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5'-AMP-activated protein kinase subunit beta-1 (AMPK subunit beta-1) (AMPKb)

 AAKB1_HUMAN             Reviewed;         270 AA.
Q9Y478; Q9UBV0; Q9UE20; Q9UEX2; Q9Y6V8;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
27-SEP-2017, entry version 174.
RecName: Full=5'-AMP-activated protein kinase subunit beta-1;
Short=AMPK subunit beta-1;
Short=AMPKb;
Name=PRKAB1; Synonyms=AMPK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Carling D.;
"Non-catalytic beta and gamma subunits isoforms of the AMP-activated
protein kinase.";
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=9224708; DOI=10.1016/S0014-5793(97)00569-3;
Stapleton D., Woollatt E., Mitchelhill K., Nicholl J.K.,
Fernandez C.S., Michell B.J., Witters L.A., Power D.A.,
Sutherland G.R., Kemp B.E.;
"AMP-activated protein kinase isoenzyme family: subunit structure and
chromosomal location.";
FEBS Lett. 409:452-456(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V.,
Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M.,
Lathrop M., Cox R.D., Bell G.I.;
"Transcription map of the 5cM region surrounding the hepatocyte
nuclear factor-1a/MODY3 gene on chromosome 12.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Wang X., Yu L., Tu Q.;
"Cloning and expression of the complete mRNA coding human AMP-
activated protein kinase.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Muscle;
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]
INTERACTION WITH FNIP1.
PubMed=17028174; DOI=10.1073/pnas.0603781103;
Baba M., Hong S.-B., Sharma N., Warren M.B., Nickerson M.L.,
Iwamatsu A., Esposito D., Gillette W.K., Hopkins R.F. III,
Hartley J.L., Furihata M., Oishi S., Zhen W., Burke T.R. Jr.,
Linehan W.M., Schmidt L.S., Zbar B.;
"Folliculin encoded by the BHD gene interacts with a binding protein,
FNIP1, and AMPK, and is involved in AMPK and mTOR signaling.";
Proc. Natl. Acad. Sci. U.S.A. 103:15552-15557(2006).
[8]
INTERACTION WITH FNIP2.
PubMed=18403135; DOI=10.1016/j.gene.2008.02.022;
Hasumi H., Baba M., Hong S.-B., Hasumi Y., Huang Y., Yao M.,
Valera V.A., Linehan W.M., Schmidt L.S.;
"Identification and characterization of a novel folliculin-interacting
protein FNIP2.";
Gene 415:60-67(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4; SER-5; SER-6 AND
SER-108, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-40 AND 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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, 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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-40; SER-108 AND
THR-148, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 AND SER-108, 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).
[15]
PHOSPHORYLATION BY ULK1.
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).
[16]
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).
[17]
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).
[18]
INTERACTION WITH PRKAA1 AND PRKAG1, MUTAGENESIS OF GLY-2, AND
MYRISTOYLATION AT GLY-2.
PubMed=21680840; DOI=10.1126/science.1200094;
Oakhill J.S., Steel R., Chen Z.P., Scott J.W., Ling N., Tam S.,
Kemp B.E.;
"AMPK is a direct adenylate charge-regulated protein kinase.";
Science 332:1433-1435(2011).
[19]
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).
[20]
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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-96 AND 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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-108, 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).
-!- 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). Interacts with
FNIP1 and FNIP2. {ECO:0000269|PubMed:17028174,
ECO:0000269|PubMed:18403135, ECO:0000269|PubMed:21680840}.
-!- INTERACTION:
P16152:CBR1; NbExp=2; IntAct=EBI-719769, EBI-351348;
O70302:Cidea (xeno); NbExp=4; IntAct=EBI-719769, EBI-7927848;
P62993:GRB2; NbExp=2; IntAct=EBI-719769, EBI-401755;
Q13131:PRKAA1; NbExp=6; IntAct=EBI-719769, EBI-1181405;
P54646:PRKAA2; NbExp=3; IntAct=EBI-719769, EBI-1383852;
O43741:PRKAB2; NbExp=2; IntAct=EBI-719769, EBI-1053424;
P54619:PRKAG1; NbExp=8; IntAct=EBI-719769, EBI-1181439;
-!- DOMAIN: The glycogen-binding domain may target AMPK to glycogen so
that other factors like glycogen-bound debranching enzyme or
protein phosphatases can directly affect AMPK activity.
{ECO:0000250}.
-!- PTM: Phosphorylated when associated with the catalytic subunit
(PRKAA1 or PRKAA2). Phosphorylated by ULK1; leading to negatively
regulate AMPK activity and suggesting the existence of a
regulatory feedback loop between ULK1 and AMPK.
{ECO:0000269|PubMed:21460634}.
