ARHA
entrez
387
canonical
uniprot
P61586
canonical
ensembl
ENSG00000067560
resolver
ensp
ENSP00000394483
resolver
ensp
ENSP00000400175
resolver
ensp
ENSP00000408402
resolver
ensp
ENSP00000413587
resolver
ensp
ENSP00000503282
resolver
ensp
ENSP00000504180
resolver
ensp
ENSP00000504603
resolver
ensp
ENSP00000550141
resolver
ensp
ENSP00000550142
resolver
ensp
ENSP00000550143
resolver
ensp
ENSP00000550144
resolver
ensp
ENSP00000588115
resolver
ensp
ENSP00000588116
resolver
ensp
ENSP00000588120
resolver
ensp
ENSP00000588122
resolver
ensp
ENSP00000588123
resolver
ensp
ENSP00000588124
resolver
ensp
ENSP00000588125
resolver
ensp
ENSP00000630795
resolver
ensp
ENSP00000630796
resolver
ensp
ENSP00000630797
resolver
ensp
ENSP00000630798
resolver
enst
ENST00000418115
resolver
enst
ENST00000422781
resolver
enst
ENST00000445425
resolver
enst
ENST00000454011
resolver
enst
ENST00000676712
resolver
enst
ENST00000678200
resolver
enst
ENST00000679208
resolver
enst
ENST00000880082
resolver
enst
ENST00000880083
resolver
enst
ENST00000880084
resolver
enst
ENST00000880085
resolver
enst
ENST00000918056
resolver
enst
ENST00000918057
resolver
enst
ENST00000918061
resolver
enst
ENST00000918063
resolver
enst
ENST00000918065
resolver
enst
ENST00000918066
resolver
enst
ENST00000960736
resolver
enst
ENST00000960737
resolver
enst
ENST00000960738
resolver
enst
ENST00000960739
resolver
genesymbol
ARHA
resolver
genesymbol
RHOA
resolver
genesymbol_syn
ARH12
resolver
genesymbol_syn
ARHA
resolver
genesymbol_syn
RHO12
resolver
hgnc
HGNC:667
resolver
uniprot
A0A024R2W1
resolver
uniprot
A0A024R324
resolver
uniprot
A0A7I2YQV1
resolver
uniprot
B4DKN9
resolver
uniprot
C9JRM1
resolver
uniprot
C9JX21
resolver
uniprot
P06749
resolver
uniprot
Q53HM4
resolver
uniprot
Q5U024
resolver
uniprot
Q9BVT0
resolver
uniprot
Q9UDJ0
resolver
uniprot
Q9UEJ4
resolver
uniprot_entry
A0A024R324_HUMAN
resolver
uniprot_entry
A0A7I2YQV1_HUMAN
resolver
uniprot_entry
B4DKN9_HUMAN
resolver
uniprot_entry
C9JRM1_HUMAN
resolver
uniprot_entry
C9JX21_HUMAN
resolver
uniprot_entry
Q9BVT0_HUMAN
resolver
uniprot_entry
RHOA_HUMAN
resolver
uniprot_sec
A0A024R2W1
resolver
uniprot_sec
P06749
resolver
uniprot_sec
Q53HM4
resolver
uniprot_sec
Q5U024
resolver
uniprot_sec
Q9UDJ0
resolver
uniprot_sec
Q9UEJ4
resolver
activity_regulation
ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP, GTPase activating proteins (GAPs) which increase the GTP hydrolysis activity and GDP dissociation inhibitors which inhibit the dissociation of the nucleotide from the GTPase. Activated by GEFs such as ARHGEF2, ARHGEF3, ARHGEF28 and BCR (PubMed:12221096, PubMed:23940119). Activated by ARHGEF40 in response to mechanotransduction in endothelial cells (By similarity). Inhibited by GAPs such as ARHGAP30 (PubMed:21565175). Inhibited by GDP dissociation inhibitors such as ARHGDIA (PubMed:20400958). {ECO:0000250|UniProtKB:P24406, ECO:0000269|PubMed:12221096, ECO:0000269|PubMed:20400958, ECO:0000269|PubMed:21565175, ECO:0000269|PubMed:23940119}.
uniprot
proteins
amino_acid_sequence
MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQARRGKKKSGCLVL
uniprot
proteins
disease_involvement
DISEASE: Ectodermal dysplasia with facial dysmorphism and acral, ocular, and brain anomalies (EDFAOB) [MIM:618727]: A neuroectodermal syndrome characterized by linear hypopigmentation, alopecia, apparently asymptomatic leukoencephalopathy, and facial, ocular, dental and acral anomalies. Patients show no intellectual or neurologic impairment. {ECO:0000269|PubMed:31570889}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.5.2
uniprot
proteins
function
FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. Mainly associated with cytoskeleton organization, in active state binds to a variety of effector proteins to regulate cellular responses such as cytoskeletal dynamics, cell migration and cell cycle (PubMed:23871831). Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers (PubMed:31570889, PubMed:8910519, PubMed:9121475). Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis (PubMed:12900402, PubMed:16236794). Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion (PubMed:20974804, PubMed:23940119). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly (PubMed:19934221). 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 (PubMed:20937854). Involved in the reorientation of endothelial cells and their actin stress fibers in response to cellular mechantransduction-mediated activation by ARHGEF40 (By similarity). Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation; promotes KCNA2 endocytosis (PubMed:19403695, PubMed:9635436). Acts as an allosteric activator of guanine nucleotide exchange factor ECT2 by binding in its activated GTP-bound form to the PH domain of ECT2 which stimulates the release of PH inhibition and promotes the binding of substrate RHOA to the ECT2 catalytic center (PubMed:31888991). May be an activator of PLCE1 (PubMed:16103226). In neurons, involved in the inhibition of the initial spine growth. Upon activation by CaMKII, modulates dendritic spine structural plasticity by relaying CaMKII transient activation to synapse-specific, long-term signaling (By similarity). Acts as a regulator of platelet alpha-granule release during activation and aggregation of platelets (By similarity). When activated by DAAM1 may signal centrosome maturation and chromosomal segregation during cell division. May also be involved in contractile ring formation during cytokinesis. {ECO:0000250|UniProtKB:P24406, ECO:0000250|UniProtKB:P61589, ECO:0000250|UniProtKB:Q9QUI0, ECO:0000269|PubMed:12900402, ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:19403695, ECO:0000269|PubMed:19934221, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:23871831, ECO:0000269|PubMed:23940119, ECO:0000269|PubMed:31570889, ECO:0000269|PubMed:31888991, 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. {ECO:0000269|PubMed:12062101, ECO:0000269|PubMed:12538863}.
uniprot
proteins
mass_dalton
21768
uniprot
proteins
mutagenesis
MUTAGEN 14; /note="G->V: Increased Rho protein signal transduction. Constitutively active."; /evidence="ECO:0000269|PubMed:19948726, ECO:0000269|PubMed:31570889"; MUTAGEN 19; /note="T->N: Decreased Rho protein signal transduction. Decreased substrate adhesion-dependent cell spreading. Decreased stress fibers assembly. Decreased cytoplasmic microtubule organization."; /evidence="ECO:0000269|PubMed:31570889"; MUTAGEN 34; /note="Y->A: Abolishes interaction with DGKQ."; /evidence="ECO:0000269|PubMed:10066731, ECO:0000269|PubMed:19362538"; MUTAGEN 34; /note="Y->F: Abolishes AMPylation by Haemophilus IbpA."; /evidence="ECO:0000269|PubMed:10066731, ECO:0000269|PubMed:19362538"; MUTAGEN 37; /note="T->A: Abolished monoglucosylation by C.difficile toxin TcdA. Abolished O-GlcNAcylation by C.novyi toxin TcdA."; /evidence="ECO:0000269|PubMed:7775453, ECO:0000269|PubMed:8810274"; MUTAGEN 63; /note="Q->L: Causes constitutive activation."; MUTAGEN 135; /note="K->R: Reduced FBXL19-mediated ubiquitination and subsequent degradation."; /evidence="ECO:0000269|PubMed:23871831"; MUTAGEN 185..187; /note="KKK->RRR: In 3KR mutant; abolished stearoylation in response to S.flexneri infection."; /evidence="ECO:0000269|PubMed:30061757"; MUTAGEN 193; /note="L->M: Converts geranyl-geranylation to farnesylation; does not prevent the cleavage by yopT."; /evidence="ECO:0000269|PubMed:12538863
uniprot
proteins
post_translational_modification
