##gff-version 3 O15392 UniProtKB Chain 1 142 . . . ID=PRO_0000122356;Note=Baculoviral IAP repeat-containing protein 5 O15392 UniProtKB Repeat 18 88 . . . Note=BIR O15392 UniProtKB Binding site 57 57 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:17956729,ECO:0007744|PDB:2QFA;Dbxref=PMID:17956729 O15392 UniProtKB Binding site 60 60 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:17956729,ECO:0007744|PDB:2QFA;Dbxref=PMID:17956729 O15392 UniProtKB Binding site 77 77 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:17956729,ECO:0007744|PDB:2QFA;Dbxref=PMID:17956729 O15392 UniProtKB Binding site 84 84 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:17956729,ECO:0007744|PDB:2QFA;Dbxref=PMID:17956729 O15392 UniProtKB Site 126 126 . . . Note=Interaction with FBXL7;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25778398;Dbxref=PMID:25778398 O15392 UniProtKB Modified residue 20 20 . . . Note=Phosphoserine%3B by AURKC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27332895;Dbxref=PMID:27332895 O15392 UniProtKB Modified residue 23 23 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20826784;Dbxref=PMID:20826784 O15392 UniProtKB Modified residue 34 34 . . . Note=Phosphothreonine%3B by CDK1 and CDK15;Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:11069302,ECO:0000269|PubMed:24866247,ECO:0007744|PubMed:18691976;Dbxref=PMID:11069302,PMID:18691976,PMID:24866247 O15392 UniProtKB Modified residue 48 48 . . . Note=Phosphothreonine%3B by CK2%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21252625;Dbxref=PMID:21252625 O15392 UniProtKB Modified residue 90 90 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20826784;Dbxref=PMID:20826784 O15392 UniProtKB Modified residue 110 110 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20826784;Dbxref=PMID:20826784 O15392 UniProtKB Modified residue 112 112 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20826784;Dbxref=PMID:20826784 O15392 UniProtKB Modified residue 115 115 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20826784;Dbxref=PMID:20826784 O15392 UniProtKB Modified residue 117 117 . . . Note=Phosphothreonine%3B by AURKB;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14610074;Dbxref=PMID:14610074 O15392 UniProtKB Modified residue 121 121 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20826784;Dbxref=PMID:20826784 O15392 UniProtKB Modified residue 129 129 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20826784;Dbxref=PMID:20826784 O15392 UniProtKB Alternative sequence 74 142 . . . ID=VSP_020338;Note=In isoform 3. IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD->MQRKPTIRRKNLRKLRRKCAVPSSSWLPWIEASGRSCLVPEWLHHFQGLFPGATSLPVGPLAMS;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:10626797;Dbxref=PMID:10626797 O15392 UniProtKB Alternative sequence 74 142 . . . ID=VSP_020339;Note=In isoform 6. IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD->MRELC;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.8 O15392 UniProtKB Alternative sequence 74 142 . . . ID=VSP_020340;Note=In isoform 7. IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD->M;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.7 O15392 UniProtKB Alternative sequence 74 74 . . . ID=VSP_002454;Note=In isoform 2. I->IGPGTVAYACNTSTLGGRGGRITR;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:10626797,ECO:0000303|Ref.6;Dbxref=PMID:10626797 O15392 UniProtKB Alternative sequence 105 142 . . . ID=VSP_020341;Note=In isoform 5. DRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD->VRETLPPPRSFIR;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:16329164;Dbxref=PMID:16329164 O15392 UniProtKB Alternative sequence 114 142 . . . ID=VSP_020342;Note=In isoform 4. AKETNNKKKEFEETAKKVRRAIEQLAAMD->ERALLAE;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14741722;Dbxref=PMID:14741722 O15392 UniProtKB Natural variant 129 129 . . . ID=VAR_021071;Note=Loss of acetylation%3B localization primarily within the cytoplasm%3B increased likelihood of existing as monomer%3B stronger binding to XPO1/CRM1. K->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16625196,ECO:0000269|PubMed:20826784;Dbxref=dbSNP:rs2071214,PMID:16625196,PMID:20826784 O15392 UniProtKB Mutagenesis 18 18 . . . Note=Disrupts interaction with histone H3pT3%2C no effect on interaction with INCENP. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20929775;Dbxref=PMID:20929775 O15392 UniProtKB Mutagenesis 23 23 . . . Note=Increases ubiquitination and blocks dissociation from centromeres%3B when associated with R-62%3B R-78 and R-79. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16322459;Dbxref=PMID:16322459 O15392 UniProtKB Mutagenesis 25 25 . . . Note=Disrupts interaction with histone H3pT3%2C no effect on interaction with INCENP. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20929775;Dbxref=PMID:20929775 O15392 UniProtKB Mutagenesis 33 33 . . . Note=Disrupts interaction with histone H3pT3%2C no effect on interaction with INCENP. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20929775;Dbxref=PMID:20929775 O15392 UniProtKB Mutagenesis 34 34 . . . Note=Loss of LAMTOR5 binding. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12773388;Dbxref=PMID:12773388 O15392 UniProtKB Mutagenesis 34 34 . . . Note=Higher affinity for LAMTOR5 binding. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12773388;Dbxref=PMID:12773388 O15392 UniProtKB Mutagenesis 48 48 . . . Note=Localizes normally during mitosis but cannot support cell proliferation. Increased affinity for CDCA8/borealin. T->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21252625;Dbxref=PMID:21252625 O15392 UniProtKB Mutagenesis 57 57 . . . Note=Disrupts interaction with histone H3pT3%2C no effect on interaction with INCENP. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20929775;Dbxref=PMID:20929775 O15392 UniProtKB Mutagenesis 62 62 . . . Note=Increases ubiquitination and blocks dissociation from centromeres%3B when associated with R-23%3B R-78 and R-79. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16322459;Dbxref=PMID:16322459 O15392 UniProtKB Mutagenesis 65 65 . . . Note=Almost abolishes RAN-binding. Does not disrupt binding to AURKB or CDCA8. Disrupts mitotic spindle assembly. Does not disrupt nuclear export. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18591255;Dbxref=PMID:18591255 O15392 UniProtKB Mutagenesis 67 67 . . . Note=Disrupts interaction with histone H3pT3%2C no effect on interaction with INCENP. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20929775;Dbxref=PMID:20929775 O15392 UniProtKB Mutagenesis 70 70 . . . Note=No change. Loss of interaction with AURKB%3B when associated with A-71. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16762323;Dbxref=PMID:16762323 O15392 UniProtKB Mutagenesis 71 71 . . . Note=No change. Loss of interaction with AURKB%3B when associated with A-70. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16762323;Dbxref=PMID:16762323 O15392 UniProtKB Mutagenesis 78 78 . . . Note=Increases ubiquitination and blocks dissociation from centromeres%3B when associated with R-23%3B R-62 and R-79. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16322459;Dbxref=PMID:16322459 O15392 UniProtKB Mutagenesis 79 79 . . . Note=Increases ubiquitination and blocks dissociation from centromeres%3B when associated with R-23%3B R-62 and R-78. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16322459;Dbxref=PMID:16322459 O15392 UniProtKB Mutagenesis 84 84 . . . Note=Loss of cytoprotection. C->A O15392 UniProtKB Mutagenesis 90 91 . . . Note=Loss of FBXL7 mediated polyubiquitination. KK->RR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25778398;Dbxref=PMID:25778398 O15392 UniProtKB Mutagenesis 117 117 . . . Note=Prevents phosphorylation by AURKB. Still able to localize correctly but prevents interaction with INCENP. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14610074;Dbxref=PMID:14610074 O15392 UniProtKB Mutagenesis 117 117 . . . Note=Mimics phosphorylation. Disrupts subcellular localization during mitosis and prevents interaction with INCENP. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14610074;Dbxref=PMID:14610074 O15392 UniProtKB Mutagenesis 126 126 . . . Note=Loss of FBXL7 binding. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25778398;Dbxref=PMID:25778398 O15392 UniProtKB Mutagenesis 129 129 . . . Note=Mimics acetylation. Localization primarily within the nucleus. K->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20826784;Dbxref=PMID:20826784 O15392 UniProtKB Mutagenesis 129 129 . . . Note=Loss of acetylation. Localization primarily within the cytoplasm. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20826784;Dbxref=PMID:20826784 O15392 UniProtKB Sequence conflict 57 58 . . . Note=CF->WV;Ontology_term=ECO:0000305;evidence=ECO:0000305 O15392 UniProtKB Sequence conflict 58 58 . . . Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 O15392 UniProtKB Sequence conflict 128 128 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 O15392 UniProtKB Turn 8 10 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QFA O15392 UniProtKB Helix 11 13 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QFA O15392 UniProtKB Helix 15 20 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QFA O15392 UniProtKB Beta strand 29 32 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YIF O15392 UniProtKB Helix 35 40 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QFA O15392 UniProtKB Beta strand 43 45 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QFA O15392 UniProtKB Beta strand 49 51 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3UIG O15392 UniProtKB Beta strand 55 57 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QFA O15392 UniProtKB Turn 58 60 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QFA O15392 UniProtKB Beta strand 63 65 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YIF O15392 UniProtKB Helix 73 80 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QFA O15392 UniProtKB Turn 81 83 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1F3H O15392 UniProtKB Helix 85 88 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QFA O15392 UniProtKB Helix 93 95 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QFA O15392 UniProtKB Helix 98 139 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2QFA