RHG05_HUMAN
ID RHG05_HUMAN Reviewed; 1502 AA.
AC Q13017; A1L375; A1L376; A8KAA1; D3DS89; D3DS90; Q05BE8; Q05BU8; Q59ER0;
AC Q6DHZ3;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Rho GTPase-activating protein 5;
DE AltName: Full=Rho-type GTPase-activating protein 5;
DE AltName: Full=p190-B {ECO:0000303|PubMed:28894085, ECO:0000303|PubMed:8537347};
GN Name=ARHGAP5; Synonyms=RHOGAP5;
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 1), FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Mesangial cell;
RX PubMed=8537347; DOI=10.1074/jbc.270.52.30919;
RA Burbelo P.D., Miyamoto S., Utani A., Brill S., Yamada K.M., Hall A.,
RA Yamada Y.;
RT "p190-B, a new member of the Rho GAP family, and Rho are induced to cluster
RT after integrin cross-linking.";
RL J. Biol. Chem. 270:30919-30926(1995).
RN [2]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Brain, Testis, and Uterus;
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 1-1239 (ISOFORM 1).
RC TISSUE=Trachea;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 364-1499 (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NITRATION [LARGE SCALE ANALYSIS] AT TYR-550, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pituitary adenoma;
RX PubMed=16777052; DOI=10.1016/j.ab.2006.05.024;
RA Zhan X., Desiderio D.M.;
RT "Nitroproteins from a human pituitary adenoma tissue discovered with a
RT nitrotyrosine affinity column and tandem mass spectrometry.";
RL Anal. Biochem. 354:279-289(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-765 AND SER-1202, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-968; SER-1115; SER-1176;
RP SER-1195; SER-1202 AND SER-1218, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1195 AND SER-1202, AND
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-765; SER-951 AND SER-1202,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1173 AND SER-1176, AND
RP IDENTIFICATION BY 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-590; SER-765; SER-968;
RP SER-1173; SER-1176; SER-1195; SER-1202 AND SER-1218, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1173 AND SER-1195, AND
RP IDENTIFICATION BY 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 STRUCTURE BY NMR OF 1245-1456.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the N-terminus extended RhoGAP domain from human Rho
RT GTPase activating protein 5 variant.";
RL Submitted (AUG-2007) to the PDB data bank.
RN [17] {ECO:0007744|PDB:5U4V}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 590-763, AND DOMAIN.
RX PubMed=28894085; DOI=10.1038/s41467-017-00483-x;
RA Stiegler A.L., Boggon T.J.;
RT "p190RhoGAP proteins contain pseudoGTPase domains.";
RL Nat. Commun. 8:506-506(2017).
CC -!- FUNCTION: GTPase-activating protein for Rho family members
CC (PubMed:8537347). {ECO:0000269|PubMed:8537347}.
CC -!- SUBUNIT: May interact with RASA1/p120GAP. {ECO:0000305|PubMed:8537347}.
CC -!- INTERACTION:
CC Q13017; P61588: Rnd3; Xeno; NbExp=2; IntAct=EBI-7237884, EBI-6930266;
CC Q13017-1; Q8IZD9: DOCK3; NbExp=2; IntAct=EBI-25409992, EBI-1752361;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8537347}. Cell
CC membrane {ECO:0000269|PubMed:8537347}; Peripheral membrane protein
CC {ECO:0000269|PubMed:8537347}. Note=Also membrane-associated in a
CC fibrillar pattern that colocalizes with the alpha5-beta1 integrin
CC receptor (ITGA5/ITGB1) for fibronectin. {ECO:0000269|PubMed:8537347}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q13017-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13017-2; Sequence=VSP_034166;
CC Name=3;
CC IsoId=Q13017-3; Sequence=VSP_034164, VSP_034167;
CC Name=4;
CC IsoId=Q13017-4; Sequence=VSP_034165;
CC -!- TISSUE SPECIFICITY: Detected in skin fibroblasts (at protein level)
CC (PubMed:8537347). {ECO:0000269|PubMed:8537347}.
CC -!- DOMAIN: The pG1 pseudoGTPase domain does not bind GTP.
CC {ECO:0000269|PubMed:28894085}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA95963.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH32723.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; U17032; AAA95963.1; ALT_FRAME; mRNA.
DR EMBL; CH471078; EAW65935.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65936.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65937.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65938.1; -; Genomic_DNA.
DR EMBL; BC032723; AAH32723.1; ALT_SEQ; mRNA.
DR EMBL; BC050059; AAH50059.1; -; mRNA.
DR EMBL; BC075799; AAH75799.1; -; mRNA.
DR EMBL; BC129928; AAI29929.1; -; mRNA.
