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Reviewed, UniProtKB/Swiss-Prot Q6R327 (RICTR_HUMAN)

Last modified June 16, 2009. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Rapamycin-insensitive companion of mTOR
Gene names
Name: RICTOR
Synonyms: KIAA1999
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1708 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Plays an essential role in embryonic growth and development By similarity. Part of the TORC2 complex which plays a critical role in AKT1 'Ser-473' phosphorylation, and may modulate the phosphorylation of PKCA and regulate actin cytoskeleton organization. Ref.1 Ref.6 Ref.2

Subunit structure

Forms part of the target of rapamycin 2 complex (TORC2) comprised of FRAP1, LST8, PROTOR1, RICTOR and MAPKAP1. TORC2 does not bind to and is not sensitive to FKBP12-rapamycin. Binds directly to FRAP1 and PROTOR1 within the TORC2 complex. May interact with PROTOR2.

Sequence similarities

Belongs to the pianissimo family.

Sequence caution

The sequence CAH18135.1 differs from that shown. Reason: Frameshift at position 251.

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.2 (identifier: Q6R327-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1467-1504: Missing.
Note: No experimental confirmation available.
Isoform 3 Ref.2 (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

Compositional bias1016 – 105843Ser-rich

Amino acid modifications

Modified residue211Phosphoserine Ref.7 Ref.10 Ref.11 Ref.12
Modified residue12821Phosphoserine Ref.12
Modified residue12951Phosphothreonine Ref.10
Modified residue13531Phosphoserine Ref.11
Modified residue13861Phosphotyrosine Ref.12
Modified residue13881Phosphoserine Ref.12
Modified residue13961Phosphoserine Ref.11 Ref.12

Natural variations

Alternative sequence13791R → RIDFKKKHVGGIRSLRPTIT NNLFR in isoform 3. Ref.2
VSP_052581
Alternative sequence1467 – 150438Missing in isoform 2. Ref.2
VSP_052582
Natural variant8371S → F: dbSNP rs2043112. Ref.2 Ref.4
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.4

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.

Checksum: 3C81D383638CBB34
Show »

FASTA1,670188,135
Isoform 3.

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: 15268862] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, IDENTIFICATION IN TORC2 COMPLEX, INTERACTION WITH FRAP1.
[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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [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]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].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT PHE-837.
Tissue: Brain and Lymph.
[5]"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: 12056414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 434-1708 (ISOFORM 1).
Tissue: Brain.
[6]"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: 15718470] [Abstract]
Cited for: FUNCTION.
[7]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"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: 17461779] [Abstract]
Cited for: IDENTIFICATION IN TORC2 COMPLEX, INTERACTION WITH PROTOR1 AND PROTOR2.
[9]"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: 17599906] [Abstract]
Cited for: IDENTIFICATION IN TORC2 COMPLEX, INTERACTION WITH PROTOR1.
[10]"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: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND THR-1295, MASS SPECTROMETRY.
[11]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-1353 AND SER-1396, MASS SPECTROMETRY.
[12]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-1282; TYR-1386; SER-1388 AND SER-1396, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AY515854 mRNA. Translation: AAS79796.1.
AL834497 mRNA. Translation: CAD39155.1.
CR749280 mRNA. Translation: CAH18135.1. Frameshift.
CH471119 Genomic DNA. Translation: EAW55980.1.
BC051729 mRNA. Translation: AAH51729.1.
BC137163 mRNA. Translation: AAI37164.1.
BC137164 mRNA. Translation: AAI37165.1.
AB082530 mRNA. Translation: BAC02708.1.
IPIIPI00166528.
IPI00455500.
IPI00868848.
RefSeqNP_689969.2.
UniGeneHs.407926

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ6R327. 33 interactions.

PTM databases

PhosphoSiteQ6R327.

Proteomic databases

PRIDEQ6R327.

Genome annotation databases

EnsemblENSG00000164327. Homo sapiens. [Contig view]
GeneID253260.
KEGGhsa:253260.

Organism-specific databases

GeneCardsGC05M038977.
H-InvDBHIX0021738.
MIM609022. gene.
HUGESearch...

Phylogenomic databases

HOGENOMQ6R327.
HOVERGENQ6R327.
OMAQ6R327. RFHEMKK.

Enzyme and pathway databases

Pathway_Interaction_DBpi3kciaktpathway. Class I PI3K signaling events mediated by Akt.

Gene expression databases

ArrayExpressQ6R327.
BgeeQ6R327.

Family and domain databases

InterProIPR000651. RasGef_N.
[Graphical view]
PfamPF00618. RasGEF_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio92081.
SOURCESearch...

Entry information

Entry nameRICTR_HUMAN
AccessionPrimary (citable) accession number: Q6R327
Secondary accession number(s): B2RNX0 expand/collapse secondary AC list , Q68DT5, Q86UB7, Q8N3A0, Q8NCM6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: July 5, 2004
Last modified: June 16, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant 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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents