##gff-version 3 P25500 UniProtKB Chain 1 739 . . . ID=PRO_0000051611;Note=Poly(A) polymerase alpha P25500 UniProtKB Region 1 23 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P25500 UniProtKB Region 501 565 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P25500 UniProtKB Region 508 643 . . . Note=Ser/Thr-rich P25500 UniProtKB Region 580 700 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P25500 UniProtKB Region 671 739 . . . Note=Required for interaction with NUDT21;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17172643;Dbxref=PMID:17172643 P25500 UniProtKB Motif 490 507 . . . Note=Nuclear localization signal 1 P25500 UniProtKB Motif 644 659 . . . Note=Nuclear localization signal 2 P25500 UniProtKB Compositional bias 1 21 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P25500 UniProtKB Compositional bias 514 565 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P25500 UniProtKB Compositional bias 580 625 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P25500 UniProtKB Compositional bias 646 666 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P25500 UniProtKB Binding site 100 102 . . . . P25500 UniProtKB Binding site 109 109 . . . . P25500 UniProtKB Binding site 113 115 . . . . P25500 UniProtKB Binding site 113 113 . . . . P25500 UniProtKB Binding site 113 113 . . . . P25500 UniProtKB Binding site 115 115 . . . . P25500 UniProtKB Binding site 115 115 . . . . P25500 UniProtKB Binding site 167 167 . . . . P25500 UniProtKB Binding site 167 167 . . . . P25500 UniProtKB Binding site 228 228 . . . . P25500 UniProtKB Binding site 237 237 . . . . P25500 UniProtKB Binding site 246 247 . . . . P25500 UniProtKB Site 153 153 . . . Note=Interaction with RNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 P25500 UniProtKB Site 158 158 . . . Note=Interaction with RNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 P25500 UniProtKB Site 328 328 . . . Note=Interaction with RNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 P25500 UniProtKB Site 399 399 . . . Note=Interaction with RNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 P25500 UniProtKB Site 524 524 . . . Note=Interaction with RNA;Ontology_term=ECO:0000250;evidence=ECO:0000250 P25500 UniProtKB Modified residue 10 10 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P51003 P25500 UniProtKB Modified residue 24 24 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P51003 P25500 UniProtKB Modified residue 537 537 . . . Note=Phosphoserine%3B by MAPK;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q61183 P25500 UniProtKB Modified residue 558 558 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P51003 P25500 UniProtKB Modified residue 635 635 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17172643;Dbxref=PMID:17172643 P25500 UniProtKB Modified residue 644 644 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17172643;Dbxref=PMID:17172643 P25500 UniProtKB Modified residue 730 730 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17172643;Dbxref=PMID:17172643 P25500 UniProtKB Modified residue 732 732 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P51003 P25500 UniProtKB Modified residue 734 734 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17172643;Dbxref=PMID:17172643 P25500 UniProtKB Cross-link 444 444 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000305;evidence=ECO:0000305 P25500 UniProtKB Cross-link 445 445 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000305;evidence=ECO:0000305 P25500 UniProtKB Cross-link 506 506 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000305;evidence=ECO:0000305 P25500 UniProtKB Cross-link 507 507 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000305;evidence=ECO:0000305 P25500 UniProtKB Cross-link 730 730 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250 P25500 UniProtKB Cross-link 734 734 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250 P25500 UniProtKB Alternative sequence 663 683 . . . ID=VSP_004524;Note=In isoform Short. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:1756732;Dbxref=PMID:1756732 P25500 UniProtKB Alternative sequence 709 710 . . . ID=VSP_004525;Note=In isoform Short. KT->II;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:1756732;Dbxref=PMID:1756732 P25500 UniProtKB Alternative sequence 711 739 . . . ID=VSP_004526;Note=In isoform Short. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:1756732;Dbxref=PMID:1756732 P25500 UniProtKB Mutagenesis 100 100 . . . Note=Strongly decreased enzyme activity. Strongly reduced affinity for RNA. F->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15328606;Dbxref=PMID:15328606 P25500 UniProtKB Mutagenesis 113 115 . . . Note=Abolishes most of the specific and non-specific polyadenylation activity. DID->AIA P25500 UniProtKB Mutagenesis 113 113 . . . Note=Abolishes most of the specific and non-specific polyadenylation activity. D->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8665867;Dbxref=PMID:8665867 P25500 UniProtKB Mutagenesis 115 115 . . . Note=Abolishes most of the specific and non-specific polyadenylation activity. D->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8665867;Dbxref=PMID:8665867 P25500 UniProtKB Mutagenesis 153 153 . . . Note=Strongly reduced affinity for RNA. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15328606;Dbxref=PMID:15328606 P25500 UniProtKB Mutagenesis 156 156 . . . Note=Strongly decreased enzyme activity. Strongly reduced affinity for RNA. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15328606;Dbxref=PMID:15328606 P25500 UniProtKB Mutagenesis 162 163 . . . Note=Small decrease in non-specific and specific polyadenylation activity. DG->HA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8665867;Dbxref=PMID:8665867 P25500 UniProtKB Mutagenesis 167 167 . . . Note=Loss of enzyme activity. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15328606,ECO:0000269|PubMed:8665867;Dbxref=PMID:15328606,PMID:8665867 P25500 UniProtKB Mutagenesis 167 167 . . . Note=Abolishes most of the specific and non-specific polyadenylation activity. D->H;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15328606,ECO:0000269|PubMed:8665867;Dbxref=PMID:15328606,PMID:8665867 P25500 UniProtKB Mutagenesis 167 167 . . . Note=Strongly decreased enzyme activity. Strongly reduced affinity for RNA. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15328606,ECO:0000269|PubMed:8665867;Dbxref=PMID:15328606,PMID:8665867 P25500 UniProtKB Mutagenesis 186 186 . . . Note=Small decrease in non-specific and specific polyadenylation activity. D->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8665867;Dbxref=PMID:8665867 P25500 UniProtKB Mutagenesis 194 194 . . . Note=No change in non-specific and specific polyadenylation activity. D->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8665867;Dbxref=PMID:8665867 P25500 UniProtKB Mutagenesis 199 199 . . . Note=Strongly reduced affinity for RNA. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15328606;Dbxref=PMID:15328606 P25500 UniProtKB Mutagenesis 202 202 . . . Note=Strongly decreased enzyme activity. Strongly reduced affinity for RNA. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15328606;Dbxref=PMID:15328606 P25500 UniProtKB Mutagenesis 203 203 . . . Note=Loss of enzyme activity. Strongly reduced affinity for RNA. G->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15328606;Dbxref=PMID:15328606 P25500 UniProtKB Mutagenesis 208 209 . . . Note=Reduces by 60%25 non-specific and specific polyadenylation activity. DE->AA P25500 UniProtKB Mutagenesis 208 208 . . . Note=Reduces by 60%25 non-specific rf and specific polyadenylation activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8665867;Dbxref=PMID:8665867 P25500 UniProtKB Mutagenesis 208 208 . . . Note=Reduces by 20%25 non-specific and specific polyadenylation activity. D->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8665867;Dbxref=PMID:8665867 P25500 UniProtKB Mutagenesis 209 209 . . . Note=No change in non-specific and specific polyadenylation activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8665867;Dbxref=PMID:8665867 P25500 UniProtKB Mutagenesis 228 228 . . . Note=Strongly decreased affinity for ATP. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15328606;Dbxref=PMID:15328606 P25500 UniProtKB Mutagenesis 232 232 . . . Note=Decreased affinity for ATP. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15328606;Dbxref=PMID:15328606 P25500 UniProtKB Mutagenesis 237 237 . . . Note=Strongly decreased affinity for ATP. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15328606;Dbxref=PMID:15328606 P25500 UniProtKB Mutagenesis 247 247 . . . Note=Strongly reduced affinity for RNA. V->A%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15328606;Dbxref=PMID:15328606 P25500 UniProtKB Mutagenesis 291 292 . . . Note=Abolishes most of non-specific polyadenylation activity. EE->AA P25500 UniProtKB Mutagenesis 291 291 . . . Note=Reduces by 60%25 non-specific polyadenylation activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8665867;Dbxref=PMID:8665867 P25500 UniProtKB Mutagenesis 292 292 . . . Note=No change in non-specific polyadenylation activity. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8665867;Dbxref=PMID:8665867 P25500 UniProtKB Mutagenesis 308 308 . . . Note=No change in non-specific and specific polyadenylation activity. D->A P25500 UniProtKB Mutagenesis 317 317 . . . Note=Strongly decreased affinity for ATP. T->G P25500 UniProtKB Mutagenesis 431 432 . . . Note=No change in non-specific and specific polyadenylation activity. EE->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8665867;Dbxref=PMID:8665867 P25500 UniProtKB Mutagenesis 455 455 . . . Note=Reduces by 30%25 non-specific polyadenylation activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8665867;Dbxref=PMID:8665867 P25500 UniProtKB Mutagenesis 459 459 . . . Note=No change in non-specific polyadenylation activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8665867;Dbxref=PMID:8665867 P25500 UniProtKB Mutagenesis 465 465 . . . Note=No change in non-specific and specific polyadenylation activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8665867;Dbxref=PMID:8665867 P25500 UniProtKB Mutagenesis 635 635 . . . Note=Weak binding to KPBN1. Cytoplasmic location%3B when associated with Q-644%3B Q-730 and Q-734. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17172643;Dbxref=PMID:17172643 P25500 UniProtKB Mutagenesis 635 635 . . . Note=Some decrease in acetylation. Binds KPBN1 and localizes to the nucleus%3B when associated with R-644%3B R-730 and R-734. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17172643;Dbxref=PMID:17172643 P25500 UniProtKB Mutagenesis 644 644 . . . Note=Weak binding to KPBN1. Cytoplasmic location%3B when associated with Q-635%3B Q-730 and Q-734. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17172643;Dbxref=PMID:17172643 P25500 UniProtKB Mutagenesis 644 644 . . . Note=Large decrease in acetylation. Binds KPBN1 and localizes to the nucleus%3B when associated with R-635%3B R-730 and R-734. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17172643;Dbxref=PMID:17172643 P25500 UniProtKB Mutagenesis 730 730 . . . Note=Weak binding to KPBN1. Cytoplasmic location%3B when associated with Q-635%3B Q-644 and Q-734. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17172643;Dbxref=PMID:17172643 P25500 UniProtKB Mutagenesis 730 730 . . . Note=Some decrease in acetylation. Binds KPBN1 and localizes to the nucleus%3B when associated with R-635%3B R-644 and R-734. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17172643;Dbxref=PMID:17172643 P25500 UniProtKB Mutagenesis 734 734 . . . Note=Weak binding to KPBN1. Cytoplasmic location%3B when associated with Q-635%3B Q-644 and Q-730. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17172643;Dbxref=PMID:17172643 P25500 UniProtKB Mutagenesis 734 734 . . . Note=Some decrease in acetylation. Binds KPBN1 and localizes to the nucleus%3B when associated with R-635%3B R-644 and R-730. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17172643;Dbxref=PMID:17172643 P25500 UniProtKB Sequence conflict 80 80 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 P25500 UniProtKB Beta strand 21 23 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Helix 33 46 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Helix 47 49 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Helix 55 82 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Helix 87 90 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Beta strand 96 100 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Helix 101 105 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Beta strand 114 120 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Helix 126 129 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Helix 132 138 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Beta strand 143 149 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Beta strand 152 154 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Beta strand 156 161 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Beta strand 164 172 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Beta strand 176 178 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Helix 187 190 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Helix 195 211 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Beta strand 213 215 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Helix 217 233 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Turn 239 242 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Helix 246 259 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Helix 265 277 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Turn 302 304 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Helix 306 310 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Beta strand 318 321 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Turn 325 328 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Helix 331 352 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Helix 358 361 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Helix 367 370 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Beta strand 372 383 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Helix 384 395 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Helix 398 406 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Beta strand 411 416 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Beta strand 428 430 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q78 P25500 UniProtKB Beta strand 433 443 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Helix 457 473 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Beta strand 482 489 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Helix 490 493 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79 P25500 UniProtKB Helix 494 496 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1Q79