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

 RHG35_HUMAN             Reviewed;        1499 AA.
Q9NRY4; A7E2A4; Q14452; Q9C0E1;
04-APR-2003, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 3.
02-JUN-2021, entry version 205.
RecName: Full=Rho GTPase-activating protein 35 {ECO:0000312|HGNC:HGNC:4591};
AltName: Full=Glucocorticoid receptor DNA-binding factor 1;
AltName: Full=Glucocorticoid receptor repression factor 1;
Short=GRF-1;
AltName: Full=Rho GAP p190A;
Short=p190-A {ECO:0000303|PubMed:11054565};
Name=ARHGAP35 {ECO:0000312|HGNC:HGNC:4591};
Synonyms=GRF1 {ECO:0000303|PubMed:1894621},
GRLF1 {ECO:0000303|PubMed:1894621}, KIAA1722,
P190A {ECO:0000303|PubMed:19673492},
p190ARHOGAP {ECO:0000303|PubMed:19673492};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606 {ECO:0000312|EMBL:AAF80386.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=11214970; DOI=10.1093/dnares/7.6.347;
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIX. The
complete sequences of 100 new cDNA clones from brain which code for large
proteins in vitro.";
DNA Res. 7:347-355(2000).
[2]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] OF 1-1491.
TISSUE=Mammary cancer;
PubMed=11054565; DOI=10.1016/s0378-1119(00)00387-5;
Tikoo A., Czekay S., Viars C., White S., Heath J.K., Arden K., Maruta H.;
"p190-A, a human tumor suppressor gene, maps to the chromosomal region
19q13.3 that is reportedly deleted in some gliomas.";
Gene 257:23-31(2000).
[6] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] OF 377-1453, AND FUNCTION.
TISSUE=Mammary cancer;
PubMed=1894621;
LeClerc S., Palaniswami R., Xie B.X., Govindan M.V.;
"Molecular cloning and characterization of a factor that binds the human
glucocorticoid receptor gene and represses its expression.";
J. Biol. Chem. 266:17333-17340(1991).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[9]
PHOSPHORYLATION AT TYR-1105.
PubMed=18829532; DOI=10.1158/0008-5472.can-08-0997;
Shen C.H., Chen H.Y., Lin M.S., Li F.Y., Chang C.C., Kuo M.L.,
Settleman J., Chen R.H.;
"Breast tumor kinase phosphorylates p190RhoGAP to regulate rho and ras and
promote breast carcinoma growth, migration, and invasion.";
Cancer Res. 68:7779-7787(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-970 AND SER-1179, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1179, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589; SER-970; SER-975;
SER-1150 AND SER-1179, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
FUNCTION, ACTIVITY REGULATION, PHOSPHORYLATION AT SER-1221; THR-1226 AND
SER-1236, MUTAGENESIS OF SER-1221; THR-1226 AND SER-1236, AND BINDING TO
PHOSPHOLIPIDS.
PubMed=19673492; DOI=10.1021/bi900667y;
Levay M., Settleman J., Ligeti E.;
"Regulation of the substrate preference of p190RhoGAP by protein kinase C-
mediated phosphorylation of a phospholipid binding site.";
Biochemistry 48:8615-8623(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589; SER-773; SER-975;
SER-1072; TYR-1087; TYR-1105; SER-1134 AND SER-1179, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
TISSUE SPECIFICITY.
PubMed=20675588; DOI=10.4049/jimmunol.0904163;
Nemeth T., Futosi K., Hably C., Brouns M.R., Jakob S.M., Kovacs M.,
Kertesz Z., Walzog B., Settleman J., Mocsai A.;
"Neutrophil functions and autoimmune arthritis in the absence of
p190RhoGAP: generation and analysis of a novel null mutation in mice.";
J. Immunol. 185:3064-3075(2010).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589 AND SER-1179, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589; SER-1134; SER-1150 AND
SER-1179, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589; SER-770; SER-773;
SER-1134; SER-1150; SER-1176 AND SER-1179, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589; SER-1001; SER-1150 AND
SER-1179, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
FUNCTION, AND DOMAIN.
PubMed=28894085; DOI=10.1038/s41467-017-00483-x;
Stiegler A.L., Boggon T.J.;
"p190RhoGAP proteins contain pseudoGTPase domains.";
Nat. Commun. 8:506-506(2017).
[23] {ECO:0007744|PDB:3C5H}
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 13-249 IN COMPLEX WITH GTP
ANALOG.
Structural genomics consortium (SGC);
"Crystal structure of the Ras homolog domain of human GRLF1 (p190RhoGAP).";
Submitted (JAN-2008) to the PDB data bank.
[24] {ECO:0007744|PDB:3FK2}
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1212-1439.
Structural genomics consortium (SGC);
"Crystal structure of the RhoGAP domain of human glucocorticoid receptor
DNA-binding factor 1.";
Submitted (DEC-2008) to the PDB data bank.
[25]
STRUCTURE BY NMR OF 267-331, PHOSPHORYLATION AT TYR-308, AND INTERACTION
WITH GTF2I.
PubMed=19393245; DOI=10.1016/j.jmb.2009.04.035;
Bonet R., Ruiz L., Aragon E., Martin-Malpartida P., Macias M.J.;
"NMR structural studies on human p190-A RhoGAPFF1 revealed that domain
phosphorylation by the PDGF-receptor alpha requires its previous
unfolding.";
J. Mol. Biol. 389:230-237(2009).
-!- 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 evidences
(PubMed:1894621). {ECO:0000250|UniProtKB:P81128,
ECO:0000250|UniProtKB:Q91YM2, ECO:0000269|PubMed:1894621,
ECO:0000269|PubMed:19673492, ECO:0000269|PubMed:28894085}.
-!- ACTIVITY REGULATION: Binding of acidic phospholipids inhibits the Rho
GAP activity and promotes the Rac GAP activity.
{ECO:0000269|PubMed:19673492}.
-!- SUBUNIT: Interacts with RASA1 (By similarity). Interacts with the
general transcription factor GTF2I, the interaction sequesters GTF2I in
the cytoplasm (PubMed:19393245). {ECO:0000250|UniProtKB:Q91YM2,
ECO:0000269|PubMed:19393245}.
-!- 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}.
-!- TISSUE SPECIFICITY: Detected in neutrophils (at protein level).
{ECO:0000269|PubMed:1894621}.
-!- 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:0000269|PubMed:28894085}.
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=AAA58618.1; Type=Frameshift; Evidence={ECO:0000305};
Sequence=AAF80386.1; Type=Frameshift; Evidence={ECO:0000305};
Sequence=AAF80386.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
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EMBL; AB051509; BAB21813.2; -; mRNA.
EMBL; CH471126; EAW57450.1; -; Genomic_DNA.
EMBL; BC150257; AAI50258.1; -; mRNA.
EMBL; AF159851; AAF80386.1; ALT_SEQ; mRNA.
EMBL; M73077; AAA58618.1; ALT_FRAME; mRNA.
CCDS; CCDS46127.1; -.
RefSeq; NP_004482.4; NM_004491.4.
RefSeq; XP_016882203.1; XM_017026714.1.
PDB; 2K85; NMR; -; A=267-331.
PDB; 3C5H; X-ray; 1.80 A; A=13-249.
PDB; 3FK2; X-ray; 2.80 A; A/B/C/D=1212-1439.
PDB; 6PXC; X-ray; 1.60 A; U=1100-1112.
PDB; 6WAY; X-ray; 1.50 A; V=1086-1093.
PDBsum; 2K85; -.
PDBsum; 3C5H; -.
PDBsum; 3FK2; -.
PDBsum; 6PXC; -.
PDBsum; 6WAY; -.
BMRB; Q9NRY4; -.
