RHG09_HUMAN
ID RHG09_HUMAN Reviewed; 750 AA.
AC Q9BRR9; B4DVI3; E9PDX9; Q8NAF3; Q8TCJ3; Q8WYR0; Q96EZ2; Q96S74;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Rho GTPase-activating protein 9;
DE AltName: Full=Rho-type GTPase-activating protein 9;
GN Name=ARHGAP9;
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, AND TISSUE SPECIFICITY.
RX PubMed=11396949; DOI=10.1006/bbrc.2001.5022;
RA Furukawa Y., Kawasoe T., Daigo Y., Nishiwaki T., Ishiguro H., Takahashi M.,
RA Kitayama J., Nakamura Y.;
RT "Isolation of a novel human gene, ARHGAP9, encoding a rho-GTPase activating
RT protein.";
RL Biochem. Biophys. Res. Commun. 284:643-649(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Kawasoe T., Furukawa Y., Daigo Y., Nishiwaki T., Ishiguro H., Fujita M.,
RA Ogawa M., Nakamura Y.;
RT "Isolation, mapping, and characterization of a novel member of human rho-
RT GAP family.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), AND VARIANT
RP ALA-370.
RC TISSUE=Small intestine, and Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ALA-370.
RC TISSUE=Lymph, and Muscle;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 384-750 (ISOFORM 2).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP INTERACTION WITH FASLG.
RX PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA Voss M., Lettau M., Janssen O.;
RT "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT phage display screening.";
RL BMC Immunol. 10:53-53(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475 AND SER-500, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 321-440 IN COMPLEXES WITH
RP PHOSPHATIDYLINOSITOL 1,4,5-TRISPHOSPHATE AND PHOSPHATIDYLINOSITOL
RP 1,3,4-TRISPHOSPHATE, DOMAIN, MUTAGENESIS OF LYS-343 AND ARG-399, AND
RP LIPID-BINDING.
RX PubMed=17339315; DOI=10.1074/jbc.m700505200;
RA Ceccarelli D.F., Blasutig I.M., Goudreault M., Li Z., Ruston J., Pawson T.,
RA Sicheri F.;
RT "Non-canonical interaction of phosphoinositides with pleckstrin homology
RT domains of Tiam1 and ArhGAP9.";
RL J. Biol. Chem. 282:13864-13874(2007).
CC -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting them
CC to an inactive GDP-bound state. Has a substantial GAP activity toward
CC CDC42 and RAC1 and less toward RHOA. Has a role in regulating adhesion
CC of hematopoietic cells to the extracellular matrix. Binds
CC phosphoinositides, and has the highest affinity for
CC phosphatidylinositol 3,4,5-trisphosphate, followed by
CC phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-
CC bisphosphate. {ECO:0000269|PubMed:11396949}.
CC -!- SUBUNIT: Interacts with FASLG. {ECO:0000269|PubMed:19807924}.
CC -!- INTERACTION:
CC Q9BRR9; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-750254, EBI-742038;
CC Q9BRR9; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-750254, EBI-3867333;
CC Q9BRR9; Q14192: FHL2; NbExp=3; IntAct=EBI-750254, EBI-701903;
CC Q9BRR9; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-750254, EBI-11163335;
CC Q9BRR9; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-750254, EBI-5916454;
CC Q9BRR9; P62993: GRB2; NbExp=3; IntAct=EBI-750254, EBI-401755;
CC Q9BRR9; Q96DV4: MRPL38; NbExp=3; IntAct=EBI-750254, EBI-720441;
CC Q9BRR9; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-750254, EBI-744782;
CC Q9BRR9; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-750254, EBI-11984663;
CC Q9BRR9; P09234: SNRPC; NbExp=3; IntAct=EBI-750254, EBI-766589;
CC Q9BRR9; Q9Y3Q8: TSC22D4; NbExp=3; IntAct=EBI-750254, EBI-739485;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9BRR9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BRR9-2; Sequence=VSP_010325;
CC Name=3;
CC IsoId=Q9BRR9-3; Sequence=VSP_010340;
CC Name=4;
CC IsoId=Q9BRR9-4; Sequence=VSP_010340, VSP_010325;
CC Name=5;
CC IsoId=Q9BRR9-5; Sequence=VSP_010325, VSP_046391;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in peripheral blood
CC leukocytes, spleen, and thymus. {ECO:0000269|PubMed:11396949}.
CC -!- DOMAIN: A region including the PH domain and partially overlapping with
CC the Rho-GAP domain mediates interaction with phosphoinositides.
CC {ECO:0000269|PubMed:17339315}.
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DR EMBL; AB051853; BAB56159.1; -; mRNA.
DR EMBL; AB030239; BAB83128.1; -; mRNA.
DR EMBL; AK092763; BAC03969.1; -; mRNA.
DR EMBL; AK301095; BAG62695.1; -; mRNA.
DR EMBL; AC022506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006107; AAH06107.1; -; mRNA.
DR EMBL; BC011820; AAH11820.1; -; mRNA.
DR EMBL; AL713803; CAD28552.1; -; mRNA.
DR CCDS; CCDS44928.1; -. [Q9BRR9-4]
DR CCDS; CCDS44929.1; -. [Q9BRR9-5]
DR CCDS; CCDS81705.1; -. [Q9BRR9-1]
DR CCDS; CCDS8941.2; -. [Q9BRR9-2]
DR PIR; JC7701; JC7701.
DR RefSeq; NP_001073625.1; NM_001080156.2. [Q9BRR9-4]
DR RefSeq; NP_001073626.1; NM_001080157.1. [Q9BRR9-5]
DR RefSeq; NP_001306779.1; NM_001319850.1. [Q9BRR9-1]
DR RefSeq; NP_001306780.1; NM_001319851.1.
DR RefSeq; NP_001306781.1; NM_001319852.1. [Q9BRR9-3]
DR RefSeq; NP_115885.2; NM_032496.3. [Q9BRR9-2]
DR RefSeq; XP_005269140.1; XM_005269083.2. [Q9BRR9-3]
DR RefSeq; XP_011536958.1; XM_011538656.2. [Q9BRR9-2]
DR RefSeq; XP_011536961.1; XM_011538659.2. [Q9BRR9-5]
DR RefSeq; XP_016875289.1; XM_017019800.1. [Q9BRR9-3]
DR RefSeq; XP_016875290.1; XM_017019801.1.
DR PDB; 2P0D; X-ray; 1.81 A; A=321-440.
DR PDB; 2P0F; X-ray; 1.91 A; A=321-440.
DR PDB; 2P0H; X-ray; 1.90 A; A=321-440.
DR PDBsum; 2P0D; -.
DR PDBsum; 2P0F; -.
DR PDBsum; 2P0H; -.
DR AlphaFoldDB; Q9BRR9; -.
DR SMR; Q9BRR9; -.
DR BioGRID; 122140; 43.
DR IntAct; Q9BRR9; 30.
DR MINT; Q9BRR9; -.
DR STRING; 9606.ENSP00000377380; -.
DR GlyConnect; 1716; 1 N-Linked glycan (1 site).
DR GlyGen; Q9BRR9; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q9BRR9; -.
DR PhosphoSitePlus; Q9BRR9; -.
DR BioMuta; ARHGAP9; -.
DR DMDM; 47117294; -.
DR jPOST; Q9BRR9; -.
DR MassIVE; Q9BRR9; -.
DR MaxQB; Q9BRR9; -.
DR PaxDb; Q9BRR9; -.
DR PeptideAtlas; Q9BRR9; -.
DR PRIDE; Q9BRR9; -.
DR ProteomicsDB; 19770; -.
DR ProteomicsDB; 78819; -. [Q9BRR9-1]
DR ProteomicsDB; 78820; -. [Q9BRR9-2]
DR ProteomicsDB; 78821; -. [Q9BRR9-3]
DR ProteomicsDB; 78822; -. [Q9BRR9-4]
DR Antibodypedia; 28612; 68 antibodies from 21 providers.
DR DNASU; 64333; -.
DR Ensembl; ENST00000393791.8; ENSP00000377380.3; ENSG00000123329.20. [Q9BRR9-2]
DR Ensembl; ENST00000393797.7; ENSP00000377386.3; ENSG00000123329.20. [Q9BRR9-1]
DR Ensembl; ENST00000424809.6; ENSP00000394307.2; ENSG00000123329.20. [Q9BRR9-5]
DR Ensembl; ENST00000430041.6; ENSP00000397950.2; ENSG00000123329.20. [Q9BRR9-4]
DR GeneID; 64333; -.
DR KEGG; hsa:64333; -.
DR MANE-Select; ENST00000393791.8; ENSP00000377380.3; NM_032496.4; NP_115885.2. [Q9BRR9-2]
DR UCSC; uc001snz.4; human. [Q9BRR9-1]
DR CTD; 64333; -.
DR DisGeNET; 64333; -.
DR GeneCards; ARHGAP9; -.
DR HGNC; HGNC:14130; ARHGAP9.
DR HPA; ENSG00000123329; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; ARHGAP9; -.
DR MIM; 610576; gene.
DR neXtProt; NX_Q9BRR9; -.
DR OpenTargets; ENSG00000123329; -.
DR PharmGKB; PA24962; -.
DR VEuPathDB; HostDB:ENSG00000123329; -.
DR eggNOG; KOG1450; Eukaryota.
DR GeneTree; ENSGT00950000182860; -.
DR HOGENOM; CLU_015883_6_1_1; -.
DR InParanoid; Q9BRR9; -.
DR OMA; RIDWARD; -.
DR OrthoDB; 1300981at2759; -.
DR PhylomeDB; Q9BRR9; -.
DR TreeFam; TF329345; -.
DR PathwayCommons; Q9BRR9; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR SignaLink; Q9BRR9; -.
DR SIGNOR; Q9BRR9; -.
DR BioGRID-ORCS; 64333; 29 hits in 1066 CRISPR screens.
DR EvolutionaryTrace; Q9BRR9; -.
DR GeneWiki; ARHGAP9; -.
DR GenomeRNAi; 64333; -.
DR Pharos; Q9BRR9; Tbio.
DR PRO; PR:Q9BRR9; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9BRR9; protein.
DR Bgee; ENSG00000123329; Expressed in granulocyte and 164 other tissues.
DR ExpressionAtlas; Q9BRR9; baseline and differential.
DR Genevisible; Q9BRR9; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd12143; SH3_ARHGAP9; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035465; ARHGAP9_SH3.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
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 InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; GTPase activation; Lipid-binding;
KW Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..750
FT /note="Rho GTPase-activating protein 9"
FT /id="PRO_0000056712"
FT DOMAIN 22..88
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 213..247
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 322..435
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 542..749
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 120..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..345
FT /note="Lipid binding"
FT REGION 397..399
FT /note="Lipid binding"
FT REGION 432..669
FT /note="Lipid binding"
FT REGION 446..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..184
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_010340"
FT VAR_SEQ 438..456
FT /note="Missing (in isoform 2, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:11396949,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_010325"
FT VAR_SEQ 659..750
FT /note="ALSESEQCLSQIQELIGSMPKPNHDTLRYLLEHLCRVIAHSDKNRMTPHNLG
FT IVFGPTLFRPEQETSDPAAHALYPGQLVQLMLTNFTSLFP -> G (in isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046391"
FT VARIANT 50
FT /note="R -> G (in dbSNP:rs33927108)"
FT /id="VAR_055830"
FT VARIANT 137
FT /note="R -> C (in dbSNP:rs3802989)"
FT /id="VAR_055831"
FT VARIANT 370
FT /note="S -> A (in dbSNP:rs11544238)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_055832"
FT MUTAGEN 343
FT /note="K->A: Strongly reduced affinity for
FT phosphoinositides."
FT /evidence="ECO:0000269|PubMed:17339315"
FT MUTAGEN 399
FT /note="R->A: Reduced affinity for phosphoinositides."
FT /evidence="ECO:0000269|PubMed:17339315"
FT CONFLICT 152
FT /note="L -> F (in Ref. 2; AAH06107)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="V -> A (in Ref. 3; BAC03969)"
FT /evidence="ECO:0000305"
FT STRAND 322..336
FT /evidence="ECO:0007829|PDB:2P0D"
FT STRAND 346..361
FT /evidence="ECO:0007829|PDB:2P0D"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:2P0H"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:2P0D"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:2P0D"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:2P0H"
FT STRAND 398..406
FT /evidence="ECO:0007829|PDB:2P0D"
FT STRAND 412..416
FT /evidence="ECO:0007829|PDB:2P0D"
FT HELIX 420..439
FT /evidence="ECO:0007829|PDB:2P0D"
SQ SEQUENCE 750 AA; 83260 MW; 7E769DBC3678DB49 CRC64;
MLSSRWWPSS WGILGLGPRS PPRGSQLCAL YAFTYTGADG QQVSLAEGDR FLLLRKTNSD
WWLARRLEAP STSRPIFVPA AYMIEESIPS QSPTTVIPGQ LLWTPGPKLF HGSLEELSQA
LPSRAQASSE QPPPLPRKMC RSVSTDNLSP SLLKPFQEGP SGRSLSQEDL PSEASASTAG
PQPLMSEPPV YCNLVDLRRC PRSPPPGPAC PLLQRLDAWE QHLDPNSGRC FYINSLTGCK
SWKPPRRSRS ETNPGSMEGT QTLKRNNDVL QPQAKGFRSD TGTPEPLDPQ GSLSLSQRTS
QLDPPALQAP RPLPQLLDDP HEVEKSGLLN MTKIAQGGRK LRKNWGPSWV VLTGNSLVFY
REPPPTAPSS GWGPAGSRPE SSVDLRGAAL AHGRHLSSRR NVLHIRTIPG HEFLLQSDHE
TELRAWHRAL RTVIERLVRW VEARREAPTG RDQGSGDREN PLELRLSGSG PAELSAGEDE
EEESELVSKP LLRLSSRRSS IRGPEGTEQN RVRNKLKRLI AKRPPLQSLQ ERGLLRDQVF
GCQLESLCQR EGDTVPSFLR LCIAAVDKRG LDVDGIYRVS GNLAVVQKLR FLVDRERAVT
SDGRYVFPEQ PGQEGRLDLD STEWDDIHVV TGALKLFLRE LPQPLVPPLL LPHFRAALAL
SESEQCLSQI QELIGSMPKP NHDTLRYLLE HLCRVIAHSD KNRMTPHNLG IVFGPTLFRP
EQETSDPAAH ALYPGQLVQL MLTNFTSLFP
