Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q6R327 (RICTR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rapamycin-insensitive companion of mTOR
Alternative name(s):
AVO3 homolog
Short name=hAVO3
Gene names
Name:RICTOR
Synonyms:KIAA1999
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1708 AA.
Sequence statusComplete.
Protein existenceEvidence 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 diversityAlternative splicing
Polymorphism
   Molecular functionDevelopmental protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-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 cell migration

Inferred from electronic annotation. Source: InterPro

regulation of protein kinase B signaling

Inferred from direct assay Ref.8. Source: UniProtKB

   Cellular_componentTORC2 complex

Inferred from direct assay Ref.1Ref.7. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

   Molecular_functionribosome binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17081708Rapamycin-insensitive companion of mTOR
PRO_0000308179

Regions

Region1 – 789789Interaction with NBN
Compositional bias1016 – 105843Ser-rich

Amino acid modifications

Modified residue211Phosphoserine Ref.9 Ref.12 Ref.13 Ref.14 Ref.16 Ref.18 Ref.20
Modified residue11351Phosphothreonine; by RPS6KB1 Ref.17
Modified residue12821Phosphoserine Ref.14
Modified residue12841Phosphoserine Ref.16
Modified residue13881Phosphoserine Ref.14 Ref.16
Modified residue13961Phosphoserine Ref.13 Ref.14
Modified residue14111Phosphoserine Ref.16
Modified residue15911Phosphoserine Ref.20

Natural variations

Alternative sequence252 – 2576RILAPY → NFSTLY in isoform 2.
VSP_038362
Alternative sequence258 – 17081451Missing in isoform 2.
VSP_038363
Alternative sequence13791R → RIDFKKKHVGGIRSLRPTIT NNLFR in isoform 3. Ref.21
VSP_052581
Natural variant8371S → F. Ref.2 Ref.5
Corresponds to variant rs2043112 [ dbSNP | Ensembl ].
VAR_051320

Experimental info

Sequence conflict5451E → G in CAH18135. Ref.2
Sequence conflict8151F → L in CAH18135. Ref.2
Sequence conflict12831N → S in CAH18135. Ref.2
Sequence conflict16991Q → R in AAH51729. Ref.5

Sequences

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

Last modified July 5, 2004. Version 1.
Checksum: DB7B1E4A45DAE2AB

FASTA1,708192,218
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 57DCA4610207FA94
Show »

FASTA25728,988
Isoform 3 [UniParc].

Checksum: 984F516A908EEC3A
Show »

FASTA1,732195,011

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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.
RefSeqNP_001272368.1. NM_001285439.1.
NP_001272369.1. NM_001285440.1.
NP_689969.2. NM_152756.4.
UniGeneHs.407926.

3D structure databases

ProteinModelPortalQ6R327.
SMRQ6R327. Positions 308-335, 399-428, 752-777, 890-975.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid128962. 46 interactions.
DIPDIP-39479N.
IntActQ6R327. 24 interactions.
MINTMINT-3976651.
STRING9606.ENSP00000349959.

Chemistry

ChEMBLCHEMBL1795179.

PTM databases

PhosphoSiteQ6R327.

Polymorphism databases

DMDM74710068.

Proteomic databases

PaxDbQ6R327.
PRIDEQ6R327.

Protocols and materials databases

DNASU253260.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296782; ENSP00000296782; ENSG00000164327. [Q6R327-3]
ENST00000357387; ENSP00000349959; ENSG00000164327. [Q6R327-1]
ENST00000511516; ENSP00000423019; ENSG00000164327. [Q6R327-4]
GeneID253260.
KEGGhsa:253260.
UCSCuc003jlo.2. human. [Q6R327-3]
uc003jlp.2. human. [Q6R327-1]

Organism-specific databases

CTD253260.
GeneCardsGC05M038977.
H-InvDBHIX0021738.
HGNCHGNC:28611. RICTOR.
HPAHPA037802.
MIM609022. gene.
neXtProtNX_Q6R327.
PharmGKBPA165660455.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG305760.
HOGENOMHOG000154126.
HOVERGENHBG060827.
InParanoidQ6R327.
KOK08267.
OMARFHEMKK.
OrthoDBEOG7SBNMS.
PhylomeDBQ6R327.
TreeFamTF343656.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ6R327.
BgeeQ6R327.
GenevestigatorQ6R327.

Family and domain databases

Gene3D1.25.10.10. 4 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR028268. Pianissimo_fam.
IPR028267. Pianissimo_N.
IPR028272. RICTOR.
[Graphical view]
PANTHERPTHR13298. PTHR13298. 1 hit.
PTHR13298:SF9. PTHR13298:SF9. 1 hit.
PfamPF14664. RICTOR_N. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 5 hits.
ProtoNetSearch...

Other

GeneWikiRICTOR.
GenomeRNAi253260.
NextBio92081.
PROQ6R327.
SOURCESearch...

Entry information

Entry nameRICTR_HUMAN
AccessionPrimary (citable) accession number: Q6R327
Secondary accession number(s): B2RNX0 expand/collapse secondary AC list , B7ZMF7, Q68DT5, Q86UB7, Q8N3A0, Q8NCM6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM