Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  GTP-binding protein Rheb  

UniProtKB / Swiss-Prot ID :  RHEB_HUMAN

Gene Name (Synonyms) : 
RHEB, RHEB2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cell membrane; Lipid-anchor; Cytoplasmic side (Potential). 

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

Protein Sequence MPQSKSRKIAILGYRSVGKSSLTIQFVEGQFVDSYDPTIENTFTKLITVNGQEYHLQLVDTAGQDEYSIF...
Predicted Secondary Structure CCCCCCEEEEEEECCCCCHHHHHHHHHCCCCCCCCCCCEEEEEEEEEEECCEEEEEEEEECCCCHHHHHH...
Protein Variant
LocationDescription
139E -> K (in a colorectal cancer sample;somatic mutation).
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LVGNKKDLH
EEECCCCCC
41.56Phosphositeplus
Link
130PhosphoserineERVISYEEG
CCCCCHHHH
24.51Phosphositeplus
Link
135Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YEEGKALAE
HHHHHHHHH
43.43Phosphositeplus
Link
151Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ESSAKENQT
EEEECCCCC
60.18Phosphositeplus
Link
169Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LEAEKMDGA
HHHHHCCCC
49.71Phosphositeplus
Link-
181S-farnesyl cysteine.GKSSCSVM
CCCCCCCC
4.60UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
RAF1_HUMANphysical interactionMINT-16189MINT9001246
RAF1_HUMANin vitro
yeast 2-hybrid
HPRD:03188HPRD9001246
TSC2_HUMANin vitroHPRD:03188HPRD12842888
TSC2_HUMANENSP00000262187STRING
KS6B1_HUMANENSP00000262187STRING
RAF1_HUMANENSP00000262187STRING
IF4E_HUMANENSP00000262187STRING
TSC1_HUMANENSP00000262187STRING
RPTOR_HUMANENSP00000262187STRING
4EBP1_HUMANENSP00000262187STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Prenylation
ReferencePubMed
"A tagging-via-substrate technology for detection and proteomics offarnesylated 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).
Cited for: ISOPRENYLATION AT CYS-181.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures