ARHGEF2
entrez
9181
canonical
uniprot
Q92974
canonical
ensembl
ENSG00000116584
resolver
ensp
ENSP00000314787
resolver
ensp
ENSP00000315325
resolver
ensp
ENSP00000354837
resolver
genesymbol
ARHGEF2
resolver
genesymbol_syn
KIAA0651
resolver
genesymbol_syn
LFP40
resolver
hgnc
HGNC:682
resolver
uniprot
D3DVA6
resolver
uniprot
O75142
resolver
uniprot
Q15079
resolver
uniprot
Q5VY92
resolver
uniprot
Q8TDA3
resolver
uniprot
Q8WUG4
resolver
uniprot
Q9H023
resolver
uniprot_entry
ARHG2_HUMAN
resolver
uniprot_sec
D3DVA6
resolver
uniprot_sec
O75142
resolver
uniprot_sec
Q15079
resolver
uniprot_sec
Q5VY92
resolver
uniprot_sec
Q8TDA3
resolver
uniprot_sec
Q8WUG4
resolver
uniprot_sec
Q9H023
resolver
amino_acid_sequence
MSRIESLTRARIDRSRELASKTREKEKMKEAKDARYTNGHLFTTISVSGMTMCYACNKSITAKEALICPTCNVTIHNRCKDTLANCTKVKQKQQKAALLKNNTALQSVSLRSKTTIRERPSSAIYPSDSFRQSLLGSRRGRSSLSLAKSVSTTNIAGHFNDESPLGLRRILSQSTDSLNMRNRTLSVESLIDEAEVIYSELMSDFEMDEKDFAADSWSLAVDSSFLQQHKKEVMKQQDVIYELIQTELHHVRTLKIMTRLFRTGMLEELHLEPGVVQGLFPCVDELSDIHTRFLSQLLERRRQALCPGSTRNFVIHRLGDLLISQFSGPSAEQMCKTYSEFCSRHSKALKLYKELYARDKRFQQFIRKVTRPAVLKRHGVQECILLVTQRITKYPLLISRILQHSHGIEEERQDLTTALGLVKELLSNVDEGIYQLEKGARLQEIYNRMDPRAQTPVPGKGPFGREELLRRKLIHDGCLLWKTATGRFKDVLVLLMTDVLVFLQEKDQKYIFPTLDKPSVVSLQNLIVRDIANQEKGMFLISAAPPEMYEVHTASRDDRSTWIRVIQQSVRTCPSREDFPLIETEDEAYLRRIKMELQQKDRALVELLREKVGLFAEMTHFQAEEDGGSGMALPTLPRGLFRSESLESPRGERLLQDAIREVEGLKDLLVGPGVELLLTPREPALPLEPDSGGNTSPGVTANGEARTFNGSIELCRADSDSSQRDRNGNQLRSPQEEALQRLVNLYGLLHGLQAAVAQQDTLMEARFPEGPERREKLCRANSRDGEAGRAGAAPVAPEKQATELALLQRQHALLQEELRRCRRLGEERATEAGSLEARLRESEQARALLEREAEEARRQLAALGQTEPLPAEAPWARRPVDPRRRSLPAGDALYLSFNPPQPSRGTDRLDLPVTTRSVHRNFEDRERQELGSPEERLQDSSDPDTGSEEEGSSRLSPPHSPRDFTRMQDIPEETESRDGEAVASES
uniprot
proteins
disease_involvement
DISEASE: Neurodevelopmental disorder with midbrain and hindbrain malformations (NEDMHM) [MIM:617523]: An autosomal recessive neurodevelopmental disorder characterized by intellectual disability, speech delay, mild microcephaly, midbrain-hindbrain malformations, and variable dysmorphic features. {ECO:0000269|PubMed:28453519}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Activates Rho-GTPases by promoting the exchange of GDP for GTP. May be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. Binds Rac-GTPases, but does not seem to promote nucleotide exchange activity toward Rac-GTPases, which was uniquely reported in PubMed:9857026. May stimulate instead the cortical activity of Rac. Inactive toward CDC42, TC10, or Ras-GTPases. Forms an intracellular sensing system along with NOD1 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIP2 dependent NF-kappaB signaling pathways activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides through NOD1 that is independent of its GEF activity, but also in the activation of NF-kappaB by Shigella effector proteins (IpgB2 and OspB) which requires its GEF activity and the activation of RhoA. Involved in innate immune signaling transduction pathway promoting cytokine IL6/interleukin-6 and TNF secretion in macrophage upon stimulation by bacterial peptidoglycans; acts as a signaling intermediate between NOD2 receptor and RIPK2 kinase. Contributes to the tyrosine phosphorylation of RIPK2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. Overexpression activates Rho-, but not Rac-GTPases, and increases paracellular permeability (By similarity). Involved in neuronal progenitor cell division and differentiation (PubMed:28453519). Involved in the migration of precerebellar neurons (By similarity). {ECO:0000250|UniProtKB:Q60875, ECO:0000250|UniProtKB:Q865S3, ECO:0000269|PubMed:19043560, ECO:0000269|PubMed:21887730, ECO:0000269|PubMed:28453519, ECO:0000269|PubMed:9857026}.
uniprot
proteins
mass_dalton
111543
uniprot
proteins
mutagenesis
MUTAGEN 53; /note="C->R: Abolishes microtubule binding, increased activity in vitro."; /evidence="ECO:0000269|PubMed:11912491"; MUTAGEN 143; /note="S->A: Abolishes phosphorylation by PAK4, self aggregation in the cytoplasm. Increases activity; when associated with A-896."; /evidence="ECO:0000269|PubMed:15827085"; MUTAGEN 394; /note="Y->A: Reduces phosphorylation level, normal microtubule localization and activity."; /evidence="ECO:0000269|PubMed:11912491"; MUTAGEN 679; /note="T->A: Reduces phosphorylation level."; /evidence="ECO:0000269|PubMed:18211802"; MUTAGEN 886; /note="S->A: Normal activity."; MUTAGEN 886; /note="S->D: Increases activity. Abolishes nucleotide exchange activity; when associated with D-960."; MUTAGEN 896; /note="S->A: Abolishes phosphorylation by PAK4, self aggregation in the cytoplasm. Increases activity; when associated with A-143."; /evidence="ECO:0000269|PubMed:15827085"; MUTAGEN 960; /note="S->A: Normal activity."; MUTAGEN 960; /note="S->D: Increases activity. Abolishes nucleotide exchange activity; when associated with D-886.
uniprot
proteins
post_translational_modification
PTM: Phosphorylation of Ser-886 by PAK1 induces binding to protein YWHAZ, promoting its relocation to microtubules and the inhibition of its activity. Phosphorylated by AURKA and CDK1 during mitosis, which negatively regulates its activity. Phosphorylation by MAPK1 or MAPK3 increases nucleotide exchange activity. Phosphorylation by PAK4 releases GEF-H1 from the microtubules. Phosphorylated on serine, threonine and tyrosine residues in a RIPK2-dependent manner. {ECO:0000269|PubMed:14970201, ECO:0000269|PubMed:15827085, ECO:0000269|PubMed:17488622, ECO:0000269|PubMed:18211802}.
uniprot
proteins
pubmed
11912491
uniprot
proteins
pubmed
14970201
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15827085
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17488622
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18211802
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18394899
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19043560
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21887730
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2466560
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26820534
uniprot
proteins
pubmed
28453519
uniprot
proteins
pubmed
9734811
uniprot
proteins
pubmed
9857026
uniprot
proteins
sequence_length
986
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11912491, ECO:0000269|PubMed:21887730, ECO:0000269|PubMed:9857026}. Cytoplasm {ECO:0000269|PubMed:15827085, ECO:0000269|PubMed:21887730}. Cell junction, tight junction {ECO:0000269|PubMed:19043560}. Golgi apparatus {ECO:0000269|PubMed:15827085}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17488622}. Cell projection, ruffle membrane {ECO:0000269|PubMed:19043560}. Cytoplasmic vesicle {ECO:0000269|PubMed:21887730}. Note=Localizes to the tips of cortical microtubules of the mitotic spindle during cell division, and is further released upon microtubule depolymerization (PubMed:15827085). Recruited into membrane ruffles induced by S.flexneri at tight junctions of polarized epithelial cells (PubMed:19043560). Colocalized with NOD2 and RIPK2 in vesicles and with the cytoskeleton (PubMed:21887730). {ECO:0000269|PubMed:15827085, ECO:0000269|PubMed:19043560, ECO:0000269|PubMed:21887730}.
uniprot
proteins