GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

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)

 RHG32_MOUSE             Reviewed;        2089 AA.
Q811P8; B9EHJ8; Q6A010;
22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
22-JUL-2008, sequence version 2.
02-JUN-2021, entry version 145.
RecName: Full=Rho GTPase-activating protein 32;
AltName: Full=Brain-specific Rho GTPase-activating protein;
AltName: Full=GAB-associated Cdc42/Rac GTPase-activating protein;
AltName: Full=GC-GAP;
AltName: Full=Rho-type GTPase-activating protein 32;
AltName: Full=Rho/Cdc42/Rac GTPase-activating protein RICS;
AltName: Full=RhoGAP involved in the beta-catenin-N-cadherin and NMDA receptor signaling;
AltName: Full=p200RhoGAP;
AltName: Full=p250GAP;
Name=Arhgap32; Synonyms=Grit, Kiaa0712, Rics;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
STRAIN=C57BL/6J;
PubMed=12819203; DOI=10.1074/jbc.m304594200;
Zhao C., Ma H., Bossy-Wetzel E., Lipton S.A., Zhang Z., Feng G.S.;
"GC-GAP, a Rho family GTPase-activating protein that interacts with
signaling adapters Gab1 and Gab2.";
J. Biol. Chem. 278:34641-34653(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of the
mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1584-2089.
TISSUE=Fetal brain;
PubMed=15368895; DOI=10.1093/dnares/11.3.205;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
DNA Res. 11:205-218(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[6]
ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), INTERACTION WITH CTTNB1; GRIN2B;
DLG4 AND CDH2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
STAGE, AND DOMAIN PX.
PubMed=17663722; DOI=10.1111/j.1365-2443.2007.01101.x;
Hayashi T., Okabe T., Nasu-Nishimura Y., Sakaue F., Ohwada S., Matsuura K.,
Akiyama T., Nakamura T.;
"PX-RICS, a novel splicing variant of RICS, is a main isoform expressed
during neural development.";
Genes Cells 12:929-939(2007).
[7]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=12454018; DOI=10.1074/jbc.m207789200;
Moon S.Y., Zang H., Zheng Y.;
"Characterization of a brain-specific Rho GTPase-activating protein,
p200RhoGAP.";
J. Biol. Chem. 278:4151-4159(2003).
[8]
FUNCTION, INTERACTION WITH CTTNB1; GRIN2B; DLG4 AND CDH2, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=12531901; DOI=10.1074/jbc.m208872200;
Okabe T., Nakamura T., Nishimura Y.N., Kohu K., Ohwada S., Morishita Y.,
Akiyama T.;
"RICS, a novel GTPase-activating protein for Cdc42 and Rac1, is involved in
the beta-catenin-N-cadherin and N-methyl-D-aspartate receptor signaling.";
J. Biol. Chem. 278:9920-9927(2003).
[9]
INTERACTION WITH GRIN2B, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12857875; DOI=10.1091/mbc.e02-09-0623;
Nakazawa T., Watabe A.M., Tezuka T., Yoshida Y., Yokoyama K., Umemori H.,
Inoue A., Okabe S., Manabe T., Yamamoto T.;
"p250GAP, a novel brain-enriched GTPase-activating protein for Rho family
GTPases, is involved in the N-methyl-d-aspartate receptor signaling.";
Mol. Biol. Cell 14:2921-2934(2003).
[10]
FUNCTION, INTERACTION WITH CDC42, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
PubMed=16716191; DOI=10.1111/j.1365-2443.2006.00966.x;
Nasu-Nishimura Y., Hayashi T., Ohishi T., Okabe T., Ohwada S., Hasegawa Y.,
Senda T., Toyoshima C., Nakamura T., Akiyama T.;
"Role of the Rho GTPase-activating protein RICS in neurite outgrowth.";
Genes Cells 11:607-614(2006).
[11]
FUNCTION, INTERACTION WITH RASA1, AND MUTAGENESIS OF ARG-58.
PubMed=17272280; DOI=10.1074/jbc.m609375200;
Shang X., Moon S.Y., Zheng Y.;
"p200 RhoGAP promotes cell proliferation by mediating cross-talk between
Ras and Rho signaling pathways.";
J. Biol. Chem. 282:8801-8811(2007).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-709; SER-732; SER-738;
SER-852; SER-856; SER-952 AND SER-1588, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Pancreas, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[14]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1526; ARG-1536 AND ARG-2039, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.o113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[15]
SUBCELLULAR LOCATION, AND INTERACTION WITH GPHN.
PubMed=27609886; DOI=10.1126/science.aag0821;
Uezu A., Kanak D.J., Bradshaw T.W., Soderblom E.J., Catavero C.M.,
Burette A.C., Weinberg R.J., Soderling S.H.;
"Identification of an elaborate complex mediating postsynaptic
inhibition.";
Science 353:1123-1129(2016).
-!- FUNCTION: GTPase-activating protein (GAP) promoting GTP hydrolysis on
RHOA, CDC42 and RAC1 small GTPases. May be involved in the
differentiation of neuronal cells during the formation of neurite
extensions. Involved in NMDA receptor activity-dependent actin
reorganization in dendritic spines. May mediate cross-talks between
Ras- and Rho-regulated signaling pathways in cell growth regulation.
Isoform 2 has higher GAP activity. {ECO:0000269|PubMed:12454018,
ECO:0000269|PubMed:12531901, ECO:0000269|PubMed:12819203,
ECO:0000269|PubMed:16716191, ECO:0000269|PubMed:17272280}.
-!- SUBUNIT: Interacts with NTRK1 (via cytoplasmic domain); the interaction
is independent of the phosphorylation state of NTRK1 (By similarity).
Interacts with SHC3 (via SH2 domain) (By similarity). Interacts with
RASA1 (via SH3 domain); the interaction is necessary for the Ras
activation and cell transforming activities of ARHGAP32. Interacts with
GAB1 and GAB2. Interacts with CRK and CRKL. Found in a complex with
CRKL and BCAR1; upon EGF stimulation BCAR1 may be replaced by EGFR (By
similarity). Interacts with NCK1 (via SH3 domain); NCK1 recruits
phosphorylated BCAR1 to the complex. Isoform 2 interacts with FYN; the
interaction appears to be dependent on tyrosine phosphorylation of
ARHGAP32 (By similarity). Interacts with EGFR; the interaction requires
EGF stimulation and is increased by SHC3. Interacts with CDC42; the
interaction requires constitutively active CDC42. Interacts with
CTNNB1, DLG4, CDH2 and GRIN2B (By similarity) (PubMed:12531901,
PubMed:12857875, PubMed:16716191, PubMed:17272280, PubMed:17663722).
Interacts with GPHN (PubMed:27609886). {ECO:0000250|UniProtKB:A7KAX9,
ECO:0000269|PubMed:12531901, ECO:0000269|PubMed:12857875,
ECO:0000269|PubMed:16716191, ECO:0000269|PubMed:17272280,
ECO:0000269|PubMed:17663722, ECO:0000269|PubMed:27609886}.
-!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic density
{ECO:0000269|PubMed:12531901, ECO:0000269|PubMed:27609886}. Cell
projection, dendritic spine {ECO:0000269|PubMed:12531901}. Cytoplasm,
cell cortex {ECO:0000250|UniProtKB:A7KAX9}. Endosome membrane
{ECO:0000269|PubMed:17663722}. Golgi apparatus membrane
{ECO:0000269|PubMed:17663722}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:17663722}. Membrane {ECO:0000250|UniProtKB:A7KAX9}.
