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Database: UniProt
Entry: O43741
LinkDB: O43741
Original site: O43741 
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   17-JUN-2020, entry version 189.
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; Q32Q52: C12orf74; NbExp=3; IntAct=EBI-1053424, EBI-12891828;
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; Q8IYA8: CCDC36; NbExp=6; IntAct=EBI-1053424, EBI-8638439;
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; 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; 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; O15499: GSC2; NbExp=3; IntAct=EBI-1053424, EBI-19954058;
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; 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; 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; 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; 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=14; IntAct=EBI-1053424, EBI-1181405;
CC       O43741; P54646: PRKAA2; NbExp=12; IntAct=EBI-1053424, EBI-1383852;
CC       O43741; O43741: PRKAB2; NbExp=2; IntAct=EBI-1053424, EBI-1053424;
CC       O43741; P54619: PRKAG1; NbExp=16; IntAct=EBI-1053424, EBI-1181439;
CC       O43741; Q9UGI9: PRKAG3; NbExp=4; 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; 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; 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; 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   -!- 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}.
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   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   SMR; O43741; -.
DR   BioGRID; 111552; 109.
DR   CORUM; O43741; -.
DR   DIP; DIP-39763N; -.
DR   IntAct; O43741; 189.
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; 291 antibodies.
DR   DNASU; 5565; -.
DR   Ensembl; ENST00000254101; ENSP00000254101; ENSG00000131791. [O43741-1]
DR   GeneID; 5565; -.
DR   KEGG; hsa:5565; -.
DR   UCSC; uc001epe.5; human. [O43741-1]
DR   CTD; 5565; -.
DR   DisGeNET; 5565; -.
DR   EuPathDB; HostDB:ENSG00000131791.7; -.
DR   GeneCards; PRKAB2; -.
DR   HGNC; HGNC:9379; PRKAB2.
DR   HPA; ENSG00000131791; Tissue enhanced (skeletal).
DR   MIM; 602741; gene.
DR   neXtProt; NX_O43741; -.
DR   OpenTargets; ENSG00000131791; -.
DR   PharmGKB; PA33747; -.
DR   eggNOG; KOG1616; Eukaryota.
DR   eggNOG; ENOG410XRB3; LUCA.
DR   GeneTree; ENSGT00940000159284; -.
DR   HOGENOM; CLU_070949_2_0_1; -.
DR   KO; K07199; -.
DR   OMA; PPHKPWE; -.
DR   OrthoDB; 956412at2759; -.
DR   PhylomeDB; O43741; -.
DR   TreeFam; TF313827; -.
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; 4 hits in 790 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 biceps brachii and 206 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:0004679; F:AMP-activated protein kinase activity; IDA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0006853; P:carnitine shuttle; TAS:Reactome.
DR   GO; GO:0007050; P:cell cycle arrest; TAS:Reactome.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016236; P:macroautophagy; TAS:Reactome.
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:0042304; P:regulation of fatty acid biosynthetic process; TAS:Reactome.
DR   GO; GO:0016241; P:regulation of macroautophagy; TAS:Reactome.
DR   GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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   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:0000244|PubMed:24275569"
FT   MOD_RES         108
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18318008,
FT                   ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:18691976,
FT                   ECO:0000244|PubMed:19369195, ECO:0000244|PubMed:19690332,
FT                   ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163,
FT                   ECO:0000244|PubMed:24275569"
FT   MOD_RES         148
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         158
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         170
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|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:0000244|PubMed:18669648,
FT                   ECO:0000244|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:0000244|PDB:2F15"
FT   STRAND          90..94
FT                   /evidence="ECO:0000244|PDB:2F15"
FT   HELIX           95..97
FT                   /evidence="ECO:0000244|PDB:2F15"
FT   STRAND          112..129
FT                   /evidence="ECO:0000244|PDB:2F15"
FT   STRAND          132..134
FT                   /evidence="ECO:0000244|PDB:2F15"
FT   STRAND          141..143
FT                   /evidence="ECO:0000244|PDB:2F15"
FT   STRAND          149..155
FT                   /evidence="ECO:0000244|PDB:2F15"
FT   TURN            159..162
FT                   /evidence="ECO:0000244|PDB:2F15"
FT   STRAND          201..204
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   HELIX           210..213
FT                   /evidence="ECO:0000244|PDB:4CFH"
FT   STRAND          214..217
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   TURN            236..239
FT                   /evidence="ECO:0000244|PDB:2V92"
FT   STRAND          242..244
FT                   /evidence="ECO:0000244|PDB:4EAI"
FT   STRAND          250..259
FT                   /evidence="ECO:0000244|PDB:2V8Q"
FT   STRAND          262..271
FT                   /evidence="ECO:0000244|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
//
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