CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-029797
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Serine/threonine-protein kinase mTOR 
Protein Synonyms/Alias
  
Gene Name
 MTOR 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
250YFGERNVKGMFEVLEubiquitination[1]
271ERGPQTLKETSFNQAubiquitination[1, 2, 3, 4, 5]
371SLQVITSKQRPRKLTubiquitination[1, 5]
423NDPTSLRKNLSIQRYubiquitination[1]
488DHLTLMQKVEVFEHAubiquitination[4]
506TAGDDLAKLLWLKSPubiquitination[4]
511LAKLLWLKSPSSEVWubiquitination[4]
575EVAMTREKFPEKIPFubiquitination[1, 5]
579TREKFPEKIPFRLTRubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Kinase; Nucleotide-binding; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 754 AA 
Protein Sequence
MNFEAVLHYK HQNQARDEKK KLRHASGANI TNATTAATTA ATATTTASTE GSNSESEAES 60
TENSPTPSPL QKKVTEDLSK TLLMYTVPAV QGFFRSISLS RGNNLQDTLR VLTLWFDYGH 120
WPDVNEALVE GVKAIQIDTW LQVIPQLIAR IDTPRPLVGR LIHQLLTDIG RYHPQALIYP 180
LTVASKSTTT ARHNAANKIL KNMCEHSNTL VQQAMMVSEE LIRVAILWHE MWHEGLEEAS 240
RLYFGERNVK GMFEVLEPLH AMMERGPQTL KETSFNQAYG RDLMEAQEWC RKYMKSGNVK 300
DLTQAWDLYY HVFRRISKQL PQLTSLELQY VSPKLLMCRD LELAVPGTYD PNQPIIRIQS 360
IAPSLQVITS KQRPRKLTLM GSNGHEFVFL LKGHEDLRQD ERVMQLFGLV NTLLANDPTS 420
LRKNLSIQRY AVIPLSTNSG LIGWVPHCDT LHALIRDYRE KKKILLNIEH RIMLRMAPDY 480
DHLTLMQKVE VFEHAVNNTA GDDLAKLLWL KSPSSEVWFD RRTNYTRSLA VMSMVGYILG 540
LGDRHPSNLM LDRLSGKILH IDFGDCFEVA MTREKFPEKI PFRLTRMLTN AMEVTGLDGN 600
YRITCHTVME VLREHKDSVM AVLEAFVYDP LLNWRLMDTN TKGNKRSRTR TDSYSAGQSV 660
EILDGVELGE PAHKKTGTTV PESIHSFIGD GLVKPEALNK KAIQIINRVR DKLTGRDFSH 720
DDTLDVPTQV ELLIKQATSH ENLCQCYIGW CPFW 754 
Gene Ontology
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0070438; C:mTOR-FKBP12-rapamycin complex; IEA:Compara.
 GO:0016605; C:PML body; IEA:Compara.
 GO:0031931; C:TORC1 complex; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0008144; F:drug binding; IEA:InterPro.
 GO:0004674; F:protein serine/threonine kinase activity; IEA:Compara.
 GO:0043022; F:ribosome binding; IEA:Compara.
 GO:0071456; P:cellular response to hypoxia; IEA:Compara.
 GO:0031669; P:cellular response to nutrient levels; IEA:Compara.
 GO:0007281; P:germ cell development; IEA:Compara.
 GO:0045792; P:negative regulation of cell size; IEA:Compara.
 GO:0016242; P:negative regulation of macroautophagy; IEA:Compara.
 GO:0051534; P:negative regulation of NFAT protein import into nucleus; IEA:Compara.
 GO:0018105; P:peptidyl-serine phosphorylation; IEA:Compara.
 GO:0018107; P:peptidyl-threonine phosphorylation; IEA:Compara.
 GO:0030838; P:positive regulation of actin filament polymerization; IEA:Compara.
 GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Compara.
 GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Compara.
 GO:0010831; P:positive regulation of myotube differentiation; IEA:Compara.
 GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Compara.
 GO:0051897; P:positive regulation of protein kinase B signaling cascade; IEA:Compara.
 GO:0051496; P:positive regulation of stress fiber assembly; IEA:Compara.
 GO:0045727; P:positive regulation of translation; IEA:Compara.
 GO:0046777; P:protein autophosphorylation; IEA:Compara.
 GO:0043610; P:regulation of carbohydrate utilization; IEA:Compara.
 GO:0031998; P:regulation of fatty acid beta-oxidation; IEA:Compara.
 GO:0005979; P:regulation of glycogen biosynthetic process; IEA:Compara.
 GO:0045859; P:regulation of protein kinase activity; IEA:Compara.
 GO:0032314; P:regulation of Rac GTPase activity; IEA:Compara.
 GO:0032095; P:regulation of response to food; IEA:Compara.
 GO:0043200; P:response to amino acid stimulus; IEA:Compara.
 GO:0032868; P:response to insulin stimulus; IEA:Compara.
 GO:0031529; P:ruffle organization; IEA:Compara. 
Interpro
 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. 
Pfam
 PF02259; FAT
 PF02260; FATC
 PF00454; PI3_PI4_kinase
 PF08771; Rapamycin_bind 
SMART
 SM00146; PI3Kc 
PROSITE
 PS51189; FAT
 PS51190; FATC
 PS00915; PI3_4_KINASE_1
 PS00916; PI3_4_KINASE_2
 PS50290; PI3_4_KINASE_3 
PRINTS