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)

Q8N122

- RPTOR_HUMAN

UniProt

Q8N122 - RPTOR_HUMAN

Protein

Regulatory-associated protein of mTOR

Gene

RPTOR

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 124 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in the control of the mammalian target of rapamycin complex 1 (mTORC1) activity which regulates cell growth and survival, and autophagy in response to nutrient and hormonal signals; functions as a scaffold for recruiting mTORC1 substrates. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Involved in ciliogenesis.3 Publications

    GO - Molecular functioni

    1. 14-3-3 protein binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein complex binding Source: UniProtKB
    4. protein kinase binding Source: UniProtKB
    5. RNA polymerase III type 1 promoter DNA binding Source: UniProtKB
    6. RNA polymerase III type 2 promoter DNA binding Source: UniProtKB
    7. RNA polymerase III type 3 promoter DNA binding Source: UniProtKB
    8. TFIIIC-class transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. cell cycle arrest Source: Reactome
    2. cell growth Source: UniProtKB
    3. cellular response to amino acid stimulus Source: UniProtKB
    4. cellular response to nutrient levels Source: UniProtKB
    5. insulin receptor signaling pathway Source: Reactome
    6. positive regulation of endothelial cell proliferation Source: Ensembl
    7. positive regulation of protein serine/threonine kinase activity Source: UniProtKB
    8. positive regulation of TOR signaling Source: UniProtKB
    9. positive regulation of transcription from RNA polymerase III promoter Source: UniProtKB
    10. regulation of cell size Source: UniProtKB
    11. TOR signaling Source: UniProtKB

    Enzyme and pathway databases

    ReactomeiREACT_200775. HSF1-dependent transactivation.
    REACT_21285. Regulation of AMPK activity via LKB1.
    REACT_6754. S6K1-mediated signalling.
    REACT_6836. Release of eIF4E.
    REACT_6838. mTOR signalling.
    SignaLinkiQ8N122.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Regulatory-associated protein of mTOR
    Short name:
    Raptor
    Alternative name(s):
    p150 target of rapamycin (TOR)-scaffold protein
    Gene namesi
    Name:RPTOR
    Synonyms:KIAA1303, RAPTOR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:30287. RPTOR.

    Subcellular locationi

    Cytoplasm. Lysosome. Cytoplasmic granule
    Note: Targeting to lysosomes depends on amino acid availability. In arsenite-stressed cells, accumulates in stress granules when associated with SPAG5 and association with lysosomes is drastically decreased.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. lysosomal membrane Source: UniProtKB
    4. lysosome Source: UniProtKB
    5. TORC1 complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Lysosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi722 – 7221S → A: Abolishes AMPK-mediated phosphorylation; when associated with A-792. 1 Publication
    Mutagenesisi792 – 7921S → A: Abolishes AMPK-mediated phosphorylation; when associated with A-722. 1 Publication

    Organism-specific databases

    PharmGKBiPA165432629.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13351335Regulatory-associated protein of mTORPRO_0000051200Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei696 – 6961Phosphoserine; by MAPK82 Publications
    Modified residuei706 – 7061Phosphothreonine; by MAPK82 Publications
    Modified residuei719 – 7191Phosphoserine; by RPS6KA12 Publications
    Modified residuei721 – 7211Phosphoserine; by RPS6KA11 Publication
    Modified residuei722 – 7221Phosphoserine; by AMPK and RPS6KA12 Publications
    Modified residuei792 – 7921Phosphoserine; by AMPK1 Publication
    Modified residuei855 – 8551Phosphoserine1 Publication
    Modified residuei859 – 8591Phosphoserine; by MTOR4 Publications
    Modified residuei863 – 8631Phosphoserine; by MAPK8 and MTOR7 Publications
    Modified residuei877 – 8771Phosphoserine7 Publications

    Post-translational modificationi

    Insulin-stimulated phosphorylation at Ser-863 by MTOR and MAPK8 up-regulates mTORC1 activity. Osmotic stress also induces phosphorylation at Ser-696, Thr-706 and Ser-863 by MAPK8. Ser-863 phosphorylation is required for phosphorylation at Ser-855 and Ser-859. In response to nutrient limitation, phosphorylated by AMPK; phosphorylation promotes interaction with 14-3-3 proteins, leading to negative regulation of the mTORC1 complex. In response to growth factors, phosphorylated at Ser-719, Ser-721 and Ser-722 by RPS6KA1, which stimulates mTORC1 activity.11 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8N122.
    PaxDbiQ8N122.
    PRIDEiQ8N122.

    PTM databases

    PhosphoSiteiQ8N122.

