Q6R327 (RICTR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rapamycin-insensitive companion of mTOR

Alternative name(s):
AVO3 homolog
Short name=hAVO3

Gene names

Name:	RICTOR
Synonyms:	KIAA1999

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 › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1708 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. Plays an essential role in embryonic growth and development. Ref.1 Ref.7 Ref.8
Subunit structure	Part of the mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR. Contrary to mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-rapamycin. Binds directly to MTOR and PRR5 within the TORC2 complex. Interacts with CCDC28B and NBN. May interact with PRR5L. Ref.1 Ref.7 Ref.10 Ref.11 Ref.21 Ref.22
Post-translational modification	Phosphorylated by MTOR; when part of mTORC2. Phosphorylated at Thr-1135 by RPS6KB1; phosphorylation of RICTOR inhibits mTORC2 and AKT1 signaling. Ref.7 Ref.17
Sequence similarities	Belongs to the pianissimo family.
Sequence caution	The sequence CAH18135.1 differs from that shown. Reason: Wrong choice of CDS.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Developmental protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Fc-epsilon receptor signaling pathway Traceable author statement. Source: Reactome T cell costimulation Traceable author statement. Source: Reactome TOR signaling Inferred from electronic annotation. Source: InterPro actin cytoskeleton reorganization Inferred from mutant phenotype Ref.1. Source: UniProtKB embryo development Inferred from sequence or structural similarity. Source: UniProtKB epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome innate immune response Traceable author statement. Source: Reactome neurotrophin TRK receptor signaling pathway Traceable author statement. Source: Reactome phosphatidylinositol-mediated signaling Traceable author statement. Source: Reactome positive regulation of TOR signaling Inferred from mutant phenotype Ref.7. Source: UniProtKB positive regulation of actin filament polymerization Inferred from electronic annotation. Source: Ensembl positive regulation of endothelial cell proliferation Inferred from electronic annotation. Source: Ensembl positive regulation of peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: Ensembl positive regulation of protein kinase B signaling Inferred from electronic annotation. Source: Ensembl regulation of Rac GTPase activity Inferred from electronic annotation. Source: Ensembl regulation of actin cytoskeleton organization Inferred from mutant phenotype Ref.7. Source: UniProtKB regulation of protein kinase B signaling Inferred from direct assay Ref.8. Source: UniProtKB
Cellular_component	TORC2 complex Inferred from direct assay Ref.1Ref.7. Source: UniProtKB cytosol Traceable author statement. Source: Reactome
Molecular_function	protein binding Inferred from physical interaction Ref.7. Source: UniProtKB ribosome binding Inferred from electronic annotation. Source: Ensembl
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ILK	Q13418	8	EBI-1387196,EBI-747644
MTOR	P42345	25	EBI-1387196,EBI-359260
PREX1	Q8TCU6	3	EBI-1387196,EBI-1046542

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.1 (identifier: Q6R327-1)

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 Ref.21 (identifier: Q6R327-4)

The sequence of this isoform differs from the canonical sequence as follows:
     252-257: RILAPY → NFSTLY
     258-1708: Missing.

Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Isoform 3 Ref.21 (identifier: Q6R327-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1379-1379: R → RIDFKKKHVGGIRSLRPTITNNLFR

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1708	1708	Rapamycin-insensitive companion of mTOR		PRO_0000308179
Regions
	Region	1 – 789	789	Interaction with NBN
	Compositional bias	1016 – 1058	43	Ser-rich
Amino acid modifications
	Modified residue	21	1	Phosphoserine Ref.9 Ref.12 Ref.13 Ref.14 Ref.16 Ref.18 Ref.20
	Modified residue	1135	1	Phosphothreonine; by RPS6KB1 Ref.17
	Modified residue	1282	1	Phosphoserine Ref.14
	Modified residue	1284	1	Phosphoserine Ref.16
	Modified residue	1388	1	Phosphoserine Ref.14 Ref.16
	Modified residue	1396	1	Phosphoserine Ref.13 Ref.14
	Modified residue	1411	1	Phosphoserine Ref.16
	Modified residue	1591	1	Phosphoserine Ref.20
Natural variations
	Alternative sequence	252 – 257	6	RILAPY → NFSTLY in isoform 2.		VSP_038362
	Alternative sequence	258 – 1708	1451	Missing in isoform 2.		VSP_038363
	Alternative sequence	1379	1	R → RIDFKKKHVGGIRSLRPTIT NNLFR in isoform 3. Ref.21		VSP_052581
	Natural variant	837	1	S → F. Ref.2 Ref.5 Corresponds to variant rs2043112 [ dbSNP | Ensembl ].		VAR_051320
Experimental info
	Sequence conflict	545	1	E → G in CAH18135. Ref.2
	Sequence conflict	815	1	F → L in CAH18135. Ref.2
	Sequence conflict	1283	1	N → S in CAH18135. Ref.2
	Sequence conflict	1699	1	Q → R in AAH51729. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: DB7B1E4A45DAE2AB	FASTA	1,708	192,218
	10 20 30 40 50 60 MAAIGRGRSL KNLRVRGRND SGEENVPLDL TREPSDNLRE ILQNVARLQG VSNMRKLGHL 70 80 90 100 110 120 NNFTKLLCDI GHSEEKLGFH YEDIIICLRL ALLNEAKEVR AAGLRALRYL IQDSSILQKV 130 140 150 160 170 180 LKLKVDYLIA RCIDIQQSNE VERTQALRLV RKMITVNASL FPSSVTNSLI AVGNDGLQER 190 200 210 220 230 240 DRMVRACIAI ICELALQNPE VVALRGGLNT ILKNVIDCQL SRINEALITT ILHLLNHPKT 250 260 270 280 290 300 RQYVRADVEL ERILAPYTDF HYRHSPDTAE GQLKEDREAR FLASKMGIIA TFRSWAGIIN 310 320 330 340 350 360 LCKPGNSGIQ SLIGVLCIPN MEIRRGLLEV LYDIFRLPLP VVTEEFIEAL LSVDPGRFQD 370 380 390 400 410 420 SWRLSDGFVA AEAKTILPHR ARSRPDLMDN YLALILSAFI RNGLLEGLVE VITNSDDHIS 430 440 450 460 470 480 VRATILLGEL LHMANTILPH SHSHHLHCLP TLMNMAASFD IPKEKRLRAS AALNCLKRFH 490 500 510 520 530 540 EMKKRGPKPY SLHLDHIIQK AIATHQKRDQ YLRVQKDIFI LKDTEEALLI NLRDSQVLQH 550 560 570 580 590 600 KENLEWNWNL IGTILKWPNV NLRNYKDEQL HRFVRRLLYF YKPSSKLYAN LDLDFAKAKQ 610 620 630 640 650 660 LTVVGCQFTE FLLESEEDGQ GYLEDLVKDI VQWLNASSGM KPERSLQNNG LLTTLSQHYF 670 680 690 700 710 720 LFIGTLSCHP HGVKMLEKCS VFQCLLNLCS LKNQDHLLKL TVSSLDYSRD GLARVILSKI 730 740 750 760 770 780 LTAATDACRL YATKHLRVLL RANVEFFNNW GIELLVTQLH DKNKTISSEA LDILDEACED 790 800 810 820 830 840 KANLHALIQM KPALSHLGDK GLLLLLRFLS IPKGFSYLNE RGYVAKQLEK WHREYNSKYV 850 860 870 880 890 900 DLIEEQLNEA LTTYRKPVDG DNYVRRSNQR LQRPHVYLPI HLYGQLVHHK TGCHLLEVQN 910 920 930 940 950 960 IITELCRNVR TPDLDKWEEI KKLKASLWAL