Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9JLN9 (MTOR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·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:Frap, Frap1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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-422'. Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.20 Ref.21

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. Ref.9 Ref.17

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. Ref.6 Ref.10 Ref.12 Ref.13 Ref.18 Ref.19

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. 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. Ref.8 Ref.13

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.

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
   Coding sequence diversityAlternative splicing
   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_processTOR signaling

Inferred from electronic annotation. Source: Ensembl

cell projection organization

Inferred from mutant phenotype PubMed 16286931. Source: MGI

cellular response to hypoxia

Inferred from direct assay Ref.13. Source: UniProtKB

cellular response to nutrient levels

Inferred from direct assay Ref.20. Source: UniProtKB

germ cell development

Inferred from direct assay PubMed 12140361. Source: MGI

negative regulation of NFAT protein import into nucleus

Inferred from mutant phenotype PubMed 18347059. Source: MGI

negative regulation of autophagy

Inferred from mutant phenotype Ref.20. Source: UniProtKB

negative regulation of cell size

Inferred from genetic interaction PubMed 15185396PubMed 16286931. Source: MGI

negative regulation of macroautophagy

Inferred from mutant phenotype PubMed 16714284. Source: MGI

peptidyl-serine phosphorylation

Inferred from mutant phenotype PubMed 18347059. Source: MGI

peptidyl-threonine phosphorylation

Inferred from direct assay PubMed 11707573. Source: MGI

positive regulation of actin filament polymerization

Inferred from direct assay Ref.10. Source: MGI

positive regulation of endothelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of lamellipodium assembly

Inferred from direct assay Ref.10. Source: MGI

positive regulation of lipid biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of myotube differentiation

Inferred from genetic interaction Ref.18. Source: MGI

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype Ref.10. Source: MGI

positive regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of stress fiber assembly

Inferred from direct assay Ref.10. Source: MGI

positive regulation of transcription from RNA polymerase III promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of translation

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from sequence orthology Ref.10. Source: MGI

protein phosphorylation

Inferred from sequence orthology Ref.10. Source: MGI

regulation of Rac GTPase activity

Inferred from mutant phenotype Ref.10. Source: MGI

regulation of carbohydrate utilization

Inferred from electronic annotation. Source: Ensembl

regulation of fatty acid beta-oxidation

Inferred from electronic annotation. Source: Ensembl

regulation of glycogen biosynthetic process

Inferred from electronic annotation. Source: Ensembl

regulation of protein kinase activity

Inferred from genetic interaction PubMed 15185396. Source: MGI

regulation of response to food

Inferred from electronic annotation. Source: Ensembl

response to amino acid

Inferred from direct assay Ref.10. Source: MGI

response to insulin

Inferred from direct assay Ref.10. Source: MGI

ruffle organization

Inferred from direct assay Ref.10. Source: MGI

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

PML body

Inferred from electronic annotation. Source: UniProtKB-SubCell

TORC1 complex

Inferred from sequence orthology Ref.10. Source: MGI

TORC2 complex

Inferred from sequence orthology Ref.10. Source: MGI

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from direct assay Ref.13. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

lysosome

Inferred from sequence or structural similarity. Source: UniProtKB

mTOR-FKBP12-rapamycin complex

Inferred from electronic annotation. Source: Ensembl

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 18347059PubMed 18381428. Source: MGI

   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

kinase activity

Inferred from sequence orthology Ref.10. Source: MGI

protein serine/threonine kinase activity

Inferred from direct assay Ref.20. Source: UniProtKB

ribosome binding

Inferred from direct assay PubMed 21045808. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9JLN9-1)

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.
Isoform 2 (identifier: Q9JLN9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     236-256: HTFEEAEKGFDETLAKEKGMN → VRDGSTQPLAKHFGLESCSWP
     257-2549: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25492549Serine/threonine-protein kinase mTOR
PRO_0000088809

