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P42346

- MTOR_RAT

UniProt

P42346 - MTOR_RAT

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Protein
Serine/threonine-protein kinase mTOR
Gene
Mtor, Frap1, Raft1
Organism
Rattus norvegicus (Rat)
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-421'.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activation of mTORC1 by growth factors such as insulin involves AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase a potent activator of the protein kinase activity of mTORC1. Insulin-stimulated and amino acid-dependent phosphorylation at Ser-1261 promotes autophosphorylation and the activation of mTORC1. Activation by amino acids requires relocalization of the mTORC1 complex to lysosomes that is mediated by the Ragulator complex and the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD. On the other hand, low cellular energy levels can inhibit mTORC1 through activation of PRKAA1 while hypoxia inhibits mTORC1 through a REDD1-dependent mechanism which may also require PRKAA1. The kinase activity of MTOR within the mTORC1 complex is positively regulated by MLST8 and negatively regulated by DEPTOR and AKT1S1. MTOR phosphorylates RPTOR which in turn inhibits mTORC1. MTOR is the target of the immunosuppressive and anti-cancer drug rapamycin which acts in complex with FKBP1A/FKBP12, and specifically inhibits its kinase activity. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. It may be regulated by RHEB but in an indirect manner through the PI3K signaling pathway By similarity.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. RNA polymerase III type 1 promoter DNA binding Source: Ensembl
  3. RNA polymerase III type 2 promoter DNA binding Source: Ensembl
  4. RNA polymerase III type 3 promoter DNA binding Source: Ensembl
  5. drug binding Source: InterPro
  6. protein binding Source: IntAct
  7. protein domain specific binding Source: RGD
  8. protein serine/threonine kinase activity Source: RGD
  9. ribosome binding Source: Ensembl
Complete GO annotation...

GO - Biological processi

  1. G1/S transition of mitotic cell cycle Source: RGD
  2. TOR signaling Source: Ensembl
  3. cell projection organization Source: MGI
  4. cellular response to hypoxia Source: UniProtKB
  5. cellular response to nutrient levels Source: UniProtKB
  6. germ cell development Source: Ensembl
  7. negative regulation of NFAT protein import into nucleus Source: Ensembl
  8. negative regulation of autophagy Source: UniProtKB
  9. negative regulation of cell size Source: MGI
  10. negative regulation of macroautophagy Source: Ensembl
  11. peptidyl-serine phosphorylation Source: Ensembl
  12. peptidyl-threonine phosphorylation Source: Ensembl
  13. positive regulation of actin filament polymerization Source: Ensembl
  14. positive regulation of endothelial cell proliferation Source: RGD
  15. positive regulation of lamellipodium assembly Source: Ensembl
  16. positive regulation of lipid biosynthetic process Source: UniProtKB
  17. positive regulation of myotube differentiation Source: Ensembl
  18. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
  19. positive regulation of protein kinase B signaling Source: RGD
  20. positive regulation of stress fiber assembly Source: Ensembl
  21. positive regulation of transcription from RNA polymerase III promoter Source: Ensembl
  22. positive regulation of translation Source: RGD
  23. protein autophosphorylation Source: RGD
  24. protein phosphorylation Source: RGD
  25. regulation of Rac GTPase activity Source: Ensembl
  26. regulation of carbohydrate metabolic process Source: RGD
  27. regulation of carbohydrate utilization Source: RGD
  28. regulation of fatty acid beta-oxidation Source: RGD
  29. regulation of glycogen biosynthetic process Source: RGD
  30. regulation of protein kinase activity Source: Ensembl
  31. regulation of response to food Source: RGD
  32. response to amino acid Source: Ensembl
  33. response to insulin Source: Ensembl
  34. ruffle organization 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_198729. Constitutive PI3K/AKT Signaling in Cancer.
REACT_216105. HSF1-dependent transactivation.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase mTOR (EC:2.7.11.1)
Alternative name(s):
FK506-binding protein 12-rapamycin complex-associated protein 1
FKBP12-rapamycin complex-associated protein
Mammalian target of rapamycin
Short name:
mTOR
Mechanistic target of rapamycin
Rapamycin target protein 1
Short name:
RAPT1
Gene namesi
Name:Mtor
Synonyms:Frap1, Raft1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 5

Organism-specific databases

RGDi68371. Mtor.

Subcellular locationi

Endoplasmic reticulum membrane; 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.

