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5'-AMP-activated protein kinase subunit beta-2 (AMPK subunit beta-2)

 AAKB2_HUMAN             Reviewed;         272 AA.
O43741; A8K9V5; B4DH06; Q5VXY0;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
18-JUL-2018, entry version 175.
RecName: Full=5'-AMP-activated protein kinase subunit beta-2;
Short=AMPK subunit beta-2;
Name=PRKAB2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9575201; DOI=10.1074/jbc.273.20.12443;
Thornton C., Snowden M.A., Carling D.;
"Identification of a novel AMP-activated protein kinase beta subunit
isoform that is highly expressed in skeletal muscle.";
J. Biol. Chem. 273:12443-12450(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12490143; DOI=10.1006/mcpr.2002.0439;
Prochazka M., Farook V.S., Ossowski V., Wolford J.K., Bogardus C.;
"Variant screening of PRKAB2, a type 2 diabetes mellitus
susceptibility candidate gene on 1q in Pima Indians.";
Mol. Cell. Probes 16:421-427(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-184, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
PHOSPHORYLATION BY ULK1 AND ULK2.
PubMed=21460634; DOI=10.4161/auto.7.7.15451;
Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M.,
Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.;
"Ulk1-mediated phosphorylation of AMPK constitutes a negative
regulatory feedback loop.";
Autophagy 7:696-706(2011).
[15]
REVIEW ON FUNCTION.
PubMed=17307971; DOI=10.1161/01.RES.0000256090.42690.05;
Towler M.C., Hardie D.G.;
"AMP-activated protein kinase in metabolic control and insulin
signaling.";
Circ. Res. 100:328-341(2007).
[16]
REVIEW ON FUNCTION.
PubMed=17712357; DOI=10.1038/nrm2249;
Hardie D.G.;
"AMP-activated/SNF1 protein kinases: conserved guardians of cellular
energy.";
Nat. Rev. Mol. Cell Biol. 8:774-785(2007).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95; SER-108; THR-148;
SER-158 AND SER-170, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 187-272 IN COMPLEX WITH
PRKAA1 AND PRKAG1.
PubMed=17851531; DOI=10.1038/nature06161;
Xiao B., Heath R., Saiu P., Leiper F.C., Leone P., Jing C.,
Walker P.A., Haire L., Eccleston J.F., Davis C.T., Martin S.R.,
Carling D., Gamblin S.J.;
"Structural basis for AMP binding to mammalian AMP-activated protein
kinase.";
Nature 449:496-500(2007).
[22]
X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 187-272 IN COMPLEX WITH
PRKAA1 AND PRKAG1, AND MUTAGENESIS OF HIS-235.
PubMed=21399626; DOI=10.1038/nature09932;
Xiao B., Sanders M.J., Underwood E., Heath R., Mayer F.V., Carmena D.,
Jing C., Walker P.A., Eccleston J.F., Haire L.F., Saiu P.,
Howell S.A., Aasland R., Martin S.R., Carling D., Gamblin S.J.;
"Structure of mammalian AMPK and its regulation by ADP.";
Nature 472:230-233(2011).
-!- FUNCTION: Non-catalytic subunit of AMP-activated protein kinase
(AMPK), an energy sensor protein kinase that plays a key role in
regulating cellular energy metabolism. In response to reduction of
intracellular ATP levels, AMPK activates energy-producing pathways
and inhibits energy-consuming processes: inhibits protein,
carbohydrate and lipid biosynthesis, as well as cell growth and
proliferation. AMPK acts via direct phosphorylation of metabolic
enzymes, and by longer-term effects via phosphorylation of
transcription regulators. Also acts as a regulator of cellular
polarity by remodeling the actin cytoskeleton; probably by
indirectly activating myosin. Beta non-catalytic subunit acts as a
scaffold on which the AMPK complex assembles, via its C-terminus
that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1,
PRKAG2 or PRKAG3).
-!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit
(PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-
catalytic subunits (PRKAG1, PRKAG2 or PRKAG3).
