UniProtKB - P42346 (MTOR_RAT)
Serine/threonine-protein kinase mTOR
Mtor
Functioni
Serine/threonine protein kinase which is a central regulator of cellular metabolism, growth and survival in response to hormones, growth factors, nutrients, energy and stress signals (By similarity).
MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins (By similarity).
Functions as part of 2 structurally and functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR complex 1 and 2) (By similarity).
Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis (By similarity).
This includes phosphorylation of EIF4EBP1 and release of its inhibition toward the elongation initiation factor 4E (eiF4E) (PubMed:9465032).
Moreover, phosphorylates and activates RPS6KB1 and RPS6KB2 that promote protein synthesis by modulating the activity of their downstream targets including ribosomal protein S6, eukaryotic translation initiation factor EIF4B, and the inhibitor of translation initiation PDCD4 (PubMed:9465032).
This also includes mTORC1 signaling cascade controlling the MiT/TFE factors TFEB and TFE3: in the presence of nutrients, mediates phosphorylation of TFEB and TFE3, promoting their cytosolic retention and inactivation (By similarity).
Upon starvation or lysosomal stress, inhibition of mTORC1 induces dephosphorylation and nuclear translocation of TFEB and TFE3, promoting their transcription factor activity (By similarity).
Stimulates the pyrimidine biosynthesis pathway, both by acute regulation through RPS6KB1-mediated phosphorylation of the biosynthetic enzyme CAD, and delayed regulation, through transcriptional enhancement of the pentose phosphate pathway which produces 5-phosphoribosyl-1-pyrophosphate (PRPP), an allosteric activator of CAD at a later step in synthesis, this function is dependent on the mTORC1 complex (By similarity).
Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 an RNA polymerase III-repressor (By similarity).
In parallel to protein synthesis, also regulates lipid synthesis through SREBF1/SREBP1 and LPIN1 (By similarity).
To maintain energy homeostasis mTORC1 may also regulate mitochondrial biogenesis through regulation of PPARGC1A (By similarity).
mTORC1 also negatively regulates autophagy through phosphorylation of ULK1 (By similarity).
Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-758', disrupting the interaction with AMPK and preventing activation of ULK1 (By similarity).
Also prevents autophagy through phosphorylation of the autophagy inhibitor DAP (By similarity).
Also prevents autophagy by phosphorylating RUBCNL/Pacer under nutrient-rich conditions (By similarity).
Prevents autophagy by mediating phosphorylation of AMBRA1, thereby inhibiting AMBRA1 ability to mediate ubiquitination of ULK1 and interaction between AMBRA1 and PPP2CA (By similarity).
mTORC1 exerts a feedback control on upstream growth factor signaling that includes phosphorylation and activation of GRB10 a INSR-dependent signaling suppressor (By similarity).
Among other potential targets mTORC1 may phosphorylate CLIP1 and regulate microtubules (By similarity).
As part of the mTORC2 complex MTOR may regulate other cellular processes including survival and organization of the cytoskeleton (By similarity).
Plays a critical role in the phosphorylation at 'Ser-473' of AKT1, a pro-survival effector of phosphoinositide 3-kinase, facilitating its activation by PDK1 (By similarity).
mTORC2 may regulate the actin cytoskeleton, through phosphorylation of PRKCA, PXN and activation of the Rho-type guanine nucleotide exchange factors RHOA and RAC1A or RAC1B (By similarity).
mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-421' (By similarity).
Regulates osteoclastogenesis by adjusting the expression of CEBPB isoforms (By similarity).
Plays an important regulatory role in the circadian clock function; regulates period length and rhythm amplitude of the suprachiasmatic nucleus (SCN) and liver clocks (By similarity).
Phosphorylates SQSTM1, promoting interaction between SQSTM1 and KEAP1 and subsequent inactivation of the BCR(KEAP1) complex (By similarity).
