Q9JLN9 (MTOR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Mtor
Synonyms:	Frap, Frap1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	2549 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 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. Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 a 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-757', 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.21 Ref.22
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. mTORC1 binds and is inhibited by the FKBP1A-rapamycin complex. 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.18
Subunit structure	Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR. 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 By similarity. Interacts with UBQLN1. Interacts with TTI1 and TELO2 By similarity. Interacts with CLIP1; phosphorylates and regulates CLIP1 By similarity. Ref.6 Ref.10 Ref.12 Ref.13 Ref.19 Ref.20
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. Nucleus › PML 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
Post-translational modification	Phosphorylated. Autophosphorylates when part of mTORC1 or mTORC2. Phosphorylation at Ser-1261 promotes autophosphorylation. Ref.17 Ref.18
Sequence similarities	Belongs to the PI3/PI4-kinase family. Contains 1 FAT domain. Contains 1 FATC domain. Contains 7 HEAT repeats. Contains 1 PI3K/PI4K domain.

Ontologies

Keywords
Cellular component	Cytoplasm Endoplasmic reticulum Golgi apparatus Lysosome Membrane Mitochondrion Mitochondrion outer membrane Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	TOR signaling cascade Inferred from electronic annotation. Source: Compara cellular response to hypoxia Inferred from direct assay Ref.13. Source: UniProtKB cellular response to nutrient levels Inferred from direct assay Ref.21. 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 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: Compara 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.19. Source: MGI positive regulation of peptidyl-tyrosine phosphorylation Inferred from mutant phenotype Ref.10. Source: MGI positive regulation of protein kinase B signaling cascade Inferred from electronic annotation. Source: Compara 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: Compara positive regulation of translation Inferred from electronic annotation. Source: Compara protein autophosphorylation 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: Compara regulation of fatty acid beta-oxidation Inferred from electronic annotation. Source: Compara regulation of glycogen biosynthetic process Inferred from electronic annotation. Source: Compara regulation of protein kinase activity Inferred from genetic interaction PubMed 15185396. Source: MGI regulation of response to food Inferred from electronic annotation. Source: Compara response to amino acid stimulus Inferred from direct assay Ref.10. Source: MGI response to insulin stimulus Inferred from direct assay Ref.10. Source: MGI ruffle organization Inferred from direct assay Ref.10. Source: MGI
Cellular_component	Golgi 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 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: Compara mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay PubMed 18347059PubMed 18381428. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase III type 1 promoter DNA binding Inferred from electronic annotation. Source: Compara RNA polymerase III type 2 promoter DNA binding Inferred from electronic annotation. Source: Compara RNA polymerase III type 3 promoter DNA binding Inferred from electronic annotation. Source: Compara drug binding Inferred from electronic annotation. Source: InterPro protein serine/threonine kinase activity Inferred from direct assay Ref.21. Source: UniProtKB ribosome binding Inferred from direct assay PubMed 21045808. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF4EBP1	Q13541	2	EBI-1571628,EBI-74090	From a different organism.
Rictor	Q6QI06	2	EBI-1571628,EBI-4286572
RPTOR	Q8N122	4	EBI-1571628,EBI-1567928	From a different organism.
Rptor	Q8K4Q0	3	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2549	2549	Serine/threonine-protein kinase mTOR		PRO_0000088809
Regions
	Repeat	16 – 53	38	HEAT 1
	Repeat	650 – 688	39	HEAT 2
	Repeat	859 – 897	39	HEAT 3
	Repeat	988 – 1025	38	HEAT 4
	Repeat	1069 – 1106	38	HEAT 5
	Repeat	1109 – 1148	40	HEAT 6
	Repeat	1150 – 1186	37	HEAT 7
	Domain	1382 – 1982	601	FAT
	Domain	2182 – 2516	335	PI3K/PI4K
	Domain	2517 – 2549	33	FATC
	Region	2012 – 2144	133	Sufficient for interaction with the FKBP1A/rapamycin complex
Amino acid modifications
	Modified residue	567	1	Phosphoserine By similarity
	Modified residue	1162	1	Phosphothreonine By similarity
	Modified residue	1218	1	N6-acetyllysine By similarity
	Modified residue	1261	1	Phosphoserine Ref.18
	Modified residue	2159	1	Phosphoserine; by autocatalysis By similarity
	Modified residue	2164	1	Phosphothreonine; by autocatalysis By similarity
	Modified residue	2446	1	Phosphothreonine; by autocatalysis By similarity
	Modified residue	2478	1	Phosphoserine Ref.15
	Modified residue	2481	1	Phosphoserine Ref.15 Ref.16
Natural variations
	Alternative sequence	236 – 256	21	HTFEE…EKGMN → VRDGSTQPLAKHFGLESCSW P in isoform 2.		VSP_011909
	Alternative sequence	257 – 2549	2293	Missing in isoform 2.		VSP_011910
Experimental info
	Mutagenesis	2035	1	S → R: Abolishes interaction with the FKBP1A-rapamycin complex. Ref.6
	Sequence conflict	33	1	N → K in AAH43920. Ref.3
	Sequence conflict	628	1	R → C in AAF73196. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 15, 2010. Version 2. Checksum: 56302E5171FB6DBD	FASTA	2,549	288,789
	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
	Isoform 2 [UniParc]. Checksum: F58320768DC9E928	FASTA	256	28,467
	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 PQWYRVRDGS 250 TQPLAKHFGL ESCSWP

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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, MASS SPECTROMETRY. Tissue: Liver.
[16]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2481, MASS SPECTROMETRY. Tissue: Melanoma.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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.
IPI	IPI00268673. IPI00457494.
RefSeq	NP_064393.2. NM_020009.2.
UniGene	Mm.21158.
3D structure databases
ProteinModelPortal	Q9JLN9.
SMR	Q9JLN9. Positions 693-725, 2019-2112, 2115-2422, 2517-2549.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-40570N.
IntAct	Q9JLN9. 7 interactions.
MINT	MINT-1899010.
STRING	10090.ENSMUSP00000099510.
PTM databases
PhosphoSite	Q9JLN9.
Proteomic databases
PaxDb	Q9JLN9.
PRIDE	Q9JLN9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000057580; ENSMUSP00000054164; ENSMUSG00000028991. ENSMUST00000103221; ENSMUSP00000099510; ENSMUSG00000028991.
GeneID	56717.
KEGG	mmu:56717.
UCSC	uc008vur.2. mouse.
Organism-specific databases
CTD	2475.
MGI	MGI:1928394. Mtor.
Phylogenomic databases
eggNOG	COG5032.
GeneTree	ENSGT00700000104444.
HOGENOM	HOG000163215.
HOVERGEN	HBG005744.
InParanoid	Q2KHT0.
KO	K07203.
OMA	DPYKHKM.
OrthoDB	EOG41RPT0.
Gene expression databases
ArrayExpress	Q9JLN9.
Bgee	Q9JLN9.
Genevestigator	Q9JLN9.
GermOnline	ENSMUSG00000028991. Mus musculus.
Family and domain databases
Gene3D	1.10.1070.11. 3 hits. 1.25.10.10. 4 hits. 1.25.40.10. 2 hits.
InterPro	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. IPR026683. TOR/Smg1. IPR011990. TPR-like_helical. [Graphical view]
PANTHER	PTHR11139:SF9. PTHR11139:SF9. 1 hit.
Pfam	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]
SMART	SM00146. PI3Kc. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 2 hits. SSF47212. FRAP_FKBP12_bind. 1 hit. SSF56112. Kinase_like. 1 hit.
PROSITE	PS51189. FAT. 1 hit. PS51190. FATC. 1 hit. PS50077. HEAT_REPEAT. False negative. PS00915. PI3_4_KINASE_1. 1 hit. PS00916. PI3_4_KINASE_2. 1 hit. PS50290. PI3_4_KINASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9JLN9.
ChEMBL	CHEMBL1255165.
ChiTaRS	MTOR. mouse.
NextBio	313190.
SOURCE	Search...

Entry information

Entry name

MTOR_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program