SMR; Q9NRY4; -.
BioGRID; 109166; 56.
DIP; DIP-34578N; -.
IntAct; Q9NRY4; 21.
MINT; Q9NRY4; -.
STRING; 9606.ENSP00000385720; -.
BindingDB; Q9NRY4; -.
ChEMBL; CHEMBL4523646; -.
iPTMnet; Q9NRY4; -.
PhosphoSitePlus; Q9NRY4; -.
BioMuta; ARHGAP35; -.
DMDM; 408360250; -.
EPD; Q9NRY4; -.
jPOST; Q9NRY4; -.
MassIVE; Q9NRY4; -.
PaxDb; Q9NRY4; -.
PeptideAtlas; Q9NRY4; -.
PRIDE; Q9NRY4; -.
ProteomicsDB; 82441; -.
Antibodypedia; 31509; 268 antibodies.
DNASU; 2909; -.
Ensembl; ENST00000404338; ENSP00000385720; ENSG00000160007.
Ensembl; ENST00000614079; ENSP00000483730; ENSG00000160007.
Ensembl; ENST00000672722; ENSP00000500409; ENSG00000160007.
GeneID; 2909; -.
KEGG; hsa:2909; -.
UCSC; uc010ekv.4; human.
CTD; 2909; -.
DisGeNET; 2909; -.
GeneCards; ARHGAP35; -.
HGNC; HGNC:4591; ARHGAP35.
HPA; ENSG00000160007; Low tissue specificity.
MIM; 605277; gene.
neXtProt; NX_Q9NRY4; -.
OpenTargets; ENSG00000160007; -.
PharmGKB; PA28988; -.
VEuPathDB; HostDB:ENSG00000160007.17; -.
eggNOG; KOG4271; Eukaryota.
GeneTree; ENSGT01030000234635; -.
HOGENOM; CLU_004268_0_0_1; -.
InParanoid; Q9NRY4; -.
OMA; WAPGSDG; -.
OrthoDB; 110157at2759; -.
TreeFam; TF324451; -.
PathwayCommons; Q9NRY4; -.
Reactome; R-HSA-194840; Rho GTPase cycle.
Reactome; R-HSA-416550; Sema4D mediated inhibition of cell attachment and migration.
Reactome; R-HSA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
SignaLink; Q9NRY4; -.
SIGNOR; Q9NRY4; -.
BioGRID-ORCS; 2909; 24 hits in 1003 CRISPR screens.
ChiTaRS; ARHGAP35; human.
EvolutionaryTrace; Q9NRY4; -.
GeneWiki; GRLF1; -.
GenomeRNAi; 2909; -.
Pharos; Q9NRY4; Tbio.
PRO; PR:Q9NRY4; -.
Proteomes; UP000005640; Chromosome 19.
RNAct; Q9NRY4; protein.
Bgee; ENSG00000160007; Expressed in frontal cortex and 242 other tissues.
Genevisible; Q9NRY4; HS.
GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
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; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0005543; F:phospholipid binding; IDA: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; ISS:ARUK-UCL.
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: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:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
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.