    Expressioni

    Tissue specificityi

    Highly expressed in skeletal muscle, and in a lesser extent in brain, lung, small intestine, kidney and placenta. Isoform 3 is widely expressed, with highest levels in nasal mucosa and pituitary and lowest in spleen.2 Publications

    Gene expression databases

    ArrayExpressiQ8N122.
    BgeeiQ8N122.
    GenevestigatoriQ8N122.

    Organism-specific databases

    HPAiCAB013514.
    HPA029821.

    Interactioni

    Subunit structurei

    Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR. mTORC1 binds to and is inhibited by FKBP12-rapamycin. Binds directly to 4EBP1 and RPS6KB1 independently of its association with MTOR. Binds preferentially to poorly or non-phosphorylated forms of EIF4EBP1, and this binding is critical to the ability of MTOR to catalyze phosphorylation. Forms a complex with MTOR under both leucine-rich and -poor conditions. Interacts with ULK1 in a nutrient-dependent manner; the interaction is reduced during starvation. Interacts (when phosphorylated by AMPK) with 14-3-3 protein, leading to inhibit its activity. Interacts with SPAG5; SPAG5 competes with MTOR for RPTOR-binding, resulting in decreased mTORC1 formation. Interacts with G3BP1. The complex formed with G3BP1 AND SPAG5 is increased by oxidative stress.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EIF4EBP1Q135415EBI-1567928,EBI-74090
    G3BP1Q132834EBI-1567928,EBI-1047359
    LARSQ9P2J53EBI-1567928,EBI-356077
    MLST8Q9BVC43EBI-1567928,EBI-1387471
    MTORP4234530EBI-1567928,EBI-359260
    MtorQ9JLN95EBI-1567928,EBI-1571628From a different organism.
    PREX1Q8TCU62EBI-1567928,EBI-1046542
    Rps6kb1P679992EBI-1567928,EBI-2639458From a different organism.
    SIRT1Q96EB63EBI-1567928,EBI-1802965
    SPAG5Q96R069EBI-1567928,EBI-413317

    Protein-protein interaction databases

    BioGridi121582. 58 interactions.
    DIPiDIP-39482N.
    IntActiQ8N122. 26 interactions.
    MINTiMINT-3038940.
    STRINGi9606.ENSP00000307272.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8N122.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati1020 – 106142WD 1Add
    BLAST
    Repeati1065 – 110642WD 2Add
    BLAST
    Repeati1121 – 116040WD 3Add
    BLAST
    Repeati1164 – 120340WD 4Add
    BLAST
    Repeati1209 – 124941WD 5Add
    BLAST
    Repeati1251 – 129141WD 6Add
    BLAST
    Repeati1299 – 133537WD 7Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi881 – 8877Poly-Ser

    Sequence similaritiesi

    Belongs to the WD repeat RAPTOR family.Curated
    Contains 7 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiNOG269318.
    HOGENOMiHOG000184479.
    HOVERGENiHBG059496.
    InParanoidiQ8N122.
    KOiK07204.
    OMAiFCDWSAK.
    PhylomeDBiQ8N122.
    TreeFamiTF105729.

    Family and domain databases

    Gene3Di1.25.10.10. 2 hits.
    2.130.10.10. 1 hit.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR000357. HEAT.
    IPR004083. Raptor.
    IPR029347. Raptor_N.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PANTHERiPTHR12848. PTHR12848. 1 hit.
    PfamiPF02985. HEAT. 1 hit.
    PF14538. Raptor_N. 1 hit.
    PF00400. WD40. 2 hits.
    [Graphical view]
    SMARTiSM00320. WD40. 7 hits.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 2 hits.
    SSF50978. SSF50978. 1 hit.
    PROSITEiPS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8N122-1) [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

