Mtor | ENSRNOG00000009615 | NCBI 56718

Details for: Mtor

Gene ID: 56718

Symbol: Mtor

Ensembl ID: ENSRNOG00000009615

Description: mechanistic target of rapamycin kinase

Associated with

Adaptive immune system
(R-RNO-1280218)
Amino acids regulate mtorc1
(R-RNO-9639288)
Autophagy
(R-RNO-9612973)
Cd28 co-stimulation
(R-RNO-389356)
Cd28 dependent pi3k/akt signaling
(R-RNO-389357)
Cellular responses to stimuli
(R-RNO-8953897)
Cellular responses to stress
(R-RNO-2262752)
Cellular response to heat stress
(R-RNO-3371556)
Costimulation by the cd28 family
(R-RNO-388841)
Energy dependent regulation of mtor by lkb1-ampk
(R-RNO-380972)
Gene expression (transcription)
(R-RNO-74160)
Generic transcription pathway
(R-RNO-212436)
Hsf1-dependent transactivation
(R-RNO-3371571)
Immune system
(R-RNO-168256)
Intracellular signaling by second messengers
(R-RNO-9006925)
Mtorc1-mediated signalling
(R-RNO-166208)
Mtor signalling
(R-RNO-165159)
Pip3 activates akt signaling
(R-RNO-1257604)
Pten regulation
(R-RNO-6807070)
Regulation of pten gene transcription
(R-RNO-8943724)
Regulation of tp53 activity
(R-RNO-5633007)
Regulation of tp53 degradation
(R-RNO-6804757)
Regulation of tp53 expression and degradation
(R-RNO-6806003)
Rna polymerase ii transcription
(R-RNO-73857)
Signaling by receptor tyrosine kinases
(R-RNO-9006934)
Signaling by vegf
(R-RNO-194138)
Signal transduction
(R-RNO-162582)
Tp53 regulates metabolic genes
(R-RNO-5628897)
Transcriptional regulation by tp53
(R-RNO-3700989)
Vegfa-vegfr2 pathway
(R-RNO-4420097)
Vegfr2 mediated vascular permeability
(R-RNO-5218920)
'de novo' pyrimidine nucleobase biosynthetic process
(GO:0006207)
Atp binding
(GO:0005524)
Cell projection organization
(GO:0030030)
Cellular component organization
(GO:0016043)
Cellular response to starvation
(GO:0009267)
Energy reserve metabolic process
(GO:0006112)
Germ cell development
(GO:0007281)
Heart morphogenesis
(GO:0003007)
Heart valve morphogenesis
(GO:0003179)
Identical protein binding
(GO:0042802)
Inflammatory response
(GO:0006954)
Kinase activity
(GO:0016301)
Long-term memory
(GO:0007616)
Lysosome organization
(GO:0007040)
Macroautophagy
(GO:0016236)
Metal ion binding
(GO:0046872)
Negative regulation of autophagy
(GO:0010507)
Negative regulation of macroautophagy
(GO:0016242)
Negative regulation of muscle atrophy
(GO:0014736)
Negative regulation of protein phosphorylation
(GO:0001933)
Negative regulation of protein ubiquitination
(GO:0031397)
Neuronal action potential
(GO:0019228)
Phosphoprotein binding
(GO:0051219)
Phosphorylation
(GO:0016310)
Positive regulation of actin filament polymerization
(GO:0030838)
Positive regulation of endothelial cell proliferation
(GO:0001938)
Positive regulation of epithelial to mesenchymal transition
(GO:0010718)
Positive regulation of gene expression
(GO:0010628)
Positive regulation of lamellipodium assembly
(GO:0010592)
Positive regulation of myotube differentiation
(GO:0010831)
Positive regulation of neuron maturation
(GO:0014042)
Positive regulation of neuron projection development
(GO:0010976)
Positive regulation of protein phosphorylation
(GO:0001934)
Post-embryonic development
(GO:0009791)
Protein-containing complex binding
(GO:0044877)
Protein binding
(GO:0005515)
Protein destabilization
(GO:0031648)
Protein domain specific binding
(GO:0019904)
Protein kinase activity
(GO:0004672)
Protein kinase binding
(GO:0019901)
Protein phosphorylation
(GO:0006468)
Protein serine/threonine kinase activity
(GO:0004674)
Protein serine kinase activity
(GO:0106310)
Regulation of autophagy
(GO:0010506)
Regulation of carbohydrate metabolic process
(GO:0006109)
Regulation of cell growth
(GO:0001558)
Regulation of cell size
(GO:0008361)
Regulation of glycogen biosynthetic process
(GO:0005979)
Regulation of myelination
(GO:0031641)
Regulation of protein phosphorylation
(GO:0001932)
Reproductive process
(GO:0022414)
Response to activity
(GO:0014823)
Response to heat
(GO:0009408)
Response to nutrient
(GO:0007584)
Ribosome binding
(GO:0043022)
Rna polymerase iii type 1 promoter sequence-specific dna binding
(GO:0001002)
Rna polymerase iii type 2 promoter sequence-specific dna binding
(GO:0001003)
Rna polymerase iii type 3 promoter sequence-specific dna binding
(GO:0001006)
Ruffle organization
(GO:0031529)
Spinal cord development
(GO:0021510)
T-helper 1 cell lineage commitment
(GO:0002296)
Tfiiic-class transcription factor complex binding
(GO:0001156)
Visual learning
(GO:0008542)

Other Information

Proteins

FK506-binding protein 12-rapamycin complex-associated protein 1

Genular Protein ID: 1910995264

Symbol: MTOR_RAT

Name: FK506-binding protein 12-rapamycin complex-associated protein 1

UniProtKB Accession Codes:

P42346

Database IDs:

Citations:

PubMed ID: 7822316

Title: Isolation of a protein target of the FKBP12-rapamycin complex in mammalian cells.

PubMed ID: 7822316

DOI: 10.1074/jbc.270.2.815

PubMed ID: 7518356

Title: RAFT1: a mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs.

PubMed ID: 7518356

DOI: 10.1016/0092-8674(94)90570-3

PubMed ID: 9465032

Title: RAFT1 phosphorylation of the translational regulators p70 S6 kinase and 4E-BP1.

PubMed ID: 9465032

DOI: 10.1073/pnas.95.4.1432

PubMed ID: 21576368

Title: mTOR kinase domain phosphorylation promotes mTORC1 signaling, cell growth, and cell cycle progression.

PubMed ID: 21576368

DOI: 10.1128/mcb.05437-11

PubMed ID: 22673903

Title: Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues.

PubMed ID: 22673903

DOI: 10.1038/ncomms1871

PubMed ID: 24187137

Title: Skeletal muscle-derived myonectin activates the mammalian target of rapamycin (mTOR) pathway to suppress autophagy in liver.

PubMed ID: 24187137

DOI: 10.1074/jbc.m113.500736

Sequence Information:

Length: 2549
Mass: 288794
Checksum: BE841EA7B9086F99
Sequence:

MLGTGPATAT AGAATSSNVS VLQQFASGLK SRNEETRAKA AKELQHYVTM ELREMSQEES 
TRFYDQLNHH IFELVSSSDA NERKGGILAI ASLIGVEGGN STRIGRFANY LRNLLPSSDP 
VVMEMASKAI GRLAMAGDTF TAEYVEFEVK RALEWLGADR NEGRRHAAVL VLRELAISVP 
TFFFQQVQPF FDNIFVAVWD PKQAIREGAV AALRACLILT TQREPKEMQK PQWYRHTFEE 
AEKGFDETLA KEKGMNRDDR IHGALLILNE LVRISSMEGE RLREEMEEIT QQQLVHDKYC 
KDLMGFGTKP RHITPFTSFQ AVQPQQSNAL VGLLGYSSHQ GLMGFGASPS PTKSTLVESR 
CCRDLMEEKF DQVCQWVLKC RSSKNSLIQM TILNLLPRLA AFRPSAFTDT QYLQDTMNHV 
LSCVKKEKER TAAFQALGLL SVAVRSEFKV YLPRVLDIIR AALPPKDFAH KRQKTVQVDA 
TVFTCISMLA RAMGPGIQQD IKELLEPMLA VGLSPALTAV LYDLSRQIPQ LKKDIQDGLL 
KMLSLVLMHK PLRHPGMPKG LAHQLASPGL TTLPEASDVA SITLALRTLG SFEFEGHSLT 
QFVRHCADHF LNSEHKEIRM EAARTCSRLL TPSIHLISGH AHVVSQTAVQ VVADVLSKLL 
VVGITDPDPD IRYCVLASLD ERFDAHLAQA ENLQALFVAL NDQVFEIREL AICTVGRLSS 
MNPAFVMPFL RKMLIQILTE LEHSGIGRIK EQSARMLGHL VSNAPRLIRP YMEPILKALI 
LKLKDPDPDP NPGVINNVLA TIGELAQVSG LEMRKWVDEL FVIIMDMLQD SSLLAKRQVA 
LWTLGQLVAS TGYVVEPYRK YPTLLEVLLN FLKTEQNQGT RREAIRVLGL LGALDPYKHK 
VNIGMIDQSR DASAVSLSES KSSQDSSDYS TSEMLVNMGN LPLDEFYPAV SMVALMRIFR 
DQSLSHHHTM VVQAITFIFK SLGLKCVQFL PQVMPTFLNV IRVCDGAIRE FLFQQLGMLV 
SFVKSHIRPY MDEIVTLMRE FWVMNTSIQS TIILLIEQIV VALGGEFKLY LPQLIPHMLR 
VFMHDNSQGR IVSIKLLAAI QLFGANLDDY LHLLLPPIVK LFDAPEVPLP SRKAALETVD 
RLTESLDFTD YASRIIHPIV RTLDQSPELR STAMDTLSSL VFQLGKKYQI FIPMVNKVLV 
RHRINHQRYD VLICRIVKGY TLADEEEDPL IYQHRMLRSS QGDALASGPV ETGPMKKLHV 
STINLQKAWG AARRVSKDDW LEWLRRLSLE LLKDSSSPSL RSCWALAQAY NPMARDLFNA 
AFVSCWSELN EDQQDELIRS IELALTSQDI AEVTQTLLNL AEFMEHSDKG PLPLRDDNGI 
VLLGERAAKC RAYAKALHYK ELEFQKGPTP AILESLISIN NKLQQPEAAS GVLEYAMKHF 
GELEIQATWY EKLHEWEDAL VAYDKKMDTN KDDPELMLGR MRCLEALGEW GQLHQQCCEK 
WTLVNDETQA KMARMAAAAA WGLGQWDSME EYTCMIPRDT HDGAFYRAVL ALHQDLFSLA 
QQCIDKARDL LDAELTAMAG ESYSRAYGAM VSCHMLSELE EVIQYKLVPE RREIIRQIWW 
ERLQGCQRIV EDWQKILMVR SLVVSPHEDM RTWLKYASLC GKSGRLALAH KTLVLLLGVD 
PSRQLDHPLP TVHPQVTYAY MKNMWKSARK IDAFQHMQHF VQTMQQQAQH AIATEDQQHK 
QELHKLMARC FLKLGEWQLN LQGINESTIP KVLQYYSAAT EHDRSWYKAW HAWAVMNFEA 
VLHYKHQNQA RDEKKKLRHA SGANITNATT TATTAASAAA ATSTEGSNSE SEAESNESSP 
TPSPLQKKVT EDLSKTLLLY TVPAVQGFFR SISLSRGNNL QDTLRVLTLW FDYGHWPDVN 
EALVEGVKAI QIDTWLQVIP QLIARIDTPR PLVGRLIHQL LTDIGRYHPQ ALIYPLTVAS 
KSTTTARHNA ANKILKNMCE HSNTLVQQAM MVSEELIRVA ILWHEMWHEG LEEASRLYFG 
ERNVKGMFEV LEPLHAMMER GPQTLKETSF NQAYGRDLME AQEWCRKYMK SGNVKDLTQA 
WDLYYHVFRR ISKQLPQLTS LELQYVSPKL LMCRDLELAV PGTYDPNQPI IRIQSIAPSL 
QVITSKQRPR KLTLMGSNGH EFVFLLKGHE DLRQDERVMQ LFGLVNTLLA NDPTSLRKNL 
SIQRYAVIPL STNSGLIGWV PHCDTLHALI RDYREKKKIL LNIEHRIMLR MAPDYDHLTL 
MQKVEVFEHA VNNTAGDDLA KLLWLKSPSS EVWFDRRTNY TRSLAVMSMV GYILGLGDRH 
PSNLMLDRLS GKILHIDFGD CFEVAMTREK FPEKIPFRLT RMLTNAMEVT GLDGNYRTTC 
HTVMEVLREH KDSVMAVLEA FVYDPLLNWR LMDTNAKGNK RSRTRTDSYS AGQSVEILDG 
VELGEPAHKK TGTTVPESIH SFIGDGLVKP EALNKKAIQI INRVRDKLTG RDFSHDDTLD 
VPTQVELLIK QATSHENLCQ CYIGWCPFW

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: Mtor

Associated with

Other Information

Isolation of a protein target of the FKBP12-rapamycin complex in mammalian cells. PubMed ID: 7822316

RAFT1: a mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs. PubMed ID: 7518356

RAFT1 phosphorylation of the translational regulators p70 S6 kinase and 4E-BP1. PubMed ID: 9465032

mTOR kinase domain phosphorylation promotes mTORC1 signaling, cell growth, and cell cycle progression. PubMed ID: 21576368

Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues. PubMed ID: 22673903