##gff-version 3 Q9H0H5 UniProtKB Chain 1 632 . . . ID=PRO_0000228808;Note=Rac GTPase-activating protein 1 Q9H0H5 UniProtKB Domain 349 539 . . . Note=Rho-GAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00172 Q9H0H5 UniProtKB Zinc finger 286 335 . . . Note=Phorbol-ester/DAG-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00226 Q9H0H5 UniProtKB Region 106 285 . . . Note=Interaction with SLC26A8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11278976;Dbxref=PMID:11278976 Q9H0H5 UniProtKB Region 183 211 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H0H5 UniProtKB Region 249 283 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H0H5 UniProtKB Region 582 632 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H0H5 UniProtKB Coiled coil 53 110 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9H0H5 UniProtKB Compositional bias 583 624 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H0H5 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378 Q9H0H5 UniProtKB Modified residue 149 149 . . . Note=Phosphoserine%3B by PLK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19468300;Dbxref=PMID:19468300 Q9H0H5 UniProtKB Modified residue 154 154 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692;Dbxref=PMID:19690332,PMID:20068231,PMID:21406692 Q9H0H5 UniProtKB Modified residue 157 157 . . . Note=Phosphoserine%3B by PLK1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:19468300,ECO:0000269|PubMed:19468302,ECO:0000269|PubMed:25068414,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692;Dbxref=PMID:19468300,PMID:19468302,PMID:19690332,PMID:20068231,PMID:21406692,PMID:25068414 Q9H0H5 UniProtKB Modified residue 161 161 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:17081983;Dbxref=PMID:17081983 Q9H0H5 UniProtKB Modified residue 164 164 . . . Note=Phosphoserine%3B by PLK1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:19468300,ECO:0000269|PubMed:19468302,ECO:0000269|PubMed:25068414,ECO:0007744|PubMed:17081983;Dbxref=PMID:17081983,PMID:19468300,PMID:19468302,PMID:25068414 Q9H0H5 UniProtKB Modified residue 170 170 . . . Note=Phosphoserine%3B by PLK1;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19468300,ECO:0000269|PubMed:19468302;Dbxref=PMID:19468300,PMID:19468302 Q9H0H5 UniProtKB Modified residue 203 203 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:16964243,ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:16964243,PMID:17081983,PMID:18669648,PMID:19690332,PMID:20068231,PMID:23186163 Q9H0H5 UniProtKB Modified residue 206 206 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:19690332,PMID:23186163 Q9H0H5 UniProtKB Modified residue 214 214 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:19468302,ECO:0007744|PubMed:23186163;Dbxref=PMID:19468302,PMID:23186163 Q9H0H5 UniProtKB Modified residue 249 249 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q9H0H5 UniProtKB Modified residue 257 257 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163 Q9H0H5 UniProtKB Modified residue 260 260 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19468302;Dbxref=PMID:19468302 Q9H0H5 UniProtKB Modified residue 342 342 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231;Dbxref=PMID:18669648,PMID:20068231 Q9H0H5 UniProtKB Modified residue 387 387 . . . Note=Phosphoserine%3B by AURKB;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12689593;Dbxref=PMID:12689593 Q9H0H5 UniProtKB Modified residue 410 410 . . . Note=Phosphoserine%3B by AURKB;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12689593;Dbxref=PMID:12689593 Q9H0H5 UniProtKB Modified residue 567 567 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:20068231;Dbxref=PMID:20068231 Q9H0H5 UniProtKB Modified residue 580 580 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163 Q9H0H5 UniProtKB Modified residue 588 588 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:16964243,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231;Dbxref=PMID:16964243,PMID:18669648,PMID:20068231 Q9H0H5 UniProtKB Modified residue 600 600 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q9H0H5 UniProtKB Modified residue 601 601 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q9H0H5 UniProtKB Modified residue 606 606 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q9H0H5 UniProtKB Modified residue 628 628 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q9H0H5 UniProtKB Cross-link 248 248 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q9H0H5 UniProtKB Cross-link 404 404 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q9H0H5 UniProtKB Natural variant 396 396 . . . ID=VAR_087032;Note=In CDAN3B%3B decreased function in erythropoiesis as shown by partial rescue of multinucleation defects in RACGAP1-deficient erythroid cells%3B decreased GAP activity towards RHOA%2C RAC1 and CDC42. L->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34818416;Dbxref=PMID:34818416 Q9H0H5 UniProtKB Natural variant 432 432 . . . ID=VAR_087033;Note=In CDAN3B%3B loss of function in erythropoiesis as it does not rescue multinucleation and cytokinesis defects in RACGAP1-deficient erythroid and Hela cells%3B increased GAP activity towards RHOA%3B no effect on GAP activity towards RAC1 and CDC42. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34818416;Dbxref=PMID:34818416 Q9H0H5 UniProtKB Mutagenesis 149 149 . . . Note=Does not inhibit interaction with ECT2. Strongly reduces phosphorylation%2C inhibits interaction with ECT2 and cleavage furrow formation%3B when associated with A-157%3B A-164 and A-170. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19468300;Dbxref=PMID:19468300 Q9H0H5 UniProtKB Mutagenesis 157 157 . . . Note=Does not inhibit interaction with ECT2. Strongly reduces phosphorylation%2C inhibits interaction with ECT2 and cleavage furrow formation%3B when associated with A-149%3B A-164 and A-170. Strongly reduces phosphorylation by PLK1%2C inhibits interaction with ECT2 and cleavage furrow formation%3B when associated with A-164%3B A-170 and A-214. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19468300,ECO:0000269|PubMed:19468302;Dbxref=PMID:19468300,PMID:19468302 Q9H0H5 UniProtKB Mutagenesis 164 164 . . . Note=Does not inhibit interaction with ECT2. Strongly reduces phosphorylation%2C inhibits interaction with ECT2 and cleavage furrow formation%3B when associated with A-149%3B A-157 and A-170. Strongly reduces phosphorylation by PLK1%2C inhibits interaction with ECT2 and cleavage furrow formation%3B when associated with A-157%3B A-170 and A-214. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19468300,ECO:0000269|PubMed:19468302;Dbxref=PMID:19468300,PMID:19468302 Q9H0H5 UniProtKB Mutagenesis 167 167 . . . Note=More than 20-fold reduction in binding to ECT2. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25068414;Dbxref=PMID:25068414 Q9H0H5 UniProtKB Mutagenesis 170 170 . . . Note=Does not inhibit interaction with ECT2. Strongly reduces phosphorylation%2C inhibits interaction with ECT2 and cleavage furrow formation%3B when associated with A-149%3B A-157 and A-164. Strongly reduces phosphorylation by PLK1%2C inhibits interaction with ECT2 and cleavage furrow formation%3B when associated with A-157%3B A-164 and A-214. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19468300,ECO:0000269|PubMed:19468302;Dbxref=PMID:19468300,PMID:19468302 Q9H0H5 UniProtKB Mutagenesis 214 214 . . . Note=Strongly reduces phosphorylation by PLK1%2C inhibits interaction with ECT2 and cleavage furrow formation%3B when associated with A-157%3B A-164 and A-170. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19468302;Dbxref=PMID:19468302 Q9H0H5 UniProtKB Mutagenesis 289 289 . . . Note=Cytokinesis failure. F->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23235882;Dbxref=PMID:23235882 Q9H0H5 UniProtKB Mutagenesis 292 292 . . . Note=Cytokinesis failure. Abolishes localization at the cell membrane. K->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23235882;Dbxref=PMID:23235882 Q9H0H5 UniProtKB Mutagenesis 306 306 . . . Note=Cytokinesis failure. Abolishes localization at the cell membrane. R->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23235882;Dbxref=PMID:23235882 Q9H0H5 UniProtKB Mutagenesis 309 309 . . . Note=Cytokinesis failure. Abolishes localization at the cell membrane. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23235882;Dbxref=PMID:23235882 Q9H0H5 UniProtKB Mutagenesis 316 316 . . . Note=Cytokinesis failure. C->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23235882;Dbxref=PMID:23235882 Q9H0H5 UniProtKB Mutagenesis 385 385 . . . Note=Abolishes GAP activity towards RAC1. Abolishes GAP activity towards CDC42 in prometaphase. Abolishes GAP activity towards RHOA. Induces multiple blebs during cytokinesis. R->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10979956,ECO:0000269|PubMed:14729465,ECO:0000269|PubMed:15642749,ECO:0000269|PubMed:34818416;Dbxref=PMID:10979956,PMID:14729465,PMID:15642749,PMID:34818416 Q9H0H5 UniProtKB Sequence conflict 155 155 . . . Note=D->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9H0H5 UniProtKB Sequence conflict 518 518 . . . Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9H0H5 UniProtKB Beta strand 289 293 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B6D Q9H0H5 UniProtKB Turn 301 303 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B6D Q9H0H5 UniProtKB Beta strand 312 320 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B6D Q9H0H5 UniProtKB Helix 325 330 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4B6D Q9H0H5 UniProtKB Helix 351 353 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C2K Q9H0H5 UniProtKB Beta strand 357 360 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C2K Q9H0H5 UniProtKB Helix 364 376 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C2K Q9H0H5 UniProtKB Turn 377 379 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C2K Q9H0H5 UniProtKB Turn 381 385 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C2K Q9H0H5 UniProtKB Helix 390 403 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C2K Q9H0H5 UniProtKB Helix 409 411 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C2K Q9H0H5 UniProtKB Helix 415 427 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C2K Q9H0H5 UniProtKB Beta strand 429 431 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C2K Q9H0H5 UniProtKB Turn 436 438 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C2K Q9H0H5 UniProtKB Helix 439 447 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C2K Q9H0H5 UniProtKB Helix 451 464 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C2K Q9H0H5 UniProtKB Helix 467 485 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C2K Q9H0H5 UniProtKB Turn 487 489 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C2K Q9H0H5 UniProtKB Helix 493 504 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C2K Q9H0H5 UniProtKB Beta strand 508 511 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C2K Q9H0H5 UniProtKB Helix 514 520 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C2K Q9H0H5 UniProtKB Helix 523 532 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C2K Q9H0H5 UniProtKB Helix 536 541 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C2K Q9H0H5 UniProtKB Turn 542 544 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5C2K