MTOR_HUMAN - dbPTM
MTOR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTOR_HUMAN
UniProt AC P42345
Protein Name Serine/threonine-protein kinase mTOR
Gene Name MTOR
Organism Homo sapiens (Human).
Sequence Length 2549
Subcellular Localization 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 . Cytopl
Protein Description 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. MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins. 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. Stimulates the pyrimidine biosynthesis pathway, both by acute regulation through RPS6KB1-mediated phosphorylation of the biosynthetic enzyme CAD, and delayed regulation, through transcriptional enhancement of the pentose phosphate pathway which produces 5-phosphoribosyl-1-pyrophosphate (PRPP), an allosteric activator of CAD at a later step in synthesis, this function is dependent on the mTORC1 complex. Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 an 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'. [PubMed: 12087098]
Protein Sequence MLGTGPAAATTAATTSSNVSVLQQFASGLKSRNEETRAKAAKELQHYVTMELREMSQEESTRFYDQLNHHIFELVSSSDANERKGGILAIASLIGVEGGNATRIGRFANYLRNLLPSNDPVVMEMASKAIGRLAMAGDTFTAEYVEFEVKRALEWLGADRNEGRRHAAVLVLRELAISVPTFFFQQVQPFFDNIFVAVWDPKQAIREGAVAALRACLILTTQREPKEMQKPQWYRHTFEEAEKGFDETLAKEKGMNRDDRIHGALLILNELVRISSMEGERLREEMEEITQQQLVHDKYCKDLMGFGTKPRHITPFTSFQAVQPQQSNALVGLLGYSSHQGLMGFGTSPSPAKSTLVESRCCRDLMEEKFDQVCQWVLKCRNSKNSLIQMTILNLLPRLAAFRPSAFTDTQYLQDTMNHVLSCVKKEKERTAAFQALGLLSVAVRSEFKVYLPRVLDIIRAALPPKDFAHKRQKAMQVDATVFTCISMLARAMGPGIQQDIKELLEPMLAVGLSPALTAVLYDLSRQIPQLKKDIQDGLLKMLSLVLMHKPLRHPGMPKGLAHQLASPGLTTLPEASDVGSITLALRTLGSFEFEGHSLTQFVRHCADHFLNSEHKEIRMEAARTCSRLLTPSIHLISGHAHVVSQTAVQVVADVLSKLLVVGITDPDPDIRYCVLASLDERFDAHLAQAENLQALFVALNDQVFEIRELAICTVGRLSSMNPAFVMPFLRKMLIQILTELEHSGIGRIKEQSARMLGHLVSNAPRLIRPYMEPILKALILKLKDPDPDPNPGVINNVLATIGELAQVSGLEMRKWVDELFIIIMDMLQDSSLLAKRQVALWTLGQLVASTGYVVEPYRKYPTLLEVLLNFLKTEQNQGTRREAIRVLGLLGALDPYKHKVNIGMIDQSRDASAVSLSESKSSQDSSDYSTSEMLVNMGNLPLDEFYPAVSMVALMRIFRDQSLSHHHTMVVQAITFIFKSLGLKCVQFLPQVMPTFLNVIRVCDGAIREFLFQQLGMLVSFVKSHIRPYMDEIVTLMREFWVMNTSIQSTIILLIEQIVVALGGEFKLYLPQLIPHMLRVFMHDNSPGRIVSIKLLAAIQLFGANLDDYLHLLLPPIVKLFDAPEAPLPSRKAALETVDRLTESLDFTDYASRIIHPIVRTLDQSPELRSTAMDTLSSLVFQLGKKYQIFIPMVNKVLVRHRINHQRYDVLICRIVKGYTLADEEEDPLIYQHRMLRSGQGDALASGPVETGPMKKLHVSTINLQKAWGAARRVSKDDWLEWLRRLSLELLKDSSSPSLRSCWALAQAYNPMARDLFNAAFVSCWSELNEDQQDELIRSIELALTSQDIAEVTQTLLNLAEFMEHSDKGPLPLRDDNGIVLLGERAAKCRAYAKALHYKELEFQKGPTPAILESLISINNKLQQPEAAAGVLEYAMKHFGELEIQATWYEKLHEWEDALVAYDKKMDTNKDDPELMLGRMRCLEALGEWGQLHQQCCEKWTLVNDETQAKMARMAAAAAWGLGQWDSMEEYTCMIPRDTHDGAFYRAVLALHQDLFSLAQQCIDKARDLLDAELTAMAGESYSRAYGAMVSCHMLSELEEVIQYKLVPERREIIRQIWWERLQGCQRIVEDWQKILMVRSLVVSPHEDMRTWLKYASLCGKSGRLALAHKTLVLLLGVDPSRQLDHPLPTVHPQVTYAYMKNMWKSARKIDAFQHMQHFVQTMQQQAQHAIATEDQQHKQELHKLMARCFLKLGEWQLNLQGINESTIPKVLQYYSAATEHDRSWYKAWHAWAVMNFEAVLHYKHQNQARDEKKKLRHASGANITNATTAATTAATATTTASTEGSNSESEAESTENSPTPSPLQKKVTEDLSKTLLMYTVPAVQGFFRSISLSRGNNLQDTLRVLTLWFDYGHWPDVNEALVEGVKAIQIDTWLQVIPQLIARIDTPRPLVGRLIHQLLTDIGRYHPQALIYPLTVASKSTTTARHNAANKILKNMCEHSNTLVQQAMMVSEELIRVAILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISKQLPQLTSLELQYVSPKLLMCRDLELAVPGTYDPNQPIIRIQSIAPSLQVITSKQRPRKLTLMGSNGHEFVFLLKGHEDLRQDERVMQLFGLVNTLLANDPTSLRKNLSIQRYAVIPLSTNSGLIGWVPHCDTLHALIRDYREKKKILLNIEHRIMLRMAPDYDHLTLMQKVEVFEHAVNNTAGDDLAKLLWLKSPSSEVWFDRRTNYTRSLAVMSMVGYILGLGDRHPSNLMLDRLSGKILHIDFGDCFEVAMTREKFPEKIPFRLTRMLTNAMEVTGLDGNYRITCHTVMEVLREHKDSVMAVLEAFVYDPLLNWRLMDTNTKGNKRSRTRTDSYSAGQSVEILDGVELGEPAHKKTGTTVPESIHSFIGDGLVKPEALNKKAIQIINRVRDKLTGRDFSHDDTLDVPTQVELLIKQATSHENLCQCYIGWCPFW
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MLGTGPAA
-------CCCCCCCC
35.8722814378
4Phosphorylation----MLGTGPAAATT
----CCCCCCCCCCC
53.2624532841
10PhosphorylationGTGPAAATTAATTSS
CCCCCCCCCCCCCCC
16.5525954137
11PhosphorylationTGPAAATTAATTSSN
CCCCCCCCCCCCCCC
15.0125954137
14PhosphorylationAAATTAATTSSNVSV
CCCCCCCCCCCCHHH
25.4221964256
15PhosphorylationAATTAATTSSNVSVL
CCCCCCCCCCCHHHH
25.9820071362
16PhosphorylationATTAATTSSNVSVLQ
CCCCCCCCCCHHHHH
18.6325954137
16UbiquitinationATTAATTSSNVSVLQ
CCCCCCCCCCHHHHH
18.6322817900
17PhosphorylationTTAATTSSNVSVLQQ
CCCCCCCCCHHHHHH
38.8820071362
24UbiquitinationSNVSVLQQFASGLKS
CCHHHHHHHHHHCCC
31.5422817900
26UbiquitinationVSVLQQFASGLKSRN
HHHHHHHHHHCCCCC
9.8022817900
27PhosphorylationSVLQQFASGLKSRNE
HHHHHHHHHCCCCCH
46.0420071362
31PhosphorylationQFASGLKSRNEETRA
HHHHHCCCCCHHHHH
45.4325954137
42UbiquitinationETRAKAAKELQHYVT
HHHHHHHHHHHHHHH
64.91-
60PhosphorylationREMSQEESTRFYDQL
HHCCHHHHHHHHHHH
24.9126657352
77PhosphorylationHIFELVSSSDANERK
HHHHHHCCCCCCCCC
25.4326657352
78PhosphorylationIFELVSSSDANERKG
HHHHHCCCCCCCCCC
32.9826657352
84UbiquitinationSSDANERKGGILAIA
CCCCCCCCCCEEEEE
56.14-
92PhosphorylationGGILAIASLIGVEGG
CCEEEEEHHHCCCCC
17.88-
102PhosphorylationGVEGGNATRIGRFAN
CCCCCCHHHHHHHHH
27.15-
110PhosphorylationRIGRFANYLRNLLPS
HHHHHHHHHHHHCCC
12.0121712546
128UbiquitinationVVMEMASKAIGRLAM
HHHHHHHHHHHHHHH
34.19-
230AcetylationREPKEMQKPQWYRHT
CCCHHHCCCHHHHHH
37.5525953088
230MalonylationREPKEMQKPQWYRHT
CCCHHHCCCHHHHHH
37.5526320211
230UbiquitinationREPKEMQKPQWYRHT
CCCHHHCCCHHHHHH
37.5529967540
243UbiquitinationHTFEEAEKGFDETLA
HHHHHHHHCCCHHHH
72.4421906983
248PhosphorylationAEKGFDETLAKEKGM
HHHCCCHHHHHHCCC
33.5826091039
251UbiquitinationGFDETLAKEKGMNRD
CCCHHHHHHCCCCCH
64.1721906983
253UbiquitinationDETLAKEKGMNRDDR
CHHHHHHCCCCCHHH
63.8522817900
298UbiquitinationQQQLVHDKYCKDLMG
HHHHHCHHHHHHHCC
37.36-
301UbiquitinationLVHDKYCKDLMGFGT
HHCHHHHHHHCCCCC
51.2929967540
308PhosphorylationKDLMGFGTKPRHITP
HHHCCCCCCCCCCCC
35.30-
309AcetylationDLMGFGTKPRHITPF
HHCCCCCCCCCCCCC
40.2027452117
309MalonylationDLMGFGTKPRHITPF
HHCCCCCCCCCCCCC
40.2026320211
309UbiquitinationDLMGFGTKPRHITPF
HHCCCCCCCCCCCCC
40.2032015554
314PhosphorylationGTKPRHITPFTSFQA
CCCCCCCCCCCCCCC
13.26-
369UbiquitinationCRDLMEEKFDQVCQW
HHHHHHHHHHHHHHH
40.7229967540
379UbiquitinationQVCQWVLKCRNSKNS
HHHHHHHHCCCCCCC
22.87-
384UbiquitinationVLKCRNSKNSLIQMT
HHHCCCCCCCHHHHH
54.85-
426UbiquitinationHVLSCVKKEKERTAA
HHHHHHHHHHHHHHH
54.33-
449UbiquitinationVAVRSEFKVYLPRVL
HHHHHHCCHHHHHHH
26.39-
482UbiquitinationAMQVDATVFTCISML
HHHCCHHHHHHHHHH
3.9221890473
484UbiquitinationQVDATVFTCISMLAR
HCCHHHHHHHHHHHH
12.4722817900
5322-HydroxyisobutyrylationSRQIPQLKKDIQDGL
HHCCHHHHHHHHHHH
43.05-
533UbiquitinationRQIPQLKKDIQDGLL
HCCHHHHHHHHHHHH
69.5229967540
567PhosphorylationGLAHQLASPGLTTLP
CHHHHHCCCCCCCCC
28.2629255136
571PhosphorylationQLASPGLTTLPEASD
HHCCCCCCCCCCCCC
32.0029255136
572PhosphorylationLASPGLTTLPEASDV
HCCCCCCCCCCCCCH
45.4129255136
577PhosphorylationLTTLPEASDVGSITL
CCCCCCCCCHHHHHH
31.0327251275
581PhosphorylationPEASDVGSITLALRT
CCCCCHHHHHHEEHH
16.5527251275
583PhosphorylationASDVGSITLALRTLG
CCCHHHHHHEEHHCC
14.0027251275
616UbiquitinationHFLNSEHKEIRMEAA
HHHCCCCHHHHHHHH
51.27-
631PhosphorylationRTCSRLLTPSIHLIS
HHHHHHHCCCEEEEC
21.41-
665PhosphorylationKLLVVGITDPDPDIR
HHCCCCCCCCCCCHH
35.2320071362
671UbiquitinationITDPDPDIRYCVLAS
CCCCCCCHHHHHHHC
4.0421890473
673UbiquitinationDPDPDIRYCVLASLD
CCCCCHHHHHHHCHH
6.3022817900
714PhosphorylationIRELAICTVGRLSSM
HHHHHHHHHHHHHCC
21.6322210691
719PhosphorylationICTVGRLSSMNPAFV
HHHHHHHHCCCHHHH
26.6122210691
720PhosphorylationCTVGRLSSMNPAFVM
HHHHHHHCCCHHHHH
27.4622210691
770UbiquitinationNAPRLIRPYMEPILK
CCCHHCHHHHHHHHH
26.3123503661
771UbiquitinationAPRLIRPYMEPILKA
CCHHCHHHHHHHHHH
12.3123503661
777UbiquitinationPYMEPILKALILKLK
HHHHHHHHHHHHHCC
41.70-
802UbiquitinationINNVLATIGELAQVS
HHHHHHHHHHHHHHC
3.1622817900
831PhosphorylationIMDMLQDSSLLAKRQ
HHHHCCCCHHHHHHH
15.2123090842
832PhosphorylationMDMLQDSSLLAKRQV
HHHCCCCHHHHHHHH
35.3723090842
840UbiquitinationLLAKRQVALWTLGQL
HHHHHHHHHHHHHHH
6.7722817900
841UbiquitinationLAKRQVALWTLGQLV
HHHHHHHHHHHHHHH
3.6422817900
861PhosphorylationVVEPYRKYPTLLEVL
CCCCHHHCHHHHHHH
7.7624719451
877UbiquitinationNFLKTEQNQGTRREA
HHHHHHCCCCCHHHH
35.7021890473
880PhosphorylationKTEQNQGTRREAIRV
HHHCCCCCHHHHHHH
19.4524719451
898UbiquitinationLGALDPYKHKVNIGM
HHHCCCCCCCCCEEC
42.1921906983
898UbiquitinationLGALDPYKHKVNIGM
HHHCCCCCCCCCEEC
42.1921890473
900UbiquitinationALDPYKHKVNIGMID
HCCCCCCCCCEECCC
32.5921906983
909PhosphorylationNIGMIDQSRDASAVS
CEECCCCCCCCCCCC
28.5120071362
913PhosphorylationIDQSRDASAVSLSES
CCCCCCCCCCCCCCC
33.2323312004
916PhosphorylationSRDASAVSLSESKSS
CCCCCCCCCCCCCCC
26.3720873877
918PhosphorylationDASAVSLSESKSSQD
CCCCCCCCCCCCCCC
32.1120071362
920PhosphorylationSAVSLSESKSSQDSS
CCCCCCCCCCCCCCC
34.1726437602
959UbiquitinationMVALMRIFRDQSLSH
HHHHHHHHCCCCCCC
5.0623503661
960UbiquitinationVALMRIFRDQSLSHH
HHHHHHHCCCCCCCC
38.3923503661
984UbiquitinationFIFKSLGLKCVQFLP
HHHHHCCCHHHHHHH
4.7523503661
990UbiquitinationGLKCVQFLPQVMPTF
CCHHHHHHHHHHHHH
1.3022817900
991UbiquitinationLKCVQFLPQVMPTFL
CHHHHHHHHHHHHHH
26.4722817900
1029UbiquitinationFVKSHIRPYMDEIVT
HHHHCCHHHHHHHHH
28.3522817900
1030UbiquitinationVKSHIRPYMDEIVTL
HHHCCHHHHHHHHHH
13.8322817900
1066UbiquitinationIVVALGGEFKLYLPQ
HHHHHCCCHHHHHHH
37.5021890473
1095UbiquitinationPGRIVSIKLLAAIQL
CCCCHHHHHHHHHHH
29.9123503661
1131PhosphorylationAPEAPLPSRKAALET
CCCCCCCCHHHHHHH
54.84-
1133UbiquitinationEAPLPSRKAALETVD
CCCCCCHHHHHHHHH
42.2029967540
1143PhosphorylationLETVDRLTESLDFTD
HHHHHHHHHCCCCCH
25.1524114839
1145PhosphorylationTVDRLTESLDFTDYA
HHHHHHHCCCCCHHH
28.1824114839
1149PhosphorylationLTESLDFTDYASRII
HHHCCCCCHHHHHHH
27.9729759185
1151PhosphorylationESLDFTDYASRIIHP
HCCCCCHHHHHHHHH
11.9229759185
1153PhosphorylationLDFTDYASRIIHPIV
CCCCHHHHHHHHHHH
20.1324114839
1162PhosphorylationIIHPIVRTLDQSPEL
HHHHHHHCCCCCHHH
24.6422167270
1166PhosphorylationIVRTLDQSPELRSTA
HHHCCCCCHHHHHHH
21.7322167270
1171PhosphorylationDQSPELRSTAMDTLS
CCCHHHHHHHHHHHH
32.8921406692
1172PhosphorylationQSPELRSTAMDTLSS
CCHHHHHHHHHHHHH
21.4021406692
1173UbiquitinationSPELRSTAMDTLSSL
CHHHHHHHHHHHHHH
8.6323503661
1176PhosphorylationLRSTAMDTLSSLVFQ
HHHHHHHHHHHHHHH
18.5621406692
1178PhosphorylationSTAMDTLSSLVFQLG
HHHHHHHHHHHHHHC
24.5821406692
1179PhosphorylationTAMDTLSSLVFQLGK
HHHHHHHHHHHHHCC
31.5021406692
1179UbiquitinationTAMDTLSSLVFQLGK
HHHHHHHHHHHHHCC
31.5022817900
1186UbiquitinationSLVFQLGKKYQIFIP
HHHHHHCCEEEEEEE
57.8323503661
1187UbiquitinationLVFQLGKKYQIFIPM
HHHHHCCEEEEEEEC
40.3623503661
1188PhosphorylationVFQLGKKYQIFIPMV
HHHHCCEEEEEEECH
15.44-
1197UbiquitinationIFIPMVNKVLVRHRI
EEEECHHHHHHHHCC
26.07-
1218AcetylationVLICRIVKGYTLADE
EEEEEEECCCCCCCC
43.7719608861
1218MalonylationVLICRIVKGYTLADE
EEEEEEECCCCCCCC
43.7726320211
1218UbiquitinationVLICRIVKGYTLADE
EEEEEEECCCCCCCC
43.7721906983
1232PhosphorylationEEEDPLIYQHRMLRS
CCCCCCHHHHCCHHC
13.1221945579
1239PhosphorylationYQHRMLRSGQGDALA
HHHCCHHCCCCCCCC
31.3528555341
1239UbiquitinationYQHRMLRSGQGDALA
HHHCCHHCCCCCCCC
31.3521890473
1255SulfoxidationGPVETGPMKKLHVST
CCCCCCCCCEEEEEE
6.7321406390
1256AcetylationPVETGPMKKLHVSTI
CCCCCCCCEEEEEEE
56.1526051181
1256UbiquitinationPVETGPMKKLHVSTI
CCCCCCCCEEEEEEE
56.1521906983
1257UbiquitinationVETGPMKKLHVSTIN
CCCCCCCEEEEEEEE
37.2622817900
1261PhosphorylationPMKKLHVSTINLQKA
CCCEEEEEEEEHHHH
16.9025159151
1262PhosphorylationMKKLHVSTINLQKAW
CCEEEEEEEEHHHHH
16.8830266825
1267UbiquitinationVSTINLQKAWGAARR
EEEEEHHHHHHCCCC
49.63-
1284UbiquitinationKDDWLEWLRRLSLEL
HHHHHHHHHHHHHHH
1.3423503661
1288PhosphorylationLEWLRRLSLELLKDS
HHHHHHHHHHHHCCC
20.27-
1293UbiquitinationRLSLELLKDSSSPSL
HHHHHHHCCCCCHHH
69.0921890473
1293UbiquitinationRLSLELLKDSSSPSL
HHHHHHHCCCCCHHH
69.0921890473
1296PhosphorylationLELLKDSSSPSLRSC
HHHHCCCCCHHHHHH
57.3020068231
1297PhosphorylationELLKDSSSPSLRSCW
HHHCCCCCHHHHHHH
23.5920068231
1299PhosphorylationLKDSSSPSLRSCWAL
HCCCCCHHHHHHHHH
38.0620068231
1395UbiquitinationAKCRAYAKALHYKEL
HHHHHHHHHHCHHHH
38.5129967540
1400UbiquitinationYAKALHYKELEFQKG
HHHHHCHHHHCCCCC
45.1123503661
1406UbiquitinationYKELEFQKGPTPAIL
HHHHCCCCCCCHHHH
72.6521906983
1409PhosphorylationLEFQKGPTPAILESL
HCCCCCCCHHHHHHH
33.7427251275
1415PhosphorylationPTPAILESLISINNK
CCHHHHHHHHHCCCC
27.7925850435
1418PhosphorylationAILESLISINNKLQQ
HHHHHHHHCCCCCCC
25.2629507054
1428UbiquitinationNKLQQPEAAAGVLEY
CCCCCHHHHHHHHHH
14.8621890473
1465UbiquitinationDALVAYDKKMDTNKD
HHHHHHHHCCCCCCC
37.0029967540
1466UbiquitinationALVAYDKKMDTNKDD
HHHHHHHCCCCCCCC
38.8329967540
1471UbiquitinationDKKMDTNKDDPELML
HHCCCCCCCCHHHHH
66.6529967540
1500UbiquitinationLHQQCCEKWTLVNDE
HHHHHHHHCCCCCHH
31.4029967540
1502PhosphorylationQQCCEKWTLVNDETQ
HHHHHHCCCCCHHHH
31.71-
1511UbiquitinationVNDETQAKMARMAAA
CCHHHHHHHHHHHHH
24.2323503661
1566UbiquitinationLAQQCIDKARDLLDA
HHHHHHHHHHHHHHH
25.96-
1635UbiquitinationRIVEDWQKILMVRSL
HHHHHHHHHHHHHEE
33.29-
1650UbiquitinationVVSPHEDMRTWLKYA
CCCCCHHHHHHHHHH
3.6127667366
1655UbiquitinationEDMRTWLKYASLCGK
HHHHHHHHHHHHCCH
30.2721890473
1655UbiquitinationEDMRTWLKYASLCGK
HHHHHHHHHHHHCCH
30.2721890473
1662UbiquitinationKYASLCGKSGRLALA
HHHHHCCHHHHHHHH
49.0629967540
1745UbiquitinationQHKQELHKLMARCFL
HHHHHHHHHHHHHHH
53.2129967540
1804PhosphorylationNFEAVLHYKHQNQAR
CHHHHHHHHHHHCCH
13.1520860994
1821PhosphorylationKKKLRHASGANITNA
HHHHHHHCCCCCCCC
32.1120873877
1826PhosphorylationHASGANITNATTAAT
HHCCCCCCCCHHHHH
20.7127080861
1829PhosphorylationGANITNATTAATTAA
CCCCCCCHHHHHHCC
21.0220873877
1830PhosphorylationANITNATTAATTAAT
CCCCCCHHHHHHCCC
16.3427080861
1833PhosphorylationTNATTAATTAATATT
CCCHHHHHHCCCCCC
17.9520873877
1834PhosphorylationNATTAATTAATATTT
CCHHHHHHCCCCCCC
15.0127080861
1837PhosphorylationTAATTAATATTTAST
HHHHHCCCCCCCCCC
23.2827080861
1839PhosphorylationATTAATATTTASTEG
HHHCCCCCCCCCCCC
21.9620873877
1839UbiquitinationATTAATATTTASTEG
HHHCCCCCCCCCCCC
21.9622817900
1840PhosphorylationTTAATATTTASTEGS
HHCCCCCCCCCCCCC
20.2120873877
1841PhosphorylationTAATATTTASTEGSN
HCCCCCCCCCCCCCC
17.7920873877
1843PhosphorylationATATTTASTEGSNSE
CCCCCCCCCCCCCCH
25.5420873877
1844PhosphorylationTATTTASTEGSNSES
CCCCCCCCCCCCCHH
41.7327080861
1847PhosphorylationTTASTEGSNSESEAE
CCCCCCCCCCHHHHC
30.8318691976
1849PhosphorylationASTEGSNSESEAEST
CCCCCCCCHHHHCCC
44.1718691976
1851PhosphorylationTEGSNSESEAESTEN
CCCCCCHHHHCCCCC
41.7620873877
1855PhosphorylationNSESEAESTENSPTP
CCHHHHCCCCCCCCC
48.3327080861
1856PhosphorylationSESEAESTENSPTPS
CHHHHCCCCCCCCCC
30.5920873877
1859PhosphorylationEAESTENSPTPSPLQ
HHCCCCCCCCCCHHH
24.7420873877
1861PhosphorylationESTENSPTPSPLQKK
CCCCCCCCCCHHHHH
35.9027080861
1863PhosphorylationTENSPTPSPLQKKVT
CCCCCCCCHHHHHHC
40.4920873877
1867UbiquitinationPTPSPLQKKVTEDLS
CCCCHHHHHHCHHHH
57.8223503661
1870PhosphorylationSPLQKKVTEDLSKTL
CHHHHHHCHHHHHHH
32.4419835603
1874PhosphorylationKKVTEDLSKTLLMYT
HHHCHHHHHHHHHHH
35.6019835603
1876PhosphorylationVTEDLSKTLLMYTVP
HCHHHHHHHHHHHHH
23.0319835603
1880PhosphorylationLSKTLLMYTVPAVQG
HHHHHHHHHHHHHHH
12.4519835603
1881PhosphorylationSKTLLMYTVPAVQGF
HHHHHHHHHHHHHHH
13.1720873877
1885UbiquitinationLMYTVPAVQGFFRSI
HHHHHHHHHHHHHHH
4.7223503661
1890UbiquitinationPAVQGFFRSISLSRG
HHHHHHHHHHHCCCC
30.7123503661
1893PhosphorylationQGFFRSISLSRGNNL
HHHHHHHHCCCCCCH
22.8724719451
1948PhosphorylationQLIARIDTPRPLVGR
HHHHHCCCCCHHHHH
20.87-
1958UbiquitinationPLVGRLIHQLLTDIG
HHHHHHHHHHHHHHH
19.4824816145
1982PhosphorylationPLTVASKSTTTARHN
EEEECCCCCHHHHHH
28.6120860994
1985PhosphorylationVASKSTTTARHNAAN
ECCCCCHHHHHHHHH
23.0620860994
1993UbiquitinationARHNAANKILKNMCE
HHHHHHHHHHHHHHH
44.6929967540
2021UbiquitinationEELIRVAILWHEMWH
HHHHHHHHHHHHHHH
3.8124816145
2032PhosphorylationEMWHEGLEEASRLYF
HHHHHCHHHHHHHHC
63.4732645325
2045UbiquitinationYFGERNVKGMFEVLE
HCCCCCCCHHHHHHH
48.48-
2056UbiquitinationEVLEPLHAMMERGPQ
HHHHHHHHHHHHCCC
13.5023503661
2062PhosphorylationHAMMERGPQTLKETS
HHHHHHCCCCHHHCC
30.1533259812
2066MalonylationERGPQTLKETSFNQA
HHCCCCHHHCCHHHH
63.4326320211
2066UbiquitinationERGPQTLKETSFNQA
HHCCCCHHHCCHHHH
63.4327667366
2068PhosphorylationGPQTLKETSFNQAYG
CCCCHHHCCHHHHHC
36.7128857561
2069PhosphorylationPQTLKETSFNQAYGR
CCCHHHCCHHHHHCH
24.2428857561
2074UbiquitinationETSFNQAYGRDLMEA
HCCHHHHHCHHHHHH
11.7023503661
2079UbiquitinationQAYGRDLMEAQEWCR
HHHCHHHHHHHHHHH
4.7423503661
2088PhosphorylationAQEWCRKYMKSGNVK
HHHHHHHHHHHCCHH
7.1623403867
2147UbiquitinationVPGTYDPNQPIIRIQ
CCCCCCCCCCEEEEE
58.3124816145
2155PhosphorylationQPIIRIQSIAPSLQV
CCEEEEECCCCCCEE
20.53-
2159PhosphorylationRIQSIAPSLQVITSK
EEECCCCCCEEECCC
23.5521576368
2164PhosphorylationAPSLQVITSKQRPRK
CCCCEEECCCCCCCE
30.8921576368
2166UbiquitinationSLQVITSKQRPRKLT
CCEEECCCCCCCEEE
41.50-
2173PhosphorylationKQRPRKLTLMGSNGH
CCCCCEEEEECCCCC
20.1024247430
2207PhosphorylationQLFGLVNTLLANDPT
HHHHHHHHHHHCCCC
18.7024043423
2210UbiquitinationGLVNTLLANDPTSLR
HHHHHHHHCCCCHHH
22.8424816145
2214PhosphorylationTLLANDPTSLRKNLS
HHHHCCCCHHHHCCC
43.1724043423
2215PhosphorylationLLANDPTSLRKNLSI
HHHCCCCHHHHCCCC
31.4024043423
2218UbiquitinationNDPTSLRKNLSIQRY
CCCCHHHHCCCCCEE
68.48-
2221PhosphorylationTSLRKNLSIQRYAVI
CHHHHCCCCCEEEEE
26.5224719451
2283UbiquitinationDHLTLMQKVEVFEHA
CCCHHHHHHHHHHHH
26.7923503661
2301UbiquitinationTAGDDLAKLLWLKSP
CCCCHHHHHHHHCCC
51.9523503661
2306UbiquitinationLAKLLWLKSPSSEVW
HHHHHHHCCCCCCCE
49.0623503661
2370UbiquitinationEVAMTREKFPEKIPF
HHHHCCCCCCCCCCH
64.03-
2374UbiquitinationTREKFPEKIPFRLTR
CCCCCCCCCCHHHHH
56.7824816145
2380PhosphorylationEKIPFRLTRMLTNAM
CCCCHHHHHHHCCCC
15.13-
2434PhosphorylationLNWRLMDTNTKGNKR
CCEEECCCCCCCCCC
30.72-
2436PhosphorylationWRLMDTNTKGNKRSR
EEECCCCCCCCCCCC
42.2821955146
2437UbiquitinationRLMDTNTKGNKRSRT
EECCCCCCCCCCCCC
63.6624816145
2442PhosphorylationNTKGNKRSRTRTDSY
CCCCCCCCCCCCCCC
39.3422322096
2444PhosphorylationKGNKRSRTRTDSYSA
CCCCCCCCCCCCCCC
38.8822322096
2446PhosphorylationNKRSRTRTDSYSAGQ
CCCCCCCCCCCCCCC
28.7830266825
2448PhosphorylationRSRTRTDSYSAGQSV
CCCCCCCCCCCCCCE
22.0019664994
2449PhosphorylationSRTRTDSYSAGQSVE
CCCCCCCCCCCCCEE
12.8327273156
2450PhosphorylationRTRTDSYSAGQSVEI
CCCCCCCCCCCCEEE
29.8530266825
2454PhosphorylationDSYSAGQSVEILDGV
CCCCCCCCEEEECCC
22.3119664994
2471PhosphorylationGEPAHKKTGTTVPES
CCCCHHCCCCCCCHH
44.5622322096
2473PhosphorylationPAHKKTGTTVPESIH
CCHHCCCCCCCHHHH
29.8322322096
2474PhosphorylationAHKKTGTTVPESIHS
CHHCCCCCCCHHHHH
35.0922322096
2478PhosphorylationTGTTVPESIHSFIGD
CCCCCCHHHHHHHCC
21.3822322096
2481PhosphorylationTVPESIHSFIGDGLV
CCCHHHHHHHCCCCC
19.5222322096
2489UbiquitinationFIGDGLVKPEALNKK
HHCCCCCCHHHCCHH
42.0329967540
2496UbiquitinationKPEALNKKAIQIINR
CHHHCCHHHHHHHHH
50.0429967540
2509PhosphorylationNRVRDKLTGRDFSHD
HHHHHHHCCCCCCCC
35.5920068231
2514PhosphorylationKLTGRDFSHDDTLDV
HHCCCCCCCCCCCCC
30.2329759185
2518PhosphorylationRDFSHDDTLDVPTQV
CCCCCCCCCCCCHHH
30.8029759185

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
1415SPhosphorylationKinaseCHUKO15111
GPS
1418SPhosphorylationKinaseIKKAO15111
PSP
2173TPhosphorylationKinaseAKT1P31749
Uniprot
2446TPhosphorylationKinaseAKT1P31749
PSP
2446TPhosphorylationKinaseKS6B1P23443
PhosphoELM
2446TPhosphorylationKinasePKB_GROUP-PhosphoELM
2446TPhosphorylationKinaseP70-SUBFAMILY-GPS
2446TPhosphorylationKinaseAKT-FAMILY-GPS
2448SPhosphorylationKinaseAKT1P31749
PSP
2448SPhosphorylationKinasePKB_GROUP-PhosphoELM
2448SPhosphorylationKinaseP70-SUBFAMILY-GPS
