ID RHG32_HUMAN Reviewed; 2087 AA. AC A7KAX9; I7H0B0; O94820; Q86YL6; Q8IUG4; Q9BWG3; DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 24-JUL-2024, entry version 148. 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=GTPase regulator interacting with TrkA; 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 Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH NTRK1; RP SHC3; BCAR1; EGFR; CRK AND CRKL, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP PHOSPHORYLATION, AND MUTAGENESIS OF ARG-407. RC TISSUE=Brain; RX PubMed=12446789; DOI=10.1128/mcb.22.24.8721-8734.2002; RA Nakamura T., Komiya M., Sone K., Hirose E., Gotoh N., Morii H., Ohta Y., RA Mori N.; RT "Grit, a GTPase-activating protein for the Rho family, regulates neurite RT extension through association with the TrkA receptor and N-Shc and CrkL/Crk RT adapter molecules."; RL Mol. Cell. Biol. 22:8721-8734(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH CTNNB1, RP AND MUTAGENESIS OF ARG-407 AND LYS-447. 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH GAB1 AND RP GAB2; BCAR1; CRK AND NCK1, AND SUBCELLULAR LOCATION. RC TISSUE=Brain; 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, FUNCTION, RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-173 AND ARG-407. 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=9872452; DOI=10.1093/dnares/5.5.277; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XI. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:277-286(1998). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Colon, and Eye; 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 [8] RP FUNCTION, INTERACTION WITH FYN, AND PHOSPHORYLATION (ISOFORM 2). RX PubMed=12788081; DOI=10.1016/s0006-291x(03)00923-9; RA Taniguchi S., Liu H., Nakazawa T., Yokoyama K., Tezuka T., Yamamoto T.; RT "p250GAP, a neural RhoGAP protein, is associated with and phosphorylated by RT Fyn."; RL Biochem. Biophys. Res. Commun. 306:151-155(2003). RN [9] RP FUNCTION, AND MUTAGENESIS OF ARG-407. 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 [10] RP FUNCTION, INTERACTION WITH GRIN2B, AND MUTAGENESIS OF ARG-407. 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 [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1203, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706 AND SER-892, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-952, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 367-577. RG Structural genomics consortium (SGC); RT "Crystal structure of the Rho-GAP domain of RICS."; RL Submitted (SEP-2009) to the PDB data bank. 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 (By similarity). {ECO:0000250, CC ECO:0000269|PubMed:12446789, ECO:0000269|PubMed:12454018, CC ECO:0000269|PubMed:12531901, ECO:0000269|PubMed:12788081, CC ECO:0000269|PubMed:12819203, ECO:0000269|PubMed:12857875, CC ECO:0000269|PubMed:17663722}. CC -!- SUBUNIT: Interacts with NTRK1 (via cytoplasmic domain); the interaction CC is independent of the phosphorylation state of NTRK1 (PubMed:12446789). CC Interacts with SHC3 (via SH2 domain) (PubMed:12446789). Interacts with CC RASA1 (via SH3 domain); the interaction is necessary for the Ras CC activation and cell transforming activities of ARHGAP32 (By CC similarity). Interacts with GAB1 and GAB2 (PubMed:12819203). Interacts CC with CRK and CRKL (PubMed:12446789, PubMed:12819203). Found in a CC complex with CRKL and BCAR1; upon EGF stimulation BCAR1 may be replaced CC by EGFR (PubMed:12446789, PubMed:12819203). Interacts with NCK1 (via