AAKB1_HUMAN
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 03-AUG-2022, entry version 205.
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="http://atlasgeneticsoncology.org/Genes/PRKAB1ID44100ch12q24.html";
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 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 AlphaFoldDB; Q9Y478; -.
DR SMR; Q9Y478; -.
DR BioGRID; 111551; 92.
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; 35.
DR MINT; Q9Y478; -.
DR STRING; 9606.ENSP00000229328; -.
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; Q9Y478; -.
DR PeptideAtlas; Q9Y478; -.
DR PRIDE; Q9Y478; -.
DR ProteomicsDB; 86122; -.
DR Antibodypedia; 1328; 846 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 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 OMA; NDRAPTQ; -.
DR OrthoDB; 956412at2759; -.
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 1088 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 176 other tissues.
DR ExpressionAtlas; Q9Y478; baseline and differential.
DR Genevisible; Q9Y478; 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; 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:0050790; P:regulation of catalytic activity; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR IDEAL; IID00686; -.
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:SF89; PTHR10343:SF89; 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; 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:5EZV"
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
