RPTOR_HUMAN
ID RPTOR_HUMAN Reviewed; 1335 AA.
AC Q8N122; B2RN36; C6KEF2; F5H7J5; Q8N4V9; Q8TB32; Q9P2P3;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Regulatory-associated protein of mTOR {ECO:0000305};
DE Short=Raptor;
DE AltName: Full=p150 target of rapamycin (TOR)-scaffold protein;
GN Name=RPTOR {ECO:0000312|HGNC:HGNC:30287}; Synonyms=KIAA1303, RAPTOR;
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], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION
RP WITH 4EBP1 AND RPS6KB1.
RX PubMed=12150925; DOI=10.1016/s0092-8674(02)00808-5;
RA Kim D.-H., Sarbassov D.D., Ali S.M., King J.E., Latek R.R.,
RA Erdjument-Bromage H., Tempst P., Sabatini D.M.;
RT "mTOR interacts with raptor to form a nutrient-sensitive complex that
RT signals to the growth machinery.";
RL Cell 110:163-175(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH 4EBP1 AND
RP RPS6KB1.
RX PubMed=12150926; DOI=10.1016/s0092-8674(02)00833-4;
RA Hara K., Maruki Y., Long X., Yoshino K., Oshiro N., Hidayat S.,
RA Tokunaga C., Avruch J., Yonezawa K.;
RT "Raptor, a binding partner of target of rapamycin (TOR), mediates TOR
RT action.";
RL Cell 110:177-189(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 995-1135 (ISOFORM 1).
RC TISSUE=Brain, Placenta, and Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 217-1335.
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 488-594 (ISOFORM 3), AND TISSUE SPECIFICITY
RP (ISOFORM 3).
RX PubMed=19388141; DOI=10.1016/j.mrfmmm.2009.01.001;
RA Sun C., Southard C., Di Rienzo A.;
RT "Characterization of a novel splicing variant in the RAPTOR gene.";
RL Mutat. Res. 662:88-92(2009).
RN [8]
RP INTERACTION WITH MTOR AND MLST8, IDENTIFICATION IN THE TORC1 COMPLEX, AND
RP TISSUE SPECIFICITY.
RX PubMed=12408816; DOI=10.1016/s1097-2765(02)00636-6;
RA Loewith R., Jacinto E., Wullschleger S., Lorberg A., Crespo J.L.,
RA Bonenfant D., Oppliger W., Jenoe P., Hall M.N.;
RT "Two TOR complexes, only one of which is rapamycin sensitive, have distinct
RT roles in cell growth control.";
RL Mol. Cell 10:457-468(2002).
RN [9]
RP INTERACTION WITH EIF4EBP1.
RX PubMed=12747827; DOI=10.1016/s0960-9822(03)00329-4;
RA Schalm S.S., Fingar D.C., Sabatini D.M., Blenis J.;
RT "TOS motif-mediated raptor binding regulates 4E-BP1 multisite
RT phosphorylation and function.";
RL Curr. Biol. 13:797-806(2003).
RN [10]
RP DISSOCIATION OF COMPLEX BY RAPAMYCIN.
RX PubMed=15066126; DOI=10.1111/j.1356-9597.2004.00727.x;
RA Oshiro N., Yoshino K., Hidayat S., Tokunaga C., Hara K., Eguchi S.,
RA Avruch J., Yonezawa K.;
RT "Dissociation of raptor from mTOR is a mechanism of rapamycin-induced
RT inhibition of mTOR function.";
RL Genes Cells 9:359-366(2004).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [13]
RP INTERACTION WITH AKT1S1.
RX PubMed=17386266; DOI=10.1016/j.molcel.2007.03.003;
RA Sancak Y., Thoreen C.C., Peterson T.R., Lindquist R.A., Kang S.A.,
RA Spooner E., Carr S.A., Sabatini D.M.;
RT "PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase.";
RL Mol. Cell 25:903-915(2007).
RN [14]
RP PHOSPHORYLATION AT SER-719; SER-721 AND SER-722.
RX PubMed=18722121; DOI=10.1016/j.cub.2008.07.078;
RA Carriere A., Cargnello M., Julien L.A., Gao H., Bonneil E., Thibault P.,
RA Roux P.P.;
RT "Oncogenic MAPK signaling stimulates mTORC1 activity by promoting RSK-
RT mediated raptor phosphorylation.";
RL Curr. Biol. 18:1269-1277(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [16]
RP PHOSPHORYLATION AT SER-722 AND SER-792, MUTAGENESIS OF SER-722 AND SER-792,
RP AND INTERACTION WITH 14-3-3.
RX PubMed=18439900; DOI=10.1016/j.molcel.2008.03.003;
RA Gwinn D.M., Shackelford D.B., Egan D.F., Mihaylova M.M., Mery A.,
RA Vasquez D.S., Turk B.E., Shaw R.J.;
RT "AMPK phosphorylation of raptor mediates a metabolic checkpoint.";
RL Mol. Cell 30:214-226(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-877, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-719; SER-859; SER-863 AND
RP SER-877, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
RP INTERACTION WITH ULK1.
RX PubMed=19211835; DOI=10.1091/mbc.e08-12-1248;
RA Hosokawa N., Hara T., Kaizuka T., Kishi C., Takamura A., Miura Y.,
RA Iemura S., Natsume T., Takehana K., Yamada N., Guan J.L., Oshiro N.,
RA Mizushima N.;
RT "Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex
RT required for autophagy.";
RL Mol. Biol. Cell 20:1981-1991(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-877, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859; SER-863 AND SER-877, 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 [23]
RP SUBCELLULAR LOCATION.
RX PubMed=20381137; DOI=10.1016/j.cell.2010.02.024;
RA Sancak Y., Bar-Peled L., Zoncu R., Markhard A.L., Nada S., Sabatini D.M.;
RT "Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is
RT necessary for its activation by amino acids.";
RL Cell 141:290-303(2010).
RN [24]
RP PHOSPHORYLATION AT SER-696; THR-706; SER-855; SER-859; SER-863 AND SER-877.
RX PubMed=19864431; DOI=10.1074/jbc.m109.029637;
RA Foster K.G., Acosta-Jaquez H.A., Romeo Y., Ekim B., Soliman G.A.,
RA Carriere A., Roux P.P., Ballif B.A., Fingar D.C.;
RT "Regulation of mTOR complex 1 (mTORC1) by raptor Ser863 and multisite
RT phosphorylation.";
RL J. Biol. Chem. 285:80-94(2010).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859; SER-863 AND SER-877, 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 [26]
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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863 AND SER-877, AND
RP IDENTIFICATION BY 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 [28]
RP INTERACTION WITH HTR6.
RX PubMed=23027611; DOI=10.1002/emmm.201201410;
RA Meffre J., Chaumont-Dubel S., Mannoury la Cour C., Loiseau F., Watson D.J.,
RA Dekeyne A., Seveno M., Rivet J.M., Gaven F., Deleris P., Herve D.,
RA Fone K.C., Bockaert J., Millan M.J., Marin P.;
RT "5-HT(6) receptor recruitment of mTOR as a mechanism for perturbed
RT cognition in schizophrenia.";
RL EMBO Mol. Med. 4:1043-1056(2012).
RN [29]
RP PHOSPHORYLATION AT SER-696; THR-706 AND SER-863.
RX PubMed=22493283; DOI=10.1074/jbc.m111.326538;
RA Kwak D., Choi S., Jeong H., Jang J.H., Lee Y., Jeon H., Lee M.N., Noh J.,
RA Cho K., Yoo J.S., Hwang D., Suh P.G., Ryu S.H.;
RT "Osmotic stress regulates mammalian target of rapamycin (mTOR) complex 1
RT via c-Jun N-terminal Kinase (JNK)-mediated Raptor protein
RT phosphorylation.";
RL J. Biol. Chem. 287:18398-18407(2012).
RN [30]
RP INTERACTION WITH G3BP1 AND SPAG5, AND SUBCELLULAR LOCATION.
RX PubMed=23953116; DOI=10.1016/j.cell.2013.07.031;
RA Thedieck K., Holzwarth B., Prentzell M.T., Boehlke C., Klasener K., Ruf S.,
RA Sonntag A.G., Maerz L., Grellscheid S.N., Kremmer E., Nitschke R.,
RA Kuehn E.W., Jonker J.W., Groen A.K., Reth M., Hall M.N., Baumeister R.;
RT "Inhibition of mTORC1 by astrin and stress granules prevents apoptosis in
RT cancer cells.";
RL Cell 154:859-874(2013).
RN [31]
RP INTERACTION WITH PIH1D1.
RX PubMed=24036451; DOI=10.1016/j.febslet.2013.09.001;
RA Kamano Y., Saeki M., Egusa H., Kakihara Y., Houry W.A., Yatani H.,
RA Kamisaki Y.;
RT "PIH1D1 interacts with mTOR complex 1 and enhances ribosome RNA
RT transcription.";
RL FEBS Lett. 587:3303-3308(2013).
RN [32]
RP FUNCTION IN CILIOGENESIS.
RX PubMed=23727834; DOI=10.1093/hmg/ddt253;
RA Cardenas-Rodriguez M., Irigoin F., Osborn D.P., Gascue C., Katsanis N.,
RA Beales P.L., Badano J.L.;
RT "The Bardet-Biedl syndrome-related protein CCDC28B modulates mTORC2
RT function and interacts with SIN1 to control cilia length independently of
RT the mTOR complex.";
RL Hum. Mol. Genet. 22:4031-4042(2013).
RN [33]
RP INTERACTION WITH BRAT1.
RX PubMed=25657994;
RA So E.Y., Ouchi T.;
RT "The potential role of BRCA1-associated ATM activator-1 (BRAT1) in
RT regulation of mTOR.";
RL J. Cancer Biol. Res. 1:0-0(2013).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696; SER-719; SER-722;
RP SER-859; SER-863; THR-865 AND SER-877, AND IDENTIFICATION BY MASS
RP 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 [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-738 AND SER-877, 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).
RN [36]
RP INTERACTION WITH LARP1 AND THE MTORC1 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=25940091; DOI=10.1074/jbc.m114.621730;
RA Fonseca B.D., Zakaria C., Jia J.J., Graber T.E., Svitkin Y., Tahmasebi S.,
RA Healy D., Hoang H.D., Jensen J.M., Diao I.T., Lussier A., Dajadian C.,
RA Padmanabhan N., Wang W., Matta-Camacho E., Hearnden J., Smith E.M.,
RA Tsukumo Y., Yanagiya A., Morita M., Petroulakis E., Gonzalez J.L.,
RA Hernandez G., Alain T., Damgaard C.K.;
RT "La-related protein 1 (LARP1) represses terminal oligopyrimidine (TOP) mRNA
RT translation downstream of mTOR complex 1 (mTORC1).";
RL J. Biol. Chem. 290:15996-16020(2015).
RN [37]
RP INTERACTION WITH WAC.
RX PubMed=26812014; DOI=10.1016/j.devcel.2015.12.019;
RA David-Morrison G., Xu Z., Rui Y.N., Charng W.L., Jaiswal M., Yamamoto S.,
RA Xiong B., Zhang K., Sandoval H., Duraine L., Zuo Z., Zhang S., Bellen H.J.;
RT "WAC regulates mTOR activity by acting as an adaptor for the TTT and
RT Pontin/Reptin complexes.";
RL Dev. Cell 36:139-151(2016).
RN [38]
RP INTERACTION WITH VACCINIA VIRUS PROTEIN F17.
RX PubMed=30078703; DOI=10.1016/j.cell.2018.06.053;
RA Meade N., Furey C., Li H., Verma R., Chai Q., Rollins M.G., DiGiuseppe S.,
RA Naghavi M.H., Walsh D.;
RT "Poxviruses Evade Cytosolic Sensing through Disruption of an mTORC1-mTORC2
RT Regulatory Circuit.";
RL Cell 0:0-0(2018).
RN [39]
RP INTERACTION WITH SIK3.
RX PubMed=30232230; DOI=10.1126/scitranslmed.aat9356;
RA Csukasi F., Duran I., Barad M., Barta T., Gudernova I., Trantirek L.,
RA Martin J.H., Kuo C.Y., Woods J., Lee H., Cohn D.H., Krejci P., Krakow D.;
RT "The PTH/PTHrP-SIK3 pathway affects skeletogenesis through altered mTOR
RT signaling.";
RL Sci. Transl. Med. 10:0-0(2018).
CC -!- FUNCTION: Involved in the control of the mammalian target of rapamycin
CC complex 1 (mTORC1) activity which regulates cell growth and survival,
CC and autophagy in response to nutrient and hormonal signals; functions
CC as a scaffold for recruiting mTORC1 substrates. mTORC1 is activated in
CC response to growth factors or amino acids. Growth factor-stimulated
CC mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-
CC TSC2, which leads to the activation of the RHEB GTPase that potently
CC activates the protein kinase activity of mTORC1. Amino acid-signaling
CC to mTORC1 requires its relocalization to the lysosomes mediated by the
CC Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates
CC protein synthesis by phosphorylating key regulators of mRNA translation
CC and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it
CC from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1
CC phosphorylates and activates S6K1 at 'Thr-389', which then promotes
CC protein synthesis by phosphorylating PDCD4 and targeting it for
CC degradation. Involved in ciliogenesis. mTORC1 complex in excitatory
CC neuronal transmission is required for the prosocial behavior induced by
CC the psychoactive substance lysergic acid diethylamide (LSD) (By
CC similarity). {ECO:0000250|UniProtKB:Q8K4Q0,
CC ECO:0000269|PubMed:12150925, ECO:0000269|PubMed:12150926,
CC ECO:0000269|PubMed:23727834}.
CC -!- SUBUNIT: Part of the mammalian target of rapamycin complex 1 (mTORC1)
CC which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR
CC (PubMed:12150925, PubMed:12408816, PubMed:17386266, PubMed:25940091).
CC mTORC1 binds to and is inhibited by FKBP12-rapamycin (PubMed:12408816,
CC PubMed:15066126). Binds directly to 4EBP1 and RPS6KB1 independently of
CC its association with MTOR (PubMed:12150925, PubMed:12150926). Binds
CC preferentially to poorly or non-phosphorylated forms of EIF4EBP1, and
CC this binding is critical to the ability of MTOR to catalyze
CC phosphorylation (PubMed:12747827). Forms a complex with MTOR under both
CC leucine-rich and -poor conditions. Interacts with ULK1 in a nutrient-
CC dependent manner; the interaction is reduced during starvation
CC (PubMed:19211835). Interacts (when phosphorylated by AMPK) with 14-3-3
CC protein, leading to inhibition of its activity (PubMed:18439900).
CC Interacts with SPAG5; SPAG5 competes with MTOR for RPTOR-binding,
CC resulting in decreased mTORC1 formation. Interacts with WAC; WAC
CC positively regulates MTOR activity by promoting the assembly of the TTT
CC complex composed of TELO2, TTI1 and TTI2 and the RUVBL complex composed
CC of RUVBL1 and RUVBL2 into the TTT-RUVBL complex which leads to the
CC dimerization of the mTORC1 complex and its subsequent activation
CC (PubMed:26812014). Interacts with G3BP1. The complex formed with G3BP1
CC AND SPAG5 is increased by oxidative stress (PubMed:23953116). Interacts
CC with HTR6 (PubMed:23027611). Interacts with PIH1D1 (PubMed:24036451).
CC Interacts with LARP1 (PubMed:25940091). Interacts with BRAT1
CC (PubMed:25657994). Interacts with SIK3 (PubMed:30232230).
CC {ECO:0000269|PubMed:12150925, ECO:0000269|PubMed:12150926,
CC ECO:0000269|PubMed:12408816, ECO:0000269|PubMed:12747827,
CC ECO:0000269|PubMed:17386266, ECO:0000269|PubMed:18439900,
CC ECO:0000269|PubMed:19211835, ECO:0000269|PubMed:23027611,
CC ECO:0000269|PubMed:23953116, ECO:0000269|PubMed:24036451,
CC ECO:0000269|PubMed:25657994, ECO:0000269|PubMed:25940091,
CC ECO:0000269|PubMed:26812014, ECO:0000269|PubMed:30232230}.
CC -!- SUBUNIT: (Microbial infection) Interacts with vaccinia virus protein
CC F17; this interaction dysregulates mTOR. {ECO:0000269|PubMed:30078703}.
CC -!- INTERACTION:
CC Q8N122; Q13541: EIF4EBP1; NbExp=5; IntAct=EBI-1567928, EBI-74090;
CC Q8N122; Q13283: G3BP1; NbExp=4; IntAct=EBI-1567928, EBI-1047359;
CC Q8N122; Q8WUA4: GTF3C2; NbExp=3; IntAct=EBI-1567928, EBI-1237062;
CC Q8N122; Q9P2J5: LARS1; NbExp=3; IntAct=EBI-1567928, EBI-356077;
CC Q8N122; P45983: MAPK8; NbExp=6; IntAct=EBI-1567928, EBI-286483;
CC Q8N122; Q9BVC4: MLST8; NbExp=3; IntAct=EBI-1567928, EBI-1387471;
CC Q8N122; Q13615: MTMR3; NbExp=3; IntAct=EBI-1567928, EBI-371938;
CC Q8N122; P42345: MTOR; NbExp=47; IntAct=EBI-1567928, EBI-359260;
CC Q8N122; Q8TCU6: PREX1; NbExp=2; IntAct=EBI-1567928, EBI-1046542;
CC Q8N122; P62820: RAB1A; NbExp=4; IntAct=EBI-1567928, EBI-716845;
CC Q8N122; Q96EB6: SIRT1; NbExp=3; IntAct=EBI-1567928, EBI-1802965;
CC Q8N122; Q96R06: SPAG5; NbExp=9; IntAct=EBI-1567928, EBI-413317;
CC Q8N122; O75385: ULK1; NbExp=3; IntAct=EBI-1567928, EBI-908831;
CC Q8N122; Q9JLN9: Mtor; Xeno; NbExp=5; IntAct=EBI-1567928, EBI-1571628;
CC Q8N122; P67999: Rps6kb1; Xeno; NbExp=2; IntAct=EBI-1567928, EBI-2639458;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Lysosome. Cytoplasmic granule
CC {ECO:0000269|PubMed:25940091}. Note=Targeting to lysosomes depends on
CC amino acid availability. In arsenite-stressed cells, accumulates in
CC stress granules when associated with SPAG5 and association with
CC lysosomes is drastically decreased.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N122-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N122-2; Sequence=VSP_010174;
CC Name=3;
CC IsoId=Q8N122-3; Sequence=VSP_054042;
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle, and in a
CC lesser extent in brain, lung, small intestine, kidney and placenta.
