CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017323
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Regulatory-associated protein of mTOR 
Protein Synonyms/Alias
 Raptor; p150 target of rapamycin (TOR)-scaffold protein 
Gene Name
 RPTOR 
Gene Synonyms/Alias
 KIAA1303; RAPTOR 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
43CEKIEGSKSLAQSWRubiquitination[1]
97PLSMGPQKALETIGAubiquitination[1]
108TIGANLQKQYENWQPubiquitination[1, 2, 3]
120WQPRARYKQSLDPTVubiquitination[1, 2]
131DPTVDEVKKLCTSLRubiquitination[1, 2]
297VTLDLIEKIPGRLNDubiquitination[1]
335LPRDLFQKLFRQDLLubiquitination[1, 2, 3, 4, 5]
511SCQADLVKDNGHKYFubiquitination[6]
603VRDSAHEKLYSLLSDubiquitination[1, 2, 3, 6, 7]
840VLNSIAYKATVNARPubiquitination[1]
932RTRKMFDKGPEQTADubiquitination[1]
973YFAQPVMKIPEEHDLubiquitination[2]
1008QAQQVIQKGITRLDDubiquitination[1, 2, 3]
1056WDWEKGEKLDYFHNGubiquitination[2]
1097DGAIRVWKNFADLEKubiquitination[2, 4, 5]
1104KNFADLEKNPEMVTAubiquitination[2]
1157WDTDREMKVQDIPTGubiquitination[1]
1221VVKASLQKRPDGHIVubiquitination[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] 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]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] 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
 Involved in the control of the mammalian target of rapamycin complex 1 (mTORC1) activity which regulates cell growth and survival, and autophagy in response to nutrient and hormonal signals; functions as a scaffold for recruiting mTORC1 substrates. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1- mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. 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-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. 
Sequence Annotation
 REPEAT 1020 1061 WD 1.
 REPEAT 1065 1106 WD 2.
 REPEAT 1121 1160 WD 3.
 REPEAT 1164 1203 WD 4.
 REPEAT 1209 1249 WD 5.
 REPEAT 1251 1291 WD 6.
 REPEAT 1299 1335 WD 7.
 MOD_RES 696 696 Phosphoserine; by MAPK8.
 MOD_RES 706 706 Phosphothreonine; by MAPK8.
 MOD_RES 719 719 Phosphoserine; by RPS6KA1.
 MOD_RES 721 721 Phosphoserine; by RPS6KA1.
 MOD_RES 722 722 Phosphoserine; by AMPK and RPS6KA1.
 MOD_RES 792 792 Phosphoserine; by AMPK.
 MOD_RES 855 855 Phosphoserine.
 MOD_RES 857 857 Phosphothreonine (By similarity).
 MOD_RES 859 859 Phosphoserine; by MTOR.
 MOD_RES 863 863 Phosphoserine; by MAPK8 and MTOR.
 MOD_RES 877 877 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Lysosome; Phosphoprotein; Reference proteome; Repeat; WD repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1335 AA 
Protein Sequence
MESEMLQSPL LGLGEEDEAD LTDWNLPLAF MKKRHCEKIE GSKSLAQSWR MKDRMKTVSV 60
ALVLCLNVGV DPPDVVKTTP CARLECWIDP LSMGPQKALE TIGANLQKQY ENWQPRARYK 120
QSLDPTVDEV KKLCTSLRRN AKEERVLFHY NGHGVPRPTV NGEVWVFNKN YTQYIPLSIY 180
DLQTWMGSPS IFVYDCSNAG LIVKSFKQFA LQREQELEVA AINPNHPLAQ MPLPPSMKNC 240
IQLAACEATE LLPMIPDLPA DLFTSCLTTP IKIALRWFCM QKCVSLVPGV TLDLIEKIPG 300
RLNDRRTPLG ELNWIFTAIT DTIAWNVLPR DLFQKLFRQD LLVASLFRNF LLAERIMRSY 360
NCTPVSSPRL PPTYMHAMWQ AWDLAVDICL SQLPTIIEEG TAFRHSPFFA EQLTAFQVWL 420
TMGVENRNPP EQLPIVLQVL LSQVHRLRAL DLLGRFLDLG PWAVSLALSV GIFPYVLKLL 480
QSSARELRPL LVFIWAKILA VDSSCQADLV KDNGHKYFLS VLADPYMPAE HRTMTAFILA 540
VIVNSYHTGQ EACLQGNLIA ICLEQLNDPH PLLRQWVAIC LGRIWQNFDS ARWCGVRDSA 600
HEKLYSLLSD PIPEVRCAAV FALGTFVGNS AERTDHSTTI DHNVAMMLAQ LVSDGSPMVR 660
KELVVALSHL VVQYESNFCT VALQFIEEEK NYALPSPATT EGGSLTPVRD SPCTPRLRSV 720
SSYGNIRAVA TARSLNKSLQ NLSLTEESGG AVAFSPGNLS TSSSASSTLG SPENEEHILS 780
FETIDKMRRA SSYSSLNSLI GVSFNSVYTQ IWRVLLHLAA DPYPEVSDVA MKVLNSIAYK 840
ATVNARPQRV LDTSSLTQSA PASPTNKGVH IHQAGGSPPA SSTSSSSLTN DVAKQPVSRD 900
LPSGRPGTTG PAGAQYTPHS HQFPRTRKMF DKGPEQTADD ADDAAGHKSF ISATVQTGFC 960
DWSARYFAQP VMKIPEEHDL ESQIRKEREW RFLRNSRVRR QAQQVIQKGI TRLDDQIFLN 1020
RNPGVPSVVK FHPFTPCIAV ADKDSICFWD WEKGEKLDYF HNGNPRYTRV TAMEYLNGQD 1080
CSLLLTATDD GAIRVWKNFA DLEKNPEMVT AWQGLSDMLP TTRGAGMVVD WEQETGLLMS 1140
SGDVRIVRIW DTDREMKVQD IPTGADSCVT SLSCDSHRSL IVAGLGDGSI RVYDRRMALS 1200
ECRVMTYREH TAWVVKASLQ KRPDGHIVSV SVNGDVRIFD PRMPESVNVL QIVKGLTALD 1260
IHPQADLIAC GSVNQFTAIY NSSGELINNI KYYDGFMGQR VGAISCLAFH PHWPHLAVGS 1320
NDYYISVYSV EKRVR 1335 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005764; C:lysosome; IDA:UniProtKB.
 GO:0031931; C:TORC1 complex; IDA:UniProtKB.
 GO:0071889; F:14-3-3 protein binding; IDA:UniProtKB.
 GO:0001030; F:RNA polymerase III type 1 promoter DNA binding; IDA:UniProtKB.
 GO:0001031; F:RNA polymerase III type 2 promoter DNA binding; IDA:UniProtKB.
 GO:0001032; F:RNA polymerase III type 3 promoter DNA binding; IDA:UniProtKB.
 GO:0001156; F:TFIIIC-class transcription factor binding; IDA:UniProtKB.
 GO:0007050; P:cell cycle arrest; TAS:Reactome.
 GO:0016049; P:cell growth; IMP:UniProtKB.
 GO:0071230; P:cellular response to amino acid stimulus; IMP:UniProtKB.
 GO:0031669; P:cellular response to nutrient levels; IMP:UniProtKB.
 GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
 GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
 GO:0032008; P:positive regulation of TOR signaling cascade; IDA:UniProtKB.
 GO:0045945; P:positive regulation of transcription from RNA polymerase III promoter; IMP:UniProtKB.
 GO:0008361; P:regulation of cell size; IMP:UniProtKB.
 GO:0031929; P:TOR signaling cascade; IDA:UniProtKB. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR000357; HEAT.
 IPR004083; Raptor.
 IPR027466; Raptor_metazoan.
 IPR015943; WD40/YVTN_repeat-like_dom.
 IPR001680; WD40_repeat.
 IPR017986; WD40_repeat_dom. 
Pfam
 PF02985; HEAT
 PF00400; WD40 
SMART
 SM00320; WD40 
PROSITE
 PS00678; WD_REPEATS_1
 PS50082; WD_REPEATS_2
 PS50294; WD_REPEATS_REGION 
PRINTS
 PR01547; YEAST176DUF.