GO - Cellular componenti

  1. Golgi membrane Source: UniProtKB-SubCell
  2. PML body Source: UniProtKB-SubCell
  3. TORC1 complex Source: RGD
  4. TORC2 complex Source: Ensembl
  5. cytosol Source: RGD
  6. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  7. lysosomal membrane Source: Ensembl
  8. lysosome Source: UniProtKB
  9. mTOR-FKBP12-rapamycin complex Source: RGD
  10. mitochondrial outer membrane Source: UniProtKB-SubCell
  11. nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25492549Serine/threonine-protein kinase mTOR
PRO_0000088810Add
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 – 12611Phosphoserine By similarity
Modified residuei2159 – 21591Phosphoserine By similarity
Modified residuei2164 – 21641Phosphothreonine1 Publication
Modified residuei2446 – 24461Phosphothreonine; by RPS6KB1 By similarity
Modified residuei2448 – 24481Phosphoserine; by RPS6KB1 By similarity
Modified residuei2478 – 24781Phosphoserine By similarity
Modified residuei2481 – 24811Phosphoserine; by autocatalysis 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 By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP42346.
PRIDEiP42346.

PTM databases

PhosphoSiteiP42346.

Expressioni

Gene expression databases

GenevestigatoriP42346.

Interactioni

Subunit structurei

Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR. The mTORC1 complex is a 1 Md obligate dimer of two stoichiometric heterotetramers with overall dimensions of 290 A x 210 A x 135 A. It has a rhomboid shape and a central cavity, the dimeric interfaces are formed by interlocking interactions between the two MTOR and the two RPTOR subunits. the MLST8 subunits forms distal foot-like protuberances, and contacts only one MTOR within the complex, while the small PRAS40 localizes to the midsection of the central core, in close proximity to RPTOR. Part of the mammalian target of rapamycin COmplex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR. Interacts with PPAPDC3 and PML. Interacts with PRR5 and RICTOR; the interaction is direct within the mTORC2 complex. Interacts with UBQLN1. Interacts with TTI1 and TELO2. Interacts with CLIP1; phosphorylates and regulates CLIP1. Interacts with NBN By similarity.

Binary interactionsi

WithEntry#Exp.IntActNotes
DEPTORQ8TB452EBI-1571489,EBI-2359040From a different organism.

Protein-protein interaction databases

BioGridi248568. 4 interactions.
DIPiDIP-261N.
IntActiP42346. 3 interactions.
MINTiMINT-87926.
STRINGi10116.ENSRNOP00000014167.

Structurei

3D structure databases

ProteinModelPortaliP42346.
SMRiP42346. Positions 2015-2114, 2517-2549.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati16 – 5338HEAT 1
Add
BLAST
Repeati55 – 9945HEAT 2
Add
BLAST
Repeati100 – 13738HEAT 3
Add
BLAST
Repeati138 – 17942HEAT 4
Add
BLAST
Repeati180 – 22041HEAT 5
Add
BLAST
Repeati222 – 27655HEAT 6
Add
BLAST
Repeati277 – 31337HEAT 7
Add
BLAST
Repeati314 – 36451HEAT 8
Add
BLAST
Repeati365 – 40945HEAT 9
Add
BLAST
Repeati410 – 44536HEAT 10
Add
BLAST
Repeati446 – 49449HEAT 11
Add
BLAST
Repeati495 – 52935HEAT 12
Add
BLAST
Repeati530 – 56334HEAT 13
Add
BLAST
Repeati564 – 59633HEAT 14
Add
BLAST
Repeati597 – 63640HEAT 15
Add
BLAST
Repeati637 – 68347HEAT 16
Add
BLAST
Repeati686 – 72439HEAT 17
Add
BLAST
Repeati727 – 76640HEAT 18
Add
BLAST
Repeati769 – 81143HEAT 19
Add
BLAST
Repeati814 – 85340HEAT 20
Add
BLAST
Repeati857 – 89337HEAT 21
Add
BLAST
Repeati894 – 94249HEAT 22
Add
BLAST
Repeati943 – 98846HEAT 23
Add
BLAST
Repeati989 – 102739HEAT 24
Add
BLAST
Repeati1029 – 106840HEAT 25
Add
BLAST
Repeati1069 – 110537HEAT 26
Add
BLAST
Repeati1106 – 114439HEAT 27
Add
BLAST
Repeati1145 – 118844HEAT 28
Add
BLAST
Repeati1189 – 122537HEAT 29
Add
BLAST
Repeati1226 – 127348HEAT 30
Add
BLAST
Repeati1274 – 131138HEAT 31
Add
BLAST
Repeati1312 – 134534HEAT 32
Add
BLAST
Repeati1346 – 138237TPR 1
Add
BLAST
Domaini1382 – 1982601FAT
Add
BLAST
Repeati1383 – 140826TPR 2
Add
BLAST
Repeati1409 – 144234TPR 3
Add
BLAST
Repeati1443 – 147331TPR 4
Add
BLAST
Repeati1474 – 150734TPR 5
Add
BLAST
Repeati1508 – 154134TPR 6
Add
BLAST
Repeati1542 – 157433TPR 7
Add
BLAST
Repeati1575 – 161440TPR 8
Add
BLAST
Repeati1615 – 164935TPR 9
Add
BLAST
Repeati1650 – 169344TPR 10
Add
BLAST
Repeati1694 – 173138TPR 11
Add
BLAST
Repeati1732 – 178655TPR 12
Add
BLAST
Repeati1787 – 184660TPR 13
Add
BLAST
Repeati1898 – 193033TPR 14
Add
BLAST
Repeati1931 – 197040TPR 15
Add
BLAST
Repeati1971 – 200535TPR 16
Add
BLAST
Domaini2182 – 2516335PI3K/PI4K
Add
BLAST
Domaini2517 – 254933FATC
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 651651Interaction with NBN By similarity
Add
BLAST
Regioni2012 – 2144133Sufficient for interaction with the FKBP1A/rapamycin complex By similarity
Add
BLAST
Regioni2258 – 229639Interaction with MLST8 By similarity
Add
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.
HOVERGENiHBG005744.
InParanoidiP42346.
KOiK07203.
OMAiTYKQNIG.
OrthoDBiEOG7CCBQ4.
PhylomeDBiP42346.
TreeFamiTF105134.

