RGAP1_HUMAN
ID RGAP1_HUMAN Reviewed; 632 AA.
AC Q9H0H5; Q6PJ26; Q9NWN2; Q9P250; Q9P2W2;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Rac GTPase-activating protein 1;
DE AltName: Full=Male germ cell RacGap;
DE Short=MgcRacGAP;
DE AltName: Full=Protein CYK4 homolog;
DE Short=CYK4;
DE Short=HsCYK-4;
GN Name=RACGAP1 {ECO:0000312|HGNC:HGNC:9804};
GN Synonyms=KIAA1478 {ECO:0000312|EMBL:BAA96002.1}, MGCRACGAP;
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] {ECO:0000305, ECO:0000312|EMBL:BAA90247.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF
RP ARG-385, AND INDUCTION.
RX PubMed=10979956;
RA Kawashima T., Hirose K., Satoh T., Kaneko A., Ikeda Y., Kaziro Y.,
RA Nosaka T., Kitamura T.;
RT "MgcRacGAP is involved in the control of growth and differentiation of
RT hematopoietic cells.";
RL Blood 96:2116-2124(2000).
RN [2] {ECO:0000312|EMBL:CAB66728.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:CAB66728.1};
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3] {ECO:0000312|EMBL:BAA91347.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hepatoma {ECO:0000312|EMBL:BAA91347.1};
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] {ECO:0000312|EMBL:CAG38596.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:AAH32754.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta {ECO:0000312|EMBL:AAH24144.1}, and
RC Testis {ECO:0000312|EMBL:AAH32754.1};
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] {ECO:0000305, ECO:0000312|EMBL:BAA96002.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 63-632.
RC TISSUE=Brain {ECO:0000269|PubMed:10819331};
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [7] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 106-632, FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=9497316; DOI=10.1074/jbc.273.11.6019;
RA Toure A., Dorseuil O., Morin L., Timmons P., Jegou B., Reibel L., Gacon G.;
RT "MgcRacGAP, a new human GTPase-activating protein for Rac and Cdc42 similar
RT to Drosophila rotundRacGAP gene product, is expressed in male germ cells.";
RL J. Biol. Chem. 273:6019-6023(1998).
RN [8] {ECO:0000305}
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=11085985; DOI=10.1074/jbc.m007252200;
RA Hirose K., Kawashima T., Iwamoto I., Nosaka T., Kitamura T.;
RT "MgcRacGAP is involved in cytokinesis through associating with mitotic
RT spindle and midbody.";
RL J. Biol. Chem. 276:5821-5828(2001).
RN [9]
RP FUNCTION, INTERACTION WITH SLC26A8, AND TISSUE SPECIFICITY.
RX PubMed=11278976; DOI=10.1074/jbc.m011740200;
RA Toure A., Morin L., Pineau C., Becq F., Dorseuil O., Gacon G.;
RT "Tat1, a novel sulfate transporter specifically expressed in human male
RT germ cells and potentially linked to rhogtpase signaling.";
RL J. Biol. Chem. 276:20309-20315(2001).
RN [10]
RP FUNCTION, IDENTIFICATION IN THE CENTRALSPINDLIN COMPLEX, ASSOCIATION TO
RP MICROTUBULES, AND INTERACTION WITH KIF23.
RX PubMed=11782313; DOI=10.1016/s1534-5807(01)00110-1;
RA Mishima M., Kaitna S., Glotzer M.;
RT "Central spindle assembly and cytokinesis require a kinesin-like
RT protein/RhoGAP complex with microtubule bundling activity.";
RL Dev. Cell 2:41-54(2002).
RN [11] {ECO:0000305}
RP INTERACTION WITH RND2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12590651; DOI=10.1042/bj20021652;
RA Naud N., Toure A., Liu J., Pineau C., Morin L., Dorseuil O., Escalier D.,
RA Chardin P., Gacon G.;
RT "Rho family GTPase Rnd2 interacts and co-localizes with MgcRacGAP in male
RT germ cells.";
RL Biochem. J. 372:105-112(2003).
RN [12] {ECO:0000305}
RP INTERACTION WITH AURKB, AND PHOSPHORYLATION AT SER-387 AND SER-410.
