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. MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins. Functions as part of 2 structurally and functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR complex 1 and 2). Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. This includes phosphorylation of EIF4EBP1 and release of its inhibition toward the elongation initiation factor 4E (eiF4E). 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. 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. Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 an RNA polymerase III-repressor. In parallel to protein synthesis, also regulates lipid synthesis through SREBF1/SREBP1 and LPIN1. To maintain energy homeostasis mTORC1 may also regulate mitochondrial biogenesis through regulation of PPARGC1A. mTORC1 also negatively regulates autophagy through phosphorylation of ULK1. Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-758', disrupting the interaction with AMPK and preventing activation of ULK1. Also prevents autophagy through phosphorylation of the autophagy inhibitor DAP. mTORC1 exerts a feedback control on upstream growth factor signaling that includes phosphorylation and activation of GRB10 a INSR-dependent signaling suppressor. Among other potential targets mTORC1 may phosphorylate CLIP1 and regulate microtubules. As part of the mTORC2 complex MTOR may regulate other cellular processes including survival and organization of the cytoskeleton. 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. 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. mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-421'. Regulates osteoclastogenesis by adjusting the expression of CEBPB isoforms (By similarity).By similarity1 Publication

Catalytic activityⁱ

ATP + a protein = ADP + a phosphoprotein.

Activity regulationⁱ

Activation of mTORC1 by growth factors such as insulin involves AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase a potent activator of the protein kinase activity of mTORC1. Insulin-stimulated and amino acid-dependent phosphorylation at Ser-1261 promotes autophosphorylation and the activation of mTORC1. Activation by amino acids requires relocalization of the mTORC1 complex to lysosomes that is mediated by the Ragulator complex, SLC38A9, and the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD. On the other hand, low cellular energy levels can inhibit mTORC1 through activation of PRKAA1 while hypoxia inhibits mTORC1 through a REDD1-dependent mechanism which may also require PRKAA1. The kinase activity of MTOR within the mTORC1 complex is positively regulated by MLST8 and negatively regulated by DEPTOR and AKT1S1. MTOR phosphorylates RPTOR which in turn inhibits mTORC1. MTOR is the target of the immunosuppressive and anti-cancer drug rapamycin which acts in complex with FKBP1A/FKBP12, and specifically inhibits its kinase activity. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. It may be regulated by RHEB but in an indirect manner through the PI3K signaling pathway.By similarity

GO - Molecular functionⁱ

ATP binding Source: UniProtKB-KW
identical protein binding Source: Ensembl
phosphoprotein binding Source: Ensembl
protein domain specific binding
Source: RGD
Inferred from physical interactionⁱ
- 11853878
protein kinase binding
Source: RGD
Inferred from physical interactionⁱ
- 24583056
protein serine/threonine kinase activity
Source: RGD
Inferred from direct assayⁱ
- 17142137
ribosome binding Source: Ensembl
RNA polymerase III type 1 promoter DNA binding Source: Ensembl
RNA polymerase III type 2 promoter DNA binding Source: Ensembl
RNA polymerase III type 3 promoter DNA binding Source: Ensembl
TFIIIC-class transcription factor binding Source: Ensembl

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

'de novo' pyrimidine nucleobase biosynthetic process Source: Ensembl
brain development
Source: RGD
Inferred from expression patternⁱ
- 19439614
cardiac muscle cell development Source: Ensembl
cardiac muscle contraction Source: Ensembl
cell aging
Source: RGD
Inferred from expression patternⁱ
- 19698731
cell projection organization
Source: MGI
Inferred from genetic interactionⁱ
- 16286931
cellular response to hypoxia Source: UniProtKB
cellular response to leucine Source: Ensembl
cellular response to leucine starvation Source: Ensembl
cellular response to nutrient levels Source: UniProtKB
DNA repair Source: GO_Central
energy reserve metabolic process Source: Ensembl
germ cell development Source: Ensembl
heart morphogenesis Source: Ensembl
heart valve morphogenesis Source: Ensembl
long-term memory
Source: RGD
Inferred from mutant phenotypeⁱ
- 24076274
maternal process involved in female pregnancy
Source: RGD
Inferred from direct assayⁱ
- 19589861
mRNA stabilization
Source: RGD
Inferred from mutant phenotypeⁱ
- 21073857
multicellular organism growth Source: Ensembl
negative regulation of autophagy
Source: RGD
Inferred from mutant phenotypeⁱ
- 24725502
negative regulation of calcineurin-NFAT signaling cascade Source: Ensembl
negative regulation of cell size
Source: MGI
Inferred from mutant phenotypeⁱ
- 16286931
negative regulation of cholangiocyte apoptotic process
Source: RGD
Inferred from mutant phenotypeⁱ
- 24498161
negative regulation of iodide transmembrane transport
Source: RGD
Inferred from mutant phenotypeⁱ
- 20392814
negative regulation of macroautophagy Source: Ensembl
negative regulation of muscle atrophy
Source: RGD
Inferred from mutant phenotypeⁱ
- 19260063
negative regulation of protein phosphorylation
Source: RGD
Inferred from mutant phenotypeⁱ
- 21357504
negative regulation of protein ubiquitination
Source: RGD
Inferred from mutant phenotypeⁱ
- 21357504
peptidyl-serine phosphorylation Source: Ensembl
peptidyl-threonine phosphorylation Source: Ensembl
positive regulation of actin filament polymerization Source: Ensembl
positive regulation of cell death
Source: RGD
Inferred from mutant phenotypeⁱ
- 21779001
positive regulation of cell growth involved in cardiac muscle cell development
Source: RGD
Inferred from mutant phenotypeⁱ
- 21318349
- 21933187
positive regulation of cholangiocyte proliferation
Source: RGD
Inferred from mutant phenotypeⁱ
- 24498161
positive regulation of dendritic spine development
Source: RGD
Inferred from mutant phenotypeⁱ
- 21683721
positive regulation of eating behavior
Source: RGD
Inferred from mutant phenotypeⁱ
- 23955309
positive regulation of endothelial cell proliferation
Source: RGD
Inferred from mutant phenotypeⁱ
- 17110594
positive regulation of epithelial to mesenchymal transition Source: Ensembl
positive regulation of glial cell proliferation
Source: RGD
Inferred from mutant phenotypeⁱ
- 19576187
positive regulation of granulosa cell proliferation
Source: RGD
Inferred from mutant phenotypeⁱ
- 22383759
positive regulation of keratinocyte migration Source: Ensembl
positive regulation of lamellipodium assembly Source: Ensembl
positive regulation of lipid biosynthetic process Source: UniProtKB
positive regulation of myotube differentiation Source: Ensembl
positive regulation of neurogenesis
Source: RGD
Inferred from mutant phenotypeⁱ
- 19474323
positive regulation of neuron death
Source: RGD
Inferred from mutant phenotypeⁱ
- 19474323
positive regulation of neuron maturation
Source: RGD
Inferred from mutant phenotypeⁱ
- 24118019
positive regulation of neuron projection development
Source: RGD
Inferred from mutant phenotypeⁱ
- 22705730
positive regulation of nitric oxide biosynthetic process
Source: RGD
Inferred from mutant phenotypeⁱ
- 19576187
positive regulation of oligodendrocyte differentiation
Source: RGD
Inferred from mutant phenotypeⁱ
- 19439614
positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
positive regulation of protein kinase B signaling
Source: RGD
Inferred from mutant phenotypeⁱ
- 17110594
positive regulation of sensory perception of pain
Source: RGD
Inferred from mutant phenotypeⁱ
- 24132796
positive regulation of skeletal muscle hypertrophy
Source: RGD
Inferred from mutant phenotypeⁱ
- 23470307
positive regulation of smooth muscle cell proliferation
Source: RGD
Inferred from mutant phenotypeⁱ
- 19589861
positive regulation of stress fiber assembly Source: Ensembl
positive regulation of transcription by RNA polymerase III Source: Ensembl
positive regulation of transcription of nucleolar large rRNA by RNA polymerase I Source: Ensembl
positive regulation of translation
Source: RGD
Inferred from mutant phenotypeⁱ
- 15525761
positive regulation of wound healing, spreading of epidermal cells Source: Ensembl
post-embryonic development Source: Ensembl
protein autophosphorylation
Source: RGD
Inferred from mutant phenotypeⁱ
- 15388509
protein phosphorylation
Source: RGD
Inferred from direct assayⁱ
- 17142137
regulation of brown fat cell differentiation
Source: RGD
Inferred from mutant phenotypeⁱ
- 20133456
regulation of carbohydrate metabolic process
Source: RGD
Inferred from direct assayⁱ
- 17142137
regulation of carbohydrate utilization
Source: RGD
Inferred from direct assayⁱ
- 17142137
regulation of fatty acid beta-oxidation
Source: RGD
Inferred from direct assayⁱ
- 17142137
regulation of glycogen biosynthetic process
Source: RGD
Inferred from direct assayⁱ
- 17142137
regulation of GTPase activity Source: Ensembl
regulation of membrane permeability Source: Ensembl
regulation of myelination Source: Ensembl
regulation of osteoclast differentiation Source: UniProtKB
regulation of protein kinase activity Source: Ensembl
regulation of response to food
Source: RGD
Inferred from direct assayⁱ
- 16690869
response to activity
Source: RGD
Inferred from expression patternⁱ
- 28536139
response to cocaine
Source: RGD
Inferred from mutant phenotypeⁱ
- 20977929
response to insulin Source: Ensembl
response to morphine
Source: RGD
Inferred from mutant phenotypeⁱ
- 24382350
response to nutrient Source: Ensembl
ruffle organization Source: Ensembl
social behavior
Source: RGD
Inferred from mutant phenotypeⁱ
- 23027611
spinal cord development
Source: RGD
Inferred from direct assayⁱ
- 23681769
T-helper 1 cell lineage commitment Source: Ensembl
TORC1 signaling Source: Ensembl
visual learning
Source: RGD
Inferred from mutant phenotypeⁱ
- 20599569
voluntary musculoskeletal movement Source: Ensembl
wound healing
Source: RGD
Inferred from expression patternⁱ
- 22490538