1: Evidence at protein level;
3D-structure; 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..1499
/note="Rho GTPase-activating protein 35"
/id="PRO_0000056730"
DOMAIN 270..327
/note="FF 1"
DOMAIN 368..422
/note="FF 2"
DOMAIN 429..483
/note="FF 3"
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 1249..1436
/note="Rho-GAP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
NP_BIND 33..37
/note="GTP"
/evidence="ECO:0000269|Ref.23, ECO:0007744|PDB:3C5H"
NP_BIND 95..97
/note="GTP"
/evidence="ECO:0000269|Ref.23, ECO:0007744|PDB:3C5H"
NP_BIND 201..203
/note="GTP"
/evidence="ECO:0000269|Ref.23, ECO:0007744|PDB:3C5H"
NP_BIND 229..231
/note="GTP"
/evidence="ECO:0000269|Ref.23, ECO:0007744|PDB:3C5H"
REGION 1..266
/note="Has GTPase activity, required for proper
localization"
/evidence="ECO:0000250|UniProtKB:Q91YM2"
REGION 1058..1089
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1124..1146
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1177..1207
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1213..1236
/note="Required for phospholipid binding and regulation of
the substrate preference"
/evidence="ECO:0000269|PubMed:19673492"
REGION 1446..1499
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1124..1139
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1182..1196
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1451..1469
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1470..1486
/note="Pro residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
BINDING 28
/note="GTP"
/evidence="ECO:0000269|Ref.23, ECO:0007744|PDB:3C5H"
BINDING 52
/note="GTP; via carbonyl oxygen"
/evidence="ECO:0000269|Ref.23, ECO:0007744|PDB:3C5H"
BINDING 56
/note="GTP"
/evidence="ECO:0000269|Ref.23, ECO:0007744|PDB:3C5H"
MOD_RES 308
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:19393245"
MOD_RES 589
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
ECO:0007744|PubMed:24275569"
MOD_RES 770
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 773
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:19690332,
ECO:0007744|PubMed:23186163"
MOD_RES 970
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18220336,
ECO:0007744|PubMed:18669648"
MOD_RES 975
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332"
MOD_RES 985
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q91YM2"
MOD_RES 1001
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:24275569"
MOD_RES 1072
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:19690332"
MOD_RES 1087
/note="Phosphotyrosine"
/evidence="ECO:0007744|PubMed:19690332"
MOD_RES 1105
/note="Phosphotyrosine; by ABL2 and PTK6"
/evidence="ECO:0000269|PubMed:18829532,
ECO:0007744|PubMed:19690332"
MOD_RES 1134
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:19690332,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
MOD_RES 1142
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q91YM2"
MOD_RES 1150
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
ECO:0007744|PubMed:24275569"
MOD_RES 1176
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 1179
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18088087,
ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
ECO:0007744|PubMed:24275569"
MOD_RES 1221
/note="Phosphoserine; by PKC/PRKCA"
/evidence="ECO:0000269|PubMed:19673492"
