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P42346

- MTOR_RAT

UniProt

P42346 - MTOR_RAT

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Protein

Serine/threonine-protein kinase mTOR

Gene

Mtor

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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'.1 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 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).By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. drug binding Source: InterPro
  3. protein domain specific binding Source: RGD
  4. protein serine/threonine kinase activity Source: RGD
  5. ribosome binding Source: Ensembl
  6. RNA polymerase III type 1 promoter DNA binding Source: Ensembl
  7. RNA polymerase III type 2 promoter DNA binding Source: Ensembl
  8. RNA polymerase III type 3 promoter DNA binding Source: Ensembl

GO - Biological processi

  1. cell projection organization Source: MGI
  2. cellular response to hypoxia Source: UniProtKB
  3. cellular response to nutrient levels Source: UniProtKB
  4. germ cell development Source: Ensembl
  5. negative regulation of autophagy Source: UniProtKB
  6. negative regulation of cell size Source: MGI
  7. negative regulation of macroautophagy Source: Ensembl
  8. negative regulation of NFAT protein import into nucleus Source: Ensembl
  9. peptidyl-serine phosphorylation Source: Ensembl
  10. peptidyl-threonine phosphorylation Source: Ensembl
  11. positive regulation of actin filament polymerization Source: Ensembl
  12. positive regulation of endothelial cell proliferation Source: RGD
  13. positive regulation of lamellipodium assembly Source: Ensembl
  14. positive regulation of lipid biosynthetic process Source: UniProtKB
  15. positive regulation of myotube differentiation Source: Ensembl
  16. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
  17. positive regulation of protein kinase B signaling Source: RGD
  18. positive regulation of stress fiber assembly Source: Ensembl
  19. positive regulation of transcription from RNA polymerase III promoter Source: Ensembl
  20. positive regulation of translation Source: RGD
  21. protein autophosphorylation Source: RGD
  22. protein phosphorylation Source: RGD
  23. regulation of carbohydrate metabolic process Source: RGD
  24. regulation of carbohydrate utilization Source: RGD
  25. regulation of fatty acid beta-oxidation Source: RGD
  26. regulation of glycogen biosynthetic process Source: RGD
  27. regulation of protein kinase activity Source: Ensembl
  28. regulation of Rac GTPase activity Source: Ensembl
  29. regulation of response to food Source: RGD
  30. response to amino acid Source: Ensembl
  31. response to insulin Source: Ensembl
  32. ruffle organization Source: Ensembl
  33. TOR signaling Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_198729. Constitutive PI3K/AKT Signaling in Cancer.
REACT_216105. HSF1-dependent transactivation.

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
ProteomesiUP000002494: 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

  1. cytosol Source: RGD
  2. endoplasmic reticulum Source: UniProtKB-KW
  3. Golgi apparatus Source: UniProtKB-KW
  4. lysosomal membrane Source: Ensembl
  5. lysosome Source: UniProtKB
  6. macromolecular complex Source: RGD
  7. mitochondrial outer membrane Source: UniProtKB-KW
  8. nucleus Source: RGD
  9. PML body Source: Ensembl
  10. TORC1 complex Source: RGD
  11. TORC2 complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25492549Serine/threonine-protein kinase mTORPRO_0000088810Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei567 – 5671PhosphoserineBy similarity
Modified residuei1162 – 11621PhosphothreonineBy similarity
Modified residuei1218 – 12181N6-acetyllysineBy similarity
Modified residuei1261 – 12611PhosphoserineBy similarity
Modified residuei2159 – 21591PhosphoserineBy similarity
Modified residuei2164 – 21641Phosphothreonine1 Publication
Modified residuei2173 – 21731Phosphothreonine; by PKB/AKT1By similarity
Modified residuei2446 – 24461Phosphothreonine; by RPS6KB1By similarity
Modified residuei2448 – 24481Phosphoserine; by RPS6KB1By similarity
Modified residuei2478 – 24781PhosphoserineBy similarity
Modified residuei2481 – 24811Phosphoserine; by autocatalysisBy similarity

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

PhosphoSiteiP42346.

Expressioni

Gene expression databases

GenevestigatoriP42346.

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 PPAPDC3 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 (By similarity).By similarity

