RHG32_HUMAN
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 03-AUG-2022, entry version 137.
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:12819203, PubMed:12446789). 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=4; 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; 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};
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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; 130.
DR IntAct; A7KAX9; 39.
DR MINT; A7KAX9; -.
DR STRING; 9606.ENSP00000310561; -.
DR iPTMnet; A7KAX9; -.
DR PhosphoSitePlus; A7KAX9; -.
DR BioMuta; ARHGAP32; -.
DR CPTAC; CPTAC-1032; -.
DR EPD; A7KAX9; -.
DR jPOST; A7KAX9; -.
DR MassIVE; A7KAX9; -.
DR MaxQB; A7KAX9; -.
DR PaxDb; A7KAX9; -.
DR PeptideAtlas; A7KAX9; -.
DR PRIDE; A7KAX9; -.
DR ProteomicsDB; 1805; -. [A7KAX9-1]
DR ProteomicsDB; 1806; -. [A7KAX9-2]
DR ProteomicsDB; 1807; -. [A7KAX9-3]
DR Antibodypedia; 51352; 97 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 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; ERAHHHG; -.
DR OrthoDB; 1300981at2759; -.
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; 12 hits in 1072 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 181 other tissues.
DR ExpressionAtlas; A7KAX9; baseline and differential.
DR Genevisible; A7KAX9; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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 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 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