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
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 Ref.17
Modified residue21591Phosphoserine By similarity
Modified residue21641Phosphothreonine By similarity
Modified residue24461Phosphothreonine; by RPS6KB1 By similarity
Modified residue24481Phosphoserine; by RPS6KB1 By similarity
Modified residue24781Phosphoserine Ref.15
Modified residue24811Phosphoserine; alternate Ref.15
Modified residue24811Phosphoserine; by autocatalysis; alternate By similarity

Natural variations

Alternative sequence236 – 25621HTFEE…EKGMN → VRDGSTQPLAKHFGLESCSW P in isoform 2.
VSP_011909
Alternative sequence257 – 25492293Missing in isoform 2.
VSP_011910

Experimental info

Mutagenesis20351S → R: Abolishes interaction with the FKBP1A-rapamycin complex. Ref.6
Sequence conflict331N → K in AAH43920. Ref.3
Sequence conflict6281R → C in AAF73196. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 15, 2010. Version 2.
Checksum: 56302E5171FB6DBD

FASTA2,549288,789
        10         20         30         40         50         60 
MLGTGPAVAT ASAATSSNVS 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 AVQPQQPNAL VGLLGYSSPQ GLMGFGTSPS PAKSTLVESR 

       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 FIIIMDMLQD 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 KEDPELMLGR 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 TAHPQVTYAY 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 AATTAASAAA ATSTEGSNSE SEAESNENSP 

      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 LMDTNTKGNK RSRTRTDSYS AGQSVEILDG 

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

      2530       2540 
VPTQVELLIK QATSHENLCQ CYIGWCPFW 

« Hide

Isoform 2 [UniParc].

Checksum: F58320768DC9E928
Show »

FASTA25628,467

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_064393.2. NM_020009.2.
UniGeneMm.21158.

3D structure databases

ProteinModelPortalQ9JLN9.
SMRQ9JLN9. Positions 115-217, 967-1080, 2025-2422, 2517-2549.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid208142. 13 interactions.
DIPDIP-40570N.
IntActQ9JLN9. 20 interactions.
MINTMINT-1899010.
STRING10090.ENSMUSP00000099510.

Chemistry

BindingDBQ9JLN9.
ChEMBLCHEMBL1255165.

PTM databases

PhosphoSiteQ9JLN9.

Proteomic databases

PaxDbQ9JLN9.
PRIDEQ9JLN9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000057580; ENSMUSP00000054164; ENSMUSG00000028991. [Q9JLN9-2]
ENSMUST00000103221; ENSMUSP00000099510; ENSMUSG00000028991. [Q9JLN9-1]
GeneID56717.
KEGGmmu:56717.
UCSCuc008vur.2. mouse. [Q9JLN9-1]

Organism-specific databases

CTD2475.
MGIMGI:1928394. Mtor.

Phylogenomic databases

eggNOGCOG5032.
GeneTreeENSGT00720000108744.
HOGENOMHOG000163215.
HOVERGENHBG005744.
InParanoidQ2KHT0.
KOK07203.
OMADPYKHKM.
OrthoDBEOG7CCBQ4.
PhylomeDBQ9JLN9.
TreeFamTF105134.

Gene expression databases

BgeeQ9JLN9.
GenevestigatorQ9JLN9.

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.
IPR026683. TOR.
IPR011990. TPR-like_helical.
[Graphical view]
PANTHERPTHR11139:SF9. PTHR11139:SF9. 1 hit.
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]
ProtoNetSearch...

Other

ChiTaRSMTOR. mouse.
NextBio313190.
PROQ9JLN9.
SOURCESearch...

Entry information

Entry nameMTOR_MOUSE
AccessionPrimary (citable) accession number: Q9JLN9
Secondary accession number(s): Q2KHT0, Q811J5, Q9CST1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: June 15, 2010
Last modified: April 16, 2014
This is version 122 of the entry and version 2 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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot