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Q9JLN9

- MTOR_MOUSE

UniProt

Q9JLN9 - MTOR_MOUSE

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Protein

Serine/threonine-protein kinase mTOR

Gene
Mtor, Frap, Frap1
Organism
Mus musculus (Mouse)
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-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
Complete GO annotation...

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; Peripheral membrane protein; Cytoplasmic side By similarity. Golgi apparatus membrane; Peripheral membrane protein; 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.2 Publications

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. mTOR-FKBP12-rapamycin complex Source: Ensembl
  9. nucleus Source: MGI
  10. PML body Source: UniProtKB-SubCell
  11. TORC1 complex Source: MGI
  12. TORC2 complex Source: MGI
Complete GO annotation...

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-acetylmethionine By similarity
Modified residuei567 – 5671Phosphoserine By similarity
Modified residuei1162 – 11621Phosphothreonine By similarity
Modified residuei1218 – 12181N6-acetyllysine By similarity
Modified residuei1261 – 12611Phosphoserine1 Publication
Modified residuei2159 – 21591Phosphoserine By similarity
Modified residuei2164 – 21641Phosphothreonine By similarity
Modified residuei2446 – 24461Phosphothreonine; by RPS6KB1 By similarity
Modified residuei2448 – 24481Phosphoserine; by RPS6KB1 By similarity
Modified residuei2478 – 24781Phosphoserine1 Publication
Modified residuei2481 – 24811Phosphoserine; alternate1 Publication
Modified residuei2481 – 24811Phosphoserine; by autocatalysis; alternate By 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.

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.

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 – 1982601FATAdd
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/PI4KAdd
BLAST
Domaini2517 – 254933FATCAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 651651Interaction with NBN By similarityAdd
BLAST
Regioni2012 – 2144133Sufficient for interaction with the FKBP1A/rapamycin complexAdd
BLAST
Regioni2258 – 229639Interaction with MLST8 By 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.

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family.
Contains 1 FAT domain.
Contains 1 FATC domain.
Contains 32 HEAT repeats.
Contains 1 PI3K/PI4K domain.
Contains 16 TPR repeats.

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.

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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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei236 – 25621HTFEE…EKGMN → VRDGSTQPLAKHFGLESCSW P in isoform 2. VSP_011909Add
BLAST
Alternative sequencei257 – 25492293Missing in isoform 2. VSP_011910Add
BLAST

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 126 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

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