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UniProtKB/Swiss-Prot entry Q8N122


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RPTOR_HUMAN
Primary accession number Q8N122
Secondary accession numbers Q8N4V9 Q8TB32 Q9P2P3
Integrated into Swiss-Prot on April 26, 2004
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 64)
Name and origin of the protein
Protein name Regulatory-associated protein of mTOR
Synonyms Raptor
P150 target of rapamycin (TOR)-scaffold protein
Gene name
Name: RAPTOR
Synonyms: KIAA1303
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH 4EBP1 AND RPS6KB1.
DOI=10.1016/S0092-8674(02)00808-5; PubMed=12150925 [NCBI, ExPASy, EBI, Israel, Japan]
Kim D.-H., Sarbassov D.D., Ali S.M., King J.E., Latek R.R., Erdjument-Bromage H., Tempst P., Sabatini D.M.;
"mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the growth machinery.";
Cell 110:163-175(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH 4EBP1 AND RPS6KB1.
DOI=10.1016/S0092-8674(02)00833-4; PubMed=12150926 [NCBI, ExPASy, EBI, Israel, Japan]
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 110:177-189(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 995-1135 (ISOFORM 1).
TISSUE=Brain, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 217-1335.
TISSUE=Brain;
DOI=10.1093/dnares/7.1.65; PubMed=10718198 [NCBI, ExPASy, EBI, Israel, Japan]
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro.";
DNA Res. 7:65-73(2000).
[5]
DISSOCIATION OF COMPLEX BY RAPAMYCIN.
DOI=10.1111/j.1356-9597.2004.00727.x; PubMed=15066126 [NCBI, ExPASy, EBI, Israel, Japan]
Oshiro N., Yoshino K., Hidayat S., Tokunaga C., Hara K., Eguchi S., Avruch J., Yonezawa K.;
"Dissociation of raptor from mTOR is a mechanism of rapamycin-induced inhibition of mTOR function.";
Genes Cells 9:359-366(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859 AND SER-863, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863 AND THR-865, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
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. 24:161-166(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-719 AND SER-722, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859; SER-863 AND SER-877, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., 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 31:438-448(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-719; SER-722; SER-859; SER-863 AND SER-877, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
  • FUNCTION: Participates in the FRAP1 pathway and associates in a near stoichiometric ratio with FRAP1 to form a nutrient-sensitive complex (NSC). Plays a pivotal role as a scaffold protein in the FRAP1-signaling pathway and this interaction is essential for the catalyzed phosphorylation of EIF4EBP1. Has a positive role in nutrient-stimulated signaling to the downstream effector RPS6KB1. Under nutrient-deprived conditions, serves as a negative regulator of FRAP1 kinase activity. Regulation of the interaction with FRAP1 is a critical mechanism by which cells coordinate the rate of cell growth and maintenance of cell size with different environmental conditions.
  • SUBUNIT: Binds directly 4EBP1 and RPS6KB1 independently of its association with FRAP1. Binds preferentially to poorly or non-phosphorylated form of EIF4EBP1, and this binding is critical to the ability of FRAP1 to catalyze phosphorylation. Complex with FRAP1 physically interacts under both leucine-rich and -poor conditions and therefore in at least two nutrient-determined states with different stability.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ8N122-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ8N122-2
    Features which should be applied to build the isoform sequence: VSP_010174.
  • TISSUE SPECIFICITY: Highly expressed in skeletal muscle, and in a lesser extent in brain, lung, small intestine, kidney and placenta.
  • MISCELLANEOUS: Rapamycin destabilizes the interaction with FRAP1 regardless of nutrient availability, and its potency for dissociation is increased under nutrient-rich conditions. This action uncouples FRAP1 from its substrates, and inhibits FRAP1 signaling without altering its intrinsic catalytic activity.
  • SIMILARITY: Belongs to the WD repeat RAPTOR family.
  • SIMILARITY: Contains 7 WD repeats.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY090663; AAM09075.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB082951; BAC06490.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC025180; AAH25180.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC033258; AAH33258.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC064515; AAH64515.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB037724; BAA92541.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00166044; -.
IPI00410411; -.
RefSeq NP_065812.1; -.
UniGene Hs.133044
3D structure databases
ModBase Q8N122.
PTM databases
PhosphoSite Q8N122; -.
Enzyme and pathway databases
Pathway_Interaction_DB pi3kciaktpathway; Class I PI3K signaling events mediated by Akt.
mtor_4pathway; mTOR signaling pathway.
Reactome REACT_498; Signaling by Insulin receptor.
Organism-specific databases
GeneCards GC17P076134; -.
H-InvDB HIX0018877; -.
HPA CAB013514; -.
MIM 607130; gene. [NCBI / EBI]
HUGE KIAA1303.
Gene expression databases
ArrayExpress Q8N122; -.
Bgee Q8N122; -.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR011989; ARM-like.
IPR000357; HEAT.
IPR004083; Raptor.
IPR015943; WD40/YVTN_repeat-like.
IPR001680; WD40_repeat.
IPR019775; WD40_repeat_CS.
IPR017986; WD40_repeat_region.
IPR019781; WD40_repeat_sg.
Graphical view of domain structure.
Gene3D G3DSA:1.25.10.10; ARM-like; 1.
G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
PANTHER PTHR12848; Raptor; 1.
Pfam PF02985; HEAT; 2.
PF00400; WD40; 2.
Pfam graphical view of domain structure.
PRINTS PR01547; YEAST176DUF.
SMART SM00320; WD40; 7.
SMART graphical view of domain structure.
PROSITE PS00678; WD_REPEATS_1; FALSE_NEG.
PS50082; WD_REPEATS_2; FALSE_NEG.
PS50294; WD_REPEATS_REGION; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q8N122; -.
Genome annotation databases
Ensembl ENSG00000141564; Homo sapiens. [Contig view]
GeneID 57521; -.
KEGG hsa:57521; -.
Phylogenomic databases
HOGENOM Q8N122; -.
HOVERGEN Q8N122; -.
OMA Q8N122; VQYTPHS.
Other
NextBio 63899; -.
SOURCE RAPTOR; Homo sapiens.
ProtoNet Q8N122.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Phosphoprotein; Repeat; WD repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1335  1335     Regulatory-associated protein of mTOR. PRO_0000051200
REPEAT   1020   1061  42     WD 1. 
REPEAT   1065   1106  42     WD 2. 
REPEAT   1121   1160  40     WD 3. 
REPEAT   1164   1203  40     WD 4. 
REPEAT   1209   1249  41     WD 5. 
REPEAT   1251   1291  41     WD 6. 
REPEAT   1299   1335  37     WD 7. 
COMPBIAS   881    887  7     Poly-Ser. 
MOD_RES   719    719        Phosphoserine. 
MOD_RES   722    722        Phosphoserine. 
MOD_RES   857    857        Phosphothreonine (By similarity). 
MOD_RES   859    859        Phosphoserine. 
MOD_RES   863    863        Phosphoserine. 
MOD_RES   865    865        Phosphothreonine. 
MOD_RES   877    877        Phosphoserine. 
VAR_SEQ   380   1335        Missing (in isoform 2). VSP_010174
CONFLICT   217    218        LE -> RQ (in Ref. 4; BAA92541). 
Sequence information
Length: 1335 AA [This is the length of the unprocessed precursor] Molecular weight: 149038 Da [This is the MW of the unprocessed precursor] CRC64: 688ED1943F45045A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MESEMLQSPL LGLGEEDEAD LTDWNLPLAF MKKRHCEKIE GSKSLAQSWR MKDRMKTVSV 

        70         80         90        100        110        120 
ALVLCLNVGV DPPDVVKTTP CARLECWIDP LSMGPQKALE TIGANLQKQY ENWQPRARYK 

       130        140        150        160        170        180 
QSLDPTVDEV KKLCTSLRRN AKEERVLFHY NGHGVPRPTV NGEVWVFNKN YTQYIPLSIY 

       190        200        210        220        230        240 
DLQTWMGSPS IFVYDCSNAG LIVKSFKQFA LQREQELEVA AINPNHPLAQ MPLPPSMKNC 

       250        260        270        280        290        300 
IQLAACEATE LLPMIPDLPA DLFTSCLTTP IKIALRWFCM QKCVSLVPGV TLDLIEKIPG 

       310        320        330        340        350        360 
RLNDRRTPLG ELNWIFTAIT DTIAWNVLPR DLFQKLFRQD LLVASLFRNF LLAERIMRSY 

       370        380        390        400        410        420 
NCTPVSSPRL PPTYMHAMWQ AWDLAVDICL SQLPTIIEEG TAFRHSPFFA EQLTAFQVWL 

       430        440        450        460        470        480 
TMGVENRNPP EQLPIVLQVL LSQVHRLRAL DLLGRFLDLG PWAVSLALSV GIFPYVLKLL 

       490        500        510        520        530        540 
QSSARELRPL LVFIWAKILA VDSSCQADLV KDNGHKYFLS VLADPYMPAE HRTMTAFILA 

       550        560        570        580        590        600 
VIVNSYHTGQ EACLQGNLIA ICLEQLNDPH PLLRQWVAIC LGRIWQNFDS ARWCGVRDSA 

       610        620        630        640        650        660 
HEKLYSLLSD PIPEVRCAAV FALGTFVGNS AERTDHSTTI DHNVAMMLAQ LVSDGSPMVR 

       670        680        690        700        710        720 
KELVVALSHL VVQYESNFCT VALQFIEEEK NYALPSPATT EGGSLTPVRD SPCTPRLRSV 

       730        740        750        760        770        780 
SSYGNIRAVA TARSLNKSLQ NLSLTEESGG AVAFSPGNLS TSSSASSTLG SPENEEHILS 

       790        800        810        820        830        840 
FETIDKMRRA SSYSSLNSLI GVSFNSVYTQ IWRVLLHLAA DPYPEVSDVA MKVLNSIAYK 

       850        860        870        880        890        900 
ATVNARPQRV LDTSSLTQSA PASPTNKGVH IHQAGGSPPA SSTSSSSLTN DVAKQPVSRD 

       910        920        930        940        950        960 
LPSGRPGTTG PAGAQYTPHS HQFPRTRKMF DKGPEQTADD ADDAAGHKSF ISATVQTGFC 

       970        980        990       1000       1010       1020 
DWSARYFAQP VMKIPEEHDL ESQIRKEREW RFLRNSRVRR QAQQVIQKGI TRLDDQIFLN 

      1030       1040       1050       1060       1070       1080 
RNPGVPSVVK FHPFTPCIAV ADKDSICFWD WEKGEKLDYF HNGNPRYTRV TAMEYLNGQD 

      1090       1100       1110       1120       1130       1140 
CSLLLTATDD GAIRVWKNFA DLEKNPEMVT AWQGLSDMLP TTRGAGMVVD WEQETGLLMS 

      1150       1160       1170       1180       1190       1200 
SGDVRIVRIW DTDREMKVQD IPTGADSCVT SLSCDSHRSL IVAGLGDGSI RVYDRRMALS 

      1210       1220       1230       1240       1250       1260 
ECRVMTYREH TAWVVKASLQ KRPDGHIVSV SVNGDVRIFD PRMPESVNVL QIVKGLTALD 

      1270       1280       1290       1300       1310       1320 
IHPQADLIAC GSVNQFTAIY NSSGELINNI KYYDGFMGQR VGAISCLAFH PHWPHLAVGS 

      1330 
NDYYISVYSV EKRVR 

Q8N122 in FASTA format

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