DR EMBL; BC129929; AAI29930.1; -; mRNA.
DR EMBL; AK292966; BAF85655.1; -; mRNA.
DR EMBL; AB209751; BAD92988.1; -; mRNA.
DR CCDS; CCDS32062.1; -. [Q13017-1]
DR CCDS; CCDS45095.1; -. [Q13017-2]
DR PIR; B59431; B59431.
DR RefSeq; NP_001025226.1; NM_001030055.1. [Q13017-1]
DR RefSeq; NP_001164.2; NM_001173.2. [Q13017-2]
DR RefSeq; XP_005267692.1; XM_005267635.3. [Q13017-1]
DR RefSeq; XP_005267693.1; XM_005267636.3. [Q13017-1]
DR RefSeq; XP_016876776.1; XM_017021287.1.
DR RefSeq; XP_016876777.1; XM_017021288.1. [Q13017-2]
DR PDB; 2EE4; NMR; -; A=1255-1456.
DR PDB; 2EE5; NMR; -; A=1245-1456.
DR PDB; 5U4V; X-ray; 2.60 A; A=590-763.
DR PDBsum; 2EE4; -.
DR PDBsum; 2EE5; -.
DR PDBsum; 5U4V; -.
DR AlphaFoldDB; Q13017; -.
DR BMRB; Q13017; -.
DR SMR; Q13017; -.
DR BioGRID; 106887; 39.
DR IntAct; Q13017; 12.
DR MINT; Q13017; -.
DR STRING; 9606.ENSP00000371897; -.
DR iPTMnet; Q13017; -.
DR PhosphoSitePlus; Q13017; -.
DR BioMuta; ARHGAP5; -.
DR DMDM; 190358871; -.
DR EPD; Q13017; -.
DR jPOST; Q13017; -.
DR MassIVE; Q13017; -.
DR MaxQB; Q13017; -.
DR PaxDb; Q13017; -.
DR PeptideAtlas; Q13017; -.
DR PRIDE; Q13017; -.
DR ProteomicsDB; 59102; -. [Q13017-1]
DR ProteomicsDB; 59103; -. [Q13017-2]
DR ProteomicsDB; 59104; -. [Q13017-3]
DR ProteomicsDB; 59105; -. [Q13017-4]
DR Antibodypedia; 23106; 158 antibodies from 28 providers.
DR DNASU; 394; -.
DR Ensembl; ENST00000345122.8; ENSP00000371897.1; ENSG00000100852.14. [Q13017-1]
DR Ensembl; ENST00000396582.6; ENSP00000379827.2; ENSG00000100852.14. [Q13017-3]
DR Ensembl; ENST00000433497.5; ENSP00000407395.1; ENSG00000100852.14. [Q13017-4]
DR Ensembl; ENST00000539826.6; ENSP00000441692.2; ENSG00000100852.14. [Q13017-1]
DR Ensembl; ENST00000556611.5; ENSP00000452222.1; ENSG00000100852.14. [Q13017-2]
DR GeneID; 394; -.
DR KEGG; hsa:394; -.
DR MANE-Select; ENST00000345122.8; ENSP00000371897.1; NM_001030055.2; NP_001025226.1.
DR UCSC; uc001wrl.4; human. [Q13017-1]
DR CTD; 394; -.
DR DisGeNET; 394; -.
DR GeneCards; ARHGAP5; -.
DR HGNC; HGNC:675; ARHGAP5.
DR HPA; ENSG00000100852; Low tissue specificity.
DR MIM; 602680; gene.
DR neXtProt; NX_Q13017; -.
DR OpenTargets; ENSG00000100852; -.
DR PharmGKB; PA24959; -.
DR VEuPathDB; HostDB:ENSG00000100852; -.
DR eggNOG; KOG4271; Eukaryota.
DR GeneTree; ENSGT00940000154553; -.
DR HOGENOM; CLU_004268_0_0_1; -.
DR InParanoid; Q13017; -.
DR OMA; TFNPPIR; -.
DR OrthoDB; 110157at2759; -.
DR PhylomeDB; Q13017; -.
DR TreeFam; TF324451; -.
DR PathwayCommons; Q13017; -.
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-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 Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR Reactome; R-HSA-9696273; RND1 GTPase cycle.
DR SignaLink; Q13017; -.
DR SIGNOR; Q13017; -.
DR BioGRID-ORCS; 394; 29 hits in 1081 CRISPR screens.
DR ChiTaRS; ARHGAP5; human.
DR EvolutionaryTrace; Q13017; -.
DR GeneWiki; ARHGAP5; -.
DR GenomeRNAi; 394; -.
DR Pharos; Q13017; Tbio.
DR PRO; PR:Q13017; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q13017; protein.
DR Bgee; ENSG00000100852; Expressed in calcaneal tendon and 203 other tissues.
DR ExpressionAtlas; Q13017; baseline and differential.
DR Genevisible; Q13017; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR GO; GO:0042169; F:SH2 domain binding; IPI:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0030879; P:mammary gland development; IEA:Ensembl.
DR GO; GO:0008361; P:regulation of cell size; IBA:GO_Central.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central.
DR Gene3D; 1.10.10.440; -; 3.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002713; FF_domain.
DR InterPro; IPR036517; FF_domain_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039007; pG1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR032835; RhoGAP-FF1.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR045786; RhoGAP_pG1_pG2.
DR InterPro; IPR039006; RhoGAP_pG2.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF01846; FF; 1.
DR Pfam; PF00071; Ras; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF16512; RhoGAP-FF1; 1.
DR Pfam; PF19518; RhoGAP_pG1_pG2; 1.
DR SMART; SM00441; FF; 4.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF81698; SSF81698; 1.
DR PROSITE; PS51676; FF; 4.
DR PROSITE; PS51852; PG1; 1.
DR PROSITE; PS51853; PG2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm;
KW GTPase activation; Membrane; Nitration; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..1502
FT /note="Rho GTPase-activating protein 5"
FT /id="PRO_0000056702"
FT DOMAIN 267..325
FT /note="FF 1"
FT DOMAIN 366..420
FT /note="FF 2"
FT DOMAIN 427..481
FT /note="FF 3"
FT DOMAIN 482..548
FT /note="FF 4"
FT DOMAIN 590..763
FT /note="pG1 pseudoGTPase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01199"
FT DOMAIN 779..944
FT /note="pG2 pseudoGTPase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01200"
FT DOMAIN 1262..1449
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 975..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1248
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 550
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0007744|PubMed:16777052"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 951
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 968
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..1265
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034164"
FT VAR_SEQ 1..1261
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034165"
FT VAR_SEQ 1240
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_034166"
FT VAR_SEQ 1266..1288
FT /note="DLVTAEKPIPLFVEKCVEFIEDT -> MSLPPPPPGPLPLRRRRRRPTLL
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034167"
FT VARIANT 17
FT /note="I -> V (in dbSNP:rs17386818)"
FT /id="VAR_043980"
FT CONFLICT 80
FT /note="Q -> R (in Ref. 3; AAH50059)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="E -> G (in Ref. 4; BAF85655)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="L -> F (in Ref. 5; BAD92988)"
FT /evidence="ECO:0000305"
FT CONFLICT 620
FT /note="D -> G (in Ref. 4; BAF85655)"
FT /evidence="ECO:0000305"
FT CONFLICT 1383
FT /note="D -> G (in Ref. 3; AAH50059)"
FT /evidence="ECO:0000305"
FT STRAND 595..601
FT /evidence="ECO:0007829|PDB:5U4V"
FT HELIX 606..615
FT /evidence="ECO:0007829|PDB:5U4V"
FT STRAND 622..625
FT /evidence="ECO:0007829|PDB:5U4V"
FT STRAND 628..637
FT /evidence="ECO:0007829|PDB:5U4V"
FT STRAND 656..664
FT /evidence="ECO:0007829|PDB:5U4V"
FT HELIX 665..683
FT /evidence="ECO:0007829|PDB:5U4V"
FT STRAND 696..701
FT /evidence="ECO:0007829|PDB:5U4V"
FT HELIX 711..725
FT /evidence="ECO:0007829|PDB:5U4V"
FT STRAND 729..732
FT /evidence="ECO:0007829|PDB:5U4V"
FT HELIX 743..760
FT /evidence="ECO:0007829|PDB:5U4V"
FT STRAND 1258..1262
FT /evidence="ECO:0007829|PDB:2EE4"
FT HELIX 1264..1267
FT /evidence="ECO:0007829|PDB:2EE4"
FT HELIX 1276..1287
FT /evidence="ECO:0007829|PDB:2EE4"
FT TURN 1293..1297
FT /evidence="ECO:0007829|PDB:2EE4"
FT HELIX 1302..1314
FT /evidence="ECO:0007829|PDB:2EE4"
FT HELIX 1320..1323
FT /evidence="ECO:0007829|PDB:2EE4"
FT HELIX 1327..1340
FT /evidence="ECO:0007829|PDB:2EE4"
FT STRAND 1341..1343
FT /evidence="ECO:0007829|PDB:2EE4"
FT TURN 1348..1350
FT /evidence="ECO:0007829|PDB:2EE4"
FT HELIX 1351..1358
FT /evidence="ECO:0007829|PDB:2EE4"
FT HELIX 1363..1373
FT /evidence="ECO:0007829|PDB:2EE4"
FT TURN 1374..1376
FT /evidence="ECO:0007829|PDB:2EE4"
FT HELIX 1381..1397
FT /evidence="ECO:0007829|PDB:2EE4"
FT HELIX 1399..1402
FT /evidence="ECO:0007829|PDB:2EE4"
FT HELIX 1406..1417
FT /evidence="ECO:0007829|PDB:2EE4"
FT STRAND 1425..1427
FT /evidence="ECO:0007829|PDB:2EE5"
FT HELIX 1434..1443
FT /evidence="ECO:0007829|PDB:2EE4"
FT HELIX 1445..1448
FT /evidence="ECO:0007829|PDB:2EE4"
SQ SEQUENCE 1502 AA; 172460 MW; 2E01B5B1D007984D CRC64;
MMAKNKEPRP PSYTISIVGL SGTEKDKGNC GVGKSCLCNR FVRSKADEYY PEHTSVLSTI
DFGGRVVNND HFLYWGDIIQ NSEDGVECKI HVIEQTEFID DQTFLPHRST NLQPYIKRAA
ASKLQSAEKL MYICTDQLGL EQDFEQKQMP EGKLNVDGFL LCIDVSQGCN RKFDDQLKFV
NNLFVQLSKS KKPVIIAATK CDECVDHYLR EVQAFASNKK NLLVVETSAR FNVNIETCFT
ALVQMLDKTR SKPKIIPYLD AYKTQRQLVV TATDKFEKLV QTVRDYHATW KTVSNKLKNH
PDYEEYINLE GTRKARNTFS KHIEQLKQEH IRKRREEYIN TLPRAFNTLL PNLEEIEHLN
WSEALKLMEK RADFQLCFVV LEKTPWDETD HIDKINDRRI PFDLLSTLEA EKVYQNHVQH
LISEKRRVEM KEKFKKTLEK IQFISPGQPW EEVMCFVMED EAYKYITEAD SKEVYGRHQR
EIVEKAKEEF QEMLFEHSEL FYDLDLNATP SSDKMSEIHT VLSEEPRYKA LQKLAPDRES
LLLKHIGFVY HPTKETCLSG QNCTDIKVEQ LLASSLLQLD HGRLRLYHDS TNIDKVNLFI
LGKDGLAQEL ANEIRTQSTD DEYALDGKIY ELDLRPVDAK SPYFLSQLWT AAFKPHGCFC
VFNSIESLSF IGEFIGKIRT EASQIRKDKY MANLPFTLIL ANQRDSISKN LPILRHQGQQ
LANKLQCPFV DVPAGTYPRK FNETQIKQAL RGVLESVKHN LDVVSPIPAN KDLSEADLRI
VMCAMCGDPF SVDLILSPFL DSHSCSAAQA GQNNSLMLDK IIGEKRRRIQ ITILSYHSSI
GVRKDELVHG YILVYSAKRK ASMGMLRAFL SEVQDTIPVQ LVAVTDSQAD FFENEAIKEL
MTEGEHIATE ITAKFTALYS LSQYHRQTEV FTLFFSDVLE KKNMIENSYL SDNTRESTHQ
SEDVFLPSPR DCFPYNNYPD SDDDTEAPPP YSPIGDDVQL LPTPSDRSRY RLDLEGNEYP
IHSTPNCHDH ERNHKVPPPI KPKPVVPKTN VKKLDPNLLK TIEAGIGKNP RKQTSRVPLA
HPEDMDPSDN YAEPIDTIFK QKGYSDEIYV VPDDSQNRIK IRNSFVNNTQ GDEENGFSDR
TSKSHGERRP SKYKYKSKTL FSKAKSYYRR THSDASDDEA FTTSKTKRKG RHRGSEEDPL
LSPVETWKGG IDNPAITSDQ ELDDKKMKKK THKVKEDKKQ KKKTKNFNPP TRRNWESNYF
GMPLQDLVTA EKPIPLFVEK CVEFIEDTGL CTEGLYRVSG NKTDQDNIQK QFDQDHNINL
VSMEVTVNAV AGALKAFFAD LPDPLIPYSL HPELLEAAKI PDKTERLHAL KEIVKKFHPV
NYDVFRYVIT HLNRVSQQHK INLMTADNLS ICFWPTLMRP DFENREFLST TKIHQSVVET
FIQQCQFFFY NGEIVETTNI VAPPPPSNPG QLVEPMVPLQ LPPPLQPQLI QPQLQTDPLG
II
