Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q6R327

- RICTR_HUMAN

UniProt

Q6R327 - RICTR_HUMAN

Protein

Rapamycin-insensitive companion of mTOR

Gene

RICTOR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. protein binding Source: UniProtKB
    2. ribosome binding Source: Ensembl

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: UniProtKB
    2. embryo development Source: UniProtKB
    3. epidermal growth factor receptor signaling pathway Source: Reactome
    4. Fc-epsilon receptor signaling pathway Source: Reactome
    5. fibroblast growth factor receptor signaling pathway Source: Reactome
    6. innate immune response Source: Reactome
    7. neurotrophin TRK receptor signaling pathway Source: Reactome
    8. phosphatidylinositol-mediated signaling Source: Reactome
    9. positive regulation of actin filament polymerization Source: Ensembl
    10. positive regulation of endothelial cell proliferation Source: Ensembl
    11. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
    12. positive regulation of protein kinase B signaling Source: Ensembl
    13. positive regulation of TOR signaling Source: UniProtKB
    14. regulation of actin cytoskeleton organization Source: UniProtKB
    15. regulation of protein kinase B signaling Source: UniProtKB
    16. regulation of Rac GTPase activity Source: Ensembl
    17. T cell costimulation Source: Reactome
    18. TOR signaling Source: InterPro

    Keywords - Molecular functioni

    Developmental protein

    Enzyme and pathway databases

    ReactomeiREACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_19358. CD28 dependent PI3K/Akt signaling.
    REACT_75829. PIP3 activates AKT signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rapamycin-insensitive companion of mTOR
    Alternative name(s):
    AVO3 homolog
    Short name:
    hAVO3
    Gene namesi
    Name:RICTORImported
    Synonyms:KIAA1999Imported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:28611. RICTOR.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. TORC2 complex Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA165660455.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17081708Rapamycin-insensitive companion of mTORPRO_0000308179Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei21 – 211Phosphoserine8 Publications
    Modified residuei1135 – 11351Phosphothreonine; by RPS6KB12 Publications
    Modified residuei1282 – 12821Phosphoserine2 Publications
    Modified residuei1284 – 12841Phosphoserine2 Publications
    Modified residuei1388 – 13881Phosphoserine3 Publications
    Modified residuei1396 – 13961Phosphoserine3 Publications
    Modified residuei1411 – 14111Phosphoserine2 Publications
    Modified residuei1591 – 15911Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated by MTOR; when part of mTORC2. Phosphorylated at Thr-1135 by RPS6KB1; phosphorylation of RICTOR inhibits mTORC2 and AKT1 signaling.9 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ6R327.
    PaxDbiQ6R327.
    PRIDEiQ6R327.

    PTM databases

    PhosphoSiteiQ6R327.

    Expressioni

    Gene expression databases

    ArrayExpressiQ6R327.
    BgeeiQ6R327.
    GenevestigatoriQ6R327.

    Organism-specific databases

    HPAiHPA037802.

    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

    WithEntry#Exp.IntActNotes
    ILKQ134188EBI-1387196,EBI-747644
    MTORP4234527EBI-1387196,EBI-359260
    PREX1Q8TCU63EBI-1387196,EBI-1046542

    Protein-protein interaction databases

    BioGridi128962. 47 interactions.
    DIPiDIP-39479N.
    IntActiQ6R327. 27 interactions.
    MINTiMINT-3976651.
    STRINGi9606.ENSP00000349959.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6R327.
    SMRiQ6R327. Positions 308-335, 399-428, 752-777, 890-975.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 789789Interaction with NBNAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1016 – 105843Ser-richSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the pianissimo family.Curated

    Phylogenomic databases

    eggNOGiNOG305760.
    HOGENOMiHOG000154126.
    HOVERGENiHBG060827.
    InParanoidiQ6R327.
    KOiK08267.
    OMAiRFHEMKK.
    OrthoDBiEOG7SBNMS.
    PhylomeDBiQ6R327.
    TreeFamiTF343656.

    Family and domain databases

    Gene3Di1.25.10.10. 4 hits.
    InterProiIPR011989. 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]
    PANTHERiPTHR13298. PTHR13298. 1 hit.
    PfamiPF14663. 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]
    SUPFAMiSSF48371. SSF48371. 5 hits.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q6R327-1) [UniParc]FASTAAdd 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

    MAAIGRGRSL KNLRVRGRND SGEENVPLDL TREPSDNLRE ILQNVARLQG     50
    VSNMRKLGHL NNFTKLLCDI GHSEEKLGFH YEDIIICLRL ALLNEAKEVR 100
    AAGLRALRYL IQDSSILQKV LKLKVDYLIA RCIDIQQSNE VERTQALRLV 150
    RKMITVNASL FPSSVTNSLI AVGNDGLQER DRMVRACIAI ICELALQNPE 200
    VVALRGGLNT ILKNVIDCQL SRINEALITT ILHLLNHPKT RQYVRADVEL 250
    ERILAPYTDF HYRHSPDTAE GQLKEDREAR FLASKMGIIA TFRSWAGIIN 300
    LCKPGNSGIQ SLIGVLCIPN MEIRRGLLEV LYDIFRLPLP VVTEEFIEAL 350
    LSVDPGRFQD SWRLSDGFVA AEAKTILPHR ARSRPDLMDN YLALILSAFI 400
    RNGLLEGLVE VITNSDDHIS VRATILLGEL LHMANTILPH SHSHHLHCLP 450
    TLMNMAASFD IPKEKRLRAS AALNCLKRFH EMKKRGPKPY SLHLDHIIQK 500
    AIATHQKRDQ YLRVQKDIFI LKDTEEALLI NLRDSQVLQH KENLEWNWNL 550
    IGTILKWPNV NLRNYKDEQL HRFVRRLLYF YKPSSKLYAN LDLDFAKAKQ 600
    LTVVGCQFTE FLLESEEDGQ GYLEDLVKDI VQWLNASSGM KPERSLQNNG 650
    LLTTLSQHYF LFIGTLSCHP HGVKMLEKCS VFQCLLNLCS LKNQDHLLKL 700
    TVSSLDYSRD GLARVILSKI LTAATDACRL YATKHLRVLL RANVEFFNNW 750
    GIELLVTQLH DKNKTISSEA LDILDEACED KANLHALIQM KPALSHLGDK 800
    GLLLLLRFLS IPKGFSYLNE RGYVAKQLEK WHREYNSKYV DLIEEQLNEA 850
    LTTYRKPVDG DNYVRRSNQR LQRPHVYLPI HLYGQLVHHK TGCHLLEVQN 900
    IITELCRNVR TPDLDKWEEI KKLKASLWAL GNIGSSNWGL NLLQEENVIP 950
    DILKLAKQCE VLSIRGTCVY VLGLIAKTKQ GCDILKCHNW DAVRHSRKHL 1000
    WPVVPDDVEQ LCNELSSIPS TLSLNSESTS SRHNSESESV PSSMFILEDD 1050
    RFGSSSTSTF FLDINEDTEP TFYDRSGPIK DKNSFPFFAS SKLVKNRILN 1100
    SLTLPNKKHR SSSDPKGGKL SSESKTSNRR IRTLTEPSVD FNHSDDFTPI 1150
    STVQKTLQLE TSFMGNKHIE DTGSTPSIGE NDLKFTKNFG TENHRENTSR 1200
    ERLVVESSTS SHMKIRSQSF NTDTTTSGIS SMSSSPSRET VGVDATTMDT 1250
    DCGSMSTVVS TKTIKTSHYL TPQSNHLSLS KSNSVSLVPP GSSHTLPRRA 1300
    QSLKAPSIAT IKSLADCNFS YTSSRDAFGY ATLKRLQQQR MHPSLSHSEA 1350
    LASPAKDVLF TDTITMKANS FESRLTPSRF MKALSYASLD KEDLLSPINQ 1400
    NTLQRSSSVR SMVSSATYGG SDDYIGLALP VDINDIFQVK DIPYFQTKNI 1450
    PPHDDRGARA FAHDAGGLPS GTGGLVKNSF HLLRQQMSLT EIMNSIHSDA 1500
    SLFLESTEDT GLQEHTDDNC LYCVCIEILG FQPSNQLSAI CSHSDFQDIP 1550
    YSDWCEQTIH NPLEVVPSKF SGISGCSDGV SQEGSASSTK STELLLGVKT 1600
    IPDDTPMCRI LLRKEVLRLV INLSSSVSTK CHETGLLTIK EKYPQTFDDI 1650
    CLYSEVSHLL SHCTFRLPCR RFIQELFQDV QFLQMHEEAE AVLATPPKQP 1700
    IVDTSAES 1708
    Length:1,708
    Mass (Da):192,218
    Last modified:July 5, 2004 - v1
    Checksum:iDB7B1E4A45DAE2AB
    GO
    Isoform 2 (identifier: Q6R327-4) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:257
    Mass (Da):28,988
    Checksum:i57DCA4610207FA94
    GO
    Isoform 3 (identifier: Q6R327-3) [UniParc]FASTAAdd to Basket

