##gff-version 3 Q01167 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:20068231;Dbxref=PMID:19413330,PMID:20068231 Q01167 UniProtKB Chain 2 660 . . . ID=PRO_0000091858;Note=Forkhead box protein K2 Q01167 UniProtKB Domain 54 128 . . . Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 Q01167 UniProtKB DNA binding 258 353 . . . Note=Fork-head;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00089 Q01167 UniProtKB Region 1 36 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01167 UniProtKB Region 85 104 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01167 UniProtKB Region 129 171 . . . Note=Required for interaction with DVL2 and SUDS3;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25805136;Dbxref=PMID:25805136 Q01167 UniProtKB Region 203 260 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01167 UniProtKB Region 300 318 . . . Note=DNA-binding%3B major groove;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624804;Dbxref=PMID:16624804 Q01167 UniProtKB Region 328 332 . . . Note=DNA-binding%3B minor groove;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624804;Dbxref=PMID:16624804 Q01167 UniProtKB Region 348 353 . . . Note=DNA-binding%3B minor groove;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624804;Dbxref=PMID:16624804 Q01167 UniProtKB Region 359 407 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01167 UniProtKB Region 610 632 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01167 UniProtKB Compositional bias 366 395 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01167 UniProtKB Binding site 310 310 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624804;Dbxref=PMID:16624804 Q01167 UniProtKB Binding site 311 311 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624804;Dbxref=PMID:16624804 Q01167 UniProtKB Binding site 313 313 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624804;Dbxref=PMID:16624804 Q01167 UniProtKB Binding site 316 316 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624804;Dbxref=PMID:16624804 Q01167 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:20068231;Dbxref=PMID:19413330,PMID:20068231 Q01167 UniProtKB Modified residue 30 30 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:20068231;Dbxref=PMID:20068231 Q01167 UniProtKB Modified residue 144 144 . . . Note=Omega-N-methylarginine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24129315;Dbxref=PMID:24129315 Q01167 UniProtKB Modified residue 239 239 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17525332,ECO:0007744|PubMed:23186163;Dbxref=PMID:17525332,PMID:23186163 Q01167 UniProtKB Modified residue 373 373 . . . Note=Phosphoserine%3B by CDK1 and CDK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20810654;Dbxref=PMID:20810654 Q01167 UniProtKB Modified residue 398 398 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:19690332,PMID:20068231,PMID:21406692,PMID:23186163,PMID:24275569 Q01167 UniProtKB Modified residue 424 424 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:20068231,PMID:23186163 Q01167 UniProtKB Modified residue 428 428 . . . Note=Phosphoserine%3B by CDK1 and CDK2;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:20810654,ECO:0007744|PubMed:18220336,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:18220336,PMID:19690332,PMID:20068231,PMID:20810654,PMID:23186163 Q01167 UniProtKB Modified residue 599 599 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q3UCQ1 Q01167 UniProtKB Cross-link 161 161 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q01167 UniProtKB Cross-link 164 164 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q01167 UniProtKB Cross-link 527 527 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:29540677,ECO:0007744|PubMed:25218447,ECO:0007744|PubMed:28112733;Dbxref=PMID:25218447,PMID:28112733,PMID:29540677 Q01167 UniProtKB Cross-link 633 633 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:29540677,ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733,PMID:29540677 Q01167 UniProtKB Alternative sequence 304 328 . . . ID=VSP_001560;Note=In isoform 3. NSIRHNLSLNRYFIKVPRSQEEPGK->RGESFAHVGNTRIRIGLPAHKAPQR;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q01167 UniProtKB Alternative sequence 329 660 . . . ID=VSP_001561;Note=In isoform 3. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q01167 UniProtKB Alternative sequence 596 660 . . . ID=VSP_001559;Note=In isoform 2. AAASPLHMLATHASASASLPTKRHNGDQPEQPELKRIKTEDGEGIVIALSVDTPPAAVREKGVQN->GPLGLRRPPCASSDWSCLS;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:1339390;Dbxref=PMID:1339390 Q01167 UniProtKB Mutagenesis 58 58 . . . Note=Reduced interaction with BAP1. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24748658;Dbxref=PMID:24748658 Q01167 UniProtKB Mutagenesis 129 129 . . . Note=No effect on interaction with DVL2. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25805136;Dbxref=PMID:25805136 Q01167 UniProtKB Mutagenesis 130 130 . . . Note=No effect on interaction with DVL2. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25805136;Dbxref=PMID:25805136 Q01167 UniProtKB Mutagenesis 131 131 . . . Note=No effect on interaction with DVL2. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25805136;Dbxref=PMID:25805136 Q01167 UniProtKB Mutagenesis 133 133 . . . Note=No effect on interaction with DVL2. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25805136;Dbxref=PMID:25805136 Q01167 UniProtKB Mutagenesis 136 136 . . . Note=No effect on interaction with DVL2. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25805136;Dbxref=PMID:25805136 Q01167 UniProtKB Mutagenesis 137 137 . . . Note=Abolishes interaction with DVL2 and SUDS3 as well as DVL2 nuclear translocation. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25805136;Dbxref=PMID:25805136 Q01167 UniProtKB Mutagenesis 138 138 . . . Note=No effect on interaction with DVL2. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25805136;Dbxref=PMID:25805136 Q01167 UniProtKB Mutagenesis 141 141 . . . Note=No effect on interaction with DVL2. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25805136;Dbxref=PMID:25805136 Q01167 UniProtKB Mutagenesis 142 142 . . . Note=No effect on interaction with DVL2. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25805136;Dbxref=PMID:25805136 Q01167 UniProtKB Mutagenesis 145 145 . . . Note=Abolishes interaction with DVL2 and SUDS3 as well as DVL2 nuclear translocation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25805136;Dbxref=PMID:25805136 Q01167 UniProtKB Mutagenesis 146 146 . . . Note=Highly reduces interaction with DVL2. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25805136;Dbxref=PMID:25805136 Q01167 UniProtKB Mutagenesis 147 147 . . . Note=No effect on interaction with DVL2. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25805136;Dbxref=PMID:25805136 Q01167 UniProtKB Mutagenesis 148 148 . . . Note=No effect on interaction with DVL2. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25805136;Dbxref=PMID:25805136 Q01167 UniProtKB Mutagenesis 150 150 . . . Note=No effect on interaction with DVL2. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25805136;Dbxref=PMID:25805136 Q01167 UniProtKB Mutagenesis 151 151 . . . Note=No effect on interaction with DVL2. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25805136;Dbxref=PMID:25805136 Q01167 UniProtKB Mutagenesis 152 152 . . . Note=No effect on interaction with DVL2. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25805136;Dbxref=PMID:25805136 Q01167 UniProtKB Mutagenesis 154 154 . . . Note=Abolishes interaction with DVL2 and SUDS3 as well as DVL2 nuclear translocation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25805136;Dbxref=PMID:25805136 Q01167 UniProtKB Mutagenesis 155 155 . . . Note=No effect on interaction with DVL2. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25805136;Dbxref=PMID:25805136 Q01167 UniProtKB Mutagenesis 157 157 . . . Note=No effect on interaction with DVL2. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25805136;Dbxref=PMID:25805136 Q01167 UniProtKB Mutagenesis 258 258 . . . Note=Decreases DNA-binding to 40%25. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624804;Dbxref=PMID:16624804 Q01167 UniProtKB Mutagenesis 300 300 . . . Note=Decreases DNA-binding to 20%25. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624804;Dbxref=PMID:16624804 Q01167 UniProtKB Mutagenesis 305 305 . . . Note=Decreases DNA-binding to 70%25. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624804;Dbxref=PMID:16624804 Q01167 UniProtKB Mutagenesis 307 307 . . . Note=Abolishes DNA-binding. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624804;Dbxref=PMID:16624804 Q01167 UniProtKB Mutagenesis 308 308 . . . Note=No effect on interaction with DVL2. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25805136;Dbxref=PMID:25805136 Q01167 UniProtKB Mutagenesis 328 328 . . . Note=Decreases DNA-binding to 25%25. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16624804;Dbxref=PMID:16624804 Q01167 UniProtKB Mutagenesis 373 373 . . . Note=Decreased phosphorylation leading to increased stability of the protein%3B when associated with A-428. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20810654;Dbxref=PMID:20810654 Q01167 UniProtKB Mutagenesis 373 373 . . . Note=Phosphomimetic mutant%3B decreased phosphorylation leading to decreased stability of the protein%3B when associated with D-428. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20810654;Dbxref=PMID:20810654 Q01167 UniProtKB Mutagenesis 428 428 . . . Note=Decreased phosphorylation leading to increased stability of the protein%3B when associated with A-373. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20810654;Dbxref=PMID:20810654 Q01167 UniProtKB Mutagenesis 428 428 . . . Note=Phosphomimetic mutant%3B decreased phosphorylation leading to decreased stability of the protein%3B when associated with D-373. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20810654;Dbxref=PMID:20810654 Q01167 UniProtKB Mutagenesis 527 527 . . . Note=Abolished SUMOylation%3B when associated with R-633. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29540677;Dbxref=PMID:29540677 Q01167 UniProtKB Mutagenesis 633 633 . . . Note=Abolished SUMOylation%3B when associated with R-527. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29540677;Dbxref=PMID:29540677 Q01167 UniProtKB Sequence conflict 3 120 . . . Note=AAAAALSGAGTPPAGGGAGGGGAGGGGSPPGGWAVARLEGREFEYLMKKRSVTIGRNSSQGSVDVSMGHSSFISRRHLEIFTPPGGGGHGGAAPELPPAQPRPDAGGDFYLRCLGKNG->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q01167 UniProtKB Helix 263 272 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2C6Y Q01167 UniProtKB Beta strand 277 279 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JXS Q01167 UniProtKB Helix 281 291 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2C6Y Q01167 UniProtKB Beta strand 295 298 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JXS Q01167 UniProtKB Helix 300 312 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2C6Y Q01167 UniProtKB Beta strand 316 319 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2C6Y Q01167 UniProtKB Beta strand 324 329 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1JXS Q01167 UniProtKB Beta strand 331 334 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2C6Y Q01167 UniProtKB Helix 336 346 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2C6Y