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP42346.
SMRiP42346. Positions 2015-2114, 2517-2549.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati16 – 5338HEAT 1Add
BLAST
Repeati55 – 9945HEAT 2Add
BLAST
Repeati100 – 13738HEAT 3Add
BLAST
Repeati138 – 17942HEAT 4Add
BLAST
Repeati180 – 22041HEAT 5Add
BLAST
Repeati222 – 27655HEAT 6Add
BLAST
Repeati277 – 31337HEAT 7Add
BLAST
Repeati314 – 36451HEAT 8Add
BLAST
Repeati365 – 40945HEAT 9Add
BLAST
Repeati410 – 44536HEAT 10Add
BLAST
Repeati446 – 49449HEAT 11Add
BLAST
Repeati495 – 52935HEAT 12Add
BLAST
Repeati530 – 56334HEAT 13Add
BLAST
Repeati564 – 59633HEAT 14Add
BLAST
Repeati597 – 63640HEAT 15Add
BLAST
Repeati637 – 68347HEAT 16Add
BLAST
Repeati686 – 72439HEAT 17Add
BLAST
Repeati727 – 76640HEAT 18Add
BLAST
Repeati769 – 81143HEAT 19Add
BLAST
Repeati814 – 85340HEAT 20Add
BLAST
Repeati857 – 89337HEAT 21Add
BLAST
Repeati894 – 94249HEAT 22Add
BLAST
Repeati943 – 98846HEAT 23Add
BLAST
Repeati989 – 102739HEAT 24Add
BLAST
Repeati1029 – 106840HEAT 25Add
BLAST
Repeati1069 – 110537HEAT 26Add
BLAST
Repeati1106 – 114439HEAT 27Add
BLAST
Repeati1145 – 118844HEAT 28Add
BLAST
Repeati1189 – 122537HEAT 29Add
BLAST
Repeati1226 – 127348HEAT 30Add
BLAST
Repeati1274 – 131138HEAT 31Add
BLAST
Repeati1312 – 134534HEAT 32Add
BLAST
Repeati1346 – 138237TPR 1Add
BLAST
Domaini1382 – 1982601FATPROSITE-ProRule annotationAdd
BLAST
Repeati1383 – 140826TPR 2Add
BLAST
Repeati1409 – 144234TPR 3Add
BLAST
Repeati1443 – 147331TPR 4Add
BLAST
Repeati1474 – 150734TPR 5Add
BLAST
Repeati1508 – 154134TPR 6Add
BLAST
Repeati1542 – 157433TPR 7Add
BLAST
Repeati1575 – 161440TPR 8Add
BLAST
Repeati1615 – 164935TPR 9Add
BLAST
Repeati1650 – 169344TPR 10Add
BLAST
Repeati1694 – 173138TPR 11Add
BLAST
Repeati1732 – 178655TPR 12Add
BLAST
Repeati1787 – 184660TPR 13Add
BLAST
Repeati1898 – 193033TPR 14Add
BLAST
Repeati1931 – 197040TPR 15Add
BLAST
Repeati1971 – 200535TPR 16Add
BLAST
Domaini2182 – 2516335PI3K/PI4KPROSITE-ProRule annotationAdd
BLAST
Domaini2517 – 254933FATCPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 651651Interaction with NBNBy similarityAdd
BLAST
Regioni2012 – 2144133Sufficient for interaction with the FKBP1A/rapamycin complexBy similarityAdd
BLAST
Regioni2258 – 229639Interaction with MLST8By similarityAdd
BLAST

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

eggNOGiCOG5032.
GeneTreeiENSGT00760000119382.
HOVERGENiHBG005744.
InParanoidiP42346.
KOiK07203.
OMAiTYKQNIG.
OrthoDBiEOG7CCBQ4.
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.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR009076. Rapamycin-bd_dom.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF11865. DUF3385. 1 hit.
PF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF08771. Rapamycin_bind. 1 hit.
[Graphical view]
SMARTiSM00146. 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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.
SMRi P42346. Positions 2015-2114, 2517-2549.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 248568. 4 interactions.
DIPi DIP-261N.
IntActi P42346. 3 interactions.
MINTi MINT-87926.
STRINGi 10116.ENSRNOP00000014167.

Chemistry

BindingDBi P42346.
ChEMBLi CHEMBL1075134.

PTM databases

PhosphoSitei P42346.

Proteomic databases

PaxDbi P42346.
PRIDEi P42346.

Protocols and materials databases

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 COG5032.
GeneTreei ENSGT00760000119382.
HOVERGENi HBG005744.
InParanoidi P42346.
KOi K07203.
OMAi TYKQNIG.
OrthoDBi EOG7CCBQ4.
PhylomeDBi P42346.
TreeFami TF105134.

Enzyme and pathway databases

Reactomei REACT_198729. Constitutive PI3K/AKT Signaling in Cancer.
REACT_216105. HSF1-dependent transactivation.

Miscellaneous databases

NextBioi 611130.
PROi P42346.

Gene expression databases

Genevestigatori P42346.

Family and domain databases

Gene3Di 1.10.1070.11. 3 hits.
1.20.120.150. 1 hit.
1.25.10.10. 4 hits.
1.25.40.10. 2 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024585. DUF3385_TOR.
IPR003152. FATC.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR009076. Rapamycin-bd_dom.
IPR011990. TPR-like_helical_dom.
[Graphical view ]
Pfami PF11865. DUF3385. 1 hit.
PF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF08771. Rapamycin_bind. 1 hit.
[Graphical view ]
SMARTi SM00146. PI3Kc. 1 hit.
[Graphical view ]
SUPFAMi SSF47212. SSF47212. 1 hit.
SSF48371. SSF48371. 5 hits.
SSF56112. SSF56112. 2 hits.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Isolation of a protein target of the FKBP12-rapamycin complex in mammalian cells."
    Sabers C.J., Martin M.M., Brunn G.J., Williams J.M., Dumont F.J., Wiederrecht G., Abraham R.T.
    J. Biol. Chem. 270:815-822(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "RAFT1: a mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs."
    Sabatini D.M., Erdjument-Bromage H., Lui M., Tempst P., Snyder S.H.
    Cell 78:35-43(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. Lubec G., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 215-226 AND 533-541, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  4. "RAFT1 phosphorylation of the translational regulators p70 S6 kinase and 4E-BP1."
    Burnett P.E., Barrow R.K., Cohen N.A., Snyder S.H., Sabatini D.M.
    Proc. Natl. Acad. Sci. U.S.A. 95:1432-1437(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF RPS6KB1 AND EIF4EBP1.
  5. "mTOR kinase domain phosphorylation promotes mTORC1 signaling, cell growth, and cell cycle progression."
    Ekim B., Magnuson B., Acosta-Jaquez H.A., Keller J.A., Feener E.P., Fingar D.C.
    Mol. Cell. Biol. 31:2787-2801(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-2164.

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: October 29, 2014
This is version 130 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

External Data

Dasty 3