ARHGAP35
entrez
2909
canonical
uniprot
Q9NRY4
canonical
ensembl
ENSG00000160007
resolver
ensp
ENSP00000500409
resolver
ensp
ENSP00000532358
resolver
enst
ENST00000672722
resolver
enst
ENST00000862299
resolver
genesymbol
ARHGAP35
resolver
genesymbol_syn
GRF1
resolver
genesymbol_syn
GRLF1
resolver
genesymbol_syn
KIAA1722
resolver
genesymbol_syn
P190A
resolver
genesymbol_syn
p190ARHOGAP
resolver
hgnc
HGNC:4591
resolver
uniprot
A7E2A4
resolver
uniprot
Q14452
resolver
uniprot
Q9C0E1
resolver
uniprot_entry
RHG35_HUMAN
resolver
uniprot_sec
A7E2A4
resolver
uniprot_sec
Q14452
resolver
uniprot_sec
Q9C0E1
resolver
activity_regulation
ACTIVITY REGULATION: Binding of acidic phospholipids inhibits the Rho GAP activity and promotes the Rac GAP activity. {ECO:0000269|PubMed:19673492}.
uniprot
proteins
amino_acid_sequence
MMMARKQDVRIPTYNISVVGLSGTEKEKGQCGIGKSCLCNRFVRPSADEFHLDHTSVLSTSDFGGRVVNNDHFLYWGEVSRSLEDCVECKMHIVEQTEFIDDQTFQPHRSTALQPYIKRAAATKLASAEKLMYFCTDQLGLEQDFEQKQMPDGKLLVDGFLLGIDVSRGMNRNFDDQLKFVSNLYNQLAKTKKPIVVVLTKCDEGVERYIRDAHTFALSKKNLQVVETSARSNVNVDLAFSTLVQLIDKSRGKTKIIPYFEALKQQSQQIATAKDKYEWLVSRIVKNHNENWLSVSRKMQASPEYQDYVYLEGTQKAKKLFLQHIHRLKHEHIERRRKLYLAALPLAFEALIPNLDEIDHLSCIKAKKLLETKPEFLKWFVVLEETPWDATSHIDNMENERIPFDLMDTVPAEQLYEAHLEKLRNERKRVEMRRAFKENLETSPFITPGKPWEEARSFIMNEDFYQWLEESVYMDIYGKHQKQIIDKAKEEFQELLLEYSELFYELELDAKPSKEKMGVIQDVLGEEQRFKALQKLQAERDALILKHIHFVYHPTKETCPSCPACVDAKIEHLISSRFIRPSDRNQKNSLSDPNIDRINLVILGKDGLARELANEIRALCTNDDKYVIDGKMYELSLRPIEGNVRLPVNSFQTPTFQPHGCLCLYNSKESLSYVVESIEKSRESTLGRRDNHLVHLPLTLILVNKRGDTSGETLHSLIQQGQQIASKLQCVFLDPASAGIGYGRNINEKQISQVLKGLLDSKRNLNLVSSTASIKDLADVDLRIVMCLMCGDPFSADDILFPVLQSQTCKSSHCGSNNSVLLELPIGLHKKRIELSVLSYHSSFSIRKSRLVHGYIVFYSAKRKASLAMLRAFLCEVQDIIPIQLVALTDGAVDVLDNDLSREQLTEGEEIAQEIDGRFTSIPCSQPQHKLEIFHPFFKDVVEKKNIIEATHMYDNAAEACSTTEEVFNSPRAGSPLCNSNLQDSEEDIEPSYSLFREDTSLPSLSKDHSKLSMELEGNDGLSFIMSNFESKLNNKVPPPVKPKPPVHFEITKGDLSYLDQGHRDGQRKSVSSSPWLPQDGFDPSDYAEPMDAVVKPRNEEENIYSVPHDSTQGKIITIRNINKAQSNGSGNGSDSEMDTSSLERGRKVSIVSKPVLYRTRCTRLGRFASYRTSFSVGSDDELGPIRKKEEDQASQGYKGDNAVIPYETDEDPRRRNILRSLRRNTKKPKPKPRPSITKATWESNYFGVPLTTVVTPEKPIPIFIERCIEYIEATGLSTEGIYRVSGNKSEMESLQRQFDQDHNLDLAEKDFTVNTVAGAMKSFFSELPDPLVPYNMQIDLVEAHKINDREQKLHALKEVLKKFPKENHEVFKYVISHLNKVSHNNKVNLMTSENLSICFWPTLMRPDFSTMDALTATRTYQTIIELFIQQCPFFFYNRPITEPPGARPSSPSAVASTVPFLTSTPVTSQPSPPQSPPPTPQSPMQPLLPSQLQAEHTL
uniprot
proteins
function
FUNCTION: Rho GTPase-activating protein (GAP) (PubMed:19673492, PubMed:28894085). Binds several acidic phospholipids which inhibits the Rho GAP activity to promote the Rac GAP activity (PubMed:19673492). This binding is inhibited by phosphorylation by PRKCA (PubMed:19673492). Involved in cell differentiation as well as cell adhesion and migration, plays an important role in retinal tissue morphogenesis, neural tube fusion, midline fusion of the cerebral hemispheres and mammary gland branching morphogenesis (By similarity). Transduces signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP) (By similarity). Transduces SRC-dependent signals from cell-surface adhesion molecules, such as laminin, to promote neurite outgrowth. Regulates axon outgrowth, guidance and fasciculation (By similarity). Modulates Rho GTPase-dependent F-actin polymerization, organization and assembly, is involved in polarized cell migration and in the positive regulation of ciliogenesis and cilia elongation (By similarity). During mammary gland development, is required in both the epithelial and stromal compartments for ductal outgrowth (By similarity). Represses transcription of the glucocorticoid receptor by binding to the cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'; this function is however unclear and would need additional experimental evidence (PubMed:1894621). {ECO:0000250|UniProtKB:P81128, ECO:0000250|UniProtKB:Q91YM2, ECO:0000269|PubMed:1894621, ECO:0000269|PubMed:19673492, ECO:0000269|PubMed:28894085}.
