ARHG
entrez
391
canonical
uniprot
P84095
canonical
ensembl
ENSG00000177105
resolver
ensp
ENSP00000339467
resolver
ensp
ENSP00000380175
resolver
ensp
ENSP00000380176
resolver
ensp
ENSP00000436932
resolver
ensp
ENSP00000551853
resolver
ensp
ENSP00000551854
resolver
ensp
ENSP00000600955
resolver
ensp
ENSP00000613935
resolver
ensp
ENSP00000613936
resolver
ensp
ENSP00000613937
resolver
ensp
ENSP00000613938
resolver
enst
ENST00000351018
resolver
enst
ENST00000396978
resolver
enst
ENST00000396979
resolver
enst
ENST00000533217
resolver
enst
ENST00000881794
resolver
enst
ENST00000881795
resolver
enst
ENST00000930896
resolver
enst
ENST00000943876
resolver
enst
ENST00000943877
resolver
enst
ENST00000943878
resolver
enst
ENST00000943879
resolver
genesymbol
ARHG
resolver
genesymbol
RHOG
resolver
genesymbol_syn
ARHG
resolver
genesymbol_syn
RHOG
resolver
hgnc
HGNC:672
resolver
uniprot
P35238
resolver
uniprot
Q6ICQ8
resolver
uniprot
Q8NI04
resolver
uniprot_entry
Q6ICQ8_HUMAN
resolver
uniprot_entry
RHOG_HUMAN
resolver
uniprot_sec
P35238
resolver
uniprot_sec
Q8NI04
resolver
amino_acid_sequence
MQSIKCVVVGDGAVGKTCLLICYTTNAFPKEYIPTVFDNYSAQSAVDGRTVNLNLWDTAGQEEYDRLRTLSYPQTNVFVICFSIASPPSYENVRHKWHPEVCHHCPDVPILLVGTKKDLRAQPDTLRRLKEQGQAPITPQQGQALAKQIHAVRYLECSALQQDGVKEVFAEAVRAVLNPTPIKRGRSCILL
uniprot
proteins
disease_involvement
DISEASE: Note=Defects in RHOG may be the cause of a severe hemophagocytic lymphohistiocytosis (HLH). The affected patient shows characteristic HLH features, such as hemophagocytosis, hepatosplenomegaly, fever, cytopenias, low hemoglobin, hypertriglyceridemia, and elevated ferritin and soluble interleukin-2 receptor. {ECO:0000269|PubMed:33513601}.
uniprot
proteins
ec_number
3.6.5.2
uniprot
proteins
function
FUNCTION: Plays a role in immunological synaptic F-actin density and architecture organization (PubMed:33513601). Regulates actin reorganization in lymphocytes, possibly through the modulation of Rac1 activity (PubMed:33513601). Acts as an activator of the ELMO-DOCK-Rac pathway (PubMed:32651375, PubMed:38857861). Required for the formation of membrane ruffles during macropinocytosis (PubMed:15133129). Plays a role in cell migration and is required for the formation of cup-like structures during trans-endothelial migration of leukocytes (PubMed:17875742). Binds phospholipids in an activation-dependent manner; thereby acting as an anchor for other proteins to the plasma membrane (PM) (PubMed:33513601). Plays a role in exocytosis of cytotoxic granules (CG) by lymphocytes/Component of the exocytosis machinery in natural killer (NK) and CD8+ T cells (PubMed:33513601). Promotes the docking of cytotoxic granules (CG) to the plasma membrane through the interaction with UNC13D (PubMed:33513601). Involved in the cytotoxic activity of lymphocytes/primary CD8+ T cells (PubMed:33513601). {ECO:0000269|PubMed:15133129, ECO:0000269|PubMed:17875742, ECO:0000269|PubMed:33513601}.; FUNCTION: (Microbial infection) In case of Salmonella enterica infection, activated by SopB and ARHGEF26/SGEF, which induces cytoskeleton rearrangements and promotes bacterial entry. {ECO:0000269|PubMed:17074883}.
uniprot
proteins
mass_dalton
21309
uniprot
proteins
mutagenesis
MUTAGEN 61; /note="Q->L: Constitutively active."; /evidence="ECO:0000269|PubMed:38857861"; MUTAGEN 66; /note="R->A: Abolishes binding to ELMO2."; /evidence="ECO:0000269|PubMed:32651375
uniprot
proteins
post_translational_modification
PTM: (Microbial infection) Glucosylated at Thr-35 by C.difficile toxin TcdB. {ECO:0000269|PubMed:24905543}.; PTM: (Microbial infection) Glycosylated (O-GlcNAcylated) at Thr-35 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}.
uniprot
proteins
protein_family
Rho family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
15133129
uniprot
proteins
pubmed
1620121
uniprot
proteins
pubmed
17074883
uniprot
proteins
pubmed
17875742
uniprot
proteins
pubmed
20679435
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24905543
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
32651375
uniprot
proteins
pubmed
33513601
uniprot
proteins
pubmed
36932164
uniprot
proteins
pubmed
38857861
uniprot
proteins
pubmed
8464478
uniprot
proteins
pubmed
8810274
uniprot
proteins
sequence_length
191
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
uniprot
proteins