Arhgap35
entrez
306400
canonical
uniprot
P81128
canonical
ensembl
ENSRNOG00000015852
resolver
ensembl
ENSRNOG00055017051
resolver
ensembl
ENSRNOG00060021410
resolver
ensembl
ENSRNOG00065031476
resolver
ensp
ENSRNOP00000075649
resolver
ensp
ENSRNOP00055023301
resolver
ensp
ENSRNOP00060030580
resolver
ensp
ENSRNOP00065044625
resolver
enst
ENSRNOT00000090519
resolver
enst
ENSRNOT00055028949
resolver
enst
ENSRNOT00060037074
resolver
enst
ENSRNOT00065054241
resolver
genesymbol
Arhgap35
resolver
genesymbol_syn
Grlf1
resolver
genesymbol_syn
P190A
resolver
genesymbol_syn
p190ARHOGAP
resolver
uniprot
A0A0G2KB46
resolver
uniprot_entry
RHG35_RAT
resolver
uniprot_sec
A0A0G2KB46
resolver
amino_acid_sequence
MMMARKQDVRIPTYNISVVGLSGTEKEKGQCGIGKSCLCNRFVRPSADEFHLDHTSVLSTSDFGGRVVNNDHFLYWGEVSRSLEDCVECKMHIVEQTEFIDDQTFQPHRSTALQPYIKRAAATKLASAEKLMYFCTDQLGLEQDFEQKQMPDGKLLVDGFLLGIDVSRGMNRNFDDQLKFVSNLYNQLAKTKKPIVIVLTKCDEGVERYIRDAHTFALSKKNLQVVETSARSNVNVDLAFSTLVQLIDKSRGKTKIIPYFEALKQQSQQIATAKDKYEWLVSRIVKSHNENWLSVSRKMQASPEYQDYVYLEGTQKAKKLFLQHIHRLKHEHIERRRKLYLAALPLAFEALIPNLDEVDHLSCIKAKKLLETKPEFLKWFVVLEETPWDETSHIDNMENERIPFDLMDTVPAEQLYETHLEKLRNERKRAEMRRAFKENLETSPFITPGKPWEEARSFIMNEDFYQWLEESVYMDIYGKHQKQIIDRAKEEFQELLLEYSELFYELELDAKPSKEKMGVIQDVLGEEQRFKALQKLQAERDALILKHIHFVYHPTKETCPSCPACVDAKIEHLISSRFIRPSDRNQKNSLSDPNIDRINLVILGKDGLARELANEIRALCTNDDKYVIDGKMYELSLRPIEGNVRLPVNSFQTPTFQPHGCLCLYNSKESLSYVVESIEKSRESTLGRRDNHLVHLPLTLILVNKRGDTSGETLHSLIQQGQQIASKLQCVFLDPASAGIGYGRNINEKQISQVLKGLLDSKRNLNLVSSTASIKDLADVDLRIVMCLMCGDPFSADDILSPVLQSQTCKSSHCGSSNSVLLELPIGVHKKRIELSVLSYHSSFSIRKSRLVHGYIVFYSAKRKASLAMLRAFLCEVQDIIPIQLVALTDGAIDVLDNDLSREQLTEGEEIAQEIDGRFTSIPCSQPQHKLELFHPFFKDVVEKKNIIEATHMYDNVAEACSTTEEVFNSPRAGSPLCNSNLQDSEEDVEPPSYHLFREDATLPSLSKDHSKFSMELEGNDGLSFIMSNFESKLNNKVPPPVKPKPPVHFEITKDLSYLDQGHREGQRKSMSSSPWMPQDGFDPSDYAEPMDAVVKPRNEEENIYSVPHDSTQGKIITIRNINKAQSNGSGNGSDSEMDTSSLERGRKVSAVSKPVLYRTRCTRLGRFASYRTSFSVGSDDELGPIRKKEEDQASQGYKGDNAVIPYETDEDPRRRNILRSLRRNTKKPKPKPRPSITKATWESNYFGVPLTTVVTPEKPIPIFIERCIEYIEATGLSTEGIYRVSGNKSEMESLQRQFDQDHNLDLAEKDFTVNTVAGAMKSFFSELPDPLVPYSMQIDLVEAHKINDREQKLHALKEVLKKFPKENHEVFKYVISHLNRVSHNNKVNLMTSENLSICFWPTLMRPDFSSMDALTATRSYQTIIELFIQQCPFFFYNRPISEPPGAAPGSPSAMAPTVPFLTSTPATSQPSPPQSPPPTPQSPMQPLLSSQLQAEHTL
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:20439493, PubMed:9852136). 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:20439493, PubMed:9852136). 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 (By similarity). {ECO:0000250|UniProtKB:Q91YM2, ECO:0000250|UniProtKB:Q9NRY4, ECO:0000269|PubMed:20439493, ECO:0000269|PubMed:9852136}.
uniprot
proteins
mass_dalton
170480
uniprot
proteins
mutagenesis
MUTAGEN 36; /note="S->N: Disrupts GTP-binding. No direct effect on GAP activity 'in vitro' but affects the activity regulation 'in vivo'."; /evidence="ECO:0000269|PubMed:9852136"; MUTAGEN 1284; /note="R->A: Abolishes GAP activity."; /evidence="ECO:0000269|PubMed:9852136"; MUTAGEN 1451; /note="S->A: Abolishes phosphorylation by MAPK, increases functional activity and enhances retention in peripheral membranes; when associated with 1476-A--A-1483."; /evidence="ECO:0000269|PubMed:20439493"; MUTAGEN 1476..1483; /note="SPPPTPQS->APPPAPQA: Abolishes phosphorylation by MAPK, increases functional activity and enhances retention in peripheral membranes; when associated with A-1451."; /evidence="ECO:0000269|PubMed:20439493
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 (By similarity). 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 (PubMed:20439493). 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:Q91YM2, ECO:0000250|UniProtKB:Q9NRY4, ECO:0000269|PubMed:20439493}.
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
1581965
uniprot
proteins
pubmed
20439493
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
9852136
uniprot
proteins
sequence_length
1499
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q91YM2}. Cytoplasm {ECO:0000269|PubMed:1581965}. Nucleus {ECO:0000269|PubMed:1581965}. 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