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Q9JLN9

- MTOR_MOUSE

UniProt

Q9JLN9 - MTOR_MOUSE

Protein

Serine/threonine-protein kinase mTOR

Gene

Mtor

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (15 Jun 2010)
      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-422'.9 Publications

    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.2 Publications

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_213550. HSF1-dependent transactivation.
    REACT_226151. CD28 dependent PI3K/Akt signaling.
    REACT_226341. PIP3 activates AKT signaling.

    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:Frap, Frap1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1928394. 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; Peripheral membrane protein; Cytoplasmic side. Lysosome By similarity. Cytoplasm. NucleusPML body
    Note: Shuttles between cytoplasm and nucleus. Accumulates in the nucleus in response to hypoxia. Targeting to lysosomes depends on amino acid availability and RRAGA and RRAGB By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    4. Golgi membrane Source: UniProtKB-SubCell
    5. lysosomal membrane Source: Ensembl
    6. lysosome Source: UniProtKB
    7. mitochondrial outer membrane Source: UniProtKB-SubCell
    8. nucleus Source: MGI
    9. PML body Source: UniProtKB-SubCell
    10. TORC1 complex Source: MGI
    11. TORC2 complex Source: MGI

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2035 – 20351S → R: Abolishes interaction with the FKBP1A-rapamycin complex. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 25492549Serine/threonine-protein kinase mTORPRO_0000088809Add
    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 – 12611Phosphoserine2 Publications
    Modified residuei2159 – 21591PhosphoserineBy similarity
    Modified residuei2164 – 21641PhosphothreonineBy similarity
    Modified residuei2173 – 21731Phosphothreonine; by PKB/AKT1By similarity
    Modified residuei2446 – 24461Phosphothreonine; by RPS6KB1By similarity
    Modified residuei2448 – 24481Phosphoserine; by RPS6KB1By similarity
    Modified residuei2478 – 24781Phosphoserine2 Publications
    Modified residuei2481 – 24811Phosphoserine; alternate2 Publications
    Modified residuei2481 – 24811Phosphoserine; by autocatalysis; alternateBy similarity

    Post-translational modificationi

    Phosphorylation at Thr-2173 in the ATP-binding region by AKT1 strongly reduces kinase activity By similarity. 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.By similarity3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9JLN9.
    PaxDbiQ9JLN9.
    PRIDEiQ9JLN9.

    PTM databases

    PhosphoSiteiQ9JLN9.

    Expressioni

    Gene expression databases

    BgeeiQ9JLN9.
    GenevestigatoriQ9JLN9.

    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.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Eif3fQ9DCH45EBI-1571628,EBI-1634316
    EIF4EBP1Q135412EBI-1571628,EBI-74090From a different organism.
    RictorQ6QI068EBI-1571628,EBI-4286572
    RPTORQ8N1225EBI-1571628,EBI-1567928From a different organism.
    RptorQ8K4Q06EBI-1571628,EBI-4567273

    Protein-protein interaction databases

    BioGridi208142. 13 interactions.
    DIPiDIP-40570N.
    IntActiQ9JLN9. 20 interactions.
    MINTiMINT-1899010.
    STRINGi10090.ENSMUSP00000099510.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JLN9.
    SMRiQ9JLN9. Positions 32-74, 187-215, 1009-1042, 1446-1498, 2025-2422, 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 complexAdd
    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.
    HOGENOMiHOG000163215.
    HOVERGENiHBG005744.
    InParanoidiQ2KHT0.
    KOiK07203.
    OMAiTYKQNIG.
    OrthoDBiEOG7CCBQ4.
    PhylomeDBiQ9JLN9.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9JLN9-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLGTGPAVAT ASAATSSNVS 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 AVQPQQPNAL VGLLGYSSPQ GLMGFGTSPS 350
    PAKSTLVESR 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 FIIIMDMLQD 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 KEDPELMLGR 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 TAHPQVTYAY 1700
    MKNMWKSARK IDAFQHMQHF VQTMQQQAQH AIATEDQQHK QELHKLMARC 1750
    FLKLGEWQLN LQGINESTIP KVLQYYSAAT EHDRSWYKAW HAWAVMNFEA 1800
    VLHYKHQNQA RDEKKKLRHA SGANITNATT AATTAASAAA ATSTEGSNSE 1850
    SEAESNENSP 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 LMDTNTKGNK RSRTRTDSYS 2450
    AGQSVEILDG VELGEPAHKK AGTTVPESIH SFIGDGLVKP EALNKKAIQI 2500
    INRVRDKLTG RDFSHDDTLD VPTQVELLIK QATSHENLCQ CYIGWCPFW 2549
    Length:2,549
    Mass (Da):288,789
    Last modified:June 15, 2010 - v2
    Checksum:i56302E5171FB6DBD
    GO
    Isoform 2 (identifier: Q9JLN9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         236-256: HTFEEAEKGFDETLAKEKGMN → VRDGSTQPLAKHFGLESCSWP
         257-2549: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:256
    Mass (Da):28,467
    Checksum:iF58320768DC9E928
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti33 – 331N → K in AAH43920. (PubMed:15489334)Curated
    Sequence conflicti628 – 6281R → C in AAF73196. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei236 – 25621HTFEE…EKGMN → VRDGSTQPLAKHFGLESCSW P in isoform 2. 1 PublicationVSP_011909Add
    BLAST
    Alternative sequencei257 – 25492293Missing in isoform 2. 1 PublicationVSP_011910Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF152838 mRNA. Translation: AAF73196.1.
    AL731654, AL713995 Genomic DNA. Translation: CAM22525.1.
    AL713995, AL731654 Genomic DNA. Translation: CAM23943.1.
    CU210865 Genomic DNA. Translation: CAQ51622.1.
    BC043920 mRNA. Translation: AAH43920.1.
    BC112904 mRNA. Translation: AAI12905.1.
    AK012031 mRNA. Translation: BAB27985.2.
    CCDSiCCDS18937.1. [Q9JLN9-1]
    RefSeqiNP_064393.2. NM_020009.2. [Q9JLN9-1]
    UniGeneiMm.21158.

