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P42346 (MTOR_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Mtor
Synonyms:Frap1, Raft1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length2549 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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'. Ref.4

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

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.

Subunit structure

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.

Subcellular location

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 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.

Domain

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.

Post-translational modification

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 similarity.

Sequence similarities

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.

Ontologies

Keywords
   Cellular componentCytoplasm
Endoplasmic reticulum
Golgi apparatus
Lysosome
Membrane
Mitochondrion
Mitochondrion outer membrane
Nucleus
   DomainRepeat
TPR repeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Traceable author statement Ref.1. Source: RGD

TOR signaling

Inferred from electronic annotation. Source: Ensembl

cell projection organization

Inferred from genetic interaction PubMed 16286931. Source: MGI

cellular response to hypoxia

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to nutrient levels

Inferred from sequence or structural similarity. Source: UniProtKB

germ cell development

Inferred from electronic annotation. Source: Ensembl

negative regulation of NFAT protein import into nucleus

Inferred from electronic annotation. Source: Ensembl

negative regulation of autophagy

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell size

Inferred from mutant phenotype PubMed 16286931. Source: MGI

negative regulation of macroautophagy

Inferred from electronic annotation. Source: Ensembl

peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

peptidyl-threonine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of actin filament polymerization

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell proliferation

Inferred from mutant phenotype PubMed 17110594. Source: RGD

positive regulation of lamellipodium assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of lipid biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of myotube differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase B signaling

Inferred from mutant phenotype PubMed 17110594. Source: RGD

positive regulation of stress fiber assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase III promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of translation

Inferred from mutant phenotype PubMed 15525761. Source: RGD

protein autophosphorylation

Inferred from mutant phenotype PubMed 15388509. Source: RGD

protein phosphorylation

Inferred from direct assay PubMed 17142137. Source: RGD

regulation of Rac GTPase activity

Inferred from electronic annotation. Source: Ensembl

regulation of carbohydrate metabolic process

Inferred from direct assay PubMed 17142137. Source: RGD

regulation of carbohydrate utilization

Inferred from direct assay PubMed 17142137. Source: RGD

regulation of fatty acid beta-oxidation

Inferred from direct assay PubMed 17142137. Source: RGD

regulation of glycogen biosynthetic process

Inferred from direct assay PubMed 17142137. Source: RGD

regulation of protein kinase activity

Inferred from electronic annotation. Source: Ensembl

regulation of response to food

Inferred from direct assay PubMed 16690869. Source: RGD

response to amino acid

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

ruffle organization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

PML body

Inferred from electronic annotation. Source: UniProtKB-SubCell

TORC1 complex

Inferred from direct assay PubMed 17110594. Source: RGD

TORC2 complex

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from direct assay PubMed 17110594. Source: RGD

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

lysosomal membrane

Inferred from electronic annotation. Source: Ensembl

lysosome

Inferred from sequence or structural similarity. Source: UniProtKB

mTOR-FKBP12-rapamycin complex

Inferred from direct assay Ref.1. Source: RGD

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 17110594. Source: RGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase III type 1 promoter DNA binding

Inferred from electronic annotation. Source: Ensembl

RNA polymerase III type 2 promoter DNA binding

Inferred from electronic annotation. Source: Ensembl

RNA polymerase III type 3 promoter DNA binding

Inferred from electronic annotation. Source: Ensembl

drug binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 19446321. Source: IntAct

protein domain specific binding

Inferred from physical interaction PubMed 11853878. Source: RGD

protein serine/threonine kinase activity

Inferred from direct assay PubMed 17142137. Source: RGD

ribosome binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DEPTORQ8TB452EBI-1571489,EBI-2359040From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25492549Serine/threonine-protein kinase mTOR
PRO_0000088810