Note=Association to membrane via PX domain (By similarity). Associated
with cortical actin in undifferentiated neuroblastoma cells, but
localized to dendritic spine and postsynaptic density after
differentiation (PubMed:12531901). Colocalizes with EGFR at the cell
membrane upon EGF treatment (By similarity). Colocalizes with GAB2 at
the cell membrane (By similarity). {ECO:0000250|UniProtKB:A7KAX9,
ECO:0000269|PubMed:12531901}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=PX-RICS;
IsoId=Q811P8-1; Sequence=Displayed;
Name=2;
IsoId=Q811P8-2; Sequence=VSP_034937;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are highly expressed in
brain, specially in cortex, corpus striatum, hippocampus and thalamus.
Low levels in cerebellum, colon, small intestine, and kidney.
{ECO:0000269|PubMed:12454018, ECO:0000269|PubMed:12531901,
ECO:0000269|PubMed:12819203, ECO:0000269|PubMed:12857875,
ECO:0000269|PubMed:16716191, ECO:0000269|PubMed:17663722}.
-!- DEVELOPMENTAL STAGE: Isoform 1 is detectable by embryonic day 13,
whereas isoform 2 is detected postnatally.
{ECO:0000269|PubMed:12819203, ECO:0000269|PubMed:17663722}.
-!- DOMAIN: The N-terminal PX domain interacts specifically with
phosphatidylinositides. {ECO:0000269|PubMed:17663722}.
-!- PTM: Isoform 2 is phosphorylated on multiple tyrosine residues by FYN
(By similarity). Phosphorylated tyrosine residues undergo
dephosphorylation after stimulation of NMDA receptors. Phosphorylated
in vitro by CaMK2 in the presence of calmodulin and calcium; which
inhibits GAP activity. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice are fertile but display abnormal neurite
growth. {ECO:0000269|PubMed:16716191}.
-!- SIMILARITY: Belongs to the PX domain-containing GAP family.
{ECO:0000305}.
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; AY194286; AAO43676.1; -; mRNA.
EMBL; AC134607; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC132390; AAI32391.1; -; mRNA.
EMBL; BC138042; AAI38043.1; -; mRNA.
EMBL; AK173008; BAD32286.1; -; mRNA.
CCDS; CCDS22951.3; -. [Q811P8-2]
CCDS; CCDS57666.1; -. [Q811P8-1]
RefSeq; NP_001182561.1; NM_001195632.1. [Q811P8-1]
RefSeq; NP_796353.3; NM_177379.4. [Q811P8-2]
SMR; Q811P8; -.
BioGRID; 237045; 14.
CORUM; Q811P8; -.
IntAct; Q811P8; 7.
MINT; Q811P8; -.
STRING; 10090.ENSMUSP00000133898; -.
iPTMnet; Q811P8; -.
PhosphoSitePlus; Q811P8; -.
SwissPalm; Q811P8; -.
jPOST; Q811P8; -.
PaxDb; Q811P8; -.
PRIDE; Q811P8; -.
ProteomicsDB; 255209; -. [Q811P8-1]
ProteomicsDB; 255210; -. [Q811P8-2]
Antibodypedia; 51352; 90 antibodies.
DNASU; 330914; -.
Ensembl; ENSMUST00000168954; ENSMUSP00000128448; ENSMUSG00000041444. [Q811P8-2]
Ensembl; ENSMUST00000174641; ENSMUSP00000133898; ENSMUSG00000041444. [Q811P8-1]
Ensembl; ENSMUST00000182802; ENSMUSP00000138145; ENSMUSG00000041444. [Q811P8-2]
GeneID; 330914; -.
KEGG; mmu:330914; -.
UCSC; uc009orv.2; mouse. [Q811P8-1]
CTD; 9743; -.
MGI; MGI:2450166; Arhgap32.
eggNOG; KOG1449; Eukaryota.
eggNOG; KOG3564; Eukaryota.
GeneTree; ENSGT00940000154313; -.
HOGENOM; CLU_002754_0_0_1; -.
InParanoid; Q811P8; -.
OMA; YVPHPKP; -.
OrthoDB; 1300981at2759; -.
PhylomeDB; Q811P8; -.
TreeFam; TF351451; -.
Reactome; R-MMU-194840; Rho GTPase cycle.
BioGRID-ORCS; 330914; 2 hits in 53 CRISPR screens.
ChiTaRS; Arhgap32; mouse.
PRO; PR:Q811P8; -.
Proteomes; UP000000589; Chromosome 9.
RNAct; Q811P8; protein.
Bgee; ENSMUSG00000041444; Expressed in cingulate cortex and 253 other tissues.
ExpressionAtlas; Q811P8; baseline and differential.
Genevisible; Q811P8; MM.
GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
GO; GO:0005938; C:cell cortex; IDA:MGI.
GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0001650; C:fibrillar center; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
GO; GO:1901981; F:phosphatidylinositol phosphate binding; IEA:InterPro.
GO; GO:0007266; P:Rho protein signal transduction; ISO:MGI.
GO; GO:0007264; P:small GTPase mediated signal transduction; IBA:GO_Central.
CDD; cd07298; PX_RICS; 1.
Gene3D; 1.10.555.10; -; 1.
Gene3D; 3.30.1520.10; -; 1.
InterPro; IPR042139; PX_ARHGAP32.
InterPro; IPR036871; PX_dom_sf.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR000198; RhoGAP_dom.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
Pfam; PF00620; RhoGAP; 1.
Pfam; PF14604; SH3_9; 1.
SMART; SM00324; RhoGAP; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF48350; SSF48350; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF64268; SSF64268; 1.
PROSITE; PS50238; RHOGAP; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell projection; Cytoplasm;
Endoplasmic reticulum; Endosome; Golgi apparatus; GTPase activation;
Membrane; Methylation; Phosphoprotein; Reference proteome; SH3 domain;
Synapse.
CHAIN 1..2089
/note="Rho GTPase-activating protein 32"
/id="PRO_0000345204"
DOMAIN 131..245
/note="PX; atypical"
DOMAIN 259..321
/note="SH3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
DOMAIN 372..567
/note="Rho-GAP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
REGION 24..52
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 828..858
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 955..1037
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1119..1141
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1154..1197
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1221..1368
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1395..1714
/note="Interaction with GAB2"
/evidence="ECO:0000250"
REGION 1688..2089
/note="Interaction with FYN"
/evidence="ECO:0000250"
REGION 1801..1865
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 1881..2002
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 32..52
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 836..858
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 995..1017
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1174..1188
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1813..1848
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1915..1939
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 1942..1974
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 706
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:A7KAX9"
MOD_RES 709
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 732
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 738
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 852
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 856
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 892
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:A7KAX9"
MOD_RES 952
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 1206
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:A7KAX9"
MOD_RES 1526
/note="Asymmetric dimethylarginine"
/evidence="ECO:0007744|PubMed:24129315"
MOD_RES 1536
/note="Asymmetric dimethylarginine"
/evidence="ECO:0007744|PubMed:24129315"
MOD_RES 1588
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:21183079"
MOD_RES 2039
/note="Omega-N-methylarginine"
/evidence="ECO:0007744|PubMed:24129315"
VAR_SEQ 1..349
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:12819203,
ECO:0000303|PubMed:15489334"
/id="VSP_034937"
MUTAGEN 58
/note="R->K: Does not affect RhoA or CDC42 activity."
/evidence="ECO:0000269|PubMed:17272280"
SEQUENCE 2089 AA; 229719 MW; C7C4BD904D903F02 CRC64;
METESETSSL GDDSVFWLDC EGVTQLTDGD EEEREESFRK MKSSIHSEED DFVPELHRNV
HPRERPDWEE TLSAMARGAD VPEIPGDLTL KSCGSTASTK VKHVKKLPFT KGHFPKMAEC
AHFHYENVEF GSIQLSLSEE QNEVMKNGCE SKELVYLVQI ACQGKSWIVK RSYEDFRVLD
KHLHLCIYDR RFSQLTELPR SDVLKDSPES VTQMLTAYLS RLSTIAGNKI NCGPALTWME
IDNKGNHLLV HEESSINTPA VGAAHVIKRY TARAPDELTL EVGDIVSVID MPPKVLSTWW
RGKHGFQVGL FPGHCVELIN QKVPQSVTNS VPKPVSKKHG KLITFLRTFM KSRPTKQKLK
QRGILKERVF GCDLGEHLLN SGFEVPQVLQ SCTAFIERYG IVDGIYRLSG VASNIQRLRH
EFDSEHVPDL TKEPYVQDIH SVGSLCKLYF RELPNPLLTY QLYEKFSDAV SAATDEERLI
KIHDVIQQLP PPHYRTLEFL MRHLSLLADY CSITNMHAKN LAIVWAPNLL RSKQIESACF
SGTAAFMEVR IQSVVVEFIL NHVDVLFSGK ISAVMQEGAA SLSRPKSLLV SSPSTKLLTL
EEAQARTQAQ VSSPIVTENK YIEVGEGPAA LQGKFHTVIE FPLERKRPQN KMKKSPVGSW
RSFFNLGKSS SVSKRKLQRN ESEPSEMKAM ALKGGRAEGT LRSAKSEESL TSLHAVDGDS
KLFRPRRPRS SSDALSASFN GDVLGNRCNS YDNLPHDNES EEEVGLLHIP ALVSPHSAED
VDLSPPDIGV ASLDFDPMSF QCSPPKAESE CLESGASFLD SLGYTRDKLS PSKKDAEAGG
SQSQTPGSTA SSEPVSPVQE KLSPFFTLDL SPTDDKSSKP SSFTEKVVYA FSPKIGRKLS
KSPSMNISEP ISVTLPPRVS EVIGTVSNTV AQNASPTSWD KSVEERDVIN RSPTQLQLGK
MKAGEREAQE TCEPEAQPLE QGAAEEVELP GTEERPVLSS QSKAVPSGQS QTGAVTHDPP
QDPVPVSSVS LIPPPPPPKN VARMLALALA ESAQQASSQT LKRPGASQAG CTSYGDTAVV
PSEEKLPSSY SSLTLDKTCF QTDRPAEQFH PQINGLGNCN QPLPEAAAMG GPTQSNTTDS
GEQLHQVDLI GNSLHRNHIS GDPEKARSTS APLTDSEKSD DHGSFPEDHA GKSSVSTVSF
LEQDQSPLHF SCGDQPLSYL GTSVDKPHHS SELTDKSPMP STLPRDKAHH PLSGSPEENS
STATMAYMMA TPARAEPSNS EASRVLAEQP SAADFVAATL QRTHRTNRPL PPPPSQRPAE
QPPVVGQVQE APSIGLNNSH KVQGTAPAPE RPPESRAMGD PAPIFLSDGT AAAQCPMGAS
APQPGLPEKV RESSRAPPLH LRAESFPGHS CGFAAPVPPT RTMESKMAAA LHSSAADATS
SSNYHSFVPS SASVDDVMPV PLPVSQPKHA SQKIAYSSFA RPDVTAEPFG PENCLHFNMT
PNCQFRPQSV PPHHNKLEPH QVYGARSEPP ASMGPRYNTY VAPGRNMSGH HSKPCSRVEY
VSSLGSSVRN PCCPEDILPY PTIRRVQSLH APPPSMIRSV PISRTEVPPD DEPAYCPRPV
YQYKPYQSSQ ARSDYHVTQL QPYFENGRVH YRYSPYSSSS SSYYSPEGAL CDVDAYGTVQ
LRPLHRLSSR DFAFYNPRLQ GKNVYNYAGL PPRPRANATG YFSGNDHNVV TMPPTADGKH
TYTSWDLEDM EKYRMQSIRR ESRARQKVKG PIMSQYDNMT PAVQEDLGGI YVIHLRSKSD
PGKTGLLSVA EGKEGRHPAK AVSPEGDERF YRKHPESEFD RAHHHGGYGS TQAEKPSLPQ
KQSSLRNRKL HDMGCSLPEH RAHQEASHRQ LCESKNGPPY PQGAGQLDYG SKGMPDTSEP
SNYHNSGKYM TSGQGSLTLN HKEVRLPKDL DRPRARQPPG PEKHSRDCYK EEEHFSQSMV
PPPKPERSHS LKLHHTQNLE RDPSVLYQYQ THSKRQSSMT VVSQYDNLED YHSLPQHQRG
GFGGAGMGAY VPSGFVHPQS RTYATALGQG AFLPTELSLP HPDTQIHAE


Related products :

Catalog number Product name Quantity
EIAAB34717 Arhgap32,Brain-specific Rho GTPase-activating protein,GAB-associated Cdc42_Rac GTPase-activating protein,GC-GAP,Grit,Kiaa0712,Mouse,Mus musculus,p200RhoGAP,p250GAP,Rho GTPase-activating protein 32,Rho
EIAAB34654 ARHGAP1,CDC42 GTPase-activating protein,CDC42GAP,GTPase-activating protein rhoOGAP,Homo sapiens,Human,p50-RhoGAP,Rho GTPase-activating protein 1,RHOGAP1,Rho-related small GTPase protein activator,Rho-
EIAAB34716 ARHGAP32,Brain-specific Rho GTPase-activating protein,GAB-associated Cdc42_Rac GTPase-activating protein,GC-GAP,GRIT,GTPase regulator interacting with TrkA,Homo sapiens,Human,KIAA0712,p200RhoGAP,p250G
EIAAB34696 ARHGAP24,Filamin-A-associated RhoGAP,FilGAP,FILGAP,Homo sapiens,Human,p73RhoGAP,RAC1- and CDC42-specific GTPase-activating protein of 72 kDa,RC-GAP72,Rho GTPase-activating protein 24,RhoGAP of 73 kDa,
EIAAB34719 ARHGAP33,Homo sapiens,Human,Rho GTPase-activating protein 33,Rho-type GTPase-activating protein 33,SNX26,Sorting nexin-26,Tc10_CDC42 GTPase-activating protein,TCGAP
EIAAB34718 Arhgap33,Mouse,Mus musculus,Rho GTPase-activating protein 33,Rho-type GTPase-activating protein 33,Snx26,Sorting nexin-26,Tc10_CDC42 GTPase-activating protein,Tcgap
EIAAB34705 Arhgap27,Camgap1,CIN85-associated multi-domain-containing Rho GTPase-activating protein 1,Rat,Rattus norvegicus,Rho GTPase-activating protein 27,Rho-type GTPase-activating protein 27
EIAAB34703 Arhgap27,Camgap1,CIN85-associated multi-domain-containing Rho GTPase-activating protein 1,Mouse,Mus musculus,Rho GTPase-activating protein 27,Rho-type GTPase-activating protein 27
EIAAB34690 ARHGAP10,ARHGAP21,Homo sapiens,Human,KIAA1424,Rho GTPase-activating protein 10,Rho GTPase-activating protein 21,Rho-type GTPase-activating protein 21
EIAAB34689 Arhgap10,Arhgap21,Kiaa1424,Mouse,Mus musculus,Rho GTPase-activating protein 10,Rho GTPase-activating protein 21,Rho-type GTPase-activating protein 21
EIAAB34704 ARHGAP27,CAMGAP1,CIN85-associated multi-domain-containing Rho GTPase-activating protein 1,Homo sapiens,Human,PP905,Rho GTPase-activating protein 27,Rho-type GTPase-activating protein 27,SH3 domain-con
EIAAB34715 ARHGAP31,Cdc42 GTPase-activating protein,CDGAP,Homo sapiens,Human,KIAA1204,Rho GTPase-activating protein 31
EIAAB34731 ARHGAP42,Homo sapiens,Human,Rho GTPase-activating protein 10-like,Rho GTPase-activating protein 42,Rho-type GTPase-activating protein 42
EIAAB34714 Arhgap31,Cdc42 GTPase-activating protein,Cdgap,Kiaa1204,Mouse,Mus musculus,Rho GTPase-activating protein 31
EIAAB34669 ARHGAP10,GRAF2,Graf-related protein 2,GTPase regulator associated with focal adhesion kinase 2,Homo sapiens,Human,Rho GTPase-activating protein 10,Rho-type GTPase-activating protein 10
EIAAB34700 ARHGAP26,GRAF,GTPase regulator associated with focal adhesion kinase,Homo sapiens,Human,KIAA0621,Oligophrenin-1-like protein,OPHN1L,Rho GTPase-activating protein 26,Rho-type GTPase-activating protein