{ECO:0000269|PubMed:17851531, ECO:0000269|PubMed:21399626}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-1053424, EBI-1053424;
Q08117-2:AES; NbExp=4; IntAct=EBI-1053424, EBI-11741437;
Q8N9N5:BANP; NbExp=3; IntAct=EBI-1053424, EBI-744695;
Q7L4P6:BEND5; NbExp=3; IntAct=EBI-1053424, EBI-724373;
Q9H2G9:BLZF1; NbExp=6; IntAct=EBI-1053424, EBI-2548012;
Q8IYA8:CCDC36; NbExp=5; IntAct=EBI-1053424, EBI-8638439;
O14627:CDX4; NbExp=3; IntAct=EBI-1053424, EBI-10181162;
Q96BA8:CREB3L1; NbExp=3; IntAct=EBI-1053424, EBI-6942903;
O43186:CRX; NbExp=5; IntAct=EBI-1053424, EBI-748171;
P14920:DAO; NbExp=4; IntAct=EBI-1053424, EBI-3908043;
Q5VWN6-2:FAM208B; NbExp=3; IntAct=EBI-1053424, EBI-10172380;
P15976:GATA1; NbExp=3; IntAct=EBI-1053424, EBI-3909284;
P15976-2:GATA1; NbExp=4; IntAct=EBI-1053424, EBI-9090198;
Q8WXI9:GATAD2B; NbExp=3; IntAct=EBI-1053424, EBI-923440;
Q7L5D6:GET4; NbExp=6; IntAct=EBI-1053424, EBI-711823;
Q08379:GOLGA2; NbExp=7; IntAct=EBI-1053424, EBI-618309;
Q13422:IKZF1; NbExp=3; IntAct=EBI-1053424, EBI-745305;
Q9UKT9:IKZF3; NbExp=8; IntAct=EBI-1053424, EBI-747204;
Q9UIH9:KLF15; NbExp=5; IntAct=EBI-1053424, EBI-2796400;
Q6A162:KRT40; NbExp=5; IntAct=EBI-1053424, EBI-10171697;
P60370:KRTAP10-5; NbExp=3; IntAct=EBI-1053424, EBI-10172150;
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-1053424, EBI-10172290;
P60410:KRTAP10-8; NbExp=5; IntAct=EBI-1053424, EBI-10171774;
P60411:KRTAP10-9; NbExp=5; IntAct=EBI-1053424, EBI-10172052;
Q9BQ66:KRTAP4-12; NbExp=3; IntAct=EBI-1053424, EBI-739863;
Q9BYR5:KRTAP4-2; NbExp=3; IntAct=EBI-1053424, EBI-10172511;
P26371:KRTAP5-9; NbExp=5; IntAct=EBI-1053424, EBI-3958099;
Q9BYQ4:KRTAP9-2; NbExp=7; IntAct=EBI-1053424, EBI-1044640;
Q9BYQ2:KRTAP9-4; NbExp=3; IntAct=EBI-1053424, EBI-10185730;
Q9BYQ0:KRTAP9-8; NbExp=4; IntAct=EBI-1053424, EBI-11958364;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-1053424, EBI-741037;
Q9Y5V3:MAGED1; NbExp=3; IntAct=EBI-1053424, EBI-716006;
Q99750:MDFI; NbExp=7; IntAct=EBI-1053424, EBI-724076;
P50222:MEOX2; NbExp=3; IntAct=EBI-1053424, EBI-748397;
O75928:PIAS2; NbExp=3; IntAct=EBI-1053424, EBI-348555;
Q13131:PRKAA1; NbExp=13; IntAct=EBI-1053424, EBI-1181405;
P54646:PRKAA2; NbExp=11; IntAct=EBI-1053424, EBI-1383852;
Q9Y478:PRKAB1; NbExp=2; IntAct=EBI-1053424, EBI-719769;
P54619:PRKAG1; NbExp=10; IntAct=EBI-1053424, EBI-1181439;
P61289:PSME3; NbExp=7; IntAct=EBI-1053424, EBI-355546;
P11217:PYGM; NbExp=5; IntAct=EBI-1053424, EBI-357469;
Q8TAI7:RHEBL1; NbExp=5; IntAct=EBI-1053424, EBI-746555;
Q9UFD9:RIMBP3; NbExp=3; IntAct=EBI-1053424, EBI-10182375;
O43597:SPRY2; NbExp=3; IntAct=EBI-1053424, EBI-742487;
O75558:STX11; NbExp=3; IntAct=EBI-1053424, EBI-714135;
Q8N4C7:STX19; NbExp=3; IntAct=EBI-1053424, EBI-8484990;
Q12933:TRAF2; NbExp=6; IntAct=EBI-1053424, EBI-355744;
Q5T124:UBXN11; NbExp=3; IntAct=EBI-1053424, EBI-746004;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O43741-1; Sequence=Displayed;
Name=2;
IsoId=O43741-2; Sequence=VSP_055820, VSP_055821;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylated when associated with the catalytic subunit
(PRKAA1 or PRKAA2). Phosphorylated by ULK1 and ULK2; leading to
negatively regulate AMPK activity and suggesting the existence of
a regulatory feedback loop between ULK1, ULK2 and AMPK.