PTM: (Microbial infection) Substrate for botulinum ADP-ribosyltransferase. {ECO:0000269|PubMed:1328215}.; PTM: (Microbial infection) 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. {ECO:0000269|PubMed:12062101, ECO:0000269|PubMed:12538863}.; PTM: (Microbial infection) 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. {ECO:0000269|PubMed:19039103, ECO:0000269|PubMed:19362538}.; PTM: (Microbial infection) Glycosylated at Tyr-34 by Photorhabdus asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230 inhibits downstream signaling by an impaired interaction with diverse regulator and effector proteins of Rho and leads to actin disassembly. {ECO:0000269|PubMed:24141704}.; PTM: (Microbial infection) Glucosylated at Thr-37 by C.difficile toxins TcdA and TcdB in the colonic epithelium (PubMed:24905543, PubMed:7775453, PubMed:7777059). Monoglucosylation completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form, leading to actin cytoskeleton disruption and cell death, resulting in the loss of colonic epithelial barrier function (PubMed:7775453, PubMed:7777059). {ECO:0000269|PubMed:24905543, ECO:0000269|PubMed:7775453, ECO:0000269|PubMed:7777059}.; PTM: (Microbial infection) Glycosylated (O-GlcNAcylated) at Thr-37 by C.novyi toxin TcdA (PubMed:8810274). O-GlcNAcylation completely prevents the recognition of the downstream effector, blocking the GTPases in their inactive form, leading to actin cytoskeleton disruption (PubMed:8810274). {ECO:0000269|PubMed:8810274}.; PTM: (Microbial infection) Stearoylated By S.flexneri N-epsilon-fatty acyltransferase IcsB, thereby disrupting the host actin cytoskeleton. {ECO:0000269|PubMed:30061757}.; PTM: Phosphorylation by PRKG1 at Ser-188 inactivates RHOA signaling (PubMed:11162591). Phosphorylation by SLK at Ser-188 in response to AGTR2 activation (By similarity). {ECO:0000250|UniProtKB:P61589, ECO:0000269|PubMed:11162591}.; PTM: Ubiquitinated by the BCR(KCTD13) and BCR(TNFAIP1) E3 ubiquitin ligase complexes, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and synaptic transmission in neurons (PubMed:19782033). Ubiquitinated at Lys-135 in a FBXL19-mediated manner; leading to proteasomal degradation (PubMed:23871831). {ECO:0000269|PubMed:19782033, ECO:0000269|PubMed:23871831}.; PTM: Serotonylation of Gln-63 by TGM2 during activation and aggregation of platelets leads to constitutive activation of GTPase activity. {ECO:0000250|UniProtKB:Q9QUI0}.
uniprot
proteins
protein_family
Rho family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
10066731
uniprot
proteins
pubmed
10388627
uniprot
proteins
pubmed
10438814
uniprot
proteins
pubmed
10748207
uniprot
proteins
pubmed
10940294
uniprot
proteins
pubmed
11162591
uniprot
proteins
pubmed
11696353
uniprot
proteins
pubmed
11927263
uniprot
proteins
pubmed
12006984
uniprot
proteins
pubmed
12062101
uniprot
proteins
pubmed
12221096
uniprot
proteins
pubmed
12538863
uniprot
proteins
pubmed
12551911
uniprot
proteins
pubmed
12777804
uniprot
proteins
pubmed
12900402
uniprot
proteins
pubmed
1328215
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1556108
uniprot
proteins
pubmed
16103226
uniprot
proteins
pubmed
16236794
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
17115030
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
19039103
uniprot
proteins
pubmed
19362538
uniprot
proteins
pubmed
19403695
uniprot
proteins
pubmed
19782033
uniprot
proteins
pubmed
19934221
uniprot
proteins
pubmed
19948726
uniprot
proteins
pubmed
20400958
uniprot
proteins
pubmed
20499158
uniprot
proteins
pubmed
20709748
uniprot
proteins
pubmed
20937854
uniprot
proteins
pubmed
20974804
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21565175
uniprot
proteins
pubmed
23325789
uniprot
proteins
pubmed
23871831
uniprot
proteins
pubmed
23940119
uniprot
proteins
pubmed
24141704
uniprot
proteins
pubmed
24259668
uniprot
proteins
pubmed
24905543
uniprot
proteins
pubmed
25588844
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
25959226
uniprot
proteins
pubmed
27807006
uniprot
proteins
pubmed
28630045
uniprot
proteins
pubmed
30061757
uniprot
proteins
pubmed
30190425
uniprot
proteins
pubmed
31570889
uniprot
proteins
pubmed
31888991
uniprot
proteins
pubmed
3822842
uniprot
proteins
pubmed
7775453
uniprot
proteins
pubmed
7777059
uniprot
proteins
pubmed
7835413
uniprot
proteins
pubmed
8039707
uniprot
proteins
pubmed
8617235
uniprot
proteins
pubmed
8641286
uniprot
proteins
pubmed
8810274
uniprot
proteins
pubmed
8910519
uniprot
proteins
pubmed
9121475
uniprot
proteins
pubmed
9302995
uniprot
proteins
pubmed
9545299
uniprot
proteins
pubmed
9635436
uniprot
proteins
pubmed
9857026
uniprot
proteins
sequence_length
193
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Cytoplasm, cell cortex {ECO:0000269|PubMed:9635436}. Midbody. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q9QUI0}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9QUI0}. Nucleus {ECO:0000269|PubMed:12551911}. Cytoplasm {ECO:0000269|PubMed:23871831}. 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 an activated form and in a myosin- and actin-independent manner. Colocalizes with KANK1 at the contractile ring. Colocalizes with DAAM1 and KANK1 around centrosomes. {ECO:0000250|UniProtKB:Q9QUI0}.
uniprot
proteins