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Q8N122 (RPTOR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Regulatory-associated protein of mTOR

Short name=Raptor
Alternative name(s):
p150 target of rapamycin (TOR)-scaffold protein
Gene names
Name:RPTOR
Synonyms:KIAA1303, RAPTOR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1335 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Involved in ciliogenesis. Ref.1 Ref.2 Ref.30

Subunit structure

Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR. mTORC1 binds to and is inhibited by FKBP12-rapamycin. Binds directly to 4EBP1 and RPS6KB1 independently of its association with MTOR. Binds preferentially to poorly or non-phosphorylated forms of EIF4EBP1, and this binding is critical to the ability of MTOR to catalyze phosphorylation. Forms a complex with MTOR under both leucine-rich and -poor conditions. Interacts with ULK1 in a nutrient-dependent manner; the interaction is reduced during starvation. Interacts (when phosphorylated by AMPK) with 14-3-3 protein, leading to inhibit its activity. Interacts with SPAG5; SPAG5 competes with MTOR for RPTOR-binding, resulting in decreased mTORC1 formation. Interacts with G3BP1. The complex formed with G3BP1 AND SPAG5 is increased by oxidative stress. Ref.1 Ref.2 Ref.8 Ref.9 Ref.13 Ref.16 Ref.20 Ref.29

Subcellular location

Cytoplasm. Lysosome. Cytoplasmic granule. Note: Targeting to lysosomes depends on amino acid availability. In arsenite-stressed cells, accumulates in stress granules when associated with SPAG5 and association with lysosomes is drastically decreased. Ref.23 Ref.29

Tissue specificity

Highly expressed in skeletal muscle, and in a lesser extent in brain, lung, small intestine, kidney and placenta. Isoform 3 is widely expressed, with highest levels in nasal mucosa and pituitary and lowest in spleen. Ref.1 Ref.7 Ref.8

Post-translational modification

Insulin-stimulated phosphorylation at Ser-863 by MTOR and MAPK8 up-regulates mTORC1 activity. Osmotic stress also induces phosphorylation at Ser-696, Thr-706 and Ser-863 by MAPK8. Ser-863 phosphorylation is required for phosphorylation at Ser-855 and Ser-859. In response to nutrient limitation, phosphorylated by AMPK; phosphorylation promotes interaction with 14-3-3 proteins, leading to negative regulation of the mTORC1 complex. In response to growth factors, phosphorylated at Ser-719, Ser-721 and Ser-722 by RPS6KA1, which stimulates mTORC1 activity. Ref.14 Ref.16 Ref.24 Ref.28

Sequence similarities

Belongs to the WD repeat RAPTOR family.

Contains 7 WD repeats.

Ontologies

Keywords
   Cellular componentCytoplasm
Lysosome
   Coding sequence diversityAlternative splicing
   DomainRepeat
WD repeat
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processTOR signaling

Inferred from direct assay Ref.23. Source: UniProtKB

cell cycle arrest

Traceable author statement. Source: Reactome

cell growth

Inferred from mutant phenotype Ref.23. Source: UniProtKB

cellular response to amino acid stimulus

Inferred from mutant phenotype Ref.23. Source: UniProtKB

cellular response to nutrient levels

Inferred from mutant phenotype Ref.1. Source: UniProtKB

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of TOR signaling

Inferred from direct assay Ref.2Ref.16. Source: UniProtKB

positive regulation of endothelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein serine/threonine kinase activity

