GenomeNet

Database: UniProt
Entry: P42345
LinkDB: P42345
Original site: P42345 
ID   MTOR_HUMAN              Reviewed;        2549 AA.
AC   P42345; Q4LE76; Q5TER1; Q6LE87; Q96QG3; Q9Y4I3;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   11-DEC-2019, entry version 213.
DE   RecName: Full=Serine/threonine-protein kinase mTOR;
DE            EC=2.7.11.1 {ECO:0000269|PubMed:12087098, ECO:0000269|PubMed:12150925, ECO:0000269|PubMed:12231510, ECO:0000269|PubMed:15268862, ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:15718470, ECO:0000269|PubMed:18925875};
DE   AltName: Full=FK506-binding protein 12-rapamycin complex-associated protein 1;
DE   AltName: Full=FKBP12-rapamycin complex-associated protein;
DE   AltName: Full=Mammalian target of rapamycin;
DE            Short=mTOR;
DE   AltName: Full=Mechanistic target of rapamycin;
DE   AltName: Full=Rapamycin and FKBP12 target 1;
DE   AltName: Full=Rapamycin target protein 1;
GN   Name=MTOR; Synonyms=FRAP, FRAP1, FRAP2, RAFT1, RAPT1;
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].
RC   TISSUE=Brain;
RX   PubMed=8008069; DOI=10.1038/369756a0;
RA   Brown E.J., Albers M.W., Shin T.B., Ichikawa K., Keith C.T., Lane W.S.,
RA   Schreiber S.L.;
RT   "A mammalian protein targeted by G1-arresting rapamycin-receptor complex.";
RL   Nature 369:756-758(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9653645; DOI=10.1006/geno.1997.5186;
RA   Onyango P., Lubyova B., Gardellin P., Kurzbauer R., Weith A.;
RT   "Molecular cloning and expression analysis of five novel genes in
RT   chromosome 1p36.";
RL   Genomics 50:187-198(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R.,
RA   Okazaki N., Koga H., Nagase T., Ohara O.;
RT   "Preparation of a set of expression-ready clones of mammalian long cDNAs
RT   encoding large proteins by the ORF trap cloning method.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cerebellum;
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 [GENOMIC DNA] OF 1362-2549.
RX   PubMed=11426320; DOI=10.1038/sj.gene.6363745;
RA   Stover C., Endo Y., Takahashi M., Lynch N., Constantinescu C.,
RA   Vorup-Jensen T., Thiel S., Friedl H., Hankeln T., Hall R., Gregory S.,
RA   Fujita T., Schwaeble W.;
RT   "The human gene for mannan-binding lectin-associated serine protease-2
RT   (MASP-2), the effector component of the lectin route of complement
RT   activation, is part of a tightly linked gene cluster on chromosome 1p36.2-
RT   3.";
RL   Genes Immun. 2:119-127(2001).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1987-2146, AND TISSUE SPECIFICITY.
RC   TISSUE=B-cell;
RX   PubMed=7809080; DOI=10.1073/pnas.91.26.12574;
RA   Chiu M.I., Katz H., Berlin V.;
RT   "RAPT1, a mammalian homolog of yeast Tor, interacts with the
RT   FKBP12/rapamycin complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:12574-12578(1994).
RN   [8]
RP   SUBCELLULAR LOCATION, AND AUTOPHOSPHORYLATION.
RX   PubMed=9434772; DOI=10.1006/bbrc.1997.7878;
RA   Withers D.J., Ouwens D.M., Nave B.T., van der Zon G.C.M., Alarcon C.M.,
RA   Cardenas M.E., Heitman J., Maassen J.A., Shepherd P.R.;
RT   "Expression, enzyme activity, and subcellular localization of mammalian
RT   target of rapamycin in insulin-responsive cells.";
RL   Biochem. Biophys. Res. Commun. 241:704-709(1997).
RN   [9]
RP   INTERACTION WITH UBQLN1.
RX   PubMed=11853878; DOI=10.1016/s0167-4889(01)00164-1;
RA   Wu S., Mikhailov A., Kallo-Hosein H., Hara K., Yonezawa K., Avruch J.;
RT   "Characterization of ubiquilin 1, an mTOR-interacting protein.";
RL   Biochim. Biophys. Acta 1542:41-56(2002).
RN   [10]
RP   FUNCTION IN NUTRIENT-DEPENDENT CELL GROWTH, CATALYTIC ACTIVITY, FUNCTION IN
RP   PHOSPHORYLATION OF RPS6KB1, AND INTERACTION WITH RPTOR.
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   [11]
RP   FUNCTION, AND INTERACTION WITH RPTOR.
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   [12]
RP   INTERACTION WITH CLIP1, FUNCTION IN PHOSPHORYLATION OF CLIP1, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=12231510; DOI=10.1093/embo-reports/kvf197;
RA   Choi J.H., Bertram P.G., Drenan R., Carvalho J., Zhou H.H., Zheng X.F.;
RT   "The FKBP12-rapamycin-associated protein (FRAP) is a CLIP-170 kinase.";
RL   EMBO Rep. 3:988-994(2002).
RN   [13]
RP   FUNCTION IN PHOSPHORYLATION OF RPS6KB2, AND CATALYTIC ACTIVITY.
RX   PubMed=12087098; DOI=10.1074/jbc.m204080200;
RA   Park I.H., Bachmann R., Shirazi H., Chen J.;
RT   "Regulation of ribosomal S6 kinase 2 by mammalian target of rapamycin.";
RL   J. Biol. Chem. 277:31423-31429(2002).
RN   [14]
RP   INTERACTION WITH MLST8 AND RPTOR, IDENTIFICATION IN THE MTORC1 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   [15]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11930000; DOI=10.1073/pnas.261702698;
RA   Desai B.N., Myers B.R., Schreiber S.L.;
RT   "FKBP12-rapamycin-associated protein associates with mitochondria and
RT   senses osmotic stress via mitochondrial dysfunction.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4319-4324(2002).
RN   [16]
RP   ACTIVITY REGULATION, AND FUNCTION IN RESPONSE TO LOW CELLULAR ENERGY.
RX   PubMed=14651849; DOI=10.1016/s0092-8674(03)00929-2;
RA   Inoki K., Zhu T., Guan K.L.;
RT   "TSC2 mediates cellular energy response to control cell growth and
RT   survival.";
RL   Cell 115:577-590(2003).
RN   [17]
RP   FUNCTION, AND INTERACTION WITH MLST8.
RX   PubMed=12718876; DOI=10.1016/s1097-2765(03)00114-x;
RA   Kim D.-H., Sarbassov D.D., Ali S.M., Latek R.R., Guntur K.V.P.,
RA   Erdjument-Bromage H., Tempst P., Sabatini D.M.;
RT   "GbetaL, a positive regulator of the rapamycin-sensitive pathway required
RT   for the nutrient-sensitive interaction between raptor and mTOR.";
RL   Mol. Cell 11:895-904(2003).
RN   [18]
RP   FUNCTION IN PHOSPHORYLATION OF PRKCA, CATALYTIC ACTIVITY, FUNCTION IN
RP   REGULATION OF THE ACTIN CYTOSKELETON, IDENTIFICATION IN THE MTORC2 COMPLEX,
RP   AND INTERACTION WITH RICTOR.
RX   PubMed=15268862; DOI=10.1016/j.cub.2004.06.054;
RA   Sarbassov D.D., Ali S.M., Kim D.-H., Guertin D.A., Latek R.R.,
RA   Erdjument-Bromage H., Tempst P., Sabatini D.M.;
RT   "Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive
RT   and raptor-independent pathway that regulates the cytoskeleton.";
RL   Curr. Biol. 14:1296-1302(2004).
RN   [19]
RP   ACTIVITY REGULATION, AND FUNCTION IN RESPONSE TO HYPOXIA.
RX   PubMed=15545625; DOI=10.1101/gad.1256804;
RA   Brugarolas J., Lei K., Hurley R.L., Manning B.D., Reiling J.H., Hafen E.,
RA   Witters L.A., Ellisen L.W., Kaelin W.G. Jr.;
RT   "Regulation of mTOR function in response to hypoxia by REDD1 and the
RT   TSC1/TSC2 tumor suppressor complex.";
RL   Genes Dev. 18:2893-2904(2004).
RN   [20]
RP   SUBCELLULAR LOCATION.
RX   PubMed=14578359; DOI=10.1074/jbc.m305912200;
RA   Drenan R.M., Liu X., Bertram P.G., Zheng X.F.S.;
RT   "FKBP12-rapamycin-associated protein or mammalian target of rapamycin
RT   (FRAP/mTOR) localization in the endoplasmic reticulum and the Golgi
RT   apparatus.";
RL   J. Biol. Chem. 279:772-778(2004).
RN   [21]
RP   FUNCTION IN REGULATION OF THE ACTIN CYTOSKELETON, CATALYTIC ACTIVITY,
RP   FUNCTION IN PHOSPHORYLATION OF PXN, IDENTIFICATION IN THE MTORC2 COMPLEX,
RP   INTERACTION WITH RICTOR, AND AUTOPHOSPHORYLATION.
RX   PubMed=15467718; DOI=10.1038/ncb1183;
RA   Jacinto E., Loewith R., Schmidt A., Lin S., Ruegg M.A., Hall A., Hall M.N.;
RT   "Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin
RT   insensitive.";
RL   Nat. Cell Biol. 6:1122-1128(2004).
RN   [22]
RP   PHOSPHORYLATION AT THR-2446 AND SER-2448.
RX   PubMed=15905173; DOI=10.1074/jbc.m504045200;
RA   Holz M.K., Blenis J.;
RT   "Identification of S6 kinase 1 as a novel mammalian target of rapamycin
RT   (mTOR)-phosphorylating kinase.";
RL   J. Biol. Chem. 280:26089-26093(2005).
RN   [23]
RP   FUNCTION IN PHOSPHORYLATION OF AKT1, AND CATALYTIC ACTIVITY.
RX   PubMed=15718470; DOI=10.1126/science.1106148;
RA   Sarbassov D.D., Guertin D.A., Ali S.M., Sabatini D.M.;
RT   "Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex.";
RL   Science 307:1098-1101(2005).
RN   [24]
RP   IDENTIFICATION IN THE MTORC2 COMPLEX, AND INTERACTION WITH PRR5.
RX   PubMed=17599906; DOI=10.1074/jbc.m704343200;
RA   Woo S.-Y., Kim D.-H., Jun C.-B., Kim Y.-M., Haar E.V., Lee S.-I.,
RA   Hegg J.W., Bandhakavi S., Griffin T.J., Kim D.-H.;
RT   "PRR5, a novel component of mTOR complex 2, regulates platelet-derived
RT   growth factor receptor beta expression and signaling.";
RL   J. Biol. Chem. 282:25604-25612(2007).
RN   [25]
RP   INTERACTION WITH AKT1S1, AND ACTIVITY REGULATION.
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   [26]
RP   IDENTIFICATION IN THE MTORC1 AND MTORC2 COMPLEXES, CATALYTIC ACTIVITY, AND
RP   FUNCTION IN PHOSPHORYLATION OF RPS6KB1 AND SGK1.
RX   PubMed=18925875; DOI=10.1042/bj20081668;
RA   Garcia-Martinez J.M., Alessi D.R.;
RT   "mTOR complex 2 (mTORC2) controls hydrophobic motif phosphorylation and
RT   activation of serum- and glucocorticoid-induced protein kinase 1 (SGK1).";
RL   Biochem. J. 416:375-385(2008).
RN   [27]
RP   FUNCTION IN LIPID SYNTHESIS AND CELL GROWTH.
RX   PubMed=18762023; DOI=10.1016/j.cmet.2008.07.007;
RA   Porstmann T., Santos C.R., Griffiths B., Cully M., Wu M., Leevers S.,
RA   Griffiths J.R., Chung Y.L., Schulze A.;
RT   "SREBP activity is regulated by mTORC1 and contributes to Akt-dependent
RT   cell growth.";
RL   Cell Metab. 8:224-236(2008).
RN   [28]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567, 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   [29]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2478 AND SER-2481, AND
RP   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   [30]
RP   FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX   PubMed=18497260; DOI=10.1126/science.1157535;
RA   Sancak Y., Peterson T.R., Shaul Y.D., Lindquist R.A., Thoreen C.C.,
RA   Bar-Peled L., Sabatini D.M.;
RT   "The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1.";
RL   Science 320:1496-1501(2008).
RN   [31]
RP   INTERACTION WITH DEPTOR, AND ACTIVITY REGULATION.
RX   PubMed=19446321; DOI=10.1016/j.cell.2009.03.046;
RA   Peterson T.R., Laplante M., Thoreen C.C., Sancak Y., Kang S.A., Kuehl W.M.,
RA   Gray N.S., Sabatini D.M.;
RT   "DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma
RT   cells and required for their survival.";
RL   Cell 137:873-886(2009).
RN   [32]
RP   PHOSPHORYLATION AT SER-1261.
RX   PubMed=19487463; DOI=10.1128/mcb.01665-08;
RA   Acosta-Jaquez H.A., Keller J.A., Foster K.G., Ekim B., Soliman G.A.,
RA   Feener E.P., Ballif B.A., Fingar D.C.;
RT   "Site-specific mTOR phosphorylation promotes mTORC1-mediated signaling and
RT   cell growth.";
RL   Mol. Cell. Biol. 29:4308-4324(2009).
RN   [33]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567, 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   [34]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1218, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [35]
RP   PHOSPHORYLATION AT SER-2448.
RX   PubMed=19145465; DOI=10.1007/s00726-008-0230-7;
RA   Rosner M., Siegel N., Valli A., Fuchs C., Hengstschlager M.;
RT   "mTOR phosphorylated at S2448 binds to raptor and rictor.";
RL   Amino Acids 38:223-228(2010).
RN   [36]
RP   SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
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   [37]
RP   FUNCTION IN PHOSPHORYLATION OF DAP, FUNCTION IN AUTOPHAGY, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=20537536; DOI=10.1016/j.cub.2010.04.041;
RA   Koren I., Reem E., Kimchi A.;
RT   "DAP1, a novel substrate of mTOR, negatively regulates autophagy.";
RL   Curr. Biol. 20:1093-1098(2010).
RN   [38]
RP   INTERACTION WITH TTI1.
RX   PubMed=20810650; DOI=10.1101/gad.1934210;
RA   Hurov K.E., Cotta-Ramusino C., Elledge S.J.;
RT   "A genetic screen identifies the Triple T complex required for DNA damage
RT   signaling and ATM and ATR stability.";
RL   Genes Dev. 24:1939-1950(2010).
RN   [39]
RP   INTERACTION WITH TELO2.
RX   PubMed=20801936; DOI=10.1101/gad.1956410;
RA   Takai H., Xie Y., de Lange T., Pavletich N.P.;
RT   "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and
RT   ATR complexes.";
RL   Genes Dev. 24:2019-2030(2010).
RN   [40]
RP   INTERACTION WITH TELO2 AND TTI1.
RX   PubMed=20427287; DOI=10.1074/jbc.m110.121699;
RA   Kaizuka T., Hara T., Oshiro N., Kikkawa U., Yonezawa K., Takehana K.,
RA   Iemura S., Natsume T., Mizushima N.;
RT   "Tti1 and Tel2 are critical factors in mammalian target of rapamycin
RT   complex assembly.";
RL   J. Biol. Chem. 285:20109-20116(2010).
RN   [41]
RP   FUNCTION IN REGULATION OF RNA POLYMERASE III TRANSCRIPTION, FUNCTION IN
RP   PHOSPHORYLATION OF MAF1, AND CATALYTIC ACTIVITY.
RX   PubMed=20516213; DOI=10.1128/mcb.00319-10;
RA   Michels A.A., Robitaille A.M., Buczynski-Ruchonnet D., Hodroj W.,
RA   Reina J.H., Hall M.N., Hernandez N.;
RT   "mTORC1 directly phosphorylates and regulates human MAF1.";
RL   Mol. Cell. Biol. 30:3749-3757(2010).
RN   [42]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567 AND THR-1162, 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   [43]
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   [44]
RP   PHOSPHORYLATION AT SER-2159; THR-2164 AND SER-2481, AND MUTAGENESIS OF
RP   SER-2159 AND THR-2164.
RX   PubMed=21576368; DOI=10.1128/mcb.05437-11;
RA   Ekim B., Magnuson B., Acosta-Jaquez H.A., Keller J.A., Feener E.P.,
RA   Fingar D.C.;
RT   "mTOR kinase domain phosphorylation promotes mTORC1 signaling, cell growth,
RT   and cell cycle progression.";
RL   Mol. Cell. Biol. 31:2787-2801(2011).
RN   [45]
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   [46]
RP   FUNCTION IN PHOSPHORYLATION OF GRB10, CATALYTIC ACTIVITY, AND FUNCTION IN
RP   INSR-DEPENDENT SIGNALING.
RX   PubMed=21659604; DOI=10.1126/science.1199498;
RA   Hsu P.P., Kang S.A., Rameseder J., Zhang Y., Ottina K.A., Lim D.,
RA   Peterson T.R., Choi Y., Gray N.S., Yaffe M.B., Marto J.A., Sabatini D.M.;
RT   "The mTOR-regulated phosphoproteome reveals a mechanism of mTORC1-mediated
RT   inhibition of growth factor signaling.";
RL   Science 332:1317-1322(2011).
RN   [47]
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   [48]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [49]
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   [50]
RP   PHOSPHORYLATION AT THR-2173, AND MUTAGENESIS OF THR-2173.
RX   PubMed=24247430; DOI=10.1083/jcb.201305103;
RA   Halova L., Du W., Kirkham S., Smith D.L., Petersen J.;
RT   "Phosphorylation of the TOR ATP binding domain by AGC kinase constitutes a
RT   novel mode of TOR inhibition.";
RL   J. Cell Biol. 203:595-604(2013).
RN   [51]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1261, AND IDENTIFICATION BY
RP   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   [52]
RP   INTERACTION WITH NBN.
RX   PubMed=23762398; DOI=10.1371/journal.pone.0065586;
RA   Wang J.Q., Chen J.H., Chen Y.C., Chen M.Y., Hsieh C.Y., Teng S.C., Wu K.J.;
RT   "Interaction between NBS1 and the mTOR/Rictor/SIN1 complex through specific
RT   domains.";
RL   PLoS ONE 8:E65586-E65586(2013).
RN   [53]
RP   FUNCTION, PHOSPHORYLATION OF RPS6KB1, AND REGULATION OF PYRIMIDINE
RP   SYNTHESIS.
RX   PubMed=23429704; DOI=10.1126/science.1228771;
RA   Robitaille A.M., Christen S., Shimobayashi M., Cornu M., Fava L.L.,
RA   Moes S., Prescianotto-Baschong C., Sauer U., Jenoe P., Hall M.N.;
RT   "Quantitative phosphoproteomics reveal mTORC1 activates de novo pyrimidine
RT   synthesis.";
RL   Science 339:1320-1323(2013).
RN   [54]
RP   FUNCTION, PHOSPHORYLATION OF RPS6KB1, AND REGULATION OF PYRIMIDINE
RP   SYNTHESIS.
RX   PubMed=23429703; DOI=10.1126/science.1228792;
RA   Ben-Sahra I., Howell J.J., Asara J.M., Manning B.D.;
RT   "Stimulation of de novo pyrimidine synthesis by growth signaling through
RT   mTOR and S6K1.";
RL   Science 339:1323-1328(2013).
RN   [55]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2448, AND IDENTIFICATION BY
RP   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   [56]
RP   INVOLVEMENT IN SKS, VARIANT SKS LYS-1799, AND CHARACTERIZATION OF VARIANT
RP   SKS LYS-1799.
RX   PubMed=25851998; DOI=10.1002/ajmg.a.37070;
RA   Baynam G., Overkov A., Davis M., Mina K., Schofield L., Allcock R.,
RA   Laing N., Cook M., Dawkins H., Goldblatt J.;
RT   "A germline MTOR mutation in Aboriginal Australian siblings with
RT   intellectual disability, dysmorphism, macrocephaly, and small thoraces.";
RL   Am. J. Med. Genet. A 167:1659-1667(2015).
RN   [57]
RP   FUNCTION, INVOLVEMENT IN FCORD2, VARIANTS FCORD2 ASP-1459; PRO-1460;
RP   PHE-2215 AND TYR-2215, AND CHARACTERIZATION OF VARIANTS FCORD2 ASP-1459;
RP   PRO-1460; PHE-2215 AND TYR-2215.
RX   PubMed=26018084; DOI=10.1002/ana.24444;
RA   Nakashima M., Saitsu H., Takei N., Tohyama J., Kato M., Kitaura H.,
RA   Shiina M., Shirozu H., Masuda H., Watanabe K., Ohba C., Tsurusaki Y.,
RA   Miyake N., Zheng Y., Sato T., Takebayashi H., Ogata K., Kameyama S.,
RA   Kakita A., Matsumoto N.;
RT   "Somatic mutations in the MTOR gene cause focal cortical dysplasia type
RT   IIb.";
RL   Ann. Neurol. 78:375-386(2015).
RN   [58]
RP   INVOLVEMENT IN SKS, VARIANT SKS LYS-1799, AND CHARACTERIZATION OF VARIANT
RP   SKS LYS-1799.
RX   PubMed=26542245; DOI=10.1186/s12881-015-0240-8;
RA   Mroske C., Rasmussen K., Shinde D.N., Huether R., Powis Z., Lu H.M.,
RA   Baxter R.M., McPherson E., Tang S.;
RT   "Germline activating MTOR mutation arising through gonadal mosaicism in two
RT   brothers with megalencephaly and neurodevelopmental abnormalities.";
RL   BMC Med. Genet. 16:102-102(2015).
RN   [59]
RP   FUNCTION, INVOLVEMENT IN FCORD2, VARIANTS FCORD2 HIS-624; ASP-1450;
RP   ARG-1483; HIS-1709; LYS-1977; CYS-2193; PHE-2215; GLN-2427 AND PRO-2427,
RP   AND CHARACTERIZATION OF VARIANTS FCORD2 ARG-1483; GLN-2427 AND PRO-2427.
