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Regulatory-associated protein of mTOR (Raptor) (p150 target of rapamycin (TOR)-scaffold protein)

 RPTOR_HUMAN             Reviewed;        1335 AA.
Q8N122; B2RN36; C6KEF2; F5H7J5; Q8N4V9; Q8TB32; Q9P2P3;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
22-NOV-2017, entry version 159.
RecName: Full=Regulatory-associated protein of mTOR;
Short=Raptor;
AltName: Full=p150 target of rapamycin (TOR)-scaffold protein;
Name=RPTOR; Synonyms=KIAA1303, RAPTOR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
INTERACTION WITH 4EBP1 AND RPS6KB1.
PubMed=12150925; DOI=10.1016/S0092-8674(02)00808-5;
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.
PubMed=12150926; DOI=10.1016/S0092-8674(02)00833-4;
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 GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
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., 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.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 995-1135 (ISOFORM 1).
TISSUE=Brain, Placenta, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 217-1335.
TISSUE=Brain;
PubMed=10718198; DOI=10.1093/dnares/7.1.65;
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 488-594 (ISOFORM 3), AND TISSUE
SPECIFICITY (ISOFORM 3).
PubMed=19388141; DOI=10.1016/j.mrfmmm.2009.01.001;
Sun C., Southard C., Di Rienzo A.;
"Characterization of a novel splicing variant in the RAPTOR gene.";
Mutat. Res. 662:88-92(2009).
[8]
INTERACTION WITH MTOR AND MLST8, IDENTIFICATION IN THE TORC1 COMPLEX,
AND TISSUE SPECIFICITY.
PubMed=12408816; DOI=10.1016/S1097-2765(02)00636-6;
Loewith R., Jacinto E., Wullschleger S., Lorberg A., Crespo J.L.,
Bonenfant D., Oppliger W., Jenoe P., Hall M.N.;
"Two TOR complexes, only one of which is rapamycin sensitive, have
distinct roles in cell growth control.";
Mol. Cell 10:457-468(2002).
[9]
INTERACTION WITH EIF4EBP1.
PubMed=12747827; DOI=10.1016/S0960-9822(03)00329-4;
Schalm S.S., Fingar D.C., Sabatini D.M., Blenis J.;
"TOS motif-mediated raptor binding regulates 4E-BP1 multisite
phosphorylation and function.";
Curr. Biol. 13:797-806(2003).
[10]
DISSOCIATION OF COMPLEX BY RAPAMYCIN.
PubMed=15066126; DOI=10.1111/j.1356-9597.2004.00727.x;
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).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
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).
[13]
INTERACTION WITH AKT1S1.
PubMed=17386266; DOI=10.1016/j.molcel.2007.03.003;
Sancak Y., Thoreen C.C., Peterson T.R., Lindquist R.A., Kang S.A.,
Spooner E., Carr S.A., Sabatini D.M.;
"PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein
kinase.";
Mol. Cell 25:903-915(2007).
[14]
PHOSPHORYLATION AT SER-719; SER-721 AND SER-722.
PubMed=18722121; DOI=10.1016/j.cub.2008.07.078;
Carriere A., Cargnello M., Julien L.A., Gao H., Bonneil E.,
Thibault P., Roux P.P.;
"Oncogenic MAPK signaling stimulates mTORC1 activity by promoting RSK-
mediated raptor phosphorylation.";
Curr. Biol. 18:1269-1277(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
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).
[16]
PHOSPHORYLATION AT SER-722 AND SER-792, MUTAGENESIS OF SER-722 AND
SER-792, AND INTERACTION WITH 14-3-3.
PubMed=18439900; DOI=10.1016/j.molcel.2008.03.003;
Gwinn D.M., Shackelford D.B., Egan D.F., Mihaylova M.M., Mery A.,
Vasquez D.S., Turk B.E., Shaw R.J.;
"AMPK phosphorylation of raptor mediates a metabolic checkpoint.";
Mol. Cell 30:214-226(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-877, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-719; SER-859; SER-863
AND SER-877, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
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).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
INTERACTION WITH ULK1.
PubMed=19211835; DOI=10.1091/mbc.E08-12-1248;
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.;
"Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200
complex required for autophagy.";
Mol. Biol. Cell 20:1981-1991(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-877, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859; SER-863 AND
SER-877, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[23]
SUBCELLULAR LOCATION.
