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Protein Page:
RHEB (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RHEB Stimulates the phosphorylation of S6K1 and EIF4EBP1 through activation of mTORC1 signaling. Activates the protein kinase activity of mTORC1. Has low intrinsic GTPase activity. Binds to mTORC1 in a guanyl nucleotide-independent manner. Interacts directly with MTOR, MLST8 and RPTOR. Interacts with TSC2. Ubiquitous. Highest levels observed in skeletal and cardiac muscle. 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. Belongs to the small GTPase superfamily. Rheb family. Note: This description may include information from UniProtKB.
Protein type: G protein, monomeric, Rheb; G protein; G protein, monomeric
Cellular Component: spliceosome; membrane; cell soma; dendrite; plasma membrane; cytosol
Molecular Function: GTPase activity; protein binding; GDP binding; GTP binding; metal ion binding; protein kinase binding
Biological Process: GTP catabolic process; small GTPase mediated signal transduction; insulin receptor signaling pathway; cell cycle arrest; signal transduction; positive regulation of TOR signaling pathway
Reference #:  Q15382 (UniProtKB)
Alt. Names/Synonyms: GTP-binding protein Rheb; MGC111559; Ras homolog enriched in brain; Ras homolog enriched in brain 2; RHEB; RHEB2
Gene Symbols: RHEB
Molecular weight: 20,497 Da
Basal Isoelectric point: 5.65  Predict pI for various phosphorylation states
CST Pathways:  Insulin Receptor Signaling  |  mTOR Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RHEB

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 6 Y14-p RKIAILGyRsVGKSS
0 1 S16-p IAILGyRsVGKSSLT
0 2 K120-ub PIMLVGNkKDLHMER
1 0 S130-p LHMERVIsYEEGkAL
0 1 K135-ub VIsYEEGkALAESWN
0 1 K151-ub AFLESSAkENQTAVD
0 1 R161 QTAVDVFRRIILEAE
0 1 R161 QTAVDVFRRIILEAE
0 1 R161 QTAVDVFRRIILEAE
0 1 K169 RIILEAEKMDGAAsQ
0 1 K169-ub RIILEAEkMDGAAsQ
0 9 S175-p EkMDGAAsQGKSSCS
  mouse

 
Y14 RKIAILGYRSVGKSS
S16 IAILGYRSVGKSSLT
K120-ub PIMLVGNkKDLHMER
S130 LHMERVISYEEGKAL
K135 VISYEEGKALAESWN
K151 AFLESSAKENQTAVD
K161-ac QTAVDVFkRIILEAE
K161-ub QTAVDVFkRIILEAE
K161-sc QTAVDVFkRIILEAE
K169-ac RIILEAEkIDGAAsQ
K169 RIILEAEKIDGAAsQ
S175-p EkIDGAAsQGKSSCS
  rat

 
Y14-p RKIAILGyRSVGKSS
S16 IAILGyRSVGKSSLT
K120 PIMLVGNKKDLHMER
S130 LHMERVISYEEGKAL
K135 VISYEEGKALAESWN
K151 AFLESSAKENQTAVD
R161 QTAVDVFRRIILEAE
R161 QTAVDVFRRIILEAE
R161 QTAVDVFRRIILEAE
K169 RIILEAEKIDGAASQ
K169 RIILEAEKIDGAASQ
S175 EKIDGAASQGKSSCS
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