Regions

Repeat16 – 5338HEAT 1
Repeat55 – 9945HEAT 2
Repeat100 – 13738HEAT 3
Repeat138 – 17942HEAT 4
Repeat180 – 22041HEAT 5
Repeat222 – 27655HEAT 6
Repeat277 – 31337HEAT 7
Repeat314 – 36451HEAT 8
Repeat365 – 40945HEAT 9
Repeat410 – 44536HEAT 10
Repeat446 – 49449HEAT 11
Repeat495 – 52935HEAT 12
Repeat530 – 56334HEAT 13
Repeat564 – 59633HEAT 14
Repeat597 – 63640HEAT 15
Repeat637 – 68347HEAT 16
Repeat686 – 72439HEAT 17
Repeat727 – 76640HEAT 18
Repeat769 – 81143HEAT 19
Repeat814 – 85340HEAT 20
Repeat857 – 89337HEAT 21
Repeat894 – 94249HEAT 22
Repeat943 – 98846HEAT 23
Repeat989 – 102739HEAT 24
Repeat1029 – 106840HEAT 25
Repeat1069 – 110537HEAT 26
Repeat1106 – 114439HEAT 27
Repeat1145 – 118844HEAT 28
Repeat1189 – 122537HEAT 29
Repeat1226 – 127348HEAT 30
Repeat1274 – 131138HEAT 31
Repeat1312 – 134534HEAT 32
Repeat1346 – 138237TPR 1
Domain1382 – 1982601FAT
Repeat1383 – 140826TPR 2
Repeat1409 – 144234TPR 3
Repeat1443 – 147331TPR 4
Repeat1474 – 150734TPR 5
Repeat1508 – 154134TPR 6
Repeat1542 – 157433TPR 7
Repeat1575 – 161440TPR 8
Repeat1615 – 164935TPR 9
Repeat1650 – 169344TPR 10
Repeat1694 – 173138TPR 11
Repeat1732 – 178655TPR 12
Repeat1787 – 184660TPR 13
Repeat1898 – 193033TPR 14
Repeat1931 – 197040TPR 15
Repeat1971 – 200535TPR 16
Domain2182 – 2516335PI3K/PI4K
Domain2517 – 254933FATC
Region1 – 651651Interaction with NBN By similarity
Region2012 – 2144133Sufficient for interaction with the FKBP1A/rapamycin complex By similarity
Region2258 – 229639Interaction with MLST8 By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue5671Phosphoserine By similarity
Modified residue11621Phosphothreonine By similarity
Modified residue12181N6-acetyllysine By similarity
Modified residue12611Phosphoserine By similarity
Modified residue21591Phosphoserine By similarity
Modified residue21641Phosphothreonine Ref.5
Modified residue24461Phosphothreonine; by RPS6KB1 By similarity
Modified residue24481Phosphoserine; by RPS6KB1 By similarity
Modified residue24781Phosphoserine By similarity
Modified residue24811Phosphoserine; by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
P42346 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: BE841EA7B9086F99

FASTA2,549288,794
        10         20         30         40         50         60 
MLGTGPATAT AGAATSSNVS VLQQFASGLK SRNEETRAKA AKELQHYVTM ELREMSQEES 

        70         80         90        100        110        120 
TRFYDQLNHH IFELVSSSDA NERKGGILAI ASLIGVEGGN STRIGRFANY LRNLLPSSDP 

       130        140        150        160        170        180 
VVMEMASKAI GRLAMAGDTF TAEYVEFEVK RALEWLGADR NEGRRHAAVL VLRELAISVP 

       190        200        210        220        230        240 
TFFFQQVQPF FDNIFVAVWD PKQAIREGAV AALRACLILT TQREPKEMQK PQWYRHTFEE 

       250        260        270        280        290        300 
AEKGFDETLA KEKGMNRDDR IHGALLILNE LVRISSMEGE RLREEMEEIT QQQLVHDKYC 

       310        320        330        340        350        360 
KDLMGFGTKP RHITPFTSFQ AVQPQQSNAL VGLLGYSSHQ GLMGFGASPS PTKSTLVESR 

       370        380        390        400        410        420 
CCRDLMEEKF DQVCQWVLKC RSSKNSLIQM TILNLLPRLA AFRPSAFTDT QYLQDTMNHV 

       430        440        450        460        470        480 
LSCVKKEKER TAAFQALGLL SVAVRSEFKV YLPRVLDIIR AALPPKDFAH KRQKTVQVDA 

       490        500        510        520        530        540 
TVFTCISMLA RAMGPGIQQD IKELLEPMLA VGLSPALTAV LYDLSRQIPQ LKKDIQDGLL 