By similarity1 PublicationCatalytic activityi
Activity regulationi
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- identical protein binding Source: RGD
- kinase activity Source: RGD
- phosphoprotein binding Source: RGD
- protein domain specific binding Source: RGD
- protein kinase activity Source: RGD
- protein kinase binding Source: RGD
- protein serine/threonine/tyrosine kinase activity Source: RHEA
- protein serine/threonine kinase activity Source: RGD
- protein serine kinase activity Source: RHEA
- ribosome binding Source: RGD
- RNA polymerase III type 1 promoter sequence-specific DNA binding Source: RGD
- RNA polymerase III type 2 promoter sequence-specific DNA binding Source: RGD
- RNA polymerase III type 3 promoter sequence-specific DNA binding Source: RGD
- TFIIIC-class transcription factor complex binding Source: RGD
- translation regulator activity Source: SynGO
GO - Biological processi
- 'de novo' pyrimidine nucleobase biosynthetic process Source: RGD
- behavioral response to pain Source: RGD
- brain development Source: RGD
- cardiac cell development Source: RGD
- cardiac muscle cell development Source: RGD
- cardiac muscle contraction Source: RGD
- cardiac muscle tissue development Source: RGD
- cell aging Source: RGD
- cell projection organization Source: MGI
- cellular response to amino acid starvation Source: UniProtKB
- cellular response to amino acid stimulus Source: RGD
- cellular response to hypoxia Source: UniProtKB
- cellular response to leucine Source: RGD
- cellular response to leucine starvation Source: RGD
- cellular response to nutrient levels Source: UniProtKB
- cellular response to starvation Source: UniProtKB
- energy reserve metabolic process Source: RGD
- germ cell development Source: RGD
- heart morphogenesis Source: RGD
- heart valve morphogenesis Source: RGD
- inflammatory response Source: RGD
- long-term memory Source: RGD
- lysosome organization Source: UniProtKB
- maternal process involved in female pregnancy Source: RGD
- mRNA stabilization Source: RGD
- multicellular organism growth Source: RGD
- negative regulation of autophagy Source: RGD
- negative regulation of calcineurin-NFAT signaling cascade Source: RGD
- negative regulation of cell size Source: MGI
- negative regulation of cholangiocyte apoptotic process Source: RGD
- negative regulation of iodide transmembrane transport Source: RGD
- negative regulation of macroautophagy Source: RGD
- negative regulation of muscle atrophy Source: RGD
- negative regulation of protein phosphorylation Source: RGD
- negative regulation of protein ubiquitination Source: RGD
- neuronal action potential Source: RGD
- nucleus localization Source: UniProtKB
- peptidyl-serine phosphorylation Source: UniProtKB
- peptidyl-threonine phosphorylation Source: RGD
- phosphorylation Source: RGD
- positive regulation of actin filament polymerization Source: RGD
- positive regulation of cell death Source: RGD
- positive regulation of cell growth involved in cardiac muscle cell development Source: RGD
- positive regulation of cholangiocyte proliferation Source: RGD
- positive regulation of dendritic spine development Source: RGD
- positive regulation of eating behavior Source: RGD
- positive regulation of endothelial cell proliferation Source: RGD
- positive regulation of epithelial to mesenchymal transition Source: RGD
- positive regulation of gene expression Source: RGD
- positive regulation of glial cell proliferation Source: RGD
- positive regulation of granulosa cell proliferation Source: RGD
- positive regulation of keratinocyte migration Source: RGD
- positive regulation of lamellipodium assembly Source: RGD
- positive regulation of lipid biosynthetic process Source: UniProtKB
- positive regulation of myotube differentiation Source: RGD
- positive regulation of neurogenesis Source: RGD
- positive regulation of neuron death Source: RGD
- positive regulation of neuron maturation Source: RGD
- positive regulation of neuron projection development Source: RGD
- positive regulation of nitric oxide biosynthetic process Source: RGD
- positive regulation of oligodendrocyte differentiation Source: RGD
- positive regulation of peptidyl-tyrosine phosphorylation Source: RGD
- positive regulation of protein kinase B signaling Source: RGD
- positive regulation of protein phosphorylation Source: RGD
- positive regulation of sensory perception of pain Source: RGD
- positive regulation of skeletal muscle hypertrophy Source: RGD
- positive regulation of smooth muscle cell proliferation Source: RGD
- positive regulation of stress fiber assembly Source: RGD
- positive regulation of transcription by RNA polymerase III Source: RGD
- positive regulation of transcription of nucleolar large rRNA by RNA polymerase I Source: RGD
- positive regulation of translation Source: RGD
- positive regulation of wound healing, spreading of epidermal cells Source: RGD
- post-embryonic development Source: RGD
- protein autophosphorylation Source: RGD
- protein phosphorylation Source: RGD
- regulation of actin cytoskeleton organization Source: RGD
- regulation of autophagy Source: UniProtKB
- regulation of brown fat cell differentiation Source: RGD
- regulation of carbohydrate metabolic process Source: RGD
- regulation of carbohydrate utilization Source: RGD
- regulation of cell growth Source: RGD
- regulation of cell size Source: RGD
- regulation of circadian rhythm Source: UniProtKB
- regulation of fatty acid beta-oxidation Source: RGD
- regulation of glycogen biosynthetic process Source: RGD
- regulation of GTPase activity Source: RGD
- regulation of locomotor rhythm Source: UniProtKB
- regulation of membrane permeability Source: RGD
- regulation of myelination Source: RGD
- regulation of osteoclast differentiation Source: UniProtKB
- regulation of protein kinase activity Source: RGD
- regulation of protein kinase B signaling Source: RGD
- regulation of protein phosphorylation Source: RGD
- regulation of response to food Source: RGD
- regulation of translation at synapse, modulating synaptic transmission Source: SynGO
- response to activity Source: RGD
- response to amino acid Source: RGD
- response to cocaine Source: RGD
- response to heat Source: RGD
- response to insulin Source: RGD
- response to morphine Source: RGD
- response to nutrient Source: RGD
- response to nutrient levels Source: UniProtKB
- rhythmic process Source: UniProtKB-KW
- ruffle organization Source: RGD
- social behavior Source: RGD
- spinal cord development Source: RGD
- T-helper 1 cell lineage commitment Source: RGD
- TORC1 signaling Source: RGD
- TOR signaling Source: UniProtKB
- visual learning Source: RGD
- voluntary musculoskeletal movement Source: RGD
- wound healing Source: RGD
Keywordsi
Molecular function | Kinase, Serine/threonine-protein kinase, Transferase |
Biological process | Biological rhythms |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
Reactomei | R-RNO-1257604, PIP3 activates AKT signaling R-RNO-1632852, Macroautophagy R-RNO-165159, MTOR signalling R-RNO-166208, mTORC1-mediated signalling R-RNO-3371571, HSF1-dependent transactivation R-RNO-380972, Energy dependent regulation of mTOR by LKB1-AMPK R-RNO-389357, CD28 dependent PI3K/Akt signaling R-RNO-5218920, VEGFR2 mediated vascular permeability R-RNO-5628897, TP53 Regulates Metabolic Genes R-RNO-6804757, Regulation of TP53 Degradation R-RNO-8943724, Regulation of PTEN gene transcription R-RNO-9639288, Amino acids regulate mTORC1 |
Names & Taxonomyi
Protein namesi | Recommended name: Serine/threonine-protein kinase mTORCurated (EC:2.7.11.11 Publication)Alternative name(s): FK506-binding protein 12-rapamycin complex-associated protein 1 FKBP12-rapamycin complex-associated protein Mammalian target of rapamycin Short name: mTOR Mechanistic target of rapamycin Rapamycin target protein 1 Short name: RAPT1 |
Gene namesi | |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 68371, Mtor |
Subcellular locationi
Mitochondrion
- Mitochondrion outer membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Cytoplasm and Cytosol
- Cytoplasm By similarity
Lysosome
- Lysosome By similarity
- Lysosome membrane By similarity
Golgi apparatus
- Golgi apparatus membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Nucleus
- PML body By similarity
Endoplasmic reticulum
- Endoplasmic reticulum membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Other locations
- phagosome By similarity
Note: 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 (By similarity). Translocates to the lysosome membrane in the presence of TM4SF5 (By similarity).By similarity
Cytosol
- cytosol Source: RGD
- postsynaptic cytosol Source: SynGO
Endoplasmic reticulum
- endoplasmic reticulum membrane Source: UniProtKB-SubCell
Golgi apparatus
- Golgi membrane Source: UniProtKB-SubCell
Lysosome
- lysosomal membrane Source: UniProtKB
- lysosome Source: UniProtKB
Mitochondrion
- mitochondrial outer membrane Source: UniProtKB-SubCell
Nucleus
- nuclear envelope Source: RGD
- nucleus Source: RGD
- PML body Source: UniProtKB-SubCell
Other locations
- cytoplasm Source: RGD
- dendrite Source: RGD
- endomembrane system Source: RGD
- glutamatergic synapse Source: SynGO
- membrane Source: RGD
- phagocytic vesicle Source: UniProtKB
- protein-containing complex Source: RGD
- TORC1 complex Source: RGD
- TORC2 complex Source: RGD
Keywords - Cellular componenti
Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Golgi apparatus, Lysosome, Membrane, Mitochondrion, Mitochondrion outer membrane, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000088810 | 1 – 2549 | Serine/threonine-protein kinase mTORAdd BLAST | 2549 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | N-acetylmethionineBy similarity | 1 | |
Modified residuei | 567 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1162 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 1218 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1261 | PhosphoserineBy similarity | 1 | |
Modified residuei | 2159 | PhosphoserineBy similarity | 1 | |
Modified residuei | 2164 | Phosphothreonine1 Publication | 1 | |
Modified residuei | 2173 | Phosphothreonine; by PKB/AKT1By similarity | 1 | |
Modified residuei | 2446 | Phosphothreonine; by RPS6KB1By similarity | 1 | |
Modified residuei | 2448 | Phosphoserine; by RPS6KB1By similarity | 1 | |
Modified residuei | 2478 | PhosphoserineBy similarity | 1 | |
Modified residuei | 2481 | Phosphoserine; by autocatalysisBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
jPOSTi | P42346 |
PaxDbi | P42346 |
PRIDEi | P42346 |
PTM databases
CarbonylDBi | P42346 |
iPTMneti | P42346 |
PhosphoSitePlusi | P42346 |
Expressioni
Gene expression databases
Bgeei | ENSRNOG00000009615, Expressed in skeletal muscle tissue and 21 other tissues |
ExpressionAtlasi | P42346, baseline and differential |
Genevisiblei | P42346, RN |
Interactioni
Subunit structurei
Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR. The mTORC1 complex is a 1 Md obligate dimer of two stoichiometric heterotetramers with overall dimensions of 290 A x 210 A x 135 A. It has a rhomboid shape and a central cavity, the dimeric interfaces are formed by interlocking interactions between the two MTOR and the two RPTOR subunits. The MLST8 subunit forms distal foot-like protuberances, and contacts only one MTOR within the complex, while the small PRAS40 localizes to the midsection of the central core, in close proximity to RPTOR. Part of the mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR.
Interacts with PRR5 and RICTOR; the interaction is direct within the mTORC2 complex and interaction with RICTOR is enhanced by deubiquitination of RICTOR by USP9X.
Interacts with WAC; WAC positively regulates MTOR activity by promoting the assembly of the TTT complex composed of TELO2, TTI1 and TTI2 and the RUVBL complex composed of RUVBL1 and RUVBL2 into the TTT-RUVBL complex which leads to the dimerization of the mTORC1 complex and its subsequent activation.
Interacts with PLPP7 and PML.
Interacts with UBQLN1.
Interacts with TTI1 and TELO2.
Interacts with CLIP1; phosphorylates and regulates CLIP1.
Interacts with NBN.
Interacts with BRAT1.
Interacts with MEAK7 (via C-terminal domain); the interaction increases upon nutrient stimulation (By similarity).
Interacts with TM4SF5; the interaction is positively regulated by arginine and is negatively regulated by leucine (By similarity).
Interacts with GPR137B (By similarity).
Interacts with NCKAP1L (By similarity).
Interacts with TPCN1 and TPCN2; the interaction is required for TPCN1 and TPCN2 sensitivity to ATP (By similarity).
Interacts with ATP6V1A and with CRYAB, forming a ternary complex (By similarity).
By similarityBinary interactionsi
P42346
With | #Exp. | IntAct |
---|---|---|
DEPTOR [Q8TB45] from Homo sapiens. | 2 | EBI-1571489,EBI-2359040 |
GO - Molecular functioni
- identical protein binding Source: RGD
- phosphoprotein binding Source: RGD
- protein domain specific binding Source: RGD
- protein kinase binding Source: RGD
- TFIIIC-class transcription factor complex binding Source: RGD
Protein-protein interaction databases
BioGRIDi | 248568, 6 interactors |
DIPi | DIP-261N |
IntActi | P42346, 10 interactors |
MINTi | P42346 |
STRINGi | 10116.ENSRNOP00000014167 |
Chemistry databases
BindingDBi | P42346 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 16 – 53 | HEAT 1Add BLAST | 38 | |
Repeati | 55 – 99 | HEAT 2Add BLAST | 45 | |
Repeati | 100 – 137 | HEAT 3Add BLAST | 38 | |
Repeati | 138 – 179 | HEAT 4Add BLAST | 42 | |
Repeati | 180 – 220 | HEAT 5Add BLAST | 41 | |
Repeati | 222 – 276 | HEAT 6Add BLAST | 55 | |
Repeati | 277 – 313 | HEAT 7Add BLAST | 37 | |
Repeati | 314 – 364 | HEAT 8Add BLAST | 51 | |
Repeati | 365 – 409 | HEAT 9Add BLAST | 45 | |
Repeati | 410 – 445 | HEAT 10Add BLAST | 36 | |
Repeati | 446 – 494 | HEAT 11Add BLAST | 49 | |
Repeati | 495 – 529 | HEAT 12Add BLAST | 35 | |
Repeati | 530 – 563 | HEAT 13Add BLAST | 34 | |
Repeati | 564 – 596 | HEAT 14Add BLAST | 33 | |
Repeati | 597 – 636 | HEAT 15Add BLAST | 40 | |
Repeati | 637 – 683 | HEAT 16Add BLAST | 47 | |
Repeati | 686 – 724 | HEAT 17Add BLAST | 39 | |
Repeati | 727 – 766 | HEAT 18Add BLAST | 40 | |
Repeati | 769 – 811 | HEAT 19Add BLAST | 43 | |
Repeati | 814 – 853 | HEAT 20Add BLAST | 40 | |
Repeati | 857 – 893 | HEAT 21Add BLAST | 37 | |
Repeati | 894 – 942 | HEAT 22Add BLAST | 49 | |
