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Protein

Serine/threonine-protein kinase mTOR

Gene

Mtor

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 osteoclastogensis by adjusting the expression of CEBPB isoforms (By similarity).By similarity1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme 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

GO - Biological processi

  • 'de novo' pyrimidine nucleobase biosynthetic process Source: Ensembl
  • brain development Source: RGD
  • cardiac muscle cell development Source: Ensembl
  • cardiac muscle contraction Source: Ensembl
  • cell aging Source: RGD
  • cell growth Source: Ensembl
  • cell projection organization Source: MGI
  • cellular response to hypoxia Source: UniProtKB
  • 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
  • maternal process involved in female pregnancy Source: RGD
  • mRNA stabilization Source: RGD
  • multicellular organism growth Source: Ensembl
  • negative regulation of autophagy Source: UniProtKB
  • 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: Ensembl
  • negative regulation of muscle atrophy Source: RGD
  • negative regulation of NFAT protein import into nucleus Source: Ensembl
  • negative regulation of protein phosphorylation Source: RGD
  • negative regulation of protein ubiquitination Source: RGD
  • 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
  • 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 glial cell proliferation Source: RGD
  • positive regulation of granulosa cell proliferation Source: RGD
  • 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
  • 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: Ensembl
  • positive regulation of protein kinase B signaling 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: Ensembl
  • positive regulation of transcription from RNA polymerase III promoter Source: Ensembl
  • positive regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter Source: Ensembl
  • positive regulation of translation Source: RGD
  • post-embryonic development Source: Ensembl
  • protein autophosphorylation Source: RGD
  • protein phosphorylation Source: RGD
  • regulation of brown fat cell differentiation Source: RGD
  • regulation of carbohydrate metabolic process Source: RGD
  • regulation of carbohydrate utilization Source: RGD
  • regulation of fatty acid beta-oxidation Source: RGD
  • regulation of glycogen biosynthetic process Source: RGD
  • 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
  • response to amino acid Source: Ensembl
  • response to cocaine Source: RGD
  • response to insulin Source: Ensembl
  • response to morphine Source: RGD
  • ruffle organization Source: Ensembl
  • social behavior Source: RGD
  • spinal cord development Source: RGD
  • TOR signaling Source: Ensembl
  • visual learning Source: RGD
  • voluntary musculoskeletal movement Source: Ensembl
  • wound healing Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-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.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi68371. Mtor.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
  • Golgi apparatus membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
  • Mitochondrion outer membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
  • Lysosome By similarity
  • Cytoplasm By similarity
  • NucleusPML body 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).By similarity

GO - Cellular componenti

  • cytosol Source: RGD
  • dendrite Source: Ensembl
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • Golgi membrane Source: UniProtKB-SubCell
  • lysosomal membrane Source: Ensembl
  • lysosome Source: UniProtKB
  • macromolecular complex Source: RGD
  • mitochondrial outer membrane Source: UniProtKB-SubCell
  • nucleus Source: RGD
  • PML body Source: UniProtKB-SubCell
  • TORC1 complex Source: RGD
  • TORC2 complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1075134.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000888101 – 2549Serine/threonine-protein kinase mTORAdd BLAST2549

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei567PhosphoserineBy similarity1
Modified residuei1162PhosphothreonineBy similarity1
Modified residuei1218N6-acetyllysineBy similarity1
Modified residuei1261PhosphoserineBy similarity1
Modified residuei2159PhosphoserineBy similarity1
Modified residuei2164Phosphothreonine1 Publication1
Modified residuei2173Phosphothreonine; by PKB/AKT1By similarity1
Modified residuei2446Phosphothreonine; by RPS6KB1By similarity1
Modified residuei2448Phosphoserine; by RPS6KB1By similarity1
Modified residuei2478PhosphoserineBy similarity1
Modified residuei2481Phosphoserine; by autocatalysisBy similarity1

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

PaxDbiP42346.
PRIDEiP42346.

PTM databases

iPTMnetiP42346.
PhosphoSitePlusiP42346.

