##gff-version 3 Q9Y6K9 UniProtKB Chain 1 419 . . . ID=PRO_0000096782;Note=NF-kappa-B essential modulator Q9Y6K9 UniProtKB Zinc finger 389 419 . . . Note=CCHC NOA-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01142 Q9Y6K9 UniProtKB Region 1 197 . . . Note=Required for interaction with and ubiquitination by MARCHF2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32935379;Dbxref=PMID:32935379 Q9Y6K9 UniProtKB Region 44 111 . . . Note=Interaction with CHUK/IKBKB Q9Y6K9 UniProtKB Region 150 257 . . . Note=Interaction with TANK Q9Y6K9 UniProtKB Region 242 350 . . . Note=Ubiquitin-binding (UBAN) Q9Y6K9 UniProtKB Region 246 365 . . . Note=Self-association Q9Y6K9 UniProtKB Region 251 419 . . . Note=Required for interaction with TNFAIP3 Q9Y6K9 UniProtKB Region 322 343 . . . Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y6K9 UniProtKB Region 358 395 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Y6K9 UniProtKB Region 382 419 . . . Note=Interaction with CYLD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12917691;Dbxref=PMID:12917691 Q9Y6K9 UniProtKB Coiled coil 49 356 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y6K9 UniProtKB Binding site 397 397 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01142 Q9Y6K9 UniProtKB Binding site 400 400 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01142 Q9Y6K9 UniProtKB Binding site 413 413 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01142 Q9Y6K9 UniProtKB Binding site 417 417 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01142 Q9Y6K9 UniProtKB Modified residue 31 31 . . . Note=Phosphoserine%3B by IKKB;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12657630;Dbxref=PMID:12657630 Q9Y6K9 UniProtKB Modified residue 43 43 . . . Note=Phosphoserine%3B by IKKB;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12657630;Dbxref=PMID:12657630 Q9Y6K9 UniProtKB Modified residue 68 68 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17977820;Dbxref=PMID:17977820 Q9Y6K9 UniProtKB Modified residue 85 85 . . . Note=Phosphoserine%3B by ATM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497931;Dbxref=PMID:16497931 Q9Y6K9 UniProtKB Modified residue 376 376 . . . Note=Phosphoserine%3B by IKKB;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12657630;Dbxref=PMID:12657630 Q9Y6K9 UniProtKB Modified residue 387 387 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:24012789,ECO:0007744|PubMed:24275569;Dbxref=PMID:24012789,PMID:24275569 Q9Y6K9 UniProtKB Disulfide bond 54 54 . . . Note=Interchain;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18164680;Dbxref=PMID:18164680 Q9Y6K9 UniProtKB Disulfide bond 347 347 . . . Note=Interchain;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18164680;Dbxref=PMID:18164680 Q9Y6K9 UniProtKB Cross-link 111 111 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21455181;Dbxref=PMID:21455181 Q9Y6K9 UniProtKB Cross-link 139 139 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21455181;Dbxref=PMID:21455181 Q9Y6K9 UniProtKB Cross-link 143 143 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21455181;Dbxref=PMID:21455181 Q9Y6K9 UniProtKB Cross-link 226 226 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21455181;Dbxref=PMID:21455181 Q9Y6K9 UniProtKB Cross-link 246 246 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21455181;Dbxref=PMID:21455181 Q9Y6K9 UniProtKB Cross-link 264 264 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21455181;Dbxref=PMID:21455181 Q9Y6K9 UniProtKB Cross-link 277 277 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14651848;Dbxref=PMID:14651848 Q9Y6K9 UniProtKB Cross-link 277 277 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14651848,ECO:0000269|PubMed:21455181;Dbxref=PMID:14651848,PMID:21455181 Q9Y6K9 UniProtKB Cross-link 283 283 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21455181;Dbxref=PMID:21455181 Q9Y6K9 UniProtKB Cross-link 285 285 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15620648,ECO:0000269|PubMed:17562858,ECO:0000269|PubMed:19136968,ECO:0000269|PubMed:21455181;Dbxref=PMID:15620648,PMID:17562858,PMID:19136968,PMID:21455181 Q9Y6K9 UniProtKB Cross-link 292 292 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21455181;Dbxref=PMID:21455181 Q9Y6K9 UniProtKB Cross-link 302 302 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21455181;Dbxref=PMID:21455181 Q9Y6K9 UniProtKB Cross-link 309 309 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14651848;Dbxref=PMID:14651848 Q9Y6K9 UniProtKB Cross-link 309 309 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14651848,ECO:0000269|PubMed:19136968,ECO:0000269|PubMed:20010814,ECO:0000269|PubMed:21455181;Dbxref=PMID:14651848,PMID:19136968,PMID:20010814,PMID:21455181 Q9Y6K9 UniProtKB Cross-link 321 321 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20010814;Dbxref=PMID:20010814 Q9Y6K9 UniProtKB Cross-link 325 325 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88522 Q9Y6K9 UniProtKB Cross-link 326 326 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin and interchain with MARCHF2);Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21455181,ECO:0000269|PubMed:32935379;Dbxref=PMID:21455181,PMID:32935379 Q9Y6K9 UniProtKB Cross-link 399 399 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14695475;Dbxref=PMID:14695475 Q9Y6K9 UniProtKB Alternative sequence 1 1 . . . ID=VSP_041000;Note=In isoform 2. M->MALVIQVGKLRPREVRTPQTINPSLFPSLPVKLSSIIEVPSGGERCCSRRTLVYKARAFWKGAPLPCWM;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.6 Q9Y6K9 UniProtKB Alternative sequence 174 224 . . . ID=VSP_041001;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q9Y6K9 UniProtKB Alternative sequence 257 304 . . . ID=VSP_041002;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q9Y6K9 UniProtKB Natural variant 57 57 . . . ID=VAR_026491;Note=In IP%3B shows the same luciferase activity as the control. E->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11590134,ECO:0000269|PubMed:15229184;Dbxref=dbSNP:rs148695964,PMID:11590134,PMID:15229184 Q9Y6K9 UniProtKB Natural variant 90 90 . . . ID=VAR_026492;Note=In IP%3B only 46.3%25 of the activation obtained with the wild-type protein. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15229184;Dbxref=PMID:15229184 Q9Y6K9 UniProtKB Natural variant 113 113 . . . ID=VAR_026493;Note=D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15229184;Dbxref=dbSNP:rs179363896,PMID:15229184 Q9Y6K9 UniProtKB Natural variant 123 123 . . . ID=VAR_026494;Note=In IP%3B shows the same luciferase activity as the control. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15229184;Dbxref=dbSNP:rs179363895,PMID:15229184 Q9Y6K9 UniProtKB Natural variant 153 153 . . . ID=VAR_026495;Note=In EDAID1. L->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12045264,ECO:0000269|PubMed:15100680;Dbxref=dbSNP:rs137853328,PMID:12045264,PMID:15100680 Q9Y6K9 UniProtKB Natural variant 170 170 . . . ID=VAR_072603;Note=In IP. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24339369;Dbxref=PMID:24339369 Q9Y6K9 UniProtKB Natural variant 173 173 . . . ID=VAR_031958;Note=In IMD33. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16950813;Dbxref=dbSNP:rs179363866,PMID:16950813 Q9Y6K9 UniProtKB Natural variant 173 173 . . . ID=VAR_072604;Note=In IP. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24339369;Dbxref=dbSNP:rs1057520292,PMID:24339369 Q9Y6K9 UniProtKB Natural variant 175 175 . . . ID=VAR_011320;Note=In EDAID1. R->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11242109;Dbxref=dbSNP:rs179363868,PMID:11242109 Q9Y6K9 UniProtKB Natural variant 183 183 . . . ID=VAR_072605;Note=In IP. Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20434027;Dbxref=dbSNP:rs1198984417,PMID:20434027 Q9Y6K9 UniProtKB Natural variant 227 227 . . . ID=VAR_011321;Note=In EDAID1. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11242109;Dbxref=dbSNP:rs179363869,PMID:11242109 Q9Y6K9 UniProtKB Natural variant 288 288 . . . ID=VAR_011322;Note=In EDAID1. A->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11242109;Dbxref=dbSNP:rs137853330,PMID:11242109 Q9Y6K9 UniProtKB Natural variant 311 311 . . . ID=VAR_011323;Note=In EDAID1%3B abolishes binding to polyubiquitin ('K63'-linked and linear) and greatly impairs tandem ubiquitin binding. D->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11242109,ECO:0000269|PubMed:16547522,ECO:0000269|PubMed:19185524,ECO:0000269|PubMed:21606507;Dbxref=dbSNP:rs179363867,PMID:11242109,PMID:16547522,PMID:19185524,PMID:21606507 Q9Y6K9 UniProtKB Natural variant 314 314 . . . ID=VAR_072606;Note=In IP. A->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24339369;Dbxref=PMID:24339369 Q9Y6K9 UniProtKB Natural variant 315 315 . . . ID=VAR_031959;Note=In IMD33%3B greatly impairs tandem ubiquitin binding. Impairs oligomerization%2C impairs binding of 'Lys-63'-linked ubiuitin and linear tetra-ubiquitin%2C impairs TNF-induced NF-kappa-B activation. E->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16818673,ECO:0000269|PubMed:19185524,ECO:0000269|PubMed:19854204;Dbxref=dbSNP:rs137853331,PMID:16818673,PMID:19185524,PMID:19854204 Q9Y6K9 UniProtKB Natural variant 319 319 . . . ID=VAR_031960;Note=In IMD33%3B impairs tandem ubiquitin binding. R->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16818673,ECO:0000269|PubMed:19185524;Dbxref=dbSNP:rs137853332,PMID:16818673,PMID:19185524 Q9Y6K9 UniProtKB Natural variant 322 322 . . . ID=VAR_072607;Note=In IP. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24339369;Dbxref=PMID:24339369 Q9Y6K9 UniProtKB Natural variant 323 323 . . . ID=VAR_042666;Note=In IP%3B diminishes interaction with TRAF6 and polyubiquitination%2C greatly impairs tandem ubiquitin binding. Impairs oligomerization%2C greatly impairs binding of 'Lys-63'-linked ubiuitin and linear tetra-ubiquitin%2C impairs TNF-induced NF-kappa-B activation. A->P;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17728323,ECO:0000269|PubMed:19185524,ECO:0000269|PubMed:19854204;Dbxref=dbSNP:rs179363865,PMID:17728323,PMID:19185524,PMID:19854204 Q9Y6K9 UniProtKB Natural variant 406 406 . . . ID=VAR_011324;Note=In EDAID1. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11224521;Dbxref=dbSNP:rs137853327,PMID:11224521 Q9Y6K9 UniProtKB Natural variant 407 407 . . . ID=VAR_009182;Note=In IP%3B impairs binding to ubiquitin. M->V;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10839543,ECO:0000269|PubMed:11590134,ECO:0000269|PubMed:19033441;Dbxref=dbSNP:rs137853322,PMID:10839543,PMID:11590134,PMID:19033441 Q9Y6K9 UniProtKB Natural variant 413 413 . . . ID=VAR_072608;Note=In IP. H->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24339369;Dbxref=PMID:24339369 Q9Y6K9 UniProtKB Natural variant 417 417 . . . ID=VAR_011325;Note=In EDAID1. C->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11047757,ECO:0000269|PubMed:11242109;Dbxref=dbSNP:rs137853326,PMID:11047757,PMID:11242109 Q9Y6K9 UniProtKB Natural variant 417 417 . . . ID=VAR_011326;Note=In EDAID1%3B loss of sumoylation. C->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11047757,ECO:0000269|PubMed:11224521,ECO:0000269|PubMed:11242109,ECO:0000269|PubMed:12045264,ECO:0000269|PubMed:14651848,ECO:0000269|PubMed:15100680;Dbxref=dbSNP:rs137853325,PMID:11047757,PMID:11224521,PMID:11242109,PMID:12045264,PMID:14651848,PMID:15100680 Q9Y6K9 UniProtKB Natural variant 417 417 . . . ID=VAR_026496;Note=In IMD33. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15100680;Dbxref=dbSNP:rs137853326,PMID:15100680 Q9Y6K9 UniProtKB Mutagenesis 68 68 . . . Note=Increases formation of homodimers. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17977820;Dbxref=PMID:17977820 Q9Y6K9 UniProtKB Mutagenesis 68 68 . . . Note=Abolishes interaction with IKBKB%3B abolishes TNF-alpha induced NF-kappa-B activity. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17977820;Dbxref=PMID:17977820 Q9Y6K9 UniProtKB Mutagenesis 85 85 . . . Note=Decreases ubiquitination and abolishes nuclear export. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16497931;Dbxref=PMID:16497931 Q9Y6K9 UniProtKB Mutagenesis 115 115 . . . Note=No change in the ubiquitination level%3B when associated with R-399. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15620648;Dbxref=PMID:15620648 Q9Y6K9 UniProtKB Mutagenesis 224 224 . . . Note=No change in the ubiquitination level%3B when associated with R-399. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15620648;Dbxref=PMID:15620648 Q9Y6K9 UniProtKB Mutagenesis 277 277 . . . Note=Partial abolition of sumoylation. Abolishes sumoylation and IKK activation%3B when associated with A-309. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14651848;Dbxref=PMID:14651848 Q9Y6K9 UniProtKB Mutagenesis 285 285 . . . Note=Decreased ability to activate NF-kappa-B. Important decrease in the ubiquitination level%3B when associated with R-399. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15620648,ECO:0000269|PubMed:17562858;Dbxref=PMID:15620648,PMID:17562858 Q9Y6K9 UniProtKB Mutagenesis 296 296 . . . Note=No effet on oligomerization%2Cimpairs binding of 'Lys-63'-linked ubiuitin and linear tetra-ubiquitin%2C impairs TNF-induced NF-kappa-B activation. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19854204;Dbxref=PMID:19854204 Q9Y6K9 UniProtKB Mutagenesis 300 300 . . . Note=Greatly impairs tandem ubiquitin binding. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19185524;Dbxref=PMID:19185524 Q9Y6K9 UniProtKB Mutagenesis 301 301 . . . Note=Impairs tandem ubiquitin binding. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19185524;Dbxref=PMID:19185524 Q9Y6K9 UniProtKB Mutagenesis 302 302 . . . Note=No effect on MARCH2F-mediated K48-linked ubiquitination. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32935379;Dbxref=PMID:32935379 Q9Y6K9 UniProtKB Mutagenesis 304 304 . . . Note=Complete loss of cleavage by HAV protease 3c. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24920812;Dbxref=PMID:24920812 Q9Y6K9 UniProtKB Mutagenesis 304 304 . . . Note=Impairs tandem ubiquitin binding. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19185524;Dbxref=PMID:19185524 Q9Y6K9 UniProtKB Mutagenesis 307 307 . . . Note=Greatly impairs tandem ubiquitin binding. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19185524;Dbxref=PMID:19185524 Q9Y6K9 UniProtKB Mutagenesis 308 308 . . . Note=Greatly impairs tandem ubiquitin binding. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19185524;Dbxref=PMID:19185524 Q9Y6K9 UniProtKB Mutagenesis 309 309 . . . Note=Partial abolition of sumoylation. Abolishes sumoylation and IKK activation%3B when associated with A-277. No effect on MARCH2F-mediated K48-linked ubiquitination. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14651848,ECO:0000269|PubMed:32935379;Dbxref=PMID:14651848,PMID:32935379 Q9Y6K9 UniProtKB Mutagenesis 312 312 . . . Note=Greatly impairs tandem ubiquitin binding%2Cimpairs oligomerization%2C impairs TNF-induced NF-kappa-B activation. F->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19185524,ECO:0000269|PubMed:19854204;Dbxref=PMID:19185524,PMID:19854204 Q9Y6K9 UniProtKB Mutagenesis 312 312 . . . Note=MNo effet on oligomerization%2C preferentially binds tri-ubiquitin chains ('Lys-48' or 'Lys-63'-linked). F->W;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19185524,ECO:0000269|PubMed:19854204;Dbxref=PMID:19185524,PMID:19854204 Q9Y6K9 UniProtKB Mutagenesis 312 312 . . . Note=Impairs tandem ubiquitin binding. F->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19185524,ECO:0000269|PubMed:19854204;Dbxref=PMID:19185524,PMID:19854204 Q9Y6K9 UniProtKB Mutagenesis 313 313 . . . Note=Impairs tandem ubiquitin binding. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19185524;Dbxref=PMID:19185524 Q9Y6K9 UniProtKB Mutagenesis 315 315 . . . Note=Greatly impairs tandem ubiquitin binding. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19854204;Dbxref=PMID:19854204 Q9Y6K9 UniProtKB Mutagenesis 317 317 . . . Note=Greatly impairs tandem ubiquitin binding. Q->A%2CW;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19185524;Dbxref=PMID:19185524 Q9Y6K9 UniProtKB Mutagenesis 321 321 . . . Note=No effect on MARCH2F-mediated K48-linked ubiquitination. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32935379;Dbxref=PMID:32935379 Q9Y6K9 UniProtKB Mutagenesis 323 323 . . . Note=Greatly impairs tandem ubiquitin binding. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19854204;Dbxref=PMID:19854204 Q9Y6K9 UniProtKB Mutagenesis 325 325 . . . Note=No effect on MARCH2F-mediated K48-linked ubiquitination. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32935379;Dbxref=PMID:32935379 Q9Y6K9 UniProtKB Mutagenesis 326 326 . . . Note=Abolishes MARCH2F-mediated K48-linked ubiquitination and subsequent suppression of antiviral and antibacterial innate immune response. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32935379;Dbxref=PMID:32935379 Q9Y6K9 UniProtKB Mutagenesis 329 329 . . . Note=Impairs oligomerization%2C impairs binding of 'Lys-63'-linked ubiuitin%2C impairs TNF-induced NF-kappa-B activation%3B when associated with A-336. L->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16547522,ECO:0000269|PubMed:19854204;Dbxref=PMID:16547522,PMID:19854204 Q9Y6K9 UniProtKB Mutagenesis 329 329 . . . Note=Abolished ubiquitin-binding. L->P;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16547522,ECO:0000269|PubMed:18287044,ECO:0000269|PubMed:19854204;Dbxref=PMID:16547522,PMID:18287044,PMID:19854204 Q9Y6K9 UniProtKB Mutagenesis 336 336 . . . Note=Impairs oligomerization%2C impairs binding of 'Lys-63'-linked ubiuitin%2C impairs TNF-induced NF-kappa-B activation%3B when associated with A-329. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19854204;Dbxref=PMID:19854204 Q9Y6K9 UniProtKB Mutagenesis 342 342 . . . Note=No effect on MARCH2F-mediated K48-linked ubiquitination. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32935379;Dbxref=PMID:32935379 Q9Y6K9 UniProtKB Mutagenesis 344 344 . . . Note=No effect on MARCH2F-mediated K48-linked ubiquitination. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32935379;Dbxref=PMID:32935379 Q9Y6K9 UniProtKB Mutagenesis 358 358 . . . Note=No effect on MARCH2F-mediated K48-linked ubiquitination. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32935379;Dbxref=PMID:32935379 Q9Y6K9 UniProtKB Mutagenesis 399 399 . . . Note=Abolishes BCL10-mediated but not RIPK2-mediated ubiquitination. Important decrease in the ubiquitination level%3B when associated with R-285. No change in the ubiquitination level%3B when associated with R-115 or R-224. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14695475,ECO:0000269|PubMed:15620648;Dbxref=PMID:14695475,PMID:15620648 Q9Y6K9 UniProtKB Mutagenesis 414 414 . . . Note=Abolishes binding to polyubiquitin. V->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19033441;Dbxref=PMID:19033441 Q9Y6K9 UniProtKB Mutagenesis 415 415 . . . Note=Impairs binding to polyubiquitin. M->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19033441;Dbxref=PMID:19033441 Q9Y6K9 UniProtKB Sequence conflict 341 341 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Y6K9 UniProtKB Sequence conflict 387 387 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Y6K9 UniProtKB Helix 38 129 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6MI3 Q9Y6K9 UniProtKB Turn 194 196 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3CL3 Q9Y6K9 UniProtKB Helix 197 249 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3CL3 Q9Y6K9 UniProtKB Helix 260 268 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4BWN Q9Y6K9 UniProtKB Helix 271 295 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4BWN Q9Y6K9 UniProtKB Helix 297 341 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4BWN Q9Y6K9 UniProtKB Beta strand 394 396 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2JVY Q9Y6K9 UniProtKB Turn 398 400 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5AAY Q9Y6K9 UniProtKB Beta strand 403 406 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2JVX Q9Y6K9 UniProtKB Helix 407 416 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2JVX