EIAAB34679 ARHGAP17,Homo sapiens,Human,MSTP066,MSTP110,Rho GTPase-activating protein 17,RhoGAP interacting with CIP4 homologs protein 1,Rho-type GTPase-activating protein 17,RICH1,RICH-1
EIAAB34659 ARHGAP6,Homo sapiens,Human,Rho GTPase-activating protein 6,RHOGAP6,Rho-type GTPase-activating protein 6,Rho-type GTPase-activating protein RhoGAPX-1
EIAAB34708 ARHGAP29,Homo sapiens,Human,PARG1,PTPL1-associated RhoGAP protein 1,Rho GTPase-activating protein 29,Rho-type GTPase-activating protein 29
EIAAB34688 Arhgap20,Kiaa1391,Mouse,Mus musculus,RA and RhoGAP domain-containing protein,RARhoGAP,Rho GTPase-activating protein 20,Rho-type GTPase-activating protein 20
EIAAB34670 Arhgap10,Mouse,Mus musculus,PH and SH3 domain-containing rhoGAP protein,PSGAP,PS-GAP,Rho GTPase-activating protein 10,Rho-type GTPase-activating protein 10
EIAAB34687 Arhgap20,RA and RhoGAP domain-containing protein,RARhoGAP,Rat,Rattus norvegicus,Rho GTPase-activating protein 20,Rho-type GTPase-activating protein 20
EIAAB34660 Arhgap7,Deleted in liver cancer 1 protein homolog,Dlc1,DLC-1,p122-RhoGAP,Rat,Rattus norvegicus,Rho GTPase-activating protein 7,Rhogap,Rho-type GTPase-activating protein 7,StARD12,Stard12,StAR-related
EIAAB34733 ARHGAP44,Homo sapiens,Human,KIAA0672,NPC-A-10,Rho GTPase-activating protein 44,RhoGAP interacting with CIP4 homologs protein 2,Rho-type GTPase-activating protein RICH2,RICH2,RICH-2
EIAAB34658 Arhgap6,Mouse,Mus musculus,Rho GTPase-activating protein 6,Rho-type GTPase-activating protein 6,Rho-type GTPase-activating protein RhoGAPX-1
Pathways :
WP2272: Pathogenic Escherichia coli infection
WP2292: Chemokine signaling pathway
WP210: Cytoplasmic Ribosomal Proteins
WP73: G Protein Signaling Pathways
WP566: canonical wnt - zebrafish
WP2218: sGC
WP1049: G Protein Signaling Pathways
WP35: G Protein Signaling Pathways
WP813: G Protein Signaling Pathways
WP2203: TSLP Signaling Pathway
WP931: G Protein Signaling Pathways
WP211: BMP signaling pathway
WP2032: TSH signaling pathway
WP1566: Citrate cycle (TCA cycle)
WP1371: G Protein Signaling Pathways
WP232: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1689: Porphyrin and chlorophyll metabolism
WP1654: gamma-Hexachlorocyclohexane degradation
WP1692: Protein export
WP1659: Glycine, serine and threonine metabolism
WP1939: Unfolded Protein Response
WP1665: Limonene and pinene degradation
WP1714: Tyrosine metabolism
WP1675: Nitrogen metabolism

Related Genes :
[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)
[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)
[ARHGAP31 CDGAP KIAA1204] Rho GTPase-activating protein 31 (Cdc42 GTPase-activating protein)
