##gff-version 3 Q12972 UniProtKB Chain 1 351 . . . ID=PRO_0000071505;Note=Nuclear inhibitor of protein phosphatase 1 Q12972 UniProtKB Domain 49 101 . . . Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 Q12972 UniProtKB Region 1 142 . . . Note=Interaction with CDC5L%2C SF3B1 and MELK;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10827081,ECO:0000269|PubMed:12105215,ECO:0000269|PubMed:14699119;Dbxref=PMID:10827081,PMID:12105215,PMID:14699119 Q12972 UniProtKB Region 143 224 . . . Note=Interaction with EED;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12788942;Dbxref=PMID:12788942 Q12972 UniProtKB Region 191 200 . . . Note=Involved in PP-1 inhibition Q12972 UniProtKB Region 200 203 . . . Note=Involved in PP-1 binding Q12972 UniProtKB Region 310 329 . . . Note=Interaction with EED;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12788942;Dbxref=PMID:12788942 Q12972 UniProtKB Region 316 351 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q12972 UniProtKB Region 330 351 . . . Note=RNA-binding Q12972 UniProtKB Region 331 337 . . . Note=Involved in PP-1 inhibition Q12972 UniProtKB Motif 185 209 . . . Note=Nuclear localization signal 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11034904;Dbxref=PMID:11034904 Q12972 UniProtKB Motif 210 240 . . . Note=Nuclear localization signal 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11034904;Dbxref=PMID:11034904 Q12972 UniProtKB Modified residue 161 161 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q28147 Q12972 UniProtKB Modified residue 178 178 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q28147 Q12972 UniProtKB Modified residue 199 199 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q28147 Q12972 UniProtKB Modified residue 204 204 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q28147 Q12972 UniProtKB Modified residue 249 249 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q12972 UniProtKB Modified residue 264 264 . . . Note=Phosphotyrosine%3B by LYN%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11104670;Dbxref=PMID:11104670 Q12972 UniProtKB Modified residue 335 335 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11104670;Dbxref=PMID:11104670 Q12972 UniProtKB Alternative sequence 1 224 . . . ID=VSP_005120;Note=In isoform Gamma. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:7524097;Dbxref=PMID:7524097 Q12972 UniProtKB Alternative sequence 1 142 . . . ID=VSP_005119;Note=In isoform Beta. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:10103062,ECO:0000303|PubMed:15489334;Dbxref=PMID:10103062,PMID:15489334 Q12972 UniProtKB Mutagenesis 68 71 . . . Note=Abolishes interaction with CDC5L%2C SF3B1 and MELK%2C and localization in nuclear speckles. No effect on repressor activity. SRVH->AAAA;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10827081,ECO:0000269|PubMed:11034904,ECO:0000269|PubMed:12105215,ECO:0000269|PubMed:12788942,ECO:0000269|PubMed:14699119;Dbxref=PMID:10827081,PMID:11034904,PMID:12105215,PMID:12788942,PMID:14699119 Q12972 UniProtKB Mutagenesis 193 197 . . . Note=No effect on interaction with EED. KRKRK->AAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12788942;Dbxref=PMID:12788942 Q12972 UniProtKB Mutagenesis 195 197 . . . Note=Abolishes nuclear import%3B when associated with A-234--237-A. KRK->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11034904;Dbxref=PMID:11034904 Q12972 UniProtKB Mutagenesis 199 199 . . . Note=No change in subcellular location%2C no effect on interaction with EED or repressor activity%3B when associated with A-204 or D-204. S->A%2CD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11034904,ECO:0000269|PubMed:12788942;Dbxref=PMID:11034904,PMID:12788942 Q12972 UniProtKB Mutagenesis 201 201 . . . Note=Reduces PP-1 binding%2C no effect on subcellular location or repressor activity and prevents retargeting of PPP1CA and PPP1CC to nuclear speckles%3B when associated with A-203. V->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11034904,ECO:0000269|PubMed:11739654,ECO:0000269|PubMed:12788942;Dbxref=PMID:11034904,PMID:11739654,PMID:12788942 Q12972 UniProtKB Mutagenesis 203 203 . . . Note=Reduces PP-1 binding%2C no effect on subcellular location or repressor activity and prevents retargeting of PPP1CA and PPP1CC to nuclear speckles%3B when associated with A-201. F->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11034904,ECO:0000269|PubMed:11739654,ECO:0000269|PubMed:12788942;Dbxref=PMID:11034904,PMID:11739654,PMID:12788942 Q12972 UniProtKB Mutagenesis 204 204 . . . Note=No change in subcellular location%2C no effect on interaction with EED or repressor activity%3B when associated with A-199 or D-199. S->A%2CD;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11034904,ECO:0000269|PubMed:12788942;Dbxref=PMID:11034904,PMID:12788942 Q12972 UniProtKB Mutagenesis 234 237 . . . Note=Abolishes nuclear import%3B when associated with A-195-197-A. KKKR->AAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11034904;Dbxref=PMID:11034904 Q12972 UniProtKB Mutagenesis 264 264 . . . Note=Abolishes in vitro phosphorylation of isoform gamma by Lyn. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11104670;Dbxref=PMID:11104670 Q12972 UniProtKB Mutagenesis 335 335 . . . Note=Decreases the ability of isoform Gamma to bind and inhibit PP-1. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11104670;Dbxref=PMID:11104670 Q12972 UniProtKB Mutagenesis 346 346 . . . Note=No effect on the ability of isoform Gamma to inhibit PP-1. T->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11104670;Dbxref=PMID:11104670 Q12972 UniProtKB Mutagenesis 348 348 . . . Note=No effect on the ability of isoform Gamma to inhibit PP-1. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11104670;Dbxref=PMID:11104670 Q12972 UniProtKB Helix 162 174 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3V4Y Q12972 UniProtKB Beta strand 208 210 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3V4Y