PubMed=20381137; DOI=10.1016/j.cell.2010.02.024;
Sancak Y., Bar-Peled L., Zoncu R., Markhard A.L., Nada S.,
Sabatini D.M.;
"Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is
necessary for its activation by amino acids.";
Cell 141:290-303(2010).
[24]
PHOSPHORYLATION AT SER-696; THR-706; SER-855; SER-859; SER-863 AND
SER-877.
PubMed=19864431; DOI=10.1074/jbc.M109.029637;
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.;
"Regulation of mTOR complex 1 (mTORC1) by raptor Ser863 and multisite
phosphorylation.";
J. Biol. Chem. 285:80-94(2010).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859; SER-863 AND
SER-877, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863 AND SER-877, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[28]
INTERACTION WITH HTR6.
PubMed=23027611; DOI=10.1002/emmm.201201410;
Meffre J., Chaumont-Dubel S., Mannoury la Cour C., Loiseau F.,
Watson D.J., Dekeyne A., Seveno M., Rivet J.M., Gaven F., Deleris P.,
Herve D., Fone K.C., Bockaert J., Millan M.J., Marin P.;
"5-HT(6) receptor recruitment of mTOR as a mechanism for perturbed
cognition in schizophrenia.";
EMBO Mol. Med. 4:1043-1056(2012).
[29]
PHOSPHORYLATION AT SER-696; THR-706 AND SER-863.
PubMed=22493283; DOI=10.1074/jbc.M111.326538;
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.;
"Osmotic stress regulates mammalian target of rapamycin (mTOR) complex
1 via c-Jun N-terminal Kinase (JNK)-mediated Raptor protein
phosphorylation.";
J. Biol. Chem. 287:18398-18407(2012).
[30]
INTERACTION WITH G3BP1 AND SPAG5, AND SUBCELLULAR LOCATION.
PubMed=23953116; DOI=10.1016/j.cell.2013.07.031;
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.;
"Inhibition of mTORC1 by astrin and stress granules prevents apoptosis
in cancer cells.";
Cell 154:859-874(2013).
[31]
INTERACTION WITH PIH1D1.
PubMed=24036451; DOI=10.1016/j.febslet.2013.09.001;
Kamano Y., Saeki M., Egusa H., Kakihara Y., Houry W.A., Yatani H.,
Kamisaki Y.;
"PIH1D1 interacts with mTOR complex 1 and enhances ribosome RNA
transcription.";
FEBS Lett. 587:3303-3308(2013).
[32]
FUNCTION IN CILIOGENESIS.
PubMed=23727834; DOI=10.1093/hmg/ddt253;
Cardenas-Rodriguez M., Irigoin F., Osborn D.P., Gascue C.,
Katsanis N., Beales P.L., Badano J.L.;
"The Bardet-Biedl syndrome-related protein CCDC28B modulates mTORC2
function and interacts with SIN1 to control cilia length independently
of the mTOR complex.";
Hum. Mol. Genet. 22:4031-4042(2013).
[33]
INTERACTION WITH BRAT1.
PubMed=25657994;
So E.Y., Ouchi T.;
"The potential role of BRCA1-associated ATM activator-1 (BRAT1) in
regulation of mTOR.";
J. Cancer. Biol. Res. 1:0-0(2013).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696; SER-719; SER-722;
SER-859; SER-863; THR-865 AND SER-877, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-738 AND SER-877, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[36]
INTERACTION WITH LARP1 AND THE MTORC1 COMPLEX, AND SUBCELLULAR
LOCATION.
PubMed=25940091; DOI=10.1074/jbc.M114.621730;
Fonseca B.D., Zakaria C., Jia J.J., Graber T.E., Svitkin Y.,
Tahmasebi S., Healy D., Hoang H.D., Jensen J.M., Diao I.T.,
Lussier A., Dajadian C., Padmanabhan N., Wang W., Matta-Camacho E.,
Hearnden J., Smith E.M., Tsukumo Y., Yanagiya A., Morita M.,
Petroulakis E., Gonzalez J.L., Hernandez G., Alain T., Damgaard C.K.;
"La-related protein 1 (LARP1) represses terminal oligopyrimidine (TOP)
mRNA translation downstream of mTOR complex 1 (mTORC1).";
J. Biol. Chem. 290:15996-16020(2015).
[37]
INTERACTION WITH WAC.
