ID RGAP1_MOUSE Reviewed; 628 AA. AC Q9WVM1; Q3THR5; Q3TI41; Q3TM81; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 02-SEP-2026, entry version 199. DE RecName: Full=Rac GTPase-activating protein 1; DE AltName: Full=Male germ cell RacGap; DE Short=MgcRacGAP; GN Name=Racgap1 {ECO:0000312|MGI:MGI:1349423}; Synonyms=Mgcracgap; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] {ECO:0000305, ECO:0000312|EMBL:AAD40487.1} RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RC TISSUE=Erythroleukemia {ECO:0000269|PubMed:10235109}; RX PubMed=10235109; DOI=10.1089/104454999315321; RA Wooltorton E.J., Haliotis T., Mueller C.R.; RT "Identification and characterization of a transcript for a novel Rac RT GTPase-activating protein in terminally differentiating 3T3-L1 RT adipocytes."; RL DNA Cell Biol. 18:265-273(1999). RN [2] {ECO:0000305, ECO:0000312|EMBL:BAA90248.1} RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=10979956; DOI=10.1182/blood.v96.6.2116; 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 [3] {ECO:0000305, ECO:0000312|EMBL:AAG43539.1} RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RC STRAIN=CD-1 {ECO:0000312|EMBL:AAG43539.1}; RX PubMed=11287179; DOI=10.1016/s0925-4773(01)00279-9; RA Van de Putte T., Zwijsen A., Lonnoy O., Rybin V., Cozijnsen M., Francis A., RA Baekelandt V., Kozak C.A., Zerial M., Huylebroeck D.; RT "Mice with a homozygous gene trap vector insertion in mgcRacGAP die during RT pre-implantation development."; RL Mech. Dev. 102:33-44(2001). RN [4] {ECO:0000312|EMBL:BAE32931.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE40528.1}, DBA/2J RC {ECO:0000312|EMBL:BAE40131.1}, and NOD {ECO:0000312|EMBL:BAE32931.1}; RC TISSUE=Heart {ECO:0000312|EMBL:BAE40528.1}, and Lung RC {ECO:0000312|EMBL:BAE38446.1}; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] {ECO:0000312|EMBL:AAH10715.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH10715.1}; RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH10715.1}; 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} RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=10493933; DOI=10.1042/bj3430225; RA Arar C., Ott M.-O., Toure A., Gacon G.; RT "Structure and expression of murine mgcRacGAP: its developmental regulation RT suggests a role for the Rac/MgcRacGAP signalling pathway in neurogenesis."; RL Biochem. J. 343:225-230(1999). RN [7] {ECO:0000305} RP SUBCELLULAR LOCATION. 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-564; THR-577 AND THR-585, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). 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 Plays key roles in controlling cell growth and differentiation of CC hematopoietic cells through mechanisms other than regulating Rac GTPase CC activity. Has a critical role in erythropoiesis (By similarity). Also CC involved in the regulation of growth-related processes in adipocytes CC and myoblasts. May be involved in regulating spermatogenesis and in the CC RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase CC activation) activity towards CDC42 and RAC1 and less towards RHOA. CC Essential for the early stages of embryogenesis. May play a role in CC regulating cortical activity through RHOA during cytokinesis. May CC participate in the regulation of sulfate transport in male germ cells. CC {ECO:0000250|UniProtKB:Q9H0H5, ECO:0000269|PubMed:10235109, CC ECO:0000269|PubMed:10493933, ECO:0000269|PubMed:10979956, CC ECO:0000269|PubMed:11287179}. 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-165 CC plays a major role in mediating binding. Interacts with RAB11FIP3; the CC interaction occurs at late telophase. Interacts with KIF23; the CC interaction is direct. Interacts with ANKLE1. CC {ECO:0000250|UniProtKB:Q9H0H5}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12590651}. Cytoplasm CC {ECO:0000269|PubMed:12590651}. Cytoplasm, cytoskeleton, spindle CC {ECO:0000269|PubMed:12590651}. Cytoplasmic vesicle, secretory vesicle, CC acrosome {ECO:0000269|PubMed:12590651}. Cleavage furrow CC {ECO:0000250|UniProtKB:Q9H0H5}. Midbody, Midbody ring CC {ECO:0000250|UniProtKB:Q9H0H5}. Cell membrane CC {ECO:0000250|UniProtKB:Q9H0H5}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:Q9H0H5}; Cytoplasmic side CC {ECO:0000250|UniProtKB:Q9H0H5}. Midbody {ECO:0000250|UniProtKB:Q9H0H5}. CC Note=During interphase, localized to the nucleus and cytoplasm along CC with microtubules, in anaphase, is redistributed to the central spindle CC and, in telophase and cytokinesis, to the midbody ring, also called CC Flemming body. Colocalizes with RHOA at the myosin contractile ring CC 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 (By similarity). CC Colocalizes with RND2 in Golgi-derived proacrosomal vesicles and the CC acrosome. Localizes to the midbody in a KIF23 and PRC1-dependent manner CC (By similarity). {ECO:0000250|UniProtKB:Q9H0H5}. CC -!- TISSUE SPECIFICITY: Highly expressed in testis, thymus and spleen and CC weakly expressed in brain, heart, skeletal muscle and kidney. In CC testis, expression is restricted to germ cells with the highest levels CC of expression found in spermatocytes. Not detected in adult liver. Also CC expressed in fetal liver and in several hematopoietic cell lines. CC {ECO:0000269|PubMed:10493933, ECO:0000269|PubMed:10979956, CC ECO:0000269|PubMed:11287179}. CC -!- DEVELOPMENTAL STAGE: At 6.5 dpc expressed in primitive endoderm, CC embryonic ectoderm, extraembryonic ectoderm and the ectoplacental cone. CC By 7.5 dpc, a widespread expression was observed in all intra- and CC extraembryonic tissues and also in the giant cells lining the inner CC boundary of the deciduum. At 9.5 dpc, expression was elevated in the CC neuroepithelium of the brain ventricles and the neural tube. By 12.5 CC dpc, expression remains widespread and in the brain higher levels were CC observed in the ventricular zone of the two telencephalic lobes, and in CC the mesencephalon and diencephalon, with the exception of the median CC sulcus. In adult brain, highest levels of expression were detected in CC cerebellum, specifically the Purkinje cell layer extending into the CC molecular layer. {ECO:0000269|PubMed:11287179}. CC -!- INDUCTION: Expression is down-regulated during macrophage CC differentiation of M1 cells. {ECO:0000269|PubMed:10979956}. CC -!- DOMAIN: The coiled coil region is indispensible for localization to the CC midbody during cytokinesis. {ECO:0000250|UniProtKB:Q9P2W2}. 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. {ECO:0000250}. CC -!- PTM: Phosphorylated at multiple sites in the midbody during cytokinesis CC (By similarity). Phosphorylation by AURKB on Ser-388 at the midbody is, CC at least in part, responsible for exerting its latent GAP activity CC towards RhoA (By similarity). Phosphorylation on multiple serine CC residues by PLK1 enhances its association with ECT2 and is critical for CC cleavage furrow formation (By similarity). Phosphorylation on Ser-165 CC plays a major role in mediating interaction with ECT2 (By similarity). CC Phosphorylation on Ser-158 does not appear to contribute to binding to CC ECT2 (By similarity). {ECO:0000250|UniProtKB:Q9H0H5}. 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; AF079974; AAD40487.1; -; mRNA. DR EMBL; AB030252; BAA90248.1; -; mRNA. DR EMBL; AF212320; AAG43539.1; -; mRNA. DR EMBL; AF212321; AAG43540.1; -; mRNA. DR EMBL; AK144608; BAE25967.1; -; mRNA. DR EMBL; AK154929; BAE32931.1; -; mRNA. DR EMBL; AK165897; BAE38446.1; -; mRNA. DR EMBL; AK166084; BAE38561.1; -; mRNA. DR EMBL; AK168020; BAE40005.1; -; mRNA. DR EMBL; AK168025; BAE40010.1; -; mRNA. DR EMBL; AK168170; BAE40131.1; -; mRNA. DR EMBL; AK168679; BAE40528.1; -; mRNA. DR EMBL; BC010715; AAH10715.1; -; mRNA. DR CCDS; CCDS27825.1; -. DR RefSeq; NP_001240737.1; NM_001253808.2. DR RefSeq; NP_001240738.1; NM_001253809.2. DR RefSeq; NP_001398794.1; NM_001411865.1. DR RefSeq; NP_001398795.1; NM_001411866.1. DR RefSeq; NP_036155.1; NM_012025.8. DR AlphaFoldDB; Q9WVM1; -. DR SMR; Q9WVM1; -. DR BioGRID; 205072; 48. DR DIP; DIP-42340N; -. DR FunCoup; Q9WVM1; 2070. DR IntAct; Q9WVM1; 46. DR MINT; Q9WVM1; -. DR STRING; 10090.ENSMUSP00000126417; -. DR GlyGen; Q9WVM1; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q9WVM1; -. DR PhosphoSitePlus; Q9WVM1; -. DR jPOST; Q9WVM1; -. DR PaxDb; 10090-ENSMUSP00000126417; -. DR PeptideAtlas; Q9WVM1; -. DR ProteomicsDB; 253121; -. DR Pumba; Q9WVM1; -. DR Antibodypedia; 14118; 608 antibodies from 43 providers. DR DNASU; 26934; -. DR Ensembl; ENSMUST00000023756.12; ENSMUSP00000023756.6; ENSMUSG00000023015.15. DR Ensembl; ENSMUST00000171702.8; ENSMUSP00000126417.2; ENSMUSG00000023015.15. DR GeneID; 26934; -. DR KEGG; mmu:26934; -. DR UCSC; uc007xpx.2; mouse. DR AGR; MGI:1349423; -. DR CTD; 29127; -. DR MGI; MGI:1349423; Racgap1. DR VEuPathDB; HostDB:ENSMUSG00000023015; -. DR eggNOG; KOG3564; Eukaryota. DR GeneTree; ENSGT00940000154610; -. DR HOGENOM; CLU_026187_1_0_1; -. DR InParanoid; Q9WVM1; -. DR OMA; FWEQYIV; -. DR OrthoDB; 2218807at2759; -. DR PhylomeDB; Q9WVM1; -. DR Reactome; R-MMU-2132295; MHC class II antigen presentation. DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic. DR Reactome; R-MMU-8980692; RHOA GTPase cycle. DR Reactome; R-MMU-9013026; RHOB GTPase cycle. DR Reactome; R-MMU-9013106; RHOC GTPase cycle. DR Reactome; R-MMU-9013148; CDC42 GTPase cycle. DR Reactome; R-MMU-9013149; RAC1 GTPase cycle. DR Reactome; R-MMU-9013404; RAC2 GTPase cycle. DR Reactome; R-MMU-9013423; RAC3 GTPase cycle. DR Reactome; R-MMU-983189; Kinesins. DR BioGRID-ORCS; 26934; 25 hits in 84 CRISPR screens. DR PRO; PR:Q9WVM1; -. DR Proteomes; UP000000589; Chromosome 15. DR RNAct; Q9WVM1; protein. DR Bgee; ENSMUSG00000023015; Expressed in ventricular zone and 234 other cell types or tissues. DR ExpressionAtlas; Q9WVM1; baseline and differential. DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell. DR GO; GO:0097149; C:centralspindlin complex; ISS:UniProtKB. DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:UniProtKB. DR GO; GO:0090543; C:Flemming body; IEA:UniProtKB-SubCell. DR GO; GO:0030496; C:midbody; ISS:UniProtKB. DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISO:GO_Central. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0005819; C:spindle; ISO:GO_Central. DR GO; GO:0051233; C:spindle midzone; ISS:UniProtKB. DR GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB. DR GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB. DR GO; GO:0043015; F:gamma-tubulin binding; ISS:UniProtKB. DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB. DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB. DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; ISO:GO_Central. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:GO_Central. DR GO; GO:0000915; P:actomyosin contractile ring assembly; ISS:UniProtKB. DR GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB. DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB. DR GO; GO:0051256; P:mitotic spindle midzone assembly; ISS:UniProtKB. DR GO; GO:0007405; P:neuroblast proliferation; IEP:UniProtKB. DR GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB. DR GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; ISS:UniProtKB. DR GO; GO:0045995; P:regulation of embryonic development; IMP:UniProtKB. DR GO; GO:0007266; P:Rho protein signal transduction; IBA:GO_Central. DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB. DR GO; GO:1902358; P:sulfate transmembrane transport; ISO:GO_Central. DR CDD; cd20821; C1_MgcRacGAP; 1. DR CDD; cd04382; RhoGAP_MgcRacGAP; 1. DR FunFam; 1.10.555.10:FF:000034; Rac GTPase-activating protein 1; 1. DR FunFam; 3.30.60.20:FF:000033; Rac GTPase-activating protein 1; 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; PKC_DAG/PE. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR InterPro; IPR000198; RhoGAP_dom. DR PANTHER; PTHR46199; RAC GTPASE-ACTIVATING PROTEIN 1; 1. DR PANTHER; PTHR46199:SF3; 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. PE 1: Evidence at protein level; KW Acetylation; Cell cycle; Cell division; Cell membrane; Coiled coil; KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Developmental protein; KW Differentiation; GTPase activation; Ion transport; Isopeptide bond; KW Lipid-binding; Membrane; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Spermatogenesis; Transport; Ubl conjugation; Zinc; KW Zinc-finger. FT CHAIN 1..628 FT /note="Rac GTPase-activating protein 1" FT /id="PRO_0000228809" FT DOMAIN 350..540 FT /note="Rho-GAP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172" FT ZN_FING 287..336 FT /note="Phorbol-ester/DAG-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226" FT REGION 107..286 FT /note="Interaction with SLC26A8" FT /evidence="ECO:0000250" FT REGION 179..201 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 242..284 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 33..110 FT /evidence="ECO:0000255" FT COMPBIAS 274..283 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 386 FT /note="Arginine finger; crucial for GTP hydrolysis by FT stabilizing the transition state" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:Q9H0H5" FT MOD_RES 150 FT /note="Phosphoserine; by PLK1" FT /evidence="ECO:0000250|UniProtKB:Q9H0H5" FT MOD_RES 155 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H0H5" FT MOD_RES 158 FT /note="Phosphoserine; by PLK1" FT /evidence="ECO:0000250|UniProtKB:Q9H0H5" FT MOD_RES 162 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9H0H5" FT MOD_RES 165 FT /note="Phosphoserine; by PLK1" FT /evidence="ECO:0000250|UniProtKB:Q9H0H5" FT MOD_RES 171 FT /note="Phosphoserine; by PLK1" FT /evidence="ECO:0000250|UniProtKB:Q9H0H5" FT MOD_RES 204 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H0H5" FT MOD_RES 207 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H0H5" FT MOD_RES 215 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H0H5" FT MOD_RES 258 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H0H5" FT MOD_RES 343 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9H0H5" FT MOD_RES 388 FT /note="Phosphoserine; by AURKB" FT /evidence="ECO:0000250|UniProtKB:Q9H0H5" FT MOD_RES 411 FT /note="Phosphoserine; by AURKB" FT /evidence="ECO:0000250|UniProtKB:Q9H0H5" FT MOD_RES 564 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 577 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 585 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 602 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9H0H5" FT CROSSLNK 249 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H0H5" FT CROSSLNK 405 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H0H5" FT CONFLICT 29..31 FT /note="IEF -> MES (in Ref. 4; BAE38561)" FT /evidence="ECO:0000305" FT CONFLICT 100 FT /note="Q -> E (in Ref. 4; BAE40131/BAE40010)" FT /evidence="ECO:0000305" FT CONFLICT 398 FT /note="K -> E (in Ref. 4; BAE40005)" FT /evidence="ECO:0000305" FT CONFLICT 623 FT /note="P -> T (in Ref. 4; BAE40005)" FT /evidence="ECO:0000305" SQ SEQUENCE 628 AA; 70158 MW; 8D1B9DEC3CE057BE CRC64; MDTTMVNLWT LFEQLVRRME IINEGNESIE FIQVVKDFED FRKKYQRTNQ ELEKFKDLLL KAETGRSALD VKLKHARNQV DVEIKRRQRA EAECAKLEQQ IQLIRDILMC DTSGSIQLSE EQKSALAFLN RGQASSGHAG NNRLSTIDES GSILSDISFD KTDESLDWDS SLVKNFKMKK REKRRSNSRQ FIDGPPGPVK KTCSIGSTVD QANESIVAKT TVTVPSDGGP IEAVSTIETL PSWTRSRGKS GPLQPVNSDS ALNSRPLEPR TDTDNLGTPQ NTGGMRLHDF VSKTVIKPES CVPCGKRIKF GKLSLKCRDC RLVSHPECRD RCPLPCIPPL VGTPVKIGEG MLADFVSQAS PMIPAIVVSC VNEIEQRGLT EAGLYRISGC DRTVKELKEK FLKVKTVPLL SKVDDIHVIC SLLKDFLRNL KEPLLTFWLS KAFMEAAEIT DEDNSTAAMY QAVSELPQAN RDTLAFLMIH LQRVSQSPDT KMDIANLAKV FGPTIVAHTV PNPDPVTMFQ DIKRQLKVVE RLLSLPLEYW NQFMMVDQEN IDSQRGNGNS TPRTPDVKVS LLGPVTTPEF QLVKTPLSSS LSQRLYNLSK STPRFGNKSK SATNLGQQGK FFPAPYLK //