Arhgap35
entrez
232906
canonical
uniprot
Q91YM2
canonical
ensembl
ENSMUSG00000058230
resolver
ensp
ENSMUSP00000075242
resolver
ensp
ENSMUSP00000243876
resolver
ensp
ENSMUSP00000243877
resolver
enst
ENSMUST00000075845
resolver
genesymbol
Arhgap35
resolver
genesymbol_syn
Grlf1
resolver
genesymbol_syn
Kiaa1722
resolver
genesymbol_syn
P190A
resolver
genesymbol_syn
p190ARHOGAP
resolver
uniprot
B2RTN5
resolver
uniprot
Q3UGY1
resolver
uniprot
Q3UVZ8
resolver
uniprot
Q69ZC4
resolver
uniprot
Q8CCL8
resolver
uniprot_entry
B2RTN5_MOUSE
resolver
uniprot_entry
Q3UVZ8_MOUSE
resolver
uniprot_entry
Q8CCL8_MOUSE
resolver
uniprot_entry
RHG35_MOUSE
resolver
uniprot_sec
Q3UGY1
resolver
uniprot_sec
Q69ZC4
resolver
amino_acid_sequence
MMMARKQDVRIPTYNISVVGLSGTEKEKGQCGIGKSCLCNRFVRPSADEFHLDHTSVLSTSDFGGRVVNNDHFLYWGEVSRSLEDCVECKMHIVEQTEFIDDQTFQPHRSTALQPYIKRAAATKLASAEKLMYFCTDQLGLEQDFEQKQMPDGKLLVDGFLLGIDVSRGMNRNFDDQLKFVSNLYNQLAKTKKPIVVVLTKCDEGVERYIRDAHTFALSKKNLQVVETSARSNVNVDLAFSTLVQLIDKSRGKTKIIPYFEALKQQSQQIATAKDKYEWLVSRIVKNHNENWPSVSRKMQASPEYQDYVYLEGTQKAKKLFLQHIHRLKHEHIERRRKLYLAALPLAFEALIPNLDEVDHLSCIKAKKLLETKPEFLKWFVVLEETPWDATSHIDNMENERIPFDLMDTVPAEQLYETHLEKLRNERKRAEMRRAFKENLETSPFITPGKPWEEARSFIMNEDFYQWLEESVYMDIYGKHQKQIIDRAKEEFQELLLEYSELFYELELDAKPSKEKMGVIQDVLGEEQRFKALQKLQAERDALILKHIHFVYHPTKETCPSCPACVDAKIEHLISSRFIRPSDRNQKNSLSDLNIDRINLVILGKDGLARELANEIRALCTNDDKYVIDGKMYELSLRPIEGNVRLPVNSFQTPTFQPHGCLCLYNSKESLSYVVESIEKSRESTLGRRDNHLVHLPLTLILVNKRGDTSGETLHSLIQQGQQIASKLQCVFLDPASAGIGYGRNINEKQISQVLKGLLDSKRNLNLVSSTASIKDLADVDLRIVMCLMCGDPFSADDVLSPVLQSQTCKSSHCGSSNSVLLELPIGLHKKRIELSVLSYHSSFSIRKSRLVHGYIVFYSAKRKASLAMLRAFLCEVQDIIPIQLVALTDGAIDVLDNDLSREQLTEGEEIAQEIDGRFTSIPCSQPQHKLELFHPFFKDVVEKKNIIEATHMYDNVAEACSTTEEVFNSPRAGSPLCNSNLQDSEEDVEPPSYHLFREDATLPSLSKDHSKFSMELEGNDGLSFIMSNFESKLNNKVPPPVKPKPPVHFDITKDLSYLDQGHREGQRKSMSSSPWMPQDGFDPSDYAEPMDAVVKPRNEEENIYSVPHDSTQGKIITIRNINKAQSNGSGNGSDSEMDTSSLERGRKVSAVSKPVLYRTRCTRLGRFASYRTSFSVGSDDELGPIRKKEEDQASQGYKGDNAVIPYETDEDPRRRNILRSLRRNTKKPKPKPRPSITKATWESNYFGVPLTTVVTPEKPIPIFIERCIEYIEATGLSTEGIYRVSGNKSEMESLQRQFDQDHNLDLAEKDFTVNTVAGAMKSFFSELPDPLVPYSMQIDLVEAHKINDREQKLHALKEVLKKFPKENHEVFKYVISHLNKVSHNNKVNLMTSENLSICFWPTLMRPDFSSMDALTATRSYQTIIELFIQQCPFFFYNRPISEPPGAAPGSPSAMAPTVPFLTSTPATSQPSPPQSPPPTPQSPMQPLLSSQLQAEHTL
uniprot
proteins
function
FUNCTION: Rho GTPase-activating protein (GAP). Binds several acidic phospholipids which inhibits the Rho GAP activity to promote the Rac GAP activity (PubMed:16971514). This binding is inhibited by phosphorylation by PRKCA (By similarity). 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 (PubMed:11044403, PubMed:11283609, PubMed:18502760, PubMed:21945077). Transduces signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP) (PubMed:16971514). Transduces SRC-dependent signals from cell-surface adhesion molecules, such as laminin, to promote neurite outgrowth. Regulates axon outgrowth, guidance and fasciculation (PubMed:11283609). 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 (PubMed:11044403, PubMed:18502760, PubMed:26859289). During mammary gland development, is required in both the epithelial and stromal compartments for ductal outgrowth (PubMed:21945077). 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 (By similarity). {ECO:0000250|UniProtKB:Q9NRY4, ECO:0000269|PubMed:11044403, ECO:0000269|PubMed:11283609, ECO:0000269|PubMed:16971514, ECO:0000269|PubMed:18502760, ECO:0000269|PubMed:21945077, ECO:0000269|PubMed:26859289}.
uniprot
proteins
mass_dalton
170393
uniprot
proteins
mutagenesis
MUTAGEN 1396; /note="L->Q: In ENU mutant Arhgap35-D34; mutant animals show hypodysplastic kidneys and neural tube closure defects; the number of ciliated cells and cilia average length are drastically reduced in the proximal tubules. Results in loss of activation of GTP hydrolysis."; /evidence="ECO:0000269|PubMed:26859289"; MUTAGEN 1472; /note="S->A: Reduces phosphorylation by GSK3B by 50%. No effect on polarized cell migration."; /evidence="ECO:0000269|PubMed:18502760"; MUTAGEN 1476; /note="S->A: Abolishes phosphorylation by GSK3B. Reduces phosphorylation by MAPK. Affects polarized cell migration. Increases RhoGAP catalytic activity."; /evidence="ECO:0000269|PubMed:18502760"; MUTAGEN 1480; /note="T->A: Abolishes phosphorylation by GSK3B. Reduces phosphorylation by MAPK. Affects polarized cell migration. Increases RhoGAP catalytic activity."; /evidence="ECO:0000269|PubMed:18502760"; MUTAGEN 1483; /note="S->A: Abolishes phosphorylation by GSK3B. Reduces phosphorylation by MAPK. No effect on polarized cell migration."; /evidence="ECO:0000269|PubMed:18502760
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 (By similarity). 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:11044403). In brain, phosphorylated by FYN and SRC (PubMed:11283609). 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 (PubMed:18502760). {ECO:0000250|UniProtKB:P81128, ECO:0000250|UniProtKB:Q9NRY4, ECO:0000269|PubMed:11044403, ECO:0000269|PubMed:11283609, ECO:0000269|PubMed:18502760}.
uniprot
proteins
pubmed
11044403
uniprot
proteins
pubmed
11283609
uniprot
proteins
pubmed
15368895
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16452087
uniprot
proteins
pubmed
16971514
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
17947660
uniprot
proteins
pubmed
18034455
uniprot
proteins
pubmed
18502760
uniprot
proteins
pubmed
20675588
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21945077
uniprot
proteins
pubmed
26859289
uniprot
proteins
sequence_length
1499
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:26859289}. Cytoplasm {ECO:0000269|PubMed:11044403}. Nucleus {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:11044403}. 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:0000269|PubMed:11044403}.
uniprot
proteins