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

UniProtKB / Swiss-Prot ID :  RRAGC_HUMAN

Gene Name (Synonyms) : 
RRAGC  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus. Lysosome. Note=Predominantly cytoplasmic. May shuttle between the cytoplasm and nucleus, depending on the bound nucleotide state of associated RRAGA. 

Protein Function :  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. 

Protein Sequence MSLQYGAEETPLAGSYGAADSFPKDFGYGVEEEEEEAAAAGGGVGAGAGGGCGPGGADSSKPRILLMGLR...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCHHHHCCCCCCHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCEEEEEEEC...
Protein Variant -
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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
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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
2Phosphoserine---MSLQYG
---CCCCCC
24.95HPRD
Link-
2Phosphoserine---MSLQYG
---CCCCCC
24.95Phosphositeplus
Link-
15PhosphoserinePLAGSYGAA
CCCCCCCCC
18.13HPRD
Link-
15PhosphoserinePLAGSYGAA
CCCCCCCCC
18.13Phosphositeplus
Link-
16PhosphotyrosineLAGSYGAAD
CCCCCCCCC
15.18HPRD
Link-
21PhosphoserineGAADSFPKD
CCCCCCHHH
38.43HPRD
Link-
21PhosphoserineGAADSFPKD
CCCCCCHHH
38.43Phosphositeplus
Link-
86PhosphoserineFHKMSPNET
HHHCCCCCE
29.40HPRD
Link
95PhosphoserineLFLESTNKI
EEEEECCCE
39.15HPRD
Link
95PhosphoserineLFLESTNKI
EEEEECCCE
39.15Phosphositeplus
Link
95PhosphoserineLFLESTNKI
EEEEECCCE
39.15SysPTM
Link
95Phosphoserine.LFLESTNKI
EEEEECCCE
39.15UniProtKB
Link
96PhosphothreonineFLESTNKIY
EEEECCCEE
31.02HPRD
Link
96PhosphothreonineFLESTNKIY
EEEECCCEE
31.02Phosphositeplus
Link
96PhosphothreonineFLESTNKIY
EEEECCCEE
31.02SysPTM
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
RRAGA_HUMANphysical interactionMINT-68464MINT16189514
RRAGA_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:12198HPRD11073942
NOL8_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:12198HPRD14660641
RRAGB_HUMANin vivoHPRD:12198HPRD11073942
RRAGC_HUMANin vitroHPRD:12198HPRD11073942
14660641
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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
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures