RICTOR

Functionⁱ

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.3 Publications

GO - Molecular functionⁱ

enzyme activator activity Source: GO_Central
protein kinase binding
Source: ParkinsonsUK-UCL
Inferred from physical interactionⁱ
- 21177249
ribosome binding Source: Ensembl

GO - Biological processⁱ

actin cytoskeleton reorganization
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 15268862
embryo development Source: UniProtKB
establishment of cell polarity Source: GO_Central
establishment or maintenance of actin cytoskeleton polarity Source: GO_Central
peptidyl-serine phosphorylation
Source: ParkinsonsUK-UCL
Inferred from genetic interactionⁱ
- 21177249
phosphatidylinositol-mediated signaling Source: Reactome
positive regulation of actin filament polymerization Source: Ensembl
positive regulation of endothelial cell proliferation Source: Ensembl
positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
positive regulation of protein kinase B signaling Source: GO_Central
positive regulation of TOR signaling
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 15467718
regulation of actin cytoskeleton organization
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 15467718
regulation of establishment of cell polarity Source: Ensembl
regulation of gene expression Source: Ensembl
regulation of GTPase activity Source: Ensembl
regulation of inflammatory response Source: Ensembl
regulation of peptidyl-serine phosphorylation Source: Ensembl
regulation of phosphorylation Source: GO_Central
regulation of protein kinase B signaling
Source: UniProtKB
Inferred from direct assayⁱ
- 15718470
T cell costimulation Source: Reactome
TOR signaling Source: InterPro

Complete GO annotation...

Keywords - Molecular functionⁱ

Developmental protein

Enzyme and pathway databases

Reactomeⁱ	R-HSA-1257604. PIP3 activates AKT signaling. R-HSA-389357. CD28 dependent PI3K/Akt signaling. R-HSA-5218920. VEGFR2 mediated vascular permeability. R-HSA-5674400. Constitutive Signaling by AKT1 E17K in Cancer. R-HSA-6804757. Regulation of TP53 Degradation.
SIGNORⁱ	Q6R327.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Rapamycin-insensitive companion of mTOR Alternative name(s): AVO3 homolog Short name: hAVO3
Gene namesⁱ	Name:RICTORImported Manual assertion inferred from database entriesⁱ EMBL:EAW55980.1 Synonyms:KIAA1999Imported Manual assertion inferred from database entriesⁱ EMBL:BAC02708.1
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	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
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 5

Organism-specific databases

HGNCⁱ	HGNC:28611. RICTOR.

HGNCⁱ

HGNC:28611. RICTOR.

Subcellular locationⁱ

GO - Cellular componentⁱ

cytosol Source: Reactome
TORC2 complex
Source: UniProtKB
Inferred from direct assayⁱ

Complete GO annotation...

Pathology & Biotechⁱ

Organism-specific databases

PharmGKBⁱ	PA165660455.

PharmGKBⁱ

PA165660455.

Chemistry

ChEMBLⁱ	CHEMBL1795179.

ChEMBLⁱ

CHEMBL1795179.

