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Q15382

- RHEB_HUMAN

UniProt

Q15382 - RHEB_HUMAN

Protein

GTP-binding protein Rheb

Gene

RHEB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Stimulates the phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1 signaling. Activates the protein kinase activity of mTORC1. Has low intrinsic GTPase activity.6 Publications

    Enzyme regulationi

    Alternates between an inactive form bound to GDP and an active form bound to GTP. Inactivated by TSC1-TSC2 via the GTPase activating protein (GAP) domain of TSC2.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi20 – 201Magnesium
    Metal bindingi38 – 381Magnesium

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi16 – 216GTP1 Publication
    Nucleotide bindingi32 – 387GTP1 Publication
    Nucleotide bindingi119 – 1224GTP1 Publication
    Nucleotide bindingi149 – 1502GTP1 Publication

    GO - Molecular functioni

    1. GDP binding Source: Ensembl
    2. GTPase activity Source: ProtInc
    3. GTP binding Source: UniProtKB
    4. metal ion binding Source: UniProtKB-KW
    5. protein binding Source: IntAct

    GO - Biological processi

    1. cell cycle arrest Source: Reactome
    2. insulin receptor signaling pathway Source: Reactome
    3. positive regulation of TOR signaling Source: UniProtKB
    4. signal transduction Source: ProtInc
    5. small GTPase mediated signal transduction Source: InterPro

    Keywords - Ligandi

    GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_21393. Regulation of Rheb GTPase activity by AMPK.
    REACT_6754. S6K1-mediated signalling.
    REACT_6836. Release of eIF4E.
    REACT_6838. mTOR signalling.
    SignaLinkiQ15382.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GTP-binding protein Rheb
    Alternative name(s):
    Ras homolog enriched in brain
    Gene namesi
    Name:RHEB
    Synonyms:RHEB2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:10011. RHEB.

    Subcellular locationi

    Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. dendrite Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: ProtInc
    5. neuronal cell body Source: Ensembl
    6. plasma membrane Source: UniProtKB-SubCell
    7. spliceosomal complex Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi15 – 151R → G: Partially resistant to inactivation by TSC1-TSC2. 1 Publication
    Mutagenesisi20 – 201S → N: Deficient in guanine nucleotide binding. Unable to rescue S6K1 from inactivation by amino-acid withdrawal. 2 Publications
    Mutagenesisi38 – 381T → M: Slightly impairs signaling through mTORC1, but still binds guanine nucleotides normally. 2 Publications
    Mutagenesisi39 – 391I → K: Impairs S6K1 activation, but still binds guanine nucleotides normally. 1 Publication
    Mutagenesisi40 – 401E → G: No effect. 1 Publication
    Mutagenesisi41 – 411N → A: Impairs interaction with MTOR. Impairs signaling through mTORC1, but still binds guanine nucleotides normally. 2 Publications
    Mutagenesisi43 – 431F → C: No effect. 1 Publication
    Mutagenesisi46 – 461L → A: Causes slight reduction in S6K1 activation. 1 Publication
    Mutagenesisi48 – 481T → A: Causes slightly reduced phosphorylation of EIF4EBP1. 1 Publication
    Mutagenesisi49 – 491V → A: Causes slightly reduced phosphorylation of EIF4EBP1. 1 Publication
    Mutagenesisi53 – 531E → A: Causes slightly reduced phosphorylation of EIF4EBP1. 1 Publication
    Mutagenesisi54 – 541Y → A: Partially deficient in guanine nucleotide binding. Fully impairs EIF4EBP1 phosphorylation and S6K1 activation. 1 Publication
    Mutagenesisi56 – 561L → A: Partially deficient in guanine nucleotide binding. Fully impairs EIF4EBP1 phosphorylation and S6K1 activation. 1 Publication
    Mutagenesisi60 – 601D → I: Deficient in guanine nucleotide binding. Unable to rescue S6K1 from inactivation by amino-acid withdrawal. 1 Publication
    Mutagenesisi64 – 641Q → L: Has a higher basal GTPase level, however, is still sensitive to TSC2 GAP activity. 1 Publication
    Mutagenesisi181 – 1811C → S: Reduces the ability to rescue S6K1 from inactivation by amino-acid withdrawal. 1 Publication

    Organism-specific databases

    PharmGKBiPA34389.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 181181GTP-binding protein RhebPRO_0000082708Add
    BLAST
    Propeptidei182 – 1843Removed in mature formPRO_0000281365

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei130 – 1301Phosphoserine; by MAPKAPK5By similarity
    Modified residuei181 – 1811Cysteine methyl esterCurated
    Lipidationi181 – 1811S-farnesyl cysteine1 Publication

    Post-translational modificationi

    Farnesylation is important for efficiently activating mTORC1-mediated signaling.
    Phosphorylation by MAPKAPK5 impairs GTP-binding and inactivation.By similarity

    Keywords - PTMi

    Lipoprotein, Methylation, Phosphoprotein, Prenylation

    Proteomic databases

    MaxQBiQ15382.
    PaxDbiQ15382.
    PRIDEiQ15382.

    PTM databases

    PhosphoSiteiQ15382.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highest levels observed in skeletal and cardiac muscle.

    Gene expression databases

    ArrayExpressiQ15382.
    BgeeiQ15382.
    CleanExiHS_RHEB.
    GenevestigatoriQ15382.

    Organism-specific databases

    HPAiCAB019436.
    HPA054743.

    Interactioni

    Subunit structurei

    Binds to mTORC1 in a guanyl nucleotide-independent manner. Interacts directly with MTOR, MLST8 and RPTOR. Interacts with TSC2.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PDE6DO439245EBI-6860739,EBI-712685

    Protein-protein interaction databases

    BioGridi111941. 27 interactions.
    DIPiDIP-42816N.
    IntActiQ15382. 12 interactions.
    MINTiMINT-1365334.
    STRINGi9606.ENSP00000262187.

    Structurei

    Secondary structure

    1
    184
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 1411
    Helixi19 – 2810
    Beta strandi41 – 499
    Beta strandi52 – 609
    Beta strandi66 – 683
    Helixi72 – 743
    Turni75 – 773
    Beta strandi79 – 868
    Helixi90 – 10617
    Beta strandi114 – 1196
    Turni124 – 1263
    Helixi131 – 14010
    Beta strandi144 – 1474
    Helixi153 – 16816

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XTQX-ray2.00A1-169[»]
    1XTRX-ray2.65A1-169[»]
    1XTSX-ray2.80A1-169[»]
    3SEAX-ray2.00A/B3-169[»]
    3T5GX-ray1.70A1-181[»]
    DisProtiDP00364.
    ProteinModelPortaliQ15382.
    SMRiQ15382. Positions 3-169.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15382.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi35 – 439Effector region

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rheb family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    HOGENOMiHOG000233973.
    HOVERGENiHBG009351.
    InParanoidiQ15382.
    KOiK07208.
    OMAiTILNSKH.
    OrthoDBiEOG7Q2N6K.
    PhylomeDBiQ15382.
    TreeFamiTF314986.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR020849. Small_GTPase_Ras.
    [Graphical view]
    PANTHERiPTHR24070. PTHR24070. 1 hit.
    PfamiPF00071. Ras. 1 hit.
    [Graphical view]
    PRINTSiPR00449. RASTRNSFRMNG.
    SMARTiSM00173. RAS. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS51421. RAS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q15382-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPQSKSRKIA ILGYRSVGKS SLTIQFVEGQ FVDSYDPTIE NTFTKLITVN    50
    GQEYHLQLVD TAGQDEYSIF PQTYSIDING YILVYSVTSI KSFEVIKVIH 100
    GKLLDMVGKV QIPIMLVGNK KDLHMERVIS YEEGKALAES WNAAFLESSA 150
    KENQTAVDVF RRIILEAEKM DGAASQGKSS CSVM 184
    Length:184
    Mass (Da):20,497
    Last modified:November 1, 1996 - v1
    Checksum:i8F4C8080BDF928FD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti118 – 1181G → W in BAA11211. (PubMed:8661031)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti139 – 1391E → K in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036310