CC Isoform 3 is widely expressed, with highest levels in nasal mucosa and
CC pituitary and lowest in spleen. {ECO:0000269|PubMed:12150925,
CC ECO:0000269|PubMed:12408816}.
CC -!- PTM: Insulin-stimulated phosphorylation at Ser-863 by MTOR and MAPK8
CC up-regulates mTORC1 activity. Osmotic stress also induces
CC phosphorylation at Ser-696, Thr-706 and Ser-863 by MAPK8. Ser-863
CC phosphorylation is required for phosphorylation at Ser-855 and Ser-859.
CC In response to nutrient limitation, phosphorylated by AMPK;
CC phosphorylation promotes interaction with 14-3-3 proteins, leading to
CC negative regulation of the mTORC1 complex. In response to growth
CC factors, phosphorylated at Ser-719, Ser-721 and Ser-722 by RPS6KA1,
CC which stimulates mTORC1 activity. {ECO:0000269|PubMed:18439900,
CC ECO:0000269|PubMed:18722121, ECO:0000269|PubMed:19864431,
CC ECO:0000269|PubMed:22493283}.
CC -!- SIMILARITY: Belongs to the WD repeat RAPTOR family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
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DR EMBL; AY090663; AAM09075.1; -; mRNA.
DR EMBL; AB082951; BAC06490.1; -; mRNA.
DR EMBL; AC016245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC127496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC133012; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471099; EAW89618.1; -; Genomic_DNA.
DR EMBL; BC025180; AAH25180.1; -; mRNA.
DR EMBL; BC033258; AAH33258.1; -; mRNA.
DR EMBL; BC064515; AAH64515.1; -; mRNA.
DR EMBL; BC136652; AAI36653.1; -; mRNA.
DR EMBL; BC136654; AAI36655.1; -; mRNA.
DR EMBL; AB037724; BAA92541.1; -; mRNA.
DR EMBL; GQ183898; ACS44766.1; -; mRNA.
DR CCDS; CCDS11773.1; -. [Q8N122-1]
DR CCDS; CCDS54175.1; -. [Q8N122-3]
DR RefSeq; NP_001156506.1; NM_001163034.1. [Q8N122-3]
DR RefSeq; NP_065812.1; NM_020761.2. [Q8N122-1]
DR PDB; 5H64; EM; 4.40 A; B/b=1-1335.
DR PDB; 6BCU; EM; 3.43 A; W/Y=2-1335.
DR PDB; 6BCX; EM; 3.00 A; W/Y=2-1335.
DR PDB; 6SB0; EM; 5.50 A; N/Y=1-1335.
DR PDB; 6SB2; EM; 6.20 A; N/Y=1-1335.
DR PDB; 6U62; EM; 3.18 A; A=1-1335.
DR PDB; 7OWG; EM; 4.70 A; Y=1-1335.
DR PDB; 7PEA; EM; 4.07 A; E/F=1-1335.
DR PDB; 7PEB; EM; 3.67 A; E=1-1335.
DR PDB; 7PEC; EM; 4.24 A; E=1-1335.
DR PDBsum; 5H64; -.
DR PDBsum; 6BCU; -.
DR PDBsum; 6BCX; -.
DR PDBsum; 6SB0; -.
DR PDBsum; 6SB2; -.
DR PDBsum; 6U62; -.
DR PDBsum; 7OWG; -.
DR PDBsum; 7PEA; -.
DR PDBsum; 7PEB; -.
DR PDBsum; 7PEC; -.
DR AlphaFoldDB; Q8N122; -.
DR SMR; Q8N122; -.
DR BioGRID; 121582; 320.
DR ComplexPortal; CPX-503; mTORC1 complex.
DR CORUM; Q8N122; -.
DR DIP; DIP-39482N; -.
DR ELM; Q8N122; -.
DR IntAct; Q8N122; 69.
DR MINT; Q8N122; -.
DR STRING; 9606.ENSP00000307272; -.
DR BindingDB; Q8N122; -.
