##gff-version 3
Q63369	UniProtKB	Chain	1	973	.	.	.	ID=PRO_0000030314;Note=Nuclear factor NF-kappa-B p105 subunit	
Q63369	UniProtKB	Chain	1	483	.	.	.	ID=PRO_0000030315;Note=Nuclear factor NF-kappa-B p50 subunit;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19838	
Q63369	UniProtKB	Domain	38	245	.	.	.	Note=RHD;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00265	
Q63369	UniProtKB	Repeat	540	570	.	.	.	Note=ANK 1	
Q63369	UniProtKB	Repeat	579	608	.	.	.	Note=ANK 2	
Q63369	UniProtKB	Repeat	612	641	.	.	.	Note=ANK 3	
Q63369	UniProtKB	Repeat	648	677	.	.	.	Note=ANK 4	
Q63369	UniProtKB	Repeat	682	711	.	.	.	Note=ANK 5	
Q63369	UniProtKB	Repeat	716	745	.	.	.	Note=ANK 6	
Q63369	UniProtKB	Repeat	769	799	.	.	.	Note=ANK 7	
Q63369	UniProtKB	Domain	803	890	.	.	.	Note=Death	
Q63369	UniProtKB	Region	371	394	.	.	.	Note=GRR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19838	
Q63369	UniProtKB	Region	434	467	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q63369	UniProtKB	Region	435	973	.	.	.	Note=Interaction with CFLAR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19838	
Q63369	UniProtKB	Region	648	682	.	.	.	Note=Essential for interaction with HIF1AN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19838	
Q63369	UniProtKB	Motif	359	364	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q63369	UniProtKB	Compositional bias	438	459	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q63369	UniProtKB	Site	433	434	.	.	.	Note=Cleavage (when cotranslationally processed);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19838	
Q63369	UniProtKB	Modified residue	60	60	.	.	.	Note=S-nitrosocysteine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19838	
Q63369	UniProtKB	Modified residue	336	336	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q63369	UniProtKB	Modified residue	440	440	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19838	
Q63369	UniProtKB	Modified residue	449	449	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25799	
Q63369	UniProtKB	Modified residue	676	676	.	.	.	Note=(3S)-3-hydroxyasparagine%3B by HIF1AN;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19838	
Q63369	UniProtKB	Modified residue	757	757	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
Q63369	UniProtKB	Modified residue	898	898	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19838	
Q63369	UniProtKB	Modified residue	912	912	.	.	.	Note=Phosphoserine%3B by GSK3-beta%3B in vitro;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19838	
Q63369	UniProtKB	Modified residue	928	928	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19838	
Q63369	UniProtKB	Modified residue	932	932	.	.	.	Note=Phosphoserine%3B by IKKB;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19838	
Q63369	UniProtKB	Modified residue	937	937	.	.	.	Note=Phosphoserine%3B by IKKB;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19838	
Q63369	UniProtKB	Modified residue	942	942	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19838	
Q63369	UniProtKB	Modified residue	948	948	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P25799	
Q63369	UniProtKB	Lipidation	60	60	.	.	.	Note=S-(15-deoxy-Delta12%2C14-prostaglandin J2-9-yl)cysteine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19838	
Q63369	UniProtKB	Cross-link	324	324	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19838