RX PubMed=12689593; DOI=10.1016/s1534-5807(03)00089-3;
RA Minoshima Y., Kawashima T., Hirose K., Tonozuka Y., Kawajiri A., Bao Y.C.,
RA Deng X., Tatsuka M., Narumiya S., May W.S. Jr., Nosaka T., Semba K.,
RA Inoue T., Satoh T., Inagaki M., Kitamura T.;
RT "Phosphorylation by aurora B converts MgcRacGAP to a RhoGAP during
RT cytokinesis.";
RL Dev. Cell 4:549-560(2003).
RN [13] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF ARG-385.
RX PubMed=14729465; DOI=10.1016/j.yexcr.2003.10.015;
RA Lee J.S., Kamijo K., Ohara N., Kitamura T., Miki T.;
RT "MgcRacGAP regulates cortical activity through RhoA during cytokinesis.";
RL Exp. Cell Res. 293:275-282(2004).
RN [14] {ECO:0000305}
RP INTERACTION WITH PRC1.
RX PubMed=14744859; DOI=10.1074/jbc.m313257200;
RA Ban R., Irino Y., Fukami K., Tanaka H.;
RT "Human mitotic spindle-associated protein PRC1 inhibits MgcRacGAP activity
RT toward Cdc42 during the metaphase.";
RL J. Biol. Chem. 279:16394-16402(2004).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=16213214; DOI=10.1016/j.cell.2005.07.027;
RA Gromley A., Yeaman C., Rosa J., Redick S., Chen C.-T., Mirabelle S.,
RA Guha M., Sillibourne J., Doxsey S.J.;
RT "Centriolin anchoring of exocyst and SNARE complexes at the midbody is
RT required for secretory-vesicle-mediated abscission.";
RL Cell 123:75-87(2005).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-385.
RX PubMed=15642749; DOI=10.1083/jcb.200408085;
RA Oceguera-Yanez F., Kimura K., Yasuda S., Higashida C., Kitamura T.,
RA Hiraoka Y., Haraguchi T., Narumiya S.;
RT "Ect2 and MgcRacGAP regulate the activation and function of Cdc42 in
RT mitosis.";
RL J. Cell Biol. 168:221-232(2005).
RN [17]
RP FUNCTION, INTERACTION WITH ECT2 AND KIF23, AND SUBCELLULAR LOCATION.
RX PubMed=16103226; DOI=10.1083/jcb.200501097;
RA Yuce O., Piekny A., Glotzer M.;
RT "An ECT2-centralspindlin complex regulates the localization and function of
RT RhoA.";
RL J. Cell Biol. 170:571-582(2005).
RN [18] {ECO:0000305}
RP FUNCTION, INTERACTION WITH ECT2, AND SUBCELLULAR LOCATION.
RX PubMed=16129829; DOI=10.1073/pnas.0504145102;
RA Zhao W.-M., Fang G.;
RT "MgcRacGAP controls the assembly of the contractile ring and the initiation
RT of cytokinesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13158-13163(2005).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161; SER-164 AND SER-203, AND
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 [20]
RP FUNCTION, IDENTIFICATION IN THE CENTRALSPINDLIN COMPLEX, INTERACTION WITH
RP ECT2 AND KIF23, AND SUBCELLULAR LOCATION.
RX PubMed=16236794; DOI=10.1091/mbc.e05-06-0569;
RA Kamijo K., Ohara N., Abe M., Uchimura T., Hosoya H., Lee J.S., Miki T.;
RT "Dissecting the role of Rho-mediated signaling in contractile ring
RT formation.";
RL Mol. Biol. Cell 17:43-55(2006).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND THR-588, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [22]
RP INTERACTION WITH RAB11FIP3.
RX PubMed=18511905; DOI=10.1038/emboj.2008.112;
RA Simon G.C., Schonteich E., Wu C.C., Piekny A., Ekiert D., Yu X.,
RA Gould G.W., Glotzer M., Prekeris R.;
RT "Sequential Cyk-4 binding to ECT2 and FIP3 regulates cleavage furrow
RT ingression and abscission during cytokinesis.";
RL EMBO J. 27:1791-1803(2008).
RN [23]
RP SUBCELLULAR LOCATION.
