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Protein Page:
RRAGC (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
RRAGC Has guanine nucleotide-binding activity but weak intrinsic GTPase activity. Probably required for the amino acid- induced relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. This is a crucial step in the activation of the TOR signaling cascade by amino acids. Forms a heterodimer with RRAGA in a sequence-independent manner. Binds GTP. Interacts with NOL8 and RRAGB. Belongs to the GTR/RAG GTP-binding protein family. Note: This description may include information from UniProtKB.
Cellular Component: intracellular membrane-bound organelle; lysosome; cytoplasm; nucleus
Molecular Function: GTPase activity; protein binding; GDP binding; GTP binding; protein heterodimerization activity; magnesium ion binding
Biological Process: transcription, DNA-dependent; GTP catabolic process; apoptosis; RNA splicing; small GTPase mediated signal transduction; cell growth
Reference #:  Q9HB90 (UniProtKB)
Alt. Names/Synonyms: FLJ13311; GTPase-interacting protein 2; GTR2; Rag C; Rag C protein; RagC; Ras-related GTP binding C; Ras-related GTP-binding protein C; RRAGC; TIB929
Gene Symbols: RRAGC
Molecular weight: 44,224 Da
Basal Isoelectric point: 4.94  Predict pI for various phosphorylation states
CST Pathways:  mTOR Signaling  |  Translation: eIF4E and p70S6K
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RRAGC

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 S2-p ______MsLQYGAEE
0 8 S15-p EETPLAGsYGAADsF
0 2 Y16 ETPLAGsYGAADsFP
0 2 S21-p GsYGAADsFPKDFGY
0 2 K79-ub SGKSSIQkVVFHKMS
0 2 S86 kVVFHKMSPNETLFL
0 19 S95-p NETLFLEstNKIYKD
0 11 T96-p ETLFLEstNKIYKDD
0 1 Y327-p LNNTTVLyLKEVTKF
0 2 T381-p HRSCGHQtsAssLKA
0 25 S382-p RSCGHQtsAssLKAL
0 2 S384-p CGHQtsAssLKALTH
0 25 S385-p GHQtsAssLKALTHN
0 8 T394-p KALTHNGtPRNAI__
  mouse

 
S2-p ______MsLQYGAEE
S15-p EETPLAGsyGAADsF
Y16-p ETPLAGsyGAADsFP
S21-p GsyGAADsFPKDFGY
K78-ub SGKSSIQkVVFHKMs
S85-p kVVFHKMsPNETLFL
S94-p NETLFLEstNKIYKD
T95-p ETLFLEstNKIYKDD
Y326 LNNTTVLYLKEVTKF
T380 HRSCSHQTsAPsLKA
S381-p RSCSHQTsAPsLKAL
P383 CSHQTsAPsLKALAH
S384-p SHQTsAPsLKALAHN
T393-p KALAHNGtPRNAI__
  rat

 
S2 ______MSLQYGAEE
S15 EETPLAGSYGAADSF
Y16 ETPLAGSYGAADSFP
S21 GSYGAADSFPKDFGY
K78 SGKSSIQKVVFHKMs
S85-p KVVFHKMsPNETLFL
S94-p NETLFLEstNKIYKD
T95-p ETLFLEstNKIYKDD
Y326 LNNTTVLYLKEVTKF
T380 HRSCSHQTSAPSLKA
S381 RSCSHQTSAPSLKAL
P383 CSHQTSAPSLKALAH
S384 SHQTSAPSLKALAHN
T393 KALAHNGTPRNAI__
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