CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015355
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Rapamycin-insensitive companion of mTOR 
Protein Synonyms/Alias
 AVO3 homolog; hAVO3 
Gene Name
 RICTOR 
Gene Synonyms/Alias
 KIAA1999 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
239LHLLNHPKTRQYVRAubiquitination[1]
274DTAEGQLKEDREARFubiquitination[1, 2, 3, 4, 5, 6]
374GFVAAEAKTILPHRAubiquitination[1, 2, 4, 5, 6]
477SAALNCLKRFHEMKKubiquitination[4]
516DQYLRVQKDIFILKDubiquitination[1]
566NVNLRNYKDEQLHRFubiquitination[4]
582RRLLYFYKPSSKLYAacetylation[7]
719LARVILSKILTAATDubiquitination[1, 4]
813LRFLSIPKGFSYLNEubiquitination[4]
838WHREYNSKYVDLIEEubiquitination[3]
856EALTTYRKPVDGDNYubiquitination[4]
922DKWEEIKKLKASLWAubiquitination[4]
1080YDRSGPIKDKNSFPFubiquitination[4]
1092FPFFASSKLVKNRILubiquitination[4]
1107NSLTLPNKKHRSSSDubiquitination[4]
1184SIGENDLKFTKNFGTubiquitination[1, 2]
1187ENDLKFTKNFGTENHubiquitination[6]
1312APSIATIKSLADCNFubiquitination[1, 4]
1334AFGYATLKRLQQQRMubiquitination[4, 6, 8]
1391LSYASLDKEDLLSPIubiquitination[4, 9]
1477SGTGGLVKNSFHLLRubiquitination[4, 6]
1590EGSASSTKSTELLLGubiquitination[1, 4]
1599TELLLGVKTIPDDTPubiquitination[1, 4]
Reference
 [1] 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]
 [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] 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]
 [5] 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]
 [6] 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]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [8] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [9] 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] 
Functional Description
 Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, 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'. Plays an essential role in embryonic growth and development. 
Sequence Annotation
 MOD_RES 21 21 Phosphoserine.
 MOD_RES 1135 1135 Phosphothreonine; by RPS6KB1.
 MOD_RES 1177 1177 Phosphoserine (By similarity).
 MOD_RES 1282 1282 Phosphoserine.
 MOD_RES 1284 1284 Phosphoserine.
 MOD_RES 1388 1388 Phosphoserine.
 MOD_RES 1396 1396 Phosphoserine.
 MOD_RES 1411 1411 Phosphoserine.
 MOD_RES 1591 1591 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Developmental protein; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1708 AA 
Protein Sequence
MAAIGRGRSL KNLRVRGRND SGEENVPLDL TREPSDNLRE ILQNVARLQG VSNMRKLGHL 60
NNFTKLLCDI GHSEEKLGFH YEDIIICLRL ALLNEAKEVR AAGLRALRYL IQDSSILQKV 120
LKLKVDYLIA RCIDIQQSNE VERTQALRLV RKMITVNASL FPSSVTNSLI AVGNDGLQER 180
DRMVRACIAI ICELALQNPE VVALRGGLNT ILKNVIDCQL SRINEALITT ILHLLNHPKT 240
RQYVRADVEL ERILAPYTDF HYRHSPDTAE GQLKEDREAR FLASKMGIIA TFRSWAGIIN 300
LCKPGNSGIQ SLIGVLCIPN MEIRRGLLEV LYDIFRLPLP VVTEEFIEAL LSVDPGRFQD 360
SWRLSDGFVA AEAKTILPHR ARSRPDLMDN YLALILSAFI RNGLLEGLVE VITNSDDHIS 420
VRATILLGEL LHMANTILPH SHSHHLHCLP TLMNMAASFD IPKEKRLRAS AALNCLKRFH 480
EMKKRGPKPY SLHLDHIIQK AIATHQKRDQ YLRVQKDIFI LKDTEEALLI NLRDSQVLQH 540
KENLEWNWNL IGTILKWPNV NLRNYKDEQL HRFVRRLLYF YKPSSKLYAN LDLDFAKAKQ 600
LTVVGCQFTE FLLESEEDGQ GYLEDLVKDI VQWLNASSGM KPERSLQNNG LLTTLSQHYF 660
LFIGTLSCHP HGVKMLEKCS VFQCLLNLCS LKNQDHLLKL TVSSLDYSRD GLARVILSKI 720
LTAATDACRL YATKHLRVLL RANVEFFNNW GIELLVTQLH DKNKTISSEA LDILDEACED 780
KANLHALIQM KPALSHLGDK GLLLLLRFLS IPKGFSYLNE RGYVAKQLEK WHREYNSKYV 840
DLIEEQLNEA LTTYRKPVDG DNYVRRSNQR LQRPHVYLPI HLYGQLVHHK TGCHLLEVQN 900
IITELCRNVR TPDLDKWEEI KKLKASLWAL GNIGSSNWGL NLLQEENVIP DILKLAKQCE 960
VLSIRGTCVY VLGLIAKTKQ GCDILKCHNW DAVRHSRKHL WPVVPDDVEQ LCNELSSIPS 1020
TLSLNSESTS SRHNSESESV PSSMFILEDD RFGSSSTSTF FLDINEDTEP TFYDRSGPIK 1080
DKNSFPFFAS SKLVKNRILN SLTLPNKKHR SSSDPKGGKL SSESKTSNRR IRTLTEPSVD 1140
FNHSDDFTPI STVQKTLQLE TSFMGNKHIE DTGSTPSIGE NDLKFTKNFG TENHRENTSR 1200
ERLVVESSTS SHMKIRSQSF NTDTTTSGIS SMSSSPSRET VGVDATTMDT DCGSMSTVVS 1260
TKTIKTSHYL TPQSNHLSLS KSNSVSLVPP GSSHTLPRRA QSLKAPSIAT IKSLADCNFS 1320
YTSSRDAFGY ATLKRLQQQR MHPSLSHSEA LASPAKDVLF TDTITMKANS FESRLTPSRF 1380
MKALSYASLD KEDLLSPINQ NTLQRSSSVR SMVSSATYGG SDDYIGLALP VDINDIFQVK 1440
DIPYFQTKNI PPHDDRGARA FAHDAGGLPS GTGGLVKNSF HLLRQQMSLT EIMNSIHSDA 1500
SLFLESTEDT GLQEHTDDNC LYCVCIEILG FQPSNQLSAI CSHSDFQDIP YSDWCEQTIH 1560
NPLEVVPSKF SGISGCSDGV SQEGSASSTK STELLLGVKT IPDDTPMCRI LLRKEVLRLV 1620
INLSSSVSTK CHETGLLTIK EKYPQTFDDI CLYSEVSHLL SHCTFRLPCR RFIQELFQDV 1680
QFLQMHEEAE AVLATPPKQP IVDTSAES 1708 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0031932; C:TORC2 complex; IDA:UniProtKB.
 GO:0043022; F:ribosome binding; IEA:Compara.
 GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
 GO:0009790; P:embryo development; ISS:UniProtKB.
 GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
 GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
 GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
 GO:0030838; P:positive regulation of actin filament polymerization; IEA:Compara.
 GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Compara.
 GO:0032008; P:positive regulation of TOR signaling cascade; IMP:UniProtKB.
 GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
 GO:0051896; P:regulation of protein kinase B signaling cascade; IDA:UniProtKB.
 GO:0032314; P:regulation of Rac GTPase activity; IEA:Compara.
 GO:0031295; P:T cell costimulation; TAS:Reactome. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold. 
Pfam
  
SMART
  
PROSITE
  
PRINTS