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Rho GTPase-activating protein 35 (Glucocorticoid receptor DNA-binding factor 1) (Rho GAP p190A) (p190-A)

 RHG35_CANLF             Reviewed;        1500 AA.
P83509;
04-APR-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
02-JUN-2021, entry version 142.
RecName: Full=Rho GTPase-activating protein 35 {ECO:0000250|UniProtKB:Q9NRY4};
AltName: Full=Glucocorticoid receptor DNA-binding factor 1 {ECO:0000303|PubMed:12234678};
AltName: Full=Rho GAP p190A;
Short=p190-A;
Name=ARHGAP35 {ECO:0000250|UniProtKB:Q9NRY4};
Synonyms=GRLF1 {ECO:0000250|UniProtKB:Q9NRY4},
P190A {ECO:0000250|UniProtKB:Q9NRY4},
p190ARHOGAP {ECO:0000250|UniProtKB:Q9NRY4};
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
NCBI_TaxID=9615 {ECO:0000312|EMBL:AAN16354.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
TISSUE=Retina;
PubMed=12234678; DOI=10.1016/s0378-1119(02)00765-5;
Zangerl B., Zhang Q., Pearce-Kelling S.E., Aguirre G.D.;
"Molecular cloning, characterization and mapping of the canine
glucocorticoid receptor DNA binding factor 1 (GRLF1).";
Gene 294:167-176(2002).
-!- FUNCTION: Rho GTPase-activating protein (GAP). Binds several acidic
phospholipids which inhibits the Rho GAP activity to promote the Rac
GAP activity. 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 (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 evidences (By
similarity). {ECO:0000250|UniProtKB:P81128,
ECO:0000250|UniProtKB:Q91YM2, ECO:0000250|UniProtKB:Q9NRY4}.
-!- SUBUNIT: Interacts with RASA1 (By similarity). Interacts with the
general transcription factor GTF2I, the interaction sequesters GTF2I in
the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q91YM2,
ECO:0000250|UniProtKB:Q9NRY4}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
{ECO:0000250|UniProtKB:Q91YM2}. Cytoplasm
{ECO:0000250|UniProtKB:Q91YM2}. Nucleus {ECO:0000250|UniProtKB:Q91YM2}.
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}.
-!- TISSUE SPECIFICITY: Strongly expressed in retina (photoreceptor layer)
and brain. Expression is maximal in the occipital, frontal, temporal
lobe and also the cerebellum. Medium expression in the medulla and also
in kidney, lung, liver, heart and spleen.
{ECO:0000269|PubMed:12234678}.
-!- DOMAIN: N-terminal part (1-266) has GTPase activity. Required for
proper cellular localization. {ECO:0000250|UniProtKB:Q91YM2}.
-!- DOMAIN: The pG1 pseudoGTPase domain does not bind GTP.
{ECO:0000250|UniProtKB:Q6NU25}.
-!- PTM: Phosphorylation of Tyr-1106 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-1222 and Thr-1227, induces relocalization from the
cytoplasm to regions of plasma membrane ruffling and prevents the
binding and substrate specificity regulation by phospholipids. 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-1452, Ser-1477, Thr-1481 and Ser-1484.
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-
1477 and Thr-1481 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:0000250|UniProtKB:Q9NRY4}.
---------------------------------------------------------------------------
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EMBL; AF483595; AAN16354.1; -; mRNA.
EMBL; AY079157; AAL91068.1; -; Genomic_DNA.
EMBL; AY079158; AAL91069.1; -; Genomic_DNA.
RefSeq; NP_001003022.1; NM_001003022.1.
BMRB; P83509; -.
SMR; P83509; -.
STRING; 9612.ENSCAFP00000036971; -.
PaxDb; P83509; -.
Ensembl; ENSCAFT00000006727; ENSCAFP00000006228; ENSCAFG00000004190.
Ensembl; ENSCAFT00030013717; ENSCAFP00030011972; ENSCAFG00030007402.
Ensembl; ENSCAFT00040004921; ENSCAFP00040004225; ENSCAFG00040002575.
GeneID; 403543; -.
KEGG; cfa:403543; -.
CTD; 2909; -.
VGNC; VGNC:38060; ARHGAP35.
eggNOG; KOG4271; Eukaryota.
GeneTree; ENSGT01030000234635; -.
HOGENOM; CLU_004268_0_0_1; -.
InParanoid; P83509; -.
OMA; WAPGSDG; -.
OrthoDB; 110157at2759; -.
Reactome; R-CFA-194840; Rho GTPase cycle.
Reactome; R-CFA-416550; Sema4D mediated inhibition of cell attachment and migration.
Reactome; R-CFA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
Proteomes; UP000002254; Chromosome 1.
Bgee; ENSCAFG00000004190; Expressed in prefrontal cortex and 54 other tissues.
GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
GO; GO:0007413; P:axonal fasciculation; ISS:UniProtKB.
GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0031668; P:cellular response to extracellular stimulus; ISS:UniProtKB.
GO; GO:0021955; P:central nervous system neuron axonogenesis; ISS:UniProtKB.
GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; ISS:UniProtKB.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0030879; P:mammary gland development; ISS:UniProtKB.
GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Ensembl.
GO; GO:0043116; P:negative regulation of vascular permeability; IEA:Ensembl.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0097485; P:neuron projection guidance; ISS:UniProtKB.
GO; GO:0045724; P:positive regulation of cilium assembly; ISS:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
GO; GO:0008064; P:regulation of actin polymerization or depolymerization; ISS:UniProtKB.
GO; GO:0050770; P:regulation of axonogenesis; ISS:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
GO; GO:0042478; P:regulation of eye photoreceptor cell development; NAS:UniProtKB.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
GO; GO:0044319; P:wound healing, spreading of cells; ISS:UniProtKB.
Gene3D; 1.10.10.440; -; 2.
Gene3D; 1.10.555.10; -; 1.
InterPro; IPR002713; FF_domain.
InterPro; IPR036517; FF_domain_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR039007; pG1.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR032835; RhoGAP-FF1.
InterPro; IPR000198; RhoGAP_dom.
InterPro; IPR039006; RhoGAP_pG2.
InterPro; IPR001806; Small_GTPase.
Pfam; PF01846; FF; 1.
Pfam; PF00071; Ras; 1.
Pfam; PF00620; RhoGAP; 1.
Pfam; PF16512; RhoGAP-FF1; 1.
SMART; SM00441; FF; 4.
SMART; SM00324; RhoGAP; 1.
SUPFAM; SSF48350; SSF48350; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF81698; SSF81698; 1.
PROSITE; PS51676; FF; 4.
PROSITE; PS51852; PG1; 1.
PROSITE; PS51853; PG2; 1.
PROSITE; PS50238; RHOGAP; 1.
2: Evidence at transcript level;
Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; DNA-binding;
GTP-binding; GTPase activation; Lipid-binding; Membrane;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Repressor; Transcription; Transcription regulation.
CHAIN 1..1500
/note="Rho GTPase-activating protein 35"
/id="PRO_0000056729"
DOMAIN 270..327
/note="FF 1"
/evidence="ECO:0000305"
DOMAIN 368..422
/note="FF 2"
DOMAIN 429..483
/note="FF 3"
/evidence="ECO:0000305"
DOMAIN 485..550
/note="FF 4"
DOMAIN 592..767
/note="pG1 pseudoGTPase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01199"
DOMAIN 783..947
/note="pG2 pseudoGTPase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01200"
DOMAIN 1250..1437
/note="Rho-GAP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
NP_BIND 33..37
/note="GTP"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
NP_BIND 95..97
/note="GTP"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
NP_BIND 201..203
/note="GTP"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
NP_BIND 229..231
/note="GTP"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
REGION 1..266
/note="Has GTPase activity, required for proper
localization"
/evidence="ECO:0000250|UniProtKB:Q91YM2"
REGION 970..989
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1058..1090
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1125..1147
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1178..1208
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1214..1237
/note="Required for phospholipid binding and regulation of
the substrate preference"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
REGION 1444..1500
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 970..988
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1125..1140
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1183..1197
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1449..1470
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1471..1486
/note="Pro residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
BINDING 28
/note="GTP"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
BINDING 52
/note="GTP; via carbonyl oxygen"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
BINDING 56
/note="GTP"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
MOD_RES 308
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
MOD_RES 589
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
MOD_RES 770
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
MOD_RES 773
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
MOD_RES 970
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
MOD_RES 975
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
MOD_RES 985
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q91YM2"
MOD_RES 1002
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
MOD_RES 1073
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
MOD_RES 1088
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
MOD_RES 1106
/note="Phosphotyrosine; by ABL2 and PTK6"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
MOD_RES 1135
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
MOD_RES 1143
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q91YM2"
MOD_RES 1151
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
MOD_RES 1177
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
MOD_RES 1180
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
MOD_RES 1222
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
MOD_RES 1227
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
MOD_RES 1237
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9NRY4"
MOD_RES 1473
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q91YM2"
MOD_RES 1477
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q91YM2"
MOD_RES 1481
