##gff-version 3 Q9H257 UniProtKB Chain 1 536 . . . ID=PRO_0000144082;Note=Caspase recruitment domain-containing protein 9 Q9H257 UniProtKB Domain 6 98 . . . Note=CARD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00046 Q9H257 UniProtKB Region 99 116 . . . Note=Linker;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:31296852;Dbxref=PMID:31296852 Q9H257 UniProtKB Region 427 536 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H257 UniProtKB Coiled coil 117 277 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9H257 UniProtKB Coiled coil 332 419 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9H257 UniProtKB Compositional bias 484 505 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H257 UniProtKB Compositional bias 512 528 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9H257 UniProtKB Binding site 3 3 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:31296852,ECO:0007744|PDB:6N2M;Dbxref=PMID:31296852 Q9H257 UniProtKB Binding site 10 10 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:30206119,ECO:0000269|PubMed:31296852,ECO:0007744|PDB:6E27,ECO:0007744|PDB:6N2M;Dbxref=PMID:30206119,PMID:31296852 Q9H257 UniProtKB Binding site 73 73 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:30206119,ECO:0000269|PubMed:31296852,ECO:0007744|PDB:6E27,ECO:0007744|PDB:6N2M;Dbxref=PMID:30206119,PMID:31296852 Q9H257 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9EPY0 Q9H257 UniProtKB Modified residue 231 231 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:A2AIV8 Q9H257 UniProtKB Modified residue 277 277 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q9H257 UniProtKB Modified residue 424 424 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9EPY0 Q9H257 UniProtKB Modified residue 425 425 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q9H257 UniProtKB Modified residue 431 431 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:A2AIV8 Q9H257 UniProtKB Modified residue 450 450 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9EPY0 Q9H257 UniProtKB Modified residue 460 460 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18088087;Dbxref=PMID:18088087 Q9H257 UniProtKB Modified residue 483 483 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q9H257 UniProtKB Modified residue 498 498 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q9H257 UniProtKB Modified residue 531 531 . . . Note=Phosphothreonine%3B by CK2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9EPY0 Q9H257 UniProtKB Modified residue 533 533 . . . Note=Phosphothreonine%3B by CK2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9EPY0 Q9H257 UniProtKB Cross-link 125 125 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26488816,ECO:0000269|PubMed:31296852,ECO:0000269|PubMed:33093067;Dbxref=PMID:26488816,PMID:31296852,PMID:33093067 Q9H257 UniProtKB Alternative sequence 360 366 . . . ID=VSP_024390;Note=In isoform 3. AIATREE->STQMEGL;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q9H257 UniProtKB Alternative sequence 367 536 . . . ID=VSP_024391;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q9H257 UniProtKB Alternative sequence 482 492 . . . ID=VSP_024392;Note=In isoform 2. LSSGEPPEKER->PAGLPGIGAVC;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q9H257 UniProtKB Alternative sequence 493 536 . . . ID=VSP_024393;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q9H257 UniProtKB Natural variant 12 12 . . . ID=VAR_048607;Note=S->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11053425,ECO:0000269|PubMed:14702039;Dbxref=dbSNP:rs4077515,PMID:11053425,PMID:14702039 Q9H257 UniProtKB Natural variant 18 18 . . . ID=VAR_084630;Note=In IMD103%3B reduced cytokine production in response to C.albicans infection%3B impaired NF-kappa-B transcriptional activity. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25057046;Dbxref=PMID:25057046 Q9H257 UniProtKB Natural variant 23 536 . . . ID=VAR_084631;Note=In IMD103%3B reduced cytokine production in response to C.albicans infection%3B impaired NF-kappa-B transcriptional activity. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29080677;Dbxref=PMID:29080677 Q9H257 UniProtKB Natural variant 35 35 . . . ID=VAR_084632;Note=In IMD103%3B abolished homooligomerization and formation of BCL10-nucleating filaments%3B reduced cytokine production in response to C.albicans infection%3B reduced production IgG antibodies in response to C.albicans infection. R->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25702837,ECO:0000269|PubMed:31296852,ECO:0000269|PubMed:33548172;Dbxref=dbSNP:rs1454037218,PMID:25702837,PMID:31296852,PMID:33548172 Q9H257 UniProtKB Natural variant 57 57 . . . ID=VAR_084633;Note=In IMD103%3B reduced cytokine production in response to C.albicans infection. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26679537;Dbxref=dbSNP:rs940550122,PMID:26679537 Q9H257 UniProtKB Natural variant 70 70 . . . ID=VAR_084634;Note=In IMD103%3B reduced cytokine production in response to C.albicans infection%3B impaired NF-kappa-B transcriptional activity%3B reduced production IgG antibodies in response to C.albicans infection. R->W;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25702837,ECO:0000269|PubMed:26961233,ECO:0000269|PubMed:33548172,ECO:0000269|PubMed:33558980;Dbxref=dbSNP:rs767522068,PMID:25702837,PMID:26961233,PMID:33548172,PMID:33558980 Q9H257 UniProtKB Natural variant 72 72 . . . ID=VAR_070828;Note=In IMD103. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23335372;Dbxref=dbSNP:rs398122362,PMID:23335372 Q9H257 UniProtKB Natural variant 91 91 . . . ID=VAR_084635;Note=In IMD103%3B does not affect formation of the CBM complex but impairs formation of a complex with RASGRF1. Y->H;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24704721,ECO:0000269|PubMed:26521038,ECO:0000269|PubMed:31469433;Dbxref=dbSNP:rs921151054,PMID:24704721,PMID:26521038,PMID:31469433 Q9H257 UniProtKB Natural variant 101 101 . . . ID=VAR_070829;Note=In IMD103. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24131138;Dbxref=dbSNP:rs398122364,PMID:24131138 Q9H257 UniProtKB Natural variant 101 101 . . . ID=VAR_084636;Note=In IMD103. R->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26044242;Dbxref=PMID:26044242 Q9H257 UniProtKB Natural variant 158 536 . . . ID=VAR_084637;Note=In IMD103%3B decreased production of cytokines in CD4(+) Th17 cells. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24231284;Dbxref=PMID:24231284 Q9H257 UniProtKB Natural variant 196 196 . . . ID=VAR_084638;Note=In IMD103%3B reduced cytokine production in response to C.albicans infection%3B does not affect NF-kappa-B transcriptional activity. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33558980;Dbxref=dbSNP:rs768281299,PMID:33558980 Q9H257 UniProtKB Natural variant 289 536 . . . ID=VAR_084639;Note=In IMD103%3B reduced production IgG antibodies in response to C.albicans infection. Missing;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24131138,ECO:0000269|PubMed:25372963,ECO:0000269|PubMed:25702837,ECO:0000269|PubMed:28391957,ECO:0000269|PubMed:33548172;Dbxref=PMID:24131138,PMID:25372963,PMID:25702837,PMID:28391957,PMID:33548172 Q9H257 UniProtKB Natural variant 295 536 . . . ID=VAR_084640;Note=In IMD103%3B reduced cytokine production in response to C.albicans infection. Missing;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19864672,ECO:0000269|PubMed:25702837,ECO:0000269|PubMed:25933095,ECO:0000269|PubMed:26658378,ECO:0000269|PubMed:27777981,ECO:0000269|PubMed:29307770;Dbxref=PMID:19864672,PMID:25702837,PMID:25933095,PMID:26658378,PMID:27777981,PMID:29307770 Q9H257 UniProtKB Natural variant 323 323 . . . ID=VAR_084641;Note=In IMD103. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25057046;Dbxref=dbSNP:rs775284320,PMID:25057046 Q9H257 UniProtKB Natural variant 373 373 . . . ID=VAR_070830;Note=In IMD103%3B reduced cytokine production in response to C.albicans infection%3B does not affect NF-kappa-B transcriptional activity. R->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23335372,ECO:0000269|PubMed:33558980;Dbxref=dbSNP:rs149712114,PMID:23335372,PMID:33558980 Q9H257 UniProtKB Natural variant 380 380 . . . ID=VAR_084642;Note=In IMD103. A->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26941346;Dbxref=PMID:26941346 Q9H257 UniProtKB Mutagenesis 10 10 . . . Note=Strongly reduced zinc-binding. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30206119;Dbxref=PMID:30206119 Q9H257 UniProtKB Mutagenesis 15 15 . . . Note=Abolished homooligomerization and formation of BCL10-nucleating filaments. E->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31296852;Dbxref=PMID:31296852 Q9H257 UniProtKB Mutagenesis 35 35 . . . Note=Abolished homooligomerization and formation of BCL10-nucleating filaments. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31296852;Dbxref=PMID:31296852 Q9H257 UniProtKB Mutagenesis 37 37 . . . Note=Does not affect zinc-binbing. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30206119;Dbxref=PMID:30206119 Q9H257 UniProtKB Mutagenesis 43 43 . . . Note=Abolished homooligomerization and formation of BCL10-nucleating filaments. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31296852;Dbxref=PMID:31296852 Q9H257 UniProtKB Mutagenesis 58 58 . . . Note=Abolished homooligomerization and formation of BCL10-nucleating filaments. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31296852;Dbxref=PMID:31296852 Q9H257 UniProtKB Mutagenesis 66 66 . . . Note=Abolished homooligomerization and formation of BCL10-nucleating filaments. D->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31296852;Dbxref=PMID:31296852 Q9H257 UniProtKB Mutagenesis 73 73 . . . Note=Strongly reduced zinc-binding. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30206119;Dbxref=PMID:30206119 Q9H257 UniProtKB Mutagenesis 101 101 . . . Note=Disruption of the linker region%2C relieving autoinhibition and leading to activation of NF-kappa-B. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31296852;Dbxref=PMID:31296852 Q9H257 UniProtKB Mutagenesis 103 103 . . . Note=Disruption of the linker region%2C relieving autoinhibition and leading to activation of NF-kappa-B. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31296852;Dbxref=PMID:31296852 Q9H257 UniProtKB Mutagenesis 107 107 . . . Note=Disruption of the linker region%2C relieving autoinhibition and leading to activation of NF-kappa-B. Constitutively forms BCL10-nucleating filaments. I->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31296852;Dbxref=PMID:31296852 Q9H257 UniProtKB Mutagenesis 111 111 . . . Note=Disruption of the linker region%2C relieving autoinhibition and leading to activation of NF-kappa-B. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31296852;Dbxref=PMID:31296852 Q9H257 UniProtKB Mutagenesis 114 114 . . . Note=Disruption of the linker region%2C relieving autoinhibition and leading to activation of NF-kappa-B. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31296852;Dbxref=PMID:31296852 Q9H257 UniProtKB Mutagenesis 115 115 . . . Note=Disruption of the linker region%2C relieving autoinhibition and leading to activation of NF-kappa-B. Constitutively forms BCL10-nucleating filaments. L->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31296852;Dbxref=PMID:31296852 Q9H257 UniProtKB Mutagenesis 125 125 . . . Note=Reduced cytokine production in response to C.albicans infection. Impaired NF-kappa-B transcriptional activity. Does not affect interaction with BCL10. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26488816;Dbxref=PMID:26488816 Q9H257 UniProtKB Turn 7 9 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6E28 Q9H257 UniProtKB Helix 10 14 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6E28 Q9H257 UniProtKB Helix 15 17 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6E28 Q9H257 UniProtKB Helix 18 24 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6E28 Q9H257 UniProtKB Helix 27 29 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6E28 Q9H257 UniProtKB Helix 31 36 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6E28 Q9H257 UniProtKB Helix 42 49 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6E28 Q9H257 UniProtKB Helix 54 69 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6E28 Q9H257 UniProtKB Turn 70 72 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6E28 Q9H257 UniProtKB Helix 73 86 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6E28 Q9H257 UniProtKB Helix 88 95 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6E28 Q9H257 UniProtKB Beta strand 96 98 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6N2M Q9H257 UniProtKB Helix 104 110 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6N2M Q9H257 UniProtKB Helix 112 138 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6N2M