DR ChEMBL; CHEMBL3120040; -.
DR GlyGen; Q8N122; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N122; -.
DR MetOSite; Q8N122; -.
DR PhosphoSitePlus; Q8N122; -.
DR BioMuta; RPTOR; -.
DR DMDM; 46577501; -.
DR EPD; Q8N122; -.
DR jPOST; Q8N122; -.
DR MassIVE; Q8N122; -.
DR MaxQB; Q8N122; -.
DR PaxDb; Q8N122; -.
DR PeptideAtlas; Q8N122; -.
DR PRIDE; Q8N122; -.
DR ProteomicsDB; 27504; -.
DR ProteomicsDB; 71521; -. [Q8N122-1]
DR ProteomicsDB; 71522; -. [Q8N122-2]
DR Antibodypedia; 4616; 619 antibodies from 44 providers.
DR CPTC; Q8N122; 2 antibodies.
DR DNASU; 57521; -.
DR Ensembl; ENST00000306801.8; ENSP00000307272.3; ENSG00000141564.15. [Q8N122-1]
DR Ensembl; ENST00000544334.6; ENSP00000442479.2; ENSG00000141564.15. [Q8N122-3]
DR Ensembl; ENST00000570891.5; ENSP00000460136.1; ENSG00000141564.15. [Q8N122-2]
DR GeneID; 57521; -.
DR KEGG; hsa:57521; -.
DR MANE-Select; ENST00000306801.8; ENSP00000307272.3; NM_020761.3; NP_065812.1.
DR UCSC; uc002jys.5; human. [Q8N122-1]
DR CTD; 57521; -.
DR DisGeNET; 57521; -.
DR GeneCards; RPTOR; -.
DR HGNC; HGNC:30287; RPTOR.
DR HPA; ENSG00000141564; Low tissue specificity.
DR MIM; 607130; gene.
DR neXtProt; NX_Q8N122; -.
DR OpenTargets; ENSG00000141564; -.
DR PharmGKB; PA165432629; -.
DR VEuPathDB; HostDB:ENSG00000141564; -.
DR eggNOG; KOG1517; Eukaryota.
DR GeneTree; ENSGT00640000091541; -.
DR HOGENOM; CLU_061814_0_0_1; -.
DR InParanoid; Q8N122; -.
DR OMA; QWSCLCL; -.
DR PhylomeDB; Q8N122; -.
DR TreeFam; TF105729; -.
DR PathwayCommons; Q8N122; -.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR Reactome; R-HSA-165159; MTOR signalling.
DR Reactome; R-HSA-166208; mTORC1-mediated signalling.
DR Reactome; R-HSA-3371571; HSF1-dependent transactivation.
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-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR SABIO-RK; Q8N122; -.
DR SignaLink; Q8N122; -.
DR SIGNOR; Q8N122; -.
DR BioGRID-ORCS; 57521; 639 hits in 1100 CRISPR screens.
DR ChiTaRS; RPTOR; human.
DR GeneWiki; RPTOR; -.
DR GenomeRNAi; 57521; -.
DR Pharos; Q8N122; Tbio.
DR PRO; PR:Q8N122; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8N122; protein.
DR Bgee; ENSG00000141564; Expressed in sural nerve and 134 other tissues.
DR ExpressionAtlas; Q8N122; baseline and differential.
DR Genevisible; Q8N122; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0031931; C:TORC1 complex; IDA:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; IDA:UniProtKB.
DR GO; GO:0030295; F:protein kinase activator activity; IDA:WormBase.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IDA:WormBase.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:WormBase.
DR GO; GO:0001002; F:RNA polymerase III type 1 promoter sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0001003; F:RNA polymerase III type 2 promoter sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0001006; F:RNA polymerase III type 3 promoter sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0001156; F:TFIIIC-class transcription factor complex binding; IDA:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IC:ComplexPortal.
DR GO; GO:0071456; P:cellular response to hypoxia; IC:ComplexPortal.
DR GO; GO:0071233; P:cellular response to leucine; IDA:CAFA.
DR GO; GO:0031669; P:cellular response to nutrient levels; IMP:UniProtKB.
DR GO; GO:0071470; P:cellular response to osmotic stress; IC:ComplexPortal.
DR GO; GO:0009267; P:cellular response to starvation; IBA:GO_Central.
DR GO; GO:0010507; P:negative regulation of autophagy; IC:ComplexPortal.
DR GO; GO:0016310; P:phosphorylation; IDA:ComplexPortal.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:ParkinsonsUK-UCL.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:ParkinsonsUK-UCL.
DR GO; GO:0045821; P:positive regulation of glycolytic process; IC:ComplexPortal.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IC:ComplexPortal.
