##gff-version 3
P05221	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17510054;Dbxref=PMID:17510054	
P05221	UniProtKB	Chain	2	200	.	.	.	ID=PRO_0000219486;Note=Nucleoplasmin	
P05221	UniProtKB	Region	35	39	.	.	.	Note=Acidic tract A1;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:11684019;Dbxref=PMID:11684019	
P05221	UniProtKB	Region	123	200	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P05221	UniProtKB	Region	128	148	.	.	.	Note=Acidic tract A2;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:11684019;Dbxref=PMID:11684019	
P05221	UniProtKB	Region	174	176	.	.	.	Note=Acidic tract A3;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:11684019;Dbxref=PMID:11684019	
P05221	UniProtKB	Motif	155	170	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10745017;Dbxref=PMID:10745017	
P05221	UniProtKB	Compositional bias	124	147	.	.	.	Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P05221	UniProtKB	Compositional bias	165	188	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P05221	UniProtKB	Site	58	58	.	.	.	Note=Interaction between pentamers;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11684019;Dbxref=PMID:11684019	
P05221	UniProtKB	Site	82	82	.	.	.	Note=Interaction between pentamers;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11684019;Dbxref=PMID:11684019	
P05221	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17510054;Dbxref=PMID:17510054	
P05221	UniProtKB	Modified residue	3	3	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17510054;Dbxref=PMID:17510054	
P05221	UniProtKB	Modified residue	4	4	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17510054;Dbxref=PMID:17510054	
P05221	UniProtKB	Modified residue	6	6	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17510054;Dbxref=PMID:17510054	
P05221	UniProtKB	Modified residue	8	8	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17510054;Dbxref=PMID:17510054	
P05221	UniProtKB	Modified residue	149	149	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17510054;Dbxref=PMID:17510054	
P05221	UniProtKB	Modified residue	177	177	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17510054;Dbxref=PMID:17510054	
P05221	UniProtKB	Modified residue	178	178	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17510054;Dbxref=PMID:17510054	
P05221	UniProtKB	Modified residue	182	182	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17510054;Dbxref=PMID:17510054	
P05221	UniProtKB	Modified residue	192	192	.	.	.	Note=Omega-N-methylarginine%3B by PRMT5%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22009756;Dbxref=PMID:22009756	
P05221	UniProtKB	Modified residue	192	192	.	.	.	Note=Symmetric dimethylarginine%3B by PRMT5%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22009756;Dbxref=PMID:22009756	
P05221	UniProtKB	Mutagenesis	192	192	.	.	.	Note=Abolishes arginine methylation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22009756;Dbxref=PMID:22009756	
P05221	UniProtKB	Mutagenesis	194	194	.	.	.	Note=Reduces arginine methylation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22009756;Dbxref=PMID:22009756	
P05221	UniProtKB	Sequence conflict	11	11	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P05221	UniProtKB	Sequence conflict	27	27	.	.	.	Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P05221	UniProtKB	Sequence conflict	31	31	.	.	.	Note=E->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P05221	UniProtKB	Sequence conflict	34	34	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P05221	UniProtKB	Sequence conflict	61	61	.	.	.	Note=N->H;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P05221	UniProtKB	Sequence conflict	72	72	.	.	.	Note=A->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P05221	UniProtKB	Sequence conflict	75	75	.	.	.	Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P05221	UniProtKB	Sequence conflict	80	80	.	.	.	Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P05221	UniProtKB	Sequence conflict	111	111	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P05221	UniProtKB	Sequence conflict	134	137	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P05221	UniProtKB	Sequence conflict	147	147	.	.	.	Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P05221	UniProtKB	Beta strand	18	23	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1K5J	
P05221	UniProtKB	Beta strand	29	32	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1K5J	
P05221	UniProtKB	Beta strand	44	52	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1K5J	
P05221	UniProtKB	Beta strand	61	67	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1K5J	
P05221	UniProtKB	Beta strand	74	82	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1K5J	
P05221	UniProtKB	Turn	83	85	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1K5J	
P05221	UniProtKB	Beta strand	88	90	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1K5J	
P05221	UniProtKB	Beta strand	100	106	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1K5J	
P05221	UniProtKB	Beta strand	111	118	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1K5J