RHG32_MOUSE
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 03-AUG-2022, entry version 149.
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}.
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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; 15.
DR CORUM; Q811P8; -.
DR IntAct; Q811P8; 8.
DR MINT; Q811P8; -.
DR STRING; 10090.ENSMUSP00000133898; -.
DR iPTMnet; Q811P8; -.
DR PhosphoSitePlus; Q811P8; -.
DR SwissPalm; Q811P8; -.
DR jPOST; Q811P8; -.
DR MaxQB; Q811P8; -.
DR PaxDb; Q811P8; -.
DR PRIDE; Q811P8; -.
DR ProteomicsDB; 255209; -. [Q811P8-1]
DR ProteomicsDB; 255210; -. [Q811P8-2]
DR Antibodypedia; 51352; 97 antibodies from 15 providers.
DR DNASU; 330914; -.
DR Ensembl; ENSMUST00000168954; ENSMUSP00000128448; ENSMUSG00000041444. [Q811P8-2]
DR Ensembl; ENSMUST00000174641; ENSMUSP00000133898; ENSMUSG00000041444. [Q811P8-1]
DR Ensembl; ENSMUST00000182802; ENSMUSP00000138145; ENSMUSG00000041444. [Q811P8-2]
DR GeneID; 330914; -.
DR KEGG; mmu:330914; -.
DR UCSC; uc009orv.2; mouse. [Q811P8-1]
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; ERAHHHG; -.
DR OrthoDB; 1300981at2759; -.
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 72 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 208 other tissues.
DR ExpressionAtlas; Q811P8; baseline and differential.
DR Genevisible; Q811P8; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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: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 Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.30.1520.10; -; 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 Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
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
