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P42346

- MTOR_RAT

UniProt

P42346 - MTOR_RAT

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
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    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 binding Source: IntAct
    4. protein domain specific binding Source: RGD
    5. protein serine/threonine kinase activity Source: RGD
    6. ribosome binding Source: Ensembl
    7. RNA polymerase III type 1 promoter DNA binding Source: Ensembl
    8. RNA polymerase III type 2 promoter DNA binding Source: Ensembl
    9. 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. G1/S transition of mitotic cell cycle Source: RGD
    5. germ cell development Source: Ensembl
    6. negative regulation of autophagy Source: UniProtKB
    7. negative regulation of cell size Source: MGI
    8. negative regulation of macroautophagy Source: Ensembl
    9. negative regulation of NFAT protein import into nucleus Source: Ensembl
    10. peptidyl-serine phosphorylation Source: Ensembl
    11. peptidyl-threonine phosphorylation Source: Ensembl
    12. positive regulation of actin filament polymerization Source: Ensembl
    13. positive regulation of endothelial cell proliferation Source: RGD
    14. positive regulation of lamellipodium assembly Source: Ensembl
    15. positive regulation of lipid biosynthetic process Source: UniProtKB
    16. positive regulation of myotube differentiation Source: Ensembl
    17. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
    18. positive regulation of protein kinase B signaling Source: RGD
    19. positive regulation of stress fiber assembly Source: Ensembl
    20. positive regulation of transcription from RNA polymerase III promoter Source: Ensembl
    21. positive regulation of translation Source: RGD
    22. protein autophosphorylation Source: RGD
    23. protein phosphorylation Source: RGD
    24. regulation of carbohydrate metabolic process Source: RGD
    25. regulation of carbohydrate utilization Source: RGD
    26. regulation of fatty acid beta-oxidation Source: RGD
    27. regulation of glycogen biosynthetic process Source: RGD
    28. regulation of protein kinase activity Source: Ensembl
    29. regulation of Rac GTPase activity Source: Ensembl
    30. regulation of response to food Source: RGD
    31. response to amino acid Source: Ensembl
    32. response to insulin Source: Ensembl
    33. ruffle organization Source: Ensembl
    34. TOR signaling Source: Ensembl

    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 membrane Source: UniProtKB-SubCell
    3. Golgi membrane Source: UniProtKB-SubCell
    4. lysosomal membrane Source: Ensembl
    5. lysosome Source: UniProtKB
    6. mitochondrial outer membrane Source: UniProtKB-SubCell
    7. nucleus Source: RGD
    8. PML body Source: UniProtKB-SubCell
    9. TORC1 complex Source: RGD
    10. TORC2 complex Source: Ensembl

    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.
    GeneTreeiENSGT00720000108744.
    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.
    [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

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    MLGTGPATAT AGAATSSNVS VLQQFASGLK SRNEETRAKA AKELQHYVTM     50
    ELREMSQEES TRFYDQLNHH IFELVSSSDA NERKGGILAI ASLIGVEGGN 100
    STRIGRFANY LRNLLPSSDP VVMEMASKAI GRLAMAGDTF TAEYVEFEVK 150
    RALEWLGADR NEGRRHAAVL VLRELAISVP TFFFQQVQPF FDNIFVAVWD 200
    PKQAIREGAV AALRACLILT TQREPKEMQK PQWYRHTFEE AEKGFDETLA 250
    KEKGMNRDDR IHGALLILNE LVRISSMEGE RLREEMEEIT QQQLVHDKYC 300
    KDLMGFGTKP RHITPFTSFQ AVQPQQSNAL VGLLGYSSHQ GLMGFGASPS 350
    PTKSTLVESR CCRDLMEEKF DQVCQWVLKC RSSKNSLIQM TILNLLPRLA 400
    AFRPSAFTDT QYLQDTMNHV LSCVKKEKER TAAFQALGLL SVAVRSEFKV 450
    YLPRVLDIIR AALPPKDFAH KRQKTVQVDA TVFTCISMLA RAMGPGIQQD 500
    IKELLEPMLA VGLSPALTAV LYDLSRQIPQ LKKDIQDGLL KMLSLVLMHK 550
    PLRHPGMPKG LAHQLASPGL TTLPEASDVA SITLALRTLG SFEFEGHSLT 600
    QFVRHCADHF LNSEHKEIRM EAARTCSRLL TPSIHLISGH AHVVSQTAVQ 650
    VVADVLSKLL VVGITDPDPD IRYCVLASLD ERFDAHLAQA ENLQALFVAL 700
    NDQVFEIREL AICTVGRLSS MNPAFVMPFL RKMLIQILTE LEHSGIGRIK 750
    EQSARMLGHL VSNAPRLIRP YMEPILKALI LKLKDPDPDP NPGVINNVLA 800
    TIGELAQVSG LEMRKWVDEL FVIIMDMLQD SSLLAKRQVA LWTLGQLVAS 850
    TGYVVEPYRK YPTLLEVLLN FLKTEQNQGT RREAIRVLGL LGALDPYKHK 900
    VNIGMIDQSR DASAVSLSES KSSQDSSDYS TSEMLVNMGN LPLDEFYPAV 950
    SMVALMRIFR DQSLSHHHTM VVQAITFIFK SLGLKCVQFL PQVMPTFLNV 1000
    IRVCDGAIRE FLFQQLGMLV SFVKSHIRPY MDEIVTLMRE FWVMNTSIQS 1050
    TIILLIEQIV VALGGEFKLY LPQLIPHMLR VFMHDNSQGR IVSIKLLAAI 1100
    QLFGANLDDY LHLLLPPIVK LFDAPEVPLP SRKAALETVD RLTESLDFTD 1150
    YASRIIHPIV RTLDQSPELR STAMDTLSSL VFQLGKKYQI FIPMVNKVLV 1200
    RHRINHQRYD VLICRIVKGY TLADEEEDPL IYQHRMLRSS QGDALASGPV 1250
    ETGPMKKLHV STINLQKAWG AARRVSKDDW LEWLRRLSLE LLKDSSSPSL 1300
    RSCWALAQAY NPMARDLFNA AFVSCWSELN EDQQDELIRS IELALTSQDI 1350
    AEVTQTLLNL AEFMEHSDKG PLPLRDDNGI VLLGERAAKC RAYAKALHYK 1400
    ELEFQKGPTP AILESLISIN NKLQQPEAAS GVLEYAMKHF GELEIQATWY 1450
    EKLHEWEDAL VAYDKKMDTN KDDPELMLGR MRCLEALGEW GQLHQQCCEK 1500
    WTLVNDETQA KMARMAAAAA WGLGQWDSME EYTCMIPRDT HDGAFYRAVL 1550
    ALHQDLFSLA QQCIDKARDL LDAELTAMAG ESYSRAYGAM VSCHMLSELE 1600
    EVIQYKLVPE RREIIRQIWW ERLQGCQRIV EDWQKILMVR SLVVSPHEDM 1650
    RTWLKYASLC GKSGRLALAH KTLVLLLGVD PSRQLDHPLP TVHPQVTYAY 1700
    MKNMWKSARK IDAFQHMQHF VQTMQQQAQH AIATEDQQHK QELHKLMARC 1750
    FLKLGEWQLN LQGINESTIP KVLQYYSAAT EHDRSWYKAW HAWAVMNFEA 1800
    VLHYKHQNQA RDEKKKLRHA SGANITNATT TATTAASAAA ATSTEGSNSE 1850
    SEAESNESSP TPSPLQKKVT EDLSKTLLLY TVPAVQGFFR SISLSRGNNL 1900
    QDTLRVLTLW FDYGHWPDVN EALVEGVKAI QIDTWLQVIP QLIARIDTPR 1950
    PLVGRLIHQL LTDIGRYHPQ ALIYPLTVAS KSTTTARHNA ANKILKNMCE 2000
    HSNTLVQQAM MVSEELIRVA ILWHEMWHEG LEEASRLYFG ERNVKGMFEV 2050
    LEPLHAMMER GPQTLKETSF NQAYGRDLME AQEWCRKYMK SGNVKDLTQA 2100
    WDLYYHVFRR ISKQLPQLTS LELQYVSPKL LMCRDLELAV PGTYDPNQPI 2150
    IRIQSIAPSL QVITSKQRPR KLTLMGSNGH EFVFLLKGHE DLRQDERVMQ 2200
    LFGLVNTLLA NDPTSLRKNL SIQRYAVIPL STNSGLIGWV PHCDTLHALI 2250
    RDYREKKKIL LNIEHRIMLR MAPDYDHLTL MQKVEVFEHA VNNTAGDDLA 2300
    KLLWLKSPSS EVWFDRRTNY TRSLAVMSMV GYILGLGDRH PSNLMLDRLS 2350
    GKILHIDFGD CFEVAMTREK FPEKIPFRLT RMLTNAMEVT GLDGNYRTTC 2400
    HTVMEVLREH KDSVMAVLEA FVYDPLLNWR LMDTNAKGNK RSRTRTDSYS 2450
    AGQSVEILDG VELGEPAHKK TGTTVPESIH SFIGDGLVKP EALNKKAIQI 2500
    INRVRDKLTG RDFSHDDTLD VPTQVELLIK QATSHENLCQ CYIGWCPFW 2549
    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 ENSGT00720000108744.
    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.
    [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 1, 2014
    This is version 129 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