{ECO:0000269|PubMed:21460634}.
-!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta
subunit family. {ECO:0000305}.
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EMBL; AJ224538; CAA12030.1; -; mRNA.
EMBL; AF504543; AAM74153.1; -; Genomic_DNA.
EMBL; AF504538; AAM74153.1; JOINED; Genomic_DNA.
EMBL; AF504539; AAM74153.1; JOINED; Genomic_DNA.
EMBL; AF504540; AAM74153.1; JOINED; Genomic_DNA.
EMBL; AF504541; AAM74153.1; JOINED; Genomic_DNA.
EMBL; AF504542; AAM74153.1; JOINED; Genomic_DNA.
EMBL; AK292820; BAF85509.1; -; mRNA.
EMBL; AK294863; BAG57967.1; -; mRNA.
EMBL; AK316005; BAH14376.1; -; mRNA.
EMBL; AL356378; CAH72644.1; -; Genomic_DNA.
EMBL; CH471223; EAW50945.1; -; Genomic_DNA.
EMBL; BC053610; AAH53610.1; -; mRNA.
CCDS; CCDS925.1; -. [O43741-1]
RefSeq; NP_005390.1; NM_005399.4. [O43741-1]
UniGene; Hs.50732; -.
PDB; 2F15; X-ray; 2.00 A; A=69-163.
PDB; 2V8Q; X-ray; 2.10 A; B=187-272.
PDB; 2V92; X-ray; 2.40 A; B=187-272.
PDB; 2V9J; X-ray; 2.53 A; B=187-272.
PDB; 2Y8L; X-ray; 2.50 A; B=187-272.
PDB; 2Y8Q; X-ray; 2.80 A; B=187-270.
PDB; 2YA3; X-ray; 2.51 A; B=187-272.
PDB; 4CFH; X-ray; 3.24 A; B=187-272.
PDB; 4EAI; X-ray; 2.28 A; B=189-272.
PDB; 4EAJ; X-ray; 2.61 A; B=189-272.
PDB; 4RER; X-ray; 4.05 A; B=76-272.
PDB; 4REW; X-ray; 4.58 A; B=76-272.
PDB; 6B2E; X-ray; 3.80 A; B=1-272.
PDBsum; 2F15; -.
PDBsum; 2V8Q; -.
PDBsum; 2V92; -.
PDBsum; 2V9J; -.
PDBsum; 2Y8L; -.
PDBsum; 2Y8Q; -.
PDBsum; 2YA3; -.
PDBsum; 4CFH; -.
PDBsum; 4EAI; -.
PDBsum; 4EAJ; -.
PDBsum; 4RER; -.
PDBsum; 4REW; -.
PDBsum; 6B2E; -.
ProteinModelPortal; O43741; -.
SMR; O43741; -.
BioGrid; 111552; 103.
CORUM; O43741; -.
DIP; DIP-39763N; -.
IntAct; O43741; 165.
MINT; O43741; -.
STRING; 9606.ENSP00000254101; -.
ChEMBL; CHEMBL2117; -.
DrugBank; DB00945; Acetylsalicylic acid.
DrugBank; DB00131; Adenosine monophosphate.
GuidetoPHARMACOLOGY; 1544; -.
CAZy; CBM48; Carbohydrate-Binding Module Family 48.
iPTMnet; O43741; -.
PhosphoSitePlus; O43741; -.
EPD; O43741; -.
MaxQB; O43741; -.
PaxDb; O43741; -.
PeptideAtlas; O43741; -.
PRIDE; O43741; -.
ProteomicsDB; 49144; -.
DNASU; 5565; -.
Ensembl; ENST00000254101; ENSP00000254101; ENSG00000131791. [O43741-1]
GeneID; 5565; -.
KEGG; hsa:5565; -.
UCSC; uc001epe.5; human. [O43741-1]
CTD; 5565; -.
DisGeNET; 5565; -.
EuPathDB; HostDB:ENSG00000131791.7; -.
GeneCards; PRKAB2; -.
HGNC; HGNC:9379; PRKAB2.
HPA; HPA044342; -.
MIM; 602741; gene.
neXtProt; NX_O43741; -.
OpenTargets; ENSG00000131791; -.
PharmGKB; PA33747; -.
eggNOG; KOG1616; Eukaryota.
eggNOG; ENOG410XRB3; LUCA.
GeneTree; ENSGT00390000001416; -.
HOGENOM; HOG000230597; -.
HOVERGEN; HBG050430; -.
KO; K07199; -.
OMA; QMGTINN; -.
OrthoDB; EOG091G0DZR; -.
PhylomeDB; O43741; -.
TreeFam; TF313827; -.
Reactome; R-HSA-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-HSA-1632852; Macroautophagy.
Reactome; R-HSA-163680; AMPK inhibits chREBP transcriptional activation activity.
Reactome; R-HSA-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
Reactome; R-HSA-2151209; Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
SignaLink; O43741; -.
SIGNOR; O43741; -.
ChiTaRS; PRKAB2; human.
EvolutionaryTrace; O43741; -.
GeneWiki; PRKAB2; -.
GenomeRNAi; 5565; -.
PRO; PR:O43741; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000131791; -.
CleanEx; HS_PRKAB2; -.
Genevisible; O43741; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0031588; C:nucleotide-activated protein kinase complex; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0007050; P:cell cycle arrest; TAS:Reactome.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:0006468; P:protein phosphorylation; IEA:GOC.
GO; GO:0042304; P:regulation of fatty acid biosynthetic process; TAS:Reactome.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR032640; AMPK1_CBM.
InterPro; IPR039160; AMPKB.
InterPro; IPR006828; ASC_dom.
InterPro; IPR037256; ASC_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
PANTHER; PTHR10343:SF80; PTHR10343:SF80; 1.
Pfam; PF16561; AMPK1_CBM; 1.
Pfam; PF04739; AMPKBI; 1.
SMART; SM01010; AMPKBI; 1.
SUPFAM; SSF160219; SSF160219; 1.
SUPFAM; SSF81296; SSF81296; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
Lipid metabolism; Phosphoprotein; Reference proteome.
CHAIN 1 272 5'-AMP-activated protein kinase subunit
beta-2.
/FTId=PRO_0000204368.
MOD_RES 39 39 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZH4}.
MOD_RES 40 40 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9QZH4}.
MOD_RES 69 69 Phosphoserine; by ULK1.
{ECO:0000250|UniProtKB:Q9QZH4}.
MOD_RES 95 95 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 108 108 Phosphoserine.
{ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 148 148 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 158 158 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 170 170 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 174 174 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QZH4}.
MOD_RES 184 184 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
VAR_SEQ 1 25 MGNTTSDRVSGERHGAKAARSEGAG -> MPRGRSTRSWWG
VRTTPACSASLTP (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055820.
VAR_SEQ 26 107 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055821.
MUTAGEN 235 235 H->A: Results in an AMPK enzyme that is
activable by phosphorylation but has
significantly increased rate of
dephosphorylation in phosphatase assays.
{ECO:0000269|PubMed:21399626}.
STRAND 76 83 {ECO:0000244|PDB:2F15}.
STRAND 90 94 {ECO:0000244|PDB:2F15}.
HELIX 95 97 {ECO:0000244|PDB:2F15}.
STRAND 112 129 {ECO:0000244|PDB:2F15}.
STRAND 132 134 {ECO:0000244|PDB:2F15}.
STRAND 141 143 {ECO:0000244|PDB:2F15}.
STRAND 149 155 {ECO:0000244|PDB:2F15}.
TURN 159 162 {ECO:0000244|PDB:2F15}.
STRAND 201 204 {ECO:0000244|PDB:2V8Q}.
HELIX 210 213 {ECO:0000244|PDB:4CFH}.
STRAND 214 217 {ECO:0000244|PDB:2V8Q}.
TURN 236 239 {ECO:0000244|PDB:2V92}.
STRAND 242 244 {ECO:0000244|PDB:4EAI}.
STRAND 250 259 {ECO:0000244|PDB:2V8Q}.
STRAND 262 271 {ECO:0000244|PDB:2V8Q}.
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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