[ARHGAP17 RICH1 MSTP066 MSTP110] Rho GTPase-activating protein 17 (Rho-type GTPase-activating protein 17) (RhoGAP interacting with CIP4 homologs protein 1) (RICH-1)
[ARHGAP21 ARHGAP10 KIAA1424] Rho GTPase-activating protein 21 (Rho GTPase-activating protein 10) (Rho-type GTPase-activating protein 21)
[Arhgap24] Rho GTPase-activating protein 24 (Rho-type GTPase-activating protein 24)
[Arhgap17] Rho GTPase-activating protein 17 (Neuron-associated developmentally-regulated protein) (Nadrin) (Rho-type GTPase-activating protein 17)
[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 P190A p190ARHOGAP] Rho GTPase-activating protein 35 (Glucocorticoid receptor DNA-binding factor 1) (Rho GAP p190A) (p190-A)
[Syde1] Rho GTPase-activating protein SYDE1 (Synapse defective protein 1 homolog 1) (Protein syd-1 homolog 1)
[RGA1 DBM1 THE1 YOR127W O3290 YOR3290W] Rho-type GTPase-activating protein 1
[Arhgap35 Grlf1 Kiaa1722 P190A p190ARHOGAP] Rho GTPase-activating protein 35 (Glucocorticoid receptor DNA-binding factor 1)
[CHN1 ARHGAP2 CHN] N-chimaerin (A-chimaerin) (Alpha-chimerin) (N-chimerin) (NC) (Rho GTPase-activating protein 2)
[rga8 SPAC13A11.01c SPAC2F7.18c] Rho-GTPase-activating protein 8
[CHN2 ARHGAP3 BCH] Beta-chimaerin (Beta-chimerin) (Rho GTPase-activating protein 3)
[CDC42] Cell division control protein 42 homolog (EC 3.6.5.2) (G25K GTP-binding protein)
[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)
[ARHGAP45 HMHA1 KIAA0223] Rho GTPase-activating protein 45 [Cleaved into: Minor histocompatibility antigen HA-1 (mHag HA-1)]
[ARHGEF9 ARHDH9 KIAA0424] Rho guanine nucleotide exchange factor 9 (Collybistin) (PEM-2 homolog) (Rac/Cdc42 guanine nucleotide exchange factor 9)
[Arhgap24 DR-NR#2] Rho GTPase-activating protein 24 (Down-regulated in nephrectomized rat kidney #2) (Rho-type GTPase-activating protein 24)
[IQGAP1 KIAA0051] Ras GTPase-activating-like protein IQGAP1 (p195)
[ARHGAP8] Rho GTPase-activating protein 8 (Rho-type GTPase-activating protein 8)
[Arhgap17] Rho GTPase-activating protein 17 (Neuron-associated developmentally-regulated protein) (Nadrin) (Rho-type GTPase-activating protein 17)
[Pak1 Paka] Serine/threonine-protein kinase PAK 1 (EC 2.7.11.1) (Alpha-PAK) (CDC42/RAC effector kinase PAK-A) (p21-activated kinase 1) (PAK-1) (p65-PAK)
[Cdc42] Cell division control protein 42 homolog (EC 3.6.5.2) (G25K GTP-binding protein)
[conu CG17082] Rho GTPase-activating protein conundrum
[Iqgap1] Ras GTPase-activating-like protein IQGAP1
[cdc-42 R07G3.1] Cell division control protein 42 homolog (CDC42Ce)
[Syngap1] Ras/Rap GTPase-activating protein SynGAP (Neuronal RasGAP) (Synaptic Ras GTPase-activating protein 1) (Synaptic Ras-GAP 1) (p135 SynGAP)

Bibliography :