RX   PubMed=25799227; DOI=10.1038/nm.3824;
RA   Lim J.S., Kim W.I., Kang H.C., Kim S.H., Park A.H., Park E.K., Cho Y.W.,
RA   Kim S., Kim H.M., Kim J.A., Kim J., Rhee H., Kang S.G., Kim H.D., Kim D.,
RA   Kim D.S., Lee J.H.;
RT   "Brain somatic mutations in MTOR cause focal cortical dysplasia type II
RT   leading to intractable epilepsy.";
RL   Nat. Med. 21:395-400(2015).
RN   [60]
RP   ACTIVITY REGULATION.
RX   PubMed=25561175; DOI=10.1038/nature14107;
RA   Rebsamen M., Pochini L., Stasyk T., de Araujo M.E., Galluccio M.,
RA   Kandasamy R.K., Snijder B., Fauster A., Rudashevskaya E.L., Bruckner M.,
RA   Scorzoni S., Filipek P.A., Huber K.V., Bigenzahn J.W., Heinz L.X.,
RA   Kraft C., Bennett K.L., Indiveri C., Huber L.A., Superti-Furga G.;
RT   "SLC38A9 is a component of the lysosomal amino acid sensing machinery that
RT   controls mTORC1.";
RL   Nature 519:477-481(2015).
RN   [61]
RP   INVOLVEMENT IN FCORD2, AND VARIANT FCORD2 GLY-1456.
RX   PubMed=25878179; DOI=10.1212/wnl.0000000000001594;
RA   Leventer R.J., Scerri T., Marsh A.P., Pope K., Gillies G., Maixner W.,
RA   MacGregor D., Harvey A.S., Delatycki M.B., Amor D.J., Crino P., Bahlo M.,
RA   Lockhart P.J.;
RT   "Hemispheric cortical dysplasia secondary to a mosaic somatic mutation in
RT   MTOR.";
RL   Neurology 84:2029-2032(2015).
RN   [62]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [63]
RP   ACTIVITY REGULATION.
RX   PubMed=25567906; DOI=10.1126/science.1257132;
RA   Wang S., Tsun Z.Y., Wolfson R.L., Shen K., Wyant G.A., Plovanich M.E.,
RA   Yuan E.D., Jones T.D., Chantranupong L., Comb W., Wang T., Bar-Peled L.,
RA   Zoncu R., Straub C., Kim C., Park J., Sabatini B.L., Sabatini D.M.;
RT   "Metabolism. Lysosomal amino acid transporter SLC38A9 signals arginine
RT   sufficiency to mTORC1.";
RL   Science 347:188-194(2015).
RN   [64]
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   [65]
RP   INVOLVEMENT IN FCORD2, VARIANTS GLU-1376 AND VAL-2501, VARIANTS FCORD2
RP   SER-1459; PRO-1460; PHE-2215 AND TYR-2215, AND VARIANTS SKS ARG-1490;
RP   ILE-1595; THR-1832; CYS-1888 AND ILE-2327.
RX   PubMed=27830187; DOI=10.1212/nxg.0000000000000118;
RA   Moeller R.S., Weckhuysen S., Chipaux M., Marsan E., Taly V., Bebin E.M.,
RA   Hiatt S.M., Prokop J.W., Bowling K.M., Mei D., Conti V., de la Grange P.,
RA   Ferrand-Sorbets S., Dorfmueller G., Lambrecq V., Larsen L.H., Leguern E.,
RA   Guerrini R., Rubboli G., Cooper G.M., Baulac S.;
RT   "Germline and somatic mutations in the MTOR gene in focal cortical
RT   dysplasia and epilepsy.";
RL   Neurol. Genet. 2:E118-E118(2016).
RN   [66]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH MEAK7.
RX   PubMed=29750193; DOI=10.1126/sciadv.aao5838;
RA   Nguyen J.T., Ray C., Fox A.L., Mendonca D.B., Kim J.K., Krebsbach P.H.;
RT   "Mammalian EAK-7 activates alternative mTOR signaling to regulate cell
RT   proliferation and migration.";
RL   Sci. Adv. 4:EAAO5838-EAAO5838(2018).
RN   [67]
RP   INTERACTION WITH TM4SF5, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-2357
RP   AND VAL-2364.
RX   PubMed=30956113; DOI=10.1016/j.cmet.2019.03.005;
RA   Jung J.W., Macalino S.J.Y., Cui M., Kim J.E., Kim H.J., Song D.G.,
RA   Nam S.H., Kim S., Choi S., Lee J.W.;
RT   "Transmembrane 4 L six family member 5 senses arginine for mTORC1
RT   signaling.";
RL   Cell Metab. 29:1306-1319(2019).
RN   [68]
RP   FUNCTION.
RX   PubMed=30704899; DOI=10.1016/j.molcel.2018.12.017;
RA   Cheng X., Ma X., Zhu Q., Song D., Ding X., Li L., Jiang X., Wang X.,
RA   Tian R., Su H., Shen Z., Chen S., Liu T., Gong W., Liu W., Sun Q.;
RT   "Pacer is a mediator of mTORC1 and GSK3-TIP60 signaling in regulation of
RT   autophagosome maturation and lipid metabolism.";
RL   Mol. Cell 73:1-15(2019).
RN   [69]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2018-2112 IN COMPLEX WITH FKBP1A
RP   AND INHIBITOR RAPAMYCIN.
RX   PubMed=8662507; DOI=10.1126/science.273.5272.239;
RA   Choi J., Chen J., Schreiber S.L., Clardy J.;
RT   "Structure of the FKBP12-rapamycin complex interacting with the binding
RT   domain of human FRAP.";
RL   Science 273:239-242(1996).
RN   [70]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2018-2112 IN COMPLEX WITH FKBP1A
RP   AND INHIBITOR RAPAMYCIN.
RX   PubMed=10089303; DOI=10.1107/s0907444998014747;
RA   Liang J., Choi J., Clardy J.;
RT   "Refined structure of the FKBP12-rapamycin-FRB ternary complex at 2.2 A
RT   resolution.";
RL   Acta Crystallogr. D 55:736-744(1999).
RN   [71]
RP   3D-STRUCTURE MODELING, HEAT-REPEATS, AND TPR-REPEATS.
RX   PubMed=20060908; DOI=10.1016/j.jsb.2010.01.002;
RA   Knutson B.A.;
RT   "Insights into the domain and repeat architecture of target of rapamycin.";
RL   J. Struct. Biol. 170:354-363(2010).
RN   [72]
RP   CRYO-ELECTRON MICROSCOPY (26 ANGSTROMS) OF MTORC1 COMPLEX, AND SUBUNIT.
RX   PubMed=20542007; DOI=10.1016/j.molcel.2010.05.017;
RA   Yip C.K., Murata K., Walz T., Sabatini D.M., Kang S.A.;
RT   "Structure of the human mTOR complex I and its implications for rapamycin
RT   inhibition.";
RL   Mol. Cell 38:768-774(2010).
RN   [73]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1376-2549 IN COMPLEX WITH MLST8,
RP   SUBUNIT, TPR-REPEATS, DOMAINS, AND MUTAGENESIS OF HIS-2340.
RX   PubMed=23636326; DOI=10.1038/nature12122;
RA   Yang H., Rudge D.G., Koos J.D., Vaidialingam B., Yang H.J., Pavletich N.P.;
RT   "mTOR kinase structure, mechanism and regulation.";
RL   Nature 497:217-223(2013).
RN   [74]
RP   VARIANTS [LARGE SCALE ANALYSIS] SER-8; THR-135; VAL-1083; VAL-1134;
RP   PHE-1178; VAL-2011; TYR-2215 AND LEU-2476.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA   Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA   Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA   Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA   Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA   Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA   Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA   Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA   Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA   Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA   Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA   Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
RN   [75]
RP   VARIANTS PHE-2220 AND ALA-2406.
RX   PubMed=21248752; DOI=10.1038/nature09639;
RA   Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA   Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA   Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA   Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA   Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA   Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA   Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA   Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT   "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT   PBRM1 in renal carcinoma.";
RL   Nature 469:539-542(2011).
CC   -!- FUNCTION: Serine/threonine protein kinase which is a central regulator
CC       of cellular metabolism, growth and survival in response to hormones,
CC       growth factors, nutrients, energy and stress signals (PubMed:12087098,
CC       PubMed:12150925, PubMed:12150926, PubMed:12231510, PubMed:12718876,
CC       PubMed:14651849, PubMed:15268862, PubMed:15467718, PubMed:15545625,
CC       PubMed:15718470, PubMed:18497260, PubMed:18762023, PubMed:18925875,
CC       PubMed:20516213, PubMed:20537536, PubMed:21659604, PubMed:23429703,
CC       PubMed:23429704, PubMed:25799227, PubMed:26018084). MTOR directly or
CC       indirectly regulates the phosphorylation of at least 800 proteins.
CC       Functions as part of 2 structurally and functionally distinct signaling
CC       complexes mTORC1 and mTORC2 (mTOR complex 1 and 2) (PubMed:15268862,
CC       PubMed:15467718, PubMed:18925875, PubMed:18497260, PubMed:20516213,
CC       PubMed:21576368, PubMed:21659604, PubMed:23429704). Activated mTORC1
CC       up-regulates protein synthesis by phosphorylating key regulators of
CC       mRNA translation and ribosome synthesis (PubMed:12087098,
CC       PubMed:12150925, PubMed:12150926, PubMed:12231510, PubMed:12718876,
CC       PubMed:14651849, PubMed:15268862, PubMed:15467718, PubMed:15545625,
CC       PubMed:15718470, PubMed:18497260, PubMed:18762023, PubMed:18925875,
CC       PubMed:20516213, PubMed:20537536, PubMed:21659604, PubMed:23429703,
CC       PubMed:23429704, PubMed:25799227, PubMed:26018084). This includes
CC       phosphorylation of EIF4EBP1 and release of its inhibition toward the
CC       elongation initiation factor 4E (eiF4E) (By similarity). Moreover,
CC       phosphorylates and activates RPS6KB1 and RPS6KB2 that promote protein
CC       synthesis by modulating the activity of their downstream targets
CC       including ribosomal protein S6, eukaryotic translation initiation
CC       factor EIF4B, and the inhibitor of translation initiation PDCD4
CC       (PubMed:12150925, PubMed:12087098, PubMed:18925875). Stimulates the
CC       pyrimidine biosynthesis pathway, both by acute regulation through
CC       RPS6KB1-mediated phosphorylation of the biosynthetic enzyme CAD, and
CC       delayed regulation, through transcriptional enhancement of the pentose
CC       phosphate pathway which produces 5-phosphoribosyl-1-pyrophosphate
CC       (PRPP), an allosteric activator of CAD at a later step in synthesis,
CC       this function is dependent on the mTORC1 complex (PubMed:23429704,
CC       PubMed:23429703). Regulates ribosome synthesis by activating RNA
CC       polymerase III-dependent transcription through phosphorylation and
CC       inhibition of MAF1 an RNA polymerase III-repressor (PubMed:20516213).
CC       In parallel to protein synthesis, also regulates lipid synthesis
CC       through SREBF1/SREBP1 and LPIN1 (By similarity). To maintain energy
CC       homeostasis mTORC1 may also regulate mitochondrial biogenesis through
CC       regulation of PPARGC1A (By similarity). mTORC1 also negatively
CC       regulates autophagy through phosphorylation of ULK1 (By similarity).