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Kinase, Serine/threonine-protein kinase, Transferase
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

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

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Serine/threonine-protein kinase mTOR (EC:2.7.11.1) 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	Name:Mtor Synonyms:Frap1, Raft1
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Chromosome 5

Organism-specific databases

Rat genome database More...RGDⁱ	68371 Mtor

RGDⁱ

68371 Mtor

Keywords - Cellular componentⁱ

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Lysosome, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus

Pathology & Biotechⁱ

Chemistry databases

ChEMBLⁱ	CHEMBL1075134

ChEMBLⁱ

CHEMBL1075134

PTM / 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	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

Autophosphorylates when part of mTORC1 or mTORC2. Phosphorylation at Ser-1261, Ser-2159 and Thr-2164 promotes autophosphorylation. Phosphorylation in the kinase domain modulates the interactions of MTOR with RPTOR and PRAS40 and leads to increased intrinsic mTORC1 kinase activity. Phosphorylation at Thr-2173 in the ATP-binding region by AKT1 strongly reduces kinase activity (By similarity).By similarity

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

PaxDbⁱ	P42346
PRIDEⁱ	P42346

PTM databases

CarbonylDBⁱ	P42346
iPTMnetⁱ	P42346
PhosphoSitePlusⁱ	P42346

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSRNOG00000009615 Expressed in 10 organ(s), highest expression level in skeletal muscle tissue
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. 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.By similarity

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
DEPTOR	Q8TB45	2	EBI-1571489,EBI-2359040	From Homo sapiens.

With

Entry

#Exp.

IntAct

Notes

DEPTOR

Q8TB45

2

EBI-1571489,EBI-2359040

From Homo sapiens.

GO - Molecular functionⁱ

identical protein binding Source: Ensembl
phosphoprotein binding Source: Ensembl
protein domain specific binding
Source: RGD
Inferred from physical interactionⁱ
- 11853878
protein kinase binding
Source: RGD
Inferred from physical interactionⁱ
- 24583056
TFIIIC-class transcription factor binding Source: Ensembl

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	248568, 4 interactors
Database of interacting proteins More...DIPⁱ	DIP-261N
IntActⁱ	P42346, 4 interactors
Molecular INTeraction database More...MINTⁱ	P42346
STRINGⁱ	10116.ENSRNOP00000014167

Chemistry databases

BindingDBⁱ

P42346

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P42346
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	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	2182 – 2516	PI3K/PI4KPROSITE-ProRule annotationAdd BLAST	335
Domainⁱ	2517 – 2549	FATCPROSITE-ProRule annotationAdd BLAST	33

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	1 – 651	Interaction with NBNBy similarityAdd BLAST	651
Regionⁱ	2012 – 2144	Sufficient for interaction with the FKBP1A/rapamycin complexBy similarityAdd BLAST	133
Regionⁱ	2258 – 2296	Interaction with MLST8By similarityAdd BLAST	39

Domainⁱ

The kinase domain (PI3K/PI4K) is intrinsically active but has a highly restricted catalytic center.By similarity

The FAT domain forms three discontinuous subdomains of alpha-helical TPR repeats plus a single subdomain of HEAT repeats. The four domains pack sequentially to form a C-shaped a-solenoid that clamps onto the kinase domain (By similarity).By similarity

Sequence similaritiesⁱ

Belongs to the PI3/PI4-kinase family.Curated

Keywords - Domainⁱ

Repeat, TPR repeat

Phylogenomic databases

eggNOGⁱ	KOG0891 Eukaryota COG5032 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00920000149065
HOVERGENⁱ	HBG005744
InParanoidⁱ	P42346
KEGG Orthology (KO) More...KOⁱ	K07203
OMAⁱ	SSHQGLM
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0046
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
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
PANTHERⁱ	PTHR11139:SF9 PTHR11139:SF9, 1 hit
Pfam protein domain database More...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, 5 hits SSF56112 SSF56112, 2 hits
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

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show all Align All

P42346-1 [UniParc]FASTA Add to basket

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        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

Length:2,549

Mass (Da):288,794

Last modified:November 1, 1995 - v1

Checksum:ⁱBE841EA7B9086F99

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	A0A0G2JX74	A0A0G2JX74_RAT		Serine/threonine-protein kinase mTO... Serine/threonine-protein kinase mTOR, EC 2.7.11.1	Mtor	2,545	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
NCBI Reference Sequences More...RefSeqⁱ	NP_063971.1, NM_019906.1
UniGeneⁱ	Rn.11008

Genome annotation databases

Ensemblⁱ	ENSRNOT00000014167; ENSRNOP00000014167; ENSRNOG00000009615
GeneIDⁱ	56718
KEGGⁱ	rno:56718
UCSC genome browser More...UCSCⁱ	RGD:68371 rat

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P42346	Serine/threonine-protein kinase mTOR		RAT		2545	UniRef100_P42346

Protein	Similar proteins		Species	Score	Length	Source
P42346	Serine/threonine-protein kinase mTOR	)	HUMAN		2549	UniRef90_P42345
Serine/threonine-protein kinase mTOR		MOUSE		2549
Serine/threonine-protein kinase mTOR		PANTR		2549
MTOR isoform 2		PONAB		754
Serine/threonine-protein kinase mTOR		MYOBR		2634
+302

Protein	Similar proteins		Species	Score	Length	Source
P42346	Serine/threonine-protein kinase mTOR	)	HUMAN		2549	UniRef50_P42345
Serine/threonine-protein kinase mTOR		MOUSE		2549
Serine/threonine-protein kinase mTOR		PANTR		2549
MTOR isoform 2		PONAB		754
Serine/threonine-protein kinase mTOR		MYOBR		2634
+454

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
UniGeneⁱ	Rn.11008

3D structure databases

ProteinModelPortalⁱ	P42346
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	248568, 4 interactors
DIPⁱ	DIP-261N
IntActⁱ	P42346, 4 interactors
MINTⁱ	P42346
STRINGⁱ	10116.ENSRNOP00000014167

Chemistry databases

BindingDBⁱ	P42346
ChEMBLⁱ	CHEMBL1075134

PTM databases

CarbonylDBⁱ	P42346
iPTMnetⁱ	P42346
PhosphoSitePlusⁱ	P42346

Proteomic databases

PaxDbⁱ	P42346
PRIDEⁱ	P42346

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSRNOT00000014167; ENSRNOP00000014167; ENSRNOG00000009615
GeneIDⁱ	56718
KEGGⁱ	rno:56718
UCSCⁱ	RGD:68371 rat

Organism-specific databases

CTDⁱ	2475
RGDⁱ	68371 Mtor

Phylogenomic databases

eggNOGⁱ	KOG0891 Eukaryota COG5032 LUCA
GeneTreeⁱ	ENSGT00920000149065
HOVERGENⁱ	HBG005744
InParanoidⁱ	P42346
KOⁱ	K07203
OMAⁱ	SSHQGLM
OrthoDBⁱ	EOG091G0046
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

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

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P42346

PROⁱ

PR:P42346

Gene expression databases

Bgeeⁱ	ENSRNOG00000009615 Expressed in 10 organ(s), highest expression level in skeletal muscle tissue
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
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
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, 5 hits SSF56112 SSF56112, 2 hits
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
ProtoNetⁱ	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:	September 12, 2018
	This is version 171 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

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UniProtKB - P42346 (MTOR_RAT)

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Serine/threonine-protein kinase mTOR

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

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<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

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<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

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<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