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

Overview
RHOA a small G protein of the Rho family. Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Controls the reorganization of actins into podosomes. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. Note: This description may include information from UniProtKB.
Protein type: G protein, monomeric; G protein, monomeric, Rho; G protein; Motility/polarity/chemotaxis; Oncoprotein
Chromosomal Location of Human Ortholog: 3p21.3
Cellular Component: apical junction complex; cell cortex; cell junction; cleavage furrow; cytosol; endoplasmic reticulum membrane; endosome; extrinsic to internal side of plasma membrane; focal adhesion; lamellipodium; plasma membrane; vesicle
Molecular Function: GTP binding; GTPase activity; myosin binding; protein binding
Biological Process: actin cytoskeleton organization and biogenesis; actin cytoskeleton reorganization; apical junction assembly; cell migration; endothelial cell migration; ephrin receptor signaling pathway; negative chemotaxis; negative regulation of axonogenesis; phosphoinositide-mediated signaling; platelet activation; positive regulation of axonogenesis; positive regulation of cytokinesis; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of lipase activity; positive regulation of neuron differentiation; positive regulation of stress fiber formation; regulation of actin cytoskeleton organization and biogenesis; regulation of cell migration; regulation of osteoblast proliferation; regulation of small GTPase mediated signal transduction; Rho protein signal transduction; stress fiber formation; substantia nigra development; transforming growth factor beta receptor signaling pathway; vascular endothelial growth factor receptor signaling pathway; Wnt receptor signaling pathway, planar cell polarity pathway
Reference #:  P61586 (UniProtKB)
Alt. Names/Synonyms: Aplysia ras-related homolog 12; ARH12; ARHA; h12; oncogene RHO H12; ras homolog gene family, member A; Rho cDNA clone 12; RHO12; RHOA; RHOH12; small GTP binding protein RhoA; Transforming protein RhoA
Gene Symbols: RHOA
Molecular weight: 21,768 Da
Basal Isoelectric point: 5.83  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics  |  Adherens Junction Dynamics  |  B Cell Receptor Signaling  |  Microtubule Dynamics  |  SAPK/JNK Signaling Cascades  |  TGF-ß Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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RHOA

Protein Structure Not Found.
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Sites Implicated In
cell motility, induced: S188‑p
cytoskeletal reorganization: S88‑p, T100‑p, S188‑p
activity, induced: S88‑p, T100‑p
activity, inhibited: S188‑p
intracellular localization: S88‑p, T100‑p, S188‑p
molecular association, regulation: S188‑p
protein stabilization: S188‑p

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



 LTP 

LTP: 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.


 HTP 

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


       human

► Hide Isoforms
 
0 2 T19‑p GDGACGKtCLLIVFs
1 2 S26‑p tCLLIVFsKDQFPEV
1 14 Y34‑p KDQFPEVyVPTVFEN
1 0 Y34‑ad KDQFPEVyVPTVFEN
1 10 Y66‑p DTAGQEDyDRLRPLS
1 0 S88‑p LMCFSIDsPDSLENI
1 0 T100‑p ENIPEKWtPEVkHFC
0 4 K104‑ub EKWtPEVkHFCPNVP
0 5 K118‑ub PIILVGNkkDLRNDE
0 3 K119‑ub IILVGNkkDLRNDEH
0 1 K133 HTRRELAKMkQEPVk
0 1 K133‑ub HTRRELAkMkQEPVk
0 1 K135 RRELAkMKQEPVkPE
1 102 K135‑ub RRELAkMkQEPVkPE
0 2 K140‑ub kMkQEPVkPEEGRDM
0 1 - gap
0 1 - gap
0 29 Y156‑p NRIGAFGyMECsAKT
0 1 S160‑p AFGyMECsAKTkDGV
0 1 K162 GyMECsAKTkDGVRE
0 1 K164‑ub MECsAKTkDGVREVF
10 0 S188‑p ARRGKKKsGCLVL__
  RHOA iso3  
T19 GDGACGKTCLLIVFS
S26 TCLLIVFSKDQFPEV
Y34 KDQFPEVYVPTVFEN
Y34 KDQFPEVYVPTVFEN
Y66 DTAGQEDYDRLRPLS
S88 LMCFSIDSPDSLENI
T100 ENIPEKWTPEVKHFC
K104 EKWTPEVKHFCPNVP
K118 PIILVGNKKDLRNDE
K119 IILVGNKKDLRNDEH
K133 HTRRELAKMKQEPHC
K133 HTRRELAKMKQEPHC
K135 RRELAKMKQEPHCVA
K135 RRELAKMKQEPHCVA
- gap
S168‑p FKRFPCLsLLSsWGY
S172‑p PCLsLLSsWGYRRPL
- gap
- gap
- gap
- gap
- gap
  mouse

 
T19‑p GDGACGKtCLLIVFs
S26‑p tCLLIVFsKDQFPEV
Y34 KDQFPEVYVPTVFEN
Y34 KDQFPEVYVPTVFEN
Y66 DTAGQEDYDRLRPLS
S88 LMCFSIDSPDSLENI
T100 ENIPEKWTPEVkHFC
K104‑ub EKWTPEVkHFCPNVP
K118‑ub PIILVGNkkDLRNDE
K119‑ub IILVGNkkDLRNDEH
K133 HTRRELAKMkQEPVK
K133 HTRRELAKMkQEPVK
K135 RRELAKMKQEPVKPE
K135‑ub RRELAKMkQEPVKPE
K140 KMkQEPVKPEEGRDM
- gap
- gap
Y156‑p NRIGAFGyMECSAkT
S160 AFGyMECSAkTKDGV
K162‑ub GyMECSAkTKDGVRE
K164 MECSAkTKDGVREVF
S188‑p ARRGKKKsGCLIL__
  rat

 
T19 GDGACGKTCLLIVFS
S26 TCLLIVFSKDQFPEV
Y34 KDQFPEVYVPTVFEN
Y34 KDQFPEVYVPTVFEN
Y66 DTAGQEDYDRLRPLS
S88 LMCFSIDSPDSLENI
T100 ENIPEKWTPEVKHFC
K104 EKWTPEVKHFCPNVP
K118 PIILVGNKKDLRNDE
K119 IILVGNKKDLRNDEH
K133‑ac HTRRELAkMkQEPVK
K133 HTRRELAKMkQEPVK
K135‑ac RRELAkMkQEPVKPE
K135‑ub RRELAkMkQEPVKPE
K140 kMkQEPVKPEEGRDM
- gap
- gap
Y156‑p NRIGAFGyMECSAKT
S160 AFGyMECSAKTKDGV
K162 GyMECSAKTKDGVRE
K164 MECSAKTKDGVREVF
S188 ARRGKKKSGCLIL__
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