ID RHG32_MOUSE Reviewed; 2089 AA. AC Q811P8; B9EHJ8; Q6A010; DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 2. DT 24-JAN-2024, entry version 157. DE RecName: Full=Rho GTPase-activating protein 32; DE AltName: Full=Brain-specific Rho GTPase-activating protein; DE AltName: Full=GAB-associated Cdc42/Rac GTPase-activating protein; DE AltName: Full=GC-GAP; DE AltName: Full=Rho-type GTPase-activating protein 32; DE AltName: Full=Rho/Cdc42/Rac GTPase-activating protein RICS; DE AltName: Full=RhoGAP involved in the beta-catenin-N-cadherin and NMDA receptor signaling; DE AltName: Full=p200RhoGAP; DE AltName: Full=p250GAP; GN Name=Arhgap32; Synonyms=Grit, Kiaa0712, Rics; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RC STRAIN=C57BL/6J; RX PubMed=12819203; DOI=10.1074/jbc.m304594200; RA Zhao C., Ma H., Bossy-Wetzel E., Lipton S.A., Zhang Z., Feng G.S.; RT "GC-GAP, a Rho family GTPase-activating protein that interacts with RT signaling adapters Gab1 and Gab2."; RL J. Biol. Chem. 278:34641-34653(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1584-2089. RC TISSUE=Fetal brain; RX PubMed=15368895; DOI=10.1093/dnares/11.3.205; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., RA Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL DNA Res. 11:205-218(2004). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). RN [6] RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), INTERACTION WITH CTTNB1; GRIN2B; RP DLG4 AND CDH2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL RP STAGE, AND DOMAIN PX. RX PubMed=17663722; DOI=10.1111/j.1365-2443.2007.01101.x; RA Hayashi T., Okabe T., Nasu-Nishimura Y., Sakaue F., Ohwada S., Matsuura K., RA Akiyama T., Nakamura T.; RT "PX-RICS, a novel splicing variant of RICS, is a main isoform expressed RT during neural development."; RL Genes Cells 12:929-939(2007). RN [7] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=12454018; DOI=10.1074/jbc.m207789200; RA Moon S.Y., Zang H., Zheng Y.; RT "Characterization of a brain-specific Rho GTPase-activating protein, RT p200RhoGAP."; RL J. Biol. Chem. 278:4151-4159(2003). RN [8] RP FUNCTION, INTERACTION WITH CTTNB1; GRIN2B; DLG4 AND CDH2, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RX PubMed=12531901; DOI=10.1074/jbc.m208872200; RA Okabe T., Nakamura T., Nishimura Y.N., Kohu K., Ohwada S., Morishita Y., RA Akiyama T.; RT "RICS, a novel GTPase-activating protein for Cdc42 and Rac1, is involved in RT the beta-catenin-N-cadherin and N-methyl-D-aspartate receptor signaling."; RL J. Biol. Chem. 278:9920-9927(2003). RN [9] RP INTERACTION WITH GRIN2B, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=12857875; DOI=10.1091/mbc.e02-09-0623; RA Nakazawa T., Watabe A.M., Tezuka T., Yoshida Y., Yokoyama K., Umemori H., RA Inoue A., Okabe S., Manabe T., Yamamoto T.; RT "p250GAP, a novel brain-enriched GTPase-activating protein for Rho family RT GTPases, is involved in the N-methyl-d-aspartate receptor signaling."; RL Mol. Biol. Cell 14:2921-2934(2003). RN [10] RP FUNCTION, INTERACTION WITH CDC42, TISSUE SPECIFICITY, AND DISRUPTION RP PHENOTYPE. RX PubMed=16716191; DOI=10.1111/j.1365-2443.2006.00966.x; RA Nasu-Nishimura Y., Hayashi T., Ohishi T., Okabe T., Ohwada S., Hasegawa Y., RA Senda T., Toyoshima C., Nakamura T., Akiyama T.; RT "Role of the Rho GTPase-activating protein RICS in neurite outgrowth."; RL Genes Cells 11:607-614(2006). RN [11] RP FUNCTION, INTERACTION WITH RASA1, AND MUTAGENESIS OF ARG-58. RX PubMed=17272280; DOI=10.1074/jbc.m609375200; RA Shang X., Moon S.Y., Zheng Y.; RT "p200 RhoGAP promotes cell proliferation by mediating cross-talk between RT Ras and Rho signaling pathways."; RL J. Biol. Chem. 282:8801-8811(2007). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-709; SER-732; SER-738; RP SER-852; SER-856; SER-952 AND SER-1588, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Kidney, Pancreas, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [14] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1526; ARG-1536 AND ARG-2039, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, and Embryo; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [15] RP SUBCELLULAR LOCATION, AND INTERACTION WITH GPHN. RX PubMed=27609886; DOI=10.1126/science.aag0821; RA Uezu A., Kanak D.J., Bradshaw T.W., Soderblom E.J., Catavero C.M., RA Burette A.C., Weinberg R.J., Soderling S.H.; RT "Identification of an elaborate complex mediating postsynaptic RT inhibition."; RL Science 353:1123-1129(2016). CC -!- FUNCTION: GTPase-activating protein (GAP) promoting GTP hydrolysis on CC RHOA, CDC42 and RAC1 small GTPases. May be involved in the CC differentiation of neuronal cells during the formation of neurite CC extensions. Involved in NMDA receptor activity-dependent actin CC reorganization in dendritic spines. May mediate cross-talks between CC Ras- and Rho-regulated signaling pathways in cell growth regulation. CC Isoform 2 has higher GAP activity. {ECO:0000269|PubMed:12454018, CC ECO:0000269|PubMed:12531901, ECO:0000269|PubMed:12819203, CC ECO:0000269|PubMed:16716191, ECO:0000269|PubMed:17272280}. CC -!- SUBUNIT: Interacts with NTRK1 (via cytoplasmic domain); the interaction CC is independent of the phosphorylation state of NTRK1 (By similarity). CC Interacts with SHC3 (via SH2 domain) (By similarity). Interacts with CC RASA1 (via SH3 domain); the interaction is necessary for the Ras CC activation and cell transforming activities of ARHGAP32. Interacts with CC GAB1 and GAB2. Interacts with CRK and CRKL. Found in a complex with CC CRKL and BCAR1; upon EGF stimulation BCAR1 may be replaced by EGFR (By CC similarity). Interacts with NCK1 (via SH3 domain); NCK1 recruits CC phosphorylated BCAR1 to the complex. Isoform 2 interacts with FYN; the CC interaction appears to be dependent on tyrosine phosphorylation of CC ARHGAP32 (By similarity). Interacts with EGFR; the interaction requires CC EGF stimulation and is increased by SHC3. Interacts with CDC42; the CC interaction requires constitutively active CDC42. Interacts with CC CTNNB1, DLG4, CDH2 and GRIN2B (By similarity) (PubMed:12531901, CC PubMed:12857875, PubMed:16716191, PubMed:17272280, PubMed:17663722). CC Interacts with GPHN (PubMed:27609886). {ECO:0000250|UniProtKB:A7KAX9, CC ECO:0000269|PubMed:12531901, ECO:0000269|PubMed:12857875, CC ECO:0000269|PubMed:16716191, ECO:0000269|PubMed:17272280, CC ECO:0000269|PubMed:17663722, ECO:0000269|PubMed:27609886}. CC -!- SUBCELLULAR LOCATION: Postsynaptic density CC {ECO:0000269|PubMed:12531901, ECO:0000269|PubMed:27609886}. Cell CC projection, dendritic spine {ECO:0000269|PubMed:12531901}. Cytoplasm, CC cell cortex {ECO:0000250|UniProtKB:A7KAX9}. Endosome membrane CC {ECO:0000269|PubMed:17663722}. Golgi apparatus membrane CC {ECO:0000269|PubMed:17663722}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:17663722}. Membrane {ECO:0000250|UniProtKB:A7KAX9}. CC Note=Association to membrane via PX domain (By similarity). Associated CC with cortical actin in undifferentiated neuroblastoma cells, but CC localized to dendritic spine and postsynaptic density after CC differentiation (PubMed:12531901). Colocalizes with EGFR at the cell CC membrane upon EGF treatment (By similarity). Colocalizes with GAB2 at CC the cell membrane (By similarity). {ECO:0000250|UniProtKB:A7KAX9, CC ECO:0000269|PubMed:12531901}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=PX-RICS; CC IsoId=Q811P8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q811P8-2; Sequence=VSP_034937; CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are highly expressed in CC brain, specially in cortex, corpus striatum, hippocampus and thalamus. CC Low levels in cerebellum, colon, small intestine, and kidney. CC {ECO:0000269|PubMed:12454018, ECO:0000269|PubMed:12531901, CC ECO:0000269|PubMed:12819203, ECO:0000269|PubMed:12857875, CC ECO:0000269|PubMed:16716191, ECO:0000269|PubMed:17663722}. CC -!- DEVELOPMENTAL STAGE: Isoform 1 is detectable by embryonic day 13, CC whereas isoform 2 is detected postnatally. CC {ECO:0000269|PubMed:12819203, ECO:0000269|PubMed:17663722}. CC -!- DOMAIN: The N-terminal PX domain interacts specifically with CC phosphatidylinositides. {ECO:0000269|PubMed:17663722}. CC -!- PTM: Isoform 2 is phosphorylated on multiple tyrosine residues by FYN CC (By similarity). Phosphorylated tyrosine residues undergo CC dephosphorylation after stimulation of NMDA receptors. Phosphorylated CC in vitro by CaMK2 in the presence of calmodulin and calcium; which CC inhibits GAP activity. {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: Mice are fertile but display abnormal neurite CC growth. {ECO:0000269|PubMed:16716191}. CC -!- SIMILARITY: Belongs to the PX domain-containing GAP family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY194286; AAO43676.1; -; mRNA. DR EMBL; AC134607; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC132390; AAI32391.1; -; mRNA. DR EMBL; BC138042; AAI38043.1; -; mRNA. DR EMBL; AK173008; BAD32286.1; -; mRNA. DR CCDS; CCDS22951.3; -. [Q811P8-2] DR CCDS; CCDS57666.1; -. [Q811P8-1] DR RefSeq; NP_001182561.1; NM_001195632.1. [Q811P8-1] DR RefSeq; NP_796353.3; NM_177379.4. [Q811P8-2] DR AlphaFoldDB; Q811P8; -. DR SMR; Q811P8; -. DR BioGRID; 237045; 16. DR CORUM; Q811P8; -. DR IntAct; Q811P8; 8. DR MINT; Q811P8; -. DR STRING; 10090.ENSMUSP00000133898; -. DR GlyGen; Q811P8; 10 sites, 1 O-linked glycan (10 sites). DR iPTMnet; Q811P8; -. DR PhosphoSitePlus; Q811P8; -. DR SwissPalm; Q811P8; -. DR jPOST; Q811P8; -. DR MaxQB; Q811P8; -. DR PaxDb; 10090-ENSMUSP00000133898; -. DR ProteomicsDB; 255209; -. [Q811P8-1] DR ProteomicsDB; 255210; -. [Q811P8-2] DR Pumba; Q811P8; -. DR Antibodypedia; 51352; 138 antibodies from 15 providers. DR DNASU; 330914; -. DR Ensembl; ENSMUST00000168954.9; ENSMUSP00000128448.3; ENSMUSG00000041444.15. [Q811P8-2] DR Ensembl; ENSMUST00000174641.8; ENSMUSP00000133898.2; ENSMUSG00000041444.15. [Q811P8-1] DR Ensembl; ENSMUST00000182802.8; ENSMUSP00000138145.2; ENSMUSG00000041444.15. [Q811P8-2] DR GeneID; 330914; -. DR KEGG; mmu:330914; -. DR UCSC; uc009orv.2; mouse. [Q811P8-1] DR AGR; MGI:2450166; -. DR CTD; 9743; -. DR MGI; MGI:2450166; Arhgap32. DR VEuPathDB; HostDB:ENSMUSG00000041444; -. DR eggNOG; KOG1449; Eukaryota. DR eggNOG; KOG3564; Eukaryota. DR GeneTree; ENSGT00940000154313; -. DR HOGENOM; CLU_002754_0_0_1; -. DR InParanoid; Q811P8; -. DR OMA; IIQVTDC; -. DR OrthoDB; 5314555at2759; -. DR PhylomeDB; Q811P8; -. DR TreeFam; TF351451; -. DR Reactome; R-MMU-8980692; RHOA GTPase cycle. DR Reactome; R-MMU-9013026; RHOB GTPase cycle. DR Reactome; R-MMU-9013106; RHOC GTPase cycle. DR Reactome; R-MMU-9013148; CDC42 GTPase cycle. DR Reactome; R-MMU-9013149; RAC1 GTPase cycle. DR Reactome; R-MMU-9013404; RAC2 GTPase cycle. DR Reactome; R-MMU-9013405; RHOD GTPase cycle. DR Reactome; R-MMU-9013406; RHOQ GTPase cycle. DR Reactome; R-MMU-9013408; RHOG GTPase cycle. DR Reactome; R-MMU-9013409; RHOJ GTPase cycle. DR Reactome; R-MMU-9013423; RAC3 GTPase cycle. DR Reactome; R-MMU-9035034; RHOF GTPase cycle. DR BioGRID-ORCS; 330914; 3 hits in 77 CRISPR screens. DR ChiTaRS; Arhgap32; mouse. DR PRO; PR:Q811P8; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; Q811P8; Protein. DR Bgee; ENSMUSG00000041444; Expressed in caudate-putamen and 209 other cell types or tissues. DR ExpressionAtlas; Q811P8; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI. DR GO; GO:0005938; C:cell cortex; IDA:MGI. DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0001650; C:fibrillar center; ISO:MGI. DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB. DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI. DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IEA:InterPro. DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl. DR GO; GO:0045773; P:positive regulation of axon extension; ISO:MGI. DR GO; GO:2001224; P:positive regulation of neuron migration; ISO:MGI. DR GO; GO:0007266; P:Rho protein signal transduction; ISO:MGI. DR GO; GO:0007264; P:small GTPase mediated signal transduction; IBA:GO_Central. DR CDD; cd07298; PX_RICS; 1. DR CDD; cd04384; RhoGAP_CdGAP; 1. DR CDD; cd11835; SH3_ARHGAP32_33; 1. DR Gene3D; 3.30.1520.10; Phox-like domain; 1. DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR042139; PX_ARHGAP32. DR InterPro; IPR036871; PX_dom_sf. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR InterPro; IPR000198; RhoGAP_dom. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR15729; CDC42 GTPASE-ACTIVATING PROTEIN; 1. DR PANTHER; PTHR15729:SF13; RHO GTPASE-ACTIVATING PROTEIN 32; 1. DR Pfam; PF00620; RhoGAP; 1. DR Pfam; PF14604; SH3_9; 1. DR SMART; SM00324; RhoGAP; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1. DR SUPFAM; SSF64268; PX domain; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS50238; RHOGAP; 1. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q811P8; MM. PE 1: Evidence at protein level; KW Alternative splicing; Cell projection; Cytoplasm; Endoplasmic reticulum; KW Endosome; Golgi apparatus; GTPase activation; Membrane; Methylation; KW Phosphoprotein; Reference proteome; SH3 domain; Synapse. FT CHAIN 1..2089 FT /note="Rho GTPase-activating protein 32" FT /id="PRO_0000345204" FT DOMAIN 131..245 FT /note="PX; atypical" FT DOMAIN 259..321 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 372..567 FT /note="Rho-GAP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172" FT REGION 24..52 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 828..858 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 955..1037 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1119..1141 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1154..1197 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1221..1368 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1395..1714 FT /note="Interaction with GAB2" FT /evidence="ECO:0000250" FT REGION 1688..2089 FT /note="Interaction with FYN" FT /evidence="ECO:0000250" FT REGION 1801..1865 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1881..2002 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 32..52 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 836..858 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 995..1017 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1174..1188 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1813..1848 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1915..1939 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1942..1974 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 706 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A7KAX9" FT MOD_RES 709 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 732 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 738 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 852 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 856 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 892 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A7KAX9" FT MOD_RES 952 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1206 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A7KAX9" FT MOD_RES 1526 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1536 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 1588 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2039 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT VAR_SEQ 1..349 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12819203, FT ECO:0000303|PubMed:15489334" FT /id="VSP_034937" FT MUTAGEN 58 FT /note="R->K: Does not affect RhoA or CDC42 activity." FT /evidence="ECO:0000269|PubMed:17272280" SQ 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 //