P42345 (MTOR_HUMAN) 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 and FKBP12 target 1
Rapamycin target protein 1

Gene names

Name:	MTOR
Synonyms:	FRAP, FRAP1, FRAP2, RAFT1, RAPT1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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-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.10 Ref.11 Ref.12 Ref.13 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.23 Ref.26 Ref.27 Ref.30 Ref.36 Ref.40 Ref.45
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.16 Ref.19 Ref.25 Ref.30 Ref.31
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 By similarity. Interacts with PRR5 and RICTOR; the interaction is direct within the mTORC2 complex By similarity. Interacts with UBQLN1 By similarity. Interacts with TTI1 and TELO2 By similarity. Interacts with CLIP1; phosphorylates and regulates CLIP1 By similarity. Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.17 Ref.18 Ref.21 Ref.24 Ref.25 Ref.26 Ref.31 Ref.37 Ref.38 Ref.39
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side. Lysosome. Cytoplasm By similarity. Nucleus › PML 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. Ref.8 Ref.15 Ref.20 Ref.30 Ref.35
Tissue specificity	Expressed in numerous tissues, with highest levels in testis. Ref.7 Ref.14
Post-translational modification	Phosphorylated. Autophosphorylates when part of mTORC1 or mTORC2. Phosphorylation at Ser-1261 promotes autophosphorylation. Ref.8 Ref.21 Ref.22 Ref.32 Ref.43
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.
Sequence caution	The sequence AAC39933.1 differs from that shown. Reason: Frameshift at positions 956 and 999. The sequence BAE06077.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cytoplasm Endoplasmic reticulum Golgi apparatus Lysosome Membrane Mitochondrion Mitochondrion outer membrane Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T cell costimulation Traceable author statement. Source: Reactome TOR signaling cascade Inferred from mutant phenotype Ref.21PubMed 17028174Ref.27. Source: UniProtKB cell growth Inferred from direct assay Ref.27. Source: UniProtKB 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 epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome germ cell development Inferred from electronic annotation. Source: Compara insulin receptor signaling pathway Traceable author statement. Source: Reactome negative regulation of NFAT protein import into nucleus Inferred from electronic annotation. Source: Compara negative regulation of autophagy Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell size Inferred from electronic annotation. Source: Compara negative regulation of macroautophagy Inferred from electronic annotation. Source: Compara nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome peptidyl-serine phosphorylation Inferred from mutant phenotype Ref.36. Source: UniProtKB peptidyl-threonine phosphorylation Inferred from electronic annotation. Source: Compara phosphatidylinositol-mediated signaling Traceable author statement. Source: Reactome positive regulation of actin filament polymerization Inferred from electronic annotation. Source: Compara positive regulation of endothelial cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of lamellipodium assembly Inferred from electronic annotation. Source: Compara positive regulation of lipid biosynthetic process Inferred from mutant phenotype Ref.27. Source: UniProtKB positive regulation of myotube differentiation Inferred from electronic annotation. Source: Compara positive regulation of peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of protein kinase B signaling cascade Inferred from electronic annotation. Source: Compara positive regulation of protein phosphorylation Inferred from direct assay PubMed 20233713. Source: UniProtKB positive regulation of stress fiber assembly Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase III promoter Inferred from mutant phenotype PubMed 20233713. Source: UniProtKB positive regulation of translation Inferred from direct assay Ref.27. Source: UniProtKB protein autophosphorylation Inferred from direct assay Ref.21. Source: MGI protein catabolic process Traceable author statement Ref.9. Source: UniProtKB regulation of Rac GTPase activity Inferred from electronic annotation. Source: Compara regulation of actin cytoskeleton organization Inferred from mutant phenotype Ref.21. Source: UniProtKB 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 electronic annotation. Source: Compara regulation of response to food Inferred from electronic annotation. Source: Compara response to amino acid stimulus Inferred from direct assay Ref.30. Source: UniProtKB response to nutrient Non-traceable author statement PubMed 15539461. Source: UniProtKB ruffle organization Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell PML body Inferred from electronic annotation. Source: UniProtKB-SubCell TORC1 complex Inferred from direct assay Ref.26. Source: UniProtKB TORC2 complex Inferred from direct assay Ref.26. Source: UniProtKB endomembrane system Inferred from direct assay Ref.30. Source: UniProtKB endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell lysosome Inferred from direct assay Ref.35. Source: UniProtKB mTOR-FKBP12-rapamycin complex Inferred from electronic annotation. Source: Compara membrane Inferred from direct assay Ref.9. Source: UniProtKB mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell phosphatidylinositol 3-kinase complex Non-traceable author statement PubMed 15539461. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase III type 1 promoter DNA binding Inferred from direct assay PubMed 20233713. Source: UniProtKB RNA polymerase III type 2 promoter DNA binding Inferred from direct assay PubMed 20233713. Source: UniProtKB RNA polymerase III type 3 promoter DNA binding Inferred from direct assay PubMed 20233713. Source: UniProtKB TFIIIC-class transcription factor binding Inferred from direct assay PubMed 20543138. Source: UniProtKB 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 electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DEPTOR	Q8TB45	5	EBI-359260,EBI-2359040
EIF4EBP1	Q13541	2	EBI-359260,EBI-74090
MLST8	Q9BVC4	4	EBI-359260,EBI-1387471
PREX1	Q8TCU6	11	EBI-359260,EBI-1046542
RICTOR	Q6R327	16	EBI-359260,EBI-1387196
RPTOR	Q8N122	12	EBI-359260,EBI-1567928
SIRT1	Q96EB6	2	EBI-359260,EBI-1802965

