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Protein

GTP-binding protein Rheb

Gene

RHEB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Activates the protein kinase activity of mTORC1, and thereby plays a role in the regulation of apoptosis. Stimulates the phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1 signaling. 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 – 201Magnesium1 Publication
Metal bindingi38 – 381Magnesium1 Publication
Binding sitei63 – 631GTP; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi16 – 216GTP2 Publications
Nucleotide bindingi32 – 387GTP2 Publications
Nucleotide bindingi119 – 1224GTP2 Publications
Nucleotide bindingi149 – 1502GTP2 Publications

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

GO - Biological processi

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

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

Endomembrane system 1 PublicationCurated; Lipid-anchor 1 PublicationCurated; Cytoplasmic side 1 PublicationCurated. Golgi apparatus membrane 1 Publication; Lipid-anchor 1 Publication; Cytoplasmic side 1 Publication. Cytoplasmcytosol 1 Publication. Endoplasmic reticulum membrane 1 Publication; Lipid-anchor 1 Publication; Cytoplasmic side 1 Publication

GO - Cellular componenti

  1. cytosol Source: UniProtKB-SubCell
  2. dendrite Source: Ensembl
  3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  4. extracellular vesicular exosome Source: UniProtKB
  5. Golgi membrane Source: UniProtKB-SubCell
  6. membrane Source: ProtInc
  7. neuronal cell body Source: Ensembl
  8. plasma membrane Source: Reactome
  9. spliceosomal complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, 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.1 Publication

Gene expression databases

BgeeiQ15382.
CleanExiHS_RHEB.
ExpressionAtlasiQ15382. baseline and differential.
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. Interacts (when prenylated) with PDE6D; this promotes release from membranes.4 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi111941. 33 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 – 1411Combined sources
Helixi19 – 2810Combined sources
Beta strandi41 – 499Combined sources
Beta strandi52 – 609Combined sources
Beta strandi66 – 683Combined sources
Helixi72 – 743Combined sources
Turni75 – 773Combined sources
Beta strandi79 – 868Combined sources
Helixi90 – 10617Combined sources
Beta strandi114 – 1196Combined sources
Turni124 – 1263Combined sources
Helixi131 – 14010Combined sources
Beta strandi144 – 1474Combined sources
Helixi153 – 16816Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 regionCurated

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rheb family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00780000121877.
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

        10         20         30         40         50
MPQSKSRKIA ILGYRSVGKS SLTIQFVEGQ FVDSYDPTIE NTFTKLITVN
60 70 80 90 100
GQEYHLQLVD TAGQDEYSIF PQTYSIDING YILVYSVTSI KSFEVIKVIH
110 120 130 140 150
GKLLDMVGKV QIPIMLVGNK KDLHMERVIS YEEGKALAES WNAAFLESSA
160 170 180
KENQTAVDVF RRIILEAEKM DGAASQGKSS CSVM
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi111941. 33 interactions.
DIPiDIP-42816N.
IntActiQ15382. 12 interactions.
MINTiMINT-1365334.
STRINGi9606.ENSP00000262187.

Chemistry

BindingDBiQ15382.
ChEMBLiCHEMBL3108656.

PTM databases

PhosphoSiteiQ15382.

Polymorphism databases

DMDMi6919957.

Proteomic databases

MaxQBiQ15382.
PaxDbiQ15382.
PRIDEiQ15382.

Protocols and materials databases

DNASUi6009.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6009.
GeneCardsiGC07M151163.
HGNCiHGNC:10011. RHEB.
HPAiCAB019436.
HPA054743.
MIMi601293. gene.
neXtProtiNX_Q15382.
PharmGKBiPA34389.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00780000121877.
HOGENOMiHOG000233973.
HOVERGENiHBG009351.
InParanoidiQ15382.
KOiK07208.
OMAiTILNSKH.
OrthoDBiEOG7Q2N6K.
PhylomeDBiQ15382.
TreeFamiTF314986.

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.

Miscellaneous databases

ChiTaRSiRHEB. human.
EvolutionaryTraceiQ15382.
GeneWikiiRHEB.
GenomeRNAii6009.
NextBioi23445.
PROiQ15382.
SOURCEiSearch...

Gene expression databases

BgeeiQ15382.
CleanExiHS_RHEB.
ExpressionAtlasiQ15382. baseline and differential.
GenevestigatoriQ15382.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 SPECIFICITY.
    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 MAGNESIUM; GDP AND GTP.
  19. "Arl2-GTP and Arl3-GTP regulate a GDI-like transport system for farnesylated cargo."
    Ismail S.A., Chen Y.X., Rusinova A., Chandra A., Bierbaum M., Gremer L., Triola G., Waldmann H., Bastiaens P.I., Wittinghofer A.
    Nat. Chem. Biol. 7:942-949(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-181 IN COMPLEX WITH GDP AND PDE6D, INTERACTION WITH PDE6D, SUBCELLULAR LOCATION.
  20. 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: March 4, 2015
This is version 164 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.Curated

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.