Inferred from direct assay Ref.2. Source: UniProtKB

positive regulation of transcription from RNA polymerase III promoter

Inferred from mutant phenotype PubMed 20233713. Source: UniProtKB

regulation of cell size

Inferred from mutant phenotype Ref.1. Source: UniProtKB

   Cellular_componentTORC1 complex

Inferred from direct assay PubMed 15467718. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.23. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

lysosomal membrane

Inferred from direct assay PubMed 17897319. Source: UniProtKB

lysosome

Inferred from direct assay Ref.23. Source: UniProtKB

   Molecular_function14-3-3 protein binding

Inferred from direct assay Ref.16. Source: UniProtKB

RNA polymerase III type 1 promoter DNA binding

Inferred from direct assay PubMed 20233713. Source: UniProtKB

RNA polymerase III type 2 promoter DNA binding

Inferred from direct assay PubMed 20233713. Source: UniProtKB

RNA polymerase III type 3 promoter DNA binding

Inferred from direct assay PubMed 20233713. Source: UniProtKB

TFIIIC-class transcription factor binding

Inferred from direct assay PubMed 20543138. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.1Ref.2Ref.13. Source: UniProtKB

protein complex binding

Inferred from physical interaction Ref.20. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.16. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N122-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8N122-2)

The sequence of this isoform differs from the canonical sequence as follows:
     380-1335: Missing.
Isoform 3 (identifier: Q8N122-3)

The sequence of this isoform differs from the canonical sequence as follows:
     504-661: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13351335Regulatory-associated protein of mTOR
PRO_0000051200

Regions

Repeat1020 – 106142WD 1
Repeat1065 – 110642WD 2
Repeat1121 – 116040WD 3
Repeat1164 – 120340WD 4
Repeat1209 – 124941WD 5
Repeat1251 – 129141WD 6
Repeat1299 – 133537WD 7
Compositional bias881 – 8877Poly-Ser

Amino acid modifications

Modified residue6961Phosphoserine; by MAPK8 Ref.24 Ref.28
Modified residue7061Phosphothreonine; by MAPK8 Ref.24 Ref.28
Modified residue7191Phosphoserine; by RPS6KA1 Ref.14 Ref.18
Modified residue7211Phosphoserine; by RPS6KA1 Ref.14
Modified residue7221Phosphoserine; by AMPK and RPS6KA1 Ref.14 Ref.16
Modified residue7921Phosphoserine; by AMPK Ref.16
Modified residue8551Phosphoserine Ref.24
Modified residue8591Phosphoserine; by MTOR Ref.18 Ref.22 Ref.24 Ref.25
Modified residue8631Phosphoserine; by MAPK8 and MTOR Ref.12 Ref.18 Ref.22 Ref.24 Ref.25 Ref.27 Ref.28
Modified residue8771Phosphoserine Ref.17 Ref.18 Ref.21 Ref.22 Ref.24 Ref.25 Ref.27

Natural variations

Alternative sequence380 – 1335956Missing in isoform 2.
VSP_010174
Alternative sequence504 – 661158Missing in isoform 3.
VSP_054042

Experimental info

Mutagenesis7221S → A: Abolishes AMPK-mediated phosphorylation; when associated with A-792. Ref.16
Mutagenesis7921S → A: Abolishes AMPK-mediated phosphorylation; when associated with A-722. Ref.16
Sequence conflict217 – 2182LE → RQ in BAA92541. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 688ED1943F45045A

FASTA1,335149,038
        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 

« Hide

Isoform 2 [UniParc].

Checksum: D67B01D4E68E859E
Show »

FASTA37943,256
Isoform 3 [UniParc].

Checksum: 1CE0DA04E72105B2
Show »

FASTA1,177131,515

References

« Hide 'large scale' references
[1]"mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the growth machinery."
Kim D.-H., Sarbassov D.D., Ali S.M., King J.E., Latek R.R., Erdjument-Bromage H., Tempst P., Sabatini D.M.
Cell 110:163-175(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH 4EBP1 AND RPS6KB1.
[2]"Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action."
Hara K., Maruki Y., Long X., Yoshino K., Oshiro N., Hidayat S., Tokunaga C., Avruch J., Yonezawa K.
Cell 110:177-189(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH 4EBP1 AND RPS6KB1.
[3]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 995-1135 (ISOFORM 1).
Tissue: Brain, Placenta and Testis.
[6]"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."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 217-1335.
Tissue: Brain.
[7]"Characterization of a novel splicing variant in the RAPTOR gene."
Sun C., Southard C., Di Rienzo A.
Mutat. Res. 662:88-92(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 488-594 (ISOFORM 3), TISSUE SPECIFICITY (ISOFORM 3).
[8]"Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control."
Loewith R., Jacinto E., Wullschleger S., Lorberg A., Crespo J.L., Bonenfant D., Oppliger W., Jenoe P., Hall M.N.
Mol. Cell 10:457-468(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MTOR AND MLST8, IDENTIFICATION IN THE TORC1 COMPLEX, TISSUE SPECIFICITY.
[9]"TOS motif-mediated raptor binding regulates 4E-BP1 multisite phosphorylation and function."
Schalm S.S., Fingar D.C., Sabatini D.M., Blenis J.
Curr. Biol. 13:797-806(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF4EBP1.
[10]"Dissociation of raptor from mTOR is a mechanism of rapamycin-induced inhibition of mTOR function."
Oshiro N., Yoshino K., Hidayat S., Tokunaga C., Hara K., Eguchi S., Avruch J., Yonezawa K.
Genes Cells 9:359-366(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DISSOCIATION OF COMPLEX BY RAPAMYCIN.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase."
Sancak Y., Thoreen C.C., Peterson T.R., Lindquist R.A., Kang S.A., Spooner E., Carr S.A., Sabatini D.M.
Mol. Cell 25:903-915(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AKT1S1.
[14]"Oncogenic MAPK signaling stimulates mTORC1 activity by promoting RSK-mediated raptor phosphorylation."
Carriere A., Cargnello M., Julien L.A., Gao H., Bonneil E., Thibault P., Roux P.P.
Curr. Biol. 18:1269-1277(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-719; SER-721 AND SER-722.
[15]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"AMPK phosphorylation of raptor mediates a metabolic checkpoint."
Gwinn D.M., Shackelford D.B., Egan D.F., Mihaylova M.M., Mery A., Vasquez D.S., Turk B.E., Shaw R.J.
Mol. Cell 30:214-226(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-722 AND SER-792, MUTAGENESIS OF SER-722 AND SER-792, INTERACTION WITH 14-3-3.
[17]"Kinase-selective enrichment enables quantitative phosphoproteomics of the 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-877, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-719; SER-859; SER-863 AND SER-877, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy."
Hosokawa N., Hara T., Kaizuka T., Kishi C., Takamura A., Miura Y., Iemura S., Natsume T., Takehana K., Yamada N., Guan J.L., Oshiro N., Mizushima N.
Mol. Biol. Cell 20:1981-1991(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ULK1.
[21]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-877, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859; SER-863 AND SER-877, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[23]"Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids."
Sancak Y., Bar-Peled L., Zoncu R., Markhard A.L., Nada S., Sabatini D.M.
Cell 141:290-303(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[24]"Regulation of mTOR complex 1 (mTORC1) by raptor Ser863 and multisite phosphorylation."
Foster K.G., Acosta-Jaquez H.A., Romeo Y., Ekim B., Soliman G.A., Carriere A., Roux P.P., Ballif B.A., Fingar D.C.
J. Biol. Chem. 285:80-94(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-696; THR-706; SER-855; SER-859; SER-863 AND SER-877.
[25]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859; SER-863 AND SER-877, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863 AND SER-877, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Osmotic stress regulates mammalian target of rapamycin (mTOR) complex 1 via c-Jun N-terminal Kinase (JNK)-mediated Raptor protein phosphorylation."
Kwak D., Choi S., Jeong H., Jang J.H., Lee Y., Jeon H., Lee M.N., Noh J., Cho K., Yoo J.S., Hwang D., Suh P.G., Ryu S.H.
J. Biol. Chem. 287:18398-18407(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-696; THR-706 AND SER-863.
[29]"Inhibition of mTORC1 by astrin and stress granules prevents apoptosis in cancer cells."
Thedieck K., Holzwarth B., Prentzell M.T., Boehlke C., Klasener K., Ruf S., Sonntag A.G., Maerz L., Grellscheid S.N., Kremmer E., Nitschke R., Kuehn E.W., Jonker J.W., Groen A.K., Reth M., Hall M.N., Baumeister R.
Cell 154:859-874(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH G3BP1 AND SPAG5, SUBCELLULAR LOCATION.
[30]"The Bardet-Biedl syndrome-related protein CCDC28B modulates mTORC2 function and interacts with SIN1 to control cilia length independently of the mTOR complex."
Cardenas-Rodriguez M., Irigoin F., Osborn D.P., Gascue C., Katsanis N., Beales P.L., Badano J.L.
Hum. Mol. Genet. 22:4031-4042(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CILIOGENESIS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY090663 mRNA. Translation: AAM09075.1.
AB082951 mRNA. Translation: BAC06490.1.
AC016245 Genomic DNA. No translation available.
AC109327 Genomic DNA. No translation available.
AC127496 Genomic DNA. No translation available.
AC133012 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89618.1.
BC025180 mRNA. Translation: AAH25180.1.
BC033258 mRNA. Translation: AAH33258.1.
BC064515 mRNA. Translation: AAH64515.1.
BC136652 mRNA. Translation: AAI36653.1.
BC136654 mRNA. Translation: AAI36655.1.
AB037724 mRNA. Translation: BAA92541.1.
GQ183898 mRNA. Translation: ACS44766.1.
CCDSCCDS11773.1. [Q8N122-1]
RefSeqNP_001156506.1. NM_001163034.1. [Q8N122-3]
NP_065812.1. NM_020761.2. [Q8N122-1]
UniGeneHs.133044.

3D structure databases

ProteinModelPortalQ8N122.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121582. 58 interactions.
DIPDIP-39482N.
IntActQ8N122. 26 interactions.
MINTMINT-3038940.
STRING9606.ENSP00000307272.

PTM databases

PhosphoSiteQ8N122.

Polymorphism databases

DMDM46577501.

Proteomic databases

MaxQBQ8N122.
PaxDbQ8N122.
PRIDEQ8N122.

Protocols and materials databases

DNASU57521.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306801; ENSP00000307272; ENSG00000141564. [Q8N122-1]
ENST00000544334; ENSP00000442479; ENSG00000141564.
ENST00000570891; ENSP00000460136; ENSG00000141564. [Q8N122-2]
GeneID57521.
KEGGhsa:57521.
UCSCuc002jys.3. human. [Q8N122-2]
uc002jyt.1. human. [Q8N122-1]

Organism-specific databases

CTD57521.
GeneCardsGC17P078518.
HGNCHGNC:30287. RPTOR.
HPACAB013514.
HPA029821.
MIM607130. gene.
neXtProtNX_Q8N122.
PharmGKBPA165432629.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG269318.
HOGENOMHOG000184479.
HOVERGENHBG059496.
InParanoidQ8N122.
KOK07204.
OMAFCDWSAK.
PhylomeDBQ8N122.
TreeFamTF105729.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_120956. Cellular responses to stress.
SignaLinkQ8N122.

Gene expression databases

ArrayExpressQ8N122.
BgeeQ8N122.
GenevestigatorQ8N122.

Family and domain databases

Gene3D1.25.10.10. 2 hits.
2.130.10.10. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR004083. Raptor.
IPR029347. Raptor_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERPTHR12848. PTHR12848. 1 hit.
PfamPF02985. HEAT. 1 hit.
PF14538. Raptor_N. 1 hit.
PF00400. WD40. 2 hits.
[Graphical view]
SMARTSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF48371. SSF48371. 2 hits.
SSF50978. SSF50978. 1 hit.
PROSITEPS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRPTOR.
GenomeRNAi57521.
NextBio35483332.
PROQ8N122.
SOURCESearch...

Entry information

Entry nameRPTOR_HUMAN
AccessionPrimary (citable) accession number: Q8N122
Secondary accession number(s): B2RN36 expand/collapse secondary AC list , C6KEF2, F5H7J5, Q8N4V9, Q8TB32, Q9P2P3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM