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Protein

GTP-binding protein Rheb homolog

Gene

Rheb

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Binds GTP and exhibits intrinsic GTPase activity.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi19 – 191MagnesiumBy similarity
Metal bindingi37 – 371MagnesiumBy similarity
Binding sitei62 – 621GTP; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 198GTPBy similarity
Nucleotide bindingi15 – 206GTPBy similarity
Nucleotide bindingi31 – 377GTPBy similarity
Nucleotide bindingi118 – 1214GTPBy similarity
Nucleotide bindingi148 – 1492GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: FlyBase
  • GTP binding Source: FlyBase
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • apical protein localization Source: FlyBase
  • axon guidance Source: FlyBase
  • carbohydrate metabolic process Source: FlyBase
  • cell growth Source: FlyBase
  • G1/S transition of mitotic cell cycle Source: FlyBase
  • imaginal disc growth Source: FlyBase
  • lipid metabolic process Source: FlyBase
  • multicellular organism growth Source: FlyBase
  • negative regulation of autophagy Source: FlyBase
  • phototaxis Source: FlyBase
  • positive regulation of cell growth Source: FlyBase
  • positive regulation of cell size Source: FlyBase
  • positive regulation of ribosome biogenesis Source: FlyBase
  • positive regulation of TOR signaling Source: FlyBase
  • positive regulation of translation Source: FlyBase
  • regulation of autophagy Source: FlyBase
  • regulation of reactive oxygen species metabolic process Source: FlyBase
  • response to starvation Source: FlyBase
  • ribosome biogenesis Source: FlyBase
  • small GTPase mediated signal transduction Source: InterPro
  • synaptic growth at neuromuscular junction Source: FlyBase
  • terminal branching, open tracheal system Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiR-DME-1632852. Macroautophagy.
R-DME-165159. mTOR signalling.
R-DME-166208. mTORC1-mediated signalling.
R-DME-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-DME-5628897. TP53 Regulates Metabolic Genes.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP-binding protein Rheb homolog
Gene namesi
Name:Rheb
ORF Names:CG1081
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0041191. Rheb.

Subcellular locationi

  • Endomembrane system By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity
  • Golgi apparatus membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity
  • Cytoplasmcytosol By similarity
  • Endoplasmic reticulum membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 179179GTP-binding protein Rheb homologPRO_0000082711Add
BLAST
Propeptidei180 – 1823Removed in mature formBy similarityPRO_0000281368

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei179 – 1791Cysteine methyl esterBy similarity
Lipidationi179 – 1791S-farnesyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

PaxDbiQ9VND8.
PRIDEiQ9VND8.

Expressioni

Gene expression databases

BgeeiQ9VND8.
ExpressionAtlasiQ9VND8. differential.
GenevisibleiQ9VND8. DM.

Interactioni

Protein-protein interaction databases

DIPiDIP-60269N.
IntActiQ9VND8. 2 interactions.
STRINGi7227.FBpp0078342.

Structurei

3D structure databases

ProteinModelPortaliQ9VND8.
SMRiQ9VND8. Positions 3-167.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi34 – 429Effector region

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rheb family.Curated

Phylogenomic databases

eggNOGiKOG0395. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00780000121877.
InParanoidiQ9VND8.
KOiK07208.
OMAiTILNSKH.
OrthoDBiEOG7Q2N6K.
PhylomeDBiQ9VND8.

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]
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.

Q9VND8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTKERHIAM MGYRSVGKSS LCIQFVEGQF VDSYDPTIEN TFTKIERVKS
60 70 80 90 100
QDYIVKLIDT AGQDEYSIFP VQYSMDYHGY VLVYSITSQK SFEVVKIIYE
110 120 130 140 150
KLLDVMGKKY VPVVLVGNKI DLHQERTVST EEGKKLAESW RAAFLETSAK
160 170 180
QNESVGDIFH QLLILIENEN GNPQEKSGCL VS
Length:182
Mass (Da):20,731
Last modified:May 1, 2000 - v1
Checksum:iCAB8AE2A988A0179
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF52004.3.
AY094697 mRNA. Translation: AAM11050.1.
RefSeqiNP_730950.2. NM_169068.3.
NP_730951.2. NM_169069.3.
UniGeneiDm.11577.

Genome annotation databases

EnsemblMetazoaiFBtr0078693; FBpp0078342; FBgn0041191.
FBtr0078694; FBpp0078343; FBgn0041191.
GeneIDi117332.
KEGGidme:Dmel_CG1081.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF52004.3.
AY094697 mRNA. Translation: AAM11050.1.
RefSeqiNP_730950.2. NM_169068.3.
NP_730951.2. NM_169069.3.
UniGeneiDm.11577.

3D structure databases

ProteinModelPortaliQ9VND8.
SMRiQ9VND8. Positions 3-167.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60269N.
IntActiQ9VND8. 2 interactions.
STRINGi7227.FBpp0078342.

Proteomic databases

PaxDbiQ9VND8.
PRIDEiQ9VND8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0078693; FBpp0078342; FBgn0041191.
FBtr0078694; FBpp0078343; FBgn0041191.
GeneIDi117332.
KEGGidme:Dmel_CG1081.

Organism-specific databases

CTDi6009.
FlyBaseiFBgn0041191. Rheb.

Phylogenomic databases

eggNOGiKOG0395. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00780000121877.
InParanoidiQ9VND8.
KOiK07208.
OMAiTILNSKH.
OrthoDBiEOG7Q2N6K.
PhylomeDBiQ9VND8.

Enzyme and pathway databases

ReactomeiR-DME-1632852. Macroautophagy.
R-DME-165159. mTOR signalling.
R-DME-166208. mTORC1-mediated signalling.
R-DME-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-DME-5628897. TP53 Regulates Metabolic Genes.

Miscellaneous databases

GenomeRNAii117332.
NextBioi841847.
PROiQ9VND8.

Gene expression databases

BgeeiQ9VND8.
ExpressionAtlasiQ9VND8. differential.
GenevisibleiQ9VND8. DM.

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]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.

Entry informationi

Entry nameiRHEB_DROME
AccessioniPrimary (citable) accession number: Q9VND8
Secondary accession number(s): Q0KIB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.