Serine/threonine-protein kinase mTOR (Protein name
), MTOR_HUMAN from NCBI database.
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Gene name:
MTOR(FRAP;FRAP1;FRAP2;RAFT1;RAPT1);
Protein name:
Serine/threonine-protein kinase mTOR;
Alternative:
FKBP12-rapamycin complex-associated protein;FK506-binding protein 12-rapamycin complex-associated protein 1;Mechanistic target of rapamycin;Mammalian target of rapamycin(mTOR);Rapamycin target protein 1;Rapamycin target protein 1(RAPT1);
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Interacts with PPAPDC3 and PML (By similarity). Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR/FRAP1, MLST8, RPTOR and AKT1S1. mTORC1 binds to and is inhibited by FKBP12-rapamycin. Part of the mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PROTOR1, RICTOR and MAPKAP1. Contrary to mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-rapamycin. Binds directly to PROTOR1 and RICTOR within the mTORC2 complex. Interacts with UBQLN1. Interacts with DEPTOR. Interacts with TTI1 and TELO2.
Function:
Kinase subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino-acids. Growth factor-stimulated mTORC1 activation involves AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino-acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-421', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Phosphorylates MAF1 leading to attenuation of its RNA polymerase III-repressive function. mTORC2 is also activated by growth. factors, but seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-757', disrupting the interaction with AMPK and preventing activation of ULK1.
Subcellular Location:
Endoplasmic reticulum membrane
Peripheral membrane protein
Cytoplasmic side
Golgi apparatus membrane
Peripheral membrane protein
Cytoplasmic side
Mitochondrion outer membrane
Peripheral membrane protein
Cytoplasmic side
Lysosome
Cytoplasm
Nucleus
PML body
Shuttles between cytoplasm and nucleus. Accumulates in the nucleus in response to hypoxia (By similarity). Targeting to lysosomes depends on amino acid availability and RRAGA and RRAGB.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1987-2146;TISSUE SPECIFICITY
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Cited for: FUNCTION IN NUTRIENT-DEPENDENT CELL GROWTH;FUNCTION IN PHOSPHORYLATION OF RPS6KB1;INTERACTION WITH RPTOR
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Cited for: INTERACTION WITH CLIP1;FUNCTION IN PHOSPHORYLATION OF CLIP1
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Cited for: INTERACTION WITH MLST8 AND RPTOR;IDENTIFICATION IN THE MTORC1 COMPLEX;TISSUE SPECIFICITY
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Cited for: ENZYME REGULATION;FUNCTION IN RESPONSE TO LOW CELLULAR ENERGY
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Cited for: FUNCTION IN PHOSPHORYLATION OF PRKCA;FUNCTION IN REGULATION OF THE ACTIN CYTOSKELETON;IDENTIFICATION IN THE MTORC2 COMPLEX;INTERACTION WITH RICTOR
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Cited for: ENZYME REGULATION;FUNCTION IN RESPONSE TO HYPOXIA
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Cited for: FUNCTION IN REGULATION OF THE ACTIN CYTOSKELETON;FUNCTION IN PHOSPHORYLATION OF PXN;IDENTIFICATION IN THE MTORC2 COMPLEX;INTERACTION WITH RICTOR;AUTOPHOSPHORYLATION
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Cited for: IDENTIFICATION IN THE MTORC2 COMPLEX;INTERACTION WITH PRR5
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Cited for: IDENTIFICATION IN THE MTORC1 AND MTORC2 COMPLEXES;FUNCTION IN PHOSPHORYLATION OF RPS6KB1 AND SGK1
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2478 AND SER-2481;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: FUNCTION;ENZYME REGULATION;SUBCELLULAR LOCATION
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1218;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: FUNCTION IN PHOSPHORYLATION OF DAP;FUNCTION IN AUTOPHAGY
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Cited for: FUNCTION IN REGULATION OF RNA POLYMERASE III TRANSCRIPTION;FUNCTION IN PHOSPHORYLATION OF MAF1
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567 AND THR-1162;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION AT SER-2159; THR-2164 AND SER-2481;MUTAGENESIS OF SER-2159 AND THR-2164
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: FUNCTION IN PHOSPHORYLATION OF GRB10;FUNCTION IN INSR-DEPENDENT SIGNALING
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Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION AT THR-2173;MUTAGENESIS OF THR-2173
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Cited for: FUNCTION;PHOSPHORYLATION OF RPS6KB1;REGULATION OF PYRIMIDINE SYNTHESIS
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Cited for: FUNCTION;PHOSPHORYLATION OF RPS6KB1;REGULATION OF PYRIMIDINE SYNTHESIS
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Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2018-2112 IN COMPLEX WITH FKBP1A AND INHIBITOR RAPAMYCIN
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Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2018-2112 IN COMPLEX WITH FKBP1A AND INHIBITOR RAPAMYCIN
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Cited for: CRYO-ELECTRON MICROSCOPY (26 ANGSTROMS) OF MTORC1 COMPLEX;SUBUNIT
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Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1376-2549 IN COMPLEX WITH MLST8;SUBUNIT;TPR-REPEATS;DOMAINS;MUTAGENESIS OF HIS-2340
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Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-8; THR-135; VAL-1083; VAL-1134; PHE-1178; VAL-2011; TYR-2215 AND LEU-2476