Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Transforming protein RhoA  

UniProtKB / Swiss-Prot ID :  RHOA_HUMAN

Gene Name (Synonyms) : 
RHOA, ARH12, ARHA, RHO12  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Cytoplasm, cell cortex. Midbody. Note=Localized to cell-cell contacts in calcium- treated keratinocytes (By similarity). Translocates to the equatorial region before 

Protein Function :  Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. Stimulates PKN2 kinase activity. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA- DIAPH1 signaling pathway plays an important role in ERBB2- dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. 

Protein Sequence MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLR...
Predicted Secondary Structure CCCCEEEEEEEECCCCCHHHHHHHHHHCCCCCCCCCCCEEEEEEEEEECCEEEEEEEEECCCCHHHHHHH...
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
34N-acetyltyrosineFPEVYVPTV
CCCCCCCCC
10.07Phosphositeplus
Link
34O-AMP-tyrosine; by Haemophilus IbpA.FPEVYVPTV
CCCCCCCCC
10.07UniProtKB
Link
34PhosphotyrosineFPEVYVPTV
CCCCCCCCC
10.07Phosphositeplus
Link
37O-AMP-threonine; by Vibrio VopS.VYVPTVFEN
CCCCCCEEE
27.99UniProtKB
Link
66PhosphotyrosineGQEDYDRLR
CCHHHHHHH
11.38Phosphositeplus
Link
104Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TPEVKHFCP
HHHHHHHCC
29.33Phosphositeplus
Link
133Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RELAKMKQE
HHHHHHHCC
60.29Phosphositeplus
Link
135Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LAKMKQEPV
HHHHHCCCC
51.29Phosphositeplus
Link
140Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QEPVKPEEG
CCCCCHHHH
58.38Phosphositeplus
Link
156PhosphotyrosineGAFGYMECS
CCCEEEEEE
5.36Phosphositeplus
Link
156Phosphotyrosine.GAFGYMECS
CCCEEEEEE
5.36UniProtKB
Link
188PhosphoserineGKKKSGCLV
CCCCCCCEE
43.55Phosphositeplus
Link-
188Phosphoserine (PKA_group)GKKKSGCLV
CCCCCCCEE
43.55PhosphoELM
Link-
188Phosphoserine (PRKACA)GKKKSGCLV
CCCCCCCEE
43.55HPRD
Link-
188Phosphoserine; by PKG/PRKG1.GKKKSGCLV
CCCCCCCEE
43.55UniProtKB
Link-
190Cysteine methyl ester.KKSGCLVL
CCCCCEEC
2.83UniProtKB
Link-
190S-geranylgeranyl cysteine.KKSGCLVL
CCCCCEEC
2.83UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
UBIQ_HUMANubiquitination reactionMINT-56526MINT15710384
RHOH_HUMANphysical interactionMINT-56521MINT15670823
CNKR1_HUMANphysical interactionMINT-56518MINT15670823
CNKR1_HUMANphysical interactionMINT-56516MINT15670823
CNKR1_HUMANphysical interactionMINT-56522MINT15670823
CNKR1_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
EBI-1244009
EBI-1244882
EBI-1
intact15670823
15670823
15670823
15670823
SMUF2_HUMAN414(enzymatic reactionEBI-1532826
intact17719543
UBIQ_HUMAN414(enzymatic reactionEBI-1532826
intact17719543
RHG01_HUMANphysical interaction
direct interaction
EBI-760378
EBI-1033210
intact16189514
11927263
PKN1_HUMANdirect interactionEBI-1028839
intact10619026
ARHGB_HUMANdirect interactionEBI-1040765
intact15530360
RTKN_HUMANphysical interactionEBI-446690
intact12879077
ITPR1_HUMANin vitro
in vivo
HPRD:01323HPRD12766172
RHOA_HUMANin vitroHPRD:01323HPRD15069594
TGFR1_HUMANin vivoHPRD:01323HPRD15761153
KPCZ_HUMANin vivoHPRD:01323HPRD15210811
DVL2_HUMANin vivoHPRD:01323HPRD12533515
DIAP1_HUMANin vitroHPRD:01323HPRD16109481
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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
"cGMP-dependent protein kinase phosphorylates and inactivates RhoA.";
Sawada N., Itoh H., Yamashita J., Doi K., Inoue M., Masatsugu K.,Fukunaga Y., Sakaguchi S., Sone M., Yamahara K., Yurugi T., Nakao K.;
Biochem. Biophys. Res. Commun. 280:798-805(2001).
Cited for: PHOSPHORYLATION AT SER-188 BY PRKG1.
"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