MOD_RES 1226
/note="Phosphothreonine; by PKC/PRKCA"
/evidence="ECO:0000269|PubMed:19673492"
MOD_RES 1236
/note="Phosphoserine; by PKC/PRKCA"
/evidence="ECO:0000269|PubMed:19673492"
MOD_RES 1472
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q91YM2"
MOD_RES 1476
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q91YM2"
MOD_RES 1480
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q91YM2"
MOD_RES 1483
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q91YM2"
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"
CONFLICT 251
/note="R -> P (in Ref. 5; AAF80386)"
/evidence="ECO:0000305"
CONFLICT 309
/note="V -> D (in Ref. 5; AAF80386)"
/evidence="ECO:0000305"
CONFLICT 362
/note="S -> G (in Ref. 5; AAF80386)"
/evidence="ECO:0000305"
CONFLICT 414
/note="Q -> A (in Ref. 5; AAF80386 and 6; AAA58618)"
/evidence="ECO:0000305"
CONFLICT 474
/note="M -> T (in Ref. 5; AAF80386 and 6; AAA58618)"
/evidence="ECO:0000305"
CONFLICT 978
/note="C -> S (in Ref. 5; AAF80386)"
/evidence="ECO:0000305"
CONFLICT 1292
/note="M -> I (in Ref. 5; AAF80386)"
/evidence="ECO:0000305"
CONFLICT 1452..1453
/note="PS -> RN (in Ref. 6; AAA58618)"
/evidence="ECO:0000305"
STRAND 14..21
/evidence="ECO:0007829|PDB:3C5H"
TURN 25..30
/evidence="ECO:0007829|PDB:3C5H"
HELIX 35..43
/evidence="ECO:0007829|PDB:3C5H"
TURN 47..49
/evidence="ECO:0007829|PDB:3C5H"
HELIX 60..63
/evidence="ECO:0007829|PDB:3C5H"
TURN 66..70
/evidence="ECO:0007829|PDB:3C5H"
STRAND 72..79
/evidence="ECO:0007829|PDB:3C5H"
STRAND 91..96
/evidence="ECO:0007829|PDB:3C5H"
TURN 102..104
/evidence="ECO:0007829|PDB:3C5H"
HELIX 110..112
/evidence="ECO:0007829|PDB:3C5H"
HELIX 116..120
/evidence="ECO:0007829|PDB:3C5H"
STRAND 123..126
/evidence="ECO:0007829|PDB:3C5H"
HELIX 136..138
/evidence="ECO:0007829|PDB:3C5H"
HELIX 142..144
/evidence="ECO:0007829|PDB:3C5H"
HELIX 151..153
/evidence="ECO:0007829|PDB:3C5H"
STRAND 154..156
/evidence="ECO:0007829|PDB:3C5H"
STRAND 159..165
/evidence="ECO:0007829|PDB:3C5H"
HELIX 174..190
/evidence="ECO:0007829|PDB:3C5H"
STRAND 195..200
/evidence="ECO:0007829|PDB:3C5H"
HELIX 202..204
/evidence="ECO:0007829|PDB:3C5H"
HELIX 207..218
/evidence="ECO:0007829|PDB:3C5H"
STRAND 220..222
/evidence="ECO:0007829|PDB:3C5H"
STRAND 225..227
/evidence="ECO:0007829|PDB:3C5H"
TURN 230..233
/evidence="ECO:0007829|PDB:3C5H"
HELIX 236..248
/evidence="ECO:0007829|PDB:3C5H"
TURN 268..271
/evidence="ECO:0007829|PDB:2K85"
HELIX 272..284
/evidence="ECO:0007829|PDB:2K85"
STRAND 286..288
/evidence="ECO:0007829|PDB:2K85"
HELIX 292..299
/evidence="ECO:0007829|PDB:2K85"
HELIX 303..311
/evidence="ECO:0007829|PDB:2K85"
HELIX 314..330
/evidence="ECO:0007829|PDB:2K85"
HELIX 1251..1254
/evidence="ECO:0007829|PDB:3FK2"
STRAND 1257..1259
/evidence="ECO:0007829|PDB:3FK2"
HELIX 1263..1275
/evidence="ECO:0007829|PDB:3FK2"
TURN 1280..1284
/evidence="ECO:0007829|PDB:3FK2"
HELIX 1289..1301
/evidence="ECO:0007829|PDB:3FK2"
HELIX 1308..1310
/evidence="ECO:0007829|PDB:3FK2"
HELIX 1314..1327
/evidence="ECO:0007829|PDB:3FK2"
STRAND 1328..1330
/evidence="ECO:0007829|PDB:3FK2"
HELIX 1335..1344
/evidence="ECO:0007829|PDB:3FK2"
HELIX 1350..1362
/evidence="ECO:0007829|PDB:3FK2"
HELIX 1366..1383
/evidence="ECO:0007829|PDB:3FK2"
HELIX 1386..1389
/evidence="ECO:0007829|PDB:3FK2"
HELIX 1393..1405
/evidence="ECO:0007829|PDB:3FK2"