2448SPhosphorylationKinaseAKT-FAMILY-GPS
2448SPhosphorylationKinaseKS6B1P23443
PhosphoELM
2454SPhosphorylationKinaseMTORP42345
PSP
2473TPhosphorylationKinaseMTORP42345
PSP
2474TPhosphorylationKinaseMTORP42345
PSP
2478SPhosphorylationKinaseMTORP42345
PSP
2481SPhosphorylationKinaseMTORP42345
PSP
-KUbiquitinationE3 ubiquitin ligaseTRAF6Q9Y4K3
PMID:23911927
-KUbiquitinationE3 ubiquitin ligaseFBXW7Q969H0
PMID:18787170

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1261SPhosphorylation

19487463
2159SPhosphorylation

21576368
2164TPhosphorylation

21576368
2173TPhosphorylation

24247430

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MTOR_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RICTR_HUMANRICTORphysical
15467718
RPTOR_HUMANRPTORphysical
15467718
RICTR_HUMANRICTORphysical
15268862
RPTOR_HUMANRPTORphysical
15268862
ABL1_HUMANABL1physical
10753870
4EBP1_HUMANEIF4EBP1physical
12747827
4EBP1_HUMANEIF4EBP1physical
12150925
4EBP1_HUMANEIF4EBP1physical
15854902
4EBP1_HUMANEIF4EBP1physical
12150926
4EBP1_HUMANEIF4EBP1physical
10971657
4EBP1_HUMANEIF4EBP1physical
9465032
FKB1A_HUMANFKBP1Aphysical
15284440
FKB1A_HUMANFKBP1Aphysical
15796538
MTOR_HUMANMTORphysical
16870609
PA2G4_HUMANPA2G4physical
15896331
PDK1_HUMANPDK1genetic
10567431
PROP_HUMANCFPphysical
11733037
PLD2_HUMANPLD2physical
16837165
2ABA_HUMANPPP2R2Aphysical
10200280
KPCD_HUMANPRKCDphysical
10698949
RAP1A_HUMANRAP1Aphysical
15854902
RHEB_HUMANRHEBphysical
15854902
KS6B1_HUMANRPS6KB1physical
10567431
KS6B1_HUMANRPS6KB1physical
15854902
KS6B1_HUMANRPS6KB1physical
15896331
KS6B1_HUMANRPS6KB1physical
15809305
KS6B1_HUMANRPS6KB1physical
11914378
KS6B1_HUMANRPS6KB1physical
12150925
KS6B1_HUMANRPS6KB1physical
14679009
KS6B1_HUMANRPS6KB1physical
16922504
KS6B1_HUMANRPS6KB1physical
10971657
KS6B1_HUMANRPS6KB1physical
9465032
KS6B1_HUMANRPS6KB1physical
16183647
CLIP1_HUMANCLIP1physical
12231510
STAT1_HUMANSTAT1physical
12807916
STAT3_HUMANSTAT3physical
10660304
STAT3_HUMANSTAT3physical
15522880
TERT_HUMANTERTphysical
15843522
EIF3F_HUMANEIF3Fphysical
16541103
GEPH_HUMANGPHNphysical
10325225
RHEB_MOUSERhebphysical
16631613
STAT3_RATStat3physical
12796477
UBQL1_HUMANUBQLN1physical
11853878
RPTOR_HUMANRPTORphysical
15459249
RPTOR_HUMANRPTORphysical
15066126
RPTOR_HUMANRPTORphysical
12719976
RPTOR_HUMANRPTORphysical
12665511
RPTOR_HUMANRPTORphysical
12150926
RPTOR_HUMANRPTORphysical
12150925
RPTOR_HUMANRPTORphysical
16847060
RPTOR_HUMANRPTORphysical
16837165
RPTOR_HUMANRPTORphysical
16798736
RPTOR_HUMANRPTORphysical
16919458
RPTOR_HUMANRPTORphysical
16631613
RPTOR_HUMANRPTORphysical
16603397
RPTOR_HUMANRPTORphysical
16354680
RPTOR_HUMANRPTORphysical
16183647
RPTOR_HUMANRPTORphysical
17043309
LST8_HUMANMLST8physical
16183647
LST8_HUMANMLST8physical
15066126
LST8_HUMANMLST8physical
12719976
KS6B1_MOUSERps6kb1physical
16452250
RICTR_HUMANRICTORphysical
16919458
RICTR_HUMANRICTORphysical
16603397
RICTR_HUMANRICTORphysical
16183647
RICTR_HUMANRICTORphysical
17043309
MTOR_HUMANMTORphysical
17360675
RPTOR_HUMANRPTORphysical
20427287
TTI1_SCHPOtti1physical
20427287
TTI1_HUMANTTI1physical
20427287
RICTR_HUMANRICTORphysical
20427287
LST8_HUMANMLST8physical
20427287
DPTOR_HUMANDEPTORphysical
22017877
PRR5_HUMANPRR5physical
17461779
RPTOR_HUMANRPTORphysical
17461779
AKT1_HUMANAKT1physical
21045808
RICTR_HUMANRICTORphysical
21045808
KPCA_HUMANPRKCAphysical
21045808
RL23_HUMANRPL23physical
21045808
RS6_HUMANRPS6physical
21045808
RPTOR_HUMANRPTORphysical
21045808
RL23A_HUMANRPL23Aphysical
21045808
RL26_HUMANRPL26physical
21045808
RL5_HUMANRPL5physical
21045808
TELO2_HUMANTELO2physical
18160036
KS6B1_HUMANRPS6KB1physical
22544753
USP9X_HUMANUSP9Xphysical
22544753
RPTOR_HUMANRPTORphysical
22544753
RICTR_HUMANRICTORphysical
