MTOR information

MTOR
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4JT6, 1AUE, 1FAP, 1NSG, 2FAP, 2GAQ, 2NPU, 2RSE, 3FAP, 4DRH, 4DRI, 4DRJ, 4FAP, 4JSN, 4JSP, 4JSV, 4JSX, 4JT5, 5FLC
Identifiers
Aliases	MTOR, FRAP, FRAP1, FRAP2, RAFT1, RAPT1, SKS, mechanistic target of rapamycin, mechanistic target of rapamycin kinase
External IDs	OMIM: 601231 MGI: 1928394 HomoloGene: 3637 GeneCards: MTOR
Gene location (Human)
Chr.	Chromosome 1 (human)
End	11,262,551 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	148,642,140 bp
RNA expression pattern
	Top expressed in
	gastrocnemius muscle; ; tibial nerve; ; anterior pituitary; ; stromal cell of endometrium; ; right lobe of liver; ; popliteal artery; ; right lobe of thyroid gland; ; gastric mucosa; ; transverse colon; ; Achilles tendon;
	Top expressed in
	spermatid; ; spermatocyte; ; superior frontal gyrus; ; yolk sac; ; proximal tubule; ; lip; ; ankle joint; ; morula; ; cerebellar cortex; ; lens;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	protein domain specific binding; TFIIIC-class transcription factor complex binding; kinase activity; ATP binding; protein serine/threonine kinase activity; transferase activity; ribosome binding; protein binding; protein kinase binding; nucleotide binding; phosphoprotein binding; protein kinase activity; protein-containing complex binding; identical protein binding; translation regulator activity;
Cellular component	cytoplasm; cytosol; phosphatidylinositol 3-kinase complex; membrane; mitochondrion; TORC1 complex; organelle membrane; protein-containing complex; mitochondrial outer membrane; endoplasmic reticulum; TORC2 complex; Golgi apparatus; intracellular membrane-bounded organelle; nucleoplasm; neuronal cell body; PML body; endoplasmic reticulum membrane; Golgi membrane; lysosomal membrane; dendrite; endomembrane system; nucleus; lysosome; glutamatergic synapse; postsynaptic cytosol;
Biological process	germ cell development; positive regulation of protein phosphorylation; response to amino acid; positive regulation of lipid biosynthetic process; positive regulation of actin filament polymerization; positive regulation of skeletal muscle hypertrophy; positive regulation of granulosa cell proliferation; regulation of carbohydrate utilization; post-embryonic development; positive regulation of dendritic spine development; positive regulation of translation; positive regulation of eating behavior; protein phosphorylation; mRNA stabilization; cell projection organization; regulation of glycogen biosynthetic process; positive regulation of cell growth involved in cardiac muscle cell development; positive regulation of neuron maturation; positive regulation of glial cell proliferation; cellular response to hypoxia; negative regulation of cell size; response to cocaine; positive regulation of protein kinase B signaling; cardiac muscle contraction; maternal process involved in female pregnancy; ruffle organization; regulation of GTPase activity; cardiac muscle cell development; positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; regulation of membrane permeability; response to insulin; regulation of myelination; regulation of fatty acid beta-oxidation; regulation of osteoclast differentiation; positive regulation of cholangiocyte proliferation; regulation of protein kinase B signaling; spinal cord development; positive regulation of peptidyl-tyrosine phosphorylation; social behavior; protein autophosphorylation; negative regulation of cholangiocyte apoptotic process; regulation of brown fat cell differentiation; regulation of protein kinase activity; negative regulation of protein phosphorylation; positive regulation of oligodendrocyte differentiation; regulation of carbohydrate metabolic process; regulation of actin cytoskeleton organization; voluntary musculoskeletal movement; phosphorylation; multicellular organism growth; negative regulation of muscle atrophy; wound healing; positive regulation of neurogenesis; response to morphine; positive regulation of sensory perception of pain; protein catabolic process; 'de novo' pyrimidine nucleobase biosynthetic process; cellular response to nutrient levels; energy reserve metabolic process; peptidyl-threonine phosphorylation; positive regulation of transcription by RNA polymerase III; positive regulation of smooth muscle cell proliferation; visual learning; positive regulation of myotube differentiation; positive regulation of cell death; positive regulation of endothelial cell proliferation; negative regulation of iodide transmembrane transport; cardiac muscle tissue development; positive regulation of nitric oxide biosynthetic process; regulation of response to food; heart morphogenesis; positive regulation of neuron death; cardiac cell development; negative regulation of protein ubiquitination; brain development; positive regulation of gene expression; long-term memory; heart valve morphogenesis; peptidyl-serine phosphorylation; positive regulation of neuron projection development; regulation of cellular response to heat; positive regulation of lamellipodium assembly; positive regulation of stress fiber assembly; signal transduction; regulation of protein phosphorylation; negative regulation of macroautophagy; anoikis; TOR signaling; DNA repair; regulation of cell size; negative regulation of autophagy; positive regulation of epithelial to mesenchymal transition; regulation of macroautophagy; cellular response to amino acid starvation; positive regulation of keratinocyte migration; cellular response to amino acid stimulus; cellular response to leucine; positive regulation of wound healing, spreading of epidermal cells; cellular response to leucine starvation; cellular response to starvation; TORC1 signaling; growth; regulation of cell growth; response to nutrient; activation of protein kinase B activity; T-helper 1 cell lineage commitment; response to activity; positive regulation of phosphoprotein phosphatase activity; negative regulation of calcineurin-NFAT signaling cascade; regulation of translation at synapse, modulating synaptic transmission; positive regulation of cytoplasmic translational initiation; response to nutrient levels;
	Sources:Amigo / QuickGO
Orthologs
	2475
	56717
	ENSG00000198793
	ENSMUSG00000028991
	P42345
	Q9JLN9
	NM_004958; NM_001386500; NM_001386501
	NM_020009
	NP_004949
	NP_064393
	Wikidata
View/Edit Human	View/Edit Mouse

The mammalian target of rapamycin (mTOR),^[5] also referred to as the mechanistic target of rapamycin, and sometimes called FK506-binding protein 12-rapamycin-associated protein 1 (FRAP1), is a kinase that in humans is encoded by the MTOR gene.^[6]^[7]^[8] mTOR is a member of the phosphatidylinositol 3-kinase-related kinase family of protein kinases.^[9]

mTOR links with other proteins and serves as a core component of two distinct protein complexes, mTOR complex 1 and mTOR complex 2, which regulate different cellular processes.^[10] In particular, as a core component of both complexes, mTOR functions as a serine/threonine protein kinase that regulates cell growth, cell proliferation, cell motility, cell survival, protein synthesis, autophagy, and transcription.^[10]^[11] As a core component of mTORC2, mTOR also functions as a tyrosine protein kinase that promotes the activation of insulin receptors and insulin-like growth factor 1 receptors.^[12] mTORC2 has also been implicated in the control and maintenance of the actin cytoskeleton.^[10]^[13]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000198793 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000028991 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Sabers CJ, Martin MM, Brunn GJ, et al. (Jan 1995). "Isolation of a Protein Target of the FKBP12-Rapamycin Complex in Mammalian Cells". J. Biol. Chem. 270 (2): 815–22. doi:10.1074/jbc.270.2.815. PMID 7822316.
^ Brown EJ, Albers MW, Shin TB, et al. (June 1994). "A mammalian protein targeted by G1-arresting rapamycin-receptor complex". Nature. 369 (6483): 756–8. Bibcode:1994Natur.369..756B. doi:10.1038/369756a0. PMID 8008069. S2CID 4359651.
^ Cite error: The named reference pmid7518356 was invoked but never defined (see the help page).
^ Sabers CJ, Martin MM, Brunn GJ, et al. (January 1995). "Isolation of a protein target of the FKBP12-rapamycin complex in mammalian cells". The Journal of Biological Chemistry. 270 (2): 815–22. doi:10.1074/jbc.270.2.815. PMID 7822316.
^ Mitra A, Luna JI, Marusina AI, et al. (November 2015). "Dual mTOR Inhibition Is Required to Prevent TGF-β-Mediated Fibrosis: Implications for Scleroderma". The Journal of Investigative Dermatology. 135 (11): 2873–6. doi:10.1038/jid.2015.252. PMC 4640976. PMID 26134944.
^ ^a ^b ^c Cite error: The named reference The neurology of mTOR was invoked but never defined (see the help page).
^ Hay N, Sonenberg N (August 2004). "Upstream and downstream of mTOR". Genes & Development. 18 (16): 1926–45. doi:10.1101/gad.1212704. PMID 15314020.
^ Yin Y, Hua H, Li M, et al. (January 2016). "mTORC2 promotes type I insulin-like growth factor receptor and insulin receptor activation through the tyrosine kinase activity of mTOR". Cell Research. 26 (1): 46–65. doi:10.1038/cr.2015.133. PMC 4816127. PMID 26584640.
^ Cite error: The named reference pmid15467718 was invoked but never defined (see the help page).

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000198793 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000028991 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[5] Sabers CJ, Martin MM, Brunn GJ, et al. (Jan 1995). "Isolation of a Protein Target of the FKBP12-Rapamycin Complex in Mammalian Cells". J. Biol. Chem. 270 (2): 815–22. doi:10.1074/jbc.270.2.815. PMID 7822316.

[pmid8008069-6] Brown EJ, Albers MW, Shin TB, et al. (June 1994). "A mammalian protein targeted by G1-arresting rapamycin-receptor complex". Nature. 369 (6483): 756–8. Bibcode:1994Natur.369..756B. doi:10.1038/369756a0. PMID 8008069. S2CID 4359651.

[pmid7518356-7] Cite error: The named reference pmid7518356 was invoked but never defined (see the help page).

[ReferenceA-8] Sabers CJ, Martin MM, Brunn GJ, et al. (January 1995). "Isolation of a protein target of the FKBP12-rapamycin complex in mammalian cells". The Journal of Biological Chemistry. 270 (2): 815–22. doi:10.1074/jbc.270.2.815. PMID 7822316.

[Mitra2015-9] Mitra A, Luna JI, Marusina AI, et al. (November 2015). "Dual mTOR Inhibition Is Required to Prevent TGF-β-Mediated Fibrosis: Implications for Scleroderma". The Journal of Investigative Dermatology. 135 (11): 2873–6. doi:10.1038/jid.2015.252. PMC 4640976. PMID 26134944.

[The_neurology_of_mTOR-10] Cite error: The named reference The neurology of mTOR was invoked but never defined (see the help page).

[Hay-11] Hay N, Sonenberg N (August 2004). "Upstream and downstream of mTOR". Genes & Development. 18 (16): 1926–45. doi:10.1101/gad.1212704. PMID 15314020.

[Yin_2016-12] Yin Y, Hua H, Li M, et al. (January 2016). "mTORC2 promotes type I insulin-like growth factor receptor and insulin receptor activation through the tyrosine kinase activity of mTOR". Cell Research. 26 (1): 46–65. doi:10.1038/cr.2015.133. PMC 4816127. PMID 26584640.

[pmid15467718-13] Cite error: The named reference pmid15467718 was invoked but never defined (see the help page).

MTOR information

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