    Genome annotation databases

    EnsembliENSMUST00000057580; ENSMUSP00000054164; ENSMUSG00000028991. [Q9JLN9-2]
    ENSMUST00000103221; ENSMUSP00000099510; ENSMUSG00000028991. [Q9JLN9-1]
    GeneIDi56717.
    KEGGimmu:56717.
    UCSCiuc008vur.2. mouse. [Q9JLN9-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF152838 mRNA. Translation: AAF73196.1 .
    AL731654 , AL713995 Genomic DNA. Translation: CAM22525.1 .
    AL713995 , AL731654 Genomic DNA. Translation: CAM23943.1 .
    CU210865 Genomic DNA. Translation: CAQ51622.1 .
    BC043920 mRNA. Translation: AAH43920.1 .
    BC112904 mRNA. Translation: AAI12905.1 .
    AK012031 mRNA. Translation: BAB27985.2 .
    CCDSi CCDS18937.1. [Q9JLN9-1 ]
    RefSeqi NP_064393.2. NM_020009.2. [Q9JLN9-1 ]
    UniGenei Mm.21158.

    3D structure databases

    ProteinModelPortali Q9JLN9.
    SMRi Q9JLN9. Positions 32-74, 187-215, 1009-1042, 1446-1498, 2025-2422, 2517-2549.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 208142. 13 interactions.
    DIPi DIP-40570N.
    IntActi Q9JLN9. 20 interactions.
    MINTi MINT-1899010.
    STRINGi 10090.ENSMUSP00000099510.

    Chemistry

    BindingDBi Q9JLN9.
    ChEMBLi CHEMBL1255165.

    PTM databases

    PhosphoSitei Q9JLN9.

    Proteomic databases

    MaxQBi Q9JLN9.
    PaxDbi Q9JLN9.
    PRIDEi Q9JLN9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000057580 ; ENSMUSP00000054164 ; ENSMUSG00000028991 . [Q9JLN9-2 ]
    ENSMUST00000103221 ; ENSMUSP00000099510 ; ENSMUSG00000028991 . [Q9JLN9-1 ]
    GeneIDi 56717.
    KEGGi mmu:56717.
    UCSCi uc008vur.2. mouse. [Q9JLN9-1 ]

    Organism-specific databases

    CTDi 2475.
    MGIi MGI:1928394. Mtor.

    Phylogenomic databases

    eggNOGi COG5032.
    GeneTreei ENSGT00720000108744.
    HOGENOMi HOG000163215.
    HOVERGENi HBG005744.
    InParanoidi Q2KHT0.
    KOi K07203.
    OMAi TYKQNIG.
    OrthoDBi EOG7CCBQ4.
    PhylomeDBi Q9JLN9.
    TreeFami TF105134.

    Enzyme and pathway databases

    Reactomei REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_213550. HSF1-dependent transactivation.
    REACT_226151. CD28 dependent PI3K/Akt signaling.
    REACT_226341. PIP3 activates AKT signaling.

    Miscellaneous databases

    ChiTaRSi MTOR. mouse.
    NextBioi 313190.
    PROi Q9JLN9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9JLN9.
    Genevestigatori Q9JLN9.

    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. "Positional cloning of mouse plasmacytoma susceptibility gene."
      Bliskovsky V., Mock B.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: BALB/c.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6 and FVB/N.
      Tissue: Kidney and Retina.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1155-1334.
      Strain: C57BL/6J.
      Tissue: Embryo.
    5. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1287-1293, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    6. "RAPT1, a mammalian homolog of yeast Tor, interacts with the FKBP12/rapamycin complex."
      Chiu M.I., Katz H., Berlin V.
      Proc. Natl. Acad. Sci. U.S.A. 91:12574-12578(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1987-2146, INTERACTION WITH THE FKBP1A-RAPAMYCIN COMPLEX, MUTAGENESIS OF SER-2035, TISSUE SPECIFICITY.
      Tissue: Embryo.
    7. "Insulin-stimulated phosphorylation of lipin mediated by the mammalian target of rapamycin."
      Huffman T.A., Mothe-Satney I., Lawrence J.C. Jr.
      Proc. Natl. Acad. Sci. U.S.A. 99:1047-1052(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF LPIN1.
    8. "FKBP12-rapamycin-associated protein associates with mitochondria and senses osmotic stress via mitochondrial dysfunction."
      Desai B.N., Myers B.R., Schreiber S.L.
      Proc. Natl. Acad. Sci. U.S.A. 99:4319-4324(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/TSC2 tumor suppressor complex."
      Brugarolas J., Lei K., Hurley R.L., Manning B.D., Reiling J.H., Hafen E., Witters L.A., Ellisen L.W., Kaelin W.G. Jr.
      Genes Dev. 18:2893-2904(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, FUNCTION IN RESPONSE TO HYPOXIA.
    10. "Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive."
      Jacinto E., Loewith R., Schmidt A., Lin S., Ruegg M.A., Hall A., Hall M.N.
      Nat. Cell Biol. 6:1122-1128(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN MTORC2 COMPLEX.
    11. "mTOR.RICTOR is the Ser473 kinase for Akt/protein kinase B in 3T3-L1 adipocytes."
      Hresko R.C., Mueckler M.
      J. Biol. Chem. 280:40406-40416(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity."
      Jacinto E., Facchinetti V., Liu D., Soto N., Wei S., Jung S.Y., Huang Q., Qin J., Su B.
      Cell 127:125-137(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN MTORC2 COMPLEX.
    13. "PML inhibits HIF-1alpha translation and neoangiogenesis through repression of mTOR."
      Bernardi R., Guernah I., Jin D., Grisendi S., Alimonti A., Teruya-Feldstein J., Cordon-Cardo C., Simon M.C., Rafii S., Pandolfi P.P.
      Nature 442:779-785(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PML.
    14. "mTOR controls mitochondrial oxidative function through a YY1-PGC-1alpha transcriptional complex."
      Cunningham J.T., Rodgers J.T., Arlow D.H., Vazquez F., Mootha V.K., Puigserver P.
      Nature 450:736-740(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MITOCHONDRIAL BIOGENESIS.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2478 AND SER-2481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    16. "Mammalian target of rapamycin complex 1 (mTORC1) activity is associated with phosphorylation of raptor by mTOR."
      Wang L., Lawrence J.C. Jr., Sturgill T.W., Harris T.E.
      J. Biol. Chem. 284:14693-14697(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION OF RPTOR.
    17. "Site-specific mTOR phosphorylation promotes mTORC1-mediated signaling and cell growth."
      Acosta-Jaquez H.A., Keller J.A., Foster K.G., Ekim B., Soliman G.A., Feener E.P., Ballif B.A., Fingar D.C.
      Mol. Cell. Biol. 29:4308-4324(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-1261, ENZYME REGULATION.
    18. "Regulation of myoblast differentiation by the nuclear envelope protein NET39."
      Liu G.H., Guan T., Datta K., Coppinger J., Yates J. III, Gerace L.
      Mol. Cell. Biol. 29:5800-5812(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPAPDC3.
    19. "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexes."
      Takai H., Xie Y., de Lange T., Pavletich N.P.
      Genes Dev. 24:2019-2030(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MLST8; PRR5 AND RPTOR.
    20. "AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1."
      Kim J., Kundu M., Viollet B., Guan K.L.
      Nat. Cell Biol. 13:132-141(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN AUTOPHAGY, FUNCTION IN PHOSPHORYLATION OF ULK1.
    21. "The mTOR-regulated phosphoproteome reveals a mechanism of mTORC1-mediated inhibition of growth factor signaling."
      Hsu P.P., Kang S.A., Rameseder J., Zhang Y., Ottina K.A., Lim D., Peterson T.R., Choi Y., Gray N.S., Yaffe M.B., Marto J.A., Sabatini D.M.
      Science 332:1317-1322(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF GRB10.

    Entry informationi

    Entry nameiMTOR_MOUSE
    AccessioniPrimary (citable) accession number: Q9JLN9
    Secondary accession number(s): Q2KHT0, Q811J5, Q9CST1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: June 15, 2010
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3