Polymorphism and mutation databases

BioMutaⁱ	RICTOR.
DMDMⁱ	74710068.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Chainⁱ	1 – 1708	1708	Rapamycin-insensitive companion of mTOR		PRO_0000308179	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description
Modified residueⁱ	21 – 21	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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]. Ref.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]. Ref.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]. Ref.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]. Ref.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]. Ref.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]. Ref.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]. Ref.22 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-1103; THR-1135; SER-1162; SER-1278; SER-1282; THR-1295; SER-1302; SER-1313; THR-1332; SER-1346; SER-1353 AND SER-1385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1103 – 1103	1	PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.22 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-1103; THR-1135; SER-1162; SER-1278; SER-1282; THR-1295; SER-1302; SER-1313; THR-1332; SER-1346; SER-1353 AND SER-1385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1135 – 1135	1	Phosphothreonine; by RPS6KB1Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.22 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-1103; THR-1135; SER-1162; SER-1278; SER-1282; THR-1295; SER-1302; SER-1313; THR-1332; SER-1346; SER-1353 AND SER-1385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 1 Publication Manual assertion based on experiment inⁱ Ref.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.
Modified residueⁱ	1162 – 1162	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.22 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-1103; THR-1135; SER-1162; SER-1278; SER-1282; THR-1295; SER-1302; SER-1313; THR-1332; SER-1346; SER-1353 AND SER-1385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1235 – 1235	1	PhosphoserineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q6QI06 (RICTR_MOUSE)
Modified residueⁱ	1278 – 1278	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.22 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-1103; THR-1135; SER-1162; SER-1278; SER-1282; THR-1295; SER-1302; SER-1313; THR-1332; SER-1346; SER-1353 AND SER-1385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1282 – 1282	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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]. Ref.22 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-1103; THR-1135; SER-1162; SER-1278; SER-1282; THR-1295; SER-1302; SER-1313; THR-1332; SER-1346; SER-1353 AND SER-1385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1284 – 1284	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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].
Modified residueⁱ	1295 – 1295	1	PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.22 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-1103; THR-1135; SER-1162; SER-1278; SER-1282; THR-1295; SER-1302; SER-1313; THR-1332; SER-1346; SER-1353 AND SER-1385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1302 – 1302	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.22 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-1103; THR-1135; SER-1162; SER-1278; SER-1282; THR-1295; SER-1302; SER-1313; THR-1332; SER-1346; SER-1353 AND SER-1385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1313 – 1313	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.22 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-1103; THR-1135; SER-1162; SER-1278; SER-1282; THR-1295; SER-1302; SER-1313; THR-1332; SER-1346; SER-1353 AND SER-1385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1332 – 1332	1	PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.22 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-1103; THR-1135; SER-1162; SER-1278; SER-1282; THR-1295; SER-1302; SER-1313; THR-1332; SER-1346; SER-1353 AND SER-1385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1346 – 1346	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.22 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-1103; THR-1135; SER-1162; SER-1278; SER-1282; THR-1295; SER-1302; SER-1313; THR-1332; SER-1346; SER-1353 AND SER-1385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1353 – 1353	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.22 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-1103; THR-1135; SER-1162; SER-1278; SER-1282; THR-1295; SER-1302; SER-1313; THR-1332; SER-1346; SER-1353 AND SER-1385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1385 – 1385	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.22 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-1103; THR-1135; SER-1162; SER-1278; SER-1282; THR-1295; SER-1302; SER-1313; THR-1332; SER-1346; SER-1353 AND SER-1385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.24 "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome." Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H. J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1385, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1388 – 1388	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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]. Ref.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].
Modified residueⁱ	1396 – 1396	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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]. Ref.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].
Modified residueⁱ	1411 – 1411	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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].
Modified residueⁱ	1591 – 1591	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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].

Post-translational modificationⁱ

Phosphorylated by MTOR; when part of mTORC2. Phosphorylated at Thr-1135 by RPS6KB1; phosphorylation of RICTOR inhibits mTORC2 and AKT1 signaling.2 Publications

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

EPDⁱ	Q6R327.
MaxQBⁱ	Q6R327.
PaxDbⁱ	Q6R327.
PeptideAtlasⁱ	Q6R327.
PRIDEⁱ	Q6R327.

PTM databases

iPTMnetⁱ	Q6R327.
PhosphoSiteⁱ	Q6R327.

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000164327.
ExpressionAtlasⁱ	Q6R327. baseline and differential.
Genevisibleⁱ	Q6R327. HS.

Organism-specific databases

HPAⁱ	HPA037802. HPA037803.

Interactionⁱ

Subunit structureⁱ

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.6 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
ILK	Q13418	8	EBI-1387196,EBI-747644
MTOR	P42345	31	EBI-1387196,EBI-359260
PREX1	Q8TCU6	3	EBI-1387196,EBI-1046542

With

Entry

#Exp.

IntAct

Notes

ILK

Q13418

8

EBI-1387196,EBI-747644

MTOR

P42345

31

EBI-1387196,EBI-359260

PREX1

Q8TCU6

3

EBI-1387196,EBI-1046542

GO - Molecular functionⁱ

protein kinase binding
Source: ParkinsonsUK-UCL
Inferred from physical interactionⁱ
- 21177249

Protein-protein interaction databases

BioGridⁱ	128962. 83 interactions.
DIPⁱ	DIP-39479N.
IntActⁱ	Q6R327. 34 interactions.
MINTⁱ	MINT-3976651.
STRINGⁱ	9606.ENSP00000349959.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q6R327.
SMRⁱ	Q6R327. Positions 308-335, 400-428, 720-778, 891-989.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Regionⁱ	1 – 789	789	Interaction with NBN			Add BLAST

Compositional bias

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Compositional biasⁱ	1016 – 1058	43	Ser-richSequence analysis			Add BLAST

Sequence similaritiesⁱ

Belongs to the RICTOR family.Curated

Phylogenomic databases

eggNOGⁱ	KOG3694. Eukaryota. ENOG410XQ5Z. LUCA.
GeneTreeⁱ	ENSGT00390000002096.
HOGENOMⁱ	HOG000154126.
HOVERGENⁱ	HBG060827.
InParanoidⁱ	Q6R327.
KOⁱ	K08267.
OMAⁱ	RIDFKKK.
OrthoDBⁱ	EOG091G01CV.
PhylomeDBⁱ	Q6R327.
TreeFamⁱ	TF343656.

Family and domain databases

Gene3Dⁱ	1.25.10.10. 4 hits.
InterProⁱ	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]
PANTHERⁱ	PTHR13298. PTHR13298. 3 hits.
Pfamⁱ	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]
SMARTⁱ	SM01307. RICTOR_M. 1 hit. SM01308. RICTOR_N. 1 hit. SM01309. RICTOR_phospho. 1 hit. SM01310. RICTOR_V. 1 hit. [Graphical view]
SUPFAMⁱ	SSF48371. SSF48371. 5 hits.

Sequences (3)ⁱ

Sequence statusⁱ: Complete.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket Added to basket

Isoform 11 Publication (identifier: Q6R327-1) [UniParc]FASTA Add to basket

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.

« Hide

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

IVDTSAES

Length:1,708

Mass (Da):192,218

Last modified:July 5, 2004 - v1

Checksum:ⁱDB7B1E4A45DAE2AB

GO

Isoform 2 (identifier: Q6R327-4) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MAAIGRGRSL KNLRVRGRND SGEENVPLDL TREPSDNLRE ILQNVARLQG 
        60         70         80         90        100
VSNMRKLGHL NNFTKLLCDI GHSEEKLGFH YEDIIICLRL ALLNEAKEVR 
       110        120        130        140        150
AAGLRALRYL IQDSSILQKV LKLKVDYLIA RCIDIQQSNE VERTQALRLV 
       160        170        180        190        200
RKMITVNASL FPSSVTNSLI AVGNDGLQER DRMVRACIAI ICELALQNPE 
       210        220        230        240        250
VVALRGGLNT ILKNVIDCQL SRINEALITT ILHLLNHPKT RQYVRADVEL 

ENFSTLY

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.

Show »

Length:257

Mass (Da):28,988

Checksum:ⁱ57DCA4610207FA94

GO

Isoform 3 (identifier: Q6R327-3) [UniParc]FASTA Add to basket

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

« Hide

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

Note: No experimental confirmation available.Curated

Show »

Length:1,732

Mass (Da):195,011

Checksum:ⁱ984F516A908EEC3A

GO

Sequence cautionⁱ

The sequence CAH18135 differs from that shown.Wrong choice of CDS.Curated

Experimental Info

Feature key	Position(s)	Length	Description
Sequence conflictⁱ	545 – 545	1	E → G in CAH18135 (PubMed:17974005).Curated
Sequence conflictⁱ	815 – 815	1	F → L in CAH18135 (PubMed:17974005).Curated
Sequence conflictⁱ	1283 – 1283	1	N → S in CAH18135 (PubMed:17974005).Curated
Sequence conflictⁱ	1699 – 1699	1	Q → R in AAH51729 (PubMed:15489334).Curated

Natural variant

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Natural variantⁱ	837 – 837	1	S → F.2 Publications Manual assertion based on experiment inⁱ Ref.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. Ref.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. Corresponds to variant rs2043112 [ dbSNP \| Ensembl ].		VAR_051320

Alternative sequence

Feature key	Position(s)	Length	Description	Feature identifier	Actions
Alternative sequenceⁱ	252 – 257	6	RILAPY → NFSTLY in isoform 2. 1 Publication Manual assertion based on opinion inⁱ Ref.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.	VSP_038362
Alternative sequenceⁱ	258 – 1708	1451	Missing in isoform 2. 1 Publication Manual assertion based on opinion inⁱ Ref.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.	VSP_038363	Add BLAST
Alternative sequenceⁱ	1379 – 1379	1	R → RIDFKKKHVGGIRSLRPTIT NNLFR in isoform 3. 2 Publications Manual assertion based on opinion inⁱ Ref.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. Ref.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.	VSP_052581

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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.
CCDSⁱ	CCDS34148.1. [Q6R327-1] CCDS68861.1. [Q6R327-3]
RefSeqⁱ	NP_001272368.1. NM_001285439.1. [Q6R327-3] NP_001272369.1. NM_001285440.1. NP_689969.2. NM_152756.4. [Q6R327-1]
UniGeneⁱ	Hs.407926.

Genome annotation databases

Ensemblⁱ	ENST00000296782; ENSP00000296782; ENSG00000164327. [Q6R327-3] ENST00000357387; ENSP00000349959; ENSG00000164327. [Q6R327-1] ENST00000511516; ENSP00000423019; ENSG00000164327. [Q6R327-4]
GeneIDⁱ	253260.
KEGGⁱ	hsa:253260.
UCSCⁱ	uc003jlo.4. human. [Q6R327-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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.
CCDSⁱ	CCDS34148.1. [Q6R327-1] CCDS68861.1. [Q6R327-3]
RefSeqⁱ	NP_001272368.1. NM_001285439.1. [Q6R327-3] NP_001272369.1. NM_001285440.1. NP_689969.2. NM_152756.4. [Q6R327-1]
UniGeneⁱ	Hs.407926.