Expressioni

Gene expression databases

BgeeiENSRNOG00000009615.
ExpressionAtlasiP42346. baseline and differential.
GenevisibleiP42346. 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 subunits 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 PLPP7 and PML. Interacts with PRR5 and RICTOR; the interaction is direct within the mTORC2 complex. Interacts with UBQLN1. Interacts with TTI1 and TELO2. Interacts with CLIP1; phosphorylates and regulates CLIP1. Interacts with NBN. Interacts with BRAT1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
DEPTORQ8TB452EBI-1571489,EBI-2359040From a different organism.

GO - Molecular functioni

  • protein domain specific binding Source: RGD
  • protein kinase binding Source: RGD

Protein-protein interaction databases

BioGridi248568. 4 interactors.
DIPiDIP-261N.
IntActiP42346. 3 interactors.
MINTiMINT-87926.
STRINGi10116.ENSRNOP00000014167.

Chemistry databases

BindingDBiP42346.

Structurei

3D structure databases

ProteinModelPortaliP42346.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati16 – 53HEAT 1Add BLAST38
Repeati55 – 99HEAT 2Add BLAST45
Repeati100 – 137HEAT 3Add BLAST38
Repeati138 – 179HEAT 4Add BLAST42
Repeati180 – 220HEAT 5Add BLAST41
Repeati222 – 276HEAT 6Add BLAST55
Repeati277 – 313HEAT 7Add BLAST37
Repeati314 – 364HEAT 8Add BLAST51
Repeati365 – 409HEAT 9Add BLAST45
Repeati410 – 445HEAT 10Add BLAST36
Repeati446 – 494HEAT 11Add BLAST49
Repeati495 – 529HEAT 12Add BLAST35
Repeati530 – 563HEAT 13Add BLAST34
Repeati564 – 596HEAT 14Add BLAST33
Repeati597 – 636HEAT 15Add BLAST40
Repeati637 – 683HEAT 16Add BLAST47
Repeati686 – 724HEAT 17Add BLAST39
Repeati727 – 766HEAT 18Add BLAST40
Repeati769 – 811HEAT 19Add BLAST43
Repeati814 – 853HEAT 20Add BLAST40
Repeati857 – 893HEAT 21Add BLAST37
Repeati894 – 942HEAT 22Add BLAST49
Repeati943 – 988HEAT 23Add BLAST46
Repeati989 – 1027HEAT 24Add BLAST39
Repeati1029 – 1068HEAT 25Add BLAST40
Repeati1069 – 1105HEAT 26Add BLAST37
Repeati1106 – 1144HEAT 27Add BLAST39
Repeati1145 – 1188HEAT 28Add BLAST44
Repeati1189 – 1225HEAT 29Add BLAST37
Repeati1226 – 1273HEAT 30Add BLAST48
Repeati1274 – 1311HEAT 31Add BLAST38
Repeati1312 – 1345HEAT 32Add BLAST34
Repeati1346 – 1382TPR 1Add BLAST37
Domaini1382 – 1982FATPROSITE-ProRule annotationAdd BLAST601
Repeati1383 – 1408TPR 2Add BLAST26
Repeati1409 – 1442TPR 3Add BLAST34
Repeati1443 – 1473TPR 4Add BLAST31
Repeati1474 – 1507TPR 5Add BLAST34
Repeati1508 – 1541TPR 6Add BLAST34
Repeati1542 – 1574TPR 7Add BLAST33
Repeati1575 – 1614TPR 8Add BLAST40
Repeati1615 – 1649TPR 9Add BLAST35
Repeati1650 – 1693TPR 10Add BLAST44
Repeati1694 – 1731TPR 11Add BLAST38
Repeati1732 – 1786TPR 12Add BLAST55
Repeati1787 – 1846TPR 13Add BLAST60
Repeati1898 – 1930TPR 14Add BLAST33
Repeati1931 – 1970TPR 15Add BLAST40
Repeati1971 – 2005TPR 16Add BLAST35
Domaini2182 – 2516PI3K/PI4KPROSITE-ProRule annotationAdd BLAST335
Domaini2517 – 2549FATCPROSITE-ProRule annotationAdd BLAST33

