Detailed entry information

Protein Information (annotations from UniProt)

Database IDHIV0006767
UniProt IDP61586
Primary gene name(s)RHOA
Synonym gene name(s)ARH12, ARHA, RHO12
Protein nameTransforming protein RhoA
Protein functionRegulates 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. 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. 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. 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, By similarity. Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation; promotes KCNA2 endocytosis, PubMed:9635436, PubMed:19403695. {ECO:0000250, ECO:0000269|PubMed:12900402, ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:19934221, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:8910519, ECO:0000269|PubMed:9121475, ECO:0000269|PubMed:9635436}.; FUNCTION:, Microbial infection Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. {ECO:0000269|PubMed:12062101, ECO:0000269|PubMed:12538863}.
Subcellular locationCell membrane;
Lipid-anchor;
Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Cytoplasm, cell cortex {ECO:0000269|PubMed:9635436}. Midbody. Cell projection, lamellipodium {ECO:0000250}. Note=Localized to cell-cell contacts in calcium-treated keratinocytes, By similarity. Translocates to the equatorial region before furrow formation in a ECT2-dependent manner. Localizes to the equatorial cell cortex, at the site of the presumptive furrow in early anaphase in a activated form and in a myosin- and actin-independent manner. {ECO:0000250}.
ECO codeClick here for more information.
Amino acid sequence
FASTA format: P61586
Gene Ontology
(Biological Process)
Complete annatation
actin cytoskeleton organization [GO:0030036];
actin cytoskeleton reorganization [GO:0031532];
apical junction assembly [GO:0043297];
apolipoprotein A-I-mediated signaling pathway [GO:0038027];
cell migration [GO:0016477];
cleavage furrow formation [GO:0036089];
endothelial cell migration [GO:0043542];
endothelial tube lumen extension [GO:0097498];
ephrin receptor signaling pathway [GO:0048013];
mitotic cleavage furrow formation [GO:1903673];
mitotic spindle assembly [GO:0090307];
negative chemotaxis [GO:0050919];
negative regulation of axonogenesis [GO:0050771];
negative regulation of cell migration involved in sprouting angiogenesis [GO:0090051];
ossification involved in bone maturation [GO:0043931];
phosphatidylinositol-mediated signaling [GO:0048015];
platelet activation [GO:0030168];
positive regulation of axonogenesis [GO:0050772];
positive regulation of cytokinesis [GO:0032467];
positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123];
positive regulation of lipase activity [GO:0060193];
positive regulation of neuron differentiation [GO:0045666];
positive regulation of NF-kappaB import into nucleus [GO:0042346];
positive regulation of protein serine/threonine kinase activity [GO:0071902];
positive regulation of stress fiber assembly [GO:0051496];
regulation of actin cytoskeleton organization [GO:0032956];
regulation of cell migration [GO:0030334];
regulation of cell motility [GO:2000145];
regulation of osteoblast proliferation [GO:0033688];
regulation of small GTPase mediated signal transduction [GO:0051056];
Rho protein signal transduction [GO:0007266];
Roundabout signaling pathway [GO:0035385];
skeletal muscle satellite cell migration [GO:1902766];
stress fiber assembly [GO:0043149];
substantia nigra development [GO:0021762];
trabecula morphogenesis [GO:0061383];
transforming growth factor beta receptor signaling pathway [GO:0007179];
vascular endothelial growth factor receptor signaling pathway [GO:0048010];
viral process [GO:0016032];
Wnt signaling pathway, planar cell polarity pathway [GO:0060071];
wound healing, spreading of cells [GO:0044319]
Gene Ontology
(Molecular Function)
Complete annatation
GTPase activity [GO:0003924];
GTP binding [GO:0005525];
myosin binding [GO:0017022]
Gene Ontology
(Cellular Component)
Complete annatation
apical junction complex [GO:0043296];
cell cortex [GO:0005938];
cell junction [GO:0030054];
cell periphery [GO:0071944];
cleavage furrow [GO:0032154];
cytoskeleton [GO:0005856];
cytosol [GO:0005829];
endoplasmic reticulum membrane [GO:0005789];
endosome [GO:0005768];
extracellular exosome [GO:0070062];
extrinsic component of cytoplasmic side of plasma membrane [GO:0031234];
focal adhesion [GO:0005925];
lamellipodium [GO:0030027];
midbody [GO:0030496];
plasma membrane [GO:0005886];
vesicle [GO:0031982]
Protein-protein interaction106880
Phylogenetic treeP61586
HIV replication factor status Zhou et al., Cell. Host. Microbe., 2008
      unknown
Brass et al., Science, 2008
      unknown
Smith et al., J. Immunol, 2010
      unknown
Interferon-stimulated
gene status
Lu et al., J. Virol., 2011
      Folds changes 8h: unknown; Folds changes 16h: unknown; Tested: unknown;
Schoggins JW and Rice CM, Curr. Opin. Virol., 2011
      Targeted viruses: unknown
      Viral life cycle: unknown
      Mechanism related to antiviral activity: unknown
Anti-viral restriction factor Liu et al., Retrovirology, 2011
      unknown (Triplicates)

Gene Expression Profile       top

            Up-regulated;            Down-regulated

For brief introduction to each study, please go to the help page.