3D structure databases

ProteinModelPortalⁱ	Q6R327.
SMRⁱ	Q6R327. Positions 308-335, 400-428, 720-778, 891-989.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	128962. 83 interactions.
DIPⁱ	DIP-39479N.
IntActⁱ	Q6R327. 34 interactions.
MINTⁱ	MINT-3976651.
STRINGⁱ	9606.ENSP00000349959.

Chemistry

ChEMBLⁱ	CHEMBL1795179.

ChEMBLⁱ

CHEMBL1795179.

PTM databases

iPTMnetⁱ	Q6R327.
PhosphoSiteⁱ	Q6R327.

Polymorphism and mutation databases

BioMutaⁱ	RICTOR.
DMDMⁱ	74710068.

Proteomic databases

EPDⁱ	Q6R327.
MaxQBⁱ	Q6R327.
PaxDbⁱ	Q6R327.
PeptideAtlasⁱ	Q6R327.
PRIDEⁱ	Q6R327.

Protocols and materials databases

DNASUⁱ	253260.
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000296782; ENSP00000296782; ENSG00000164327. [Q6R327-3] ENST00000357387; ENSP00000349959; ENSG00000164327. [Q6R327-1] ENST00000511516; ENSP00000423019; ENSG00000164327. [Q6R327-4]
GeneIDⁱ	253260.
KEGGⁱ	hsa:253260.
UCSCⁱ	uc003jlo.4. human. [Q6R327-1]

Organism-specific databases

CTDⁱ	253260.
GeneCardsⁱ	RICTOR.
H-InvDB	HIX0021738.
HGNCⁱ	HGNC:28611. RICTOR.
HPAⁱ	HPA037802. HPA037803.
MIMⁱ	609022. gene.
neXtProtⁱ	NX_Q6R327.
PharmGKBⁱ	PA165660455.
HUGEⁱ	Search...
GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3694. Eukaryota. ENOG410XQ5Z. LUCA.
GeneTreeⁱ	ENSGT00390000002096.
HOGENOMⁱ	HOG000154126.
HOVERGENⁱ	HBG060827.
InParanoidⁱ	Q6R327.
KOⁱ	K08267.
OMAⁱ	RIDFKKK.
OrthoDBⁱ	EOG091G01CV.
PhylomeDBⁱ	Q6R327.
TreeFamⁱ	TF343656.

Enzyme and pathway databases

Reactomeⁱ	R-HSA-1257604. PIP3 activates AKT signaling. R-HSA-389357. CD28 dependent PI3K/Akt signaling. R-HSA-5218920. VEGFR2 mediated vascular permeability. R-HSA-5674400. Constitutive Signaling by AKT1 E17K in Cancer. R-HSA-6804757. Regulation of TP53 Degradation.
SIGNORⁱ	Q6R327.

Miscellaneous databases

GeneWikiⁱ	RICTOR.
GenomeRNAiⁱ	253260.
PROⁱ	Q6R327.
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000164327.
ExpressionAtlasⁱ	Q6R327. baseline and differential.
Genevisibleⁱ	Q6R327. HS.

Family and domain databases

Gene3Dⁱ	1.25.10.10. 4 hits.
InterProⁱ	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]
PANTHERⁱ	PTHR13298. PTHR13298. 3 hits.
Pfamⁱ	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]
SMARTⁱ	SM01307. RICTOR_M. 1 hit. SM01308. RICTOR_N. 1 hit. SM01309. RICTOR_phospho. 1 hit. SM01310. RICTOR_V. 1 hit. [Graphical view]
SUPFAMⁱ	SSF48371. SSF48371. 5 hits.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ

RICTR_HUMAN

Accessionⁱ

Primary (citable) accession number: Q6R327
Secondary accession number(s): B2RNX0

Q8NCM6

Entry historyⁱ

Integrated into UniProtKB/Swiss-Prot:	October 23, 2007
Last sequence update:	July 5, 2004
Last modified:	September 7, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry statusⁱ

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.

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

Human chromosome 5
Human chromosome 5: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
SIMILARITY comments
Index of protein domains and families

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

UniProtKB

UniParc

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UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q6R327 (RICTR_HUMAN)

UniProt

Q6R327 - RICTR_HUMAN

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Rapamycin-insensitive companion of mTOR

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<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>Provides information on the disease(s) and phenotype(s) associated with a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

Chemistry

Polymorphism and mutation databases

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.</p><p><a href='../manual/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Protein-protein interaction databases

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Compositional bias

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequences (3)i

<p>Reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.</p><p><a href='../manual/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequences (3)ⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