Repeati | 943 – 988 | HEAT 23Add BLAST | 46 | |
Repeati | 989 – 1027 | HEAT 24Add BLAST | 39 | |
Repeati | 1029 – 1068 | HEAT 25Add BLAST | 40 | |
Repeati | 1069 – 1105 | HEAT 26Add BLAST | 37 | |
Repeati | 1106 – 1144 | HEAT 27Add BLAST | 39 | |
Repeati | 1145 – 1188 | HEAT 28Add BLAST | 44 | |
Repeati | 1189 – 1225 | HEAT 29Add BLAST | 37 | |
Repeati | 1226 – 1273 | HEAT 30Add BLAST | 48 | |
Repeati | 1274 – 1311 | HEAT 31Add BLAST | 38 | |
Repeati | 1312 – 1345 | HEAT 32Add BLAST | 34 | |
Repeati | 1346 – 1382 | TPR 1Add BLAST | 37 | |
Domaini | 1382 – 1982 | FATPROSITE-ProRule annotationAdd BLAST | 601 | |
Repeati | 1383 – 1408 | TPR 2Add BLAST | 26 | |
Repeati | 1409 – 1442 | TPR 3Add BLAST | 34 | |
Repeati | 1443 – 1473 | TPR 4Add BLAST | 31 | |
Repeati | 1474 – 1507 | TPR 5Add BLAST | 34 | |
Repeati | 1508 – 1541 | TPR 6Add BLAST | 34 | |
Repeati | 1542 – 1574 | TPR 7Add BLAST | 33 | |
Repeati | 1575 – 1614 | TPR 8Add BLAST | 40 | |
Repeati | 1615 – 1649 | TPR 9Add BLAST | 35 | |
Repeati | 1650 – 1693 | TPR 10Add BLAST | 44 | |
Repeati | 1694 – 1731 | TPR 11Add BLAST | 38 | |
Repeati | 1732 – 1786 | TPR 12Add BLAST | 55 | |
Repeati | 1787 – 1846 | TPR 13Add BLAST | 60 | |
Repeati | 1898 – 1930 | TPR 14Add BLAST | 33 | |
Repeati | 1931 – 1970 | TPR 15Add BLAST | 40 | |
Repeati | 1971 – 2005 | TPR 16Add BLAST | 35 | |
Domaini | 2156 – 2469 | PI3K/PI4K catalyticPROSITE-ProRule annotationAdd BLAST | 314 | |
Domaini | 2517 – 2549 | FATCPROSITE-ProRule annotationAdd BLAST | 33 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 651 | Interaction with NBNBy similarityAdd BLAST | 651 | |
Regioni | 1812 – 1867 | DisorderedSequence analysisAdd BLAST | 56 | |
Regioni | 2012 – 2144 | Sufficient for interaction with the FKBP1A/rapamycin complexBy similarityAdd BLAST | 133 | |
Regioni | 2162 – 2168 | G-loopPROSITE-ProRule annotation | 7 | |
Regioni | 2258 – 2296 | Interaction with MLST8By similarityAdd BLAST | 39 | |
Regioni | 2335 – 2343 | Catalytic loopPROSITE-ProRule annotation | 9 | |
Regioni | 2355 – 2380 | Activation loopPROSITE-ProRule annotationAdd BLAST | 26 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 1822 – 1867 | Polar residuesSequence analysisAdd BLAST | 46 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Repeat, TPR repeatPhylogenomic databases
eggNOGi | KOG0891, Eukaryota |
GeneTreei | ENSGT00930000151037 |
HOGENOMi | CLU_000178_7_1_1 |
InParanoidi | P42346 |
OMAi | DPYKHQQ |
OrthoDBi | 26975at2759 |
PhylomeDBi | P42346 |
TreeFami | TF105134 |
Family and domain databases
Gene3Di | 1.10.1070.11, 1 hit 1.20.120.150, 1 hit 1.25.10.10, 4 hits 1.25.40.10, 1 hit |
InterProi | View protein in InterPro IPR011989, ARM-like IPR016024, ARM-type_fold IPR024585, DUF3385_TOR IPR003152, FATC_dom IPR009076, FRB_dom IPR036738, FRB_sf IPR011009, Kinase-like_dom_sf IPR000403, PI3/4_kinase_cat_dom IPR036940, PI3/4_kinase_cat_sf IPR018936, PI3/4_kinase_CS IPR003151, PIK-rel_kinase_FAT IPR014009, PIK_FAT IPR026683, TOR IPR011990, TPR-like_helical_dom_sf |