Family and domain databases

Gene3Di1.10.1070.11. 3 hits.
1.20.120.150. 1 hit.
1.25.10.10. 4 hits.
1.25.40.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024585. DUF3385_TOR.
IPR003152. FATC.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR009076. Rapamycin-bd_dom.
IPR011990. TPR-like_helical.
[Graphical view]
PfamiPF11865. DUF3385. 1 hit.
PF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF08771. Rapamycin_bind. 1 hit.
[Graphical view]
SMARTiSM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF47212. SSF47212. 1 hit.
SSF48371. SSF48371. 5 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42346-1 [UniParc]FASTAAdd to Basket

« Hide

MLGTGPATAT AGAATSSNVS VLQQFASGLK SRNEETRAKA AKELQHYVTM     50
ELREMSQEES TRFYDQLNHH IFELVSSSDA NERKGGILAI ASLIGVEGGN 100
STRIGRFANY LRNLLPSSDP VVMEMASKAI GRLAMAGDTF TAEYVEFEVK 150
RALEWLGADR NEGRRHAAVL VLRELAISVP TFFFQQVQPF FDNIFVAVWD 200
PKQAIREGAV AALRACLILT TQREPKEMQK PQWYRHTFEE AEKGFDETLA 250
KEKGMNRDDR IHGALLILNE LVRISSMEGE RLREEMEEIT QQQLVHDKYC 300
KDLMGFGTKP RHITPFTSFQ AVQPQQSNAL VGLLGYSSHQ GLMGFGASPS 350
PTKSTLVESR CCRDLMEEKF DQVCQWVLKC RSSKNSLIQM TILNLLPRLA 400
AFRPSAFTDT QYLQDTMNHV LSCVKKEKER TAAFQALGLL SVAVRSEFKV 450
YLPRVLDIIR AALPPKDFAH KRQKTVQVDA TVFTCISMLA RAMGPGIQQD 500
IKELLEPMLA VGLSPALTAV LYDLSRQIPQ LKKDIQDGLL KMLSLVLMHK 550
PLRHPGMPKG LAHQLASPGL TTLPEASDVA SITLALRTLG SFEFEGHSLT 600
QFVRHCADHF LNSEHKEIRM EAARTCSRLL TPSIHLISGH AHVVSQTAVQ 650
VVADVLSKLL VVGITDPDPD IRYCVLASLD ERFDAHLAQA ENLQALFVAL 700
NDQVFEIREL AICTVGRLSS MNPAFVMPFL RKMLIQILTE LEHSGIGRIK 750
EQSARMLGHL VSNAPRLIRP YMEPILKALI LKLKDPDPDP NPGVINNVLA 800
TIGELAQVSG LEMRKWVDEL FVIIMDMLQD SSLLAKRQVA LWTLGQLVAS 850
TGYVVEPYRK YPTLLEVLLN FLKTEQNQGT RREAIRVLGL LGALDPYKHK 900
VNIGMIDQSR DASAVSLSES KSSQDSSDYS TSEMLVNMGN LPLDEFYPAV 950
SMVALMRIFR DQSLSHHHTM VVQAITFIFK SLGLKCVQFL PQVMPTFLNV 1000
IRVCDGAIRE FLFQQLGMLV SFVKSHIRPY MDEIVTLMRE FWVMNTSIQS 1050
TIILLIEQIV VALGGEFKLY LPQLIPHMLR VFMHDNSQGR IVSIKLLAAI 1100
QLFGANLDDY LHLLLPPIVK LFDAPEVPLP SRKAALETVD RLTESLDFTD 1150
YASRIIHPIV RTLDQSPELR STAMDTLSSL VFQLGKKYQI FIPMVNKVLV 1200
RHRINHQRYD VLICRIVKGY TLADEEEDPL IYQHRMLRSS QGDALASGPV 1250
ETGPMKKLHV STINLQKAWG AARRVSKDDW LEWLRRLSLE LLKDSSSPSL 1300
RSCWALAQAY NPMARDLFNA AFVSCWSELN EDQQDELIRS IELALTSQDI 1350
AEVTQTLLNL AEFMEHSDKG PLPLRDDNGI VLLGERAAKC RAYAKALHYK 1400
ELEFQKGPTP AILESLISIN NKLQQPEAAS GVLEYAMKHF GELEIQATWY 1450
EKLHEWEDAL VAYDKKMDTN KDDPELMLGR MRCLEALGEW GQLHQQCCEK 1500
WTLVNDETQA KMARMAAAAA WGLGQWDSME EYTCMIPRDT HDGAFYRAVL 1550
ALHQDLFSLA QQCIDKARDL LDAELTAMAG ESYSRAYGAM VSCHMLSELE 1600
EVIQYKLVPE RREIIRQIWW ERLQGCQRIV EDWQKILMVR SLVVSPHEDM 1650
RTWLKYASLC GKSGRLALAH KTLVLLLGVD PSRQLDHPLP TVHPQVTYAY 1700
MKNMWKSARK IDAFQHMQHF VQTMQQQAQH AIATEDQQHK QELHKLMARC 1750
FLKLGEWQLN LQGINESTIP KVLQYYSAAT EHDRSWYKAW HAWAVMNFEA 1800
VLHYKHQNQA RDEKKKLRHA SGANITNATT TATTAASAAA ATSTEGSNSE 1850
SEAESNESSP TPSPLQKKVT EDLSKTLLLY TVPAVQGFFR SISLSRGNNL 1900
QDTLRVLTLW FDYGHWPDVN EALVEGVKAI QIDTWLQVIP QLIARIDTPR 1950
PLVGRLIHQL LTDIGRYHPQ ALIYPLTVAS KSTTTARHNA ANKILKNMCE 2000
HSNTLVQQAM MVSEELIRVA ILWHEMWHEG LEEASRLYFG ERNVKGMFEV 2050
LEPLHAMMER GPQTLKETSF NQAYGRDLME AQEWCRKYMK SGNVKDLTQA 2100
WDLYYHVFRR ISKQLPQLTS LELQYVSPKL LMCRDLELAV PGTYDPNQPI 2150
IRIQSIAPSL QVITSKQRPR KLTLMGSNGH EFVFLLKGHE DLRQDERVMQ 2200
LFGLVNTLLA NDPTSLRKNL SIQRYAVIPL STNSGLIGWV PHCDTLHALI 2250
RDYREKKKIL LNIEHRIMLR MAPDYDHLTL MQKVEVFEHA VNNTAGDDLA 2300
KLLWLKSPSS EVWFDRRTNY TRSLAVMSMV GYILGLGDRH PSNLMLDRLS 2350
GKILHIDFGD CFEVAMTREK FPEKIPFRLT RMLTNAMEVT GLDGNYRTTC 2400
HTVMEVLREH KDSVMAVLEA FVYDPLLNWR LMDTNAKGNK RSRTRTDSYS 2450
AGQSVEILDG VELGEPAHKK TGTTVPESIH SFIGDGLVKP EALNKKAIQI 2500
INRVRDKLTG RDFSHDDTLD VPTQVELLIK QATSHENLCQ CYIGWCPFW 2549
Length:2,549
Mass (Da):288,794
Last modified:November 1, 1995 - v1
Checksum:iBE841EA7B9086F99
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L37085 mRNA. Translation: AAA65929.1.
U11681 mRNA. Translation: AAA20091.1.
PIRiA54837.
RefSeqiNP_063971.1. NM_019906.1.
UniGeneiRn.11008.