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 651Interaction with NBNBy similarityAdd BLAST651
Regioni2012 – 2144Sufficient for interaction with the FKBP1A/rapamycin complexBy similarityAdd BLAST133
Regioni2258 – 2296Interaction with MLST8By similarityAdd BLAST39

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
Contains 1 FAT domain.PROSITE-ProRule annotation
Contains 1 FATC domain.PROSITE-ProRule annotation
Contains 32 HEAT repeats.Curated
Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation
Contains 16 TPR repeats.Curated

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG0891. Eukaryota.
COG5032. LUCA.
GeneTreeiENSGT00860000133856.
HOVERGENiHBG005744.
InParanoidiP42346.
KOiK07203.
OMAiCCKLVAH.
OrthoDBiEOG091G0046.
PhylomeDBiP42346.
TreeFamiTF105134.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
1.20.120.150. 1 hit.
1.25.10.10. 4 hits.
1.25.40.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024585. DUF3385_TOR.
IPR003152. FATC_dom.
IPR009076. FRB_dom.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR026683. TOR.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PANTHERiPTHR11139:SF9. PTHR11139:SF9. 2 hits.
PfamiPF11865. DUF3385. 1 hit.
PF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF08771. FRB_dom. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
[Graphical view]
SMARTiSM01346. DUF3385. 1 hit.
SM01343. FATC. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF47212. SSF47212. 1 hit.
SSF48371. SSF48371. 5 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51189. 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42346-1 [UniParc]FASTAAdd to basket

« Hide

        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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37085 mRNA. Translation: AAA65929.1.
U11681 mRNA. Translation: AAA20091.1.
PIRiA54837.
RefSeqiNP_063971.1. NM_019906.1.
UniGeneiRn.11008.

Genome annotation databases

EnsembliENSRNOT00000014167; ENSRNOP00000014167; ENSRNOG00000009615.
GeneIDi56718.
KEGGirno:56718.
UCSCiRGD:68371. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37085 mRNA. Translation: AAA65929.1.
U11681 mRNA. Translation: AAA20091.1.
PIRiA54837.
RefSeqiNP_063971.1. NM_019906.1.
UniGeneiRn.11008.

3D structure databases

ProteinModelPortaliP42346.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248568. 4 interactors.
DIPiDIP-261N.
IntActiP42346. 3 interactors.
MINTiMINT-87926.
STRINGi10116.ENSRNOP00000014167.

Chemistry databases

BindingDBiP42346.
ChEMBLiCHEMBL1075134.

PTM databases

iPTMnetiP42346.
PhosphoSitePlusiP42346.

Proteomic databases

PaxDbiP42346.
PRIDEiP42346.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000014167; ENSRNOP00000014167; ENSRNOG00000009615.
GeneIDi56718.
KEGGirno:56718.
UCSCiRGD:68371. rat.

Organism-specific databases

CTDi2475.
RGDi68371. Mtor.

Phylogenomic databases

eggNOGiKOG0891. Eukaryota.
COG5032. LUCA.
GeneTreeiENSGT00860000133856.
HOVERGENiHBG005744.
InParanoidiP42346.
KOiK07203.
OMAiCCKLVAH.
OrthoDBiEOG091G0046.
PhylomeDBiP42346.
TreeFamiTF105134.

Enzyme and pathway databases

ReactomeiR-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.

Miscellaneous databases

PROiP42346.

Gene expression databases

BgeeiENSRNOG00000009615.
ExpressionAtlasiP42346. baseline and differential.
GenevisibleiP42346. RN.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
1.20.120.150. 1 hit.
1.25.10.10. 4 hits.
1.25.40.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024585. DUF3385_TOR.
IPR003152. FATC_dom.
IPR009076. FRB_dom.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR026683. TOR.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PANTHERiPTHR11139:SF9. PTHR11139:SF9. 2 hits.
PfamiPF11865. DUF3385. 1 hit.
PF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF08771. FRB_dom. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
[Graphical view]
SMARTiSM01346. DUF3385. 1 hit.
SM01343. FATC. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF47212. SSF47212. 1 hit.
SSF48371. SSF48371. 5 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51189. 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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMTOR_RAT
AccessioniPrimary (citable) accession number: P42346
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 30, 2016
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.