Hmdb loader

Showing Protein Serine/threonine-protein kinase mTOR (HMDBP02611)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 4 metabolites
Identification
HMDB Protein ID HMDBP02611
Secondary Accession Numbers
  • 8110
Name Serine/threonine-protein kinase mTOR
Synonyms
  1. FK506-binding protein 12-rapamycin complex-associated protein 1
  2. FKBP12-rapamycin complex-associated protein
  3. Mammalian target of rapamycin
  4. Mechanistic target of rapamycin
  5. RAPT1
  6. Rapamycin target protein 1
  7. mTOR
Gene Name MTOR
Protein Type Enzyme
Biological Properties
General Function Involved in binding
Specific Function Kinase subunit of both mTORC1 and mTORC2, which regulate cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino-acids. Amino-acid-signaling to mTORC1 is mediated by Rag GTPases, which cause amino-acid-induced relocalization of mTOR within the endomembrane system. Growth factor-stimulated mTORC1 activation involves AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-421', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. mTORC2 is also activated by growth factors, but seems to be nutrient- insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'
Pathways
  • Bafetinib Inhibition of BCR-ABL
  • BCR-ABL Action in CML Pathogenesis
  • Bosutinib Inhibition of BCR-ABL
  • Dasatinib Inhibition of BCR-ABL
  • Glutaminolysis and Cancer
  • Imatinib Inhibition of BCR-ABL
  • Leucine Stimulation on Insulin Signaling
  • Nilotinib Inhibition of BCR-ABL
  • Ponatinib Inhibition of BCR-ABL
Reactions Not Available
GO Classification
Function
binding
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
phosphotransferase activity, alcohol group as acceptor
Cellular Location
  1. Golgi apparatus membrane
  2. Peripheral membrane protein
  3. Peripheral membrane protein
  4. Peripheral membrane protein
  5. Endoplasmic reticulum membrane
  6. Cytoplasmic side
  7. Cytoplasmic side
  8. Cytoplasmic side
  9. Mitochondrion outer membrane
Gene Properties
Chromosome Location Chromosome:1
Locus 1p36.2
SNPs MTOR
Gene Sequence 
>7650 bp
ATGCTTGGAACCGGACCTGCCGCCGCCACCACCGCTGCCACCACATCTAGCAATGTGAGC
GTCCTGCAGCAGTTTGCCAGTGGCCTAAAGAGCCGGAATGAGGAAACCAGGGCCAAAGCC
GCCAAGGAGCTCCAGCACTATGTCACCATGGAACTCCGAGAGATGAGTCAAGAGGAGTCT
ACTCGCTTCTATGACCAACTGAACCATCACATTTTTGAATTGGTTTCCAGCTCAGATGCC
AATGAGAGGAAAGGTGGCATCTTGGCCATAGCTAGCCTCATAGGAGTGGAAGGTGGGAAT
GCCACCCGAATTGGCAGATTTGCCAACTATCTTCGGAACCTCCTCCCCTCCAATGACCCA
GTTGTCATGGAAATGGCATCCAAGGCCATTGGCCGTCTTGCCATGGCAGGGGACACTTTT
ACCGCTGAGTACGTGGAATTTGAGGTGAAGCGAGCCCTGGAATGGCTGGGTGCTGACCGC
AATGAGGGCCGGAGACATGCAGCTGTCCTGGTTCTCCGTGAGCTGGCCATCAGCGTCCCT
ACCTTCTTCTTCCAGCAAGTGCAACCCTTCTTTGACAACATTTTTGTGGCCGTGTGGGAC
CCCAAACAGGCCATCCGTGAGGGAGCTGTAGCCGCCCTTCGTGCCTGTCTGATTCTCACA
ACCCAGCGTGAGCCGAAGGAGATGCAGAAGCCTCAGTGGTACAGGCACACATTTGAAGAA
GCAGAGAAGGGATTTGATGAGACCTTGGCCAAAGAGAAGGGCATGAATCGGGATGATCGG
ATCCATGGAGCCTTGTTGATCCTTAACGAGCTGGTCCGAATCAGCAGCATGGAGGGAGAG
CGTCTGAGAGAAGAAATGGAAGAAATCACACAGCAGCAGCTGGTACACGACAAGTACTGC
AAAGATCTCATGGGCTTCGGAACAAAACCTCGTCACATTACCCCCTTCACCAGTTTCCAG
GCTGTACAGCCCCAGCAGTCAAATGCCTTGGTGGGGCTGCTGGGGTACAGCTCTCACCAA
GGCCTCATGGGATTTGGGACCTCCCCCAGTCCAGCTAAGTCCACCCTGGTGGAGAGCCGG
TGTTGCAGAGACTTGATGGAGGAGAAATTTGATCAGGTGTGCCAGTGGGTGCTGAAATGC
AGGAATAGCAAGAACTCGCTGATCCAAATGACAATCCTTAATTTGTTGCCCCGCTTGGCT
GCATTCCGACCTTCTGCCTTCACAGATACCCAGTATCTCCAAGATACCATGAACCATGTC
CTAAGCTGTGTCAAGAAGGAGAAGGAACGTACAGCGGCCTTCCAAGCCCTGGGGCTACTT
TCTGTGGCTGTGAGGTCTGAGTTTAAGGTCTATTTGCCTCGCGTGCTGGACATCATCCGA
GCGGCCCTGCCCCCAAAGGACTTCGCCCATAAGAGGCAGAAGGCAATGCAGGTGGACGCC
ACAGTCTTCACTTGCATCAGCATGCTGGCTCGAGCAATGGGGCCAGGCATCCAGCAGGAT
ATCAAGGAGCTGCTGGAGCCCATGCTGGCAGTGGGACTAAGCCCTGCCCTCACTGCAGTG
CTCTACGACCTGAGCCGTCAGATTCCACAGCTAAAGAAGGACATTCAAGATGGGCTACTG
AAAATGCTGTCCCTGGTCCTTATGCACAAACCCCTTCGCCACCCAGGCATGCCCAAGGGC
CTGGCCCATCAGCTGGCCTCTCCTGGCCTCACGACCCTCCCTGAGGCCAGCGATGTGGGC
AGCATCACTCTTGCCCTCCGAACGCTTGGCAGCTTTGAATTTGAAGGCCACTCTCTGACC
CAATTTGTTCGCCACTGTGCGGATCATTTCCTGAACAGTGAGCACAAGGAGATCCGCATG
GAGGCTGCCCGCACCTGCTCCCGCCTGCTCACACCCTCCATCCACCTCATCAGTGGCCAT
GCTCATGTGGTTAGCCAGACCGCAGTGCAAGTGGTGGCAGATGTGCTTAGCAAACTGCTC
GTAGTTGGGATAACAGATCCTGACCCTGACATTCGCTACTGTGTCTTGGCGTCCCTGGAC
GAGCGCTTTGATGCACACCTGGCCCAGGCGGAGAACTTGCAGGCCTTGTTTGTGGCTCTG
AATGACCAGGTGTTTGAGATCCGGGAGCTGGCCATCTGCACTGTGGGCCGACTCAGTAGC
ATGAACCCTGCCTTTGTCATGCCTTTCCTGCGCAAGATGCTCATCCAGATTTTGACAGAG
TTGGAGCACAGTGGGATTGGAAGAATCAAAGAGCAGAGTGCCCGCATGCTGGGGCACCTG
GTCTCCAATGCCCCCCGACTCATCCGCCCCTACATGGAGCCTATTCTGAAGGCATTAATT
TTGAAACTGAAAGATCCAGACCCTGATCCAAACCCAGGTGTGATCAATAATGTCCTGGCA
ACAATAGGAGAATTGGCACAGGTTAGTGGCCTGGAAATGAGGAAATGGGTTGATGAACTT
TTTATTATCATCATGGACATGCTCCAGGATTCCTCTTTGTTGGCCAAAAGGCAGGTGGCT
CTGTGGACCCTGGGACAGTTGGTGGCCAGCACTGGCTATGTAGTAGAGCCCTACAGGAAG
TACCCTACTTTGCTTGAGGTGCTACTGAATTTTCTGAAGACTGAGCAGAACCAGGGTACA
CGCAGAGAGGCCATCCGTGTGTTAGGGCTTTTAGGGGCTTTGGATCCTTACAAGCACAAA
GTGAACATTGGCATGATAGACCAGTCCCGGGATGCCTCTGCTGTCAGCCTGTCAGAATCC
AAGTCAAGTCAGGATTCCTCTGACTATAGCACTAGTGAAATGCTGGTCAACATGGGAAAC
TTGCCTCTGGATGAGTTCTACCCAGCTGTGTCCATGGTGGCCCTGATGCGGATCTTCCGA
GACCAGTCACTCTCTCATCATCACACCATGGTTGTCCAGGCCATCACCTTCATCTTCAAG
TCCCTGGGACTCAAATGTGTGCAGTTCCTGCCCCAGGTCATGCCCACGTTCCTTAATGTC
ATTCGAGTCTGTGATGGGGCCATCCGGGAATTTTTGTTCCAGCAGCTGGGAATGTTGGTG
TCCTTTGTGAAGAGCCACATCAGACCTTATATGGATGAAATAGTCACCCTCATGAGAGAA
TTCTGGGTCATGAACACCTCAATTCAGAGCACGATCATTCTTCTCATTGAGCAAATTGTG
GTAGCTCTTGGGGGTGAATTTAAGCTCTACCTGCCCCAGCTGATCCCACACATGCTGCGT
GTCTTCATGCATGACAACAGCCCAGGCCGCATTGTCTCTATCAAGTTACTGGCTGCAATC
CAGCTGTTTGGCGCCAACCTGGATGACTACCTGCATTTACTGCTGCCTCCTATTGTTAAG
TTGTTTGATGCCCCTGAAGCTCCACTGCCATCTCGAAAGGCAGCGCTAGAGACTGTGGAC
CGCCTGACGGAGTCCCTGGATTTCACTGACTATGCCTCCCGGATCATTCACCCTATTGTT
CGAACACTGGACCAGAGCCCAGAACTGCGCTCCACAGCCATGGACACGCTGTCTTCACTT
GTTTTTCAGCTGGGGAAGAAGTACCAAATTTTCATTCCAATGGTGAATAAAGTTCTGGTG
CGACACCGAATCAATCATCAGCGCTATGATGTGCTCATCTGCAGAATTGTCAAGGGATAC
ACACTTGCTGATGAAGAGGAGGATCCTTTGATTTACCAGCATCGGATGCTTAGGAGTGGC
CAAGGGGATGCATTGGCTAGTGGACCAGTGGAAACAGGACCCATGAAGAAACTGCACGTC
AGCACCATCAACCTCCAAAAGGCCTGGGGCGCTGCCAGGAGGGTCTCCAAAGATGACTGG
CTGGAATGGCTGAGACGGCTGAGCCTGGAGCTGCTGAAGGACTCATCATCGCCCTCCCTG
CGCTCCTGCTGGGCCCTGGCACAGGCCTACAACCCGATGGCCAGGGATCTCTTCAATGCT
GCATTTGTGTCCTGCTGGTCTGAACTGAATGAAGATCAACAGGATGAGCTCATCAGAAGC
ATCGAGTTGGCCCTCACCTCACAAGACATCGCTGAAGTCACACAGACCCTCTTAAACTTG
GCTGAATTCATGGAACACAGTGACAAGGGCCCCCTGCCACTGAGAGATGACAATGGCATT
GTTCTGCTGGGTGAGAGAGCTGCCAAGTGCCGAGCATATGCCAAAGCACTACACTACAAA
GAACTGGAGTTCCAGAAAGGCCCCACCCCTGCCATTCTAGAATCTCTCATCAGCATTAAT
AATAAGCTACAGCAGCCGGAGGCAGCGGCCGGAGTGTTAGAATATGCCATGAAACACTTT
GGAGAGCTGGAGATCCAGGCTACCTGGTATGAGAAACTGCACGAGTGGGAGGATGCCCTT
GTGGCCTATGACAAGAAAATGGACACCAACAAGGACGACCCAGAGCTGATGCTGGGCCGC
ATGCGCTGCCTCGAGGCCTTGGGGGAATGGGGTCAACTCCACCAGCAGTGCTGTGAAAAG
TGGACCCTGGTTAATGATGAGACCCAAGCCAAGATGGCCCGGATGGCTGCTGCAGCTGCA
TGGGGTTTAGGTCAGTGGGACAGCATGGAAGAATACACCTGTATGATCCCTCGGGACACC
CATGATGGGGCATTTTATAGAGCTGTGCTGGCACTGCATCAGGACCTCTTCTCCTTGGCA
CAACAGTGCATTGACAAGGCCAGGGACCTGCTGGATGCTGAATTAACTGCAATGGCAGGA
GAGAGTTACAGTCGGGCATATGGGGCCATGGTTTCTTGCCACATGCTGTCCGAGCTGGAG
GAGGTTATCCAGTACAAACTTGTCCCCGAGCGACGAGAGATCATCCGCCAGATCTGGTGG
GAGAGACTGCAGGGCTGCCAGCGTATCGTAGAGGACTGGCAGAAAATCCTTATGGTGCGG
TCCCTTGTGGTCAGCCCTCATGAAGACATGAGAACCTGGCTCAAGTATGCAAGCCTGTGC
GGCAAGAGTGGCAGGCTGGCTCTTGCTCATAAAACTTTAGTGTTGCTCCTGGGAGTTGAT
CCGTCTCGGCAACTTGACCATCCTCTGCCAACAGTTCACCCTCAGGTGACCTATGCCTAC
ATGAAAAACATGTGGAAGAGTGCCCGCAAGATCGATGCCTTCCAGCACATGCAGCATTTT
GTCCAGACCATGCAGCAACAGGCCCAGCATGCCATCGCTACTGAGGACCAGCAGCATAAG
CAGGAACTGCACAAGCTCATGGCCCGATGCTTCCTGAAACTTGGAGAGTGGCAGCTGAAT
CTACAGGGCATCAATGAGAGCACAATCCCCAAAGTGCTGCAGTACTACAGCGCCGCCACA
GAGCACGACCGCAGCTGGTACAAGGCCTGGCATGCGTGGGCAGTGATGAACTTCGAAGCT
GTGCTACACTACAAACATCAGAACCAAGCCCGCGATGAGAAGAAGAAACTGCGTCATGCC
AGCGGGGCCAACATCACCAACGCCACCACTGCCGCCACCACGGCCGCCACTGCCACCACC
ACTGCCAGCACCGAGGGCAGCAACAGTGAGAGCGAGGCCGAGAGCACCGAGAACAGCCCC
ACCCCATCGCCGCTGCAGAAGAAGGTCACTGAGGATCTGTCCAAAACCCTCCTGATGTAC
ACGGTGCCTGCCGTCCAGGGCTTCTTCCGTTCCATCTCCTTGTCACGAGGCAACAACCTC
CAGGATACACTCAGAGTTCTCACCTTATGGTTTGATTATGGTCACTGGCCAGATGTCAAT
GAGGCCTTAGTGGAGGGGGTGAAAGCCATCCAGATTGATACCTGGCTACAGGTTATACCT
CAGCTCATTGCAAGAATTGATACGCCCAGACCCTTGGTGGGACGTCTCATTCACCAGCTT
CTCACAGACATTGGTCGGTACCACCCCCAGGCCCTCATCTACCCACTGACAGTGGCTTCT
AAGTCTACCACGACAGCCCGGCACAATGCAGCCAACAAGATTCTGAAGAACATGTGTGAG
CACAGCAACACCCTGGTCCAGCAGGCCATGATGGTGAGCGAGGAGCTGATCCGAGTGGCC
ATCCTCTGGCATGAGATGTGGCATGAAGGCCTGGAAGAGGCATCTCGTTTGTACTTTGGG
GAAAGGAACGTGAAAGGCATGTTTGAGGTGCTGGAGCCCTTGCATGCTATGATGGAACGG
GGCCCCCAGACTCTGAAGGAAACATCCTTTAATCAGGCCTATGGTCGAGATTTAATGGAG
GCCCAAGAGTGGTGCAGGAAGTACATGAAATCAGGGAATGTCAAGGACCTCACCCAAGCC
TGGGACCTCTATTATCATGTGTTCCGACGAATCTCAAAGCAGCTGCCTCAGCTCACATCC
TTAGAGCTGCAATATGTTTCCCCAAAACTTCTGATGTGCCGGGACCTTGAATTGGCTGTG
CCAGGAACATATGACCCCAACCAGCCAATCATTCGCATTCAGTCCATAGCACCGTCTTTG
CAAGTCATCACATCCAAGCAGAGGCCCCGGAAATTGACACTTATGGGCAGCAACGGACAT
GAGTTTGTTTTCCTTCTAAAAGGCCATGAAGATCTGCGCCAGGATGAGCGTGTGATGCAG
CTCTTCGGCCTGGTTAACACCCTTCTGGCCAATGACCCAACATCTCTTCGGAAAAACCTC
AGCATCCAGAGATACGCTGTCATCCCTTTATCGACCAACTCGGGCCTCATTGGCTGGGTT
CCCCACTGTGACACACTGCACGCCCTCATCCGGGACTACAGGGAGAAGAAGAAGATCCTT
CTCAACATCGAGCATCGCATCATGTTGCGGATGGCTCCGGACTATGACCACTTGACTCTG
ATGCAGAAGGTGGAGGTGTTTGAGCATGCCGTCAATAATACAGCTGGGGACGACCTGGCC
AAGCTGCTGTGGCTGAAAAGCCCCAGCTCCGAGGTGTGGTTTGACCGAAGAACCAATTAT
ACCCGTTCTTTAGCGGTCATGTCAATGGTTGGGTATATTTTAGGCCTGGGAGATAGACAC