22544753
TTI1_HUMANTTI1physical
22544753
RUVB2_HUMANRUVBL2physical
22544753
RUVB1_HUMANRUVBL1physical
22544753
AKT1_HUMANAKT1physical
15718470
RPTOR_HUMANRPTORphysical
22356909
KS6B1_HUMANRPS6KB1physical
17386266
AKTS1_HUMANAKT1S1physical
17386266
RPTOR_HUMANRPTORphysical
17386266
SIN1_HUMANMAPKAP1physical
17043309
IRS1_HUMANIRS1physical
16354680
KS6B1_HUMANRPS6KB1physical
15066126
4EBP1_HUMANEIF4EBP1physical
15066126
4EBP1_HUMANEIF4EBP1physical
16798736
4EBP2_HUMANEIF4EBP2physical
16798736
LST8_HUMANMLST8physical
16798736
LST8_HUMANMLST8physical
15459249
4EBP1_HUMANEIF4EBP1physical
15459249
RICTR_HUMANRICTORphysical
16962653
RPTOR_HUMANRPTORphysical
16962653
4EBP1_HUMANEIF4EBP1physical
21460630
4EBP1_HUMANEIF4EBP1physical
16824195
4EBP1_HUMANEIF4EBP1physical
17693255
RPTOR_HUMANRPTORphysical
12718876
LST8_HUMANMLST8physical
12718876
KS6B1_HUMANRPS6KB1physical
12718876
4EBP1_HUMANEIF4EBP1physical
15767663
4EBP1_HUMANEIF4EBP1physical
18722121
4EBP1_HUMANEIF4EBP1physical
12665511
KS6B1_HUMANRPS6KB1physical
12604610
4EBP1_HUMANEIF4EBP1physical
12604610
DPTOR_HUMANDEPTORphysical
22017875
RICTR_HUMANRICTORphysical
18566587
AKT1_HUMANAKT1physical
18566587
AKT1_HUMANAKT1physical
21177249
RICTR_HUMANRICTORphysical
21177249
RICTR_HUMANRICTORphysical
19875983
SIN1_HUMANMAPKAP1physical
19875983
STK38_HUMANSTK38physical
19875983
RPTOR_HUMANRPTORphysical
19875983
RICTR_HUMANRICTORphysical
23297343
RPTOR_HUMANRPTORphysical
23297343
DDB1_HUMANDDB1physical
23297343
4EBP1_HUMANEIF4EBP1physical
18337751
DPTOR_HUMANDEPTORphysical
19446321
AKTS1_HUMANAKT1S1physical
19446321
LST8_HUMANMLST8physical
19446321
RPTOR_HUMANRPTORphysical
19446321
RICTR_HUMANRICTORphysical
19446321
RICTR_HUMANRICTORphysical
19619545
RPTOR_HUMANRPTORphysical
19619545
P53_HUMANTP53physical
19619545
PREX1_HUMANPREX1physical
17565979
RPTOR_HUMANRPTORphysical
22258093
LST8_HUMANMLST8physical
22258093
PDIA3_HUMANPDIA3physical
21321085
RPTOR_HUMANRPTORphysical
21321085
RICTR_HUMANRICTORphysical
21321085
LST8_HUMANMLST8physical
21321085
HSP74_HUMANHSPA4physical
18505677
RICTR_HUMANRICTORphysical
18505677
SIN1_HUMANMAPKAP1physical
18505677
PRR5_HUMANPRR5physical
18505677
LST8_HUMANMLST8physical
18505677
RPTOR_HUMANRPTORphysical
18505677
AKT1_HUMANAKT1physical
18505677
KS6B1_HUMANRPS6KB1physical
18505677
STAT1_HUMANSTAT1physical
19553685
AMRA1_HUMANAMBRA1physical
23524951
RPTOR_HUMANRPTORphysical
23911927
MTA2_HUMANMTA2physical
22863883
4EBP1_HUMANEIF4EBP1physical
17991864
FKB1A_HUMANFKBP1Aphysical
17991864
FKBP8_HUMANFKBP8physical
17991864
GBB1_HUMANGNB1physical
24462769
GBG2_HUMANGNG2physical
24462769
GBB2_HUMANGNB2physical
24462769
GBB3_HUMANGNB3physical
24462769
GNB5_HUMANGNB5physical
24462769
RICTR_HUMANRICTORphysical
18030348
RPTOR_HUMANRPTORphysical
18030348
SIN1_HUMANMAPKAP1physical
18030348
PRR5L_HUMANPRR5Lphysical
18030348
LST8_HUMANMLST8physical
18030348
AKTS1_HUMANAKT1S1physical
18030348
4EBP1_HUMANEIF4EBP1physical
18030348
MTOR_HUMANMTORphysical
18030348
ILK_HUMANILKphysical
18339839
RICTR_HUMANRICTORphysical
18339839
IKKA_HUMANCHUKphysical
18519641
IKKB_HUMANIKBKBphysical
18519641
NEMO_HUMANIKBKGphysical
18519641
RPTOR_HUMANRPTORphysical
18519641
IKBA_HUMANNFKBIAphysical
18519641
SGK1_HUMANSGK1physical
18570873
RPTOR_HUMANRPTORphysical
18570873
AKTS1_HUMANAKT1S1physical
18570873
RICTR_HUMANRICTORphysical
18570873
SIN1_HUMANMAPKAP1physical
18570873
AKT1_HUMANAKT1physical
18566586
SIN1_HUMANMAPKAP1physical
18566586
RICTR_HUMANRICTORphysical
18566586
GA45A_HUMANGADD45Aphysical
23329839
STAT3_HUMANSTAT3physical
23329839
RPTOR_HUMANRPTORphysical
18955708
4EBP1_HUMANEIF4EBP1physical
18955708
RHEB_HUMANRHEBphysical
16098514
REBL1_HUMANRHEBL1physical
16098514
RICTR_HUMANRICTORphysical
19114562
RPTOR_HUMANRPTORphysical
19114562
