P42346 (MTOR_RAT) 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:	Frap1, Raft1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [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 › Rattus

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-421'. Ref.4
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activation of mTORC1 by growth factors such as insulin involves AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase a potent activator of the protein kinase activity of mTORC1. Insulin-stimulated and amino acid-dependent phosphorylation at Ser-1261 promotes autophosphorylation and the activation of mTORC1. Activation by amino acids requires relocalization of the mTORC1 complex to lysosomes that is mediated by the Ragulator complex and the Rag GTPases RRAGA, RRAGB, RRAGC and RRAGD. On the other hand, low cellular energy levels can inhibit mTORC1 through activation of PRKAA1 while hypoxia inhibits mTORC1 through a REDD1-dependent mechanism which may also require PRKAA1. The kinase activity of MTOR within the mTORC1 complex is positively regulated by MLST8 and negatively regulated by DEPTOR and AKT1S1. MTOR phosphorylates RPTOR which in turn inhibits mTORC1. 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 By similarity.
Subunit structure	Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR By similarity. Part of the mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR By similarity. 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.
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Lysosome By similarity. Cytoplasm By similarity. 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 By similarity.
Post-translational modification	Phosphorylated. Autophosphorylates when part of mTORC1 or mTORC2. Phosphorylation at Ser-1261 promotes autophosphorylation By similarity. Ref.5
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
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	G1/S transition of mitotic cell cycle Traceable author statement Ref.1. Source: RGD TOR signaling cascade Inferred from electronic annotation. Source: Compara cell projection organization Inferred from genetic interaction PubMed 16286931. Source: MGI cellular response to hypoxia Inferred from sequence or structural similarity. Source: UniProtKB cellular response to nutrient levels Inferred from sequence or structural similarity. Source: UniProtKB germ cell development Inferred from electronic annotation. Source: Compara 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 mutant phenotype PubMed 16286931. Source: MGI negative regulation of macroautophagy Inferred from electronic annotation. Source: Compara peptidyl-serine phosphorylation Inferred from electronic annotation. Source: Compara peptidyl-threonine phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of actin filament polymerization Inferred from electronic annotation. Source: Compara positive regulation of endothelial cell proliferation Inferred from mutant phenotype PubMed 17110594. Source: RGD positive regulation of lamellipodium assembly Inferred from electronic annotation. Source: Compara positive regulation of lipid biosynthetic process Inferred from sequence or structural similarity. 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 mutant phenotype PubMed 17110594. Source: RGD positive regulation of stress fiber assembly Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase III promoter Inferred from electronic annotation. Source: Compara positive regulation of translation Inferred from mutant phenotype PubMed 15525761. Source: RGD protein autophosphorylation Inferred from mutant phenotype PubMed 15388509. Source: RGD regulation of Rac GTPase activity Inferred from electronic annotation. Source: Compara regulation of carbohydrate utilization Inferred from direct assay PubMed 17142137. Source: RGD regulation of fatty acid beta-oxidation Inferred from direct assay PubMed 17142137. Source: RGD regulation of glycogen biosynthetic process Inferred from direct assay PubMed 17142137. Source: RGD regulation of protein kinase activity Inferred from electronic annotation. Source: Compara regulation of response to food Inferred from direct assay PubMed 16690869. Source: RGD response to amino acid stimulus Inferred from electronic annotation. Source: Compara response to insulin stimulus Inferred from electronic annotation. Source: Compara 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 PubMed 17110594. Source: RGD cytosol Inferred from direct assay PubMed 17110594. Source: RGD 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 direct assay Ref.1. Source: RGD mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay PubMed 17110594. Source: RGD
Molecular_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 PubMed 17142137. Source: RGD ribosome binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DEPTOR	Q8TB45	2	EBI-1571489,EBI-2359040	From a different organism.