GNIGSSNWGL NLLQEENVIP DILKLAKQCE 970 980 990 1000 1010 1020 VLSIRGTCVY VLGLIAKTKQ GCDILKCHNW DAVRHSRKHL WPVVPDDVEQ LCNELSSIPS 1030 1040 1050 1060 1070 1080 TLSLNSESTS SRHNSESESV PSSMFILEDD RFGSSSTSTF FLDINEDTEP TFYDRSGPIK 1090 1100 1110 1120 1130 1140 DKNSFPFFAS SKLVKNRILN SLTLPNKKHR SSSDPKGGKL SSESKTSNRR IRTLTEPSVD 1150 1160 1170 1180 1190 1200 FNHSDDFTPI STVQKTLQLE TSFMGNKHIE DTGSTPSIGE NDLKFTKNFG TENHRENTSR 1210 1220 1230 1240 1250 1260 ERLVVESSTS SHMKIRSQSF NTDTTTSGIS SMSSSPSRET VGVDATTMDT DCGSMSTVVS 1270 1280 1290 1300 1310 1320 TKTIKTSHYL TPQSNHLSLS KSNSVSLVPP GSSHTLPRRA QSLKAPSIAT IKSLADCNFS 1330 1340 1350 1360 1370 1380 YTSSRDAFGY ATLKRLQQQR MHPSLSHSEA LASPAKDVLF TDTITMKANS FESRLTPSRF 1390 1400 1410 1420 1430 1440 MKALSYASLD KEDLLSPINQ NTLQRSSSVR SMVSSATYGG SDDYIGLALP VDINDIFQVK 1450 1460 1470 1480 1490 1500 DIPYFQTKNI PPHDDRGARA FAHDAGGLPS GTGGLVKNSF HLLRQQMSLT EIMNSIHSDA 1510 1520 1530 1540 1550 1560 SLFLESTEDT GLQEHTDDNC LYCVCIEILG FQPSNQLSAI CSHSDFQDIP YSDWCEQTIH 1570 1580 1590 1600 1610 1620 NPLEVVPSKF SGISGCSDGV SQEGSASSTK STELLLGVKT IPDDTPMCRI LLRKEVLRLV 1630 1640 1650 1660 1670 1680 INLSSSVSTK CHETGLLTIK EKYPQTFDDI CLYSEVSHLL SHCTFRLPCR RFIQELFQDV 1690 1700 QFLQMHEEAE AVLATPPKQP IVDTSAES
	Isoform 2 [UniParc]. Checksum: 57DCA4610207FA94	FASTA	257	28,988
	10 20 30 40 50 60 MAAIGRGRSL KNLRVRGRND SGEENVPLDL TREPSDNLRE ILQNVARLQG VSNMRKLGHL 70 80 90 100 110 120 NNFTKLLCDI GHSEEKLGFH YEDIIICLRL ALLNEAKEVR AAGLRALRYL IQDSSILQKV 130 140 150 160 170 180 LKLKVDYLIA RCIDIQQSNE VERTQALRLV RKMITVNASL FPSSVTNSLI AVGNDGLQER 190 200 210 220 230 240 DRMVRACIAI ICELALQNPE VVALRGGLNT ILKNVIDCQL SRINEALITT ILHLLNHPKT 250 RQYVRADVEL ENFSTLY
	Isoform 3 [UniParc]. Checksum: 984F516A908EEC3A	FASTA	1,732	195,011
	10 20 30 40 50 60 MAAIGRGRSL KNLRVRGRND SGEENVPLDL TREPSDNLRE ILQNVARLQG VSNMRKLGHL 70 80 90 100 110 120 NNFTKLLCDI GHSEEKLGFH YEDIIICLRL ALLNEAKEVR AAGLRALRYL IQDSSILQKV 130 140 150 160 170 180 LKLKVDYLIA RCIDIQQSNE VERTQALRLV RKMITVNASL FPSSVTNSLI AVGNDGLQER 190 200 210 220 230 240 DRMVRACIAI ICELALQNPE VVALRGGLNT ILKNVIDCQL SRINEALITT ILHLLNHPKT 250 260 270 280 290 300 RQYVRADVEL ERILAPYTDF HYRHSPDTAE GQLKEDREAR FLASKMGIIA TFRSWAGIIN 310 320 330 340 350 360 LCKPGNSGIQ SLIGVLCIPN MEIRRGLLEV LYDIFRLPLP VVTEEFIEAL LSVDPGRFQD 370 380 390 400 410 420 SWRLSDGFVA AEAKTILPHR ARSRPDLMDN YLALILSAFI RNGLLEGLVE VITNSDDHIS 430 440 450 460 470 480 VRATILLGEL LHMANTILPH SHSHHLHCLP TLMNMAASFD IPKEKRLRAS AALNCLKRFH 490 500 510 520 530 540 EMKKRGPKPY SLHLDHIIQK AIATHQKRDQ YLRVQKDIFI LKDTEEALLI NLRDSQVLQH 550 560 570 580 590 600 KENLEWNWNL IGTILKWPNV NLRNYKDEQL HRFVRRLLYF YKPSSKLYAN LDLDFAKAKQ 610 620 630 640 650 660 LTVVGCQFTE FLLESEEDGQ GYLEDLVKDI VQWLNASSGM KPERSLQNNG LLTTLSQHYF 670 680 690 700 710 720 LFIGTLSCHP HGVKMLEKCS VFQCLLNLCS LKNQDHLLKL TVSSLDYSRD GLARVILSKI 730 740 750 760 770 780 LTAATDACRL YATKHLRVLL RANVEFFNNW GIELLVTQLH DKNKTISSEA LDILDEACED 790 800 810 820 830 840 KANLHALIQM KPALSHLGDK GLLLLLRFLS IPKGFSYLNE RGYVAKQLEK WHREYNSKYV 850 860 870 880 890 900 DLIEEQLNEA LTTYRKPVDG DNYVRRSNQR LQRPHVYLPI HLYGQLVHHK TGCHLLEVQN 910 920 930 940 950 960 IITELCRNVR TPDLDKWEEI KKLKASLWAL GNIGSSNWGL NLLQEENVIP DILKLAKQCE 970 980 990 1000 1010 1020 VLSIRGTCVY VLGLIAKTKQ GCDILKCHNW DAVRHSRKHL WPVVPDDVEQ LCNELSSIPS 1030 1040 1050 1060 1070 1080 TLSLNSESTS SRHNSESESV PSSMFILEDD RFGSSSTSTF FLDINEDTEP TFYDRSGPIK 1090 1100 1110 1120 1130 1140 DKNSFPFFAS SKLVKNRILN SLTLPNKKHR SSSDPKGGKL SSESKTSNRR IRTLTEPSVD 1150 1160 1170 1180 1190 1200 FNHSDDFTPI STVQKTLQLE TSFMGNKHIE DTGSTPSIGE NDLKFTKNFG TENHRENTSR 1210 1220 1230 1240 1250 1260 ERLVVESSTS SHMKIRSQSF NTDTTTSGIS SMSSSPSRET VGVDATTMDT DCGSMSTVVS 1270 1280 1290 1300 1310 1320 TKTIKTSHYL TPQSNHLSLS KSNSVSLVPP GSSHTLPRRA QSLKAPSIAT IKSLADCNFS 1330 1340 1350 1360 1370 1380 YTSSRDAFGY ATLKRLQQQR MHPSLSHSEA LASPAKDVLF TDTITMKANS FESRLTPSRI 1390 1400 1410 1420 1430 1440 DFKKKHVGGI RSLRPTITNN LFRFMKALSY ASLDKEDLLS PINQNTLQRS SSVRSMVSSA 1450 1460 1470 1480 1490 1500 TYGGSDDYIG LALPVDINDI FQVKDIPYFQ TKNIPPHDDR GARAFAHDAG GLPSGTGGLV 1510 1520 1530 1540 1550 1560 KNSFHLLRQQ MSLTEIMNSI HSDASLFLES TEDTGLQEHT DDNCLYCVCI EILGFQPSNQ 1570 1580 1590 1600 1610 1620 LSAICSHSDF QDIPYSDWCE QTIHNPLEVV PSKFSGISGC SDGVSQEGSA SSTKSTELLL 1630 1640 1650 1660 1670 1680 GVKTIPDDTP MCRILLRKEV LRLVINLSSS VSTKCHETGL LTIKEKYPQT FDDICLYSEV 1690 1700 1710 1720 1730 SHLLSHCTFR LPCRRFIQEL FQDVQFLQMH EEAEAVLATP PKQPIVDTSA ES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton." Sarbassov D.D., Ali S.M., Kim D.-H., Guertin D.A., Latek R.R., Erdjument-Bromage H., Tempst P., Sabatini D.M. Curr. Biol. 14:1296-1302(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, IDENTIFICATION IN THE TORC2 COMPLEX, INTERACTION WITH MTOR.
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 932-1708 (ISOFORM 3), VARIANT PHE-837. Tissue: Amygdala.
[3]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [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] (ISOFORMS 1 AND 3), VARIANT PHE-837. Tissue: Brain and Lymph.
[6]	"Characterization of size-fractionated cDNA libraries generated by the in vitro recombination-assisted method." Ohara O., Nagase T., Mitsui G., Kohga H., Kikuno R., Hiraoka S., Takahashi Y., Kitajima S., Saga Y., Koseki H. DNA Res. 9:47-57(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 434-1708 (ISOFORM 1). Tissue: Brain.
[7]	"Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive." Jacinto E., Loewith R., Schmidt A., Lin S., Ruegg M.A., Hall A., Hall M.N. Nat. Cell Biol. 6:1122-1128(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE TORC2 COMPLEX, PHOSPHORYLATION.
