##gff-version 3
Q587J8	UniProtKB	Chain	1	217	.	.	.	ID=PRO_0000311967;Note=KH domain-containing protein 3	
Q587J8	UniProtKB	Domain	40	103	.	.	.	Note=KH%3B atypical	
Q587J8	UniProtKB	Region	1	40	.	.	.	Note=Involved in RNA binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9CWU5	
Q587J8	UniProtKB	Region	129	217	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q587J8	UniProtKB	Compositional bias	129	143	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q587J8	UniProtKB	Compositional bias	160	199	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q587J8	UniProtKB	Compositional bias	202	217	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q587J8	UniProtKB	Modified residue	145	145	.	.	.	Note=Phosphothreonine%3B by ATM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31609975;Dbxref=PMID:31609975	
Q587J8	UniProtKB	Modified residue	156	156	.	.	.	Note=Phosphothreonine%3B by ATM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31609975;Dbxref=PMID:31609975	
Q587J8	UniProtKB	Modified residue	182	182	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9CWU5	
Q587J8	UniProtKB	Natural variant	5	5	.	.	.	ID=VAR_085059;Note=In HYDM2%3B uncertain significance. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23963444;Dbxref=dbSNP:rs144291287,PMID:23963444	
Q587J8	UniProtKB	Natural variant	97	97	.	.	.	ID=VAR_054052;Note=In HYDM2%3B uncertain significance. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23963444;Dbxref=dbSNP:rs564533,PMID:23963444	
Q587J8	UniProtKB	Natural variant	201	201	.	.	.	ID=VAR_054053;Note=In HYDM2%3B uncertain significance. A->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23963444;Dbxref=dbSNP:rs561930,PMID:23963444	
Q587J8	UniProtKB	Mutagenesis	145	145	.	.	.	Note=Decreases recruitment of RAD51 to DNA double-strand breaks%2C PARP1 activity and ATM-CHK2 signaling resulting in a decrease in DNA double-strand break repair. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31609975;Dbxref=PMID:31609975	
Q587J8	UniProtKB	Mutagenesis	150	172	.	.	.	Note=Abolishes DNA double-strand break repair. Reduces the localization of the homologous recombination DNA repair pathway protein RAD51 to sites of DNA double-strand breaks. May exhibit a dominant negative effect on PARP1 activation%2C homologous recombination repair and ATM-CHK2 signaling. No effect on restart of stalled replication forks%2C nascent DNA stability%2C localization to DNA double-strand break repair sites or interaction with PARP1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31609975;Dbxref=PMID:31609975	
Q587J8	UniProtKB	Mutagenesis	150	159	.	.	.	Note=Abolishes DNA double-strand break repair. Reduces the localization of the homologous recombination DNA repair pathway protein RAD51 to sites of DNA double-strand breaks. May exhibit a dominant negative effect on PARP1 activation%2C homologous recombination repair and ATM-CHK2 signaling. No effect on restart of stalled replication forks%2C nascent DNA stability%2C localization to DNA double-strand break repair sites or interaction with PARP1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31609975;Dbxref=PMID:31609975	
Q587J8	UniProtKB	Mutagenesis	156	156	.	.	.	Note=Decreases recruitment of RAD51 to DNA double-strand breaks%2C PARP1 activity and ATM-CHK2 signaling resulting in a decrease in DNA double-strand break repair. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31609975;Dbxref=PMID:31609975	
Q587J8	UniProtKB	Mutagenesis	156	156	.	.	.	Note=No effect on recruitment of RAD51 to DNA double-strand breaks%2C PARP1 activity%2C ATM-CHK2 signaling or DNA double-strand break repair. T->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31609975;Dbxref=PMID:31609975