##gff-version 3
O14777	UniProtKB	Chain	1	642	.	.	.	ID=PRO_0000249550;Note=Kinetochore protein NDC80 homolog	
O14777	UniProtKB	Region	1	445	.	.	.	Note=Interaction with the N-terminus of CDCA1	
O14777	UniProtKB	Region	1	250	.	.	.	Note=Nuclear localization	
O14777	UniProtKB	Region	1	74	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O14777	UniProtKB	Region	128	251	.	.	.	Note=Interaction with RB1	
O14777	UniProtKB	Region	251	618	.	.	.	Note=Interaction with NEK2 and ZWINT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16732327;Dbxref=PMID:16732327	
O14777	UniProtKB	Region	251	431	.	.	.	Note=Interaction with SMC1A	
O14777	UniProtKB	Region	361	547	.	.	.	Note=Interaction with PSMC2 and SMC1A	
O14777	UniProtKB	Region	446	642	.	.	.	Note=Interaction with the C-terminus of CDCA1 and the SPBC24-SPBC25 subcomplex	
O14777	UniProtKB	Coiled coil	261	403	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
O14777	UniProtKB	Coiled coil	458	642	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
O14777	UniProtKB	Compositional bias	1	51	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O14777	UniProtKB	Modified residue	44	44	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
O14777	UniProtKB	Modified residue	53	53	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30409912;Dbxref=PMID:30409912	
O14777	UniProtKB	Modified residue	55	55	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30409912;Dbxref=PMID:30409912	
O14777	UniProtKB	Modified residue	59	59	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30409912;Dbxref=PMID:30409912	
O14777	UniProtKB	Modified residue	62	62	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30409912;Dbxref=PMID:30409912	
O14777	UniProtKB	Modified residue	69	69	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:20068231,PMID:23186163	
O14777	UniProtKB	Modified residue	165	165	.	.	.	Note=Phosphoserine%3B by NEK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12386167;Dbxref=PMID:12386167	
O14777	UniProtKB	Modified residue	242	242	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9D0F1	
O14777	UniProtKB	Modified residue	527	527	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30409912;Dbxref=PMID:30409912	
O14777	UniProtKB	Natural variant	66	66	.	.	.	ID=VAR_027436;Note=S->A;Dbxref=dbSNP:rs16943490	
O14777	UniProtKB	Natural variant	348	348	.	.	.	ID=VAR_027437;Note=E->D;Dbxref=dbSNP:rs12456560	
O14777	UniProtKB	Natural variant	605	605	.	.	.	ID=VAR_027438;Note=A->P;Dbxref=dbSNP:rs9051	
O14777	UniProtKB	Mutagenesis	53	53	.	.	.	Note=Mimics acetylation%2C leading to increased kinetochore-microtubule attachment%3B when associated with Q-59. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30409912;Dbxref=PMID:30409912	
O14777	UniProtKB	Mutagenesis	53	53	.	.	.	Note=Impaired acetylation%2C leading to reduced kinetochore-microtubule attachment%3B when associated with R-59. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30409912;Dbxref=PMID:30409912	
O14777	UniProtKB	Mutagenesis	59	59	.	.	.	Note=Mimics acetylation%2C leading to increased kinetochore-microtubule attachment%3B when associated with Q-53. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30409912;Dbxref=PMID:30409912	
O14777	UniProtKB	Mutagenesis	59	59	.	.	.	Note=Impaired acetylation%2C leading to reduced kinetochore-microtubule attachment%3B when associated with R-53. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30409912;Dbxref=PMID:30409912	
O14777	UniProtKB	Mutagenesis	234	234	.	.	.	Note=Abrogates binding to RB1. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10779342;Dbxref=PMID:10779342	
O14777	UniProtKB	Helix	89	105	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2IGP	
O14777	UniProtKB	Turn	114	117	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2IGP	
O14777	UniProtKB	Helix	122	133	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2IGP	
O14777	UniProtKB	Turn	134	136	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2IGP	
O14777	UniProtKB	Helix	147	157	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2IGP	
O14777	UniProtKB	Helix	166	170	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2IGP	
O14777	UniProtKB	Turn	171	173	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2IGP	
O14777	UniProtKB	Turn	175	177	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2IGP	
O14777	UniProtKB	Helix	178	194	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2IGP	
O14777	UniProtKB	Helix	222	238	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VE7	
O14777	UniProtKB	Helix	244	258	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VE7	
O14777	UniProtKB	Helix	264	286	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2VE7	
O14777	UniProtKB	Helix	371	421	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8G0P	
O14777	UniProtKB	Helix	451	453	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8G0P	
O14777	UniProtKB	Helix	454	509	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8G0P