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

UniProtKB / Swiss-Prot ID :  RHOC_HUMAN

Gene Name (Synonyms) : 
RHOC, ARH9, ARHC  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cell membrane; Lipid-anchor; Cytoplasmic side (Potential). Cleavage furrow. Note=Translocates to the equatorial region before furrow formation in a ECT2-dependent manner. 

Protein Function :  Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Regulates apical junction formation in bronchial epithelial cells. 

Protein Sequence MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYIADIEVDGKQVELALWDTAGQEDYDRLR...
Predicted Secondary Structure CCCCCEEEEEEECCCCCHHHHHHHHHCCCCCCCCCCCCEEEEEEEEEECCEEEEEEEEECCCCHHHHHHH...
Protein Variant
LocationDescription
120D -> H (in dbSNP:rs11538959). VAR_051974
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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
34PhosphotyrosineFPEVYVPTV
CCCCCCCCC
10.07Phosphositeplus
Link
66PhosphotyrosineGQEDYDRLR
CCHHHHHHH
11.38Phosphositeplus
Link
104Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TPEVKHFCP
HHHHHHHCC
29.33Phosphositeplus
Link
156PhosphotyrosineSAFGYLECS
CCCEEEEEE
7.90Phosphositeplus
Link
156Phosphotyrosine.SAFGYLECS
CCCEEEEEE
7.90UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
CNKR1_HUMANphysical interactionMINT-56517MINT15670823
RHG01_HUMANphysical interactionEBI-755929
intact16189514
RHG01_HUMANyeast 2-hybridHPRD:01322HPRD16189514
RBP1_HUMANENSP00000345236STRING
GMIP_HUMANENSP00000345236STRING
PKHG2_HUMANENSP00000345236STRING
PKHG2_HUMANENSP00000345236STRING
PKHG2_HUMANENSP00000345236STRING
RHG05_HUMANENSP00000345236STRING
PDIA2_HUMANENSP00000345236STRING
CHIO_HUMANENSP00000345236STRING
GDIR2_HUMANENSP00000345236STRING
ECT2_HUMANENSP00000345236STRING
CEND3_HUMANENSP00000345236STRING
KALRN_HUMANENSP00000345236STRING
ARHG9_HUMANENSP00000345236STRING
RGRF1_HUMANENSP00000345236STRING
RICH2_HUMANENSP00000345236STRING
NGEF_HUMANENSP00000345236STRING
CDGAP_HUMANENSP00000345236STRING
CDGAP_HUMANENSP00000345236STRING
FGD4_HUMANENSP00000345236STRING
GDIR1_HUMANENSP00000345236STRING
RHG26_HUMANENSP00000345236STRING
FGD2_HUMANENSP00000345236STRING
TIAM2_HUMANENSP00000345236STRING
TIAM2_HUMANENSP00000345236STRING
TIAM1_HUMANENSP00000345236STRING
TIAM1_HUMANENSP00000345236STRING
KALRN_HUMANENSP00000345236STRING
RHG15_HUMANENSP00000345236STRING
RHG15_HUMANENSP00000345236STRING
RHG15_HUMANENSP00000345236STRING
RHG15_HUMANENSP00000345236STRING
RHG15_HUMANENSP00000345236STRING
RHG15_HUMANENSP00000345236STRING
RHG15_HUMANENSP00000345236STRING
RHG15_HUMANENSP00000345236STRING
RHG15_HUMANENSP00000345236STRING
RHG15_HUMANENSP00000345236STRING
RHG15_HUMANENSP00000345236STRING
RHG15_HUMANENSP00000345236STRING
FNBP2_HUMANENSP00000345236STRING
VAV_HUMANENSP00000345236STRING
CEND1_HUMANENSP00000345236STRING
BCR_HUMANENSP00000345236STRING
ABR_HUMANENSP00000345236STRING
RHG01_HUMANENSP00000345236STRING
MYO9B_HUMANENSP00000345236STRING
RHG24_HUMANENSP00000345236STRING
CIP4_HUMANENSP00000345236STRING
GRLF1_HUMANENSP00000345236STRING
TP4A3_HUMANENSP00000345236STRING
RHG10_HUMANENSP00000345236STRING
RHG10_HUMANENSP00000345236STRING
RHG10_HUMANENSP00000345236STRING
RHG10_HUMANENSP00000345236STRING
RHG10_HUMANENSP00000345236STRING
RHG10_HUMANENSP00000345236STRING
PRR5_HUMANENSP00000345236STRING
RHG08_HUMANENSP00000345236STRING
STA13_HUMANENSP00000345236STRING
STA13_HUMANENSP00000345236STRING
RHG06_HUMANENSP00000345236STRING
TRIO_HUMANENSP00000345236STRING
ARHG3_HUMANENSP00000345236STRING
RHG12_HUMANENSP00000345236STRING
SRGP1_HUMANENSP00000345236STRING
RHG09_HUMANENSP00000345236STRING
3BP1_HUMANENSP00000345236STRING
3BP1_HUMANENSP00000345236STRING
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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
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-156, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures