EBI-1053424, EBI-742487;
CC O43741; O75558: STX11; NbExp=4; IntAct=EBI-1053424, EBI-714135;
CC O43741; Q8N4C7: STX19; NbExp=4; IntAct=EBI-1053424, EBI-8484990;
CC O43741; Q5VWN6-2: TASOR2; NbExp=3; IntAct=EBI-1053424, EBI-10172380;
CC O43741; Q99081-3: TCF12; NbExp=3; IntAct=EBI-1053424, EBI-11952764;
CC O43741; Q9Y242: TCF19; NbExp=3; IntAct=EBI-1053424, EBI-7413767;
CC O43741; Q9NQB0-10: TCF7L2; NbExp=3; IntAct=EBI-1053424, EBI-11746252;
CC O43741; Q96PF1: TGM7; NbExp=3; IntAct=EBI-1053424, EBI-12029034;
CC O43741; Q08117-2: TLE5; NbExp=5; IntAct=EBI-1053424, EBI-11741437;
CC O43741; P19237: TNNI1; NbExp=3; IntAct=EBI-1053424, EBI-746692;
CC O43741; Q12933: TRAF2; NbExp=8; IntAct=EBI-1053424, EBI-355744;
CC O43741; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-1053424, EBI-492476;
CC O43741; Q14142: TRIM14; NbExp=3; IntAct=EBI-1053424, EBI-2820256;
CC O43741; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-1053424, EBI-17716262;
CC O43741; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-1053424, EBI-5235829;
CC O43741; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-1053424, EBI-2130429;
CC O43741; Q969E8: TSR2; NbExp=3; IntAct=EBI-1053424, EBI-746981;
CC O43741; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-1053424, EBI-9090990;
CC O43741; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-1053424, EBI-741480;
CC O43741; Q5T124: UBXN11; NbExp=3; IntAct=EBI-1053424, EBI-746004;
CC O43741; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-1053424, EBI-11975223;
CC O43741; P61758: VBP1; NbExp=3; IntAct=EBI-1053424, EBI-357430;
CC O43741; Q9UK41-2: VPS28; NbExp=3; IntAct=EBI-1053424, EBI-12146727;
CC O43741; Q9BRX9: WDR83; NbExp=3; IntAct=EBI-1053424, EBI-7705033;
CC O43741; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-1053424, EBI-14104088;
CC O43741; Q8TF47: ZFP90; NbExp=3; IntAct=EBI-1053424, EBI-11419867;
CC O43741; Q96E35: ZMYND19; NbExp=5; IntAct=EBI-1053424, EBI-746595;
CC O43741; Q13360-2: ZNF177; NbExp=3; IntAct=EBI-1053424, EBI-12272076;
CC O43741; Q9UL36: ZNF236; NbExp=3; IntAct=EBI-1053424, EBI-23928087;
CC O43741; Q6S9Z5: ZNF474; NbExp=3; IntAct=EBI-1053424, EBI-17269964;
CC O43741; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-1053424, EBI-11035148;
CC O43741; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-1053424, EBI-745520;
CC O43741; A0A1U9X8X8; NbExp=3; IntAct=EBI-1053424, EBI-17234977;
CC O43741; Q7Z783; NbExp=3; IntAct=EBI-1053424, EBI-9088990;
CC O43741; Q9Y649; NbExp=3; IntAct=EBI-1053424, EBI-25900580;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43741-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43741-2; Sequence=VSP_055820, VSP_055821;
CC -!- PTM: Phosphorylated when associated with the catalytic subunit (PRKAA1
CC or PRKAA2). Phosphorylated by ULK1 and ULK2; leading to negatively
CC regulate AMPK activity and suggesting the existence of a regulatory
CC feedback loop between ULK1, ULK2 and AMPK.
CC {ECO:0000269|PubMed:21460634}.
CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC family. {ECO:0000305}.
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DR EMBL; AJ224538; CAA12030.1; -; mRNA.
DR EMBL; AF504543; AAM74153.1; -; Genomic_DNA.
DR EMBL; AF504538; AAM74153.1; JOINED; Genomic_DNA.
DR EMBL; AF504539; AAM74153.1; JOINED; Genomic_DNA.
DR EMBL; AF504540; AAM74153.1; JOINED; Genomic_DNA.
DR EMBL; AF504541; AAM74153.1; JOINED; Genomic_DNA.
DR EMBL; AF504542; AAM74153.1; JOINED; Genomic_DNA.
DR EMBL; AK292820; BAF85509.1; -; mRNA.
DR EMBL; AK294863; BAG57967.1; -; mRNA.
DR EMBL; AK316005; BAH14376.1; -; mRNA.
DR EMBL; AL356378; CAH72644.1; -; Genomic_DNA.
DR EMBL; CH471223; EAW50945.1; -; Genomic_DNA.
DR EMBL; BC053610; AAH53610.1; -; mRNA.
DR CCDS; CCDS925.1; -. [O43741-1]
DR RefSeq; NP_005390.1; NM_005399.4. [O43741-1]
DR PDB; 2F15; X-ray; 2.00 A; A=69-163.
DR PDB; 2V8Q; X-ray; 2.10 A; B=187-272.
DR PDB; 2V92; X-ray; 2.40 A; B=187-272.
DR PDB; 2V9J; X-ray; 2.53 A; B=187-272.
DR PDB; 2Y8L; X-ray; 2.50 A; B=187-272.
DR PDB; 2Y8Q; X-ray; 2.80 A; B=187-270.
DR PDB; 2YA3; X-ray; 2.51 A; B=187-272.
DR PDB; 4CFH; X-ray; 3.24 A; B=187-272.
DR PDB; 4EAI; X-ray; 2.28 A; B=189-272.
DR PDB; 4EAJ; X-ray; 2.61 A; B=189-272.
DR PDB; 4RER; X-ray; 4.05 A; B=76-272.
DR PDB; 4REW; X-ray; 4.58 A; B=76-272.
DR PDB; 6B2E; X-ray; 3.80 A; B=1-272.
DR PDB; 7JHG; EM; 3.47 A; B=75-272.
DR PDB; 7JHH; EM; 3.92 A; B=75-272.
DR PDB; 7JIJ; X-ray; 5.50 A; B=75-272.
DR PDB; 7M74; EM; 3.93 A; B=75-272.
DR PDBsum; 2F15; -.
DR PDBsum; 2V8Q; -.
DR PDBsum; 2V92; -.
DR PDBsum; 2V9J; -.
DR PDBsum; 2Y8L; -.
DR PDBsum; 2Y8Q; -.
DR PDBsum; 2YA3; -.
DR PDBsum; 4CFH; -.
DR PDBsum; 4EAI; -.
DR PDBsum; 4EAJ; -.
DR PDBsum; 4RER; -.
DR PDBsum; 4REW; -.
DR PDBsum; 6B2E; -.
DR PDBsum; 7JHG; -.
DR PDBsum; 7JHH; -.
DR PDBsum; 7JIJ; -.
DR PDBsum; 7M74; -.
DR AlphaFoldDB; O43741; -.
DR BMRB; O43741; -.
DR SMR; O43741; -.
DR BioGRID; 111552; 225.
DR ComplexPortal; CPX-5790; AMPK complex, alpha2-beta2-gamma1 variant.
DR ComplexPortal; CPX-5791; AMPK complex, alpha1-beta2-gamma1 variant.
DR ComplexPortal; CPX-5840; AMPK complex, alpha2-beta2-gamma3 variant.
DR ComplexPortal; CPX-5841; AMPK complex, alpha1-beta2-gamma3 variant.
DR ComplexPortal; CPX-5845; AMPK complex, alpha2-beta2-gamma2 variant.
DR ComplexPortal; CPX-5846; AMPK complex, alpha1-beta2-gamma2 variant.
DR CORUM; O43741; -.
DR DIP; DIP-39763N; -.
DR IntAct; O43741; 211.
DR MINT; O43741; -.
DR STRING; 9606.ENSP00000254101; -.
DR BindingDB; O43741; -.
DR ChEMBL; CHEMBL2117; -.
DR DrugBank; DB00945; Acetylsalicylic acid.
DR DrugBank; DB00131; Adenosine phosphate.
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB00273; Topiramate.
DR GuidetoPHARMACOLOGY; 1544; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR iPTMnet; O43741; -.
DR PhosphoSitePlus; O43741; -.
DR BioMuta; PRKAB2; -.
DR EPD; O43741; -.
DR jPOST; O43741; -.
DR MassIVE; O43741; -.
DR MaxQB; O43741; -.
DR PaxDb; O43741; -.
DR PeptideAtlas; O43741; -.
DR PRIDE; O43741; -.
DR ProteomicsDB; 4178; -.
DR ProteomicsDB; 49144; -. [O43741-1]
DR Antibodypedia; 33978; 321 antibodies from 33 providers.
DR DNASU; 5565; -.
DR Ensembl; ENST00000254101.4; ENSP00000254101.3; ENSG00000131791.8. [O43741-1]
DR GeneID; 5565; -.
