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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.
25-OCT-2017, entry version 117.
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).
-!- 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.
{ECO:0000250, ECO:0000269|PubMed:12531901,
ECO:0000269|PubMed:12857875, ECO:0000269|PubMed:16716191,
ECO:0000269|PubMed:17272280, ECO:0000269|PubMed:17663722}.
-!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
membrane, postsynaptic density {ECO:0000269|PubMed:12531901}. 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}.
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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]
UniGene; Mm.46683; -.
ProteinModelPortal; Q811P8; -.
SMR; Q811P8; -.
BioGrid; 237045; 9.
IntAct; Q811P8; 1.
MINT; MINT-268399; -.
STRING; 10090.ENSMUSP00000133898; -.
iPTMnet; Q811P8; -.
PhosphoSitePlus; Q811P8; -.
PaxDb; Q811P8; -.
PRIDE; Q811P8; -.
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; ENOG410Y1FN; LUCA.
GeneTree; ENSGT00900000140777; -.
HOGENOM; HOG000090208; -.
HOVERGEN; HBG108407; -.
InParanoid; Q811P8; -.
KO; K20647; -.
OMA; CDVDAYG; -.
OrthoDB; EOG091G02IN; -.
PhylomeDB; Q811P8; -.
TreeFam; TF351451; -.
Reactome; R-MMU-194840; Rho GTPase cycle.
ChiTaRS; Arhgap32; mouse.
PRO; PR:Q811P8; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000041444; -.
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:0030054; C:cell junction; IEA:UniProtKB-KW.
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; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
GO; GO:0035091; F:phosphatidylinositol 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.
Gene3D; 1.10.555.10; -; 1.
Gene3D; 3.30.1520.10; -; 1.
InterPro; IPR001683; Phox.
InterPro; IPR036871; PX_dom_sf.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR000198; RhoGAP_dom.
InterPro; IPR036028; SH3-like_dom.
InterPro; IPR001452; SH3_domain.
Pfam; PF00787; PX; 1.
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 membrane; Cell projection;
Complete proteome; Cytoplasm; Endoplasmic reticulum; Endosome;
Golgi apparatus; GTPase activation; Membrane; Methylation;
Phosphoprotein; Postsynaptic cell membrane; Reference proteome;
SH3 domain; Synapse.
CHAIN 1 2089 Rho GTPase-activating protein 32.
/FTId=PRO_0000345204.
DOMAIN 131 245 PX; atypical.
DOMAIN 259 321 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 372 567 Rho-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00172}.
REGION 1395 1714 Interaction with GAB2. {ECO:0000250}.
REGION 1688 2089 Interaction with FYN. {ECO:0000250}.
COMPBIAS 1033 1038 Poly-Pro.
COMPBIAS 1309 1314 Poly-Pro.
MOD_RES 706 706 Phosphoserine.
{ECO:0000250|UniProtKB:A7KAX9}.
MOD_RES 709 709 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 732 732 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 738 738 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 852 852 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 856 856 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 892 892 Phosphoserine.
{ECO:0000250|UniProtKB:A7KAX9}.
MOD_RES 952 952 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1206 1206 Phosphoserine.
{ECO:0000250|UniProtKB:A7KAX9}.
MOD_RES 1526 1526 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1536 1536 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1588 1588 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2039 2039 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
VAR_SEQ 1 349 Missing (in isoform 2).
{ECO:0000303|PubMed:12819203,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_034937.
MUTAGEN 58 58 R->K: Does not affect RhoA or CDC42
activity. {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


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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


 

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