RX PubMed=18445686; DOI=10.1242/jcs.019174;
RA Tegha-Dunghu J., Neumann B., Reber S., Krause R., Erfle H., Walter T.,
RA Held M., Rogers P., Hupfeld K., Ruppert T., Ellenberg J., Gruss O.J.;
RT "EML3 is a nuclear microtubule-binding protein required for the correct
RT alignment of chromosomes in metaphase.";
RL J. Cell Sci. 121:1718-1726(2008).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-206; SER-257;
RP THR-342; THR-580; THR-588; SER-600; THR-601 AND THR-606, AND IDENTIFICATION
RP 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 [25]
RP FUNCTION, PHOSPHORYLATION AT SER-157; SER-164; SER-170; SER-214 AND
RP THR-260, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-157; SER-164; SER-170
RP AND SER-214.
RX PubMed=19468302; DOI=10.1371/journal.pbio.1000111;
RA Burkard M.E., Maciejowski J., Rodriguez-Bravo V., Repka M., Lowery D.M.,
RA Clauser K.R., Zhang C., Shokat K.M., Carr S.A., Yaffe M.B.,
RA Jallepalli P.V.;
RT "Plk1 self-organization and priming phosphorylation of HsCYK-4 at the
RT spindle midzone regulate the onset of division in human cells.";
RL PLoS Biol. 7:E1000111-E1000111(2009).
RN [26]
RP FUNCTION, INTERACTION WITH ECT2, PHOSPHORYLATION AT SER-149; SER-157;
RP SER-164 AND SER-170, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-149;
RP SER-157; SER-164 AND SER-170.
RX PubMed=19468300; DOI=10.1371/journal.pbio.1000110;
RA Wolfe B.A., Takaki T., Petronczki M., Glotzer M.;
RT "Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF
RT complex to initiate cleavage furrow formation.";
RL PLoS Biol. 7:E1000110-E1000110(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-157; SER-203 AND
RP SER-206, AND 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 [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-157; SER-203;
RP THR-342; THR-567 AND THR-588, 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 [29]
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 [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154 AND SER-157, 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 [31]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-206; SER-214;
RP THR-249; SER-257; THR-580 AND SER-628, AND IDENTIFICATION BY MASS
RP 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 [33]
RP INTERACTION WITH ECT2, PHOSPHORYLATION AT SER-157 AND SER-164, AND
RP MUTAGENESIS OF TRP-167.
RX PubMed=25068414; DOI=10.1016/j.febslet.2014.07.019;
RA Zou Y., Shao Z., Peng J., Li F., Gong D., Wang C., Zuo X., Zhang Z., Wu J.,
RA Shi Y., Gong Q.;
RT "Crystal structure of triple-BRCT-domain of ECT2 and insights into the
RT binding characteristics to CYK-4.";
RL FEBS Lett. 588:2911-2920(2014).
RN [34]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-248 AND LYS-404, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 284-339 IN COMPLEX WITH ZINC IONS,
RP FUNCTION, INTERACTION WITH KIF23, DOMAIN, LIPID-BINDING, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF PHE-289; LYS-292; ARG-306; PHE-309 AND
RP CYS-316.
RX PubMed=23235882; DOI=10.1038/nature11773;
RA Lekomtsev S., Su K.C., Pye V.E., Blight K., Sundaramoorthy S., Takaki T.,
RA Collinson L.M., Cherepanov P., Divecha N., Petronczki M.;
RT "Centralspindlin links the mitotic spindle to the plasma membrane during
RT cytokinesis.";
RL Nature 492:276-279(2012).
CC -!- FUNCTION: Component of the centralspindlin complex that serves as a
CC microtubule-dependent and Rho-mediated signaling required for the
CC myosin contractile ring formation during the cell cycle cytokinesis.
CC Required for proper attachment of the midbody to the cell membrane
CC during cytokinesis. Plays key roles in controlling cell growth and
CC differentiation of hematopoietic cells through mechanisms other than
CC regulating Rac GTPase activity. Also involved in the regulation of
CC growth-related processes in adipocytes and myoblasts. May be involved
CC in regulating spermatogenesis and in the RACGAP1 pathway in neuronal
CC proliferation. Shows strong GAP (GTPase activation) activity towards
CC CDC42 and RAC1 and less towards RHOA. Essential for the early stages of
CC embryogenesis. May play a role in regulating cortical activity through
CC RHOA during cytokinesis. May participate in the regulation of sulfate
CC transport in male germ cells. {ECO:0000269|PubMed:10979956,
CC ECO:0000269|PubMed:11085985, ECO:0000269|PubMed:11278976,
CC ECO:0000269|PubMed:11782313, ECO:0000269|PubMed:14729465,
CC ECO:0000269|PubMed:15642749, ECO:0000269|PubMed:16103226,
CC ECO:0000269|PubMed:16129829, ECO:0000269|PubMed:16236794,
CC ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:19468302,
CC ECO:0000269|PubMed:23235882, ECO:0000269|PubMed:9497316}.
CC -!- SUBUNIT: Heterotetramer of two molecules each of RACGAP1 and KIF23.
CC Found in the centralspindlin complex. Associates with alpha-, beta- and
CC gamma-tubulin and microtubules. Interacts via its Rho-GAP domain with
CC RND2. Associates with AURKB during M phase. Interacts via its Rho-GAP
CC domain and basic region with PRC1. The interaction with PRC1 inhibits
CC its GAP activity towards CDC42 in vitro, which may be required for
CC maintaining normal spindle morphology. Interacts with SLC26A8 via its
CC N-terminus. Interacts with RAB11FIP3. Interacts with ECT2; the
CC interaction is direct, occurs at anaphase and during cytokinesis in a
CC microtubule-dependent manner, is enhanced by phosphorylation by PLK1
CC and phosphorylation at Ser-164 plays a major role in mediating binding
CC (PubMed:25068414). Interacts with KIF23; the interaction is direct.
CC {ECO:0000269|PubMed:11085985, ECO:0000269|PubMed:11278976,
CC ECO:0000269|PubMed:11782313, ECO:0000269|PubMed:12590651,
CC ECO:0000269|PubMed:12689593, ECO:0000269|PubMed:14744859,
CC ECO:0000269|PubMed:16103226, ECO:0000269|PubMed:16129829,
CC ECO:0000269|PubMed:16236794, ECO:0000269|PubMed:18511905,
CC ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:23235882,
CC ECO:0000269|PubMed:25068414}.
CC -!- INTERACTION:
CC Q9H0H5; Q13895: BYSL; NbExp=3; IntAct=EBI-717233, EBI-358049;
CC Q9H0H5; Q00526: CDK3; NbExp=3; IntAct=EBI-717233, EBI-1245761;
CC Q9H0H5; P35221: CTNNA1; NbExp=2; IntAct=EBI-717233, EBI-701918;
CC Q9H0H5; Q9H8V3: ECT2; NbExp=15; IntAct=EBI-717233, EBI-1054039;
CC Q9H0H5; Q02241: KIF23; NbExp=12; IntAct=EBI-717233, EBI-306852;
CC Q9H0H5; Q9UBU8: MORF4L1; NbExp=3; IntAct=EBI-717233, EBI-399246;
CC Q9H0H5; P53350: PLK1; NbExp=4; IntAct=EBI-717233, EBI-476768;
CC Q9H0H5; Q16537: PPP2R5E; NbExp=5; IntAct=EBI-717233, EBI-968374;
CC Q9H0H5; O75154: RAB11FIP3; NbExp=7; IntAct=EBI-717233, EBI-7942186;
CC Q9H0H5; Q96RN1: SLC26A8; NbExp=2; IntAct=EBI-717233, EBI-1792052;
CC Q9H0H5; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-717233, EBI-765817;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18445686}. Cytoplasm.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18445686}.
CC Cytoplasmic vesicle, secretory vesicle, acrosome. Cleavage furrow.
CC Midbody, Midbody ring {ECO:0000269|PubMed:16213214}. Cell membrane;
CC Peripheral membrane protein; Cytoplasmic side. Note=Colocalizes with
CC RND2 in Golgi-derived proacrosomal vesicles and the acrosome (By
CC similarity). During interphase, localized to the nucleus and cytoplasm
CC along with microtubules, in anaphase, is redistributed to the central
CC spindle and, in telophase and cytokinesis, to the midbody ring, also
CC called Flemming body. Colocalizes with RHOA at the myosin contractile
CC ring during cytokinesis. Colocalizes with ECT2 to the mitotic spindles
CC during anaphase/metaphase, the cleavage furrow during telophase and at
CC the midbody at the end of cytokinesis. Colocalizes with Cdc42 to
CC spindle microtubules from prometaphase to telophase. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, thymus and placenta.
CC Expressed at lower levels in spleen and peripheral blood lymphocytes.
