##gff-version 3 P38806 UniProtKB Chain 1 282 . . . ID=PRO_0000212679;Note=Chromatin modification-related protein YNG2 P38806 UniProtKB Zinc finger 222 271 . . . Note=PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 P38806 UniProtKB Region 123 217 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P38806 UniProtKB Coiled coil 35 86 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 P38806 UniProtKB Compositional bias 133 162 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P38806 UniProtKB Binding site 225 225 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 P38806 UniProtKB Binding site 227 227 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 P38806 UniProtKB Binding site 238 238 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 P38806 UniProtKB Binding site 243 243 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 P38806 UniProtKB Binding site 249 249 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 P38806 UniProtKB Binding site 252 252 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 P38806 UniProtKB Binding site 265 265 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 P38806 UniProtKB Binding site 268 268 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 P38806 UniProtKB Site 224 224 . . . Note=Histone H3K4me3 binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 P38806 UniProtKB Site 235 235 . . . Note=Histone H3K4me3 binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 P38806 UniProtKB Site 239 239 . . . Note=Histone H3K4me3 binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 P38806 UniProtKB Site 247 247 . . . Note=Histone H3K4me3 binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9UK53 P38806 UniProtKB Modified residue 183 183 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19779198;Dbxref=PMID:19779198 P38806 UniProtKB Modified residue 185 185 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19779198;Dbxref=PMID:19779198 P38806 UniProtKB Modified residue 188 188 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19779198;Dbxref=PMID:19779198 P38806 UniProtKB Helix 3 13 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5J9T P38806 UniProtKB Turn 14 16 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5J9T P38806 UniProtKB Helix 17 56 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5J9T P38806 UniProtKB Beta strand 58 60 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5J9T P38806 UniProtKB Helix 65 113 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5J9T P38806 UniProtKB Beta strand 225 227 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2MUM P38806 UniProtKB Turn 250 254 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2MUM P38806 UniProtKB Helix 266 270 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2MUM