RHG21_HUMAN
ID RHG21_HUMAN Reviewed; 1958 AA.
AC Q5T5U3; Q0VF98; Q7Z3P7; Q8N3A2; Q8NI19; Q8TBV5; Q9P2C3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Rho GTPase-activating protein 21;
DE AltName: Full=Rho GTPase-activating protein 10;
DE AltName: Full=Rho-type GTPase-activating protein 21;
GN Name=ARHGAP21; Synonyms=ARHGAP10, KIAA1424;
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), TISSUE SPECIFICITY, INDUCTION, AND
RP VARIANT SER-713.
RC TISSUE=Brain;
RX PubMed=12056806; DOI=10.1016/s0006-291x(02)00514-4;
RA Basseres D.S., Tizzei E.V., Duarte A.A.S., Costa F.F., Saad S.T.O.;
RT "ARHGAP10, a novel human gene coding for a potentially cytoskeletal Rho-
RT GTPase activating protein.";
RL Biochem. Biophys. Res. Commun. 294:579-585(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-1958 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 162-1958 (ISOFORM 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 638-1958 (ISOFORM 1), AND VARIANT SER-713.
RC TISSUE=Amygdala, and Cervix;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1523-1958 (ISOFORM 1).
RC TISSUE=Urinary bladder;
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 [7]
RP IDENTIFICATION.
RX PubMed=15375573; DOI=10.3892/ijo.25.4.1201;
RA Katoh M., Katoh M.;
RT "Characterization of human ARHGAP10 gene in silico.";
RL Int. J. Oncol. 25:1201-1206(2004).
RN [8]
RP FUNCTION, INTERACTION WITH ARF1 AND ARF6, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ARG-1184.
RX PubMed=15793564; DOI=10.1038/ncb1244;
RA Dubois T., Paleotti O., Mironov A.A. Jr., Fraisier V., Stradal T.E.B.,
RA De Matteis M.A., Franco M., Chavrier P.;
RT "Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control
RT Arp2/3 complex and F-actin dynamics.";
RL Nat. Cell Biol. 7:353-364(2005).
RN [9]
RP FUNCTION, INTERACTION WITH CTNNA1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ARG-1184.
RX PubMed=16184169; DOI=10.1038/ncb1308;
RA Sousa S., Cabanes D., Archambaud C., Colland F., Lemichez E., Popoff M.,
RA Boisson-Dupuis S., Gouin E., Lecuit M., Legrain P., Cossart P.;
RT "ARHGAP10 is necessary for alpha-catenin recruitment at adherens junctions
RT and for Listeria invasion.";
RL Nat. Cell Biol. 7:954-960(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP INTERACTION WITH ARF6.
RX PubMed=16527809; DOI=10.1074/jbc.m601021200;
RA Klein S., Franco M., Chardin P., Luton F.;
RT "Role of the Arf6 GDP/GTP cycle and Arf6 GTPase-activating proteins in
RT actin remodeling and intracellular transport.";
RL J. Biol. Chem. 281:12352-12361(2006).
RN [12]
RP IDENTIFICATION.
RX PubMed=16261155; DOI=10.1038/sj.onc.1209203;
RA Carles A., Millon R., Cromer A., Ganguli G., Lemaire F., Young J.,
RA Wasylyk C., Muller D., Schultz I., Rabouel Y., Dembele D., Zhao C.,
RA Marchal P., Ducray C., Bracco L., Abecassis J., Poch O., Wasylyk B.;
RT "Head and neck squamous cell carcinoma transcriptome analysis by
RT comprehensive validated differential display.";
RL Oncogene 25:1821-1831(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459; SER-924 AND SER-1669,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-717; SER-857;
RP SER-1432; SER-1433 AND SER-1527, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [17]
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 [18]
RP SUMOYLATION AT LYS-1444.
RX PubMed=22922005; DOI=10.1016/j.febslet.2012.08.012;
RA Bigarella C.L., Vieira Ferro K.P., Barcellos K.S., Martins-de-Souza D.,
RA Traina F., Novello J.C., Olalla Saad S.T., Archangelo L.F.;
RT "Post-translational modification of the RhoGTPase activating protein 21,
RT ARHGAP21, by SUMO2/3.";
RL FEBS Lett. 586:3522-3528(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612; SER-616; SER-625;
RP THR-747; SER-857; SER-881; SER-924; SER-954; SER-1115; SER-1418; SER-1432;
RP SER-1433; SER-1504; SER-1527; SER-1669 AND SER-1742, 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-882 AND THR-1516, 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 [21]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-554 AND ARG-575, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 930-1097 IN COMPLEX WITH ARF1,
RP MUTAGENESIS OF TYR-1000 AND ILE-1054, AND SUBCELLULAR LOCATION.
