Human RhoA (phospho S188) peptide (ab42767)

General Info

• Alternative names
  • Aplysia ras related homolog 12
  • ARH12
  • ARHA

  • H 12
  • H12
  • Oncogene RHO H12
  • Ras homolog family member A
  • Ras homolog gene family member A
  • Rho A
  • Rho cDNA clone 12
  • RHO H12
  • RHO12
  • RHOA
  • RHOA_HUMAN
  • RHOH12
  • Small GTP binding protein Rho A
  • Transforming protein Rho A
  • Transforming protein RhoA

  see all
• FunctionRegulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP.
• Sequence similaritiesBelongs to the small GTPase superfamily. Rho family.
• DomainThe basic-rich region is essential for yopT recognition and cleavage.
• Post-translational
  modificationsSubstrate for botulinum ADP-ribosyltransferase.
  Cleaved by yopT protease when the cell is infected by some Yersinia pathogens. This removes the lipid attachment, and leads to its displacement from plasma membrane and to subsequent cytoskeleton cleavage.
  AMPylation at Tyr-34 and Thr-37 are mediated by bacterial enzymes in case of infection by H.somnus and V.parahaemolyticus, respectively. AMPylation occurs in the effector region and leads to inactivation of the GTPase activity by preventing the interaction with downstream effectors, thereby inhibiting actin assembly in infected cells. It is unclear whether some human enzyme mediates AMPylation; FICD has such ability in vitro but additional experiments remain to be done to confirm results in vivo.
  Ubiquitinated by the BCR(BACURD1) and BCR(BACURD2) E3 ubiquitin ligase complexes, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration.
• Cellular localizationCell membrane. Cytoplasm > cytoskeleton.

• Target information above from: UniProt accession P61586 The UniProt Consortium
  The Universal Protein Resource (UniProt) in 2010
  Nucleic Acids Res. 38:D142-D148 (2010) .

  Information by UniProt