       550        560        570        580        590        600 
KMLSLVLMHK PLRHPGMPKG LAHQLASPGL TTLPEASDVA SITLALRTLG SFEFEGHSLT 

       610        620        630        640        650        660 
QFVRHCADHF LNSEHKEIRM EAARTCSRLL TPSIHLISGH AHVVSQTAVQ VVADVLSKLL 

       670        680        690        700        710        720 
VVGITDPDPD IRYCVLASLD ERFDAHLAQA ENLQALFVAL NDQVFEIREL AICTVGRLSS 

       730        740        750        760        770        780 
MNPAFVMPFL RKMLIQILTE LEHSGIGRIK EQSARMLGHL VSNAPRLIRP YMEPILKALI 

       790        800        810        820        830        840 
LKLKDPDPDP NPGVINNVLA TIGELAQVSG LEMRKWVDEL FVIIMDMLQD SSLLAKRQVA 

       850        860        870        880        890        900 
LWTLGQLVAS TGYVVEPYRK YPTLLEVLLN FLKTEQNQGT RREAIRVLGL LGALDPYKHK 

       910        920        930        940        950        960 
VNIGMIDQSR DASAVSLSES KSSQDSSDYS TSEMLVNMGN LPLDEFYPAV SMVALMRIFR 

       970        980        990       1000       1010       1020 
DQSLSHHHTM VVQAITFIFK SLGLKCVQFL PQVMPTFLNV IRVCDGAIRE FLFQQLGMLV 

      1030       1040       1050       1060       1070       1080 
SFVKSHIRPY MDEIVTLMRE FWVMNTSIQS TIILLIEQIV VALGGEFKLY LPQLIPHMLR 

      1090       1100       1110       1120       1130       1140 
VFMHDNSQGR IVSIKLLAAI QLFGANLDDY LHLLLPPIVK LFDAPEVPLP SRKAALETVD 

      1150       1160       1170       1180       1190       1200 
RLTESLDFTD YASRIIHPIV RTLDQSPELR STAMDTLSSL VFQLGKKYQI FIPMVNKVLV 

      1210       1220       1230       1240       1250       1260 
RHRINHQRYD VLICRIVKGY TLADEEEDPL IYQHRMLRSS QGDALASGPV ETGPMKKLHV 

      1270       1280       1290       1300       1310       1320 
STINLQKAWG AARRVSKDDW LEWLRRLSLE LLKDSSSPSL RSCWALAQAY NPMARDLFNA 

      1330       1340       1350       1360       1370       1380 
AFVSCWSELN EDQQDELIRS IELALTSQDI AEVTQTLLNL AEFMEHSDKG PLPLRDDNGI 

      1390       1400       1410       1420       1430       1440 
VLLGERAAKC RAYAKALHYK ELEFQKGPTP AILESLISIN NKLQQPEAAS GVLEYAMKHF 

      1450       1460       1470       1480       1490       1500 
GELEIQATWY EKLHEWEDAL VAYDKKMDTN KDDPELMLGR MRCLEALGEW GQLHQQCCEK 

      1510       1520       1530       1540       1550       1560 
WTLVNDETQA KMARMAAAAA WGLGQWDSME EYTCMIPRDT HDGAFYRAVL ALHQDLFSLA 

      1570       1580       1590       1600       1610       1620 
QQCIDKARDL LDAELTAMAG ESYSRAYGAM VSCHMLSELE EVIQYKLVPE RREIIRQIWW 

      1630       1640       1650       1660       1670       1680 
ERLQGCQRIV EDWQKILMVR SLVVSPHEDM RTWLKYASLC GKSGRLALAH KTLVLLLGVD 

      1690       1700       1710       1720       1730       1740 
PSRQLDHPLP TVHPQVTYAY MKNMWKSARK IDAFQHMQHF VQTMQQQAQH AIATEDQQHK 

      1750       1760       1770       1780       1790       1800 
QELHKLMARC FLKLGEWQLN LQGINESTIP KVLQYYSAAT EHDRSWYKAW HAWAVMNFEA 

      1810       1820       1830       1840       1850       1860 
VLHYKHQNQA RDEKKKLRHA SGANITNATT TATTAASAAA ATSTEGSNSE SEAESNESSP 

      1870       1880       1890       1900       1910       1920 
TPSPLQKKVT EDLSKTLLLY TVPAVQGFFR SISLSRGNNL QDTLRVLTLW FDYGHWPDVN 

      1930       1940       1950       1960       1970       1980 
EALVEGVKAI QIDTWLQVIP QLIARIDTPR PLVGRLIHQL LTDIGRYHPQ ALIYPLTVAS 

      1990       2000       2010       2020       2030       2040 
KSTTTARHNA ANKILKNMCE HSNTLVQQAM MVSEELIRVA ILWHEMWHEG LEEASRLYFG 

      2050       2060       2070       2080       2090       2100 
ERNVKGMFEV LEPLHAMMER GPQTLKETSF NQAYGRDLME AQEWCRKYMK SGNVKDLTQA 

      2110       2120       2130       2140       2150       2160 
WDLYYHVFRR ISKQLPQLTS LELQYVSPKL LMCRDLELAV PGTYDPNQPI IRIQSIAPSL 

      2170       2180       2190       2200       2210       2220 
QVITSKQRPR KLTLMGSNGH EFVFLLKGHE DLRQDERVMQ LFGLVNTLLA NDPTSLRKNL 

      2230       2240       2250       2260       2270       2280 
SIQRYAVIPL STNSGLIGWV PHCDTLHALI RDYREKKKIL LNIEHRIMLR MAPDYDHLTL 

      2290       2300       2310       2320       2330       2340 
MQKVEVFEHA VNNTAGDDLA KLLWLKSPSS EVWFDRRTNY TRSLAVMSMV GYILGLGDRH 

      2350       2360       2370       2380       2390       2400 
PSNLMLDRLS GKILHIDFGD CFEVAMTREK FPEKIPFRLT RMLTNAMEVT GLDGNYRTTC 

      2410       2420       2430       2440       2450       2460 
HTVMEVLREH KDSVMAVLEA FVYDPLLNWR LMDTNAKGNK RSRTRTDSYS AGQSVEILDG 

      2470       2480       2490       2500       2510       2520 
VELGEPAHKK TGTTVPESIH SFIGDGLVKP EALNKKAIQI INRVRDKLTG RDFSHDDTLD 

      2530       2540 
VPTQVELLIK QATSHENLCQ CYIGWCPFW 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L37085 mRNA. Translation: AAA65929.1.
U11681 mRNA. Translation: AAA20091.1.
PIRA54837.
RefSeqNP_063971.1. NM_019906.1.
UniGeneRn.11008.

3D structure databases

ProteinModelPortalP42346.
SMRP42346. Positions 2015-2114, 2517-2549.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248568. 4 interactions.
DIPDIP-261N.
IntActP42346. 3 interactions.
MINTMINT-87926.
STRING10116.ENSRNOP00000014167.

Chemistry

BindingDBP42346.
ChEMBLCHEMBL1075134.

PTM databases

PhosphoSiteP42346.

Proteomic databases

PaxDbP42346.
PRIDEP42346.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000014167; ENSRNOP00000014167; ENSRNOG00000009615.
GeneID56718.
KEGGrno:56718.
UCSCRGD:68371. rat.

Organism-specific databases

CTD2475.
RGD68371. Mtor.

Phylogenomic databases

eggNOGCOG5032.
GeneTreeENSGT00720000108744.
HOVERGENHBG005744.
InParanoidP42346.
KOK07203.
OMATYKQNIG.
OrthoDBEOG7CCBQ4.
PhylomeDBP42346.
TreeFamTF105134.

Gene expression databases

GenevestigatorP42346.

Family and domain databases

Gene3D1.10.1070.11. 3 hits.
1.20.120.150. 1 hit.
1.25.10.10. 4 hits.
1.25.40.10. 2 hits.
InterProIPR011989. 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]
PfamPF11865. DUF3385. 1 hit.
PF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF08771. Rapamycin_bind. 1 hit.
[Graphical view]
SMARTSM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMSSF47212. SSF47212. 1 hit.
SSF48371. SSF48371. 5 hits.
SSF56112. SSF56112. 2 hits.
PROSITEPS51189. 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]
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Other

NextBio611130.
PROP42346.

Entry information

Entry nameMTOR_RAT
AccessionPrimary (citable) accession number: P42346
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 11, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families