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z29677 mRNA. Translation: CAA82774.1.
    D78132 mRNA. Translation: BAA11211.1.
    AF148645 mRNA. Translation: AAF73125.1.
    AF493921 mRNA. Translation: AAM12635.1.
    AK125446 mRNA. Translation: BAG54198.1.
    BT006958 mRNA. Translation: AAP35604.1.
    AC005996 Genomic DNA. Translation: AAD15548.1.
    CH471173 Genomic DNA. Translation: EAW53989.1.
    BC016155 mRNA. Translation: AAH16155.1.
    BC107705 mRNA. Translation: AAI07706.1.
    CCDSiCCDS5927.1.
    PIRiS68419. S41960.
    RefSeqiNP_005605.1. NM_005614.3.
    UniGeneiHs.283521.
    Hs.568850.
    Hs.647068.

    Genome annotation databases

    EnsembliENST00000262187; ENSP00000262187; ENSG00000106615.
    GeneIDi6009.
    KEGGihsa:6009.
    UCSCiuc003wkh.1. human.

    Polymorphism databases

    DMDMi6919957.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z29677 mRNA. Translation: CAA82774.1 .
    D78132 mRNA. Translation: BAA11211.1 .
    AF148645 mRNA. Translation: AAF73125.1 .
    AF493921 mRNA. Translation: AAM12635.1 .
    AK125446 mRNA. Translation: BAG54198.1 .
    BT006958 mRNA. Translation: AAP35604.1 .
    AC005996 Genomic DNA. Translation: AAD15548.1 .
    CH471173 Genomic DNA. Translation: EAW53989.1 .
    BC016155 mRNA. Translation: AAH16155.1 .
    BC107705 mRNA. Translation: AAI07706.1 .
    CCDSi CCDS5927.1.
    PIRi S68419. S41960.
    RefSeqi NP_005605.1. NM_005614.3.
    UniGenei Hs.283521.
    Hs.568850.
    Hs.647068.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XTQ X-ray 2.00 A 1-169 [» ]
    1XTR X-ray 2.65 A 1-169 [» ]
    1XTS X-ray 2.80 A 1-169 [» ]
    3SEA X-ray 2.00 A/B 3-169 [» ]
    3T5G X-ray 1.70 A 1-181 [» ]
    DisProti DP00364.
    ProteinModelPortali Q15382.
    SMRi Q15382. Positions 3-169.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111941. 27 interactions.
    DIPi DIP-42816N.
    IntActi Q15382. 12 interactions.
    MINTi MINT-1365334.
    STRINGi 9606.ENSP00000262187.

    PTM databases

    PhosphoSitei Q15382.

    Polymorphism databases

    DMDMi 6919957.

    Proteomic databases

    MaxQBi Q15382.
    PaxDbi Q15382.
    PRIDEi Q15382.

    Protocols and materials databases

    DNASUi 6009.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262187 ; ENSP00000262187 ; ENSG00000106615 .
    GeneIDi 6009.
    KEGGi hsa:6009.
    UCSCi uc003wkh.1. human.

    Organism-specific databases

    CTDi 6009.
    GeneCardsi GC07M151163.
    HGNCi HGNC:10011. RHEB.
    HPAi CAB019436.
    HPA054743.
    MIMi 601293. gene.
    neXtProti NX_Q15382.
    PharmGKBi PA34389.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233973.
    HOVERGENi HBG009351.
    InParanoidi Q15382.
    KOi K07208.
    OMAi TILNSKH.
    OrthoDBi EOG7Q2N6K.
    PhylomeDBi Q15382.
    TreeFami TF314986.

    Enzyme and pathway databases

    Reactomei REACT_21393. Regulation of Rheb GTPase activity by AMPK.
    REACT_6754. S6K1-mediated signalling.
    REACT_6836. Release of eIF4E.
    REACT_6838. mTOR signalling.
    SignaLinki Q15382.