CC SH3 domain); NCK1 recruits phosphorylated BCAR1 to the complex CC (PubMed:12819203). Isoform 2 interacts with FYN; the interaction CC appears to be dependent on tyrosine phosphorylation of ARHGAP32 CC (PubMed:12788081). Interacts with EGFR; the interaction requires EGF CC stimulation and is increased by SHC3 (PubMed:12446789). Interacts with CC CDC42; the interaction requires constitutively active CDC42. Interacts CC with CTNNB1 (PubMed:12531901). Interacts with GRIN2B (PubMed:12857875). CC Interacts with DLG4 and CDH2 (By similarity). Interacts with GPHN (By CC similarity). {ECO:0000250|UniProtKB:Q811P8, CC ECO:0000269|PubMed:12446789, ECO:0000269|PubMed:12531901, CC ECO:0000269|PubMed:12788081, ECO:0000269|PubMed:12819203, CC ECO:0000269|PubMed:12857875}. CC -!- INTERACTION: CC A7KAX9; Q9NYB9: ABI2; NbExp=4; IntAct=EBI-308663, EBI-743598; CC A7KAX9; P46108: CRK; NbExp=3; IntAct=EBI-308663, EBI-886; CC A7KAX9; Q86Y13: DZIP3; NbExp=3; IntAct=EBI-308663, EBI-948630; CC A7KAX9; P06241: FYN; NbExp=4; IntAct=EBI-308663, EBI-515315; CC A7KAX9; P50458: LHX2; NbExp=3; IntAct=EBI-308663, EBI-12179869; CC A7KAX9; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-308663, EBI-741037; CC A7KAX9; Q99750: MDFI; NbExp=3; IntAct=EBI-308663, EBI-724076; CC A7KAX9; O43639: NCK2; NbExp=3; IntAct=EBI-308663, EBI-713635; CC A7KAX9; P31947: SFN; NbExp=3; IntAct=EBI-308663, EBI-476295; CC A7KAX9; Q08117: TLE5; NbExp=3; IntAct=EBI-308663, EBI-717810; CC -!- SUBCELLULAR LOCATION: Postsynaptic density CC {ECO:0000250|UniProtKB:Q811P8}. Cell projection, dendritic spine CC {ECO:0000250|UniProtKB:Q811P8}. Cytoplasm, cell cortex CC {ECO:0000269|PubMed:12446789}. Endosome membrane CC {ECO:0000269|PubMed:17663722}. Golgi apparatus membrane CC {ECO:0000269|PubMed:17663722}. Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:Q811P8}. Membrane {ECO:0000269|PubMed:17663722}. CC Note=Association to membrane via PX domain (PubMed:17663722). CC Associated with cortical actin in undifferentiated neuroblastoma cells, CC but localized to dendritic spine and postsynaptic density after CC differentiation (By similarity). Colocalizes with EGFR at the cell CC membrane upon EGF treatment (PubMed:12446789). Colocalizes with GAB2 at CC the cell membrane (PubMed:12819203). {ECO:0000250|UniProtKB:Q811P8, CC ECO:0000269|PubMed:12446789, ECO:0000269|PubMed:12819203, CC ECO:0000269|PubMed:17663722}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=PX-RICS; CC IsoId=A7KAX9-1; Sequence=Displayed; CC Name=2; CC IsoId=A7KAX9-2; Sequence=VSP_034933; CC Name=3; CC IsoId=A7KAX9-3; Sequence=VSP_034934, VSP_034935, VSP_034936; CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are highly expressed in CC brain and testis. Isoform 1 is also expressed in other tissues such as CC lung, liver and spleen. {ECO:0000269|PubMed:12446789}. CC -!- DOMAIN: The N-terminal PX domain interacts specifically with CC phosphatidylinositides. {ECO:0000250}. CC -!- PTM: Isoform 2 is phosphorylated on multiple tyrosine residues by FYN. CC Phosphorylated tyrosine residues undergo dephosphorylation after CC stimulation of NMDA receptors (By similarity). Phosphorylated in vitro CC by CaMK2 in the presence of calmodulin and calcium; which inhibits GAP CC activity (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PX domain-containing GAP family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA34432.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AB079856; BAC24802.1; -; mRNA. DR EMBL; AY194287; AAO43677.1; -; mRNA. DR EMBL; AB088416; BAM34446.1; -; mRNA. DR EMBL; EF127492; ABO33171.1; -; mRNA. DR EMBL; AB018255; BAA34432.2; ALT_INIT; mRNA. DR EMBL; CH471065; EAW67740.1; -; Genomic_DNA. DR EMBL; BC000277; AAH00277.2; -; mRNA. DR EMBL; BC104898; AAI04899.1; -; mRNA. DR EMBL; BC113429; AAI13430.1; -; mRNA. DR CCDS; CCDS31718.1; -. [A7KAX9-2] DR CCDS; CCDS44769.1; -. [A7KAX9-1] DR RefSeq; NP_001136157.1; NM_001142685.1. [A7KAX9-1] DR RefSeq; NP_055530.2; NM_014715.3. [A7KAX9-2] DR PDB; 3IUG; X-ray; 1.77 A; A/B=367-577. DR PDBsum; 3IUG; -. DR AlphaFoldDB; A7KAX9; -. DR SMR; A7KAX9; -. DR BioGRID; 115091; 151. DR IntAct; A7KAX9; 49. DR MINT; A7KAX9; -. DR STRING; 9606.ENSP00000310561; -. DR GlyGen; A7KAX9; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; A7KAX9; -. DR PhosphoSitePlus; A7KAX9; -. DR BioMuta; ARHGAP32; -. DR CPTAC; CPTAC-1032; -. DR jPOST; A7KAX9; -. DR MassIVE; A7KAX9; -. DR PaxDb; 9606-ENSP00000310561; -. DR PeptideAtlas; A7KAX9; -. DR ProteomicsDB; 1805; -. [A7KAX9-1] DR ProteomicsDB; 1806; -. [A7KAX9-2] DR ProteomicsDB; 1807; -. [A7KAX9-3] DR Pumba; A7KAX9; -. DR Antibodypedia; 51352; 109 antibodies from 15 providers. DR DNASU; 9743; -. DR Ensembl; ENST00000310343.13; ENSP00000310561.8; ENSG00000134909.19. [A7KAX9-1] DR Ensembl; ENST00000392657.7; ENSP00000376425.3; ENSG00000134909.19. [A7KAX9-2] DR Ensembl; ENST00000527272.1; ENSP00000432862.1; ENSG00000134909.19. [A7KAX9-2] DR GeneID; 9743; -. DR KEGG; hsa:9743; -. DR UCSC; uc001qez.4; human. [A7KAX9-1] DR AGR; HGNC:17399; -. DR CTD; 9743; -. DR DisGeNET; 9743; -. DR GeneCards; ARHGAP32; -. DR HGNC; HGNC:17399; ARHGAP32. DR HPA; ENSG00000134909; Low tissue specificity. DR MIM; 608541; gene. DR neXtProt; NX_A7KAX9; -. DR OpenTargets; ENSG00000134909; -. DR PharmGKB; PA165543138; -. DR VEuPathDB; HostDB:ENSG00000134909; -. DR eggNOG; KOG1449; Eukaryota. DR eggNOG; KOG3564; Eukaryota. DR GeneTree; ENSGT00940000154313; -. DR HOGENOM; CLU_002754_0_0_1; -. DR InParanoid; A7KAX9; -. DR OMA; IIQVTDC; -. DR OrthoDB; 5314555at2759; -. DR PhylomeDB; A7KAX9; -. DR TreeFam; TF351451; -. DR PathwayCommons; A7KAX9; -. DR Reactome; R-HSA-8980692; RHOA GTPase cycle. DR Reactome; R-HSA-9013026; RHOB GTPase cycle. DR Reactome; R-HSA-9013106; RHOC GTPase cycle. DR Reactome; R-HSA-9013148; CDC42 GTPase cycle. DR Reactome; R-HSA-9013149; RAC1 GTPase cycle. DR Reactome; R-HSA-9013404; RAC2 GTPase cycle. DR Reactome; R-HSA-9013405; RHOD GTPase cycle. DR Reactome; R-HSA-9013406; RHOQ GTPase cycle. DR Reactome; R-HSA-9013408; RHOG GTPase cycle. DR Reactome; R-HSA-9013409; RHOJ GTPase cycle. DR Reactome; R-HSA-9013423; RAC3 GTPase cycle. DR Reactome; R-HSA-9035034; RHOF GTPase cycle. DR SignaLink; A7KAX9; -. DR SIGNOR; A7KAX9; -. DR BioGRID-ORCS; 9743; 15 hits in 1150 CRISPR screens. DR ChiTaRS; ARHGAP32; human. DR EvolutionaryTrace; A7KAX9; -. DR GeneWiki; RICS_(gene); -. DR GenomeRNAi; 9743; -. DR Pharos; A7KAX9; Tbio. DR PRO; PR:A7KAX9; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; A7KAX9; Protein. DR Bgee; ENSG00000134909; Expressed in middle temporal gyrus and 182 other cell types or tissues. DR ExpressionAtlas; A7KAX9; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central. DR GO; GO:0005938; C:cell cortex; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. 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; IDA:HPA. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB. DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central. DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IEA:InterPro. DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome. 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; IPR051576; PX-Rho_GAP. 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. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell projection; Cytoplasm; KW Endoplasmic reticulum; Endosome; Golgi apparatus; GTPase activation; KW Membrane; Methylation; Phosphoprotein; Reference proteome; SH3 domain; KW Synapse. FT CHAIN 1..2087 FT /note="Rho GTPase-activating protein 32" FT /id="PRO_0000345203" 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 818..858 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 927..1038 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1103..1143 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1169..1257 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1391..1711 FT /note="Interaction with GAB2" FT /evidence="ECO:0000269|PubMed:12819203" FT REGION 1685..2087 FT /note="Interaction with FYN" FT /evidence="ECO:0000269|PubMed:12788081" FT REGION 1798..1896 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 835..858 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 949..969 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 991..1026 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1126..1143 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1169..1184 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1185..1209 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1810..1847 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1850..1866 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1870..1887 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 706 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 709 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q811P8" FT MOD_RES 732 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q811P8" FT MOD_RES 738 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q811P8" FT MOD_RES 852 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q811P8" FT MOD_RES 856 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q811P8" FT MOD_RES 892 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 952 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1203 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 1523 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:Q811P8" FT MOD_RES 1533 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:Q811P8" FT MOD_RES 1585 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q811P8" FT MOD_RES 2037 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q811P8" FT VAR_SEQ 1..349 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12446789, FT ECO:0000303|PubMed:12531901, ECO:0000303|PubMed:12819203, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9872452" FT /id="VSP_034933" FT VAR_SEQ 1..290 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_034934" FT VAR_SEQ 567..612 FT /note="FSGRISMAMQEGAASLSRPKSLLVSSPSTKLLTLEEAQARTQAQVN -> LP FT HFSARTELIVPFPLRLLRKQFTPPLLGPMSPLNPLVQITVCISI (in isoform FT 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_034935" FT VAR_SEQ 613..2087 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_034936" FT MUTAGEN 173 FT /note="Y->A: Loss of binding to phospholipids. Cytoplasmic FT localization." FT /evidence="ECO:0000269|PubMed:17663722" FT MUTAGEN 407 FT /note="R->A: Mild effect on GAP activity and neurite- FT promotion upon nerve growth factor stimulation." FT /evidence="ECO:0000269|PubMed:12446789, FT ECO:0000269|PubMed:12454018, ECO:0000269|PubMed:12531901, FT