DR KEGG; hsa:5565; -.
DR MANE-Select; ENST00000254101.4; ENSP00000254101.3; NM_005399.5; NP_005390.1.
DR UCSC; uc001epe.5; human. [O43741-1]
DR CTD; 5565; -.
DR DisGeNET; 5565; -.
DR GeneCards; PRKAB2; -.
DR HGNC; HGNC:9379; PRKAB2.
DR HPA; ENSG00000131791; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 602741; gene.
DR neXtProt; NX_O43741; -.
DR OpenTargets; ENSG00000131791; -.
DR PharmGKB; PA33747; -.
DR VEuPathDB; HostDB:ENSG00000131791; -.
DR eggNOG; KOG1616; Eukaryota.
DR GeneTree; ENSGT00940000159284; -.
DR HOGENOM; CLU_070949_2_0_1; -.
DR OMA; PPHKPWE; -.
DR OrthoDB; 956412at2759; -.
DR PhylomeDB; O43741; -.
DR TreeFam; TF313827; -.
DR BRENDA; 2.7.11.31; 2681.
DR PathwayCommons; O43741; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR Reactome; R-HSA-163680; AMPK inhibits chREBP transcriptional activation activity.
DR Reactome; R-HSA-200425; Carnitine metabolism.
DR Reactome; R-HSA-2151209; Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
DR Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-9613354; Lipophagy.
DR Reactome; R-HSA-9619483; Activation of AMPK downstream of NMDARs.
DR SignaLink; O43741; -.
DR SIGNOR; O43741; -.
DR BioGRID-ORCS; 5565; 16 hits in 1087 CRISPR screens.
DR ChiTaRS; PRKAB2; human.
DR EvolutionaryTrace; O43741; -.
DR GeneWiki; PRKAB2; -.
DR GenomeRNAi; 5565; -.
DR Pharos; O43741; Tchem.
DR PRO; PR:O43741; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O43741; protein.
DR Bgee; ENSG00000131791; Expressed in jejunal mucosa and 190 other tissues.
DR Genevisible; O43741; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0031669; P:cellular response to nutrient levels; IDA:ComplexPortal.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR032640; AMPK1_CBM.
DR InterPro; IPR039160; AMPKB.
DR InterPro; IPR006828; ASC_dom.
DR InterPro; IPR037256; ASC_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR10343:SF83; PTHR10343:SF83; 1.
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 3D-structure; Alternative splicing; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..272
FT /note="5'-AMP-activated protein kinase subunit beta-2"
FT /id="PRO_0000204368"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZH4"
FT MOD_RES 40
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZH4"
FT MOD_RES 69
FT /note="Phosphoserine; by ULK1"
FT /evidence="ECO:0000250|UniProtKB:Q9QZH4"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 148
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZH4"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..25
FT /note="MGNTTSDRVSGERHGAKAARSEGAG -> MPRGRSTRSWWGVRTTPACSASL
FT TP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055820"
FT VAR_SEQ 26..107
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055821"
FT MUTAGEN 235
FT /note="H->A: Results in an AMPK enzyme that is activable by
FT phosphorylation but has significantly increased rate of
FT dephosphorylation in phosphatase assays."
FT /evidence="ECO:0000269|PubMed:21399626"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:2F15"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:2F15"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:2F15"
FT STRAND 112..129
FT /evidence="ECO:0007829|PDB:2F15"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:2F15"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:2F15"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:2F15"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:2F15"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:2V8Q"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:4CFH"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:2V8Q"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:7JHG"
FT TURN 236..239
FT /evidence="ECO:0007829|PDB:2V92"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:4EAI"
FT STRAND 250..259
FT /evidence="ECO:0007829|PDB:2V8Q"
FT STRAND 262..271
FT /evidence="ECO:0007829|PDB:2V8Q"
SQ SEQUENCE 272 AA; 30302 MW; 42B23BD70B92519C CRC64;
MGNTTSDRVS GERHGAKAAR SEGAGGHAPG KEHKIMVGST DDPSVFSLPD SKLPGDKEFV
SWQQDLEDSV KPTQQARPTV IRWSEGGKEV FISGSFNNWS TKIPLIKSHN DFVAILDLPE
GEHQYKFFVD GQWVHDPSEP VVTSQLGTIN NLIHVKKSDF EVFDALKLDS MESSETSCRD
LSSSPPGPYG QEMYAFRSEE RFKSPPILPP HLLQVILNKD TNISCDPALL PEPNHVMLNH
LYALSIKDSV MVLSATHRYK KKYVTTLLYK PI
