Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-01181
Entry Name
UniProt Accession
Theoretical PI
5.65
Molecular Weight
20479.45
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
GTP-binding protein Rheb
Protein Synonyms/Alias
Ras homolog enriched in brain;
Gene Name
Rheb
Gene Synonyms/Alias
Created Date
30-MAY-2000
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
181
Canonical
ASQGKSSCSVM****
[1]
S-Farnesylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] Clark GJ, Kinch MS, Rogers-Graham K, Sebti SM, Hamilton AD, Der CJ. TheRas-related protein Rheb is farnesylated and antagonizes Ras signaling andtransformation. J Biol Chem. 1997 Apr 18;272(16):10608-15.[PMID:9099708]
Functional Description
Stimulates the phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1 signaling. Activates the protein kinase activity of mTORC1. Has low intrinsic GTPase activity (By similarity).
Sequence Annotation
Nucleotide-binding: 16 21 GTP.
Nucleotide-binding: 32 38 GTP.
Nucleotide-binding: 149 150 GTP.
Motif: 35 43 Effector region.
Metal binding site: 20 20 Magnesium.
Metal binding site: 38 38 Magnesium.
Modified residue: 130 130 Phosphoserine; by MAPKAPK5.
Modified residue: 181 181 Cysteine methyl ester.
Protein Length
184 AA.
Protein Sequence
(Canonical)
MPQSKSRKIA ILGYRSVGKS SLTIQFVEGQ FVDSYDPTIE NTFTKLITVN GQEYHLQLVD  60
TAGQDEYSIF PQTYSIDING YILVYSVTSI KSFEVIKVIH GKLLDMVGKV QIPIMLVGNK  120
KDLHMERVIS YEEGKALAES WNAAFLESSA KENQTAVDVF RRIILEAEKI DGAASQGKSS  180
CSVM                                                               184
FASTA
(Canonical)
>LipidDB-10116-01181|Q62639
MPQSKSRKIAILGYRSVGKSSLTIQFVEGQFVDSYDPTIENTFTKLITVNGQEYHLQLVD
TAGQDEYSIFPQTYSIDINGYILVYSVTSIKSFEVIKVIHGKLLDMVGKVQIPIMLVGNK
KDLHMERVISYEEGKALAESWNAAFLESSAKENQTAVDVFRRIILEAEKIDGAASQGKSS
CSVM
Gene Ontology
GO:0030425; C:dendrite; IDA:RGD
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl
GO:0043025; C:neuronal cell body; IDA:RGD
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW
GO:0005681; C:spliceosomal complex; IEA:Ensembl
GO:0019003; F:GDP binding; IDA:RGD
GO:0005525; F:GTP binding; IDA:RGD
GO:0003924; F:GTPase activity; IDA:RGD
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0032008; P:positive regulation of TOR signaling; ISS:UniProtKB
GO:0048168; P:regulation of neuronal synaptic plasticity; NAS:RGD
GO:0007264; P:small GTPase mediated signal transduction; IDA:RGD
Interpro
InterPro; IPR027417; P-loop_NTPase
InterPro; IPR005225; Small_GTP-bd_dom
InterPro; IPR001806; Small_GTPase
InterPro; IPR020849; Small_GTPase_Ras
Pfam
Pfam; PF00071; Ras;
SMART
SMART; SM00173; RAS;
PROSITE
PROSITE; PS51421; RAS;
PRINTS
PRINTS; PR00449; RASTRNSFRMNG;