RX PubMed=17347647; DOI=10.1038/sj.emboj.7601634;
RA Menetrey J., Perderiset M., Cicolari J., Dubois T., Elkhatib N.,
RA El Khadali F., Franco M., Chavrier P., Houdusse A.;
RT "Structural basis for ARF1-mediated recruitment of ARHGAP21 to Golgi
RT membranes.";
RL EMBO J. 26:1953-1962(2007).
RN [23]
RP STRUCTURE BY NMR OF 931-1042.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PH domain of Rho GTPase-activating protein 21
RT from human.";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- FUNCTION: Functions as a GTPase-activating protein (GAP) for RHOA and
CC CDC42. Downstream partner of ARF1 which may control Golgi apparatus
CC structure and function. Also required for CTNNA1 recruitment to
CC adherens junctions. {ECO:0000269|PubMed:15793564,
CC ECO:0000269|PubMed:16184169}.
CC -!- SUBUNIT: Interacts with GTP-bound ARF1 and ARF6. Interacts with CTNNA1.
CC {ECO:0000269|PubMed:15793564, ECO:0000269|PubMed:16184169,
CC ECO:0000269|PubMed:16527809, ECO:0000269|PubMed:17347647}.
CC -!- INTERACTION:
CC Q5T5U3; P29692: EEF1D; NbExp=2; IntAct=EBI-1642518, EBI-358607;
CC Q5T5U3; P63104: YWHAZ; NbExp=2; IntAct=EBI-1642518, EBI-347088;
CC Q5T5U3; P84078: Arf1; Xeno; NbExp=3; IntAct=EBI-1642518, EBI-2308190;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane
CC protein. Cell junction. Cytoplasmic vesicle membrane; Peripheral
CC membrane protein. Cytoplasm, cytoskeleton. Note=Localization to the
CC Golgi is dependent on interaction with GTP-bound ARF1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5T5U3-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q5T5U3-3; Sequence=VSP_028298, VSP_028300, VSP_028301;
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in brain,
CC heart, skeletal muscle and placenta. {ECO:0000269|PubMed:12056806}.
CC -!- INDUCTION: Up-regulated upon cell differentiation.
CC {ECO:0000269|PubMed:12056806}.
CC -!- PTM: Sumoylated with SUMO2 and SUMO3 in proliferating lymphocytes.
CC {ECO:0000269|PubMed:22922005}.
CC -!- MISCELLANEOUS: Depletion of ARHGAP21 induces cell spreading and
CC accumulation of F-actin stress fibers.
CC -!- MISCELLANEOUS: Required for In1A-dependent entry of Listeria
CC monocytogenes into cells.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM22955.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF480466; AAM22955.1; ALT_INIT; mRNA.
DR EMBL; AL355979; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL392104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB037845; BAA92662.2; -; mRNA.
DR EMBL; BX537570; CAD97787.1; -; mRNA.
DR EMBL; AL834495; CAD39153.1; -; mRNA.
DR EMBL; BC022931; AAH22931.1; -; mRNA.
DR CCDS; CCDS7144.2; -. [Q5T5U3-1]
DR PIR; A59438; A59438.
DR RefSeq; NP_065875.3; NM_020824.3. [Q5T5U3-1]
DR RefSeq; XP_005252599.1; XM_005252542.3.
DR RefSeq; XP_016871948.1; XM_017016459.1. [Q5T5U3-1]
DR PDB; 2DHJ; NMR; -; A=931-1042.
DR PDB; 2J59; X-ray; 2.10 A; M/N/O/P/Q/R=930-1097.
DR PDB; 2YUY; NMR; -; A=47-159.
DR PDBsum; 2DHJ; -.
DR PDBsum; 2J59; -.
DR PDBsum; 2YUY; -.
DR AlphaFoldDB; Q5T5U3; -.
DR BMRB; Q5T5U3; -.