CCATCCAACCTGATGCTGGACCGTCTGAGTGGGAAGATCCTGCACATTGACTTTGGGGAC
TGCTTTGAGGTTGCTATGACCCGAGAGAAGTTTCCAGAGAAGATTCCATTTAGACTAACA
AGAATGTTGACCAATGCTATGGAGGTTACAGGCCTGGATGGCAACTACAGAATCACATGC
CACACAGTGATGGAGGTGCTGCGAGAGCACAAGGACAGTGTCATGGCCGTGCTGGAAGCC
TTTGTCTATGACCCCTTGCTGAACTGGAGGCTGATGGACACAAATACCAAAGGCAACAAG
CGATCCCGAACGAGGACGGATTCCTACTCTGCTGGCCAGTCAGTCGAAATTTTGGACGGT
GTGGAACTTGGAGAGCCAGCCCATAAGAAAACGGGGACCACAGTGCCAGAATCTATTCAT
TCTTTCATTGGAGACGGTTTGGTGAAACCAGAGGCCCTAAATAAGAAAGCTATCCAGATT
ATTAACAGGGTTCGAGATAAGCTCACTGGTCGGGACTTCTCTCATGATGACACTTTGGAT
GTTCCAACGCAAGTTGAGCTGCTCATCAAACAAGCGACATCCCATGAAAACCTCTGCCAG
TGCTATATTGGCTGGTGCCCTTTCTGGTAA
Protein Properties
Number of Residues 2549
Molecular Weight 288889.0
Theoretical pI 7.17
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>Serine/threonine-protein kinase mTOR
MLGTGPAAATTAATTSSNVSVLQQFASGLKSRNEETRAKAAKELQHYVTMELREMSQEES
TRFYDQLNHHIFELVSSSDANERKGGILAIASLIGVEGGNATRIGRFANYLRNLLPSNDP
VVMEMASKAIGRLAMAGDTFTAEYVEFEVKRALEWLGADRNEGRRHAAVLVLRELAISVP
TFFFQQVQPFFDNIFVAVWDPKQAIREGAVAALRACLILTTQREPKEMQKPQWYRHTFEE
AEKGFDETLAKEKGMNRDDRIHGALLILNELVRISSMEGERLREEMEEITQQQLVHDKYC
KDLMGFGTKPRHITPFTSFQAVQPQQSNALVGLLGYSSHQGLMGFGTSPSPAKSTLVESR
CCRDLMEEKFDQVCQWVLKCRNSKNSLIQMTILNLLPRLAAFRPSAFTDTQYLQDTMNHV
LSCVKKEKERTAAFQALGLLSVAVRSEFKVYLPRVLDIIRAALPPKDFAHKRQKAMQVDA
TVFTCISMLARAMGPGIQQDIKELLEPMLAVGLSPALTAVLYDLSRQIPQLKKDIQDGLL
KMLSLVLMHKPLRHPGMPKGLAHQLASPGLTTLPEASDVGSITLALRTLGSFEFEGHSLT
QFVRHCADHFLNSEHKEIRMEAARTCSRLLTPSIHLISGHAHVVSQTAVQVVADVLSKLL
VVGITDPDPDIRYCVLASLDERFDAHLAQAENLQALFVALNDQVFEIRELAICTVGRLSS
MNPAFVMPFLRKMLIQILTELEHSGIGRIKEQSARMLGHLVSNAPRLIRPYMEPILKALI
LKLKDPDPDPNPGVINNVLATIGELAQVSGLEMRKWVDELFIIIMDMLQDSSLLAKRQVA
LWTLGQLVASTGYVVEPYRKYPTLLEVLLNFLKTEQNQGTRREAIRVLGLLGALDPYKHK
VNIGMIDQSRDASAVSLSESKSSQDSSDYSTSEMLVNMGNLPLDEFYPAVSMVALMRIFR
DQSLSHHHTMVVQAITFIFKSLGLKCVQFLPQVMPTFLNVIRVCDGAIREFLFQQLGMLV
SFVKSHIRPYMDEIVTLMREFWVMNTSIQSTIILLIEQIVVALGGEFKLYLPQLIPHMLR
VFMHDNSPGRIVSIKLLAAIQLFGANLDDYLHLLLPPIVKLFDAPEAPLPSRKAALETVD
RLTESLDFTDYASRIIHPIVRTLDQSPELRSTAMDTLSSLVFQLGKKYQIFIPMVNKVLV
RHRINHQRYDVLICRIVKGYTLADEEEDPLIYQHRMLRSGQGDALASGPVETGPMKKLHV
STINLQKAWGAARRVSKDDWLEWLRRLSLELLKDSSSPSLRSCWALAQAYNPMARDLFNA
AFVSCWSELNEDQQDELIRSIELALTSQDIAEVTQTLLNLAEFMEHSDKGPLPLRDDNGI
VLLGERAAKCRAYAKALHYKELEFQKGPTPAILESLISINNKLQQPEAAAGVLEYAMKHF
GELEIQATWYEKLHEWEDALVAYDKKMDTNKDDPELMLGRMRCLEALGEWGQLHQQCCEK
WTLVNDETQAKMARMAAAAAWGLGQWDSMEEYTCMIPRDTHDGAFYRAVLALHQDLFSLA
QQCIDKARDLLDAELTAMAGESYSRAYGAMVSCHMLSELEEVIQYKLVPERREIIRQIWW
ERLQGCQRIVEDWQKILMVRSLVVSPHEDMRTWLKYASLCGKSGRLALAHKTLVLLLGVD
PSRQLDHPLPTVHPQVTYAYMKNMWKSARKIDAFQHMQHFVQTMQQQAQHAIATEDQQHK
QELHKLMARCFLKLGEWQLNLQGINESTIPKVLQYYSAATEHDRSWYKAWHAWAVMNFEA
VLHYKHQNQARDEKKKLRHASGANITNATTAATTAATATTTASTEGSNSESEAESTENSP
TPSPLQKKVTEDLSKTLLMYTVPAVQGFFRSISLSRGNNLQDTLRVLTLWFDYGHWPDVN
EALVEGVKAIQIDTWLQVIPQLIARIDTPRPLVGRLIHQLLTDIGRYHPQALIYPLTVAS
KSTTTARHNAANKILKNMCEHSNTLVQQAMMVSEELIRVAILWHEMWHEGLEEASRLYFG
ERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQA
WDLYYHVFRRISKQLPQLTSLELQYVSPKLLMCRDLELAVPGTYDPNQPIIRIQSIAPSL
QVITSKQRPRKLTLMGSNGHEFVFLLKGHEDLRQDERVMQLFGLVNTLLANDPTSLRKNL
SIQRYAVIPLSTNSGLIGWVPHCDTLHALIRDYREKKKILLNIEHRIMLRMAPDYDHLTL
MQKVEVFEHAVNNTAGDDLAKLLWLKSPSSEVWFDRRTNYTRSLAVMSMVGYILGLGDRH
PSNLMLDRLSGKILHIDFGDCFEVAMTREKFPEKIPFRLTRMLTNAMEVTGLDGNYRITC
HTVMEVLREHKDSVMAVLEAFVYDPLLNWRLMDTNTKGNKRSRTRTDSYSAGQSVEILDG
VELGEPAHKKTGTTVPESIHSFIGDGLVKPEALNKKAIQIINRVRDKLTGRDFSHDDTLD
VPTQVELLIKQATSHENLCQCYIGWCPFW
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P42345
UniProtKB/Swiss-Prot Entry Name MTOR_HUMAN
PDB IDs
GenBank Gene ID L34075
GeneCard ID MTOR
GenAtlas ID MTOR
HGNC ID HGNC:3942
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed:16710414 ]
  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  4. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  5. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
  6. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. [PubMed:19369195 ]
  7. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed:18187866 ]
  8. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, 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 DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed:17344846 ]
  9. Onyango P, Lubyova B, Gardellin P, Kurzbauer R, Weith A: Molecular cloning and expression analysis of five novel genes in chromosome 1p36. Genomics. 1998 Jun 1;50(2):187-98. [PubMed:9653645 ]
  10. Kaizuka T, Hara T, Oshiro N, Kikkawa U, Yonezawa K, Takehana K, Iemura S, Natsume T, Mizushima N: Tti1 and Tel2 are critical factors in mammalian target of rapamycin complex assembly. J Biol Chem. 2010 Jun 25;285(26):20109-16. doi: 10.1074/jbc.M110.121699. Epub 2010 Apr 28. [PubMed:20427287 ]
  11. Sarbassov DD, Guertin DA, Ali SM, Sabatini DM: Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science. 2005 Feb 18;307(5712):1098-101. [PubMed:15718470 ]
  12. Hara K, Maruki Y, Long X, Yoshino K, Oshiro N, Hidayat S, Tokunaga C, Avruch J, Yonezawa K: Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action. Cell. 2002 Jul 26;110(2):177-89. [PubMed:12150926 ]
  13. Garcia-Martinez JM, Alessi DR: mTOR complex 2 (mTORC2) controls hydrophobic motif phosphorylation and activation of serum- and glucocorticoid-induced protein kinase 1 (SGK1). Biochem J. 2008 Dec 15;416(3):375-85. doi: 10.1042/BJ20081668. [PubMed:18925875 ]
  14. Brown EJ, Albers MW, Shin TB, Ichikawa K, Keith CT, Lane WS, Schreiber SL: A mammalian protein targeted by G1-arresting rapamycin-receptor complex. Nature. 1994 Jun 30;369(6483):756-8. [PubMed:8008069 ]
  15. Stover C, Endo Y, Takahashi M, Lynch NJ, Constantinescu C, Vorup-Jensen T, Thiel S, Friedl H, Hankeln T, Hall R, Gregory S, Fujita T, Schwaeble W: 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. Genes Immun. 2001 May;2(3):119-27. [PubMed:11426320 ]
  16. Chiu MI, Katz H, Berlin V: RAPT1, a mammalian homolog of yeast Tor, interacts with the FKBP12/rapamycin complex. Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12574-8. [PubMed:7809080 ]
  17. Withers DJ, Ouwens DM, Nave BT, van der Zon GC, Alarcon CM, Cardenas ME, Heitman J, Maassen JA, Shepherd PR: Expression, enzyme activity, and subcellular localization of mammalian target of rapamycin in insulin-responsive cells. Biochem Biophys Res Commun. 1997 Dec 29;241(3):704-9. [PubMed:9434772 ]
  18. Wu S, Mikhailov A, Kallo-Hosein H, Hara K, Yonezawa K, Avruch J: Characterization of ubiquilin 1, an mTOR-interacting protein. Biochim Biophys Acta. 2002 Jan 30;1542(1-3):41-56. [PubMed:11853878 ]
  19. Kim DH, Sarbassov DD, Ali SM, King JE, Latek RR, Erdjument-Bromage H, Tempst P, Sabatini DM: mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell. 2002 Jul 26;110(2):163-75. [PubMed:12150925 ]
  20. Loewith R, Jacinto E, Wullschleger S, Lorberg A, Crespo JL, Bonenfant D, Oppliger W, Jenoe P, Hall MN: Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control. Mol Cell. 2002 Sep;10(3):457-68. [PubMed:12408816 ]
  21. Desai BN, Myers BR, Schreiber SL: FKBP12-rapamycin-associated protein associates with mitochondria and senses osmotic stress via mitochondrial dysfunction. Proc Natl Acad Sci U S A. 2002 Apr 2;99(7):4319-24. [PubMed:11930000 ]
  22. Kim DH, Sarbassov DD, Ali SM, Latek RR, Guntur KV, Erdjument-Bromage H, Tempst P, Sabatini DM: GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR. Mol Cell. 2003 Apr;11(4):895-904. [PubMed:12718876 ]
  23. Sarbassov DD, Ali SM, Kim DH, Guertin DA, Latek RR, Erdjument-Bromage H, Tempst P, Sabatini DM: Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton. Curr Biol. 2004 Jul 27;14(14):1296-302. [PubMed:15268862 ]
  24. Drenan RM, Liu X, Bertram PG, Zheng XF: FKBP12-rapamycin-associated protein or mammalian target of rapamycin (FRAP/mTOR) localization in the endoplasmic reticulum and the Golgi apparatus. J Biol Chem. 2004 Jan 2;279(1):772-8. Epub 2003 Oct 24. [PubMed:14578359 ]
  25. Jacinto E, Loewith R, Schmidt A, Lin S, Ruegg MA, Hall A, Hall MN: Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive. Nat Cell Biol. 2004 Nov;6(11):1122-8. Epub 2004 Oct 3. [PubMed:15467718 ]
  26. Woo SY, Kim DH, Jun CB, Kim YM, Haar EV, Lee SI, Hegg JW, Bandhakavi S, Griffin TJ, Kim DH: PRR5, a novel component of mTOR complex 2, regulates platelet-derived growth factor receptor beta expression and signaling. J Biol Chem. 2007 Aug 31;282(35):25604-12. Epub 2007 Jun 28. [PubMed:17599906 ]
  27. Sancak Y, Peterson TR, Shaul YD, Lindquist RA, Thoreen CC, Bar-Peled L, Sabatini DM: The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1. Science. 2008 Jun 13;320(5882):1496-501. doi: 10.1126/science.1157535. Epub 2008 May 22. [PubMed:18497260 ]
  28. Peterson TR, Laplante M, Thoreen CC, Sancak Y, Kang SA, Kuehl WM, Gray NS, Sabatini DM: DEPTOR is an mTOR inhibitor frequently overexpressed in multiple myeloma cells and required for their survival. Cell. 2009 May 29;137(5):873-86. doi: 10.1016/j.cell.2009.03.046. Epub 2009 May 14. [PubMed:19446321 ]
  29. Choi J, Chen J, Schreiber SL, Clardy J: Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP. Science. 1996 Jul 12;273(5272):239-42. [PubMed:8662507 ]
  30. Liang J, Choi J, Clardy J: Refined structure of the FKBP12-rapamycin-FRB ternary complex at 2.2 A resolution. Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):736-44. [PubMed:10089303 ]