CC       Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-758',
CC       disrupting the interaction with AMPK and preventing activation of ULK1
CC       (By similarity). Also prevents autophagy through phosphorylation of the
CC       autophagy inhibitor DAP (PubMed:20537536). Also prevents autophagy by
CC       phosphorylating RUBCNL/Pacer under nutrient-rich conditions
CC       (PubMed:30704899). mTORC1 exerts a feedback control on upstream growth
CC       factor signaling that includes phosphorylation and activation of GRB10
CC       a INSR-dependent signaling suppressor (PubMed:21659604). Among other
CC       potential targets mTORC1 may phosphorylate CLIP1 and regulate
CC       microtubules (PubMed:12231510). As part of the mTORC2 complex MTOR may
CC       regulate other cellular processes including survival and organization
CC       of the cytoskeleton (PubMed:15268862, PubMed:15467718). Plays a
CC       critical role in the phosphorylation at 'Ser-473' of AKT1, a pro-
CC       survival effector of phosphoinositide 3-kinase, facilitating its
CC       activation by PDK1 (PubMed:15718470). mTORC2 may regulate the actin
CC       cytoskeleton, through phosphorylation of PRKCA, PXN and activation of
CC       the Rho-type guanine nucleotide exchange factors RHOA and RAC1A or
CC       RAC1B (PubMed:15268862). mTORC2 also regulates the phosphorylation of
CC       SGK1 at 'Ser-422' (PubMed:18925875). Regulates osteoclastogenesis by
CC       adjusting the expression of CEBPB isoforms (By similarity). Plays an
CC       important regulatory role in the circadian clock function; regulates
CC       period length and rhythm amplitude of the suprachiasmatic nucleus (SCN)
CC       and liver clocks (By similarity). Phosphorylates SQSTM1, promoting
CC       interaction between SQSTM1 and KEAP1 and subsequent inactivation of the
CC       BCR(KEAP1) complex (By similarity). {ECO:0000250|UniProtKB:P42346,
CC       ECO:0000250|UniProtKB:Q9JLN9, ECO:0000269|PubMed:12087098,
CC       ECO:0000269|PubMed:12150925, ECO:0000269|PubMed:12150926,
CC       ECO:0000269|PubMed:12231510, ECO:0000269|PubMed:12718876,
CC       ECO:0000269|PubMed:14651849, ECO:0000269|PubMed:15268862,
CC       ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:15545625,
CC       ECO:0000269|PubMed:15718470, ECO:0000269|PubMed:18497260,
CC       ECO:0000269|PubMed:18762023, ECO:0000269|PubMed:18925875,
CC       ECO:0000269|PubMed:20516213, ECO:0000269|PubMed:20537536,
CC       ECO:0000269|PubMed:21576368, ECO:0000269|PubMed:21659604,
CC       ECO:0000269|PubMed:23429703, ECO:0000269|PubMed:23429704,
CC       ECO:0000269|PubMed:25799227, ECO:0000269|PubMed:26018084,
CC       ECO:0000269|PubMed:30704899}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000269|PubMed:12087098, ECO:0000269|PubMed:12150925,
CC         ECO:0000269|PubMed:12231510, ECO:0000269|PubMed:15268862,
CC         ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:15718470,
CC         ECO:0000269|PubMed:18925875, ECO:0000269|PubMed:20516213,
CC         ECO:0000269|PubMed:20537536, ECO:0000269|PubMed:21659604};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000269|PubMed:12087098,
CC         ECO:0000269|PubMed:12150925, ECO:0000269|PubMed:12231510,
CC         ECO:0000269|PubMed:15268862, ECO:0000269|PubMed:15467718,
CC         ECO:0000269|PubMed:15718470, ECO:0000269|PubMed:18925875,
CC         ECO:0000269|PubMed:20516213, ECO:0000269|PubMed:20537536,
CC         ECO:0000269|PubMed:21659604};
CC   -!- ACTIVITY REGULATION: Activation of mTORC1 by growth factors such as
CC       insulin involves AKT1-mediated phosphorylation of TSC1-TSC2, which
CC       leads to the activation of the RHEB GTPase a potent activator of the
CC       protein kinase activity of mTORC1. Insulin-stimulated and amino acid-
CC       dependent phosphorylation at Ser-1261 promotes autophosphorylation and
CC       the activation of mTORC1. Activation by amino acids requires
CC       relocalization of the mTORC1 complex to lysosomes that is mediated by
CC       the Ragulator complex, SLC38A9, and the Rag GTPases RRAGA, RRAGB, RRAGC
CC       and RRAGD (PubMed:18497260, PubMed:20381137, PubMed:25561175,
CC       PubMed:25567906). On the other hand, low cellular energy levels can
CC       inhibit mTORC1 through activation of PRKAA1 while hypoxia inhibits
CC       mTORC1 through a REDD1-dependent mechanism which may also require
CC       PRKAA1. The kinase activity of MTOR within the mTORC1 complex is
CC       positively regulated by MLST8 and negatively regulated by DEPTOR and
CC       AKT1S1. MTOR phosphorylates RPTOR which in turn inhibits mTORC1. MTOR
CC       is the target of the immunosuppressive and anti-cancer drug rapamycin
CC       which acts in complex with FKBP1A/FKBP12, and specifically inhibits its
CC       kinase activity. mTORC2 is also activated by growth factors, but seems
CC       to be nutrient-insensitive. It may be regulated by RHEB but in an
CC       indirect manner through the PI3K signaling pathway.
CC       {ECO:0000269|PubMed:14651849, ECO:0000269|PubMed:15545625,
CC       ECO:0000269|PubMed:17386266, ECO:0000269|PubMed:18497260,
CC       ECO:0000269|PubMed:19446321, ECO:0000269|PubMed:20381137,
CC       ECO:0000269|PubMed:25561175, ECO:0000269|PubMed:25567906}.
CC   -!- SUBUNIT: Part of the mammalian target of rapamycin complex 1 (mTORC1)
CC       which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR. The mTORC1
CC       complex is a 1 Md obligate dimer of two stoichiometric heterotetramers
CC       with overall dimensions of 290 A x 210 A x 135 A. It has a rhomboid
CC       shape and a central cavity, the dimeric interfaces are formed by
CC       interlocking interactions between the two MTOR and the two RPTOR
CC       subunits. The MLST8 subunit forms distal foot-like protuberances, and
CC       contacts only one MTOR within the complex, while the small PRAS40
CC       localizes to the midsection of the central core, in close proximity to
CC       RPTOR. Part of the mammalian target of rapamycin complex 2 (mTORC2)
CC       which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR. Interacts
CC       with PLPP7 and PML. Interacts with PRR5 and RICTOR; the interaction is
CC       direct within the mTORC2 complex. Interacts with WAC; WAC positively
CC       regulates MTOR activity by promoting the assembly of the TTT complex
CC       composed of TELO2, TTI1 and TTI2 and the RUVBL complex composed of
CC       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 UBQLN1. Interacts with TTI1 and
CC       TELO2. Interacts with CLIP1; phosphorylates and regulates CLIP1.
CC       Interacts with NBN. Interacts with HTR6 (PubMed:23027611). Interacts
CC       with BRAT1. Interacts with MEAK7 (via C-terminal domain); the
CC       interaction increases upon nutrient stimulation (PubMed:29750193).
CC       Interacts with TM4SF5; the interaction is positively regulated by
CC       arginine and is negatively regulated by leucine (PubMed:30956113).
CC       {ECO:0000269|PubMed:10089303, ECO:0000269|PubMed:11853878,
CC       ECO:0000269|PubMed:12150925, ECO:0000269|PubMed:12150926,
CC       ECO:0000269|PubMed:12231510, ECO:0000269|PubMed:12408816,
CC       ECO:0000269|PubMed:12718876, ECO:0000269|PubMed:15268862,
CC       ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:17386266,
CC       ECO:0000269|PubMed:17599906, ECO:0000269|PubMed:18925875,
CC       ECO:0000269|PubMed:19446321, ECO:0000269|PubMed:20427287,
CC       ECO:0000269|PubMed:20542007, ECO:0000269|PubMed:20801936,
CC       ECO:0000269|PubMed:20810650, ECO:0000269|PubMed:23027611,
CC       ECO:0000269|PubMed:23636326, ECO:0000269|PubMed:23762398,
CC       ECO:0000269|PubMed:25657994, ECO:0000269|PubMed:26812014,
CC       ECO:0000269|PubMed:29750193, ECO:0000269|PubMed:30956113,
CC       ECO:0000269|PubMed:8662507}.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-359260, EBI-359260;
CC       P31749:AKT1; NbExp=4; IntAct=EBI-359260, EBI-296087;
CC       Q07817-1:BCL2L1; NbExp=4; IntAct=EBI-359260, EBI-287195;
CC       Q8TB45:DEPTOR; NbExp=5; IntAct=EBI-359260, EBI-2359040;
CC       Q13541:EIF4EBP1; NbExp=2; IntAct=EBI-359260, EBI-74090;
CC       P62942:FKBP1A; NbExp=5; IntAct=EBI-359260, EBI-1027571;
CC       Q8WUA4:GTF3C2; NbExp=3; IntAct=EBI-359260, EBI-1237062;
CC       Q9BVC4:MLST8; NbExp=5; IntAct=EBI-359260, EBI-1387471;
CC       Q9BVC4-1:MLST8; NbExp=7; IntAct=EBI-359260, EBI-16056342;
CC       Q13615:MTMR3; NbExp=3; IntAct=EBI-359260, EBI-371938;
CC       Q8TCU6:PREX1; NbExp=11; IntAct=EBI-359260, EBI-1046542;
CC       P62820:RAB1A; NbExp=4; IntAct=EBI-359260, EBI-716845;
CC       Q15382:RHEB; NbExp=2; IntAct=EBI-359260, EBI-1055287;
CC       Q6R327:RICTOR; NbExp=34; IntAct=EBI-359260, EBI-1387196;
CC       Q8N122:RPTOR; NbExp=47; IntAct=EBI-359260, EBI-1567928;
CC       Q96EB6:SIRT1; NbExp=2; IntAct=EBI-359260, EBI-1802965;
CC       Q8NHX9:TPCN2; NbExp=2; IntAct=EBI-359260, EBI-5239949;
CC       O75385:ULK1; NbExp=7; IntAct=EBI-359260, EBI-908831;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:14578359}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:14578359}; Cytoplasmic side
CC       {ECO:0000269|PubMed:14578359}. Golgi apparatus membrane
CC       {ECO:0000269|PubMed:14578359}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:14578359}; Cytoplasmic side
CC       {ECO:0000269|PubMed:14578359}. Mitochondrion outer membrane
CC       {ECO:0000269|PubMed:11930000, ECO:0000269|PubMed:14578359}; Peripheral
CC       membrane protein {ECO:0000269|PubMed:11930000,
CC       ECO:0000269|PubMed:14578359}; Cytoplasmic side
CC       {ECO:0000269|PubMed:11930000, ECO:0000269|PubMed:14578359}. Lysosome
CC       {ECO:0000269|PubMed:18497260, ECO:0000269|PubMed:20381137,
CC       ECO:0000269|PubMed:29750193}. Cytoplasm {ECO:0000269|PubMed:11930000,
CC       ECO:0000269|PubMed:18497260}. Nucleus, PML body
CC       {ECO:0000250|UniProtKB:Q9JLN9}. Microsome membrane
CC       {ECO:0000269|PubMed:9434772}. Lysosome membrane
CC       {ECO:0000269|PubMed:30956113}. Note=Shuttles between cytoplasm and
CC       nucleus. Accumulates in the nucleus in response to hypoxia (By
CC       similarity). Targeting to lysosomes depends on amino acid availability
CC       and RRAGA and RRAGB (PubMed:18497260, PubMed:20381137). Lysosome
CC       targeting also depends on interaction with MEAK7. Translocates to the
CC       lysosome membrane in the presence of TM4SF5 (PubMed:30956113).