DR GO; GO:1905857; P:positive regulation of pentose-phosphate shunt; IC:ComplexPortal.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:ParkinsonsUK-UCL.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IMP:ParkinsonsUK-UCL.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IDA:UniProtKB.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IMP:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central.
DR GO; GO:0001558; P:regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0008361; P:regulation of cell size; IMP:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0035176; P:social behavior; ISS:UniProtKB.
DR GO; GO:0031929; P:TOR signaling; IDA:UniProtKB.
DR GO; GO:0038202; P:TORC1 signaling; IMP:WormBase.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR004083; Raptor.
DR InterPro; IPR029347; Raptor_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR12848; PTHR12848; 1.
DR Pfam; PF02985; HEAT; 1.
DR Pfam; PF14538; Raptor_N; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM01302; Raptor_N; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Host-virus interaction;
KW Lysosome; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1335
FT /note="Regulatory-associated protein of mTOR"
FT /id="PRO_0000051200"
FT REPEAT 1020..1061
FT /note="WD 1"
FT REPEAT 1065..1106
FT /note="WD 2"
FT REPEAT 1121..1160
FT /note="WD 3"
FT REPEAT 1164..1203
FT /note="WD 4"
FT REPEAT 1209..1249
FT /note="WD 5"
FT REPEAT 1251..1291
FT /note="WD 6"
FT REPEAT 1299..1335
FT /note="WD 7"
FT REGION 850..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..943
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 696
FT /note="Phosphoserine; by MAPK8"
FT /evidence="ECO:0000269|PubMed:19864431,
FT ECO:0000269|PubMed:22493283, ECO:0007744|PubMed:23186163"
FT MOD_RES 706
FT /note="Phosphothreonine; by MAPK8"
FT /evidence="ECO:0000269|PubMed:19864431,
FT ECO:0000269|PubMed:22493283"
FT MOD_RES 719
FT /note="Phosphoserine; by RPS6KA1"
FT /evidence="ECO:0000269|PubMed:18722121,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 721
FT /note="Phosphoserine; by RPS6KA1"
FT /evidence="ECO:0000269|PubMed:18722121"
FT MOD_RES 722
FT /note="Phosphoserine; by AMPK and RPS6KA1"
FT /evidence="ECO:0000269|PubMed:18439900,
FT ECO:0000269|PubMed:18722121, ECO:0007744|PubMed:23186163"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 792
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000269|PubMed:18439900"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19864431"
FT MOD_RES 859
FT /note="Phosphoserine; by MTOR"
FT /evidence="ECO:0000269|PubMed:19864431,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 863
FT /note="Phosphoserine; by MAPK8 and MTOR"
FT /evidence="ECO:0000269|PubMed:19864431,
FT ECO:0000269|PubMed:22493283, ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 865
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 877
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19864431,
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 VAR_SEQ 380..1335
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010174"
FT VAR_SEQ 504..661
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19388141"
FT /id="VSP_054042"
FT MUTAGEN 722
FT /note="S->A: Abolishes AMPK-mediated phosphorylation; when
FT associated with A-792."
FT /evidence="ECO:0000269|PubMed:18439900"
FT MUTAGEN 792
FT /note="S->A: Abolishes AMPK-mediated phosphorylation; when
FT associated with A-722."