    Miscellaneous databases

    ChiTaRSi RHEB. human.
    EvolutionaryTracei Q15382.
    GeneWikii RHEB.
    GenomeRNAii 6009.
    NextBioi 23445.
    PROi Q15382.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15382.
    Bgeei Q15382.
    CleanExi HS_RHEB.
    Genevestigatori Q15382.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR020849. Small_GTPase_Ras.
    [Graphical view ]
    PANTHERi PTHR24070. PTHR24070. 1 hit.
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00173. RAS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51421. RAS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel approach for expression cloning of small GTPases: identification, tissue distribution and chromosome mapping of the human homolog of rheb."
      Gromov P.S., Madsen P., Tomerup N., Celis J.E.
      FEBS Lett. 377:221-226(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Psoriatic skin.
    2. "Isolation of cDNA and genomic clones of a human Ras-related GTP-binding protein gene and its chromosomal localization to the long arm of chromosome 7, 7q36."
      Mizuki N., Kimura M., Ohno S., Miyata S., Sato M., Ando H., Ishihara M., Goto K., Watanabe S., Yamazaki M., Ono A., Taguchi S., Okumura K., Nogami M., Taguchi H., Ando A., Inoko H.
      Genomics 34:114-118(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Skin.
    3. "Detection of membrane-associated proteins using serum of mice immunized with membrane fractions of breast carcinoma cells."
      Weidenmueller U., Tur M.K., Tawadros S., Engert A., Barth S.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Mammary carcinoma.
    4. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
      Puhl H.L. III, Ikeda S.R., Aronstam R.S.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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].
      Tissue: Muscle and Testis.
    10. "Tuberous sclerosis complex-1 and -2 gene products function together to inhibit mammalian target of rapamycin (mTOR)-mediated downstream signaling."
      Tee A.R., Fingar D.C., Manning B.D., Kwiatkowski D.J., Cantley L.C., Blenis J.
      Proc. Natl. Acad. Sci. U.S.A. 99:13571-13576(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling."
      Inoki K., Li Y., Xu T., Guan K.-L.
      Genes Dev. 17:1829-1834(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Biochemical and functional characterizations of small GTPase Rheb and TSC2 GAP activity."
      Li Y., Inoki K., Guan K.-L.
      Mol. Cell. Biol. 24:7965-7975(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ARG-15; SER-20; ASP-60; GLN-64 AND CYS-181.
    13. "A tagging-via-substrate technology for detection and proteomics of farnesylated proteins."
      Kho Y., Kim S.C., Jiang C., Barma D., Kwon S.W., Cheng J., Jaunbergs J., Weinbaum C., Tamanoi F., Falck J., Zhao Y.
      Proc. Natl. Acad. Sci. U.S.A. 101:12479-12484(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISOPRENYLATION AT CYS-181.
    14. Cited for: FUNCTION, INTERACTION WITH MTOR; MLST8; RPTOR AND TSC2, MUTAGENESIS OF SER-20; THR-38; ILE-39 AND ASN-41.
    15. "Analysis of mTOR signaling by the small G-proteins, Rheb and RhebL1."
      Tee A.R., Blenis J., Proud C.G.
      FEBS Lett. 579:4763-4768(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF THR-38; GLU-40; ASN-41; PHE-43; LEU-46; THR-48; VAL-49; GLU-53; TYR-54 AND LEU-56, INTERACTION WITH MTOR.
    16. "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: FUNCTION.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Structural basis for the unique biological function of small GTPase RHEB."
      Yu Y., Li S., Xu X., Li Y., Guan K., Arnold E., Ding J.
      J. Biol. Chem. 280:17093-17100(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-169 IN COMPLEX WITH GDP AND GTP.
    19. Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-139.

    Entry informationi

    Entry nameiRHEB_HUMAN
    AccessioniPrimary (citable) accession number: Q15382
    Secondary accession number(s): B3KWN6
    , D3DX13, Q53Y56, Q99444
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 159 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

    Miscellaneous

    The conserved catalytic Gln-64 found in other Ras-like GTPases seems not to be involved in GTP hydrolysis in RHEB.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3