PANTHERi | PTHR11139:SF9, PTHR11139:SF9, 1 hit |
Pfami | View protein in Pfam PF11865, DUF3385, 1 hit PF02259, FAT, 1 hit PF02260, FATC, 1 hit PF08771, FRB_dom, 1 hit PF00454, PI3_PI4_kinase, 1 hit |
SMARTi | View protein in SMART SM01346, DUF3385, 1 hit SM01343, FATC, 1 hit SM00146, PI3Kc, 1 hit |
SUPFAMi | SSF47212, SSF47212, 1 hit SSF48371, SSF48371, 1 hit SSF56112, SSF56112, 1 hit |
PROSITEi | View protein in PROSITE PS51189, FAT, 1 hit PS51190, FATC, 1 hit PS00915, PI3_4_KINASE_1, 1 hit PS00916, PI3_4_KINASE_2, 1 hit PS50290, PI3_4_KINASE_3, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
10 20 30 40 50
MLGTGPATAT AGAATSSNVS VLQQFASGLK SRNEETRAKA AKELQHYVTM
60 70 80 90 100
ELREMSQEES TRFYDQLNHH IFELVSSSDA NERKGGILAI ASLIGVEGGN
110 120 130 140 150
STRIGRFANY LRNLLPSSDP VVMEMASKAI GRLAMAGDTF TAEYVEFEVK
160 170 180 190 200
RALEWLGADR NEGRRHAAVL VLRELAISVP TFFFQQVQPF FDNIFVAVWD
210 220 230 240 250
PKQAIREGAV AALRACLILT TQREPKEMQK PQWYRHTFEE AEKGFDETLA
260 270 280 290 300
KEKGMNRDDR IHGALLILNE LVRISSMEGE RLREEMEEIT QQQLVHDKYC
310 320 330 340 350
KDLMGFGTKP RHITPFTSFQ AVQPQQSNAL VGLLGYSSHQ GLMGFGASPS
360 370 380 390 400
PTKSTLVESR CCRDLMEEKF DQVCQWVLKC RSSKNSLIQM TILNLLPRLA
410 420 430 440 450
AFRPSAFTDT QYLQDTMNHV LSCVKKEKER TAAFQALGLL SVAVRSEFKV
460 470 480 490 500
YLPRVLDIIR AALPPKDFAH KRQKTVQVDA TVFTCISMLA RAMGPGIQQD
510 520 530 540 550
IKELLEPMLA VGLSPALTAV LYDLSRQIPQ LKKDIQDGLL KMLSLVLMHK
560 570 580 590 600
PLRHPGMPKG LAHQLASPGL TTLPEASDVA SITLALRTLG SFEFEGHSLT
610 620 630 640 650
QFVRHCADHF LNSEHKEIRM EAARTCSRLL TPSIHLISGH AHVVSQTAVQ
660 670 680 690 700
VVADVLSKLL VVGITDPDPD IRYCVLASLD ERFDAHLAQA ENLQALFVAL
710 720 730 740 750
NDQVFEIREL AICTVGRLSS MNPAFVMPFL RKMLIQILTE LEHSGIGRIK
760 770 780 790 800
EQSARMLGHL VSNAPRLIRP YMEPILKALI LKLKDPDPDP NPGVINNVLA
810 820 830 840 850
TIGELAQVSG LEMRKWVDEL FVIIMDMLQD SSLLAKRQVA LWTLGQLVAS
860 870 880 890 900
TGYVVEPYRK YPTLLEVLLN FLKTEQNQGT RREAIRVLGL LGALDPYKHK
910 920 930 940 950
VNIGMIDQSR DASAVSLSES KSSQDSSDYS TSEMLVNMGN LPLDEFYPAV
960 970 980 990 1000
SMVALMRIFR DQSLSHHHTM VVQAITFIFK SLGLKCVQFL PQVMPTFLNV
1010 1020 1030 1040 1050
IRVCDGAIRE FLFQQLGMLV SFVKSHIRPY MDEIVTLMRE FWVMNTSIQS
1060 1070 1080 1090 1100
TIILLIEQIV VALGGEFKLY LPQLIPHMLR VFMHDNSQGR IVSIKLLAAI
1110 1120 1130 1140 1150
QLFGANLDDY LHLLLPPIVK LFDAPEVPLP SRKAALETVD RLTESLDFTD
1160 1170 1180 1190 1200
YASRIIHPIV RTLDQSPELR STAMDTLSSL VFQLGKKYQI FIPMVNKVLV
1210 1220 1230 1240 1250
RHRINHQRYD VLICRIVKGY TLADEEEDPL IYQHRMLRSS QGDALASGPV
1260 1270 1280 1290 1300
ETGPMKKLHV STINLQKAWG AARRVSKDDW LEWLRRLSLE LLKDSSSPSL
1310 1320 1330 1340 1350
RSCWALAQAY NPMARDLFNA AFVSCWSELN EDQQDELIRS IELALTSQDI
