ID AAKB1_HUMAN Reviewed; 270 AA. AC Q9Y478; Q9UBV0; Q9UE20; Q9UEX2; Q9Y6V8; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 214. DE RecName: Full=5'-AMP-activated protein kinase subunit beta-1; DE Short=AMPK subunit beta-1; DE Short=AMPKb; GN Name=PRKAB1; Synonyms=AMPK; 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]. RA Carling D.; RT "Non-catalytic beta and gamma subunits isoforms of the AMP-activated RT protein kinase."; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=9224708; DOI=10.1016/s0014-5793(97)00569-3; RA Stapleton D., Woollatt E., Mitchelhill K., Nicholl J.K., Fernandez C.S., RA Michell B.J., Witters L.A., Power D.A., Sutherland G.R., Kemp B.E.; RT "AMP-activated protein kinase isoenzyme family: subunit structure and RT chromosomal location."; RL FEBS Lett. 409:452-456(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RA Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V., RA Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M., RA Lathrop M., Cox R.D., Bell G.I.; RT "Transcription map of the 5cM region surrounding the hepatocyte nuclear RT factor-1a/MODY3 gene on chromosome 12."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Wang X., Yu L., Tu Q.; RT "Cloning and expression of the complete mRNA coding human AMP-activated RT protein kinase."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung, and Muscle; 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 INTERACTION WITH FNIP1. RX PubMed=17028174; DOI=10.1073/pnas.0603781103; RA Baba M., Hong S.-B., Sharma N., Warren M.B., Nickerson M.L., Iwamatsu A., RA Esposito D., Gillette W.K., Hopkins R.F. III, Hartley J.L., Furihata M., RA Oishi S., Zhen W., Burke T.R. Jr., Linehan W.M., Schmidt L.S., Zbar B.; RT "Folliculin encoded by the BHD gene interacts with a binding protein, RT FNIP1, and AMPK, and is involved in AMPK and mTOR signaling."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15552-15557(2006). RN [8] RP INTERACTION WITH FNIP2. RX PubMed=18403135; DOI=10.1016/j.gene.2008.02.022; RA Hasumi H., Baba M., Hong S.-B., Hasumi Y., Huang Y., Yao M., Valera V.A., RA Linehan W.M., Schmidt L.S.; RT "Identification and characterization of a novel folliculin-interacting RT protein FNIP2."; RL Gene 415:60-67(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4; SER-5; SER-6 AND SER-108, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-40 AND SER-108, AND RP IDENTIFICATION BY 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY RP 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-40; SER-108 AND RP THR-148, AND IDENTIFICATION BY 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-108, AND RP IDENTIFICATION BY 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 AND SER-108, AND RP IDENTIFICATION BY 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 [15] RP PHOSPHORYLATION BY ULK1. 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 [16] 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 [17] 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 [18] RP INTERACTION WITH PRKAA1 AND PRKAG1, MUTAGENESIS OF GLY-2, AND RP MYRISTOYLATION AT GLY-2. RX PubMed=21680840; DOI=10.1126/science.1200094; RA Oakhill J.S., Steel R., Chen Z.P., Scott J.W., Ling N., Tam S., Kemp B.E.; RT "AMPK is a direct adenylate charge-regulated protein kinase."; RL Science 332:1433-1435(2011). RN [19] 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 [20] 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-96 AND SER-108, AND RP IDENTIFICATION BY 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 [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-108, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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). 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). Interacts with FNIP1 and FNIP2. CC {ECO:0000269|PubMed:17028174, ECO:0000269|PubMed:18403135, CC ECO:0000269|PubMed:21680840}. CC -!- INTERACTION: CC Q9Y478; P62993: GRB2; NbExp=2; IntAct=EBI-719769, EBI-401755; CC Q9Y478; Q13131: PRKAA1; NbExp=9; IntAct=EBI-719769, EBI-1181405; CC Q9Y478; P54646: PRKAA2; NbExp=8; IntAct=EBI-719769, EBI-1383852; CC Q9Y478; P54619: PRKAG1; NbExp=12; IntAct=EBI-719769, EBI-1181439; CC Q9Y478; O75385: ULK1; NbExp=3; IntAct=EBI-719769, EBI-908831; CC Q9Y478; O70302: Cidea; Xeno; NbExp=4; IntAct=EBI-719769, EBI-7927848; CC -!- DOMAIN: The glycogen-binding domain may target AMPK to glycogen so that CC other factors like glycogen-bound debranching enzyme or protein CC phosphatases can directly affect AMPK activity. {ECO:0000250}. CC -!- PTM: Phosphorylated when associated with the catalytic subunit (PRKAA1 CC or PRKAA2). Phosphorylated by ULK1; leading to negatively regulate AMPK CC activity and suggesting the existence of a regulatory feedback loop CC between ULK1 and AMPK. {ECO:0000269|PubMed:21460634}. CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB71326.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=AAC98897.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44100/PRKAB1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ224515; CAA12024.1; -; mRNA. DR EMBL; Y12556; CAA73146.1; -; mRNA. DR EMBL; U83994; AAD09237.1; -; mRNA. DR EMBL; U87276; AAD00625.1; -; Genomic_DNA. DR EMBL; U87271; AAD00625.1; JOINED; Genomic_DNA. DR EMBL; U87272; AAD00625.1; JOINED; Genomic_DNA. DR EMBL; U87273; AAD00625.1; JOINED; Genomic_DNA. DR EMBL; U87274; AAD00625.1; JOINED; Genomic_DNA. DR EMBL; U87275; AAD00625.1; JOINED; Genomic_DNA. DR EMBL; AF022116; AAC98897.1; ALT_FRAME; mRNA. DR EMBL; AC002563; AAB71326.1; ALT_SEQ; Genomic_DNA. DR EMBL; BC001007; AAH01007.1; -; mRNA. DR EMBL; BC001056; AAH01056.1; -; mRNA. DR EMBL; BC001823; AAH01823.1; -; mRNA. DR EMBL; BC017671; AAH17671.1; -; mRNA. DR CCDS; CCDS9191.1; -. DR PIR; T09514; T09514. DR RefSeq; NP_006244.2; NM_006253.4. DR RefSeq; XP_005253966.1; XM_005253909.1. DR PDB; 4CFE; X-ray; 3.02 A; B/D=1-270. DR PDB; 4CFF; X-ray; 3.92 A; B/D=1-270. DR PDB; 4ZHX; X-ray; 2.99 A; B/D=1-270. DR PDB; 5EZV; X-ray; 2.99 A; B/D=1-270. DR PDB; 5ISO; X-ray; 2.63 A; B/D=1-270. DR PDB; 6B1U; X-ray; 2.77 A; B/D=1-270. DR PDB; 6C9F; X-ray; 2.92 A; B=68-270. DR PDB; 6C9G; X-ray; 2.70 A; B=67-270. DR PDB; 6C9H; X-ray; 2.65 A; B=68-270. DR PDB; 6C9J; X-ray; 3.05 A; B=68-270. DR PDB; 7MYJ; X-ray; 2.95 A; B/D=1-270. DR PDBsum; 4CFE; -. DR PDBsum; 4CFF; -. DR PDBsum; 4ZHX; -. DR PDBsum; 5EZV; -. DR PDBsum; 5ISO; -. DR PDBsum; 6B1U; -. DR PDBsum; 6C9F; -. DR PDBsum; 6C9G; -. DR PDBsum; 6C9H; -. DR PDBsum; 6C9J; -. DR PDBsum; 7MYJ; -. DR AlphaFoldDB; Q9Y478; -. DR SMR; Q9Y478; -. DR BioGRID; 111551; 103. DR ComplexPortal; CPX-5633; AMPK complex, alpha1-beta1-gamma1 variant. DR ComplexPortal; CPX-5786; AMPK complex, alpha1-beta1-gamma2 variant. DR ComplexPortal; CPX-5787; AMPK complex, alpha2-beta1-gamma1 variant. DR ComplexPortal; CPX-5842; AMPK complex, alpha1-beta1-gamma3 variant. DR ComplexPortal; CPX-5843; AMPK complex, alpha2-beta1-gamma3 variant. DR ComplexPortal; CPX-5844; AMPK complex, alpha2-beta1-gamma2 variant. DR CORUM; Q9Y478; -. DR DIP; DIP-39736N; -. DR IntAct; Q9Y478; 37. DR MINT; Q9Y478; -. DR STRING; 9606.ENSP00000441369; -. DR BindingDB; Q9Y478; -. DR ChEMBL; CHEMBL3847; -. DR DrugBank; DB00945; Acetylsalicylic acid. DR DrugBank; DB00131; Adenosine phosphate. DR DrugBank; DB12010; Fostamatinib. DR DrugBank; DB00331; Metformin. DR DrugBank; DB00273; Topiramate. DR DrugCentral; Q9Y478; -. DR GuidetoPHARMACOLOGY; 1543; -. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR iPTMnet; Q9Y478; -. DR PhosphoSitePlus; Q9Y478; -. DR SwissPalm; Q9Y478; -. DR BioMuta; PRKAB1; -. DR DMDM; 14194425; -. DR EPD; Q9Y478; -. DR jPOST; Q9Y478; -. DR MassIVE; Q9Y478; -. DR MaxQB; Q9Y478; -. DR PaxDb; 9606-ENSP00000229328; -. DR PeptideAtlas; Q9Y478; -. DR ProteomicsDB; 86122; -. DR Pumba; Q9Y478; -. DR Antibodypedia; 1328; 978 antibodies from 42 providers. DR DNASU; 5564; -. DR Ensembl; ENST00000229328.10; ENSP00000229328.5; ENSG00000111725.11. DR Ensembl; ENST00000541640.5; ENSP00000441369.1; ENSG00000111725.11. DR GeneID; 5564; -. DR KEGG; hsa:5564; -. DR MANE-Select; ENST00000229328.10; ENSP00000229328.5; NM_006253.5; NP_006244.2. DR UCSC; uc001txg.4; human. DR AGR; HGNC:9378; -. DR CTD; 5564; -. DR DisGeNET; 5564; -. DR GeneCards; PRKAB1; -. DR HGNC; HGNC:9378; PRKAB1. DR HPA; ENSG00000111725; Low tissue specificity. DR MIM; 602740; gene. DR neXtProt; NX_Q9Y478; -. DR OpenTargets; ENSG00000111725; -. DR PharmGKB; PA33746; -. DR VEuPathDB; HostDB:ENSG00000111725; -. DR eggNOG; KOG1616; Eukaryota. DR GeneTree; ENSGT00940000155307; -. DR HOGENOM; CLU_070949_2_0_1; -. DR InParanoid; Q9Y478; -. DR OMA; QPTVFRW; -. DR OrthoDB; 120305at2759; -. DR PhylomeDB; Q9Y478; -. DR TreeFam; TF313827; -. DR BRENDA; 2.7.11.31; 2681. DR PathwayCommons; Q9Y478; -. DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane. DR Reactome; R-HSA-1632852; Macroautophagy. 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; Q9Y478; -. DR SIGNOR; Q9Y478; -. DR BioGRID-ORCS; 5564; 19 hits in 1176 CRISPR screens. DR ChiTaRS; PRKAB1; human. DR GeneWiki; PRKAB1; -. DR GenomeRNAi; 5564; -. DR Pharos; Q9Y478; Tchem. DR PRO; PR:Q9Y478; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9Y478; Protein. DR Bgee; ENSG00000111725; Expressed in metanephros cortex and 178 other cell types or tissues. DR ExpressionAtlas; Q9Y478; baseline and differential. 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; IPI:ComplexPortal. DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal. DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB. 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:0035878; P:nail development; IEA:Ensembl. DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd02859; E_set_AMPKbeta_like_N; 1. DR Gene3D; 6.20.250.60; -; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR IDEAL; IID00686; -. DR InterPro; IPR032640; AMPK1_CBM. 