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 27-MAR-2024, entry version 204. 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 Testis RC {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 FUNCTION, AND 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). RN [36] RP VARIANTS CDAN3B GLN-396 AND SER-432, INVOLVEMENT IN CDAN3B, RP CHARACTERIZATION OF VARIANTS CDAN3B GLN-396 AND SER-432, MUTAGENESIS OF RP ARG-385, AND FUNCTION. RX PubMed=34818416; DOI=10.1182/blood.2021012334; RA Wontakal S.N., Britto M., Zhang H., Han Y., Gao C., Tannenbaum S., RA Durham B.H., Lee M.T., An X., Mishima M.; RT "RACGAP1 variants in a sporadic case of CDA III implicate the dysfunction RT of centralspindlin as the basis of the disease."; RL Blood 139:1413-1418(2022). 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. Sequentially binds to ECT2 and RAB11FIP3 which CC regulates cleavage furrow ingression and abscission during cytokinesis CC (PubMed:18511905). Plays key roles in controlling cell growth and CC differentiation of hematopoietic cells through mechanisms other than CC regulating Rac GTPase activity (PubMed:10979956). Has a critical role CC in erythropoiesis (PubMed:34818416). 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:18511905, ECO:0000269|PubMed:19468300, CC ECO:0000269|PubMed:19468302, ECO:0000269|PubMed:23235882, CC 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 ECT2; the interaction is direct, occurs at CC anaphase and during cytokinesis in a microtubule-dependent manner, is CC enhanced by phosphorylation by PLK1 and phosphorylation at Ser-164 CC plays a major role in mediating binding (PubMed:25068414). Interacts CC with RAB11FIP3; the interaction occurs at late telophase CC (PubMed:18511905). 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 -!- DISEASE: Anemia, congenital dyserythropoietic, 3B, autosomal recessive CC (CDAN3B) [MIM:619789]: An autosomal recessive blood disorder CC characterized by marked dyserythropoiesis, hemolytic anemia, CC macrocytosis in the peripheral blood, and giant multinucleated CC erythroblasts in the bone marrow. {ECO:0000269|PubMed:34818416}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAH24144.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 206. DR CORUM; Q9H0H5; -. DR DIP; DIP-33087N; -. DR ELM; Q9H0H5; -. DR IntAct; Q9H0H5; 103. DR MINT; Q9H0H5; -. DR STRING; 9606.ENSP00000404190; -. DR ChEMBL; CHEMBL2146306; -. DR GlyGen; Q9H0H5; 2 sites, 1 O-linked glycan (2 sites). 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; 9606-ENSP00000404190; -. DR PeptideAtlas; Q9H0H5; -. DR ProteomicsDB; 80279; -. DR Pumba; Q9H0H5; -. DR Antibodypedia; 14118; 666 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 AGR; HGNC:9804; -. 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 MalaCards; RACGAP1; -. DR MIM; 604980; gene. DR MIM; 619789; phenotype. DR neXtProt; NX_Q9H0H5; -. DR OpenTargets; ENSG00000161800; -. DR Orphanet; 98870; Congenital dyserythropoietic anemia type III. 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; 22770at2759; -. 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; 795 hits in 1164 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 186 other cell types or tissues. DR ExpressionAtlas; Q9H0H5; baseline and differential. 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:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA: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:0030218; P:erythrocyte differentiation; 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:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW. 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; cd20821; C1_MgcRacGAP; 1. DR CDD; cd04382; RhoGAP_MgcRacGAP; 1. DR Gene3D; 3.30.60.20; -; 1. DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 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 PANTHER; PTHR46199; RAC GTPASE-ACTIVATING PROTEIN 1; 1. DR PANTHER; PTHR46199:SF1; RAC GTPASE-ACTIVATING PROTEIN 1; 1. DR Pfam; PF00130; C1_1; 1. DR Pfam; PF00620; RhoGAP; 1. DR SMART; SM00109; C1; 1. DR SMART; SM00324; RhoGAP; 1. DR SUPFAM; SSF57889; Cysteine-rich domain; 1. DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1. DR PROSITE; PS50238; RHOGAP; 1. DR PROSITE; PS00479; ZF_DAG_PE_1; 1. DR PROSITE; PS50081; ZF_DAG_PE_2; 1. DR Genevisible; Q9H0H5; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cell cycle; Cell division; Cell membrane; KW Coiled coil; Congenital dyserythropoietic anemia; Cytoplasm; KW Cytoplasmic vesicle; Cytoskeleton; Developmental protein; Differentiation; KW Disease variant; GTPase activation; Hereditary hemolytic anemia; KW Ion transport; Isopeptide bond; Lipid-binding; Membrane; Metal-binding; KW Microtubule; Nucleus; Phosphoprotein; Reference proteome; Spermatogenesis; KW Transport; 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 VARIANT 396 FT /note="L -> Q (in CDAN3B; decreased function in FT erythropoiesis as shown by partial rescue of FT multinucleation defects in RACGAP1-deficient erythroid FT cells; decreased GAP activity towards RHOA, RAC1 and FT CDC42)" FT /evidence="ECO:0000269|PubMed:34818416" FT /id="VAR_087032" FT VARIANT 432 FT /note="P -> S (in CDAN3B; loss of function in FT erythropoiesis as it does not rescue multinucleation and FT cytokinesis defects in RACGAP1-deficient erythroid and Hela FT cells; increased GAP activity towards RHOA; no effect on FT GAP activity towards RAC1 and CDC42)" FT /evidence="ECO:0000269|PubMed:34818416" FT /id="VAR_087033" FT MUTAGEN 149 FT /note="S->A: Does not inhibit interaction with ECT2. FT Strongly reduces phosphorylation, inhibits interaction with FT ECT2 and cleavage furrow formation; when associated with FT A-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 Strongly reduces phosphorylation, inhibits interaction with FT ECT2 and cleavage furrow formation; when associated with FT A-149; A-164 and A-170. Strongly reduces 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 Strongly reduces phosphorylation, inhibits interaction with FT ECT2 and cleavage furrow formation; when associated with FT A-149; A-157 and A-170. Strongly reduces 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 Strongly reduces phosphorylation, inhibits interaction with FT ECT2 and cleavage furrow formation; when associated with FT A-149; A-157 and A-164. Strongly reduces 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: Strongly reduces 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. Abolishes GAP FT activity towards RHOA. Induces multiple blebs during FT cytokinesis." FT /evidence="ECO:0000269|PubMed:10979956, FT ECO:0000269|PubMed:14729465, ECO:0000269|PubMed:15642749, FT ECO:0000269|PubMed:34818416" 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 //