DR SMR; Q5T5U3; -.
DR BioGRID; 121636; 154.
DR IntAct; Q5T5U3; 67.
DR MINT; Q5T5U3; -.
DR STRING; 9606.ENSP00000379709; -.
DR GlyGen; Q5T5U3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5T5U3; -.
DR PhosphoSitePlus; Q5T5U3; -.
DR BioMuta; ARHGAP21; -.
DR DMDM; 74745129; -.
DR EPD; Q5T5U3; -.
DR jPOST; Q5T5U3; -.
DR MassIVE; Q5T5U3; -.
DR MaxQB; Q5T5U3; -.
DR PaxDb; Q5T5U3; -.
DR PeptideAtlas; Q5T5U3; -.
DR PRIDE; Q5T5U3; -.
DR ProteomicsDB; 64551; -. [Q5T5U3-1]
DR ProteomicsDB; 64552; -. [Q5T5U3-3]
DR Antibodypedia; 51888; 30 antibodies from 14 providers.
DR DNASU; 57584; -.
DR Ensembl; ENST00000396432.7; ENSP00000379709.2; ENSG00000107863.20. [Q5T5U3-1]
DR GeneID; 57584; -.
DR KEGG; hsa:57584; -.
DR MANE-Select; ENST00000396432.7; ENSP00000379709.2; NM_020824.4; NP_065875.3.
DR UCSC; uc001isb.2; human. [Q5T5U3-1]
DR CTD; 57584; -.
DR DisGeNET; 57584; -.
DR GeneCards; ARHGAP21; -.
DR HGNC; HGNC:23725; ARHGAP21.
DR HPA; ENSG00000107863; Tissue enhanced (brain).
DR MIM; 609870; gene.
DR neXtProt; NX_Q5T5U3; -.
DR OpenTargets; ENSG00000107863; -.
DR PharmGKB; PA134973559; -.
DR VEuPathDB; HostDB:ENSG00000107863; -.
DR eggNOG; KOG4407; Eukaryota.
DR GeneTree; ENSGT00940000155406; -.
DR HOGENOM; CLU_001776_0_0_1; -.
DR InParanoid; Q5T5U3; -.
DR OMA; DPHPHKL; -.
DR OrthoDB; 142586at2759; -.
DR PhylomeDB; Q5T5U3; -.
DR TreeFam; TF329345; -.
DR PathwayCommons; Q5T5U3; -.
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 Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR SignaLink; Q5T5U3; -.
DR SIGNOR; Q5T5U3; -.
DR BioGRID-ORCS; 57584; 25 hits in 1084 CRISPR screens.
DR ChiTaRS; ARHGAP21; human.
DR EvolutionaryTrace; Q5T5U3; -.
DR GenomeRNAi; 57584; -.
DR Pharos; Q5T5U3; Tbio.
DR PRO; PR:Q5T5U3; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q5T5U3; protein.
DR Bgee; ENSG00000107863; Expressed in right hemisphere of cerebellum and 151 other tissues.
DR ExpressionAtlas; Q5T5U3; baseline and differential.
DR Genevisible; Q5T5U3; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005096; F:GTPase activator activity; TAS:Reactome.
DR GO; GO:0051683; P:establishment of Golgi localization; IDA:BHF-UCL.
DR GO; GO:0051645; P:Golgi localization; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IMP:BHF-UCL.
DR GO; GO:0051684; P:maintenance of Golgi location; IMP:BHF-UCL.
DR GO; GO:0072384; P:organelle transport along microtubule; IMP:BHF-UCL.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
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 Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Golgi apparatus; GTPase activation;
KW Isopeptide bond; Membrane; Methylation; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..1958
FT /note="Rho GTPase-activating protein 21"
FT /id="PRO_0000305245"
FT DOMAIN 50..159
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 931..1040
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1147..1339
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..1097
FT /note="Interaction with ARF1 and ARF6"
FT /evidence="ECO:0000269|PubMed:15793564"
FT REGION 1086..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1348..1401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1418..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1592..1861
FT /note="Interaction with CTNNA1"
FT /evidence="ECO:0000269|PubMed:16184169"
FT REGION 1598..1642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1655..1686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1860..1958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1349..1366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1427..1496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1497..1516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1530..1565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1613..1636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1668..1686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1864..1945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DFV3"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 554
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 575
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 717
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 747
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 857
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 862
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DFV3"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 882
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 926
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DFV3"
FT MOD_RES 954
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1099
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DFV3"
FT MOD_RES 1115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1504
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1516
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1669
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1682
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6DFV3"
FT MOD_RES 1742
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1917
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DFV3"
FT CROSSLNK 1444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:22922005"
FT VAR_SEQ 166..175
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_028298"
FT VAR_SEQ 1160..1175
FT /note="YIPLIVDICCKLVEER -> VGDTSPPDFLKSLIQF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_028300"
FT VAR_SEQ 1176..1958
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_028301"
FT VARIANT 713
FT /note="N -> S (in dbSNP:rs3748222)"
FT /evidence="ECO:0000269|PubMed:12056806,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_035187"
FT VARIANT 1594
FT /note="T -> A (in dbSNP:rs1133897)"
FT /id="VAR_035188"
FT VARIANT 1611
FT /note="V -> A (in dbSNP:rs1143051)"
FT /id="VAR_035189"
FT VARIANT 1629
FT /note="E -> K (in dbSNP:rs1143057)"
FT /id="VAR_035190"
FT VARIANT 1727
FT /note="A -> T (in dbSNP:rs1143075)"
FT /id="VAR_035191"
FT VARIANT 1950
FT /note="S -> N (in dbSNP:rs1127893)"
FT /id="VAR_035192"
FT MUTAGEN 1000
FT /note="Y->A: Altered interaction with ARF1 and loss of
FT association to membranes."
FT /evidence="ECO:0000269|PubMed:17347647"
FT MUTAGEN 1054
FT /note="I->A: Altered interaction with ARF1 and loss of
FT association to membranes."
FT /evidence="ECO:0000269|PubMed:17347647"
FT MUTAGEN 1184
FT /note="R->A: Loss of GTPase activity and loss of function."
FT /evidence="ECO:0000269|PubMed:15793564,
FT ECO:0000269|PubMed:16184169"
FT CONFLICT 306
FT /note="S -> N (in Ref. 1; AAM22955)"
FT /evidence="ECO:0000305"
FT CONFLICT 901
FT /note="S -> P (in Ref. 1; AAM22955)"
FT /evidence="ECO:0000305"
FT CONFLICT 1783
FT /note="V -> A (in Ref. 1; AAM22955)"
FT /evidence="ECO:0000305"
FT CONFLICT 1950
FT /note="S -> T (in Ref. 1; AAM22955, 5; CAD39153 and 6;
FT AAH22931)"
FT /evidence="ECO:0000305"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:2YUY"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2YUY"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2YUY"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:2YUY"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:2YUY"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:2YUY"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:2YUY"
FT STRAND 934..944
FT /evidence="ECO:0007829|PDB:2J59"
FT STRAND 959..966
FT /evidence="ECO:0007829|PDB:2J59"
FT STRAND 969..974
FT /evidence="ECO:0007829|PDB:2J59"
FT STRAND 979..981
FT /evidence="ECO:0007829|PDB:2DHJ"
FT STRAND 984..986
FT /evidence="ECO:0007829|PDB:2DHJ"
FT STRAND 995..998
FT /evidence="ECO:0007829|PDB:2J59"
FT STRAND 1000..1002
FT /evidence="ECO:0007829|PDB:2J59"
FT STRAND 1006..1012
FT /evidence="ECO:0007829|PDB:2J59"
FT STRAND 1017..1021
FT /evidence="ECO:0007829|PDB:2J59"
FT HELIX 1025..1038
FT /evidence="ECO:0007829|PDB:2J59"
FT HELIX 1043..1063
FT /evidence="ECO:0007829|PDB:2J59"
SQ SEQUENCE 1958 AA; 217462 MW; 1F2AC6A88F4EA9CB CRC64;
MMATRRTGLS EGDGDKLKAC EVSKNKDGKE QSETVSLSED ETFSWPGPKT VTLKRTSQGF
GFTLRHFIVY PPESAIQFSY KDEENGNRGG KQRNRLEPMD TIFVKQVKEG GPAFEAGLCT
GDRIIKVNGE SVIGKTYSQV IALIQNSDTT LELSVMPKDE DILQVLQFTK DVTALAYSQD
AYLKGNEAYS GNARNIPEPP PICYPWLPSA PSAMAQPVEI SPPDSSLSKQ QTSTPVLTQP
GRAYRMEIQV PPSPTDVAKS NTAVCVCNES VRTVIVPSEK VVDLLSNRNN HTGPSHRTEE
VRYGVSEQTS LKTVSRTTSP PLSIPTTHLI HQPAGSRSLE PSGILLKSGN YSGHSDGISS
SRSQAVEAPS VSVNHYSPNS HQHIDWKNYK TYKEYIDNRR LHIGCRTIQE RLDSLRAASQ
STTDYNQVVP NRTTLQGRRR STSHDRVPQS VQIRQRSVSQ ERLEDSVLMK YCPRSASQGA
LTSPSVSFSN HRTRSWDYIE GQDETLENVN SGTPIPDSNG EKKQTYKWSG FTEQDDRRGI
CERPRQQEIH KSFRGSNFTV APSVVNSDNR RMSGRGVGSV SQFKKIPPDL KTLQSNRNFQ
TTCGMSLPRG ISQDRSPLVK VRSNSLKAPS THVTKPSFSQ KSFVSIKDQR PVNHLHQNSL
LNQQTWVRTD SAPDQQVETG KSPSLSGASA KPAPQSSENA GTSDLELPVS QRNQDLSLQE
AETEQSDTLD NKEAVILREK PPSGRQTPQP LRHQSYILAV NDQETGSDTT CWLPNDARRE
VHIKRMEERK ASSTSPPGDS LASIPFIDEP TSPSIDHDIA HIPASAVISA STSQVPSIAT
VPPCLTTSAP LIRRQLSHDH ESVGPPSLDA QPNSKTERSK SYDEGLDDYR EDAKLSFKHV
SSLKGIKIAD SQKSSEDSGS RKDSSSEVFS DAAKEGWLHF RPLVTDKGKR VGGSIRPWKQ
MYVVLRGHSL YLYKDKREQT TPSEEEQPIS VNACLIDISY SETKRKNVFR LTTSDCECLF
QAEDRDDMLA WIKTIQESSN LNEEDTGVTN RDLISRRIKE YNNLMSKAEQ LPKTPRQSLS
IRQTLLGAKS EPKTQSPHSP KEESERKLLS KDDTSPPKDK GTWRKGIPSI MRKTFEKKPT
ATGTFGVRLD DCPPAHTNRY IPLIVDICCK LVEERGLEYT GIYRVPGNNA AISSMQEELN
KGMADIDIQD DKWRDLNVIS SLLKSFFRKL PEPLFTNDKY ADFIEANRKE DPLDRLKTLK
RLIHDLPEHH YETLKFLSAH LKTVAENSEK NKMEPRNLAI VFGPTLVRTS EDNMTHMVTH
MPDQYKIVET LIQHHDWFFT EEGAEEPLTT VQEESTVDSQ PVPNIDHLLT NIGRTGVSPG
DVSDSATSDS TKSKGSWGSG KDQYSRELLV SSIFAAASRK RKKPKEKAQP SSSEDELDNV
FFKKENVEQC HNDTKEESKK ESETLGRKQK IIIAKENSTR KDPSTTKDEK ISLGKESTPS
EEPSPPHNSK HNKSPTLSCR FAILKESPRS LLAQKSSHLE ETGSDSGTLL STSSQASLAR
FSMKKSTSPE TKHSEFLANV STITSDYSTT SSATYLTSLD SSRLSPEVQS VAESKGDEAD
DERSELISEG RPVETDSESE FPVFPTALTS ERLFRGKLQE VTKSSRRNSE GSELSCTEGS
LTSSLDSRRQ LFSSHKLIEC DTLSRKKSAR FKSDSGSLGD AKNEKEAPSL TKVFDVMKKG
KSTGSLLTPT RGESEKQEPT WKTKIADRLK LRPRAPADDM FGVGNHKVNA ETAKRKSIRR
RHTLGGHRDA TEISVLNFWK VHEQSGERES ELSAVNRLKP KCSAQDLSIS DWLARERLRT
STSDLSRGEI GDPQTENPST REIATTDTPL SLHCNTGSSS STLASTNRPL LSIPPQSPDQ
INGESFQNVS KNASSAANAQ PHKLSETPGS KAEFHPCL