-!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta
subunit family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB71326.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAC98897.1; Type=Frameshift; Positions=245; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PRKAB1ID44100ch12q24.html";
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EMBL; AJ224515; CAA12024.1; -; mRNA.
EMBL; Y12556; CAA73146.1; -; mRNA.
EMBL; U83994; AAD09237.1; -; mRNA.
EMBL; U87276; AAD00625.1; -; Genomic_DNA.
EMBL; U87271; AAD00625.1; JOINED; Genomic_DNA.
EMBL; U87272; AAD00625.1; JOINED; Genomic_DNA.
EMBL; U87273; AAD00625.1; JOINED; Genomic_DNA.
EMBL; U87274; AAD00625.1; JOINED; Genomic_DNA.
EMBL; U87275; AAD00625.1; JOINED; Genomic_DNA.
EMBL; AF022116; AAC98897.1; ALT_FRAME; mRNA.
EMBL; AC002563; AAB71326.1; ALT_SEQ; Genomic_DNA.
EMBL; BC001007; AAH01007.1; -; mRNA.
EMBL; BC001056; AAH01056.1; -; mRNA.
EMBL; BC001823; AAH01823.1; -; mRNA.
EMBL; BC017671; AAH17671.1; -; mRNA.
CCDS; CCDS9191.1; -.
PIR; T09514; T09514.
RefSeq; NP_006244.2; NM_006253.4.
RefSeq; XP_005253966.1; XM_005253909.1.
UniGene; Hs.741184; -.
PDB; 4CFE; X-ray; 3.02 A; B/D=1-270.
PDB; 4CFF; X-ray; 3.92 A; B/D=1-270.
PDB; 4ZHX; X-ray; 2.99 A; B/D=1-270.
PDB; 5EZV; X-ray; 2.99 A; B/D=1-270.
PDB; 5ISO; X-ray; 2.63 A; B/D=1-270.
PDBsum; 4CFE; -.
PDBsum; 4CFF; -.
PDBsum; 4ZHX; -.
PDBsum; 5EZV; -.
PDBsum; 5ISO; -.
ProteinModelPortal; Q9Y478; -.
SMR; Q9Y478; -.
BioGrid; 111551; 59.
DIP; DIP-39736N; -.
IntAct; Q9Y478; 163.
MINT; MINT-1400840; -.
STRING; 9606.ENSP00000229328; -.
BindingDB; Q9Y478; -.
ChEMBL; CHEMBL3847; -.
DrugBank; DB00945; Acetylsalicylic acid.
DrugBank; DB00131; Adenosine monophosphate.
DrugBank; DB00331; Metformin.
GuidetoPHARMACOLOGY; 1543; -.
CAZy; CBM48; Carbohydrate-Binding Module Family 48.
iPTMnet; Q9Y478; -.
PhosphoSitePlus; Q9Y478; -.
SwissPalm; Q9Y478; -.
BioMuta; PRKAB1; -.
DMDM; 14194425; -.
EPD; Q9Y478; -.
MaxQB; Q9Y478; -.
PaxDb; Q9Y478; -.
PeptideAtlas; Q9Y478; -.
PRIDE; Q9Y478; -.
Ensembl; ENST00000229328; ENSP00000229328; ENSG00000111725.
Ensembl; ENST00000541640; ENSP00000441369; ENSG00000111725.
GeneID; 5564; -.
KEGG; hsa:5564; -.
UCSC; uc001txg.4; human.
CTD; 5564; -.
DisGeNET; 5564; -.
EuPathDB; HostDB:ENSG00000111725.10; -.
GeneCards; PRKAB1; -.
HGNC; HGNC:9378; PRKAB1.
HPA; CAB005058; -.
HPA; HPA004247; -.
MIM; 602740; gene.
neXtProt; NX_Q9Y478; -.
OpenTargets; ENSG00000111725; -.
PharmGKB; PA33746; -.
eggNOG; KOG1616; Eukaryota.
eggNOG; ENOG410XRB3; LUCA.
GeneTree; ENSGT00390000001416; -.
HOGENOM; HOG000230597; -.
HOVERGEN; HBG050430; -.
KO; K07199; -.
OMA; KCSDMSE; -.
OrthoDB; EOG091G0DZR; -.
PhylomeDB; Q9Y478; -.
TreeFam; TF313827; -.
Reactome; R-HSA-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-HSA-1632852; Macroautophagy.
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; Q9Y478; -.
SIGNOR; Q9Y478; -.
GeneWiki; PRKAB1; -.
GenomeRNAi; 5564; -.
PRO; PR:Q9Y478; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111725; -.
CleanEx; HS_PRKAB1; -.
ExpressionAtlas; Q9Y478; baseline and differential.