[8]	"Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex." Sarbassov D.D., Guertin D.A., Ali S.M., Sabatini D.M. Science 307:1098-1101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[10]	"Identification of Protor as a novel Rictor-binding component of mTOR complex-2." Pearce L.R., Huang X., Boudeau J., Pawlowski R., Wullschleger S., Deak M., Ibrahim A.F.M., Gourlay R., Magnuson M.A., Alessi D.R. Biochem. J. 405:513-522(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE TORC2 COMPLEX, INTERACTION WITH PRR5 AND PRR5L.
[11]	"PRR5, a novel component of mTOR complex 2, regulates platelet-derived growth factor receptor beta expression and signaling." Woo S.-Y., Kim D.-H., Jun C.-B., Kim Y.-M., Haar E.V., Lee S.-I., Hegg J.W., Bandhakavi S., Griffin T.J., Kim D.-H. J. Biol. Chem. 282:25604-25612(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE TORC2 COMPLEX, INTERACTION WITH PRR5.
[12]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[13]	"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-21 AND SER-1396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[14]	"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-21; SER-1282; SER-1388 AND SER-1396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[15]	"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].
[16]	"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-21; SER-1284; SER-1388 AND SER-1411, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[17]	"mTORC1-activated S6K1 phosphorylates Rictor on threonine 1135 and regulates mTORC2 signaling." Julien L.A., Carriere A., Moreau J., Roux P.P. Mol. Cell. Biol. 30:908-921(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-1135.
[18]	"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-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[19]	"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].
[20]	"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-21 AND SER-1591, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"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: INTERACTION WITH CCDC28B.
[22]	"Interaction between NBS1 and the mTOR/Rictor/SIN1 complex through specific domains." Wang J.Q., Chen J.H., Chen Y.C., Chen M.Y., Hsieh C.Y., Teng S.C., Wu K.J. PLoS ONE 8:E65586-E65586(2013) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NBN.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY515854 mRNA. Translation: AAS79796.1. AL834497 mRNA. Translation: CAD39155.1. CR749280 mRNA. Translation: CAH18135.1. Sequence problems. AC008964 Genomic DNA. No translation available. AC109467 Genomic DNA. No translation available. CH471119 Genomic DNA. Translation: EAW55980.1. BC051729 mRNA. Translation: AAH51729.1. BC137163 mRNA. Translation: AAI37164.1. BC137164 mRNA. Translation: AAI37165.1. BC144509 mRNA. Translation: AAI44510.1. AB082530 mRNA. Translation: BAC02708.1.