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_0000088808

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 By similarity

Amino acid modifications

Modified residue

567

1

Phosphoserine Ref.28 Ref.33 Ref.41

Modified residue

1162

1

Phosphothreonine Ref.41

Modified residue

1218

1

N6-acetyllysine Ref.34

Modified residue

1261

1

Phosphoserine Ref.32

Modified residue

2159

1

Phosphoserine; by autocatalysis Ref.43

Modified residue

2164

1

Phosphothreonine; by autocatalysis By similarity

Modified residue

2446

1

Phosphothreonine; by autocatalysis Ref.22

Modified residue

2478

1

Phosphoserine Ref.29

Modified residue

2481

1

Phosphoserine Ref.29

Natural variations

Natural variant

8

1

A → S in a lung large cell carcinoma sample; somatic mutation. Ref.48

VAR_041537

Natural variant

135

1

M → T in a metastatic melanoma sample; somatic mutation. Ref.48

VAR_041538

Natural variant

1083

1

M → V. Ref.48
Corresponds to variant rs56164650 [ dbSNP | Ensembl ].

VAR_041539

Natural variant

1134

1

A → V. Ref.48
Corresponds to variant rs28730685 [ dbSNP | Ensembl ].

VAR_041540

Natural variant

1178

1

S → F. Ref.48
Corresponds to variant rs55975118 [ dbSNP | Ensembl ].

VAR_041541

Natural variant

2011

1

M → V in an ovarian mucinous carcinoma sample; somatic mutation. Ref.48

VAR_041542

Natural variant

2215

1

S → Y in a colorectal adenocarcinoma sample; somatic mutation. Ref.48

VAR_041543

Natural variant

2220

1

L → F Found in a renal cell carcinoma sample; somatic mutation. Ref.49

VAR_064733

Natural variant

2406

1

V → A Found in a renal cell carcinoma sample; somatic mutation. Ref.49

VAR_064734

Natural variant

2476

1

P → L in a glioblastoma multiforme sample; somatic mutation. Ref.48

VAR_041544

Experimental info

Sequence conflict

353

1

K → N in AAC39933. Ref.2

Sequence conflict

359

1

S → N in AAC39933. Ref.2

Sequence conflict

364

1

D → N in AAC39933. Ref.2

Sequence conflict

390

1

M → L in AAC39933. Ref.2

Sequence conflict

430

1

R → L in AAC39933. Ref.2

Sequence conflict

455 – 457

3

VLD → GVE in AAC39933. Ref.2

Sequence conflict

461

1

A → G in AAC39933. Ref.2

Sequence conflict

482 – 484

3

VFT → FFN in AAC39933. Ref.2

Sequence conflict

489

1

L → V in AAC39933. Ref.2

Sequence conflict

513

1

L → I in AAC39933. Ref.2

Sequence conflict

539

1

L → V in AAC39933. Ref.2

Sequence conflict

553

1

R → C in AAC39933. Ref.2

Sequence conflict

857

1

P → L in BAE06077. Ref.3

Sequence conflict

1075

1

I → S in AAC39933. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

2549

Helix Strand Turn

Details...