ECO:0000269|PubMed:12857875, ECO:0000269|PubMed:17663722" FT MUTAGEN 407 FT /note="R->I: Loss of GAP activity." FT /evidence="ECO:0000269|PubMed:12446789, FT ECO:0000269|PubMed:12454018, ECO:0000269|PubMed:12531901, FT ECO:0000269|PubMed:12857875, ECO:0000269|PubMed:17663722" FT MUTAGEN 407 FT /note="R->M: Loss of GAP activity. In isoform 1, no FT inhibitory effect on neurite extension." FT /evidence="ECO:0000269|PubMed:12446789, FT ECO:0000269|PubMed:12454018, ECO:0000269|PubMed:12531901, FT ECO:0000269|PubMed:12857875, ECO:0000269|PubMed:17663722" FT MUTAGEN 447 FT /note="K->A: Loss of GAP activity." FT /evidence="ECO:0000269|PubMed:12531901" FT HELIX 374..381 FT /evidence="ECO:0007829|PDB:3IUG" FT HELIX 387..399 FT /evidence="ECO:0007829|PDB:3IUG" FT TURN 403..407 FT /evidence="ECO:0007829|PDB:3IUG" FT HELIX 412..423 FT /evidence="ECO:0007829|PDB:3IUG" FT TURN 433..437 FT /evidence="ECO:0007829|PDB:3IUG" FT HELIX 439..452 FT /evidence="ECO:0007829|PDB:3IUG" FT TURN 460..462 FT /evidence="ECO:0007829|PDB:3IUG" FT HELIX 463..470 FT /evidence="ECO:0007829|PDB:3IUG" FT STRAND 472..474 FT /evidence="ECO:0007829|PDB:3IUG" FT HELIX 475..486 FT /evidence="ECO:0007829|PDB:3IUG" FT HELIX 491..508 FT /evidence="ECO:0007829|PDB:3IUG" FT HELIX 511..514 FT /evidence="ECO:0007829|PDB:3IUG" FT HELIX 518..529 FT /evidence="ECO:0007829|PDB:3IUG" FT HELIX 553..561 FT /evidence="ECO:0007829|PDB:3IUG" FT HELIX 563..566 FT /evidence="ECO:0007829|PDB:3IUG" SQ SEQUENCE 2087 AA; 230529 MW; 075E5B4902857D06 CRC64; METESESSTL GDDSVFWLES EVIIQVTDCE EEEREEKFRK MKSSVHSEED DFVPELHRNV HPRERPDWEE TLSAMARGAD VPEIPGDLTL KTCGSTASMK VKHVKKLPFT KGHFPKMAEC AHFHYENVEF GSIQLSLSEE QNEVMKNGCE SKELVYLVQI ACQGKSWIVK RSYEDFRVLD KHLHLCIYDR RFSQLSELPR SDTLKDSPES VTQMLMAYLS RLSAIAGNKI 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 NHVDVLFSGR ISMAMQEGAA SLSRPKSLLV SSPSTKLLTL EEAQARTQAQ VNSPIVTENK YIEVGEGPAA LQGKFHTIIE FPLERKRPQN KMKKSPVGSW RSFFNLGKSS SVSKRKLQRN ESEPSEMKAM ALKGGRAEGT LRSAKSEESL TSLHAVDGDS KLFRPRRPRS SSDALSASFN GEMLGNRCNS YDNLPHDNES EEEGGLLHIP ALMSPHSAED VDLSPPDIGV ASLDFDPMSF QCSPPKAESE CLESGASFLD SPGYSKDKPS ANKKDAETGS SQCQTPGSTA SSEPVSPLQE KLSPFFTLDL SPTEDKSSKP SSFTEKVVYA FSPKIGRKLS KSPSMSISEP ISVTLPPRVS EVIGTVSNTT AQNASSSTWD KCVEERDATN RSPTQIVKMK TNETVAQEAY ESEVQPLDQV AAEEVELPGK EDQSVSSSQS KAVASGQTQT GAVTHDPPQD SVPVSSVSLI PPPPPPKNVA RMLALALAES AQQASTQSLK RPGTSQAGYT NYGDIAVATT EDNLSSSYSA VALDKAYFQT DRPAEQFHLQ NNAPGNCDHP LPETTATGDP THSNTTESGE QHHQVDLTGN QPHQAYLSGD PEKARITSVP LDSEKSDDHV SFPEDQSGKN SMPTVSFLDQ DQSPPRFYSG DQPPSYLGAS VDKLHHPLEF ADKSPTPPNL PSDKIYPPSG SPEENTSTAT MTYMTTTPAT AQMSTKEASW DVAEQPTTAD FAAATLQRTH RTNRPLPPPP SQRSAEQPPV VGQVQAATNI GLNNSHKVQG VVPVPERPPE PRAMDDPASA FISDSGAAAA QCPMATAVQP GLPEKVRDGA RVPLLHLRAE SVPAHPCGFP APLPPTRMME SKMIAAIHSS SADATSSSNY HSFVTASSTS VDDALPLPLP VPQPKHASQK TVYSSFARPD VTTEPFGPDN CLHFNMTPNC QYRPQSVPPH HNKLEQHQVY GARSEPPASM GLRYNTYVAP GRNASGHHSK PCSRVEYVSS LSSSVRNTCY PEDIPPYPTI RRVQSLHAPP SSMIRSVPIS RTEVPPDDEP AYCPRPLYQY KPYQSSQARS DYHVTQLQPY FENGRVHYRY SPYSSSSSSY YSPDGALCDV DAYGTVQLRP LHRLPNRDFA FYNPRLQGKS LYSYAGLAPR PRANVTGYFS PNDHNVVSMP PAADVKHTYT SWDLEDMEKY RMQSIRRESR ARQKVKGPVM SQYDNMTPAV QDDLGGIYVI HLRSKSDPGK TGLLSVAEGK ESRHAAKAIS PEGEDRFYRR HPEAEMDRAH HHGGHGSTQP EKPSLPQKQS SLRSRKLPDM GCSLPEHRAH QEASHRQFCE SKNGPPYPQG AGQLDYGSKG IPDTSEPVSY HNSGVKYAAS GQESLRLNHK EVRLSKEMER PWVRQPSAPE KHSRDCYKEE EHLTQSIVPP PKPERSHSLK LHHTQNVERD PSVLYQYQPH GKRQSSVTVV SQYDNLEDYH SLPQHQRGVF GGGGMGTYVP PGFPHPQSRT YATALGQGAF LPAELSLQHP ETQIHAE //