Genome annotation databases

EnsembliENSRNOT00000014167; ENSRNOP00000014167; ENSRNOG00000009615.
GeneIDi56718.
KEGGirno:56718.
UCSCiRGD:68371. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L37085 mRNA. Translation: AAA65929.1 .
U11681 mRNA. Translation: AAA20091.1 .
PIRi A54837.
RefSeqi NP_063971.1. NM_019906.1.
UniGenei Rn.11008.

3D structure databases

ProteinModelPortali P42346.
SMRi P42346. Positions 2015-2114, 2517-2549.
ModBasei Search...

Protein-protein interaction databases

BioGridi 248568. 4 interactions.
DIPi DIP-261N.
IntActi P42346. 3 interactions.
MINTi MINT-87926.
STRINGi 10116.ENSRNOP00000014167.

Chemistry

BindingDBi P42346.
ChEMBLi CHEMBL1075134.

PTM databases

PhosphoSitei P42346.

Proteomic databases

PaxDbi P42346.
PRIDEi P42346.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000014167 ; ENSRNOP00000014167 ; ENSRNOG00000009615 .
GeneIDi 56718.
KEGGi rno:56718.
UCSCi RGD:68371. rat.

Organism-specific databases

CTDi 2475.
RGDi 68371. Mtor.

Phylogenomic databases

eggNOGi COG5032.
GeneTreei ENSGT00720000108744.
HOVERGENi HBG005744.
InParanoidi P42346.
KOi K07203.
OMAi TYKQNIG.
OrthoDBi EOG7CCBQ4.
PhylomeDBi P42346.
TreeFami TF105134.

Enzyme and pathway databases

Reactomei REACT_198729. Constitutive PI3K/AKT Signaling in Cancer.
REACT_216105. HSF1-dependent transactivation.

Miscellaneous databases

NextBioi 611130.
PROi P42346.

Gene expression databases

Genevestigatori P42346.

Family and domain databases

Gene3Di 1.10.1070.11. 3 hits.
1.20.120.150. 1 hit.
1.25.10.10. 4 hits.
1.25.40.10. 2 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR024585. DUF3385_TOR.
IPR003152. FATC.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
IPR009076. Rapamycin-bd_dom.
IPR011990. TPR-like_helical.
[Graphical view ]
Pfami PF11865. DUF3385. 1 hit.
PF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF08771. Rapamycin_bind. 1 hit.
[Graphical view ]
SMARTi SM00146. PI3Kc. 1 hit.
[Graphical view ]
SUPFAMi SSF47212. SSF47212. 1 hit.
SSF48371. SSF48371. 5 hits.
SSF56112. SSF56112. 2 hits.
PROSITEi PS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
[Graphical view ]
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Publicationsi

  1. "Isolation of a protein target of the FKBP12-rapamycin complex in mammalian cells."
    Sabers C.J., Martin M.M., Brunn G.J., Williams J.M., Dumont F.J., Wiederrecht G., Abraham R.T.
    J. Biol. Chem. 270:815-822(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "RAFT1: a mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs."
    Sabatini D.M., Erdjument-Bromage H., Lui M., Tempst P., Snyder S.H.
    Cell 78:35-43(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. Lubec G., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 215-226 AND 533-541, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  4. "RAFT1 phosphorylation of the translational regulators p70 S6 kinase and 4E-BP1."
    Burnett P.E., Barrow R.K., Cohen N.A., Snyder S.H., Sabatini D.M.
    Proc. Natl. Acad. Sci. U.S.A. 95:1432-1437(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF RPS6KB1 AND EIF4EBP1.
  5. "mTOR kinase domain phosphorylation promotes mTORC1 signaling, cell growth, and cell cycle progression."
    Ekim B., Magnuson B., Acosta-Jaquez H.A., Keller J.A., Feener E.P., Fingar D.C.
    Mol. Cell. Biol. 31:2787-2801(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-2164.

Entry informationi

Entry nameiMTOR_RAT
AccessioniPrimary (citable) accession number: P42346
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 3, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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