##gff-version 3
Q95NE7	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16539	
Q95NE7	UniProtKB	Chain	2	360	.	.	.	ID=PRO_0000186293;Note=Mitogen-activated protein kinase 14	
Q95NE7	UniProtKB	Domain	24	308	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q95NE7	UniProtKB	Active site	150	150	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q95NE7	UniProtKB	Binding site	30	38	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q95NE7	UniProtKB	Binding site	53	53	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q95NE7	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16539	
Q95NE7	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16539	
Q95NE7	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16539	
Q95NE7	UniProtKB	Modified residue	53	53	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16539	
Q95NE7	UniProtKB	Modified residue	152	152	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16539	
Q95NE7	UniProtKB	Modified residue	180	180	.	.	.	Note=Phosphothreonine%3B by MAP2K3%2C MAP2K4%2C MAP2K6 and autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16539	
Q95NE7	UniProtKB	Modified residue	182	182	.	.	.	Note=Phosphotyrosine%3B by MAP2K3%2C MAP2K4%2C MAP2K6 and autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16539	
Q95NE7	UniProtKB	Modified residue	263	263	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16539	
Q95NE7	UniProtKB	Modified residue	323	323	.	.	.	Note=Phosphotyrosine%3B by ZAP70;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q16539