1360 1370 1380 1390 1400
AEVTQTLLNL AEFMEHSDKG PLPLRDDNGI VLLGERAAKC RAYAKALHYK
1410 1420 1430 1440 1450
ELEFQKGPTP AILESLISIN NKLQQPEAAS GVLEYAMKHF GELEIQATWY
1460 1470 1480 1490 1500
EKLHEWEDAL VAYDKKMDTN KDDPELMLGR MRCLEALGEW GQLHQQCCEK
1510 1520 1530 1540 1550
WTLVNDETQA KMARMAAAAA WGLGQWDSME EYTCMIPRDT HDGAFYRAVL
1560 1570 1580 1590 1600
ALHQDLFSLA QQCIDKARDL LDAELTAMAG ESYSRAYGAM VSCHMLSELE
1610 1620 1630 1640 1650
EVIQYKLVPE RREIIRQIWW ERLQGCQRIV EDWQKILMVR SLVVSPHEDM
1660 1670 1680 1690 1700
RTWLKYASLC GKSGRLALAH KTLVLLLGVD PSRQLDHPLP TVHPQVTYAY
1710 1720 1730 1740 1750
MKNMWKSARK IDAFQHMQHF VQTMQQQAQH AIATEDQQHK QELHKLMARC
1760 1770 1780 1790 1800
FLKLGEWQLN LQGINESTIP KVLQYYSAAT EHDRSWYKAW HAWAVMNFEA
1810 1820 1830 1840 1850
VLHYKHQNQA RDEKKKLRHA SGANITNATT TATTAASAAA ATSTEGSNSE
1860 1870 1880 1890 1900
SEAESNESSP TPSPLQKKVT EDLSKTLLLY TVPAVQGFFR SISLSRGNNL
1910 1920 1930 1940 1950
QDTLRVLTLW FDYGHWPDVN EALVEGVKAI QIDTWLQVIP QLIARIDTPR
1960 1970 1980 1990 2000
PLVGRLIHQL LTDIGRYHPQ ALIYPLTVAS KSTTTARHNA ANKILKNMCE
2010 2020 2030 2040 2050
HSNTLVQQAM MVSEELIRVA ILWHEMWHEG LEEASRLYFG ERNVKGMFEV
2060 2070 2080 2090 2100
LEPLHAMMER GPQTLKETSF NQAYGRDLME AQEWCRKYMK SGNVKDLTQA
2110 2120 2130 2140 2150
WDLYYHVFRR ISKQLPQLTS LELQYVSPKL LMCRDLELAV PGTYDPNQPI
2160 2170 2180 2190 2200
IRIQSIAPSL QVITSKQRPR KLTLMGSNGH EFVFLLKGHE DLRQDERVMQ
2210 2220 2230 2240 2250
LFGLVNTLLA NDPTSLRKNL SIQRYAVIPL STNSGLIGWV PHCDTLHALI
2260 2270 2280 2290 2300
RDYREKKKIL LNIEHRIMLR MAPDYDHLTL MQKVEVFEHA VNNTAGDDLA
2310 2320 2330 2340 2350
KLLWLKSPSS EVWFDRRTNY TRSLAVMSMV GYILGLGDRH PSNLMLDRLS
2360 2370 2380 2390 2400
GKILHIDFGD CFEVAMTREK FPEKIPFRLT RMLTNAMEVT GLDGNYRTTC
2410 2420 2430 2440 2450
HTVMEVLREH KDSVMAVLEA FVYDPLLNWR LMDTNAKGNK RSRTRTDSYS
2460 2470 2480 2490 2500
AGQSVEILDG VELGEPAHKK TGTTVPESIH SFIGDGLVKP EALNKKAIQI
2510 2520 2530 2540
INRVRDKLTG RDFSHDDTLD VPTQVELLIK QATSHENLCQ CYIGWCPFW
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A0G2JX74 | A0A0G2JX74_RAT | Serine/threonine-protein kinase mTO... | Mtor | 2,553 | Annotation score: | ||
A0A8I6APT3 | A0A8I6APT3_RAT | Serine/threonine-protein kinase mTO... | Mtor | 2,559 | Annotation score: |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L37085 mRNA Translation: AAA65929.1 U11681 mRNA Translation: AAA20091.1 |
PIRi | A54837 |
RefSeqi | NP_063971.1, NM_019906.1 |
Genome annotation databases
GeneIDi | 56718 |
KEGGi | rno:56718 |
UCSCi | RGD:68371, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L37085 mRNA Translation: AAA65929.1 U11681 mRNA Translation: AAA20091.1 |
PIRi | A54837 |
RefSeqi | NP_063971.1, NM_019906.1 |
3D structure databases
AlphaFoldDBi | P42346 |
BMRBi | P42346 |
SMRi | P42346 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 248568, 6 interactors |
DIPi | DIP-261N |
IntActi | P42346, 10 interactors |
MINTi | P42346 |