FT /evidence="ECO:0000269|PubMed:18439900"
FT CONFLICT 217..218
FT /note="LE -> RQ (in Ref. 6; BAA92541)"
FT /evidence="ECO:0000305"
FT TURN 22..25
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 95..111
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 128..140
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 179..185
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 200..218
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 262..268
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 270..279
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 310..327
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 332..337
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 341..356
FT /evidence="ECO:0007829|PDB:6U62"
FT TURN 357..361
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 378..391
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 408..422
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 433..439
FT /evidence="ECO:0007829|PDB:6U62"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 446..457
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 461..470
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 473..478
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 488..499
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 506..511
FT /evidence="ECO:0007829|PDB:6U62"
FT TURN 512..514
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 515..523
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 532..542
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 547..555
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 558..563
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 571..584
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 589..596
FT /evidence="ECO:0007829|PDB:6U62"
FT TURN 597..599
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 600..603
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 605..609
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 615..626
FT /evidence="ECO:0007829|PDB:6U62"
FT TURN 630..632
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 637..648
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 649..652
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 657..673
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 675..688
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 689..691
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 781..789
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 790..793
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 807..819
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 824..843
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 919..922
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 959..963
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 964..968
FT /evidence="ECO:0007829|PDB:6U62"
FT HELIX 983..1004
FT /evidence="ECO:0007829|PDB:6U62"
FT TURN 1005..1008
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1015..1021
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1028..1031
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1033..1036
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1038..1041
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1043..1049
FT /evidence="ECO:0007829|PDB:6U62"
FT TURN 1051..1053
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1056..1061
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1070..1081
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1083..1090
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1092..1097
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1107..1117
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1127..1131
FT /evidence="ECO:0007829|PDB:6U62"
FT TURN 1133..1135
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1137..1151
FT /evidence="ECO:0007829|PDB:6U62"
FT TURN 1152..1154
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1156..1162
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1165..1167
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1171..1175
FT /evidence="ECO:0007829|PDB:6U62"
FT TURN 1176..1179
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1180..1184
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1186..1188
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1190..1193
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1195..1197
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1199..1201
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1203..1207
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1214..1217
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1222..1224
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1228..1233
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1243..1245
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1257..1261
FT /evidence="ECO:0007829|PDB:6U62"
FT TURN 1263..1265
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1268..1271
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1277..1280
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1282..1284
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1286..1290
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1304..1309
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1311..1314
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1316..1320
FT /evidence="ECO:0007829|PDB:6U62"
FT STRAND 1323..1329
FT /evidence="ECO:0007829|PDB:6U62"
SQ SEQUENCE 1335 AA; 149038 MW; 688ED1943F45045A CRC64;
MESEMLQSPL LGLGEEDEAD LTDWNLPLAF MKKRHCEKIE GSKSLAQSWR MKDRMKTVSV
ALVLCLNVGV DPPDVVKTTP CARLECWIDP LSMGPQKALE TIGANLQKQY ENWQPRARYK
QSLDPTVDEV KKLCTSLRRN AKEERVLFHY NGHGVPRPTV NGEVWVFNKN YTQYIPLSIY
DLQTWMGSPS IFVYDCSNAG LIVKSFKQFA LQREQELEVA AINPNHPLAQ MPLPPSMKNC
IQLAACEATE LLPMIPDLPA DLFTSCLTTP IKIALRWFCM QKCVSLVPGV TLDLIEKIPG
RLNDRRTPLG ELNWIFTAIT DTIAWNVLPR DLFQKLFRQD LLVASLFRNF LLAERIMRSY
NCTPVSSPRL PPTYMHAMWQ AWDLAVDICL SQLPTIIEEG TAFRHSPFFA EQLTAFQVWL
TMGVENRNPP EQLPIVLQVL LSQVHRLRAL DLLGRFLDLG PWAVSLALSV GIFPYVLKLL
QSSARELRPL LVFIWAKILA VDSSCQADLV KDNGHKYFLS VLADPYMPAE HRTMTAFILA
VIVNSYHTGQ EACLQGNLIA ICLEQLNDPH PLLRQWVAIC LGRIWQNFDS ARWCGVRDSA
HEKLYSLLSD PIPEVRCAAV FALGTFVGNS AERTDHSTTI DHNVAMMLAQ LVSDGSPMVR
KELVVALSHL VVQYESNFCT VALQFIEEEK NYALPSPATT EGGSLTPVRD SPCTPRLRSV
SSYGNIRAVA TARSLNKSLQ NLSLTEESGG AVAFSPGNLS TSSSASSTLG SPENEEHILS
FETIDKMRRA SSYSSLNSLI GVSFNSVYTQ IWRVLLHLAA DPYPEVSDVA MKVLNSIAYK
ATVNARPQRV LDTSSLTQSA PASPTNKGVH IHQAGGSPPA SSTSSSSLTN DVAKQPVSRD
LPSGRPGTTG PAGAQYTPHS HQFPRTRKMF DKGPEQTADD ADDAAGHKSF ISATVQTGFC
DWSARYFAQP VMKIPEEHDL ESQIRKEREW RFLRNSRVRR QAQQVIQKGI TRLDDQIFLN
RNPGVPSVVK FHPFTPCIAV ADKDSICFWD WEKGEKLDYF HNGNPRYTRV TAMEYLNGQD
CSLLLTATDD GAIRVWKNFA DLEKNPEMVT AWQGLSDMLP TTRGAGMVVD WEQETGLLMS
SGDVRIVRIW DTDREMKVQD IPTGADSCVT SLSCDSHRSL IVAGLGDGSI RVYDRRMALS
ECRVMTYREH TAWVVKASLQ KRPDGHIVSV SVNGDVRIFD PRMPESVNVL QIVKGLTALD
IHPQADLIAC GSVNQFTAIY NSSGELINNI KYYDGFMGQR VGAISCLAFH PHWPHLAVGS
NDYYISVYSV EKRVR