    MESEMLQSPL LGLGEEDEAD LTDWNLPLAF MKKRHCEKIE GSKSLAQSWR     50
    MKDRMKTVSV ALVLCLNVGV DPPDVVKTTP CARLECWIDP LSMGPQKALE 100
    TIGANLQKQY ENWQPRARYK QSLDPTVDEV KKLCTSLRRN AKEERVLFHY 150
    NGHGVPRPTV NGEVWVFNKN YTQYIPLSIY DLQTWMGSPS IFVYDCSNAG 200
    LIVKSFKQFA LQREQELEVA AINPNHPLAQ MPLPPSMKNC IQLAACEATE 250
    LLPMIPDLPA DLFTSCLTTP IKIALRWFCM QKCVSLVPGV TLDLIEKIPG 300
    RLNDRRTPLG ELNWIFTAIT DTIAWNVLPR DLFQKLFRQD LLVASLFRNF 350
    LLAERIMRSY NCTPVSSPRL PPTYMHAMWQ AWDLAVDICL SQLPTIIEEG 400
    TAFRHSPFFA EQLTAFQVWL TMGVENRNPP EQLPIVLQVL LSQVHRLRAL 450
    DLLGRFLDLG PWAVSLALSV GIFPYVLKLL QSSARELRPL LVFIWAKILA 500
    VDSSCQADLV KDNGHKYFLS VLADPYMPAE HRTMTAFILA VIVNSYHTGQ 550
    EACLQGNLIA ICLEQLNDPH PLLRQWVAIC LGRIWQNFDS ARWCGVRDSA 600
    HEKLYSLLSD PIPEVRCAAV FALGTFVGNS AERTDHSTTI DHNVAMMLAQ 650
    LVSDGSPMVR KELVVALSHL VVQYESNFCT VALQFIEEEK NYALPSPATT 700
    EGGSLTPVRD SPCTPRLRSV SSYGNIRAVA TARSLNKSLQ NLSLTEESGG 750
    AVAFSPGNLS TSSSASSTLG SPENEEHILS FETIDKMRRA SSYSSLNSLI 800
    GVSFNSVYTQ IWRVLLHLAA DPYPEVSDVA MKVLNSIAYK ATVNARPQRV 850
    LDTSSLTQSA PASPTNKGVH IHQAGGSPPA SSTSSSSLTN DVAKQPVSRD 900
    LPSGRPGTTG PAGAQYTPHS HQFPRTRKMF DKGPEQTADD ADDAAGHKSF 950
    ISATVQTGFC DWSARYFAQP VMKIPEEHDL ESQIRKEREW RFLRNSRVRR 1000
    QAQQVIQKGI TRLDDQIFLN RNPGVPSVVK FHPFTPCIAV ADKDSICFWD 1050
    WEKGEKLDYF HNGNPRYTRV TAMEYLNGQD CSLLLTATDD GAIRVWKNFA 1100
    DLEKNPEMVT AWQGLSDMLP TTRGAGMVVD WEQETGLLMS SGDVRIVRIW 1150
    DTDREMKVQD IPTGADSCVT SLSCDSHRSL IVAGLGDGSI RVYDRRMALS 1200
    ECRVMTYREH TAWVVKASLQ KRPDGHIVSV SVNGDVRIFD PRMPESVNVL 1250
    QIVKGLTALD IHPQADLIAC GSVNQFTAIY NSSGELINNI KYYDGFMGQR 1300
    VGAISCLAFH PHWPHLAVGS NDYYISVYSV EKRVR 1335
    Length:1,335
    Mass (Da):149,038
    Last modified:October 1, 2002 - v1
    Checksum:i688ED1943F45045A
    GO
    Isoform 2 (identifier: Q8N122-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         380-1335: Missing.

    Show »
    Length:379
    Mass (Da):43,256
    Checksum:iD67B01D4E68E859E
    GO
    Isoform 3 (identifier: Q8N122-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         504-661: Missing.

    Show »
    Length:1,177
    Mass (Da):131,515
    Checksum:i1CE0DA04E72105B2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti217 – 2182LE → RQ in BAA92541. (PubMed:10718198)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei380 – 1335956Missing in isoform 2. 1 PublicationVSP_010174Add
    BLAST
    Alternative sequencei504 – 661158Missing in isoform 3. 1 PublicationVSP_054042Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY090663 mRNA. Translation: AAM09075.1.
    AB082951 mRNA. Translation: BAC06490.1.
    AC016245 Genomic DNA. No translation available.
    AC109327 Genomic DNA. No translation available.
    AC127496 Genomic DNA. No translation available.
    AC133012 Genomic DNA. No translation available.
    CH471099 Genomic DNA. Translation: EAW89618.1.
    BC025180 mRNA. Translation: AAH25180.1.
    BC033258 mRNA. Translation: AAH33258.1.
    BC064515 mRNA. Translation: AAH64515.1.
    BC136652 mRNA. Translation: AAI36653.1.
    BC136654 mRNA. Translation: AAI36655.1.
    AB037724 mRNA. Translation: BAA92541.1.
    GQ183898 mRNA. Translation: ACS44766.1.
    CCDSiCCDS11773.1. [Q8N122-1]
    CCDS54175.1. [Q8N122-3]
    RefSeqiNP_001156506.1. NM_001163034.1. [Q8N122-3]
    NP_065812.1. NM_020761.2. [Q8N122-1]
    UniGeneiHs.133044.

    Genome annotation databases

    EnsembliENST00000306801; ENSP00000307272; ENSG00000141564. [Q8N122-1]
    ENST00000544334; ENSP00000442479; ENSG00000141564. [Q8N122-3]
    ENST00000570891; ENSP00000460136; ENSG00000141564. [Q8N122-2]
    GeneIDi57521.
    KEGGihsa:57521.
    UCSCiuc002jys.3. human. [Q8N122-2]
    uc002jyt.1. human. [Q8N122-1]

    Polymorphism databases

    DMDMi46577501.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY090663 mRNA. Translation: AAM09075.1 .
    AB082951 mRNA. Translation: BAC06490.1 .
    AC016245 Genomic DNA. No translation available.
    AC109327 Genomic DNA. No translation available.
    AC127496 Genomic DNA. No translation available.
    AC133012 Genomic DNA. No translation available.
    CH471099 Genomic DNA. Translation: EAW89618.1 .
    BC025180 mRNA. Translation: AAH25180.1 .
    BC033258 mRNA. Translation: AAH33258.1 .
    BC064515 mRNA. Translation: AAH64515.1 .
    BC136652 mRNA. Translation: AAI36653.1 .
    BC136654 mRNA. Translation: AAI36655.1 .
    AB037724 mRNA. Translation: BAA92541.1 .
    GQ183898 mRNA. Translation: ACS44766.1 .
    CCDSi CCDS11773.1. [Q8N122-1 ]
    CCDS54175.1. [Q8N122-3 ]
    RefSeqi NP_001156506.1. NM_001163034.1. [Q8N122-3 ]
    NP_065812.1. NM_020761.2. [Q8N122-1 ]
    UniGenei Hs.133044.

    3D structure databases

    ProteinModelPortali Q8N122.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121582. 58 interactions.
    DIPi DIP-39482N.
    IntActi Q8N122. 26 interactions.
    MINTi MINT-3038940.
    STRINGi 9606.ENSP00000307272.

    PTM databases

    PhosphoSitei Q8N122.

    Polymorphism databases

    DMDMi 46577501.

    Proteomic databases

    MaxQBi Q8N122.
    PaxDbi Q8N122.
    PRIDEi Q8N122.

    Protocols and materials databases

    DNASUi 57521.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000306801 ; ENSP00000307272 ; ENSG00000141564 . [Q8N122-1 ]
    ENST00000544334 ; ENSP00000442479 ; ENSG00000141564 . [Q8N122-3 ]
    ENST00000570891 ; ENSP00000460136 ; ENSG00000141564 . [Q8N122-2 ]
    GeneIDi 57521.
    KEGGi hsa:57521.
    UCSCi uc002jys.3. human. [Q8N122-2 ]
    uc002jyt.1. human. [Q8N122-1 ]

    Organism-specific databases

    CTDi 57521.
    GeneCardsi GC17P078518.
    HGNCi HGNC:30287. RPTOR.
    HPAi CAB013514.
    HPA029821.
    MIMi 607130. gene.
    neXtProti NX_Q8N122.
    PharmGKBi PA165432629.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG269318.
    HOGENOMi HOG000184479.
    HOVERGENi HBG059496.
    InParanoidi Q8N122.
    KOi K07204.
    OMAi FCDWSAK.
    PhylomeDBi Q8N122.
    TreeFami TF105729.

    Enzyme and pathway databases

    Reactomei REACT_200775. HSF1-dependent transactivation.
    REACT_21285. Regulation of AMPK activity via LKB1.
    REACT_6754. S6K1-mediated signalling.
    REACT_6836. Release of eIF4E.
    REACT_6838. mTOR signalling.
    SignaLinki Q8N122.

    Miscellaneous databases

    GeneWikii RPTOR.
    GenomeRNAii 57521.
    NextBioi 35483332.
    PROi Q8N122.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8N122.
    Bgeei Q8N122.
    Genevestigatori Q8N122.

    Family and domain databases

    Gene3Di 1.25.10.10. 2 hits.
    2.130.10.10. 1 hit.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR000357. HEAT.
    IPR004083. Raptor.
    IPR029347. Raptor_N.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    PANTHERi PTHR12848. PTHR12848. 1 hit.
    Pfami PF02985. HEAT. 1 hit.
    PF14538. Raptor_N. 1 hit.
    PF00400. WD40. 2 hits.
    [Graphical view ]
    SMARTi SM00320. WD40. 7 hits.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 2 hits.
    SSF50978. SSF50978. 1 hit.
    PROSITEi PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the growth machinery."
      Kim D.-H., Sarbassov D.D., Ali S.M., King J.E., Latek R.R., Erdjument-Bromage H., Tempst P., Sabatini D.M.
      Cell 110:163-175(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH 4EBP1 AND RPS6KB1.
    2. "Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action."
      Hara K., Maruki Y., Long X., Yoshino K., Oshiro N., Hidayat S., Tokunaga C., Avruch J., Yonezawa K.
      Cell 110:177-189(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH 4EBP1 AND RPS6KB1.
    3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 995-1135 (ISOFORM 1).
      Tissue: Brain, Placenta and Testis.
    6. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 217-1335.
      Tissue: Brain.
    7. "Characterization of a novel splicing variant in the RAPTOR gene."
      Sun C., Southard C., Di Rienzo A.
      Mutat. Res. 662:88-92(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 488-594 (ISOFORM 3), TISSUE SPECIFICITY (ISOFORM 3).
    8. "Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control."
      Loewith R., Jacinto E., Wullschleger S., Lorberg A., Crespo J.L., Bonenfant D., Oppliger W., Jenoe P., Hall M.N.
      Mol. Cell 10:457-468(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MTOR AND MLST8, IDENTIFICATION IN THE TORC1 COMPLEX, TISSUE SPECIFICITY.
    9. "TOS motif-mediated raptor binding regulates 4E-BP1 multisite phosphorylation and function."
      Schalm S.S., Fingar D.C., Sabatini D.M., Blenis J.
      Curr. Biol. 13:797-806(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF4EBP1.
    10. "Dissociation of raptor from mTOR is a mechanism of rapamycin-induced inhibition of mTOR function."
      Oshiro N., Yoshino K., Hidayat S., Tokunaga C., Hara K., Eguchi S., Avruch J., Yonezawa K.
      Genes Cells 9:359-366(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISSOCIATION OF COMPLEX BY RAPAMYCIN.
    11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase."
      Sancak Y., Thoreen C.C., Peterson T.R., Lindquist R.A., Kang S.A., Spooner E., Carr S.A., Sabatini D.M.
      Mol. Cell 25:903-915(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AKT1S1.
    14. "Oncogenic MAPK signaling stimulates mTORC1 activity by promoting RSK-mediated raptor phosphorylation."
      Carriere A., Cargnello M., Julien L.A., Gao H., Bonneil E., Thibault P., Roux P.P.
      Curr. Biol. 18:1269-1277(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-719; SER-721 AND SER-722.
    15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: PHOSPHORYLATION AT SER-722 AND SER-792, MUTAGENESIS OF SER-722 AND SER-792, INTERACTION WITH 14-3-3.
    17. "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-877, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-719; SER-859; SER-863 AND SER-877, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "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].
    20. "Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy."
      Hosokawa N., Hara T., Kaizuka T., Kishi C., Takamura A., Miura Y., Iemura S., Natsume T., Takehana K., Yamada N., Guan J.L., Oshiro N., Mizushima N.
      Mol. Biol. Cell 20:1981-1991(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ULK1.
    21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-877, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "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-859; SER-863 AND SER-877, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    23. "Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids."
      Sancak Y., Bar-Peled L., Zoncu R., Markhard A.L., Nada S., Sabatini D.M.
      Cell 141:290-303(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    24. "Regulation of mTOR complex 1 (mTORC1) by raptor Ser863 and multisite phosphorylation."
      Foster K.G., Acosta-Jaquez H.A., Romeo Y., Ekim B., Soliman G.A., Carriere A., Roux P.P., Ballif B.A., Fingar D.C.
      J. Biol. Chem. 285:80-94(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-696; THR-706; SER-855; SER-859; SER-863 AND SER-877.
    25. "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-859; SER-863 AND SER-877, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "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-863 AND SER-877, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Osmotic stress regulates mammalian target of rapamycin (mTOR) complex 1 via c-Jun N-terminal Kinase (JNK)-mediated Raptor protein phosphorylation."
      Kwak D., Choi S., Jeong H., Jang J.H., Lee Y., Jeon H., Lee M.N., Noh J., Cho K., Yoo J.S., Hwang D., Suh P.G., Ryu S.H.
      J. Biol. Chem. 287:18398-18407(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-696; THR-706 AND SER-863.
    29. Cited for: INTERACTION WITH G3BP1 AND SPAG5, SUBCELLULAR LOCATION.
    30. "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: FUNCTION IN CILIOGENESIS.

    Entry informationi

    Entry nameiRPTOR_HUMAN
    AccessioniPrimary (citable) accession number: Q8N122
    Secondary accession number(s): B2RN36
    , C6KEF2, F5H7J5, Q8N4V9, Q8TB32, Q9P2P3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 124 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 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3