uniprot
proteins
mass_dalton
170514
uniprot
proteins
mutagenesis
MUTAGEN 1221; /note="S->A: No effect on total phosphorylation levels. Abolishes inhibition of phospholipid binding by PRKCA phosphorylation. Decreases phosphorylation by PRKCA; when associated with A-1226. Abolishes phosphorylation by PRKCA; when associated with A-1126 and A-1236."; /evidence="ECO:0000269|PubMed:19673492"; MUTAGEN 1221; /note="S->D: Enhances Rac GAP activity."; /evidence="ECO:0000269|PubMed:19673492"; MUTAGEN 1226; /note="T->A: No effect on total phosphorylation levels. Abolishes inhibition of phospholipid binding by PRKCA phosphorylation. Decreases phosphorylation by PRKCA; when associated with A-1221. Abolishes phosphorylation by PRKCA; when associated with A-1121 and A-1236."; /evidence="ECO:0000269|PubMed:19673492"; MUTAGEN 1226; /note="T->D: Enhances Rac GAP activity."; /evidence="ECO:0000269|PubMed:19673492"; MUTAGEN 1236; /note="S->A: No effect on total phosphorylation levels. No effect on inhibition of phospholipid binding by PRKCA phosphorylation. Abolishes phosphorylation by PRKCA; when associated with A-1121 and A-1226."; /evidence="ECO:0000269|PubMed:19673492
uniprot
proteins
post_translational_modification
PTM: Phosphorylation of Tyr-1105 by PTK6 promotes the association with RASA1, inactivating RHOA while activating RAS. Phosphorylation at Tyr-308 by PDGFRA inhibits binding to GTF2I (PubMed:18829532, PubMed:19393245). Phosphorylated by PRKCA at Ser-1221 and Thr-1226, induces relocalization from the cytoplasm to regions of plasma membrane ruffling and prevents the binding and substrate specificity regulation by phospholipids (PubMed:19673492). In brain, phosphorylated by FYN and SRC (By similarity). During focal adhesion formation, phosphorylated by MAPK1 and MAPK3 at the C-terminal region, probably at Ser-1451, Ser-1476, Thr-1480 and Ser-1483. Phosphorylation by MAPK1 and MAPK3 inhibits GAP function and localizes ARGHAP35 away from newly forming focal adhesions and stress fibers in cells spreading on fibronectin (By similarity). Phosphorylation at Ser-1476 and Thr-1480 by GSK3B requires priming by MAPK and inhibits RhoGAP activity and modulates polarized cell migration (By similarity). {ECO:0000250|UniProtKB:P81128, ECO:0000250|UniProtKB:Q91YM2, ECO:0000269|PubMed:18829532, ECO:0000269|PubMed:19393245, ECO:0000269|PubMed:19673492}.
uniprot
proteins
pubmed
11054565
uniprot
proteins
pubmed
11214970
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18829532
uniprot
proteins
pubmed
1894621
uniprot
proteins
pubmed
19393245
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19673492
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20675588
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
28894085
uniprot
proteins
sequence_length
1499
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q91YM2}. Cytoplasm {ECO:0000250|UniProtKB:Q91YM2}. Nucleus {ECO:0000305|PubMed:1894621}. Cell membrane {ECO:0000250|UniProtKB:Q91YM2}. Note=In response to integrins and SDC4 and upon phosphorylation by PKC, relocalizes from the cytoplasm to regions of plasma membrane ruffling where it colocalizes with polymerized actin. {ECO:0000250|UniProtKB:Q91YM2}.
uniprot
proteins