##gff-version 3
Q8WVY7	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:22223895;Dbxref=PMID:19413330,PMID:22223895	
Q8WVY7	UniProtKB	Chain	2	318	.	.	.	ID=PRO_0000242640;Note=Ubiquitin-like domain-containing CTD phosphatase 1	
Q8WVY7	UniProtKB	Domain	3	81	.	.	.	Note=Ubiquitin-like;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00214	
Q8WVY7	UniProtKB	Domain	133	294	.	.	.	Note=FCP1 homology;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00336	
Q8WVY7	UniProtKB	Binding site	143	143	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9XZ16	
Q8WVY7	UniProtKB	Binding site	145	145	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9XZ16	
Q8WVY7	UniProtKB	Binding site	253	253	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9XZ16	
Q8WVY7	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylalanine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:22223895;Dbxref=PMID:19413330,PMID:22223895	
Q8WVY7	UniProtKB	Modified residue	117	117	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861	
Q8WVY7	UniProtKB	Mutagenesis	10	10	.	.	.	Note=No effect on proteasome binding or nuclear localization. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21949367;Dbxref=PMID:21949367	
Q8WVY7	UniProtKB	Mutagenesis	44	44	.	.	.	Note=Aberrant diffuse pan-cellular localization and loss of binding to PSMD2. K->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21949367,ECO:0000269|PubMed:28539385;Dbxref=PMID:21949367,PMID:28539385	
Q8WVY7	UniProtKB	Mutagenesis	46	46	.	.	.	Note=No effect on proteasome binding or nuclear localization. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21949367;Dbxref=PMID:21949367	
Q8WVY7	UniProtKB	Mutagenesis	49	49	.	.	.	Note=Loss of binding to PSMD2 and PSMC2%2C and loss of inhibitory effect on proteasome activity%3B when associated with E-51. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28539385;Dbxref=PMID:28539385	
Q8WVY7	UniProtKB	Mutagenesis	51	51	.	.	.	Note=Loss of binding to PSMD2 and PSMC2%2C and loss of inhibitory effect on proteasome activity%3B when associated with E-49. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28539385;Dbxref=PMID:28539385	
Q8WVY7	UniProtKB	Mutagenesis	143	143	.	.	.	Note=Loss of catalytic activity. No effect on interaction with 19S regulatory particle but loss of catalytic activity%3B when associated with A-145. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21949367,ECO:0000269|PubMed:28539385;Dbxref=PMID:21949367,PMID:28539385	
Q8WVY7	UniProtKB	Mutagenesis	145	145	.	.	.	Note=No effect on interaction with 19S regulatory particle but loss of catalytic activity%3B when associated with A-143. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28539385;Dbxref=PMID:28539385	
Q8WVY7	UniProtKB	Sequence conflict	83	83	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q8WVY7	UniProtKB	Beta strand	5	9	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KX3	
Q8WVY7	UniProtKB	Beta strand	12	16	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KX3	
Q8WVY7	UniProtKB	Turn	21	23	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2LGD	
Q8WVY7	UniProtKB	Helix	25	35	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KX3	
Q8WVY7	UniProtKB	Turn	39	41	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KX3	
Q8WVY7	UniProtKB	Beta strand	46	49	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KX3	
Q8WVY7	UniProtKB	Beta strand	57	59	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M17	
Q8WVY7	UniProtKB	Helix	61	64	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KX3	
Q8WVY7	UniProtKB	Helix	68	70	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KX3	
Q8WVY7	UniProtKB	Beta strand	71	76	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M17