CC In testis, expression is restricted to germ cells with the highest
CC levels of expression found in spermatocytes. Expression is regulated in
CC a cell cycle-dependent manner and peaks during G2/M phase.
CC {ECO:0000269|PubMed:10979956, ECO:0000269|PubMed:11278976,
CC ECO:0000269|PubMed:12590651, ECO:0000269|PubMed:9497316}.
CC -!- INDUCTION: Expression is down-regulated during macrophage differention
CC of HL-60 cells. {ECO:0000269|PubMed:10979956}.
CC -!- DOMAIN: The coiled coil region is indispensible for localization to the
CC midbody during cytokinesis. {ECO:0000269|PubMed:11085985}.
CC -!- DOMAIN: The phorbol-ester/DAG-type zinc finger domain mediates
CC interaction with membranes enriched in phosphatidylinositol 3,4,5-
CC trisphosphate and is required during mitotic cytokinesis for normal
CC attachment of the midbody to the cell membrane.
CC -!- PTM: Phosphorylated at multiple sites in the midbody during cytokinesis
CC (PubMed:12689593). Phosphorylation by AURKB on Ser-387 at the midbody
CC is, at least in part, responsible for exerting its latent GAP activity
CC towards RhoA (PubMed:12689593). Phosphorylation on multiple serine
CC residues by PLK1 enhances its association with ECT2 and is critical for
CC cleavage furrow formation (PubMed:19468302, PubMed:19468300).
CC Phosphorylation on Ser-164 plays a major role in mediating interaction
CC with ECT2 (PubMed:25068414). Phosphorylation on Ser-157 does not appear
CC to contribute to binding to ECT2 (PubMed:25068414).
CC {ECO:0000269|PubMed:12689593, ECO:0000269|PubMed:19468300,
CC ECO:0000269|PubMed:19468302, ECO:0000269|PubMed:25068414}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH24144.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB030251; BAA90247.1; -; mRNA.
DR EMBL; AL136794; CAB66728.1; -; mRNA.
DR EMBL; AK000733; BAA91347.1; -; mRNA.
DR EMBL; CR533565; CAG38596.1; -; mRNA.
DR EMBL; BC024144; AAH24144.1; ALT_FRAME; mRNA.
DR EMBL; BC032754; AAH32754.1; -; mRNA.
DR EMBL; AB040911; BAA96002.1; -; mRNA.
DR CCDS; CCDS8795.1; -.
DR PIR; D59430; D59430.
DR RefSeq; NP_001119575.1; NM_001126103.2.
DR RefSeq; NP_001119576.1; NM_001126104.2.
DR RefSeq; NP_001306928.1; NM_001319999.1.
DR RefSeq; NP_001306929.1; NM_001320000.1.
DR RefSeq; NP_001306930.1; NM_001320001.1.
DR RefSeq; NP_001306931.1; NM_001320002.1.
DR RefSeq; NP_001306932.1; NM_001320003.1.
DR RefSeq; NP_001306933.1; NM_001320004.1.
DR RefSeq; NP_001306934.1; NM_001320005.1.
DR RefSeq; NP_001306935.1; NM_001320006.1.
DR RefSeq; NP_001306936.1; NM_001320007.1.
DR RefSeq; NP_037409.2; NM_013277.4.
DR RefSeq; XP_006719422.1; XM_006719359.1.
DR RefSeq; XP_011536540.1; XM_011538238.1.
DR RefSeq; XP_016874709.1; XM_017019220.1.
DR PDB; 2OVJ; X-ray; 1.49 A; A=348-546.
DR PDB; 3W6R; X-ray; 1.90 A; A=348-546.
DR PDB; 3WPQ; X-ray; 1.84 A; A/B=346-546.
DR PDB; 3WPS; X-ray; 2.70 A; A/B=346-546.
DR PDB; 4B6D; X-ray; 2.20 A; A/B/C/D/E/F=284-339.
DR PDB; 5C2J; X-ray; 2.50 A; A=346-546.
DR PDB; 5C2K; X-ray; 1.42 A; A=346-546.
DR PDBsum; 2OVJ; -.
DR PDBsum; 3W6R; -.
DR PDBsum; 3WPQ; -.
DR PDBsum; 3WPS; -.
DR PDBsum; 4B6D; -.
DR PDBsum; 5C2J; -.
DR PDBsum; 5C2K; -.
DR AlphaFoldDB; Q9H0H5; -.
DR SMR; Q9H0H5; -.
DR BioGRID; 118892; 175.
DR CORUM; Q9H0H5; -.
DR DIP; DIP-33087N; -.
DR ELM; Q9H0H5; -.
DR IntAct; Q9H0H5; 101.
DR MINT; Q9H0H5; -.
DR STRING; 9606.ENSP00000404190; -.
DR ChEMBL; CHEMBL2146306; -.
DR iPTMnet; Q9H0H5; -.
DR PhosphoSitePlus; Q9H0H5; -.
DR SwissPalm; Q9H0H5; -.
DR BioMuta; RACGAP1; -.
DR DMDM; 74762727; -.
DR EPD; Q9H0H5; -.
DR jPOST; Q9H0H5; -.
DR MassIVE; Q9H0H5; -.
DR MaxQB; Q9H0H5; -.
DR PaxDb; Q9H0H5; -.
DR PeptideAtlas; Q9H0H5; -.
DR PRIDE; Q9H0H5; -.
DR ProteomicsDB; 80279; -.
DR Antibodypedia; 14118; 606 antibodies from 41 providers.
DR DNASU; 29127; -.
DR Ensembl; ENST00000312377.10; ENSP00000309871.5; ENSG00000161800.13.
DR Ensembl; ENST00000427314.6; ENSP00000404190.2; ENSG00000161800.13.
DR Ensembl; ENST00000454520.6; ENSP00000404808.2; ENSG00000161800.13.
DR Ensembl; ENST00000547905.5; ENSP00000449370.1; ENSG00000161800.13.
DR Ensembl; ENST00000551016.5; ENSP00000449374.1; ENSG00000161800.13.
DR GeneID; 29127; -.
DR KEGG; hsa:29127; -.
DR MANE-Select; ENST00000312377.10; ENSP00000309871.5; NM_001319999.2; NP_001306928.1.
DR UCSC; uc001rvs.3; human.
DR CTD; 29127; -.
DR DisGeNET; 29127; -.
DR GeneCards; RACGAP1; -.
DR HGNC; HGNC:9804; RACGAP1.
DR HPA; ENSG00000161800; Tissue enhanced (bone marrow, lymphoid tissue, testis).
DR MIM; 604980; gene.
DR neXtProt; NX_Q9H0H5; -.
DR OpenTargets; ENSG00000161800; -.
DR PharmGKB; PA34165; -.
DR VEuPathDB; HostDB:ENSG00000161800; -.
DR eggNOG; KOG3564; Eukaryota.
DR GeneTree; ENSGT00940000154610; -.
DR HOGENOM; CLU_026187_1_0_1; -.
DR InParanoid; Q9H0H5; -.
DR OMA; ECKMPIS; -.
DR OrthoDB; 372767at2759; -.
DR PhylomeDB; Q9H0H5; -.
DR TreeFam; TF318102; -.
DR PathwayCommons; Q9H0H5; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
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-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q9H0H5; -.
DR SIGNOR; Q9H0H5; -.
DR BioGRID-ORCS; 29127; 762 hits in 1085 CRISPR screens.
DR ChiTaRS; RACGAP1; human.
DR EvolutionaryTrace; Q9H0H5; -.
DR GeneWiki; RACGAP1; -.
DR GenomeRNAi; 29127; -.
DR Pharos; Q9H0H5; Tbio.
DR PRO; PR:Q9H0H5; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9H0H5; protein.
DR Bgee; ENSG00000161800; Expressed in ventricular zone and 184 other tissues.
DR ExpressionAtlas; Q9H0H5; baseline and differential.
DR Genevisible; Q9H0H5; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0097149; C:centralspindlin complex; IDA:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
DR GO; GO:0043014; F:alpha-tubulin binding; IDA:UniProtKB.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
DR GO; GO:0043015; F:gamma-tubulin binding; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; IMP:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; IDA:UniProtKB.
DR GO; GO:0051256; P:mitotic spindle midzone assembly; IDA:UniProtKB.
DR GO; GO:0007405; P:neuroblast proliferation; ISS:UniProtKB.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IDA:UniProtKB.
DR GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; IMP:UniProtKB.
DR GO; GO:0045995; P:regulation of embryonic development; ISS:UniProtKB.
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 GO; GO:0007283; P:spermatogenesis; IEP:UniProtKB.
DR GO; GO:0008272; P:sulfate transport; IDA:UniProtKB.
DR CDD; cd00029; C1; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Cell membrane;
KW Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Developmental protein; Differentiation; GTPase activation; Ion transport;
KW Isopeptide bond; Lipid-binding; Membrane; Metal-binding; Microtubule;
KW Nucleus; Phosphoprotein; Reference proteome; Spermatogenesis; Transport;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..632
FT /note="Rac GTPase-activating protein 1"
FT /id="PRO_0000228808"
FT DOMAIN 349..539
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 286..335
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 106..285
FT /note="Interaction with SLC26A8"
FT /evidence="ECO:0000269|PubMed:11278976"
FT REGION 183..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 53..110
FT /evidence="ECO:0000255"
FT COMPBIAS 583..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 149
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:19468300"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 157
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:19468300,
FT ECO:0000269|PubMed:19468302, ECO:0000269|PubMed:25068414,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 164
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:19468300,
FT ECO:0000269|PubMed:19468302, ECO:0000269|PubMed:25068414,
FT ECO:0007744|PubMed:17081983"
FT MOD_RES 170
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:19468300,
FT ECO:0000269|PubMed:19468302"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19468302,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 249
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 260
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19468302"
FT MOD_RES 342
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 387
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000269|PubMed:12689593"
FT MOD_RES 410
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000269|PubMed:12689593"
FT MOD_RES 567
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 580
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 588
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 601
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 606
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 404
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 149
FT /note="S->A: Does not inhibit interaction with ECT2.
FT Reduces strongly phosphorylation, inhibits interaction with
FT ECT2 and cleavage furrow formation; when associated with A-
FT 157; A-164 and A-170."
FT /evidence="ECO:0000269|PubMed:19468300"
FT MUTAGEN 157
FT /note="S->A: Does not inhibit interaction with ECT2.
FT Reduces strongly phosphorylation, inhibits interaction with
FT ECT2 and cleavage furrow formation; when associated with A-
FT 149; A-164 and A-170. Reduces strongly phosphorylation by
FT PLK1, inhibits interaction with ECT2 and cleavage furrow
FT formation; when associated with A-164; A-170 and A-214."
FT /evidence="ECO:0000269|PubMed:19468300,
FT ECO:0000269|PubMed:19468302"
FT MUTAGEN 164
FT /note="S->A: Does not inhibit interaction with ECT2.
FT Reduces strongly phosphorylation, inhibits interaction with
FT ECT2 and cleavage furrow formation; when associated with A-
FT 149; A-157 and A-170. Reduces strongly phosphorylation by
FT PLK1, inhibits interaction with ECT2 and cleavage furrow
FT formation; when associated with A-157; A-170 and A-214."
FT /evidence="ECO:0000269|PubMed:19468300,
FT ECO:0000269|PubMed:19468302"
FT MUTAGEN 167
FT /note="W->A: More than 20-fold reduction in binding to
FT ECT2."
FT /evidence="ECO:0000269|PubMed:25068414"
FT MUTAGEN 170
FT /note="S->A: Does not inhibit interaction with ECT2.
FT Reduces strongly phosphorylation, inhibits interaction with
FT ECT2 and cleavage furrow formation; when associated with A-
FT 149; A-157 and A-164. Reduces strongly phosphorylation by
FT PLK1, inhibits interaction with ECT2 and cleavage furrow
FT formation; when associated with A-157; A-164 and A-214."
FT /evidence="ECO:0000269|PubMed:19468300,
FT ECO:0000269|PubMed:19468302"
FT MUTAGEN 214
FT /note="S->A: Reduces strongly phosphorylation by PLK1,
FT inhibits interaction with ECT2 and cleavage furrow
FT formation; when associated with A-157; A-164 and A-170."
FT /evidence="ECO:0000269|PubMed:19468302"
FT MUTAGEN 289
FT /note="F->G: Cytokinesis failure."
FT /evidence="ECO:0000269|PubMed:23235882"
FT MUTAGEN 292
FT /note="K->L: Cytokinesis failure. Abolishes localization at
FT the cell membrane."
FT /evidence="ECO:0000269|PubMed:23235882"
FT MUTAGEN 306
FT /note="R->L: Cytokinesis failure. Abolishes localization at
FT the cell membrane."
FT /evidence="ECO:0000269|PubMed:23235882"
FT MUTAGEN 309
FT /note="F->A: Cytokinesis failure. Abolishes localization at
FT the cell membrane."
FT /evidence="ECO:0000269|PubMed:23235882"
FT MUTAGEN 316
FT /note="C->G: Cytokinesis failure."
FT /evidence="ECO:0000269|PubMed:23235882"
FT MUTAGEN 385
FT /note="R->A: Abolishes GAP activity towards RAC1. Abolishes
FT GAP activity towards CDC42 in prometaphase. Induces
FT multiple blebs during cytokinesis."
FT /evidence="ECO:0000269|PubMed:10979956,
FT ECO:0000269|PubMed:14729465, ECO:0000269|PubMed:15642749"
FT CONFLICT 155
FT /note="D -> H (in Ref. 3; BAA91347)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="L -> S (in Ref. 1; BAA90247)"
FT /evidence="ECO:0000305"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:4B6D"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:4B6D"
FT STRAND 312..320
FT /evidence="ECO:0007829|PDB:4B6D"
FT HELIX 325..330
FT /evidence="ECO:0007829|PDB:4B6D"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:5C2K"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:5C2K"
FT HELIX 364..376
FT /evidence="ECO:0007829|PDB:5C2K"
FT TURN 377..379
FT /evidence="ECO:0007829|PDB:5C2K"
FT TURN 381..385
FT /evidence="ECO:0007829|PDB:5C2K"
FT HELIX 390..403
FT /evidence="ECO:0007829|PDB:5C2K"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:5C2K"
FT HELIX 415..427
FT /evidence="ECO:0007829|PDB:5C2K"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:5C2K"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:5C2K"
FT HELIX 439..447
FT /evidence="ECO:0007829|PDB:5C2K"
FT HELIX 451..464
FT /evidence="ECO:0007829|PDB:5C2K"
FT HELIX 467..485
FT /evidence="ECO:0007829|PDB:5C2K"
FT TURN 487..489
FT /evidence="ECO:0007829|PDB:5C2K"
FT HELIX 493..504
FT /evidence="ECO:0007829|PDB:5C2K"
FT STRAND 508..511
FT /evidence="ECO:0007829|PDB:5C2K"
FT HELIX 514..520
FT /evidence="ECO:0007829|PDB:5C2K"
FT HELIX 523..532
FT /evidence="ECO:0007829|PDB:5C2K"
FT HELIX 536..541
FT /evidence="ECO:0007829|PDB:5C2K"
FT TURN 542..544
FT /evidence="ECO:0007829|PDB:5C2K"
SQ SEQUENCE 632 AA; 71027 MW; 032B7DF9CEA8F39D CRC64;
MDTMMLNVRN LFEQLVRRVE ILSEGNEVQF IQLAKDFEDF RKKWQRTDHE LGKYKDLLMK
AETERSALDV KLKHARNQVD VEIKRRQRAE ADCEKLERQI QLIREMLMCD TSGSIQLSEE
QKSALAFLNR GQPSSSNAGN KRLSTIDESG SILSDISFDK TDESLDWDSS LVKTFKLKKR
EKRRSTSRQF VDGPPGPVKK TRSIGSAVDQ GNESIVAKTT VTVPNDGGPI EAVSTIETVP
YWTRSRRKTG TLQPWNSDST LNSRQLEPRT ETDSVGTPQS NGGMRLHDFV SKTVIKPESC
VPCGKRIKFG KLSLKCRDCR VVSHPECRDR CPLPCIPTLI GTPVKIGEGM LADFVSQTSP
MIPSIVVHCV NEIEQRGLTE TGLYRISGCD RTVKELKEKF LRVKTVPLLS KVDDIHAICS
LLKDFLRNLK EPLLTFRLNR AFMEAAEITD EDNSIAAMYQ AVGELPQANR DTLAFLMIHL
QRVAQSPHTK MDVANLAKVF GPTIVAHAVP NPDPVTMLQD IKRQPKVVER LLSLPLEYWS
QFMMVEQENI DPLHVIENSN AFSTPQTPDI KVSLLGPVTT PEHQLLKTPS SSSLSQRVRS
TLTKNTPRFG SKSKSATNLG RQGNFFASPM LK