Gene expression during HIV latency

(1). Mohammadi et al., PLoS Pathog., 2014

Differentially expressed transcripts (Pairwise) during latency and subsequent viral reactivation using several agents - Primary CD4+ T-cell based model


DMSO: Dimethyl suloxyde (negative control) - 0.0033% final
SAHA: Vorinostat (Histone deacetylase inhibitor) - 0.5 μM
CD3: TCR Stimulation by IL-2+ antiCD3/anti-CD28 antibodies
IL7: Interleukin-7 based stimulation
DISU: Disulfiram (alcohol dehydrogenase inhibitor) - 0.5 μM
AZA: 5-azacytidine (AZA; DNA methylation inhibitor) - 1 μM
Experimental Condition Log2 Fold Change P value Adjusted P value
AZA vs. CD30.3342653861695010.3077994806182390.426706564742283
AZA vs. DISU-0.02495927250911550.9211864454563820.994889252656529
AZA vs. IL70.1919757760452590.3165640622867120.999311006273513
AZA vs. SAHA-0.08864789369588830.715775048585810.92034803561728
DISU vs. CD3-0.3711317182274110.3062182155064080.43806903108509
DISU vs. IL70.2074376660613640.4093416540507110.768682063133983
DISU vs. SAHA-0.06187736185623130.8316225396470480.956308812377588
DMSO vs. AZA0.0044928177343940.9785032319469021
DMSO vs. CD3-0.3397694801750170.2880794879795610.397829084830149
DMSO vs. DISU0.02797557237190880.9084686281291110.988283279918411
DMSO vs. IL70.1945571207123430.277571917346410.770410560710448
DMSO vs. SAHA-0.09954057574456220.6724660542259480.897786781843686
HIV vs. Mock in Activation-0.06321102000283310.9189412273205970.999983755607037
HIV vs. Mock in Latency-0.02614811157004570.8737969182279570.999834320637052
IL7 vs. CD3-0.13550365905760.6726148752716690.776187679886121
SAHA vs. CD3-0.4467661172092010.2085024781629660.311750406381179
SAHA vs. IL7-0.2832126276614860.2452807108633990.487533828899691
(2). Iglesias-Ussel et al., J. Virol., 2013

Up and Downregulated transcripts during Latency (Latently infected CD4+ T cells vs Uninfected)- Primary CD4+Tcell based model
Log2 Fold Change P Value
unknown unknown

Gene expression during HIV infection and replication

(1). Imbeault et al., PloS Pathog., 2012

Transcriptomic profiling of HIV-1 infected CD4+ T cells - Primary CD4+ T cells
Experiment type Log2 Fold Change P Value Adjusted P Value
Infected vs. Mock unknown unknown unknown
Infected vs. Bystander unknown unknown unknown
(2). Lefebvre et al., J. Virol., 2011

Transcriptome analysis of T-cell line (Sup T1)
Log2 Fold Change unknown
(3). Li et al., J. Immunol., 2013

Lymphatic tissue
Acute Fold Change Acute P Value Asymt Fold Change Asypt P Value AIDS Fold Change AIDS P Value
unknown unknown unknown unknown unknown unknown
(4). Chang et al., MBio., 2011

Transcriptome analysis of T-cell line (Sup T1)

Derived from Sherrill-Mix et al., BMC Retrovirol., 2015 cross validation
Up-regulated (True) unknown
(5). Sherrill-Mix et al., BMC Retrovirol., 2015

Deep RNA-seq analysis of primary human T cell infected with low passage HIV isolate HIV89.6 - Primary CD4+ T cell based
Test Status Log2 Fold Change P Value
OK -0.17384 0.245114
(6). Rotger et al., PLoS Pathog., 2010

Genome-wide mRNA expression of CD4+ T cells from HIV-infected patient
(Genes differentially expressed (at adjusted p<0.01) according to the empirical Bayes approach)
Log2 Fold Change P Value
unknown unknown

Proteomic/Transcriptomics studies indicating differentially expressed genes mediated by HIV

(1). Greenwood et al., Elife, 2016

Activated (CD3/CD28) Primary human CD4+ T cells infected with pNL4-3-dE-EGFP. The table shows the complete (unfiltered) TMT (tandem mass tag)-based proteomic time course dataset
6 h 24 h 48 h 72 h RTi
1.08 0.967 1.011 1.096 0.928
(2). Navare et al., Virology, 2012

SUP-T1 cell line
FC-4hpi P-value FC-8hpi P-value FC-20hpi P-value Category
unknown unknown unknown unknown unknown unknown unknown
(3). Hyrcza et al., J. Virolo., 2007

Primary human CD4+ and CD8+ T Cells
Affymetrix Prob ID Fold Change In CD8? Category
unknown unknown unknown unknown

