Q8N122 (RPTOR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1335 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.1 Ref.2
Subunit structure	Interacts with MTOR By similarity. 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. Ref.1 Ref.2 Ref.7 Ref.8 Ref.12 Ref.15 Ref.18
Subcellular location	Cytoplasm. Lysosome. Note: Targeting to lysosomes depends on amino acid availability. Ref.21
Tissue specificity	Highly expressed in skeletal muscle, and in a lesser extent in brain, lung, small intestine, kidney and placenta. Ref.1 Ref.7
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.13 Ref.15 Ref.22 Ref.26
Sequence similarities	Belongs to the WD repeat RAPTOR family. Contains 7 WD repeats.

Ontologies

Keywords
Cellular component	Cytoplasm Lysosome
Coding sequence diversity	Alternative splicing
Domain	Repeat WD repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	TOR signaling cascade Inferred from direct assay Ref.21. Source: UniProtKB cell cycle arrest Traceable author statement. Source: Reactome cell growth Inferred from mutant phenotype Ref.21. Source: UniProtKB cellular response to amino acid stimulus Inferred from mutant phenotype Ref.21. 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 cascade Inferred from direct assay Ref.2Ref.15. Source: UniProtKB 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_component	TORC1 complex Inferred from direct assay PubMed 15467718. Source: UniProtKB cytosol Traceable author statement. Source: Reactome lysosome Inferred from direct assay Ref.21. Source: UniProtKB
Molecular_function	14-3-3 protein binding Inferred from direct assay Ref.15. 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF4EBP1	Q13541	4	EBI-1567928,EBI-74090
LARS	Q9P2J5	3	EBI-1567928,EBI-356077
MLST8	Q9BVC4	3	EBI-1567928,EBI-1387471
MTOR	P42345	12	EBI-1567928,EBI-359260
Mtor	Q9JLN9	4	EBI-1567928,EBI-1571628	From a different organism.
PREX1	Q8TCU6	2	EBI-1567928,EBI-1046542
Rps6kb1	P67999	2	EBI-1567928,EBI-2639458	From a different organism.
SIRT1	Q96EB6	3	EBI-1567928,EBI-1802965

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1335	1335	Regulatory-associated protein of mTOR		PRO_0000051200
Regions
	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
	Compositional bias	881 – 887	7	Poly-Ser
Amino acid modifications
	Modified residue	696	1	Phosphoserine; by MAPK8 Ref.22 Ref.26
	Modified residue	706	1	Phosphothreonine; by MAPK8 Ref.22 Ref.26
	Modified residue	719	1	Phosphoserine; by RPS6KA1 Ref.13 Ref.17
	Modified residue	721	1	Phosphoserine; by RPS6KA1 Ref.13
	Modified residue	722	1	Phosphoserine; by AMPK and RPS6KA1 Ref.13 Ref.15
	Modified residue	792	1	Phosphoserine; by AMPK Ref.15
	Modified residue	855	1	Phosphoserine Ref.22
	Modified residue	857	1	Phosphothreonine By similarity
	Modified residue	859	1	Phosphoserine; by MTOR Ref.17 Ref.20 Ref.22 Ref.23
	Modified residue	863	1	Phosphoserine; by MAPK8 and MTOR Ref.11 Ref.17 Ref.20 Ref.22 Ref.23 Ref.25 Ref.26
	Modified residue	877	1	Phosphoserine Ref.16 Ref.17 Ref.19 Ref.20 Ref.22 Ref.23 Ref.25
Natural variations
	Alternative sequence	380 – 1335	956	Missing in isoform 2.		VSP_010174
Experimental info
	Mutagenesis	722	1	S → A: Abolishes AMPK-mediated phosphorylation; when associated with A-792. Ref.15
	Mutagenesis	792	1	S → A: Abolishes AMPK-mediated phosphorylation; when associated with A-722. Ref.15
	Sequence conflict	217 – 218	2	LE → RQ in BAA92541. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 688ED1943F45045A	FASTA	1,335	149,038
	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
	Isoform 2 [UniParc]. Checksum: D67B01D4E68E859E	FASTA	379	43,256
	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 NCTPVSSPRL PPTYMHAMW

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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.
[19]	"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, MASS SPECTROMETRY.
[20]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[21]	"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.
[22]	"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.
[23]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"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].
[25]	"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, MASS SPECTROMETRY.
[26]	"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.
+	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.
IPI	IPI00166044. IPI00410411.
RefSeq	NP_065812.1. NM_020761.2.
UniGene	Hs.133044.
3D structure databases
ProteinModelPortal	Q8N122.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-39482N.
IntAct	Q8N122. 18 interactions.
MINT	MINT-3038940.
STRING	9606.ENSP00000307272.
PTM databases
PhosphoSite	Q8N122.
Polymorphism databases
DMDM	46577501.
Proteomic databases
PaxDb	Q8N122.
PRIDE	Q8N122.
Protocols and materials databases
DNASU	57521.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000306801; ENSP00000307272; ENSG00000141564. ENST00000570891; ENSP00000460136; ENSG00000141564.
GeneID	57521.
KEGG	hsa:57521.
UCSC	uc002jys.3. human. uc002jyt.1. human.
Organism-specific databases
CTD	57521.
GeneCards	GC17P078518.
HGNC	HGNC:30287. RPTOR.
HPA	CAB013514. HPA029821.
MIM	607130. gene.
neXtProt	NX_Q8N122.
PharmGKB	PA165432629.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG269318.
HOGENOM	HOG000184479.
HOVERGEN	HBG059496.
InParanoid	Q8N122.
KO	K07204.
OMA	SAHEKLC.
OrthoDB	EOG46Q6RQ.
PhylomeDB	Q8N122.
Enzyme and pathway databases
Pathway_Interaction_DB	pi3kciaktpathway. Class I PI3K signaling events mediated by Akt. mtor_4pathway. mTOR signaling pathway.
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	Q8N122.
Bgee	Q8N122.
Genevestigator	Q8N122.
Family and domain databases
Gene3D	1.25.10.10. 2 hits. 2.130.10.10. 1 hit.
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR000357. HEAT. IPR004083. Raptor. IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR017986. WD40_repeat_dom. [Graphical view]
PANTHER	PTHR12848. PTHR12848. 1 hit.
Pfam	PF02985. HEAT. 1 hit. PF00400. WD40. 2 hits. [Graphical view]
PRINTS	PR01547. YEAST176DUF.
SMART	SM00320. WD40. 7 hits. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit. SSF50978. WD40_like. 1 hit.
PROSITE	PS00678. WD_REPEATS_1. False negative. PS50082. WD_REPEATS_2. False negative. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	57521.
NextBio	63899.
SOURCE	Search...

Entry information

Entry name

RPTOR_HUMAN

Accession

Primary (citable) accession number: Q8N122
Secondary accession number(s): B2RN36 , Q8N4V9, Q8TB32, Q9P2P3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.