Genevisible; Q9Y478; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0031588; C:nucleotide-activated protein kinase complex; IEA:Ensembl.
GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:Ensembl.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
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:0035878; P:nail development; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0016241; P:regulation of macroautophagy; TAS:Reactome.
GO; GO:0045859; P:regulation of protein kinase activity; IEA:InterPro.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR032640; AMPK1_CBM.
InterPro; IPR030080; AMPK_beta-1.
InterPro; IPR006828; ASC_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
PANTHER; PTHR10343:SF67; PTHR10343:SF67; 1.
Pfam; PF16561; AMPK1_CBM; 1.
Pfam; PF04739; AMPKBI; 1.
SMART; SM01010; AMPKBI; 1.
SUPFAM; SSF81296; SSF81296; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Fatty acid biosynthesis;
Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
Lipoprotein; Myristate; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed.
CHAIN 2 270 5'-AMP-activated protein kinase subunit
beta-1.
/FTId=PRO_0000204363.
REGION 68 163 Glycogen-binding domain. {ECO:0000250}.
MOD_RES 4 4 Phosphothreonine.
{ECO:0000244|PubMed:18088087}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000244|PubMed:18088087}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000244|PubMed:18088087}.
MOD_RES 19 19 Phosphothreonine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 24 24 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:P80386}.
MOD_RES 25 25 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:P80386}.
MOD_RES 40 40 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 96 96 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 101 101 Phosphoserine.
{ECO:0000250|UniProtKB:P80386}.
MOD_RES 108 108 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 148 148 Phosphothreonine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 182 182 Phosphoserine.
{ECO:0000250|UniProtKB:Q9R078}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:21680840}.
MUTAGEN 2 2 G->A: Abolishes myristoylation and AMP-
enhanced phosphorylation of PRKAA1 or
PRKAA2. {ECO:0000269|PubMed:21680840}.
CONFLICT 10 10 A -> G (in Ref. 2; CAA73146 and 4;
AAC98897). {ECO:0000305}.
CONFLICT 15 15 G -> A (in Ref. 1; CAA12024).
{ECO:0000305}.
CONFLICT 20 20 P -> A (in Ref. 2; CAA73146 and 4;
AAC98897). {ECO:0000305}.
CONFLICT 22 22 R -> K (in Ref. 3; AAD09237/AAD00625).
{ECO:0000305}.
CONFLICT 56 56 E -> Y (in Ref. 3; AAD09237/AAD00625).
{ECO:0000305}.
STRAND 79 84 {ECO:0000244|PDB:5ISO}.
STRAND 91 95 {ECO:0000244|PDB:5ISO}.
HELIX 96 98 {ECO:0000244|PDB:5ISO}.
STRAND 106 110 {ECO:0000244|PDB:4ZHX}.
STRAND 112 117 {ECO:0000244|PDB:5ISO}.
STRAND 120 129 {ECO:0000244|PDB:5ISO}.
STRAND 132 134 {ECO:0000244|PDB:5ISO}.
STRAND 137 139 {ECO:0000244|PDB:4ZHX}.
STRAND 141 143 {ECO:0000244|PDB:5ISO}.
STRAND 145 147 {ECO:0000244|PDB:4CFE}.
STRAND 149 155 {ECO:0000244|PDB:5ISO}.
HELIX 157 159 {ECO:0000244|PDB:5ISO}.
HELIX 162 176 {ECO:0000244|PDB:5ISO}.
HELIX 208 211 {ECO:0000244|PDB:5ISO}.
HELIX 214 216 {ECO:0000244|PDB:5ISO}.
STRAND 221 223 {ECO:0000244|PDB:5EZV}.
HELIX 233 235 {ECO:0000244|PDB:5ISO}.
STRAND 238 241 {ECO:0000244|PDB:4ZHX}.
STRAND 248 257 {ECO:0000244|PDB:5ISO}.
STRAND 260 269 {ECO:0000244|PDB:5ISO}.
SEQUENCE 270 AA; 30382 MW; F0BCAA94D5BC15FC CRC64;
MGNTSSERAA LERHGGHKTP RRDSSGGTKD GDRPKILMDS PEDADLFHSE EIKAPEKEEF
LAWQHDLEVN DKAPAQARPT VFRWTGGGKE VYLSGSFNNW SKLPLTRSHN NFVAILDLPE
GEHQYKFFVD GQWTHDPSEP IVTSQLGTVN NIIQVKKTDF EVFDALMVDS QKCSDVSELS
SSPPGPYHQE PYVCKPEERF RAPPILPPHL LQVILNKDTG ISCDPALLPE PNHVMLNHLY
ALSIKDGVMV LSATHRYKKK YVTTLLYKPI


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