PubMed=26812014; DOI=10.1016/j.devcel.2015.12.019;
David-Morrison G., Xu Z., Rui Y.N., Charng W.L., Jaiswal M.,
Yamamoto S., Xiong B., Zhang K., Sandoval H., Duraine L., Zuo Z.,
Zhang S., Bellen H.J.;
"WAC regulates mTOR activity by acting as an adaptor for the TTT and
Pontin/Reptin complexes.";
Dev. Cell 36:139-151(2016).
-!- 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.
{ECO:0000269|PubMed:12150925, ECO:0000269|PubMed:12150926,
ECO:0000269|PubMed:23727834}.
-!- SUBUNIT: Part of the mammalian target of rapamycin complex 1
(mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and
DEPTOR (PubMed:12150925, PubMed:12408816, PubMed:17386266,
PubMed:25940091). mTORC1 binds to and is inhibited by FKBP12-
rapamycin (PubMed:12408816, PubMed:15066126). Binds directly to
4EBP1 and RPS6KB1 independently of its association with MTOR
(PubMed:12150925, PubMed:12150926). Binds preferentially to poorly
or non-phosphorylated forms of EIF4EBP1, and this binding is
critical to the ability of MTOR to catalyze phosphorylation
(PubMed:12747827). 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
(PubMed:19211835). Interacts (when phosphorylated by AMPK) with
14-3-3 protein, leading to inhibition of its activity
(PubMed:18439900). Interacts with SPAG5; SPAG5 competes with MTOR
for RPTOR-binding, resulting in decreased mTORC1 formation.
Interacts with WAC; WAC positively regulates MTOR activity by
promoting the assembly of the TTT complex composed of TELO2, TTI1
and TTI2 and the RUVBL complex composed of RUVBL1 and RUVBL2 into
the TTT-RUVBL complex which leads to the dimerization of the
mTORC1 complex and its subsequent activation (PubMed:26812014).
Interacts with G3BP1. The complex formed with G3BP1 AND SPAG5 is
increased by oxidative stress (PubMed:23953116). Interacts with
HTR6 (PubMed:23027611). Interacts with PIH1D1 (PubMed:24036451).
Interacts with LARP1 (PubMed:25940091). Interacts with BRAT1
(PubMed:25657994). {ECO:0000269|PubMed:12150925,
ECO:0000269|PubMed:12150926, ECO:0000269|PubMed:12408816,
ECO:0000269|PubMed:12747827, ECO:0000269|PubMed:17386266,
ECO:0000269|PubMed:18439900, ECO:0000269|PubMed:19211835,
ECO:0000269|PubMed:23027611, ECO:0000269|PubMed:23953116,
ECO:0000269|PubMed:24036451, ECO:0000269|PubMed:25657994,
ECO:0000269|PubMed:25940091, ECO:0000269|PubMed:26812014}.
-!- INTERACTION:
Q13541:EIF4EBP1; NbExp=5; IntAct=EBI-1567928, EBI-74090;
Q13283:G3BP1; NbExp=4; IntAct=EBI-1567928, EBI-1047359;
Q8WUA4:GTF3C2; NbExp=3; IntAct=EBI-1567928, EBI-1237062;
Q9P2J5:LARS; NbExp=3; IntAct=EBI-1567928, EBI-356077;
P45983:MAPK8; NbExp=6; IntAct=EBI-1567928, EBI-286483;
Q9BVC4:MLST8; NbExp=3; IntAct=EBI-1567928, EBI-1387471;
Q13615:MTMR3; NbExp=3; IntAct=EBI-1567928, EBI-371938;
P42345:MTOR; NbExp=45; IntAct=EBI-1567928, EBI-359260;
Q9JLN9:Mtor (xeno); NbExp=5; IntAct=EBI-1567928, EBI-1571628;
Q8TCU6:PREX1; NbExp=2; IntAct=EBI-1567928, EBI-1046542;
P62820:RAB1A; NbExp=4; IntAct=EBI-1567928, EBI-716845;
P67999:Rps6kb1 (xeno); NbExp=2; IntAct=EBI-1567928, EBI-2639458;
Q9HB90:RRAGC; NbExp=6; IntAct=EBI-1567928, EBI-752390;
Q96EB6:SIRT1; NbExp=3; IntAct=EBI-1567928, EBI-1802965;
Q96R06:SPAG5; NbExp=9; IntAct=EBI-1567928, EBI-413317;
O75385:ULK1; NbExp=3; IntAct=EBI-1567928, EBI-908831;
-!- SUBCELLULAR LOCATION: Cytoplasm. Lysosome. Cytoplasmic granule
{ECO:0000269|PubMed:25940091}. 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8N122-1; Sequence=Displayed;
Name=2;
IsoId=Q8N122-2; Sequence=VSP_010174;
Name=3;
IsoId=Q8N122-3; Sequence=VSP_054042;
-!- 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.
{ECO:0000269|PubMed:12150925, ECO:0000269|PubMed:12408816}.
-!- PTM: 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.
{ECO:0000269|PubMed:18439900, ECO:0000269|PubMed:18722121,
ECO:0000269|PubMed:19864431, ECO:0000269|PubMed:22493283}.
-!- SIMILARITY: Belongs to the WD repeat RAPTOR family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY090663; AAM09075.1; -; mRNA.
EMBL; AB082951; BAC06490.1; -; mRNA.
EMBL; AC016245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC109327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC127496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC133012; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471099; EAW89618.1; -; Genomic_DNA.
EMBL; BC025180; AAH25180.1; -; mRNA.
EMBL; BC033258; AAH33258.1; -; mRNA.
EMBL; BC064515; AAH64515.1; -; mRNA.
EMBL; BC136652; AAI36653.1; -; mRNA.
EMBL; BC136654; AAI36655.1; -; mRNA.
EMBL; AB037724; BAA92541.1; -; mRNA.
EMBL; GQ183898; ACS44766.1; -; mRNA.
CCDS; CCDS11773.1; -. [Q8N122-1]
CCDS; CCDS54175.1; -. [Q8N122-3]
RefSeq; NP_001156506.1; NM_001163034.1. [Q8N122-3]
RefSeq; NP_065812.1; NM_020761.2. [Q8N122-1]
UniGene; Hs.133044; -.
PDB; 5H64; EM; 4.40 A; B/b=1-1335.
PDBsum; 5H64; -.
ProteinModelPortal; Q8N122; -.
SMR; Q8N122; -.
BioGrid; 121582; 132.
CORUM; Q8N122; -.
DIP; DIP-39482N; -.
ELM; Q8N122; -.
IntAct; Q8N122; 45.
MINT; MINT-3038940; -.
STRING; 9606.ENSP00000307272; -.
ChEMBL; CHEMBL3120040; -.
iPTMnet; Q8N122; -.
PhosphoSitePlus; Q8N122; -.
BioMuta; RPTOR; -.
DMDM; 46577501; -.
EPD; Q8N122; -.
MaxQB; Q8N122; -.
PaxDb; Q8N122; -.
PeptideAtlas; Q8N122; -.
PRIDE; Q8N122; -.
DNASU; 57521; -.
Ensembl; ENST00000306801; ENSP00000307272; ENSG00000141564. [Q8N122-1]
Ensembl; ENST00000544334; ENSP00000442479; ENSG00000141564. [Q8N122-3]
Ensembl; ENST00000570891; ENSP00000460136; ENSG00000141564. [Q8N122-2]
GeneID; 57521; -.
KEGG; hsa:57521; -.
UCSC; uc002jys.5; human. [Q8N122-1]
CTD; 57521; -.
DisGeNET; 57521; -.
EuPathDB; HostDB:ENSG00000141564.13; -.
GeneCards; RPTOR; -.
HGNC; HGNC:30287; RPTOR.
HPA; CAB013514; -.
HPA; HPA064306; -.
MIM; 607130; gene.
neXtProt; NX_Q8N122; -.
OpenTargets; ENSG00000141564; -.
PharmGKB; PA165432629; -.
eggNOG; KOG1517; Eukaryota.
eggNOG; ENOG410XQKJ; LUCA.
GeneTree; ENSGT00640000091541; -.
HOGENOM; HOG000184479; -.
HOVERGEN; HBG059496; -.
InParanoid; Q8N122; -.
KO; K07204; -.
OMA; PIEMALW; -.
OrthoDB; EOG091G00H9; -.
PhylomeDB; Q8N122; -.
TreeFam; TF105729; -.
Reactome; R-HSA-1632852; Macroautophagy.
Reactome; R-HSA-165159; mTOR signalling.
Reactome; R-HSA-166208; mTORC1-mediated signalling.
Reactome; R-HSA-3371571; HSF1-dependent transactivation.
Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
SignaLink; Q8N122; -.
SIGNOR; Q8N122; -.
ChiTaRS; RPTOR; human.
GeneWiki; RPTOR; -.
GenomeRNAi; 57521; -.
PRO; PR:Q8N122; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000141564; -.
ExpressionAtlas; Q8N122; baseline and differential.
Genevisible; Q8N122; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0031931; C:TORC1 complex; IDA:UniProtKB.
GO; GO:0071889; F:14-3-3 protein binding; IDA:UniProtKB.
GO; GO:0030674; F:protein binding, bridging; IDA:WormBase.
GO; GO:0032403; F:protein complex binding; IPI:UniProtKB.
GO; GO:0030295; F:protein kinase activator activity; IDA:WormBase.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IDA:WormBase.
GO; GO:0001030; F:RNA polymerase III type 1 promoter DNA binding; IDA:UniProtKB.
GO; GO:0001031; F:RNA polymerase III type 2 promoter DNA binding; IDA:UniProtKB.
GO; GO:0001032; F:RNA polymerase III type 3 promoter DNA binding; IDA:UniProtKB.
GO; GO:0001156; F:TFIIIC-class transcription factor binding; IDA:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; TAS:Reactome.
GO; GO:0016049; P:cell growth; IMP:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:UniProtKB.
GO; GO:0071233; P:cellular response to leucine; IDA:CAFA.
GO; GO:0031669; P:cellular response to nutrient levels; IMP:UniProtKB.
GO; GO:0009267; P:cellular response to starvation; IBA:GO_Central.
GO; GO:0030307; P:positive regulation of cell growth; IMP:ParkinsonsUK-UCL.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:ParkinsonsUK-UCL.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:ParkinsonsUK-UCL.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IMP:ParkinsonsUK-UCL.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0032008; P:positive regulation of TOR signaling; IDA:UniProtKB.
GO; GO:0045945; P:positive regulation of transcription from RNA polymerase III promoter; IMP:UniProtKB.
GO; GO:0010506; P:regulation of autophagy; IBA:GO_Central.
GO; GO:0008361; P:regulation of cell size; IMP:UniProtKB.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0016241; P:regulation of macroautophagy; TAS:Reactome.
GO; GO:0031929; P:TOR signaling; IDA:UniProtKB.
GO; GO:0038202; P:TORC1 signaling; IMP:WormBase.
Gene3D; 1.25.10.10; -; 2.
Gene3D; 2.130.10.10; -; 2.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000357; HEAT.
InterPro; IPR004083; Raptor.
InterPro; IPR029347; Raptor_N.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR12848; PTHR12848; 1.
Pfam; PF02985; HEAT; 1.
Pfam; PF14538; Raptor_N; 1.
Pfam; PF00400; WD40; 1.
SMART; SM01302; Raptor_N; 1.
SMART; SM00320; WD40; 7.
SUPFAM; SSF48371; SSF48371; 2.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Lysosome; Phosphoprotein; Reference proteome; Repeat; WD repeat.
CHAIN 1 1335 Regulatory-associated protein of mTOR.
/FTId=PRO_0000051200.
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.
COMPBIAS 881 887 Poly-Ser.
MOD_RES 696 696 Phosphoserine; by MAPK8.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19864431,
ECO:0000269|PubMed:22493283}.
MOD_RES 706 706 Phosphothreonine; by MAPK8.
{ECO:0000269|PubMed:19864431,
ECO:0000269|PubMed:22493283}.
MOD_RES 719 719 Phosphoserine; by RPS6KA1.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:18722121}.
MOD_RES 721 721 Phosphoserine; by RPS6KA1.
{ECO:0000269|PubMed:18722121}.
MOD_RES 722 722 Phosphoserine; by AMPK and RPS6KA1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:18439900,
ECO:0000269|PubMed:18722121}.
MOD_RES 738 738 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 792 792 Phosphoserine; by AMPK.
{ECO:0000269|PubMed:18439900}.
MOD_RES 855 855 Phosphoserine.
{ECO:0000269|PubMed:19864431}.