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_0000088810
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 By similarity
	Modified residue	1162	1	Phosphothreonine By similarity
	Modified residue	1218	1	N6-acetyllysine By similarity
	Modified residue	1261	1	Phosphoserine By similarity
	Modified residue	2159	1	Phosphoserine; by autocatalysis By similarity
	Modified residue	2164	1	Phosphothreonine; by autocatalysis Ref.5
	Modified residue	2446	1	Phosphothreonine; by autocatalysis By similarity
	Modified residue	2478	1	Phosphoserine By similarity
	Modified residue	2481	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P42346 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: BE841EA7B9086F99	FASTA	2,549	288,794
	10 20 30 40 50 60 MLGTGPATAT AGAATSSNVS VLQQFASGLK SRNEETRAKA AKELQHYVTM ELREMSQEES 70 80 90 100 110 120 TRFYDQLNHH IFELVSSSDA NERKGGILAI ASLIGVEGGN STRIGRFANY LRNLLPSSDP 130 140 150 160 170 180 VVMEMASKAI GRLAMAGDTF TAEYVEFEVK RALEWLGADR NEGRRHAAVL VLRELAISVP 190 200 210 220 230 240 TFFFQQVQPF FDNIFVAVWD PKQAIREGAV AALRACLILT TQREPKEMQK PQWYRHTFEE 250 260 270 280 290 300 AEKGFDETLA KEKGMNRDDR IHGALLILNE LVRISSMEGE RLREEMEEIT QQQLVHDKYC 310 320 330 340 350 360 KDLMGFGTKP RHITPFTSFQ AVQPQQSNAL VGLLGYSSHQ GLMGFGASPS PTKSTLVESR 370 380 390 400 410 420 CCRDLMEEKF DQVCQWVLKC RSSKNSLIQM TILNLLPRLA AFRPSAFTDT QYLQDTMNHV 430 440 450 460 470 480 LSCVKKEKER TAAFQALGLL SVAVRSEFKV YLPRVLDIIR AALPPKDFAH KRQKTVQVDA 490 500 510 520 530 540 TVFTCISMLA RAMGPGIQQD IKELLEPMLA VGLSPALTAV LYDLSRQIPQ LKKDIQDGLL 550 560 570 580 590 600 KMLSLVLMHK PLRHPGMPKG LAHQLASPGL TTLPEASDVA SITLALRTLG SFEFEGHSLT 610 620 630 640 650 660 QFVRHCADHF LNSEHKEIRM EAARTCSRLL TPSIHLISGH AHVVSQTAVQ VVADVLSKLL 670 680 690 700 710 720 VVGITDPDPD IRYCVLASLD ERFDAHLAQA ENLQALFVAL NDQVFEIREL AICTVGRLSS 730 740 750 760 770 780 MNPAFVMPFL RKMLIQILTE LEHSGIGRIK EQSARMLGHL VSNAPRLIRP YMEPILKALI 790 800 810 820 830 840 LKLKDPDPDP NPGVINNVLA TIGELAQVSG LEMRKWVDEL FVIIMDMLQD SSLLAKRQVA 850 860 870 880 890 900 LWTLGQLVAS TGYVVEPYRK YPTLLEVLLN FLKTEQNQGT RREAIRVLGL LGALDPYKHK 910 920 930 940 950 960 VNIGMIDQSR DASAVSLSES KSSQDSSDYS TSEMLVNMGN LPLDEFYPAV SMVALMRIFR 970 980 990 1000 1010 1020 DQSLSHHHTM VVQAITFIFK SLGLKCVQFL PQVMPTFLNV IRVCDGAIRE FLFQQLGMLV 1030 1040 1050 1060 1070 1080 SFVKSHIRPY MDEIVTLMRE FWVMNTSIQS TIILLIEQIV VALGGEFKLY LPQLIPHMLR 1090 1100 1110 1120 1130 1140 VFMHDNSQGR IVSIKLLAAI QLFGANLDDY LHLLLPPIVK LFDAPEVPLP SRKAALETVD 1150 1160 1170 1180 1190 1200 RLTESLDFTD YASRIIHPIV RTLDQSPELR STAMDTLSSL VFQLGKKYQI FIPMVNKVLV 1210 1220 1230 1240 1250 1260 RHRINHQRYD VLICRIVKGY TLADEEEDPL IYQHRMLRSS QGDALASGPV ETGPMKKLHV 1270 1280 1290 1300 1310 1320 STINLQKAWG AARRVSKDDW LEWLRRLSLE LLKDSSSPSL RSCWALAQAY NPMARDLFNA 1330 1340 1350 1360 1370 1380 AFVSCWSELN EDQQDELIRS IELALTSQDI AEVTQTLLNL AEFMEHSDKG PLPLRDDNGI 1390 1400 1410 1420 1430 1440 VLLGERAAKC RAYAKALHYK ELEFQKGPTP AILESLISIN NKLQQPEAAS GVLEYAMKHF 1450 1460 1470 1480 1490 1500 GELEIQATWY EKLHEWEDAL VAYDKKMDTN KDDPELMLGR MRCLEALGEW GQLHQQCCEK 1510 1520 1530 1540 1550 1560 WTLVNDETQA KMARMAAAAA WGLGQWDSME EYTCMIPRDT HDGAFYRAVL ALHQDLFSLA 1570 1580 1590 1600 1610 1620 QQCIDKARDL LDAELTAMAG ESYSRAYGAM VSCHMLSELE EVIQYKLVPE RREIIRQIWW 1630 1640 1650 1660 1670 1680 ERLQGCQRIV EDWQKILMVR SLVVSPHEDM RTWLKYASLC GKSGRLALAH KTLVLLLGVD 1690 1700 1710 1720 1730 1740 PSRQLDHPLP TVHPQVTYAY MKNMWKSARK IDAFQHMQHF VQTMQQQAQH AIATEDQQHK 1750 1760 1770 1780 1790 1800 QELHKLMARC FLKLGEWQLN LQGINESTIP KVLQYYSAAT EHDRSWYKAW HAWAVMNFEA 1810 1820 1830 1840 1850 1860 VLHYKHQNQA RDEKKKLRHA SGANITNATT TATTAASAAA ATSTEGSNSE SEAESNESSP 1870 1880 1890 1900 1910 1920 TPSPLQKKVT EDLSKTLLLY TVPAVQGFFR SISLSRGNNL QDTLRVLTLW FDYGHWPDVN 1930 1940 1950 1960 1970 1980 EALVEGVKAI QIDTWLQVIP QLIARIDTPR PLVGRLIHQL LTDIGRYHPQ ALIYPLTVAS 1990 2000 2010 2020 2030 2040 KSTTTARHNA ANKILKNMCE HSNTLVQQAM MVSEELIRVA ILWHEMWHEG LEEASRLYFG 2050 2060 2070 2080 2090 2100 ERNVKGMFEV LEPLHAMMER GPQTLKETSF NQAYGRDLME AQEWCRKYMK SGNVKDLTQA 2110 2120 2130 2140 2150 2160 WDLYYHVFRR ISKQLPQLTS LELQYVSPKL LMCRDLELAV PGTYDPNQPI IRIQSIAPSL 2170 2180 2190 2200 2210 2220 QVITSKQRPR KLTLMGSNGH EFVFLLKGHE DLRQDERVMQ LFGLVNTLLA NDPTSLRKNL 2230 2240 2250 2260 2270 2280 SIQRYAVIPL STNSGLIGWV PHCDTLHALI RDYREKKKIL LNIEHRIMLR MAPDYDHLTL 2290 2300 2310 2320 2330 2340 MQKVEVFEHA VNNTAGDDLA KLLWLKSPSS EVWFDRRTNY TRSLAVMSMV GYILGLGDRH 2350 2360 2370 2380 2390 2400 PSNLMLDRLS GKILHIDFGD CFEVAMTREK FPEKIPFRLT RMLTNAMEVT GLDGNYRTTC 2410 2420 2430 2440 2450 2460 HTVMEVLREH KDSVMAVLEA FVYDPLLNWR LMDTNAKGNK RSRTRTDSYS AGQSVEILDG 2470 2480 2490 2500 2510 2520 VELGEPAHKK TGTTVPESIH SFIGDGLVKP EALNKKAIQI INRVRDKLTG RDFSHDDTLD 2530 2540 VPTQVELLIK QATSHENLCQ CYIGWCPFW

References

[1]	"Isolation of a protein target of the FKBP12-rapamycin complex in mammalian cells." Sabers C.J., Martin M.M., Brunn G.J., Williams J.M., Dumont F.J., Wiederrecht G., Abraham R.T. J. Biol. Chem. 270:815-822(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"RAFT1: a mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs." Sabatini D.M., Erdjument-Bromage H., Lui M., Tempst P., Snyder S.H. Cell 78:35-43(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	Lubec G., Kang S.U., Lubec S. Submitted (SEP-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 215-226 AND 533-541, 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: AUTOPHOSPHORYLATION AT THR-2164.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L37085 mRNA. Translation: AAA65929.1. U11681 mRNA. Translation: AAA20091.1.
IPI	IPI00339164.
PIR	A54837.
RefSeq	NP_063971.1. NM_019906.1.
UniGene	Rn.11008.
3D structure databases
ProteinModelPortal	P42346.
SMR	P42346. Positions 2015-2114, 2517-2549.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-261N.
IntAct	P42346. 3 interactions.
MINT	MINT-87926.
STRING	10116.ENSRNOP00000014167.
PTM databases
PhosphoSite	P42346.
Proteomic databases
PaxDb	P42346.
PRIDE	P42346.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000014167; ENSRNOP00000014167; ENSRNOG00000009615.
GeneID	56718.
KEGG	rno:56718.
UCSC	RGD:68371. rat.
Organism-specific databases
CTD	2475.
RGD	68371. Mtor.
Phylogenomic databases
eggNOG	COG5032.
GeneTree	ENSGT00700000104444.
HOVERGEN	HBG005744.
InParanoid	P42346.
KO	K07203.
OrthoDB	EOG41RPT0.
Gene expression databases
Genevestigator	P42346.
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	P42346.
ChEMBL	CHEMBL1075134.
NextBio	611130.

Entry information

Entry name

MTOR_RAT

Accession

Primary (citable) accession number: P42346

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program