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

    Note: No experimental confirmation available.Curated

    Show »
    Length:1,732
    Mass (Da):195,011
    Checksum:i984F516A908EEC3A
    GO

    Sequence cautioni

    The sequence CAH18135.1 differs from that shown. Reason: Wrong choice of CDS.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti545 – 5451E → G in CAH18135. (PubMed:17974005)Curated
    Sequence conflicti815 – 8151F → L in CAH18135. (PubMed:17974005)Curated
    Sequence conflicti1283 – 12831N → S in CAH18135. (PubMed:17974005)Curated
    Sequence conflicti1699 – 16991Q → R in AAH51729. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti837 – 8371S → F.2 Publications
    Corresponds to variant rs2043112 [ dbSNP | Ensembl ].
    VAR_051320

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei252 – 2576RILAPY → NFSTLY in isoform 2. 1 PublicationVSP_038362
    Alternative sequencei258 – 17081451Missing in isoform 2. 1 PublicationVSP_038363Add
    BLAST
    Alternative sequencei1379 – 13791R → RIDFKKKHVGGIRSLRPTIT NNLFR in isoform 3. 2 PublicationsVSP_052581

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSiCCDS34148.1. [Q6R327-1]
    CCDS68861.1. [Q6R327-3]
    RefSeqiNP_001272368.1. NM_001285439.1. [Q6R327-3]
    NP_001272369.1. NM_001285440.1.
    NP_689969.2. NM_152756.4. [Q6R327-1]
    UniGeneiHs.407926.

    Genome annotation databases

    EnsembliENST00000296782; ENSP00000296782; ENSG00000164327. [Q6R327-3]
    ENST00000357387; ENSP00000349959; ENSG00000164327. [Q6R327-1]
    ENST00000511516; ENSP00000423019; ENSG00000164327. [Q6R327-4]
    GeneIDi253260.
    KEGGihsa:253260.
    UCSCiuc003jlo.2. human. [Q6R327-3]
    uc003jlp.2. human. [Q6R327-1]

    Polymorphism databases

    DMDMi74710068.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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, 399-428, 752-777, 890-975.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 128962. 47 interactions.
    DIPi DIP-39479N.
    IntActi Q6R327. 27 interactions.
    MINTi MINT-3976651.
    STRINGi 9606.ENSP00000349959.

    Chemistry

    ChEMBLi CHEMBL1795179.

    PTM databases

    PhosphoSitei Q6R327.

    Polymorphism databases

    DMDMi 74710068.

    Proteomic databases

    MaxQBi Q6R327.
    PaxDbi 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.2. human. [Q6R327-3 ]
    uc003jlp.2. human. [Q6R327-1 ]

    Organism-specific databases

    CTDi 253260.
    GeneCardsi GC05M038977.
    H-InvDB HIX0021738.
    HGNCi HGNC:28611. RICTOR.
    HPAi HPA037802.
    MIMi 609022. gene.
    neXtProti NX_Q6R327.
    PharmGKBi PA165660455.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG305760.
    HOGENOMi HOG000154126.
    HOVERGENi HBG060827.
    InParanoidi Q6R327.
    KOi K08267.
    OMAi RFHEMKK.
    OrthoDBi EOG7SBNMS.
    PhylomeDBi Q6R327.
    TreeFami TF343656.

    Enzyme and pathway databases

    Reactomei REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_19358. CD28 dependent PI3K/Akt signaling.
    REACT_75829. PIP3 activates AKT signaling.

    Miscellaneous databases

    GeneWikii RICTOR.
    GenomeRNAii 253260.
    NextBioi 92081.
    PROi Q6R327.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6R327.
    Bgeei Q6R327.
    Genevestigatori Q6R327.

    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. 1 hit.
    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 ]
    SUPFAMi SSF48371. SSF48371. 5 hits.
    ProtoNeti Search...

    Publicationsi

    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. 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. 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 LymphImported.
    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: BrainImported.
    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. 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. 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. 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.

    Entry informationi

    Entry nameiRICTR_HUMAN
    AccessioniPrimary (citable) accession number: Q6R327
    Secondary accession number(s): B2RNX0
    , B7ZMF7, Q68DT5, Q86UB7, Q8N3A0, Q8NCM6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 23, 2007
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3