CC       {ECO:0000250|UniProtKB:Q9JLN9, ECO:0000269|PubMed:18497260,
CC       ECO:0000269|PubMed:20381137, ECO:0000269|PubMed:29750193,
CC       ECO:0000269|PubMed:30956113}.
CC   -!- TISSUE SPECIFICITY: Expressed in numerous tissues, with highest levels
CC       in testis. {ECO:0000269|PubMed:12408816, ECO:0000269|PubMed:7809080}.
CC   -!- DOMAIN: The kinase domain (PI3K/PI4K) is intrinsically active but has a
CC       highly restricted catalytic center. {ECO:0000269|PubMed:23636326}.
CC   -!- DOMAIN: The FAT domain forms three discontinuous subdomains of alpha-
CC       helical TPR repeats plus a single subdomain of HEAT repeats. The four
CC       domains pack sequentially to form a C-shaped a-solenoid that clamps
CC       onto the kinase domain (PubMed:23636326).
CC       {ECO:0000269|PubMed:23636326}.
CC   -!- PTM: Autophosphorylates when part of mTORC1 or mTORC2. Phosphorylation
CC       at Ser-1261, Ser-2159 and Thr-2164 promotes autophosphorylation.
CC       Phosphorylation in the kinase domain modulates the interactions of MTOR
CC       with RPTOR and PRAS40 and leads to increased intrinsic mTORC1 kinase
CC       activity. Phosphorylation at Thr-2173 in the ATP-binding region by AKT1
CC       strongly reduces kinase activity. {ECO:0000269|PubMed:15905173,
CC       ECO:0000269|PubMed:19145465, ECO:0000269|PubMed:19487463,
CC       ECO:0000269|PubMed:21576368, ECO:0000269|PubMed:23429703,
CC       ECO:0000269|PubMed:23429704, ECO:0000269|PubMed:24247430}.
CC   -!- DISEASE: Smith-Kingsmore syndrome (SKS) [MIM:616638]: An autosomal
CC       dominant syndrome characterized by intellectual disability,
CC       macrocephaly, seizures, umbilical hernia, and facial dysmorphic
CC       features. {ECO:0000269|PubMed:25851998, ECO:0000269|PubMed:26542245,
CC       ECO:0000269|PubMed:27830187}. Note=The disease is caused by mutations
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Focal cortical dysplasia 2 (FCORD2) [MIM:607341]: A form of
CC       focal cortical dysplasia, a malformation of cortical development that
CC       results in medically refractory epilepsy in the pediatric population
CC       and in adults. FCORD2 is a severe form, with onset usually in
CC       childhood, characterized by disrupted cortical lamination and specific
CC       cytological abnormalities. It is classified in 2 subtypes: type IIA
CC       characterized by dysmorphic neurons and lack of balloon cells; type IIB
CC       with dysmorphic neurons and balloon cells.
CC       {ECO:0000269|PubMed:25799227, ECO:0000269|PubMed:25878179,
CC       ECO:0000269|PubMed:26018084, ECO:0000269|PubMed:27830187}. Note=The
CC       disease is caused by mutations affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC39933.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAE06077.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/FRAP1ID40639ch1p36.html";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Mammalian target of rapamycin entry;
CC       URL="https://en.wikipedia.org/wiki/Mammalian_target_of_rapamycin";
DR   EMBL; L34075; AAA58486.1; -; mRNA.
DR   EMBL; U88966; AAC39933.1; ALT_FRAME; mRNA.
DR   EMBL; AB209995; BAE06077.1; ALT_INIT; mRNA.
DR   EMBL; AL109811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL391561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL049653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC117166; AAI17167.1; -; mRNA.
DR   EMBL; AJ300188; CAC15570.1; -; Genomic_DNA.
DR   EMBL; L35478; AAC41713.1; -; mRNA.
DR   CCDS; CCDS127.1; -.
DR   PIR; S45340; S45340.
DR   RefSeq; NP_004949.1; NM_004958.3.
DR   RefSeq; XP_005263495.1; XM_005263438.2.
DR   PDB; 1AUE; X-ray; 2.33 A; A/B=2015-2114.
DR   PDB; 1FAP; X-ray; 2.70 A; B=2018-2112.
DR   PDB; 1NSG; X-ray; 2.20 A; B=2019-2112.
DR   PDB; 2FAP; X-ray; 2.20 A; B=2019-2112.
DR   PDB; 2GAQ; NMR; -; A=2015-2114.
DR   PDB; 2NPU; NMR; -; A=2015-2114.
DR   PDB; 2RSE; NMR; -; B=2019-2112.
DR   PDB; 3FAP; X-ray; 1.85 A; B=2019-2112.
DR   PDB; 3JBZ; EM; 28.00 A; A=1385-2549.
DR   PDB; 4DRH; X-ray; 2.30 A; B/E=2025-2114.
DR   PDB; 4DRI; X-ray; 1.45 A; B=2025-2114.
DR   PDB; 4DRJ; X-ray; 1.80 A; B=2025-2114.
DR   PDB; 4FAP; X-ray; 2.80 A; B=2019-2112.
DR   PDB; 4JSN; X-ray; 3.20 A; A/B=1376-2549.
DR   PDB; 4JSP; X-ray; 3.30 A; A/B=1376-2549.
DR   PDB; 4JSV; X-ray; 3.50 A; A/B=1376-2549.
DR   PDB; 4JSX; X-ray; 3.50 A; A/B=1376-2549.
DR   PDB; 4JT5; X-ray; 3.45 A; A/B=1376-2549.
DR   PDB; 4JT6; X-ray; 3.60 A; A/B=1376-2549.
DR   PDB; 5FLC; EM; 5.90 A; B/F=1382-2549.
DR   PDB; 5GPG; X-ray; 1.67 A; B=2021-2112.
DR   PDB; 5H64; EM; 4.40 A; A/a=1-2549.
DR   PDB; 5WBH; X-ray; 1.75 A; A/B/C/D/E=2018-2114.
DR   PDB; 5WBU; X-ray; 3.42 A; A/B=1376-2549.
DR   PDB; 5WBY; X-ray; 3.10 A; A/B=1376-2549.
DR   PDB; 5ZCS; EM; 4.90 A; A/B=1-2549.
DR   PDB; 6BCU; EM; 3.43 A; A/B=1-2549.
DR   PDB; 6BCX; EM; 3.00 A; A/B=1-2549.
DR   PDBsum; 1AUE; -.
DR   PDBsum; 1FAP; -.
DR   PDBsum; 1NSG; -.
DR   PDBsum; 2FAP; -.
DR   PDBsum; 2GAQ; -.
DR   PDBsum; 2NPU; -.
DR   PDBsum; 2RSE; -.
DR   PDBsum; 3FAP; -.
DR   PDBsum; 3JBZ; -.
DR   PDBsum; 4DRH; -.
DR   PDBsum; 4DRI; -.
DR   PDBsum; 4DRJ; -.
DR   PDBsum; 4FAP; -.
DR   PDBsum; 4JSN; -.
DR   PDBsum; 4JSP; -.
DR   PDBsum; 4JSV; -.
DR   PDBsum; 4JSX; -.
DR   PDBsum; 4JT5; -.
DR   PDBsum; 4JT6; -.
DR   PDBsum; 5FLC; -.
DR   PDBsum; 5GPG; -.
DR   PDBsum; 5H64; -.
DR   PDBsum; 5WBH; -.
DR   PDBsum; 5WBU; -.
DR   PDBsum; 5WBY; -.
DR   PDBsum; 5ZCS; -.
DR   PDBsum; 6BCU; -.
DR   PDBsum; 6BCX; -.
DR   SMR; P42345; -.
DR   BioGrid; 108757; 228.
DR   ComplexPortal; CPX-4402; mTORC2 complex.
DR   ComplexPortal; CPX-503; mTORC1 complex.
DR   CORUM; P42345; -.
DR   DIP; DIP-790N; -.
DR   IntAct; P42345; 102.
DR   MINT; P42345; -.
DR   STRING; 9606.ENSP00000354558; -.
DR   BindingDB; P42345; -.
DR   ChEMBL; CHEMBL2842; -.
DR   DrugBank; DB04974; AP1903.
DR   DrugBank; DB01590; Everolimus.
DR   DrugBank; DB12010; Fostamatinib.
DR   DrugBank; DB00337; Pimecrolimus.
DR   DrugBank; DB06233; Ridaforolimus.
DR   DrugBank; DB05210; SF1126.
DR   DrugBank; DB00877; Sirolimus.
DR   DrugBank; DB06287; Temsirolimus.
DR   DrugBank; DB05241; XL765.
DR   DrugCentral; P42345; -.
DR   GuidetoPHARMACOLOGY; 2109; -.
DR   iPTMnet; P42345; -.
DR   PhosphoSitePlus; P42345; -.
DR   SwissPalm; P42345; -.
DR   BioMuta; MTOR; -.
DR   DMDM; 1169735; -.
DR   CPTAC; CPTAC-1360; -.
DR   CPTAC; CPTAC-1361; -.
DR   EPD; P42345; -.
DR   jPOST; P42345; -.
DR   MassIVE; P42345; -.
DR   MaxQB; P42345; -.
DR   PaxDb; P42345; -.
DR   PeptideAtlas; P42345; -.
DR   PRIDE; P42345; -.
DR   ProteomicsDB; 55511; -.
DR   Ensembl; ENST00000361445; ENSP00000354558; ENSG00000198793.
DR   GeneID; 2475; -.
DR   KEGG; hsa:2475; -.
DR   UCSC; uc001asd.4; human.
DR   CTD; 2475; -.
DR   DisGeNET; 2475; -.
DR   EuPathDB; HostDB:ENSG00000198793.12; -.
DR   GeneCards; MTOR; -.
DR   HGNC; HGNC:3942; MTOR.
DR   HPA; CAB069425; -.
DR   HPA; HPA071227; -.
DR   MalaCards; MTOR; -.
DR   MIM; 601231; gene.
DR   MIM; 607341; phenotype.
DR   MIM; 616638; phenotype.
DR   neXtProt; NX_P42345; -.
DR   OpenTargets; ENSG00000198793; -.
DR   Orphanet; 269001; Isolated focal cortical dysplasia type IIa.
DR   Orphanet; 269008; Isolated focal cortical dysplasia type IIb.
DR   Orphanet; 457485; Macrocephaly-intellectual disability-neurodevelopmental disorder-small thorax syndrome.
DR   PharmGKB; PA28360; -.
DR   eggNOG; KOG0891; Eukaryota.
DR   eggNOG; COG5032; LUCA.
DR   GeneTree; ENSGT00930000151037; -.
DR   HOGENOM; HOG000163215; -.
DR   InParanoid; P42345; -.
DR   KO; K07203; -.
DR   OMA; LNIQRYP; -.
DR   OrthoDB; 26975at2759; -.
DR   PhylomeDB; P42345; -.
DR   TreeFam; TF105134; -.
DR   Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
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-389357; CD28 dependent PI3K/Akt signaling.
DR   Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
DR   Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
DR   Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
DR   Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR   Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR   SABIO-RK; P42345; -.
DR   SignaLink; P42345; -.
DR   SIGNOR; P42345; -.
DR   ChiTaRS; MTOR; human.
DR   EvolutionaryTrace; P42345; -.
DR   GeneWiki; Mammalian_target_of_rapamycin; -.
DR   GenomeRNAi; 2475; -.
DR   Pharos; P42345; Tclin.
DR   PRO; PR:P42345; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P42345; protein.
DR   Bgee; ENSG00000198793; Expressed in 167 organ(s), highest expression level in testis.
DR   ExpressionAtlas; P42345; baseline and differential.
DR   Genevisible; P42345; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0012505; C:endomembrane system; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR   GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0099524; C:postsynaptic cytosol; IEA:Ensembl.
DR   GO; GO:0031931; C:TORC1 complex; IDA:UniProtKB.
DR   GO; GO:0031932; C:TORC2 complex; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0016301; F:kinase activity; IDA:MGI.
DR   GO; GO:0051219; F:phosphoprotein binding; IPI:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR   GO; GO:0004672; F:protein kinase activity; IDA:WormBase.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0043022; F:ribosome binding; IEA:Ensembl.
DR   GO; GO:0001030; F:RNA polymerase III type 1 promoter DNA binding; IDA:UniProtKB.
DR   GO; GO:0001031; F:RNA polymerase III type 2 promoter DNA binding; IDA:UniProtKB.
DR   GO; GO:0001032; F:RNA polymerase III type 3 promoter DNA binding; IDA:UniProtKB.
DR   GO; GO:0001156; F:TFIIIC-class transcription factor complex binding; IDA:UniProtKB.
DR   GO; GO:0045182; F:translation regulator activity; IEA:Ensembl.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:Ensembl.
DR   GO; GO:0032148; P:activation of protein kinase B activity; TAS:Reactome.
DR   GO; GO:0043276; P:anoikis; NAS:ParkinsonsUK-UCL.
DR   GO; GO:0007420; P:brain development; IEA:Ensembl.
DR   GO; GO:0055013; P:cardiac muscle cell development; IEA:Ensembl.
DR   GO; GO:0060048; P:cardiac muscle contraction; IEA:Ensembl.
DR   GO; GO:0007569; P:cell aging; IEA:Ensembl.
DR   GO; GO:0007050; P:cell cycle arrest; TAS:Reactome.
DR   GO; GO:0034198; P:cellular response to amino acid starvation; IDA:CAFA.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:CAFA.
DR   GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
DR   GO; GO:0071233; P:cellular response to leucine; IDA:CAFA.
DR   GO; GO:1990253; P:cellular response to leucine starvation; IDA:CAFA.
DR   GO; GO:0031669; P:cellular response to nutrient levels; ISS:UniProtKB.
DR   GO; GO:0009267; P:cellular response to starvation; IDA:UniProtKB.
DR   GO; GO:0006112; P:energy reserve metabolic process; IEA:Ensembl.
DR   GO; GO:0007281; P:germ cell development; IEA:Ensembl.
DR   GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
DR   GO; GO:0003179; P:heart valve morphogenesis; IEA:Ensembl.
DR   GO; GO:0007616; P:long-term memory; IEA:Ensembl.
DR   GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
DR   GO; GO:0048255; P:mRNA stabilization; IEA:Ensembl.
DR   GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0010507; P:negative regulation of autophagy; IDA:UniProtKB.
DR   GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; IEA:Ensembl.
DR   GO; GO:0045792; P:negative regulation of cell size; IEA:Ensembl.
DR   GO; GO:1904193; P:negative regulation of cholangiocyte apoptotic process; IEA:Ensembl.
DR   GO; GO:1904213; P:negative regulation of iodide transmembrane transport; IEA:Ensembl.
DR   GO; GO:0016242; P:negative regulation of macroautophagy; IDA:MGI.
DR   GO; GO:0014736; P:negative regulation of muscle atrophy; IEA:Ensembl.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:UniProtKB.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IDA:UniProtKB.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR   GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; IEA:Ensembl.
DR   GO; GO:1904056; P:positive regulation of cholangiocyte proliferation; IEA:Ensembl.
DR   GO; GO:1904690; P:positive regulation of cytoplasmic translational initiation; TAS:ARUK-UCL.
DR   GO; GO:0060999; P:positive regulation of dendritic spine development; IEA:Ensembl.
DR   GO; GO:1904000; P:positive regulation of eating behavior; IEA:Ensembl.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0060252; P:positive regulation of glial cell proliferation; IEA:Ensembl.
DR   GO; GO:1904197; P:positive regulation of granulosa cell proliferation; IEA:Ensembl.
DR   GO; GO:0051549; P:positive regulation of keratinocyte migration; IMP:BHF-UCL.
DR   GO; GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Ensembl.
DR   GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0010831; P:positive regulation of myotube differentiation; IEA:Ensembl.
DR   GO; GO:1901216; P:positive regulation of neuron death; IEA:Ensembl.
DR   GO; GO:0014042; P:positive regulation of neuron maturation; IEA:Ensembl.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; TAS:ARUK-UCL.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:1904058; P:positive regulation of sensory perception of pain; IEA:Ensembl.
DR   GO; GO:1904206; P:positive regulation of skeletal muscle hypertrophy; IEA:Ensembl.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR   GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IMP:UniProtKB.
DR   GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; IMP:UniProtKB.
DR   GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB.
DR   GO; GO:1903691; P:positive regulation of wound healing, spreading of epidermal cells; IMP:BHF-UCL.
DR   GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR   GO; GO:0030163; P:protein catabolic process; TAS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
DR   GO; GO:0090335; P:regulation of brown fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0043610; P:regulation of carbohydrate utilization; IEA:Ensembl.
DR   GO; GO:0001558; P:regulation of cell growth; IDA:UniProtKB.
DR   GO; GO:0008361; P:regulation of cell size; IMP:CAFA.
DR   GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
DR   GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR   GO; GO:0031998; P:regulation of fatty acid beta-oxidation; IEA:Ensembl.
DR   GO; GO:0005979; P:regulation of glycogen biosynthetic process; IEA:Ensembl.
DR   GO; GO:0043087; P:regulation of GTPase activity; IEA:Ensembl.
DR   GO; GO:1904059; P:regulation of locomotor rhythm; ISS:UniProtKB.
DR   GO; GO:0016241; P:regulation of macroautophagy; TAS:Reactome.
DR   GO; GO:0090559; P:regulation of membrane permeability; IEA:Ensembl.
DR   GO; GO:0031641; P:regulation of myelination; IEA:Ensembl.
DR   GO; GO:0045670; P:regulation of osteoclast differentiation; ISS:UniProtKB.
DR   GO; GO:0032095; P:regulation of response to food; IEA:Ensembl.
DR   GO; GO:0099547; P:regulation of translation at synapse, modulating synaptic transmission; IEA:Ensembl.
DR   GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR   GO; GO:0043200; P:response to amino acid; IDA:UniProtKB.
DR   GO; GO:0042220; P:response to cocaine; IEA:Ensembl.
DR   GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR   GO; GO:0043278; P:response to morphine; IEA:Ensembl.
DR   GO; GO:0007584; P:response to nutrient; IMP:UniProtKB.
DR   GO; GO:0031667; P:response to nutrient levels; IDA:UniProtKB.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0031529; P:ruffle organization; IEA:Ensembl.
DR   GO; GO:0035176; P:social behavior; IEA:Ensembl.
DR   GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR   GO; GO:0002296; P:T-helper 1 cell lineage commitment; IEA:Ensembl.
DR   GO; GO:0031929; P:TOR signaling; IMP:UniProtKB.
DR   GO; GO:0038202; P:TORC1 signaling; IDA:UniProtKB.
DR   GO; GO:0008542; P:visual learning; IEA:Ensembl.
DR   GO; GO:0050882; P:voluntary musculoskeletal movement; IEA:Ensembl.
DR   GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR   Gene3D; 1.10.1070.11; -; 1.
DR   Gene3D; 1.20.120.150; -; 1.
DR   Gene3D; 1.25.10.10; -; 4.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR024585; DUF3385_TOR.
DR   InterPro; IPR003152; FATC_dom.
DR   InterPro; IPR009076; FRB_dom.
DR   InterPro; IPR036738; FRB_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR   InterPro; IPR018936; PI3/4_kinase_CS.
DR   InterPro; IPR003151; PIK-rel_kinase_FAT.
DR   InterPro; IPR014009; PIK_FAT.
DR   InterPro; IPR026683; TOR.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR11139:SF9; PTHR11139:SF9; 1.
DR   Pfam; PF11865; DUF3385; 1.
DR   Pfam; PF02259; FAT; 1.
DR   Pfam; PF02260; FATC; 1.
DR   Pfam; PF08771; FRB_dom; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   SMART; SM01346; DUF3385; 1.
DR   SMART; SM01343; FATC; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF47212; SSF47212; 1.
DR   SUPFAM; SSF48371; SSF48371; 2.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51189; FAT; 1.
DR   PROSITE; PS51190; FATC; 1.
DR   PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Biological rhythms; Cytoplasm;
KW   Disease mutation; Endoplasmic reticulum; Epilepsy; Golgi apparatus; Kinase;
KW   Lysosome; Membrane; Mental retardation; Microsome; Mitochondrion;
KW   Mitochondrion outer membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Polymorphism; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW   TPR repeat; Transferase.
FT   CHAIN           1..2549
FT                   /note="Serine/threonine-protein kinase mTOR"
FT                   /id="PRO_0000088808"
FT   REPEAT          16..53
FT                   /note="HEAT 1"
FT   REPEAT          55..99
FT                   /note="HEAT 2"
FT   REPEAT          100..137
FT                   /note="HEAT 3"
FT   REPEAT          138..179
FT                   /note="HEAT 4"
FT   REPEAT          180..220
FT                   /note="HEAT 5"
FT   REPEAT          222..276
FT                   /note="HEAT 6"
FT   REPEAT          277..313
FT                   /note="HEAT 7"
FT   REPEAT          314..364
FT                   /note="HEAT 8"
FT   REPEAT          365..409
FT                   /note="HEAT 9"
FT   REPEAT          410..445
FT                   /note="HEAT 10"
FT   REPEAT          446..494
FT                   /note="HEAT 11"
FT   REPEAT          495..529
FT                   /note="HEAT 12"
FT   REPEAT          530..563
FT                   /note="HEAT 13"
FT   REPEAT          564..596
FT                   /note="HEAT 14"
FT   REPEAT          597..636
FT                   /note="HEAT 15"
FT   REPEAT          637..683
FT                   /note="HEAT 16"
FT   REPEAT          686..724
FT                   /note="HEAT 17"
FT   REPEAT          727..766
FT                   /note="HEAT 18"
FT   REPEAT          769..811
FT                   /note="HEAT 19"
FT   REPEAT          814..853
FT                   /note="HEAT 20"
FT   REPEAT          857..893
FT                   /note="HEAT 21"
FT   REPEAT          894..942
FT                   /note="HEAT 22"
FT   REPEAT          943..988
FT                   /note="HEAT 23"
FT   REPEAT          989..1027
FT                   /note="HEAT 24"
FT   REPEAT          1029..1068
FT                   /note="HEAT 25"
FT   REPEAT          1069..1105
FT                   /note="HEAT 26"
FT   REPEAT          1106..1144
FT                   /note="HEAT 27"
FT   REPEAT          1145..1188
FT                   /note="HEAT 28"
FT   REPEAT          1189..1225
FT                   /note="HEAT 29"
FT   REPEAT          1226..1273
FT                   /note="HEAT 30"
FT   REPEAT          1274..1311
FT                   /note="HEAT 31"
FT   REPEAT          1312..1345
FT                   /note="HEAT 32"
FT   REPEAT          1346..1382
FT                   /note="TPR 1"
FT   DOMAIN          1382..1982
FT                   /note="FAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT   REPEAT          1383..1408
FT                   /note="TPR 2"
FT   REPEAT          1409..1442
FT                   /note="TPR 3"
FT   REPEAT          1443..1473
FT                   /note="TPR 4"
FT   REPEAT          1474..1507
FT                   /note="TPR 5"
FT   REPEAT          1508..1541
FT                   /note="TPR 6"
FT   REPEAT          1542..1574
FT                   /note="TPR 7"
FT   REPEAT          1575..1614
FT                   /note="TPR 8"
FT   REPEAT          1615..1649
FT                   /note="TPR 9"
FT   REPEAT          1650..1693
FT                   /note="TPR 10"
FT   REPEAT          1694..1731
FT                   /note="TPR 11"
FT   REPEAT          1732..1786
FT                   /note="TPR 12"
FT   REPEAT          1787..1846
FT                   /note="TPR 13"
FT   REPEAT          1898..1930
FT                   /note="TPR 14"
FT   REPEAT          1931..1970
FT                   /note="TPR 15"
FT   REPEAT          1971..2005
FT                   /note="TPR 16"
FT   DOMAIN          2182..2516
FT                   /note="PI3K/PI4K"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   DOMAIN          2517..2549
FT                   /note="FATC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT                   ECO:0000255|PROSITE-ProRule:PRU00535"
FT   REGION          1..651
FT                   /note="Interaction with NBN"
FT                   /evidence="ECO:0000269|PubMed:23762398"
FT   REGION          2012..2144
FT                   /note="Sufficient for interaction with the FKBP1A/rapamycin
FT                   complex"
FT                   /evidence="ECO:0000250"
FT   REGION          2258..2296
FT                   /note="Interaction with MLST8"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000244|PubMed:22814378"
FT   MOD_RES         567
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18691976,
FT                   ECO:0000244|PubMed:19369195, ECO:0000244|PubMed:20068231"
FT   MOD_RES         1162
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:20068231"
FT   MOD_RES         1218
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   MOD_RES         1261
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163,
FT                   ECO:0000269|PubMed:19487463"
FT   MOD_RES         2159
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:21576368"
FT   MOD_RES         2164
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:21576368"
FT   MOD_RES         2173
FT                   /note="Phosphothreonine; by PKB/AKT1"
FT                   /evidence="ECO:0000269|PubMed:24247430"
FT   MOD_RES         2446
FT                   /note="Phosphothreonine; by RPS6KB1"
FT                   /evidence="ECO:0000269|PubMed:15905173"
FT   MOD_RES         2448
FT                   /note="Phosphoserine; by RPS6KB1"
FT                   /evidence="ECO:0000244|PubMed:24275569,
FT                   ECO:0000269|PubMed:15905173, ECO:0000269|PubMed:19145465"
FT   MOD_RES         2478
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   MOD_RES         2481
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000269|PubMed:21576368"
FT   VARIANT         8
FT                   /note="A -> S (in a lung large cell carcinoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041537"
FT   VARIANT         135
FT                   /note="M -> T (in a metastatic melanoma sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041538"
FT   VARIANT         624
FT                   /note="R -> H (in FCORD2; somatic mutation; unknown
FT                   pathological significance; dbSNP:rs913197212)"
FT                   /evidence="ECO:0000269|PubMed:25799227"
FT                   /id="VAR_078824"
FT   VARIANT         1083
FT                   /note="M -> V (in dbSNP:rs56164650)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041539"
FT   VARIANT         1134
FT                   /note="A -> V (in dbSNP:rs28730685)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041540"
FT   VARIANT         1178
FT                   /note="S -> F (in dbSNP:rs55975118)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041541"
FT   VARIANT         1376
FT                   /note="D -> E (found in a patient with focal epilepsy;
FT                   unknown pathological significance; dbSNP:rs975577894)"
FT                   /evidence="ECO:0000269|PubMed:27830187"
FT                   /id="VAR_078825"
FT   VARIANT         1450
FT                   /note="Y -> D (in FCORD2; somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:25799227"
FT                   /id="VAR_078826"
FT   VARIANT         1456
FT                   /note="W -> G (in FCORD2; somatic mutation;
FT                   dbSNP:rs1085307114)"
FT                   /evidence="ECO:0000269|PubMed:25878179"
FT                   /id="VAR_078827"
FT   VARIANT         1459
FT                   /note="A -> D (in FCORD2; somatic mutation; increased TOR
FT                   signaling)"
FT                   /evidence="ECO:0000269|PubMed:26018084"
FT                   /id="VAR_078828"
FT   VARIANT         1459
FT                   /note="A -> S (in FCORD2; somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:27830187"
FT                   /id="VAR_078829"
FT   VARIANT         1460
FT                   /note="L -> P (in FCORD2; somatic mutation; increased TOR
FT                   signaling; dbSNP:rs1057519779)"
FT                   /evidence="ECO:0000269|PubMed:26018084,
FT                   ECO:0000269|PubMed:27830187"
FT                   /id="VAR_078830"
FT   VARIANT         1483
FT                   /note="C -> R (in FCORD2; somatic mutation; increased TOR
FT                   signaling; increased kinase activity; dbSNP:rs1057519914)"
FT                   /evidence="ECO:0000269|PubMed:25799227"
FT                   /id="VAR_078831"
FT   VARIANT         1490
FT                   /note="W -> R (in SKS)"
FT                   /evidence="ECO:0000269|PubMed:27830187"
FT                   /id="VAR_078832"
FT   VARIANT         1595
FT                   /note="M -> I (in SKS; dbSNP:rs869312671)"
FT                   /evidence="ECO:0000269|PubMed:27830187"
FT                   /id="VAR_078833"
FT   VARIANT         1709
FT                   /note="R -> H (in FCORD2; somatic mutation; unknown
FT                   pathological significance; dbSNP:rs587777895)"
FT                   /evidence="ECO:0000269|PubMed:25799227"
FT                   /id="VAR_078834"
FT   VARIANT         1799
FT                   /note="E -> K (in SKS; results in increased mTOR signaling;
FT                   dbSNP:rs863225264)"
FT                   /evidence="ECO:0000269|PubMed:25851998,
FT                   ECO:0000269|PubMed:26542245"
FT                   /id="VAR_075072"
FT   VARIANT         1832
FT                   /note="A -> T (in SKS; dbSNP:rs369088781)"
FT                   /evidence="ECO:0000269|PubMed:27830187"
FT                   /id="VAR_078835"
FT   VARIANT         1888
FT                   /note="F -> C (in SKS; dbSNP:rs869312666)"
FT                   /evidence="ECO:0000269|PubMed:27830187"
FT                   /id="VAR_078836"
FT   VARIANT         1977
FT                   /note="T -> K (in FCORD2; somatic mutation;
FT                   dbSNP:rs587777893)"
FT                   /evidence="ECO:0000269|PubMed:25799227"
FT                   /id="VAR_078837"
FT   VARIANT         2011
FT                   /note="M -> V (in an ovarian mucinous carcinoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041542"
FT   VARIANT         2193
FT                   /note="R -> C (in FCORD2; somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:25799227"
FT                   /id="VAR_078838"
FT   VARIANT         2215
FT                   /note="S -> F (in FCORD2; somatic mutation; increased TOR
FT                   signaling; dbSNP:rs587777894)"
FT                   /evidence="ECO:0000269|PubMed:25799227,
FT                   ECO:0000269|PubMed:26018084, ECO:0000269|PubMed:27830187"
FT                   /id="VAR_078839"
FT   VARIANT         2215
FT                   /note="S -> Y (in FCORD2; also found in a colorectal
FT                   adenocarcinoma sample; somatic mutation; increased TOR
FT                   signaling; dbSNP:rs587777894)"
FT                   /evidence="ECO:0000269|PubMed:17344846,
FT                   ECO:0000269|PubMed:26018084, ECO:0000269|PubMed:27830187"
FT                   /id="VAR_041543"
FT   VARIANT         2220
FT                   /note="L -> F (found in a renal cell carcinoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:21248752"
FT                   /id="VAR_064733"
FT   VARIANT         2327
FT                   /note="M -> I (in SKS; dbSNP:rs878855328)"
FT                   /evidence="ECO:0000269|PubMed:27830187"
FT                   /id="VAR_078840"
FT   VARIANT         2406
FT                   /note="V -> A (found in a renal cell carcinoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:21248752"
FT                   /id="VAR_064734"
FT   VARIANT         2427
FT                   /note="L -> P (in FCORD2; somatic mutation; increased TOR
FT                   signaling; increased kinase activity; dbSNP:rs1085307113)"
FT                   /evidence="ECO:0000269|PubMed:25799227"
FT                   /id="VAR_078841"
FT   VARIANT         2427
FT                   /note="L -> Q (in FCORD2; somatic mutation; increased TOR
FT                   signaling; increased kinase activity; dbSNP:rs1085307113)"
FT                   /evidence="ECO:0000269|PubMed:25799227"
FT                   /id="VAR_078842"
FT   VARIANT         2476
FT                   /note="P -> L (in a glioblastoma multiforme sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041544"
FT   VARIANT         2501
FT                   /note="I -> V (found in a patient with non-lesional
FT                   nocturnal frontal epilepsy; unknown pathological
FT                   significance; dbSNP:rs968817513)"
FT                   /evidence="ECO:0000269|PubMed:27830187"
FT                   /id="VAR_078843"
FT   MUTAGEN         2159
FT                   /note="S->A: Reduces mTORC1-associated S-2481
FT                   autophosphorylation; when associated with A-2164."
FT                   /evidence="ECO:0000269|PubMed:21576368"
FT   MUTAGEN         2159
FT                   /note="S->D: Stronger phosphorylation of RPS6KB1; when
FT                   associated with E-2164."
FT                   /evidence="ECO:0000269|PubMed:21576368"
FT   MUTAGEN         2164
FT                   /note="T->A: Reduces mTORC1-associated S-2481
FT                   autophosphorylation; when associated with A-2159."
FT                   /evidence="ECO:0000269|PubMed:21576368"
FT   MUTAGEN         2164
FT                   /note="T->E: Stronger phosphorylation of RPS6KB1; when
FT                   associated with D-2159."
FT                   /evidence="ECO:0000269|PubMed:21576368"
FT   MUTAGEN         2173
FT                   /note="T->A: Increased mTOR kinase activity."
FT                   /evidence="ECO:0000269|PubMed:24247430"
FT   MUTAGEN         2340
FT                   /note="H->A: Barely detectable kinase activity."
FT                   /evidence="ECO:0000269|PubMed:23636326"
FT   MUTAGEN         2357
FT                   /note="D->E: Kinase-dead mutant, loss of interaction with
FT                   TM4SF5 and loss of lysosome membrane localization; when
FT                   associated with I-2364."
FT                   /evidence="ECO:0000269|PubMed:30956113"
FT   MUTAGEN         2364
FT                   /note="V->I: Kinase-dead mutant, loss of interaction with
FT                   TM4SF5 and loss of lysosome membrane localization; when
FT                   associated with E-2357."
FT                   /evidence="ECO:0000269|PubMed:30956113"
FT   CONFLICT        353
FT                   /note="K -> N (in Ref. 2; AAC39933)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        359
FT                   /note="S -> N (in Ref. 2; AAC39933)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        364
FT                   /note="D -> N (in Ref. 2; AAC39933)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        390
FT                   /note="M -> L (in Ref. 2; AAC39933)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        430
FT                   /note="R -> L (in Ref. 2; AAC39933)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        455..457
FT                   /note="VLD -> GVE (in Ref. 2; AAC39933)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        461
FT                   /note="A -> G (in Ref. 2; AAC39933)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        482..484
FT                   /note="VFT -> FFN (in Ref. 2; AAC39933)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        489
FT                   /note="L -> V (in Ref. 2; AAC39933)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        513
FT                   /note="L -> I (in Ref. 2; AAC39933)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        539
FT                   /note="L -> V (in Ref. 2; AAC39933)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        553
FT                   /note="R -> C (in Ref. 2; AAC39933)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        857
FT                   /note="P -> L (in Ref. 3; BAE06077)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1075
FT                   /note="I -> S (in Ref. 2; AAC39933)"
FT                   /evidence="ECO:0000305"
FT   HELIX           1386..1406
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1410..1421
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   TURN            1422..1424
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1426..1439
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1446..1452
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1456..1469
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1474..1487
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1490..1498
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   STRAND          1501..1503
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1506..1523
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1526..1535
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   STRAND          1538..1540
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1541..1553
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1557..1577
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   TURN            1584..1586
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1587..1605
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   STRAND          1606..1608
FT                   /evidence="ECO:0000244|PDB:4JSP"
FT   HELIX           1609..1611
FT                   /evidence="ECO:0000244|PDB:4JSX"
FT   HELIX           1613..1624
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1630..1640
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   TURN            1641..1643
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   TURN            1646..1648
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1650..1663
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1666..1677
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   STRAND          1681..1684
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1694..1706
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1710..1729
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1738..1761
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1768..1782
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   TURN            1783..1785
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1787..1813
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1868..1893
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   STRAND          1896..1898
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1900..1913
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1917..1929
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1932..1938
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1939..1943
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   TURN            1944..1947
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1951..1966
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1969..1971
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1973..1980
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           1985..2020
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           2025..2039
FT                   /evidence="ECO:0000244|PDB:4DRI"
FT   HELIX           2044..2058
FT                   /evidence="ECO:0000244|PDB:4DRI"
FT   HELIX           2065..2091
FT                   /evidence="ECO:0000244|PDB:4DRI"
FT   HELIX           2094..2111
FT                   /evidence="ECO:0000244|PDB:4DRI"
FT   TURN            2115..2117
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   STRAND          2119..2122
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           2123..2126
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           2128..2132
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   STRAND          2137..2139
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   TURN            2141..2143
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   STRAND          2146..2148
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   STRAND          2152..2156
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   STRAND          2158..2162
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   STRAND          2165..2167
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   STRAND          2170..2176
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   STRAND          2181..2189
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           2193..2211
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           2213..2217
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   STRAND          2227..2229
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   STRAND          2231..2233
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   STRAND          2235..2238
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   STRAND          2243..2245
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           2246..2256
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           2263..2271
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           2275..2277
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           2280..2292
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           2298..2306
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           2310..2334
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   TURN            2341..2343
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   STRAND          2344..2347
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   TURN            2348..2350
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   STRAND          2353..2355
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           2364..2367
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   STRAND          2369..2371
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           2381..2386
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   TURN            2389..2394
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           2395..2409
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           2411..2422
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   TURN            2425..2428
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           2429..2432
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           2433..2435
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           2493..2509
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   STRAND          2512..2516
FT                   /evidence="ECO:0000244|PDB:4JT5"
FT   HELIX           2521..2533
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           2535..2540
FT                   /evidence="ECO:0000244|PDB:5WBY"
FT   HELIX           2543..2545
FT                   /evidence="ECO:0000244|PDB:5WBY"
SQ   SEQUENCE   2549 AA;  288892 MW;  7D9AD6E784882AB4 CRC64;
     MLGTGPAAAT TAATTSSNVS VLQQFASGLK SRNEETRAKA AKELQHYVTM ELREMSQEES
     TRFYDQLNHH IFELVSSSDA NERKGGILAI ASLIGVEGGN ATRIGRFANY LRNLLPSNDP
     VVMEMASKAI GRLAMAGDTF TAEYVEFEVK RALEWLGADR NEGRRHAAVL VLRELAISVP
     TFFFQQVQPF FDNIFVAVWD PKQAIREGAV AALRACLILT TQREPKEMQK PQWYRHTFEE
     AEKGFDETLA KEKGMNRDDR IHGALLILNE LVRISSMEGE RLREEMEEIT QQQLVHDKYC
     KDLMGFGTKP RHITPFTSFQ AVQPQQSNAL VGLLGYSSHQ GLMGFGTSPS PAKSTLVESR
     CCRDLMEEKF DQVCQWVLKC RNSKNSLIQM TILNLLPRLA AFRPSAFTDT QYLQDTMNHV
     LSCVKKEKER TAAFQALGLL SVAVRSEFKV YLPRVLDIIR AALPPKDFAH KRQKAMQVDA
     TVFTCISMLA RAMGPGIQQD IKELLEPMLA VGLSPALTAV LYDLSRQIPQ LKKDIQDGLL
     KMLSLVLMHK PLRHPGMPKG LAHQLASPGL TTLPEASDVG SITLALRTLG SFEFEGHSLT
     QFVRHCADHF LNSEHKEIRM EAARTCSRLL TPSIHLISGH AHVVSQTAVQ VVADVLSKLL
     VVGITDPDPD IRYCVLASLD ERFDAHLAQA ENLQALFVAL NDQVFEIREL AICTVGRLSS
     MNPAFVMPFL RKMLIQILTE LEHSGIGRIK EQSARMLGHL VSNAPRLIRP YMEPILKALI
     LKLKDPDPDP NPGVINNVLA TIGELAQVSG LEMRKWVDEL FIIIMDMLQD SSLLAKRQVA
     LWTLGQLVAS TGYVVEPYRK YPTLLEVLLN FLKTEQNQGT RREAIRVLGL LGALDPYKHK
     VNIGMIDQSR DASAVSLSES KSSQDSSDYS TSEMLVNMGN LPLDEFYPAV SMVALMRIFR
     DQSLSHHHTM VVQAITFIFK SLGLKCVQFL PQVMPTFLNV IRVCDGAIRE FLFQQLGMLV
     SFVKSHIRPY MDEIVTLMRE FWVMNTSIQS TIILLIEQIV VALGGEFKLY LPQLIPHMLR
     VFMHDNSPGR IVSIKLLAAI QLFGANLDDY LHLLLPPIVK LFDAPEAPLP SRKAALETVD
     RLTESLDFTD YASRIIHPIV RTLDQSPELR STAMDTLSSL VFQLGKKYQI FIPMVNKVLV
     RHRINHQRYD VLICRIVKGY TLADEEEDPL IYQHRMLRSG QGDALASGPV ETGPMKKLHV
     STINLQKAWG AARRVSKDDW LEWLRRLSLE LLKDSSSPSL RSCWALAQAY NPMARDLFNA
     AFVSCWSELN EDQQDELIRS IELALTSQDI AEVTQTLLNL AEFMEHSDKG PLPLRDDNGI
     VLLGERAAKC RAYAKALHYK ELEFQKGPTP AILESLISIN NKLQQPEAAA GVLEYAMKHF
     GELEIQATWY EKLHEWEDAL VAYDKKMDTN KDDPELMLGR MRCLEALGEW GQLHQQCCEK
     WTLVNDETQA KMARMAAAAA WGLGQWDSME EYTCMIPRDT HDGAFYRAVL ALHQDLFSLA
     QQCIDKARDL LDAELTAMAG ESYSRAYGAM VSCHMLSELE EVIQYKLVPE RREIIRQIWW
     ERLQGCQRIV EDWQKILMVR SLVVSPHEDM RTWLKYASLC GKSGRLALAH KTLVLLLGVD
     PSRQLDHPLP TVHPQVTYAY MKNMWKSARK IDAFQHMQHF VQTMQQQAQH AIATEDQQHK
     QELHKLMARC FLKLGEWQLN LQGINESTIP KVLQYYSAAT EHDRSWYKAW HAWAVMNFEA
     VLHYKHQNQA RDEKKKLRHA SGANITNATT AATTAATATT TASTEGSNSE SEAESTENSP
     TPSPLQKKVT EDLSKTLLMY TVPAVQGFFR SISLSRGNNL QDTLRVLTLW FDYGHWPDVN
     EALVEGVKAI QIDTWLQVIP QLIARIDTPR PLVGRLIHQL LTDIGRYHPQ ALIYPLTVAS
     KSTTTARHNA ANKILKNMCE HSNTLVQQAM MVSEELIRVA ILWHEMWHEG LEEASRLYFG
     ERNVKGMFEV LEPLHAMMER GPQTLKETSF NQAYGRDLME AQEWCRKYMK SGNVKDLTQA
     WDLYYHVFRR ISKQLPQLTS LELQYVSPKL LMCRDLELAV PGTYDPNQPI IRIQSIAPSL
     QVITSKQRPR KLTLMGSNGH EFVFLLKGHE DLRQDERVMQ LFGLVNTLLA NDPTSLRKNL
     SIQRYAVIPL STNSGLIGWV PHCDTLHALI RDYREKKKIL LNIEHRIMLR MAPDYDHLTL
     MQKVEVFEHA VNNTAGDDLA KLLWLKSPSS EVWFDRRTNY TRSLAVMSMV GYILGLGDRH
     PSNLMLDRLS GKILHIDFGD CFEVAMTREK FPEKIPFRLT RMLTNAMEVT GLDGNYRITC
     HTVMEVLREH KDSVMAVLEA FVYDPLLNWR LMDTNTKGNK RSRTRTDSYS AGQSVEILDG
     VELGEPAHKK TGTTVPESIH SFIGDGLVKP EALNKKAIQI INRVRDKLTG RDFSHDDTLD
     VPTQVELLIK QATSHENLCQ CYIGWCPFW
//
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