##gff-version 3 Q9NQR1 UniProtKB Chain 1 393 . . . ID=PRO_0000186081;Note=N-lysine methyltransferase KMT5A Q9NQR1 UniProtKB Domain 257 378 . . . Note=SET;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00190 Q9NQR1 UniProtKB Region 68 88 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NQR1 UniProtKB Region 135 241 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NQR1 UniProtKB Coiled coil 134 163 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9NQR1 UniProtKB Compositional bias 202 216 . . . Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NQR1 UniProtKB Compositional bias 226 241 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NQR1 UniProtKB Binding site 267 269 . . . . Q9NQR1 UniProtKB Binding site 312 312 . . . . Q9NQR1 UniProtKB Binding site 339 340 . . . . Q9NQR1 UniProtKB Modified residue 100 100 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231;Dbxref=PMID:18669648,PMID:20068231 Q9NQR1 UniProtKB Modified residue 162 162 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23468428;Dbxref=PMID:23468428 Q9NQR1 UniProtKB Modified residue 181 181 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q9NQR1 UniProtKB Alternative sequence 1 41 . . . ID=VSP_002226;Note=In isoform 2. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:12121615,ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:15489334;Dbxref=PMID:12121615,PMID:14702039,PMID:15489334 Q9NQR1 UniProtKB Alternative sequence 42 57 . . . ID=VSP_002227;Note=In isoform 2. PGRAAGGKMSKPCAVE->MARGRKMSKPRAVEAA;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:12121615,ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:15489334;Dbxref=PMID:12121615,PMID:14702039,PMID:15489334 Q9NQR1 UniProtKB Mutagenesis 162 162 . . . Note=Does not affect the interaction with SIRT2. Increases the number of mitotic foci formation. Does not affect methyltransferase activity. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23468428;Dbxref=PMID:23468428 Q9NQR1 UniProtKB Mutagenesis 162 162 . . . Note=Increases the interaction with SIRT2. Reduces the number of mitotic foci formation. Does not affect methyltransferase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23468428;Dbxref=PMID:23468428 Q9NQR1 UniProtKB Mutagenesis 286 286 . . . Note=Strongly reduces affinity for histone H4 and abolishes methyltransferase activity. Y->A%2CF;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15933070;Dbxref=PMID:15933070 Q9NQR1 UniProtKB Mutagenesis 300 300 . . . Note=Strongly reduces affinity for histone H4. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15933070;Dbxref=PMID:15933070 Q9NQR1 UniProtKB Mutagenesis 311 311 . . . Note=Strongly reduces affinity for histone H4. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15933070;Dbxref=PMID:15933070 Q9NQR1 UniProtKB Mutagenesis 336 336 . . . Note=Abolishes methyltransferase activity. R->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12086618,ECO:0000269|PubMed:23478445;Dbxref=PMID:12086618,PMID:23478445 Q9NQR1 UniProtKB Mutagenesis 340 340 . . . Note=Strongly decreases methyltransferase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12121615;Dbxref=PMID:12121615 Q9NQR1 UniProtKB Mutagenesis 375 375 . . . Note=Strongly reduces affinity for histone H4 and methyltransferase activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15933070;Dbxref=PMID:15933070 Q9NQR1 UniProtKB Mutagenesis 375 375 . . . Note=Alters methyltransferase activity%2C so that both monomethylation and dimethylation take place. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15933070;Dbxref=PMID:15933070 Q9NQR1 UniProtKB Mutagenesis 379 379 . . . Note=Abolishes histone H4 binding and methyltransferase activity. D->A%2CN;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15933070,ECO:0000269|PubMed:17707234,ECO:0000269|PubMed:20870725,ECO:0000269|PubMed:23478445;Dbxref=PMID:15933070,PMID:17707234,PMID:20870725,PMID:23478445 Q9NQR1 UniProtKB Mutagenesis 385 393 . . . Note=Abolishes methyltransferase activity. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12121615;Dbxref=PMID:12121615 Q9NQR1 UniProtKB Mutagenesis 388 388 . . . Note=Strongly reduces affinity for histone H4. H->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15933070;Dbxref=PMID:15933070 Q9NQR1 UniProtKB Mutagenesis 388 388 . . . Note=Increases affinity for histone H4. H->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15933070;Dbxref=PMID:15933070 Q9NQR1 UniProtKB Sequence conflict 162 163 . . . Note=KG->RR;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NQR1 UniProtKB Sequence conflict 281 281 . . . Note=D->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NQR1 UniProtKB Sequence conflict 343 343 . . . Note=C->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NQR1 UniProtKB Sequence conflict 357 357 . . . Note=P->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NQR1 UniProtKB Sequence conflict 373 373 . . . Note=L->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NQR1 UniProtKB Helix 236 253 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F9X Q9NQR1 UniProtKB Beta strand 259 264 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F9X Q9NQR1 UniProtKB Turn 265 267 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F9X Q9NQR1 UniProtKB Beta strand 268 275 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F9X Q9NQR1 UniProtKB Beta strand 282 285 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F9X Q9NQR1 UniProtKB Beta strand 288 292 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F9X Q9NQR1 UniProtKB Helix 293 303 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F9X Q9NQR1 UniProtKB Helix 307 309 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TH7 Q9NQR1 UniProtKB Helix 310 312 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4IJ8 Q9NQR1 UniProtKB Beta strand 313 318 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F9X Q9NQR1 UniProtKB Beta strand 321 326 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F9X Q9NQR1 UniProtKB Helix 335 337 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F9X Q9NQR1 UniProtKB Beta strand 338 340 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TH7 Q9NQR1 UniProtKB Beta strand 345 353 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F9X Q9NQR1 UniProtKB Beta strand 356 365 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F9X Q9NQR1 UniProtKB Beta strand 372 375 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5TH7 Q9NQR1 UniProtKB Turn 377 380 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5V2N Q9NQR1 UniProtKB Helix 382 387 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F9X Q9NQR1 UniProtKB Helix 389 392 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F9X