##gff-version 3
Q60867	UniProtKB	Chain	1	357	.	.	.	ID=PRO_0000127383;Note=Neurogenic differentiation factor 1	
Q60867	UniProtKB	Domain	101	153	.	.	.	Note=BHLH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00981	
Q60867	UniProtKB	Region	1	94	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q60867	UniProtKB	Motif	87	93	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q60867	UniProtKB	Compositional bias	27	53	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q60867	UniProtKB	Compositional bias	54	76	.	.	.	Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q60867	UniProtKB	Modified residue	162	162	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12810726;Dbxref=PMID:12810726	
Q60867	UniProtKB	Modified residue	259	259	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12810726,ECO:0000269|PubMed:15797719;Dbxref=PMID:12810726,PMID:15797719	
Q60867	UniProtKB	Modified residue	266	266	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12810726,ECO:0000269|PubMed:15797719;Dbxref=PMID:12810726,PMID:15797719	
Q60867	UniProtKB	Modified residue	274	274	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12810726,ECO:0000269|PubMed:15797719;Dbxref=PMID:12810726,PMID:15797719	
Q60867	UniProtKB	Modified residue	336	336	.	.	.	Note=Phosphoserine%3B by CaMK2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q64289	
Q60867	UniProtKB	Mutagenesis	162	162	.	.	.	Note=Reduces weakly phosphorylation. Reduces strongly phosphorylation%3B when associated with A-259 and A-266. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12810726;Dbxref=PMID:12810726	
Q60867	UniProtKB	Mutagenesis	259	259	.	.	.	Note=Reduces weakly phosphorylation. Reduces strongly phosphorylation%3B when associated with A-162 and A-266. Reduces transactivation on the insulin promoter in glucose-stimulated insulinoma cells%3B when associated with A-266 and A-274. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12810726,ECO:0000269|PubMed:15797719;Dbxref=PMID:12810726,PMID:15797719	
Q60867	UniProtKB	Mutagenesis	266	266	.	.	.	Note=Reduces weakly phosphorylation. Reduces strongly phosphorylation%3B when associated with A-162 and A-259. Reduces transactivation on the insulin promoter in glucose-stimulated insulinoma cells%3B when associated with A-259 and A-274. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12810726,ECO:0000269|PubMed:15797719;Dbxref=PMID:12810726,PMID:15797719	
Q60867	UniProtKB	Mutagenesis	274	274	.	.	.	Note=Strongly reduces phosphorylation. Reduces transactivation on the insulin promoter in glucose-stimulated insulinoma cells%3B when associated with A-259 and A-266. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12810726,ECO:0000269|PubMed:15797719;Dbxref=PMID:12810726,PMID:15797719	
Q60867	UniProtKB	Mutagenesis	279	279	.	.	.	Note=Promotes the formation of differentiated late retinal amacrine cells. I->V	
Q60867	UniProtKB	Helix	102	126	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QL2	
Q60867	UniProtKB	Beta strand	128	130	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QL2	
Q60867	UniProtKB	Beta strand	133	135	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QL2	
Q60867	UniProtKB	Helix	139	156	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QL2