MOD_RES 859 859 Phosphoserine; by MTOR.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19864431}.
MOD_RES 863 863 Phosphoserine; by MAPK8 and MTOR.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19864431,
ECO:0000269|PubMed:22493283}.
MOD_RES 865 865 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 877 877 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:19864431}.
VAR_SEQ 380 1335 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_010174.
VAR_SEQ 504 661 Missing (in isoform 3).
{ECO:0000303|PubMed:19388141}.
/FTId=VSP_054042.
MUTAGEN 722 722 S->A: Abolishes AMPK-mediated
phosphorylation; when associated with A-
792. {ECO:0000269|PubMed:18439900}.
MUTAGEN 792 792 S->A: Abolishes AMPK-mediated
phosphorylation; when associated with A-
722. {ECO:0000269|PubMed:18439900}.
CONFLICT 217 218 LE -> RQ (in Ref. 6; BAA92541).
{ECO:0000305}.
SEQUENCE 1335 AA; 149038 MW; 688ED1943F45045A CRC64;
MESEMLQSPL LGLGEEDEAD LTDWNLPLAF MKKRHCEKIE GSKSLAQSWR MKDRMKTVSV
ALVLCLNVGV DPPDVVKTTP CARLECWIDP LSMGPQKALE TIGANLQKQY ENWQPRARYK
QSLDPTVDEV KKLCTSLRRN AKEERVLFHY NGHGVPRPTV NGEVWVFNKN YTQYIPLSIY
DLQTWMGSPS IFVYDCSNAG LIVKSFKQFA LQREQELEVA AINPNHPLAQ MPLPPSMKNC
IQLAACEATE LLPMIPDLPA DLFTSCLTTP IKIALRWFCM QKCVSLVPGV TLDLIEKIPG
RLNDRRTPLG ELNWIFTAIT DTIAWNVLPR DLFQKLFRQD LLVASLFRNF LLAERIMRSY
NCTPVSSPRL PPTYMHAMWQ AWDLAVDICL SQLPTIIEEG TAFRHSPFFA EQLTAFQVWL
TMGVENRNPP EQLPIVLQVL LSQVHRLRAL DLLGRFLDLG PWAVSLALSV GIFPYVLKLL
QSSARELRPL LVFIWAKILA VDSSCQADLV KDNGHKYFLS VLADPYMPAE HRTMTAFILA
VIVNSYHTGQ EACLQGNLIA ICLEQLNDPH PLLRQWVAIC LGRIWQNFDS ARWCGVRDSA
HEKLYSLLSD PIPEVRCAAV FALGTFVGNS AERTDHSTTI DHNVAMMLAQ LVSDGSPMVR
KELVVALSHL VVQYESNFCT VALQFIEEEK NYALPSPATT EGGSLTPVRD SPCTPRLRSV
SSYGNIRAVA TARSLNKSLQ NLSLTEESGG AVAFSPGNLS TSSSASSTLG SPENEEHILS
FETIDKMRRA SSYSSLNSLI GVSFNSVYTQ IWRVLLHLAA DPYPEVSDVA MKVLNSIAYK
ATVNARPQRV LDTSSLTQSA PASPTNKGVH IHQAGGSPPA SSTSSSSLTN DVAKQPVSRD
LPSGRPGTTG PAGAQYTPHS HQFPRTRKMF DKGPEQTADD ADDAAGHKSF ISATVQTGFC
DWSARYFAQP VMKIPEEHDL ESQIRKEREW RFLRNSRVRR QAQQVIQKGI TRLDDQIFLN
RNPGVPSVVK FHPFTPCIAV ADKDSICFWD WEKGEKLDYF HNGNPRYTRV TAMEYLNGQD
CSLLLTATDD GAIRVWKNFA DLEKNPEMVT AWQGLSDMLP TTRGAGMVVD WEQETGLLMS
SGDVRIVRIW DTDREMKVQD IPTGADSCVT SLSCDSHRSL IVAGLGDGSI RVYDRRMALS
ECRVMTYREH TAWVVKASLQ KRPDGHIVSV SVNGDVRIFD PRMPESVNVL QIVKGLTALD
IHPQADLIAC GSVNQFTAIY NSSGELINNI KYYDGFMGQR VGAISCLAFH PHWPHLAVGS
NDYYISVYSV EKRVR


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