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q91YM2"
MOD_RES 1484
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q91YM2"
SEQUENCE 1500 AA; 170428 MW; EB3AB65FE36E2F18 CRC64;
MMMARKQDVR IPTYNISVVG LSGTEKEKGQ CGIGKSCLCN RFVRPSADEF HLDHTSVLST
SDFGGRVVNN DHFLYWGEVS RSLEDCVECK MHIVEQTEFI DDQTFQPHRS TALQPYIKRA
AATKLASAEK LMYFCTDQLG LEQDFEQKQM PDGKLLIDGF LLGIDVSRGM NRNFDDQLKF
VSNLYNQLAK TKKPIVVVLT KCDEGVERYI RDAHTFALSK KNLQVVETSA RSNVNVDLAF
STLVQLIDKS RGKTKIIPYF EALKQQSQQI ATAKDKYEWL VSRIVKNHNE NWLSVSRKMQ
ASPEYQDYVY LEGTQKAKKL FLQHIHRLKH EHIERRRKLY LAALPLAFEA LIPNLDEIDH
LSCIKTKKLL ETKPEFLKWF VVLEETPWDA TSHIDNMENE RIPFDLMDTV PAEQLYEAHL
EKLRNERKRA EMRRAFKENL ETSPFITPGK PWEEARSFIM NEDFYQWLEE SVYMDIYGKH
QKQIIDKAKE EFQELLLEYS ELFYELELDA KPSKEKMGVI QDVLGEEQRF KALQKLQAER
DALILKHIHF VYHPTKETCP SCPACVDAKI EHLISSRFIR PSDRNQKNSL SDPNIDRINL
VILGKDGLAR ELANEIRALC TNDDKYVIDG KMYELSLRPI EGNVRLPVNS FQTPTFQPHG
CLCLYNSKES LSYVVESIEK SRESTLGRRD NHLVHLPLTL ILVNKRGDTS GETLHSLIQQ
GQQIASKLQC VFLDPASAGI GYGRNINEKQ ISQVLKGLLD SKRNLNLVSS TASIKDLADV
DLRIVMCLMC GDPFSADDIL FPVLQSQTCK SSHCGSNNSV LLELPIGLHK KRIELSILSY
HSSFSIRKSR LVHGYIVFYS AKRKASLAML RAFLCEVQDI IPIQLVALTD GAIDVLDNDL
SREQLSEGEE IAQEIDGRFT SIPCSQPQHK LEIFHPFFKD VVDKKNIIEA THMYDNAAEA
CSTTEEVFNS PRAGSPLCNS NLQDSEEDIE PPSYSLFRED TSLPSLSKDH SKLSMELEGN
DGLSFIMSNF ESKLNNKVPP PVKPKPPVQF DITKGDLSYL DQGHRDGQRK SVSSSTWLPP
DGFDPSDYAE PMDAVVKPRN EEENIYSVPH DSTQGKIITI RNINKAQSNG SGNGSDSEMD
TSSLERGRKV SIVSKPVLYR TRCSRLGRFA SYRTSFSVGS DDELGPIRKK EEDQASQGYK
GDNAVIPYET DEDPRRRNIL RSLRRNTKKP KPKPRPSITK ATWESNYFGV PLTTVVTPEK
PIPVFIERCI EYIEATGLST EGIYRVSGNK SEMESLQRQF DQDHNLDLAE KDFTVNTVAG
AMKSFFSELP DPLVPYNMQI DLVEAHKIND REQKLHALKE VLKKFPKENH EVFKYVISHL
NKVSHNNKVN LMTSENLSIC FWPTLMRPDF STMDALTATR TYQTIIELFI QQCPFFFHNR
PISEPPGATP SSPSAVASTV PFLTSTPVTS QPSPPQSPPP TPQSPMQALL PSQLQAEHTL


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WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1531: Vitamin D synthesis
WP1616: ABC transporters
WP590: Cardiovascular Signaling
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP731: Sterol regulatory element binding protein related
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP1869: Neuroransmitter Receptor Binding And Downstream Transmission In The Postsynaptic Cell
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP1963: The effect of Glucocorticoids on target gene expression
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP2272: Pathogenic Escherichia coli infection
WP1183: Toll-like receptor signaling pathway
WP1659: Glycine, serine and threonine metabolism
WP1967: Glucocorticoid action and resistance
WP35: G Protein Signaling Pathways
WP894: T Cell Receptor Signaling Pathway

Related Genes :
[ARHGAP35 GRF1 GRLF1 KIAA1722 P190A p190ARHOGAP] Rho GTPase-activating protein 35 (Glucocorticoid receptor DNA-binding factor 1) (Glucocorticoid receptor repression factor 1) (GRF-1) (Rho GAP p190A) (p190-A)
[Arhgap35 Grlf1 P190A p190ARHOGAP] Rho GTPase-activating protein 35 (GAP-associated protein p190) (Glucocorticoid receptor DNA-binding factor 1)
[Arhgap35 Grlf1 Kiaa1722 P190A p190ARHOGAP] Rho GTPase-activating protein 35 (Glucocorticoid receptor DNA-binding factor 1)
[ARHGAP35 GRLF1 P190A p190ARHOGAP] Rho GTPase-activating protein 35 (Glucocorticoid receptor DNA-binding factor 1) (Rho GAP p190A) (p190-A)
[Arhgap32 Grit Kiaa0712 Rics] Rho GTPase-activating protein 32 (Brain-specific Rho GTPase-activating protein) (GAB-associated Cdc42/Rac GTPase-activating protein) (GC-GAP) (Rho-type GTPase-activating protein 32) (Rho/Cdc42/Rac GTPase-activating protein RICS) (RhoGAP involved in the beta-catenin-N-cadherin and NMDA receptor signaling) (p200RhoGAP) (p250GAP)
[AKAP13 BRX HT31 LBC] A-kinase anchor protein 13 (AKAP-13) (AKAP-Lbc) (Breast cancer nuclear receptor-binding auxiliary protein) (Guanine nucleotide exchange factor Lbc) (Human thyroid-anchoring protein 31) (Lymphoid blast crisis oncogene) (LBC oncogene) (Non-oncogenic Rho GTPase-specific GTP exchange factor) (Protein kinase A-anchoring protein 13) (PRKA13) (p47)
[ARHGAP24 FILGAP] Rho GTPase-activating protein 24 (Filamin-A-associated RhoGAP) (FilGAP) (RAC1- and CDC42-specific GTPase-activating protein of 72 kDa) (RC-GAP72) (Rho-type GTPase-activating protein 24) (RhoGAP of 73 kDa) (Sarcoma antigen NY-SAR-88) (p73RhoGAP)
[ARHGAP17 RICH1 MSTP066 MSTP110] Rho GTPase-activating protein 17 (Rho-type GTPase-activating protein 17) (RhoGAP interacting with CIP4 homologs protein 1) (RICH-1)
[CHN1 ARHGAP2 CHN] N-chimaerin (A-chimaerin) (Alpha-chimerin) (N-chimerin) (NC) (Rho GTPase-activating protein 2)
[ARHGAP21 ARHGAP10 KIAA1424] Rho GTPase-activating protein 21 (Rho GTPase-activating protein 10) (Rho-type GTPase-activating protein 21)
[ARHGAP45 HMHA1 KIAA0223] Rho GTPase-activating protein 45 [Cleaved into: Minor histocompatibility antigen HA-1 (mHag HA-1)]
[RHO1 YPR165W P9325.3] GTP-binding protein RHO1 (Rho-type GTPase 1)
[RGA1 DBM1 THE1 YOR127W O3290 YOR3290W] Rho-type GTPase-activating protein 1
[RASA1 GAP RASA] Ras GTPase-activating protein 1 (GAP) (GTPase-activating protein) (RasGAP) (Ras p21 protein activator) (p120GAP)
[Asap1 Ddef1 Kiaa1249 Shag1] Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)
[ARHGAP31 CDGAP KIAA1204] Rho GTPase-activating protein 31 (Cdc42 GTPase-activating protein)
[Arhgap17] Rho GTPase-activating protein 17 (Neuron-associated developmentally-regulated protein) (Nadrin) (Rho-type GTPase-activating protein 17)
[Arhgap24] Rho GTPase-activating protein 24 (Rho-type GTPase-activating protein 24)
[rga8 SPAC13A11.01c SPAC2F7.18c] Rho-GTPase-activating protein 8
[Syde1] Rho GTPase-activating protein SYDE1 (Synapse defective protein 1 homolog 1) (Protein syd-1 homolog 1)
[G3BP1 G3BP] Ras GTPase-activating protein-binding protein 1 (G3BP-1) (EC 3.6.4.12) (EC 3.6.4.13) (ATP-dependent DNA helicase VIII) (hDH VIII) (GAP SH3 domain-binding protein 1)
[ARHGEF1] Rho guanine nucleotide exchange factor 1 (115 kDa guanine nucleotide exchange factor) (p115-RhoGEF) (p115RhoGEF) (Sub1.5)
[TY1B-OR YORWTy1-2 POL YOR142W-B O3367 YOR3367W] Transposon Ty1-OR Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (RT-RH) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)]
[Arfgap1 Arf1gap] ADP-ribosylation factor GTPase-activating protein 1 (ARF GAP 1) (ADP-ribosylation factor 1 GTPase-activating protein) (ARF1 GAP) (ARF1-directed GTPase-activating protein)
[ARFGAP1 ARF1GAP] ADP-ribosylation factor GTPase-activating protein 1 (ARF GAP 1) (ADP-ribosylation factor 1 GTPase-activating protein) (ARF1 GAP) (ARF1-directed GTPase-activating protein)
[ASAP1 DDEF1 KIAA1249 PAG2] Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)
[CHN2 ARHGAP3 BCH] Beta-chimaerin (Beta-chimerin) (Rho GTPase-activating protein 3)
[rga4 SPBC28E12.03] Probable Rho-type GTPase-activating protein 4
[conu CG17082] Rho GTPase-activating protein conundrum
[Arhgef1 Lbcl2 Lsc] Rho guanine nucleotide exchange factor 1 (Lbc's second cousin) (Lymphoid blast crisis-like 2)

Bibliography :