##gff-version 3
Q9GZM8	UniProtKB	Chain	1	345	.	.	.	ID=PRO_0000240210;Note=Nuclear distribution protein nudE-like 1	
Q9GZM8	UniProtKB	Region	56	166	.	.	.	Note=Self-association;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9GZM8	UniProtKB	Region	64	189	.	.	.	Note=Interaction with KATNB1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9GZM8	UniProtKB	Region	114	133	.	.	.	Note=Required for interaction with PAFAH1B1	
Q9GZM8	UniProtKB	Region	175	345	.	.	.	Note=Interaction with CENPF;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17600710;Dbxref=PMID:17600710	
Q9GZM8	UniProtKB	Region	189	256	.	.	.	Note=Interaction with YWHAE;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9GZM8	UniProtKB	Region	191	345	.	.	.	Note=Interaction with NEFL;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9GZM8	UniProtKB	Region	195	256	.	.	.	Note=Interaction with KATNA1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9GZM8	UniProtKB	Region	241	280	.	.	.	Note=Interaction with DISC1	
Q9GZM8	UniProtKB	Region	256	291	.	.	.	Note=Required for localization to the centrosome and interaction with dynein%2C dynactin%2C tubulin gamma%2C PCM1 and PCNT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16291865;Dbxref=PMID:16291865	
Q9GZM8	UniProtKB	Region	315	345	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9GZM8	UniProtKB	Coiled coil	28	190	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9GZM8	UniProtKB	Modified residue	215	215	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:20068231,PMID:23186163	
Q9GZM8	UniProtKB	Modified residue	219	219	.	.	.	Note=Phosphothreonine%3B by CDK1 and MAPK1;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231;Dbxref=PMID:18669648,PMID:20068231	
Q9GZM8	UniProtKB	Modified residue	231	231	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q9GZM8	UniProtKB	Modified residue	242	242	.	.	.	Note=Phosphoserine%3B by CDK1;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:20068231;Dbxref=PMID:20068231	
Q9GZM8	UniProtKB	Modified residue	245	245	.	.	.	Note=Phosphothreonine%3B by CDK1 and MAPK1;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231;Dbxref=PMID:18669648,PMID:20068231	
Q9GZM8	UniProtKB	Modified residue	344	344	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q78PB6	
Q9GZM8	UniProtKB	Lipidation	273	273	.	.	.	Note=S-palmitoyl cysteine%3B by ZDHHC2%2C ZDHHC3 and ZDHHC7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19927128;Dbxref=PMID:19927128	
Q9GZM8	UniProtKB	Alternative sequence	316	345	.	.	.	ID=VSP_019310;Note=In isoform 2. AVNGFDPAPPPPGLGSSRPSSAPGMLPLSV->SSSSCAIRASRRRFSSSSADLAGRGGGDGSIPAQHSTGASGKAPPPTLLLET;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:17974005;Dbxref=PMID:17974005	
Q9GZM8	UniProtKB	Alternative sequence	316	345	.	.	.	ID=VSP_047509;Note=In isoform 3. AVNGFDPAPPPPGLGSSRPSSAPGMLPLSV->QEKVIFPTLFMGQ;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
Q9GZM8	UniProtKB	Mutagenesis	198	198	.	.	.	Note=Abrogates mitotic phosphorylation%3B when associated with V-219%3B A-231%3B A-242 and V-245. Abrogates phosphorylation by CDK5%3B when associated with A-219 and A-231. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11163260,ECO:0000269|PubMed:12556484;Dbxref=PMID:11163260,PMID:12556484	
Q9GZM8	UniProtKB	Mutagenesis	198	198	.	.	.	Note=Enhances interaction with PAFAH1B1 and impairs centrosomal localization%3B when associated with E-219%3B E-231%3B E-242 and E-245. S->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11163260,ECO:0000269|PubMed:12556484;Dbxref=PMID:11163260,PMID:12556484	
Q9GZM8	UniProtKB	Mutagenesis	219	219	.	.	.	Note=Abrogates phosphorylation by CDK5%3B when associated with A-198 and A-231. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11163260,ECO:0000269|PubMed:12556484;Dbxref=PMID:11163260,PMID:12556484	
Q9GZM8	UniProtKB	Mutagenesis	219	219	.	.	.	Note=Enhances interaction with PAFAH1B1 and impairs centrosomal localization%3B when associated with E-198%3B E-231%3B E-242 and E-245. T->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11163260,ECO:0000269|PubMed:12556484;Dbxref=PMID:11163260,PMID:12556484	
Q9GZM8	UniProtKB	Mutagenesis	219	219	.	.	.	Note=Abrogates mitotic phosphorylation%3B when associated with A-198%3B A-231%3B A-242 and V-245. T->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11163260,ECO:0000269|PubMed:12556484;Dbxref=PMID:11163260,PMID:12556484	
Q9GZM8	UniProtKB	Mutagenesis	231	231	.	.	.	Note=Abrogates mitotic phosphorylation%3B when associated with A-198%3B V-219%3B A-242 and V-245. Abrogates phosphorylation by CDK5%3B when associated with A-198 and A-219. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11163260,ECO:0000269|PubMed:12556484;Dbxref=PMID:11163260,PMID:12556484	
Q9GZM8	UniProtKB	Mutagenesis	231	231	.	.	.	Note=Enhances interaction with PAFAH1B1 and impairs centrosomal localization%3B when associated with E-198%3B E-219%3B E-242 and E-245. S->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11163260,ECO:0000269|PubMed:12556484;Dbxref=PMID:11163260,PMID:12556484	
Q9GZM8	UniProtKB	Mutagenesis	242	242	.	.	.	Note=Abrogates mitotic phosphorylation%3B when associated with A-198%3B V-219%3B A-231 and V-245. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12556484;Dbxref=PMID:12556484	
Q9GZM8	UniProtKB	Mutagenesis	242	242	.	.	.	Note=Enhances interaction with PAFAH1B1 and impairs centrosomal localization%3B when associated with E-198%3B E-219%3B E-231 and E-245. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12556484;Dbxref=PMID:12556484	
Q9GZM8	UniProtKB	Mutagenesis	245	245	.	.	.	Note=Enhances interaction with PAFAH1B1 and impairs centrosomal localization%3B when associated with E-198%3B E-219%3B E-231 and E-242. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12556484;Dbxref=PMID:12556484	
Q9GZM8	UniProtKB	Mutagenesis	245	245	.	.	.	Note=Abrogates mitotic phosphorylation%3B when associated with A-198%3B V-219%3B A-231 and A-242. T->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12556484;Dbxref=PMID:12556484	
Q9GZM8	UniProtKB	Mutagenesis	266	266	.	.	.	Note=Abolishes interaction with DISC1%3B when associated with A-267. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17035248;Dbxref=PMID:17035248	
Q9GZM8	UniProtKB	Mutagenesis	267	267	.	.	.	Note=Abolishes interaction with DISC1%3B when associated with A-266. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17035248;Dbxref=PMID:17035248	
Q9GZM8	UniProtKB	Mutagenesis	273	273	.	.	.	Note=Abolishes oligopeptidase activity. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15728732;Dbxref=PMID:15728732	
Q9GZM8	UniProtKB	Sequence conflict	322	322	.	.	.	Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9GZM8	UniProtKB	Helix	59	165	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2V66