Protein Overview       top

Drug-protein Interaction       (annotations from DrugBank)      top

Drugbank ID Drug Name Drug Status Pharmacological Action Drug Action
DB04315 Guanosine-5&,39;-Diphosphate experimental unknown unknown

Protein Secondary Structure       (annotations from PDB)      top

PDB Accession Method Resolution Chain Structure Preview
1A2B X-ray 2.4Å A=1-181.
1CC0 X-ray 5.0Å A/C=1-190.
1CXZ X-ray 2.2Å A=1-181.
1DPF X-ray 2.0Å A=1-180.
1FTN X-ray 2.1Å A=1-193.
1KMQ X-ray 1.5Å A=4-181.
1LB1 X-ray 2.8Å B/D/F/H=1-190.
1OW3 X-ray 1.8Å B=1-193.
1S1C X-ray 2.6Å A/B=1-181.
1TX4 X-ray 1.6Å B=3-179.
1X86 X-ray 3.2Å B/D/F/H=1-193.
1XCG X-ray 2.5Å B/F=3-180.
2RGN X-ray 3.5Å C/F=1-193.
3KZ1 X-ray 2.7Å E/F=1-181.
3LW8 X-ray 1.8Å A/B/C/D=2-181.
3LWN X-ray 2.2Å A/B=2-181.
3LXR X-ray 1.6Å A=2-181.
3MSX X-ray 1.6Å A=1-180.
3T06 X-ray 2.8Å B/F=3-180.
4D0N X-ray 2.1Å A=1-184.
4XH9 X-ray 2.0Å B/E=2-180.
4XOI X-ray 2.0Å A/C=1-180.
4XSG X-ray 1.8Å A=1-179.
4XSH X-ray 2.5Å A=1-179.
5A0F X-ray 2.0Å A=1-181.
5BWM X-ray 2.5Å A=1-179.
5C2K X-ray 1.4Å A=1-193.
5C4M X-ray 1.3Å A=1-193.
5FR1 X-ray 2.7Å A=1-193.
5FR2 X-ray 3.3Å A=1-193.
5HPY X-ray 2.4Å B/F=3-181.
5IRC X-ray 1.7Å D/F=2-181.
5JCP X-ray 2.1Å A/B=1-181.

HIV-1 Interaction       (annotations from NCBI HIV-1 Interaction Database)      top

HIV Partner Interaction Type PubMed
Envelope surface glycoprotein gp120 interacts with 17572668
Tat activates 16105876
1794028617940286
2045780817940286
2045780819794400
19794400
2435956124578133
Vpr upregulates 10713718
Nef downregulates 24949636
capsid downregulated by 24586238
Envelope surface glycoprotein gp120 enhanced by 21936715
Tat requires 22197032

Metabolic/Signalling Pathway       (annotations from KEGG database)      top

Pathway Accession Number Description
hsa04014 Ras signaling pathway - Homo sapiens (human)
hsa04015 Rap1 signaling pathway - Homo sapiens (human)
hsa04022 cGMP-PKG signaling pathway - Homo sapiens (human)
hsa04024 cAMP signaling pathway - Homo sapiens (human)
hsa04062 Chemokine signaling pathway - Homo sapiens (human)
hsa04071 Sphingolipid signaling pathway - Homo sapiens (human)
hsa04072 Phospholipase D signaling pathway - Homo sapiens (human)
hsa04144 Endocytosis - Homo sapiens (human)
hsa04150 mTOR signaling pathway - Homo sapiens (human)
hsa04270 Vascular smooth muscle contraction - Homo sapiens (human)
hsa04310 Wnt signaling pathway - Homo sapiens (human)
hsa04350 TGF-beta signaling pathway - Homo sapiens (human)
hsa04360 Axon guidance - Homo sapiens (human)
hsa04510 Focal adhesion - Homo sapiens (human)
hsa04520 Adherens junction - Homo sapiens (human)
hsa04530 Tight junction - Homo sapiens (human)
hsa04611 Platelet activation - Homo sapiens (human)
hsa04621 NOD-like receptor signaling pathway - Homo sapiens (human)
hsa04660 T cell receptor signaling pathway - Homo sapiens (human)
hsa04670 Leukocyte transendothelial migration - Homo sapiens (human)
hsa04722 Neurotrophin signaling pathway - Homo sapiens (human)
hsa04810 Regulation of actin cytoskeleton - Homo sapiens (human)
hsa04921 Oxytocin signaling pathway - Homo sapiens (human)
hsa04972 Pancreatic secretion - Homo sapiens (human)
hsa05100 Bacterial invasion of epithelial cells - Homo sapiens (human)
hsa05130 Pathogenic Escherichia coli infection - Homo sapiens (human)
hsa05133 Pertussis - Homo sapiens (human)
hsa05152 Tuberculosis - Homo sapiens (human)
hsa05200 Pathways in cancer - Homo sapiens (human)
hsa05203 Viral carcinogenesis - Homo sapiens (human)
hsa05205 Proteoglycans in cancer - Homo sapiens (human)
hsa05206 MicroRNAs in cancer - Homo sapiens (human)
hsa05210 Colorectal cancer - Homo sapiens (human)
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