AKTS1_HUMANAKT1S1physical
19114562
MAF1_HUMANMAF1physical
20543138
RICTR_HUMANRICTORphysical
20978191
AKT1_HUMANAKT1physical
21343617
RICTR_HUMANRICTORphysical
21343617
AKT1_HUMANAKT1physical
23872070
RICTR_HUMANRICTORphysical
23872070
RPTOR_HUMANRPTORphysical
23872070
NBN_HUMANNBNphysical
23762398
RPTOR_HUMANRPTORphysical
20381137
AKT1_HUMANAKT1physical
22084251
LST8_HUMANMLST8physical
22084251
RICTR_HUMANRICTORphysical
22084251
SIN1_HUMANMAPKAP1physical
22084251
4EBP1_HUMANEIF4EBP1physical
16354698
B2CL1_HUMANBCL2L1physical
20080789
SUMO1_HUMANSUMO1physical
20537536
4EBP1_HUMANEIF4EBP1physical
20537536
TF3C1_HUMANGTF3C1physical
20543138
KAP0_HUMANPRKAR1Aphysical
16963469
RPTOR_HUMANRPTORphysical
17277771
RICTR_HUMANRICTORphysical
17277771
SIN1_HUMANMAPKAP1physical
17277771
LST8_HUMANMLST8physical
17277771
AKTS1_HUMANAKT1S1physical
17277771
1433Z_HUMANYWHAZphysical
17277771
4EBP1_HUMANEIF4EBP1physical
17386266
RICTR_HUMANRICTORphysical
25897075
MLXIP_HUMANMLXIPphysical
25332233
RPTOR_HUMANRPTORphysical
25332233
MLXPL_HUMANMLXIPLphysical
25332233
RPTOR_HUMANRPTORphysical
24516643
PDK1_HUMANPDK1physical
24516643
FKB1A_HUMANFKBP1Aphysical
26344197
TRM61_HUMANTRMT61Aphysical
26344197
RAB1A_HUMANRAB1Aphysical
25446900
RPTOR_HUMANRPTORphysical
25446900
PRKN_HUMANPARK2physical
25007995
RPTOR_HUMANRPTORphysical
25007995
SQSTM_HUMANSQSTM1physical
26279575
M3K3_HUMANMAP3K3physical
26279575
ULK1_HUMANULK1physical
25686248
4EBP1_HUMANEIF4EBP1physical
25686248
DCP2_HUMANDCP2physical
26098573
KS6B1_HUMANRPS6KB1physical
25738361
FKB1A_HUMANFKBP1Aphysical
20851351
ZNRF2_HUMANZNRF2physical
27244671
FBX8_HUMANFBXO8physical
27916606
PGFRA_HUMANPDGFRAgenetic
28319113
PRKDC_HUMANPRKDCgenetic
28319113
SMAD4_HUMANSMAD4genetic
28319113
TOP1_HUMANTOP1genetic
28319113
PTEN_HUMANPTENgenetic
28319113
AKT1_HUMANAKT1physical
22337773
P53_HUMANTP53genetic
27438146
THADA_HUMANTHADAphysical
27173435
LST8_HUMANMLST8physical
27173435
CHK1_HUMANCHEK1genetic
27453043
1433Z_HUMANYWHAZgenetic
27453043
RPTOR_HUMANRPTORphysical
26522726
ESR1_HUMANESR1physical
26522726
SKP2_HUMANSKP2physical
28446188
FKBP8_HUMANFKBP8physical
24205284
EP300_HUMANEP300physical
29033323

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D00753 Sirolimus (USAN/INN); Rapamune (TN); Rapamycin (TN)
D02714 Everolimus (JAN/USAN/INN); Afinitor (TN); Votubia (TN); Zortress (TN)
D06068 Temsirolimus (JAN/USAN/INN); Torisel (TN)
D08900 Ridaforolimus (JAN/USAN); Deforolimus
D10076 Olcorolimus (USAN)
DrugBank
DB01590Everolimus
DB00337Pimecrolimus
DB00877Sirolimus
DB06287Temsirolimus
Regulatory Network of MTOR_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1218, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"mTOR kinase domain phosphorylation promotes mTORC1 signaling, cellgrowth, 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).
Cited for: AUTOPHOSPHORYLATION AT SER-2159.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567; SER-916; SER-1261;THR-1829; THR-1839; THR-1840; THR-1841; SER-1843; SER-1847; SER-1849;SER-1851; THR-1856; SER-1859; SER-1863; SER-2448; TYR-2449 ANDTHR-2471, AND MASS SPECTROMETRY.
"Site-specific mTOR phosphorylation promotes mTORC1-mediated signalingand 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).
Cited for: PHOSPHORYLATION AT SER-1261.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2478 AND SER-2481, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567 AND SER-1261, ANDMASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1162, AND MASSSPECTROMETRY.
"Identification of S6 kinase 1 as a novel mammalian target ofrapamycin (mTOR)-phosphorylating kinase.";
Holz M.K., Blenis J.;
J. Biol. Chem. 280:26089-26093(2005).
Cited for: AUTOPHOSPHORYLATION AT THR-2446.

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