Beta strand

2017 – 2019

3

Beta strand

2020 – 2022

3

Helix

2025 – 2039

15

Helix

2044 – 2058

15

Helix

2065 – 2091

27

Helix

2094 – 2111

18

Sequences

	Sequence		Length	Mass (Da)
	P42345 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 7D9AD6E784882AB4	FASTA	2,549	288,892
	10 20 30 40 50 60 MLGTGPAAAT TAATTSSNVS VLQQFASGLK SRNEETRAKA AKELQHYVTM ELREMSQEES 70 80 90 100 110 120 TRFYDQLNHH IFELVSSSDA NERKGGILAI ASLIGVEGGN ATRIGRFANY LRNLLPSNDP 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 GLMGFGTSPS PAKSTLVESR 370 380 390 400 410 420 CCRDLMEEKF DQVCQWVLKC RNSKNSLIQM TILNLLPRLA AFRPSAFTDT QYLQDTMNHV 430 440 450 460 470 480 LSCVKKEKER TAAFQALGLL SVAVRSEFKV YLPRVLDIIR AALPPKDFAH KRQKAMQVDA 490 500 510 520 530 540 TVFTCISMLA RAMGPGIQQD IKELLEPMLA VGLSPALTAV LYDLSRQIPQ LKKDIQDGLL 550 560 570 580 590 600 KMLSLVLMHK PLRHPGMPKG LAHQLASPGL TTLPEASDVG 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 VFMHDNSPGR IVSIKLLAAI QLFGANLDDY LHLLLPPIVK LFDAPEAPLP SRKAALETVD 1150 1160 1170 1180 1190 1200 RLTESLDFTD YASRIIHPIV RTLDQSPELR STAMDTLSSL VFQLGKKYQI FIPMVNKVLV 1210 1220 1230 1240 1250 1260 RHRINHQRYD VLICRIVKGY TLADEEEDPL IYQHRMLRSG 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 NKLQQPEAAA 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 AATTAATATT TASTEGSNSE SEAESTENSP 1870 1880 1890 1900 1910 1920 TPSPLQKKVT EDLSKTLLMY 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 GLDGNYRITC 2410 2420 2430 2440 2450 2460 HTVMEVLREH KDSVMAVLEA FVYDPLLNWR LMDTNTKGNK RSRTRTDSYS AGQSVEILDG 2470 2480 2490 2500 2510 2520 VELGEPAHKK TGTTVPESIH SFIGDGLVKP EALNKKAIQI INRVRDKLTG RDFSHDDTLD 2530 2540 VPTQVELLIK QATSHENLCQ CYIGWCPFW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A mammalian protein targeted by G1-arresting rapamycin-receptor complex." Brown E.J., Albers M.W., Shin T.B., Ichikawa K., Keith C.T., Lane W.S., Schreiber S.L. Nature 369:756-758(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Molecular cloning and expression analysis of five novel genes in chromosome 1p36." Onyango P., Lubyova B., Gardellin P., Kurzbauer R., Weith A. Genomics 50:187-198(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method." Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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]. Tissue: Cerebellum.
[6]	"The human gene for mannan-binding lectin-associated serine protease-2 (MASP-2), the effector component of the lectin route of complement activation, is part of a tightly linked gene cluster on chromosome 1p36.2-3." Stover C., Endo Y., Takahashi M., Lynch N., Constantinescu C., Vorup-Jensen T., Thiel S., Friedl H., Hankeln T., Hall R., Gregory S., Fujita T., Schwaeble W. Genes Immun. 2:119-127(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1362-2549.
[7]	"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, TISSUE SPECIFICITY. Tissue: B-cell.
[8]	"Expression, enzyme activity, and subcellular localization of mammalian target of rapamycin in insulin-responsive cells." Withers D.J., Ouwens D.M., Nave B.T., van der Zon G.C.M., Alarcon C.M., Cardenas M.E., Heitman J., Maassen J.A., Shepherd P.R. Biochem. Biophys. Res. Commun. 241:704-709(1997) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION.
[9]	"Characterization of ubiquilin 1, an mTOR-interacting protein." Wu S., Mikhailov A., Kallo-Hosein H., Hara K., Yonezawa K., Avruch J. Biochim. Biophys. Acta 1542:41-56(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH UBQLN1.
[10]	"mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the growth machinery." Kim D.-H., Sarbassov D.D., Ali S.M., King J.E., Latek R.R., Erdjument-Bromage H., Tempst P., Sabatini D.M. Cell 110:163-175(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN NUTRIENT-DEPENDENT CELL GROWTH, FUNCTION IN PHOSPHORYLATION OF RPS6KB1, INTERACTION WITH RPTOR.
[11]	"Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action." Hara K., Maruki Y., Long X., Yoshino K., Oshiro N., Hidayat S., Tokunaga C., Avruch J., Yonezawa K. Cell 110:177-189(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RPTOR.
[12]	"The FKBP12-rapamycin-associated protein (FRAP) is a CLIP-170 kinase." Choi J.H., Bertram P.G., Drenan R., Carvalho J., Zhou H.H., Zheng X.F. EMBO Rep. 3:988-994(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CLIP1, FUNCTION IN PHOSPHORYLATION OF CLIP1.
[13]	"Regulation of ribosomal S6 kinase 2 by mammalian target of rapamycin." Park I.H., Bachmann R., Shirazi H., Chen J. J. Biol. Chem. 277:31423-31429(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF RPS6KB2.
[14]	"Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control." Loewith R., Jacinto E., Wullschleger S., Lorberg A., Crespo J.L., Bonenfant D., Oppliger W., Jenoe P., Hall M.N. Mol. Cell 10:457-468(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MLST8 AND RPTOR, IDENTIFICATION IN THE MTORC1 COMPLEX, TISSUE SPECIFICITY.
[15]	"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.
[16]	"TSC2 mediates cellular energy response to control cell growth and survival." Inoki K., Zhu T., Guan K.L. Cell 115:577-590(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, FUNCTION IN RESPONSE TO LOW CELLULAR ENERGY.
[17]	"GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR." Kim D.-H., Sarbassov D.D., Ali S.M., Latek R.R., Guntur K.V.P., Erdjument-Bromage H., Tempst P., Sabatini D.M. Mol. Cell 11:895-904(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MLST8.
[18]	"Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton." Sarbassov D.D., Ali S.M., Kim D.-H., Guertin D.A., Latek R.R., Erdjument-Bromage H., Tempst P., Sabatini D.M. Curr. Biol. 14:1296-1302(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PRKCA, FUNCTION IN REGULATION OF THE ACTIN CYTOSKELETON, IDENTIFICATION IN THE MTORC2 COMPLEX, INTERACTION WITH RICTOR.
[19]	"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.
[20]	"FKBP12-rapamycin-associated protein or mammalian target of rapamycin (FRAP/mTOR) localization in the endoplasmic reticulum and the Golgi apparatus." Drenan R.M., Liu X., Bertram P.G., Zheng X.F.S. J. Biol. Chem. 279:772-778(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[21]	"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 IN REGULATION OF THE ACTIN CYTOSKELETON, FUNCTION IN PHOSPHORYLATION OF PXN, IDENTIFICATION IN THE MTORC2 COMPLEX, INTERACTION WITH RICTOR, AUTOPHOSPHORYLATION.
[22]	"Identification of S6 kinase 1 as a novel mammalian target of rapamycin (mTOR)-phosphorylating kinase." Holz M.K., Blenis J. J. Biol. Chem. 280:26089-26093(2005) [PubMed] [Europe PMC] [Abstract] Cited for: AUTOPHOSPHORYLATION AT THR-2446.
[23]	"Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex." Sarbassov D.D., Guertin D.A., Ali S.M., Sabatini D.M. Science 307:1098-1101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF AKT1.
[24]	"PRR5, a novel component of mTOR complex 2, regulates platelet-derived growth factor receptor beta expression and signaling." Woo S.-Y., Kim D.-H., Jun C.-B., Kim Y.-M., Haar E.V., Lee S.-I., Hegg J.W., Bandhakavi S., Griffin T.J., Kim D.-H. J. Biol. Chem. 282:25604-25612(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE MTORC2 COMPLEX, INTERACTION WITH PRR5.
[25]	"PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase." Sancak Y., Thoreen C.C., Peterson T.R., Lindquist R.A., Kang S.A., Spooner E., Carr S.A., Sabatini D.M. Mol. Cell 25:903-915(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AKT1S1, ENZYME REGULATION.
[26]	"mTOR complex 2 (mTORC2) controls hydrophobic motif phosphorylation and activation of serum- and glucocorticoid-induced protein kinase 1 (SGK1)." Garcia-Martinez J.M., Alessi D.R. Biochem. J. 416:375-385(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE MTORC1 AND MTORC2 COMPLEXES, FUNCTION IN PHOSPHORYLATION OF RPS6KB1 AND SGK1.