STRINGi | 10116.ENSRNOP00000014167 |
Chemistry databases
BindingDBi | P42346 |
ChEMBLi | CHEMBL1075134 |
PTM databases
CarbonylDBi | P42346 |
iPTMneti | P42346 |
PhosphoSitePlusi | P42346 |
Proteomic databases
jPOSTi | P42346 |
PaxDbi | P42346 |
PRIDEi | P42346 |
Genome annotation databases
GeneIDi | 56718 |
KEGGi | rno:56718 |
UCSCi | RGD:68371, rat |
Organism-specific databases
CTDi | 2475 |
RGDi | 68371, Mtor |
Phylogenomic databases
eggNOGi | KOG0891, Eukaryota |
GeneTreei | ENSGT00930000151037 |
HOGENOMi | CLU_000178_7_1_1 |
InParanoidi | P42346 |
OMAi | DPYKHQQ |
OrthoDBi | 26975at2759 |
PhylomeDBi | P42346 |
TreeFami | TF105134 |
Enzyme and pathway databases
Reactomei | R-RNO-1257604, PIP3 activates AKT signaling R-RNO-1632852, Macroautophagy R-RNO-165159, MTOR signalling R-RNO-166208, mTORC1-mediated signalling R-RNO-3371571, HSF1-dependent transactivation R-RNO-380972, Energy dependent regulation of mTOR by LKB1-AMPK R-RNO-389357, CD28 dependent PI3K/Akt signaling R-RNO-5218920, VEGFR2 mediated vascular permeability R-RNO-5628897, TP53 Regulates Metabolic Genes R-RNO-6804757, Regulation of TP53 Degradation R-RNO-8943724, Regulation of PTEN gene transcription R-RNO-9639288, Amino acids regulate mTORC1 |
Miscellaneous databases
PROi | PR:P42346 |
Gene expression databases
Bgeei | ENSRNOG00000009615, Expressed in skeletal muscle tissue and 21 other tissues |
ExpressionAtlasi | P42346, baseline and differential |
Genevisiblei | P42346, RN |
Family and domain databases
Gene3Di | 1.10.1070.11, 1 hit 1.20.120.150, 1 hit 1.25.10.10, 4 hits 1.25.40.10, 1 hit |
InterProi | View protein in InterPro IPR011989, ARM-like IPR016024, ARM-type_fold IPR024585, DUF3385_TOR IPR003152, FATC_dom IPR009076, FRB_dom IPR036738, FRB_sf IPR011009, Kinase-like_dom_sf IPR000403, PI3/4_kinase_cat_dom IPR036940, PI3/4_kinase_cat_sf IPR018936, PI3/4_kinase_CS IPR003151, PIK-rel_kinase_FAT IPR014009, PIK_FAT IPR026683, TOR IPR011990, TPR-like_helical_dom_sf |
PANTHERi | PTHR11139:SF9, PTHR11139:SF9, 1 hit |
Pfami | View protein in Pfam PF11865, DUF3385, 1 hit PF02259, FAT, 1 hit PF02260, FATC, 1 hit PF08771, FRB_dom, 1 hit PF00454, PI3_PI4_kinase, 1 hit |
SMARTi | View protein in SMART SM01346, DUF3385, 1 hit SM01343, FATC, 1 hit SM00146, PI3Kc, 1 hit |
SUPFAMi | SSF47212, SSF47212, 1 hit SSF48371, SSF48371, 1 hit SSF56112, SSF56112, 1 hit |
PROSITEi | View protein in PROSITE PS51189, FAT, 1 hit PS51190, FATC, 1 hit PS00915, PI3_4_KINASE_1, 1 hit PS00916, PI3_4_KINASE_2, 1 hit PS50290, PI3_4_KINASE_3, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | MTOR_RAT | |
Accessioni | P42346Primary (citable) accession number: P42346 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
Last sequence update: | November 1, 1995 | |
Last modified: | May 25, 2022 | |
This is version 194 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families