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; 5'-AMP-ACTIVATED PROTEIN KINASE , BETA SUBUNIT; 1. DR PANTHER; PTHR10343:SF96; 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-1; 1. DR Pfam; PF16561; AMPK1_CBM; 1. DR Pfam; PF04739; AMPKBI; 1. DR SMART; SM01010; AMPKBI; 1. DR SUPFAM; SSF160219; AMPKBI-like; 1. DR SUPFAM; SSF81296; E set domains; 1. DR Genevisible; Q9Y478; HS. PE 1: Evidence at protein level; KW 3D-structure; Fatty acid biosynthesis; Fatty acid metabolism; KW Lipid biosynthesis; Lipid metabolism; Lipoprotein; Myristate; KW Phosphoprotein; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..270 FT /note="5'-AMP-activated protein kinase subunit beta-1" FT /id="PRO_0000204363" FT REGION 1..43 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 68..163 FT /note="Glycogen-binding domain" FT /evidence="ECO:0000250" FT COMPBIAS 10..43 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 4 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18088087" FT MOD_RES 5 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087" FT MOD_RES 6 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087" FT MOD_RES 19 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195" FT MOD_RES 24 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P80386" FT MOD_RES 25 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P80386" FT MOD_RES 40 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 96 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 101 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P80386" FT MOD_RES 108 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 148 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19369195" FT MOD_RES 182 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9R078" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000269|PubMed:21680840" FT MUTAGEN 2 FT /note="G->A: Abolishes myristoylation and AMP-enhanced FT phosphorylation of PRKAA1 or PRKAA2." FT /evidence="ECO:0000269|PubMed:21680840" FT CONFLICT 10 FT /note="A -> G (in Ref. 2; CAA73146 and 4; AAC98897)" FT /evidence="ECO:0000305" FT CONFLICT 15 FT /note="G -> A (in Ref. 1; CAA12024)" FT /evidence="ECO:0000305" FT CONFLICT 20 FT /note="P -> A (in Ref. 2; CAA73146 and 4; AAC98897)" FT /evidence="ECO:0000305" FT CONFLICT 22 FT /note="R -> K (in Ref. 3; AAD09237/AAD00625)" FT /evidence="ECO:0000305" FT CONFLICT 56 FT /note="E -> Y (in Ref. 3; AAD09237/AAD00625)" FT /evidence="ECO:0000305" FT STRAND 79..84 FT /evidence="ECO:0007829|PDB:5ISO" FT STRAND 91..95 FT /evidence="ECO:0007829|PDB:5ISO" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:5ISO" FT STRAND 106..108 FT /evidence="ECO:0007829|PDB:6C9H" FT STRAND 112..117 FT /evidence="ECO:0007829|PDB:5ISO" FT STRAND 120..129 FT /evidence="ECO:0007829|PDB:5ISO" FT STRAND 132..134 FT /evidence="ECO:0007829|PDB:5ISO" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:6C9G" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:5ISO" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:4CFE" FT STRAND 149..155 FT /evidence="ECO:0007829|PDB:5ISO" FT HELIX 157..159 FT /evidence="ECO:0007829|PDB:5ISO" FT HELIX 162..176 FT /evidence="ECO:0007829|PDB:5ISO" FT HELIX 208..211 FT /evidence="ECO:0007829|PDB:5ISO" FT HELIX 214..216 FT /evidence="ECO:0007829|PDB:5ISO" FT STRAND 221..223 FT /evidence="ECO:0007829|PDB:7MYJ" FT HELIX 233..235 FT /evidence="ECO:0007829|PDB:5ISO" FT STRAND 238..245 FT /evidence="ECO:0007829|PDB:6C9H" FT STRAND 248..257 FT /evidence="ECO:0007829|PDB:5ISO" FT STRAND 260..269 FT /evidence="ECO:0007829|PDB:5ISO" SQ 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 //