##gff-version 3 P32455 UniProtKB Chain 1 589 . . . ID=PRO_0000190963;Note=Guanylate-binding protein 1 P32455 UniProtKB Propeptide 590 592 . . . ID=PRO_0000396777;Note=Removed in mature form;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:8830800;Dbxref=PMID:8830800 P32455 UniProtKB Domain 35 278 . . . Note=GB1/RHD3-type G;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01052 P32455 UniProtKB Region 1 311 . . . Note=GTPase domain (Globular);Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10676968;Dbxref=PMID:10676968 P32455 UniProtKB Binding site 45 52 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:10676968,ECO:0000269|PubMed:10970849,ECO:0000269|PubMed:16511497,ECO:0007744|PDB:1F5N,ECO:0007744|PDB:2B8W,ECO:0007744|PDB:2B92,ECO:0007744|PDB:2D4H;Dbxref=PMID:10676968,PMID:10970849,PMID:16511497 P32455 UniProtKB Binding site 67 69 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:10676968,ECO:0000269|PubMed:10970849,ECO:0000269|PubMed:16511497,ECO:0007744|PDB:1F5N,ECO:0007744|PDB:2B8W,ECO:0007744|PDB:2B92,ECO:0007744|PDB:2D4H;Dbxref=PMID:10676968,PMID:10970849,PMID:16511497 P32455 UniProtKB Binding site 97 101 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10676968,ECO:0000269|PubMed:10970849,ECO:0007744|PDB:1F5N;Dbxref=PMID:10676968,PMID:10970849 P32455 UniProtKB Modified residue 156 156 . . . Note=Phosphoserine%3B by PIM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:37797010;Dbxref=PMID:37797010 P32455 UniProtKB Modified residue 589 589 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:8830800;Dbxref=PMID:8830800 P32455 UniProtKB Modified residue 590 590 . . . Note=Phosphothreonine%3B by PIM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:37797010;Dbxref=PMID:37797010 P32455 UniProtKB Lipidation 589 589 . . . Note=S-farnesyl cysteine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29144452,ECO:0000269|PubMed:31268602,ECO:0000269|PubMed:32510692,ECO:0000269|PubMed:8830800;Dbxref=PMID:29144452,PMID:31268602,PMID:32510692,PMID:8830800 P32455 UniProtKB Cross-link 207 207 . . . Note=(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29144452;Dbxref=PMID:29144452 P32455 UniProtKB Cross-link 209 209 . . . Note=(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29144452;Dbxref=PMID:29144452 P32455 UniProtKB Cross-link 210 210 . . . Note=(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29144452;Dbxref=PMID:29144452 P32455 UniProtKB Cross-link 382 382 . . . Note=(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29144452;Dbxref=PMID:29144452 P32455 UniProtKB Cross-link 562 562 . . . Note=(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29144452;Dbxref=PMID:29144452 P32455 UniProtKB Cross-link 567 567 . . . Note=(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29144452;Dbxref=PMID:29144452 P32455 UniProtKB Cross-link 573 573 . . . Note=(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29144452;Dbxref=PMID:29144452 P32455 UniProtKB Cross-link 587 587 . . . Note=(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29144452;Dbxref=PMID:29144452 P32455 UniProtKB Natural variant 78 78 . . . ID=VAR_033950;Note=I->V;Dbxref=dbSNP:rs1048401 P32455 UniProtKB Natural variant 166 166 . . . ID=VAR_033951;Note=E->D;Dbxref=dbSNP:rs17130717 P32455 UniProtKB Natural variant 349 349 . . . ID=VAR_014849;Note=T->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:1715024,ECO:0000269|Ref.2;Dbxref=dbSNP:rs1048425,PMID:15489334,PMID:1715024 P32455 UniProtKB Natural variant 409 409 . . . ID=VAR_046550;Note=A->G;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:1715024,ECO:0000269|Ref.2;Dbxref=dbSNP:rs1048443,PMID:15489334,PMID:1715024 P32455 UniProtKB Mutagenesis 48 48 . . . Note=Abolished GTPase activity. R->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28645896,ECO:0000269|PubMed:29144452,ECO:0000269|PubMed:32510692;Dbxref=PMID:28645896,PMID:29144452,PMID:32510692 P32455 UniProtKB Mutagenesis 51 51 . . . Note=Loss of GTPase activity. Constitutively monomeric. Expressed throughout the cytoplasm%2C loss of vesicular accumulation. Impaired ability to promote pyroptosis in response to T.gondii infection. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:31268602,ECO:0000269|PubMed:32510692,ECO:0000305|PubMed:21151871;Dbxref=PMID:21151871,PMID:31268602,PMID:32510692 P32455 UniProtKB Mutagenesis 61 63 . . . Note=Impaired homooligomarization and localization to bacterial surface. KKK->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32581219;Dbxref=PMID:32581219 P32455 UniProtKB Mutagenesis 74 74 . . . Note=Abolished GDP hydrolysis. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32510692;Dbxref=PMID:32510692 P32455 UniProtKB Mutagenesis 76 76 . . . Note=Abolished GDPase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28645896;Dbxref=PMID:28645896 P32455 UniProtKB Mutagenesis 87 88 . . . Note=Does not affect localization to bacterial surface. KK->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32581219;Dbxref=PMID:32581219 P32455 UniProtKB Mutagenesis 151 151 . . . Note=Reduced phosphorylation by PIM1. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:37797010;Dbxref=PMID:37797010 P32455 UniProtKB Mutagenesis 153 158 . . . Note=Abolished phosphorylation by PIM1 and interaction with 14-3-3 protein sigma (SFN). RSKSSP->ASKSSA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:37797010;Dbxref=PMID:37797010 P32455 UniProtKB Mutagenesis 153 153 . . . Note=Abolished phosphorylation by PIM1. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:37797010;Dbxref=PMID:37797010 P32455 UniProtKB Mutagenesis 155 155 . . . Note=Abolished phosphorylation by PIM1. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:37797010;Dbxref=PMID:37797010 P32455 UniProtKB Mutagenesis 156 156 . . . Note=Reduced phosphorylation by PIM1%2C leading to hyperactivation and Golgi fragmentation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:37797010;Dbxref=PMID:37797010 P32455 UniProtKB Mutagenesis 157 157 . . . Note=No effect. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:37797010;Dbxref=PMID:37797010 P32455 UniProtKB Mutagenesis 184 184 . . . Note=Strongly decreased nucleotide-binding. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29144452;Dbxref=PMID:29144452 P32455 UniProtKB Mutagenesis 207 210 . . . Note=Does not affect localization to bacterial surface. KLKK->ALAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32581219;Dbxref=PMID:32581219 P32455 UniProtKB Mutagenesis 207 207 . . . Note=In 8KR mutant%3B abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-209%2C R-210%2C R-382%2C R-562%2C R-567%2C R-573 and R-587. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29144452;Dbxref=PMID:29144452 P32455 UniProtKB Mutagenesis 209 209 . . . Note=In 8KR mutant%3B abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-207%2C R-210%2C R-382%2C R-562%2C R-567%2C R-573 and R-587. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29144452;Dbxref=PMID:29144452 P32455 UniProtKB Mutagenesis 210 210 . . . Note=In 8KR mutant%3B abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-207%2C R-209%2C R-382%2C R-562%2C R-567%2C R-573 and R-587. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29144452;Dbxref=PMID:29144452 P32455 UniProtKB Mutagenesis 227 228 . . . Note=Constitutively dimeric. Localizes at vesicle-like structures at the plasma membrane. RK->EE;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21151871,ECO:0000269|PubMed:31268602;Dbxref=PMID:21151871,PMID:31268602 P32455 UniProtKB Mutagenesis 244 246 . . . Note=Does not affect localization to bacterial surface. RRK->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32581219;Dbxref=PMID:32581219 P32455 UniProtKB Mutagenesis 382 382 . . . Note=In 8KR mutant%3B abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-207%2C R-209%2C R-210%2C R-562%2C R-567%2C R-573 and R-587. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29144452;Dbxref=PMID:29144452 P32455 UniProtKB Mutagenesis 427 427 . . . Note=No effect. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:37797010;Dbxref=PMID:37797010 P32455 UniProtKB Mutagenesis 562 562 . . . Note=In 8KR mutant%3B abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-207%2C R-209%2C R-210%2C R-382%2C R-567%2C R-573 and R-587. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29144452;Dbxref=PMID:29144452 P32455 UniProtKB Mutagenesis 567 567 . . . Note=In 8KR mutant%3B abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-207%2C R-209%2C R-210%2C R-382%2C R-562%2C R-573 and R-587. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29144452;Dbxref=PMID:29144452 P32455 UniProtKB Mutagenesis 573 573 . . . Note=In 8KR mutant%3B abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-207%2C R-209%2C R-210%2C R-382%2C R-562%2C R-567 and R-587. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29144452;Dbxref=PMID:29144452 P32455 UniProtKB Mutagenesis 584 586 . . . Note=Abolished localization to pathogen-containing vacuoles. Abolished binding to bacterial surface. RRR->AAA;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29233899,ECO:0000269|PubMed:32510692;Dbxref=PMID:29233899,PMID:32510692 P32455 UniProtKB Mutagenesis 584 586 . . . Note=Abolished localization to pathogen-containing vacuoles. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29233899;Dbxref=PMID:29233899 P32455 UniProtKB Mutagenesis 587 587 . . . Note=In 8KR mutant%3B abolished ubiquitination by S. flexneri IpaH9.8 when associated with R-207%2C R-209%2C R-210%2C R-382%2C R-562%2C R-567 and R-573. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29144452;Dbxref=PMID:29144452 P32455 UniProtKB Mutagenesis 589 592 . . . Note=Loss of association with membranes. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21151871;Dbxref=PMID:21151871 P32455 UniProtKB Mutagenesis 589 589 . . . Note=Abolished farnesylation and recruitment to the pathogen-containing vacuoles or vacuole-escaped bacteria. Impaired ability to promote pyroptosis in response to T.gondii infection. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29144452,ECO:0000269|PubMed:31268602;Dbxref=PMID:29144452,PMID:31268602 P32455 UniProtKB Mutagenesis 590 590 . . . Note=Does not affect interaction with 14-3-3 protein sigma (SFN). T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:37797010;Dbxref=PMID:37797010 P32455 UniProtKB Beta strand 11 17 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Beta strand 20 23 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 25 32 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Beta strand 36 46 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 47 49 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DG3 P32455 UniProtKB Helix 51 58 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Beta strand 62 65 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2B8W P32455 UniProtKB Beta strand 70 72 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Beta strand 77 84 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Beta strand 86 88 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Beta strand 92 98 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Turn 101 103 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DG3 P32455 UniProtKB Helix 104 106 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 112 122 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Beta strand 124 132 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 136 140 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 143 146 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 148 151 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Beta strand 156 158 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2D4H P32455 UniProtKB Helix 167 170 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 171 174 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Beta strand 177 183 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Beta strand 192 194 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 198 205 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 214 229 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Beta strand 233 237 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 244 252 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 255 257 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 260 276 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Turn 283 285 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 290 306 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 312 342 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 350 371 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 376 378 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 379 423 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Turn 424 427 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 432 449 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 457 467 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 469 478 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Beta strand 480 482 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 484 563 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N P32455 UniProtKB Helix 566 582 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F5N