CCDS	CCDS34148.1. [Q6R327-1] CCDS68861.1. [Q6R327-3]
RefSeq	NP_001272368.1. NM_001285439.1. [Q6R327-3] NP_001272369.1. NM_001285440.1. NP_689969.2. NM_152756.4. [Q6R327-1]
UniGene	Hs.407926.
3D structure databases
ProteinModelPortal	Q6R327.
SMR	Q6R327. Positions 308-335, 399-428, 752-777, 890-975.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	128962. 47 interactions.
DIP	DIP-39479N.
IntAct	Q6R327. 24 interactions.
MINT	MINT-3976651.
STRING	9606.ENSP00000349959.
Chemistry
ChEMBL	CHEMBL1795179.
PTM databases
PhosphoSite	Q6R327.
Polymorphism databases
DMDM	74710068.
Proteomic databases
MaxQB	Q6R327.
PaxDb	Q6R327.
PRIDE	Q6R327.
Protocols and materials databases
DNASU	253260.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000296782; ENSP00000296782; ENSG00000164327. [Q6R327-3] ENST00000357387; ENSP00000349959; ENSG00000164327. [Q6R327-1] ENST00000511516; ENSP00000423019; ENSG00000164327. [Q6R327-4]
GeneID	253260.
KEGG	hsa:253260.
UCSC	uc003jlo.2. human. [Q6R327-3] uc003jlp.2. human. [Q6R327-1]
Organism-specific databases
CTD	253260.
GeneCards	GC05M038977.
H-InvDB	HIX0021738.
HGNC	HGNC:28611. RICTOR.
HPA	HPA037802.
MIM	609022. gene.
neXtProt	NX_Q6R327.
PharmGKB	PA165660455.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG305760.
HOGENOM	HOG000154126.
HOVERGEN	HBG060827.
InParanoid	Q6R327.
KO	K08267.
OMA	RFHEMKK.
OrthoDB	EOG7SBNMS.
PhylomeDB	Q6R327.
TreeFam	TF343656.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_116125. Disease. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	Q6R327.
Bgee	Q6R327.
Genevestigator	Q6R327.
Family and domain databases
Gene3D	1.25.10.10. 4 hits.
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR028268. Pianissimo_fam. IPR028267. Pianissimo_N. IPR029453. Rictor_IV. IPR029451. RICTOR_M. IPR029259. RICTOR_phospho. IPR029452. RICTOR_V. [Graphical view]
PANTHER	PTHR13298. PTHR13298. 1 hit.
Pfam	PF14663. RasGEF_N_2. 1 hit. PF14666. RICTOR_M. 1 hit. PF14664. RICTOR_N. 1 hit. PF14665. RICTOR_phospho. 1 hit. PF14668. RICTOR_V. 1 hit. [Graphical view]
SUPFAM	SSF48371. SSF48371. 5 hits.
ProtoNet	Search...
Other
GeneWiki	RICTOR.
GenomeRNAi	253260.
NextBio	92081.
PRO	Q6R327.
SOURCE	Search...

Entry information

Entry name

RICTR_HUMAN

Accession

Primary (citable) accession number: Q6R327
Secondary accession number(s): B2RNX0 , B7ZMF7, Q68DT5, Q86UB7, Q8N3A0, Q8NCM6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 2007
Last sequence update:	July 5, 2004
Last modified:	July 9, 2014
This is version 97 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.