##gff-version 3 Q29502 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13177 Q29502 UniProtKB Chain 2 524 . . . ID=PRO_0000086467;Note=Serine/threonine-protein kinase PAK 2 Q29502 UniProtKB Chain 2 212 . . . ID=PRO_0000304926;Note=PAK-2p27;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13177 Q29502 UniProtKB Chain 213 524 . . . ID=PRO_0000304927;Note=PAK-2p34;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13177 Q29502 UniProtKB Domain 74 87 . . . Note=CRIB;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00057 Q29502 UniProtKB Domain 249 500 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q29502 UniProtKB Region 1 81 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q29502 UniProtKB Region 69 137 . . . Note=Autoregulatory region;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13153 Q29502 UniProtKB Region 69 112 . . . Note=GTPase-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13153 Q29502 UniProtKB Region 88 248 . . . Note=Linker Q29502 UniProtKB Region 169 188 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q29502 UniProtKB Region 204 228 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q29502 UniProtKB Motif 245 251 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13177 Q29502 UniProtKB Compositional bias 61 78 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q29502 UniProtKB Compositional bias 213 228 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q29502 UniProtKB Active site 368 368 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 Q29502 UniProtKB Binding site 255 263 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q29502 UniProtKB Binding site 278 278 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q29502 UniProtKB Site 212 213 . . . Note=Cleavage%3B by caspase-3 or caspase-3-like proteases;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13177 Q29502 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13177 Q29502 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13177 Q29502 UniProtKB Modified residue 20 20 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13177 Q29502 UniProtKB Modified residue 55 55 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13177 Q29502 UniProtKB Modified residue 58 58 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13177 Q29502 UniProtKB Modified residue 60 60 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13177 Q29502 UniProtKB Modified residue 62 62 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8CIN4 Q29502 UniProtKB Modified residue 64 64 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13177 Q29502 UniProtKB Modified residue 128 128 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13177 Q29502 UniProtKB Modified residue 134 134 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13177 Q29502 UniProtKB Modified residue 139 139 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13177 Q29502 UniProtKB Modified residue 141 141 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13177 Q29502 UniProtKB Modified residue 143 143 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13177 Q29502 UniProtKB Modified residue 152 152 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8CIN4 Q29502 UniProtKB Modified residue 159 159 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8CIN4 Q29502 UniProtKB Modified residue 169 169 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13177 Q29502 UniProtKB Modified residue 197 197 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13177 Q29502 UniProtKB Modified residue 402 402 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13177