STRAND 1409..1412
/evidence="ECO:0007829|PDB:3FK2"
HELIX 1414..1430
/evidence="ECO:0007829|PDB:3FK2"
HELIX 1432..1436
/evidence="ECO:0007829|PDB:3FK2"
SEQUENCE 1499 AA; 170514 MW; 8CCB493414A7E3E6 CRC64;
MMMARKQDVR IPTYNISVVG LSGTEKEKGQ CGIGKSCLCN RFVRPSADEF HLDHTSVLST
SDFGGRVVNN DHFLYWGEVS RSLEDCVECK MHIVEQTEFI DDQTFQPHRS TALQPYIKRA
AATKLASAEK LMYFCTDQLG LEQDFEQKQM PDGKLLVDGF LLGIDVSRGM NRNFDDQLKF
VSNLYNQLAK TKKPIVVVLT KCDEGVERYI RDAHTFALSK KNLQVVETSA RSNVNVDLAF
STLVQLIDKS RGKTKIIPYF EALKQQSQQI ATAKDKYEWL VSRIVKNHNE NWLSVSRKMQ
ASPEYQDYVY LEGTQKAKKL FLQHIHRLKH EHIERRRKLY LAALPLAFEA LIPNLDEIDH
LSCIKAKKLL ETKPEFLKWF VVLEETPWDA TSHIDNMENE RIPFDLMDTV PAEQLYEAHL
EKLRNERKRV 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 KRIELSVLSY
HSSFSIRKSR LVHGYIVFYS AKRKASLAML RAFLCEVQDI IPIQLVALTD GAVDVLDNDL
SREQLTEGEE IAQEIDGRFT SIPCSQPQHK LEIFHPFFKD VVEKKNIIEA THMYDNAAEA
CSTTEEVFNS PRAGSPLCNS NLQDSEEDIE PSYSLFREDT SLPSLSKDHS KLSMELEGND
GLSFIMSNFE SKLNNKVPPP VKPKPPVHFE ITKGDLSYLD QGHRDGQRKS VSSSPWLPQD
GFDPSDYAEP MDAVVKPRNE EENIYSVPHD STQGKIITIR NINKAQSNGS GNGSDSEMDT
SSLERGRKVS IVSKPVLYRT RCTRLGRFAS YRTSFSVGSD DELGPIRKKE EDQASQGYKG
DNAVIPYETD EDPRRRNILR SLRRNTKKPK PKPRPSITKA TWESNYFGVP LTTVVTPEKP
IPIFIERCIE YIEATGLSTE GIYRVSGNKS EMESLQRQFD QDHNLDLAEK DFTVNTVAGA
MKSFFSELPD PLVPYNMQID LVEAHKINDR EQKLHALKEV LKKFPKENHE VFKYVISHLN
KVSHNNKVNL MTSENLSICF WPTLMRPDFS TMDALTATRT YQTIIELFIQ QCPFFFYNRP
ITEPPGARPS SPSAVASTVP FLTSTPVTSQ PSPPQSPPPT PQSPMQPLLP SQLQAEHTL


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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)
[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)
[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)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[Nr3c1 Grl Grl1] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[Nr3c1 Grl] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[MYOC GLC1A TIGR] Myocilin (Myocilin 55 kDa subunit) (Trabecular meshwork-induced glucocorticoid response protein) [Cleaved into: Myocilin, N-terminal fragment (Myocilin 20 kDa N-terminal fragment); Myocilin, C-terminal fragment (Myocilin 35 kDa N-terminal fragment)]
[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)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[nr3c1 grl] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[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)
[ARHGAP17 RICH1 MSTP066 MSTP110] Rho GTPase-activating protein 17 (Rho-type GTPase-activating protein 17) (RhoGAP interacting with CIP4 homologs protein 1) (RICH-1)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[Rora Nr1f1 Rzra] Nuclear receptor ROR-alpha (Nuclear receptor RZR-alpha) (Nuclear receptor subfamily 1 group F member 1) (RAR-related orphan receptor A) (Retinoid-related orphan receptor-alpha)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1) (Fragment)
[GMEB2 KIAA1269] Glucocorticoid modulatory element-binding protein 2 (GMEB-2) (DNA-binding protein p79PIF) (Parvovirus initiation factor p79) (PIF p79)
[ARHGEF1] Rho guanine nucleotide exchange factor 1 (115 kDa guanine nucleotide exchange factor) (p115-RhoGEF) (p115RhoGEF) (Sub1.5)
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[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)

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