##gff-version 3
P49138	UniProtKB	Chain	1	386	.	.	.	ID=PRO_0000086289;Note=MAP kinase-activated protein kinase 2	
P49138	UniProtKB	Domain	50	311	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P49138	UniProtKB	Region	1	29	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P49138	UniProtKB	Region	314	350	.	.	.	Note=Autoinhibitory helix	
P49138	UniProtKB	Region	352	376	.	.	.	Note=P38 MAPK-binding site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P49138	UniProtKB	Motif	331	354	.	.	.	Note=Nuclear export signal (NES)	
P49138	UniProtKB	Motif	342	351	.	.	.	Note=Nuclear export signal (NES);Ontology_term=ECO:0000250;evidence=ECO:0000250	
P49138	UniProtKB	Motif	357	360	.	.	.	Note=Bipartite nuclear localization signal 1	
P49138	UniProtKB	Motif	371	375	.	.	.	Note=Bipartite nuclear localization signal 2	
P49138	UniProtKB	Compositional bias	8	29	.	.	.	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P49138	UniProtKB	Active site	172	172	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
P49138	UniProtKB	Binding site	56	64	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P49138	UniProtKB	Binding site	79	79	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
P49138	UniProtKB	Binding site	125	127	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P49138	UniProtKB	Modified residue	208	208	.	.	.	Note=Phosphothreonine%3B by MAPK14;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7592979,ECO:0000269|PubMed:9628873;Dbxref=PMID:7592979,PMID:9628873	
P49138	UniProtKB	Modified residue	258	258	.	.	.	Note=Phosphoserine%3B by MAPK14;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P49137	
P49138	UniProtKB	Modified residue	314	314	.	.	.	Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P49138	UniProtKB	Modified residue	320	320	.	.	.	Note=Phosphothreonine%3B by MAPK14;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:7592979,ECO:0000269|PubMed:9628873;Dbxref=PMID:7592979,PMID:9628873	
P49138	UniProtKB	Cross-link	339	339	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000250;evidence=ECO:0000250	
P49138	UniProtKB	Mutagenesis	208	208	.	.	.	Note=Strong decrease in kinase activity%3B when associated with A-320. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592979;Dbxref=PMID:7592979	
P49138	UniProtKB	Mutagenesis	208	208	.	.	.	Note=Mimicks phosphorylation state and constitutive protein kinase activity%3B when associated with E-320. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592979;Dbxref=PMID:7592979	
P49138	UniProtKB	Mutagenesis	320	320	.	.	.	Note=Strong decrease in kinase activity%3B when associated with A-208. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592979;Dbxref=PMID:7592979	
P49138	UniProtKB	Mutagenesis	320	320	.	.	.	Note=Mimicks phosphorylation state and constitutive protein kinase activity%3B when associated with E-208. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592979;Dbxref=PMID:7592979	
P49138	UniProtKB	Mutagenesis	329	329	.	.	.	Note=Leads to constitutive protein kinase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592979;Dbxref=PMID:7592979	
P49138	UniProtKB	Mutagenesis	335	335	.	.	.	Note=Leads to constitutive protein kinase activity. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7592979;Dbxref=PMID:7592979	
P49138	UniProtKB	Sequence conflict	2	3	.	.	.	Note=LS->IR;Ontology_term=ECO:0000305;evidence=ECO:0000305