[27]	"SREBP activity is regulated by mTORC1 and contributes to Akt-dependent cell growth." Porstmann T., Santos C.R., Griffiths B., Cully M., Wu M., Leevers S., Griffiths J.R., Chung Y.L., Schulze A. Cell Metab. 8:224-236(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN LIPID SYNTHESIS AND CELL GROWTH.
[28]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[29]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2478 AND SER-2481, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[30]	"The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1." Sancak Y., Peterson T.R., Shaul Y.D., Lindquist R.A., Thoreen C.C., Bar-Peled L., Sabatini D.M. Science 320:1496-1501(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION.
[31]	"DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma cells and required for their survival." Peterson T.R., Laplante M., Thoreen C.C., Sancak Y., Kang S.A., Kuehl W.M., Gray N.S., Sabatini D.M. Cell 137:873-886(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DEPTOR, ENZYME REGULATION.
[32]	"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.
[33]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567, MASS SPECTROMETRY.
[34]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1218, MASS SPECTROMETRY.
[35]	"Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids." Sancak Y., Bar-Peled L., Zoncu R., Markhard A.L., Nada S., Sabatini D.M. Cell 141:290-303(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[36]	"DAP1, a novel substrate of mTOR, negatively regulates autophagy." Koren I., Reem E., Kimchi A. Curr. Biol. 20:1093-1098(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF DAP, FUNCTION IN AUTOPHAGY.
[37]	"A genetic screen identifies the Triple T complex required for DNA damage signaling and ATM and ATR stability." Hurov K.E., Cotta-Ramusino C., Elledge S.J. Genes Dev. 24:1939-1950(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TTI1.
[38]	"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 TELO2.
[39]	"Tti1 and Tel2 are critical factors in mammalian target of rapamycin complex assembly." Kaizuka T., Hara T., Oshiro N., Kikkawa U., Yonezawa K., Takehana K., Iemura S., Natsume T., Mizushima N. J. Biol. Chem. 285:20109-20116(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TELO2 AND TTI1.
[40]	"mTORC1 directly phosphorylates and regulates human MAF1." Michels A.A., Robitaille A.M., Buczynski-Ruchonnet D., Hodroj W., Reina J.H., Hall M.N., Hernandez N. Mol. Cell. Biol. 30:3749-3757(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF RNA POLYMERASE III TRANSCRIPTION, FUNCTION IN PHOSPHORYLATION OF MAF1.
[41]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567 AND THR-1162, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[42]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[43]	"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: AUTOPHOSPHORYLATION AT SER-2159.
[44]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[45]	"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, FUNCTION IN INSR-DEPENDENT SIGNALING.
[46]	"Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP." Choi J., Chen J., Schreiber S.L., Clardy J. Science 273:239-242(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2018-2112.
[47]	"Refined structure of the FKBP12-rapamycin-FRB ternary complex at 2.2 A resolution." Liang J., Choi J., Clardy J. Acta Crystallogr. D 55:736-744(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2018-2112.
[48]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-8; THR-135; VAL-1083; VAL-1134; PHE-1178; VAL-2011; TYR-2215 AND LEU-2476.
[49]	"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma." Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A. Nature 469:539-542(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PHE-2220 AND ALA-2406.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Wikipedia

Mammalian target of rapamycin entry

Target mTOR

mTOR signaling pathway and mTOR inhibition resource

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L34075 mRNA. Translation: AAA58486.1.
U88966 mRNA. Translation: AAC39933.1. Frameshift.
AB209995 mRNA. Translation: BAE06077.1. Different initiation.
AL109811, AL049653, AL391561 Genomic DNA. Translation: CAI22105.1.
AL391561, AL049653, AL109811 Genomic DNA. Translation: CAI17228.1.
AL049653, AL109811, AL391561 Genomic DNA. Translation: CAI22145.1.
BC117166 mRNA. Translation: AAI17167.1.
AJ300188 Genomic DNA. Translation: CAC15570.1.
L35478 mRNA. Translation: AAC41713.1.

IPI

IPI00031410.

PIR

S45340.

RefSeq

NP_004949.1. NM_004958.3.

UniGene

Hs.338207.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AUE	X-ray	2.33	A/B	2015-2114	[»]
1FAP	X-ray	2.70	B	2018-2112	[»]
1NSG	X-ray	2.20	B	2019-2112	[»]
2FAP	X-ray	2.20	B	2019-2112	[»]
2GAQ	NMR	-	A	2015-2114	[»]
2NPU	NMR	-	A	2015-2114	[»]
2RSE	NMR	-	B	2019-2112	[»]
3FAP	X-ray	1.85	B	2019-2112	[»]
4DRH	X-ray	2.30	B/E	2025-2114	[»]
4DRI	X-ray	1.45	B	2025-2114	[»]
4DRJ	X-ray	1.80	B	2025-2114	[»]
4FAP	X-ray	2.80	B	2019-2112	[»]

ProteinModelPortal

P42345.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-790N.

IntAct

P42345. 31 interactions.

MINT

MINT-121301.

STRING

9606.ENSP00000354558.

PTM databases

PhosphoSite

P42345.

Polymorphism databases

DMDM

1169735.

Proteomic databases

PaxDb

P42345.

PRIDE

P42345.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000361445; ENSP00000354558; ENSG00000198793.

GeneID

2475.

KEGG

hsa:2475.

UCSC

uc001asd.3. human.

Organism-specific databases

CTD

2475.

GeneCards

GC01M011166.

HGNC

HGNC:3942. MTOR.

HPA

CAB005057.

MIM

601231. gene.

neXtProt

NX_P42345.

PharmGKB

PA28360.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5032.

HOGENOM

HOG000163215.

HOVERGEN

HBG005744.

InParanoid

P42345.

KO

K07203.

OMA

DPYKHKM.

OrthoDB

EOG41RPT0.

Enzyme and pathway databases

Pathway_Interaction_DB

pi3kciaktpathway. Class I PI3K signaling events mediated by Akt.
endothelinpathway. Endothelins.
ifngpathway. IFN-gamma pathway.
il12_2pathway. IL12-mediated signaling events.
il2_pi3kpathway. IL2 signaling events mediated by PI3K.
il4_2pathway. IL4-mediated signaling events.
mtor_4pathway. mTOR signaling pathway.
telomerasepathway. Regulation of Telomerase.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P42345.

Bgee

P42345.

CleanEx

HS_FRAP1.

Genevestigator

P42345.

GermOnline

ENSG00000198793. Homo sapiens.

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

P42345.

ChEMBL

CHEMBL2842.

ChiTaRS

MTOR. human.

EvolutionaryTrace

P42345.

GenomeRNAi

2475.

NextBio

9805.

SOURCE

Search...

Entry information

Entry name

MTOR_HUMAN

Accession

Primary (citable) accession number: P42345
Secondary accession number(s): Q4LE76 , Q5TER1, Q6LE87, Q96QG3, Q9Y4I3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 138 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.