##gff-version 3 O95863 UniProtKB Chain 1 264 . . . ID=PRO_0000047029;Note=Zinc finger protein SNAI1 O95863 UniProtKB Zinc finger 154 176 . . . Note=C2H2-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 O95863 UniProtKB Zinc finger 178 202 . . . Note=C2H2-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 O95863 UniProtKB Zinc finger 208 230 . . . Note=C2H2-type 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 O95863 UniProtKB Zinc finger 236 259 . . . Note=C2H2-type 4%3B atypical;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00042 O95863 UniProtKB Region 1 27 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O95863 UniProtKB Region 1 20 . . . Note=SNAG domain;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:20389281,ECO:0000305|PubMed:21300290;Dbxref=PMID:20389281,PMID:21300290 O95863 UniProtKB Region 2 7 . . . Note=Required and sufficient for interaction with KDM1A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20389281,ECO:0000269|PubMed:23721412;Dbxref=PMID:20389281,PMID:23721412 O95863 UniProtKB Region 10 40 . . . Note=LATS2 binding O95863 UniProtKB Region 86 115 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O95863 UniProtKB Region 120 151 . . . Note=Required for FBXL14-triggered degradation O95863 UniProtKB Region 151 264 . . . Note=Required for nuclear localization and interaction with KPNB1%2C NOTCH1 and PARP1;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21577210,ECO:0000269|PubMed:22128911;Dbxref=PMID:21577210,PMID:22128911 O95863 UniProtKB Motif 95 100 . . . Note=Destruction motif O95863 UniProtKB Compositional bias 86 100 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O95863 UniProtKB Modified residue 11 11 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19923321;Dbxref=PMID:19923321 O95863 UniProtKB Modified residue 82 82 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19923321;Dbxref=PMID:19923321 O95863 UniProtKB Modified residue 92 92 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19923321;Dbxref=PMID:19923321 O95863 UniProtKB Modified residue 96 96 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:20305697,ECO:0000305|PubMed:15448698;Dbxref=PMID:15448698,PMID:20305697 O95863 UniProtKB Modified residue 100 100 . . . Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15448698;Dbxref=PMID:15448698 O95863 UniProtKB Modified residue 104 104 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:15647282,ECO:0000269|PubMed:19923321,ECO:0000305|PubMed:15448698;Dbxref=PMID:15448698,PMID:15647282,PMID:19923321 O95863 UniProtKB Modified residue 107 107 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:15647282,ECO:0000269|PubMed:19923321,ECO:0000305|PubMed:15448698;Dbxref=PMID:15448698,PMID:15647282,PMID:19923321 O95863 UniProtKB Modified residue 111 111 . . . Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15448698;Dbxref=PMID:15448698 O95863 UniProtKB Modified residue 115 115 . . . Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15448698;Dbxref=PMID:15448698 O95863 UniProtKB Modified residue 119 119 . . . Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15448698;Dbxref=PMID:15448698 O95863 UniProtKB Modified residue 203 203 . . . Note=Phosphothreonine%3B by LATS2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21952048;Dbxref=PMID:21952048 O95863 UniProtKB Modified residue 246 246 . . . Note=Phosphoserine%3B by PAK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15833848;Dbxref=PMID:15833848 O95863 UniProtKB Glycosylation 112 112 . . . Note=O-linked (GlcNAc) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20959806;Dbxref=PMID:20959806 O95863 UniProtKB Cross-link 98 98 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) O95863 UniProtKB Cross-link 137 137 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) O95863 UniProtKB Cross-link 146 146 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) O95863 UniProtKB Natural variant 66 66 . . . ID=VAR_069162;Note=A->V;Dbxref=dbSNP:rs34261470 O95863 UniProtKB Natural variant 118 118 . . . ID=VAR_019969;Note=V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11245431;Dbxref=dbSNP:rs4647958,PMID:11245431 O95863 UniProtKB Mutagenesis 2 2 . . . Note=Abolishes repressor activity on E-cadherin/CDH1 promoter and binding to KDM1A. P->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20389281,ECO:0000269|PubMed:20562920;Dbxref=PMID:20389281,PMID:20562920 O95863 UniProtKB Mutagenesis 3 3 . . . Note=Loss of interaction with KDM1A. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20389281;Dbxref=PMID:20389281 O95863 UniProtKB Mutagenesis 4 4 . . . Note=Loss of interaction with KDM1A. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20389281;Dbxref=PMID:20389281 O95863 UniProtKB Mutagenesis 5 5 . . . Note=Loss of interaction with KDM1A. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20389281;Dbxref=PMID:20389281 O95863 UniProtKB Mutagenesis 8 8 . . . Note=Loss of interaction with KDM1A. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20389281;Dbxref=PMID:20389281 O95863 UniProtKB Mutagenesis 9 9 . . . Note=Loss of interaction with KDM1A. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20389281;Dbxref=PMID:20389281 O95863 UniProtKB Mutagenesis 9 9 . . . Note=Does not affect E-cadherin/CDH1 repression%3B when associated with R-16. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096638;Dbxref=PMID:16096638 O95863 UniProtKB Mutagenesis 11 11 . . . Note=Abolishes PKA phosphorylation. Strongly decreases repressor activity on E-cadherin/CDH1 and CLDN1 promoters. Increases protein stability. Affects function in EMT. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19923321;Dbxref=PMID:19923321 O95863 UniProtKB Mutagenesis 16 16 . . . Note=Does not affect E-cadherin repression%3B when associated with R-9. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16096638;Dbxref=PMID:16096638 O95863 UniProtKB Mutagenesis 92 92 . . . Note=Abolishes CK2 phosphorylation. Strongly decreases repressor activity on E-cadherin/CDH1 and CLDN1 promoters. Increases protein stability. Affects function in cell survival. Abolishes phosphorylation in the serine-rich region%3B when associated with A-104 and A-107. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19923321;Dbxref=PMID:19923321 O95863 UniProtKB Mutagenesis 92 92 . . . Note=Does not affect repressor activity on E-cadherin/CDH1 promoter. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19923321;Dbxref=PMID:19923321 O95863 UniProtKB Mutagenesis 96 96 . . . Note=Abolishes recognition and ubiquitination by BTRC which increases steady state level and half-life. Preferentially localizes to the nucleus. Induces a more aggressive tissue invasion program. Lower sensitivity to BTRC-triggered degradation%2C impairs phosphorylation by GSK3B and does not affect NOTCH1-induced degradation%3B when associated with A-100. Lower sensitivity to BTRC-triggered degradation%2C impaired phosphorylation by GSK3B and loss of cytoplasmic localization%3B when associated with A-100%3B A-107%3B A-111%3B A-115 and A-119. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15448698,ECO:0000269|PubMed:15647282,ECO:0000269|PubMed:20305697,ECO:0000269|PubMed:22128911;Dbxref=PMID:15448698,PMID:15647282,PMID:20305697,PMID:22128911 O95863 UniProtKB Mutagenesis 98 98 . . . Note=No change. Complete loss of sensitivity to FBXL14- and BTRC-triggered degradation and loss of ability to repress E-cadherin/CDH1%3B when associated with R-137 and R-146. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16096638,ECO:0000269|PubMed:19955572;Dbxref=PMID:16096638,PMID:19955572 O95863 UniProtKB Mutagenesis 100 100 . . . Note=Lower sensitivity to BTRC-triggered degradation and impaired phosphorylation by GSK3B%3B when associated with A-96. Lower sensitivity to BTRC-triggered degradation%2C impaired phosphorylation by GSK3B and loss of cytoplasmic localization%3B when associated with A-96%3B A-107%3B A-111%3B A-115 and A-119. Does not affect NOTCH1-induced degradation%3B when associated with A-96. Abolishes phosphorylation at S-96. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15448698,ECO:0000269|PubMed:20305697,ECO:0000269|PubMed:22128911;Dbxref=PMID:15448698,PMID:20305697,PMID:22128911 O95863 UniProtKB Mutagenesis 104 104 . . . Note=Increases protein stability%2C does not affect repressor activity on E-cadherin/CDH1 promoter%2C preferentially localizes to the nucleus%2C induces a more aggressive tissue invasion program and impairs phosphorylation by GSK3B%2C binding to BTRC and ubiquitination%3B when associated with A-107. Impairs phosphorylation in the serine-rich domain/region%3B when associated with A-92 and A-107. Abolishes phosphorylation at S-96. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15647282,ECO:0000269|PubMed:19923321,ECO:0000269|PubMed:20305697;Dbxref=PMID:15647282,PMID:19923321,PMID:20305697 O95863 UniProtKB Mutagenesis 107 107 . . . Note=Lower sensitivity to BTRC-triggered degradation%2C impaired phosphorylation by GSK3B and loss of cytoplasmic localization%3B when associated with A-111%3B A-115 and A-119. Lower sensitivity to BTRC-triggered degradation%2C impaired phosphorylation by GSK3B and loss of cytoplasmic localization%3B when associated with A-96%3B A-100%3B A-111%3B A-115 and A-119. Increases protein stability%2C does not affect repressor activity on E-cadherin promoter%2C preferentially localizes to the nucleus%2C induces a more aggressive tissue invasion program and impairs phosphorylation by GSK3B%2C binding to BTRC and ubiquitination%3B when associated with A-104. Impairs phosphorylation in the serine-rich region%3B when associated with A-92 and A-104. Abolishes phosphorylation at S-96. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15448698,ECO:0000269|PubMed:15647282,ECO:0000269|PubMed:19923321,ECO:0000269|PubMed:20305697;Dbxref=PMID:15448698,PMID:15647282,PMID:19923321,PMID:20305697 O95863 UniProtKB Mutagenesis 107 107 . . . Note=Predominantly localized to the cytoplasm%3B when associated with E-111%3B E-115 and E-119. S->E;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15448698,ECO:0000269|PubMed:15647282,ECO:0000269|PubMed:19923321,ECO:0000269|PubMed:20305697;Dbxref=PMID:15448698,PMID:15647282,PMID:19923321,PMID:20305697 O95863 UniProtKB Mutagenesis 111 111 . . . Note=Lower sensitivity to BTRC-triggered degradation%2C impaired phosphorylation by GSK3B and loss of cytoplasmic localization%3B when associated with A-107%3B A-115 and A-119. Lower sensitivity to BTRC-triggered degradation%2C impaired phosphorylation by GSK3B and loss of cytoplasmic localization%3B when associated with A-96%3B A-100%3B A-107%3B A-115 and A-119. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15448698;Dbxref=PMID:15448698 O95863 UniProtKB Mutagenesis 111 111 . . . Note=Predominantly localized to the cytoplasm%3B when associated with E-107%3B E-115 and E-119. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15448698;Dbxref=PMID:15448698 O95863 UniProtKB Mutagenesis 115 115 . . . Note=Lower sensitivity to BTRC-triggered degradation%2C impaired phosphorylation by GSK3B and loss of cytoplasmic localization%3B when associated with A-107%3B A-111 and A-119. Lower sensitivity to BTRC-triggered degradation%2C impaired phosphorylation by GSK3B and loss of cytoplasmic localization%3B when associated with A-96%3B A-100%3B A-107%3B A-111 and A-119. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15448698;Dbxref=PMID:15448698 O95863 UniProtKB Mutagenesis 115 115 . . . Note=Predominantly localized to the cytoplasm%3B when associated with E-107%3B E-111 and E-119. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15448698;Dbxref=PMID:15448698 O95863 UniProtKB Mutagenesis 119 119 . . . Note=Lower sensitivity to BTRC-triggered degradation%2C impaired phosphorylation by GSK3B and loss of cytoplasmic localization%3B when associated with A-107%3B A-111 and A-119. Lower sensitivity to BTRC-triggered degradation%2C impaired phosphorylation by GSK3B and loss of cytoplasmic localization%3B when associated with A-96%3B A-100%3B A-107%3B A-111 and A-115. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15448698;Dbxref=PMID:15448698 O95863 UniProtKB Mutagenesis 119 119 . . . Note=Predominantly localized to the cytoplasm%3B when associated with E-107%3B E-111 and E-115. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15448698;Dbxref=PMID:15448698 O95863 UniProtKB Mutagenesis 137 137 . . . Note=Lower sensitivity to FBXL14-triggered degradation. Lower sensitivity to FBXL14-triggered degradation%3B when associated with R-146. Complete loss of sensitivity to FBXL14- and BTRC-triggered degradation and loss of ability to repress E-cadherin%3B when associated with R-98 and R-146. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16096638,ECO:0000269|PubMed:19955572;Dbxref=PMID:16096638,PMID:19955572 O95863 UniProtKB Mutagenesis 146 146 . . . Note=Lower sensitivity to FBXL14-triggered degradation. Lower sensitivity to FBXL14-triggered degradation%3B when associated with R-137. Complete loss of sensitivity to FBXL14- and BTRC-triggered degradation%3B when associated with R-98 and R-137. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19955572;Dbxref=PMID:19955572 O95863 UniProtKB Mutagenesis 151 152 . . . Note=Does not affect binding to KPNB1%2C KPNA2%2C IPO7 or TNPO1. RK->EE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19386897;Dbxref=PMID:19386897 O95863 UniProtKB Mutagenesis 156 156 . . . Note=Abolishes binding to KPNB1%2C KPNA2%2C IPO7 and TNPO1 and nuclear localization. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19386897;Dbxref=PMID:19386897 O95863 UniProtKB Mutagenesis 161 161 . . . Note=Does not affect binding to KPNB1%2C KPNA2%2C IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1%2C KPNA2%2C IPO7 and TNPO1 and abolishes nuclear localization%2C DNA binding and repressor activity on E-cadherin/CDH1 promoter%3B when associated with E-170. Abolishes binding to KPNB1%2C KPNA2%2C IPO7 and TNPO1 and nuclear localization%3B when associated with E-187 and/or E-220. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19386897;Dbxref=PMID:19386897 O95863 UniProtKB Mutagenesis 170 170 . . . Note=Does not affect binding to KPNB1%2C KPNA2%2C IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1%2C KPNA2%2C IPO7 and TNPO1 and abolishes nuclear localization%2C DNA binding and repressor activity on E-cadherin/CDH1 promoter%3B when associated with E-161. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19386897;Dbxref=PMID:19386897 O95863 UniProtKB Mutagenesis 182 182 . . . Note=Impairs binding to KPNB1%2C IPO7 and TNPO1 and abolishes binding to KPNA2. Localizes to cytoplasm and nucleus. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19386897;Dbxref=PMID:19386897 O95863 UniProtKB Mutagenesis 187 187 . . . Note=Does not affect binding to KPNB1%2C KPNA2%2C IPO7 or TNPO1. Impairs binding to KPNB1%2C KPNA2%2C IPO7 and TNPO1 and abolishes nuclear localization%2C DNA binding and repressor activity on E-cadherin/CDH1 promoter%3B when associated with E-191. Abolishes binding to KPNB1%2C KPNA2%2C IPO7 and TNPO1 and nuclear localization%3B when associated with E-161 and/or E-220. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19386897;Dbxref=PMID:19386897 O95863 UniProtKB Mutagenesis 191 191 . . . Note=Mildly reduces binding to KPNB1 and nuclear import. Strongly reduces binding to KPNB1 and nuclear import%3B when associated with A-193. Loss of binding to KPNB1 and nuclear import%3B when associated with A-193 and A-196. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24699649;Dbxref=PMID:24699649 O95863 UniProtKB Mutagenesis 191 191 . . . Note=Mildly reduces binding to KPNB1. Does not affect binding to KPNA2%2C IPO7 or TNPO1. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19386897;Dbxref=PMID:19386897 O95863 UniProtKB Mutagenesis 193 193 . . . Note=Mildly reduces binding to KPNB1 and nuclear import. Strongly reduces binding to KPNB1 and nuclear import%3B when associated with E-191. Loss of binding to KPNB1 and nuclear import%3B when associated with E-191 and A-196. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24699649;Dbxref=PMID:24699649 O95863 UniProtKB Mutagenesis 196 196 . . . Note=Loss of binding to KPNB1 and nuclear import%3B when associated with E-191 and A-193. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24699649;Dbxref=PMID:24699649 O95863 UniProtKB Mutagenesis 203 203 . . . Note=Abolishes LATS2 phosphorylation. Does not affect binding to LATS2. Reduces protein stability. Equally distributed between nucleus and cytoplasm. Increases capacity to associate with nuclear pore importins. Unable to accumulate in the nucleus. Does not abrogate function. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21952048;Dbxref=PMID:21952048 O95863 UniProtKB Mutagenesis 203 203 . . . Note=Exclusively localizes to the cytoplasm. Reduces capacity to associate with nuclear pore importins. Unable to enter the nucleus. Does not abrogate function. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21952048;Dbxref=PMID:21952048 O95863 UniProtKB Mutagenesis 210 210 . . . Note=Impairs binding to KPNB1%2C IPO7 and TNPO1 and abolishes binding to KPNA2. Localizes to cytoplasm and nucleus. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19386897;Dbxref=PMID:19386897 O95863 UniProtKB Mutagenesis 215 215 . . . Note=Impairs binding to KPNB1%2C KPNA2%2C IPO7 and TNPO1. No change in subcellular localization. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19386897;Dbxref=PMID:19386897 O95863 UniProtKB Mutagenesis 220 220 . . . Note=Does not affect binding to KPNB1%2C KPNA2%2C IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1%2C KPNA2%2C IPO7 and TNPO1%3B when associated with E-222 and E-224. Impairs binding to KPNB1%2C KPNA2%2C IPO7 and TNPO1 and abolishes nuclear localization%2C DNA binding and repressor activity on E-cadherin/CDH1 promoter%3B when associated with E-224. Abolishes binding to KPNB1%2C KPNA2%2C IPO7 and TNPO1 and nuclear localization%3B when associated with E-161 and/or E-187. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19386897;Dbxref=PMID:19386897 O95863 UniProtKB Mutagenesis 222 222 . . . Note=Does not affect binding to KPNB1%2C KPNA2%2C IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1%2C KPNA2%2C IPO7 and TNPO1%3B when associated with E-220 and E-224. N->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19386897;Dbxref=PMID:19386897 O95863 UniProtKB Mutagenesis 224 224 . . . Note=Does not affect binding to KPNB1%2C KPNA2%2C IPO7 or TNPO1. No change in subcellular localization. Impairs binding to KPNB1%2C KPNA2%2C IPO7 and TNPO1%3B when associated with E-220 and E-222. Impairs binding to KPNB1%2C KPNA2%2C IPO7 and TNPO1 and abolishes nuclear localization%2C DNA binding and repressor activity on E-cadherin/CDH1 promoter%3B when associated with E-220. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19386897;Dbxref=PMID:19386897 O95863 UniProtKB Mutagenesis 224 224 . . . Note=Mildly reduces binding to KPNB1 and nuclear import. Strongly reduces binding to KPNB1 and nuclear import%3B when associated with A-228. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24699649;Dbxref=PMID:24699649 O95863 UniProtKB Mutagenesis 228 228 . . . Note=Very minor effect on binding to KPNB1 and nuclear import. Strongly reduces binding to KPNB1 and nuclear import%3B when associated with E-224. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24699649;Dbxref=PMID:24699649 O95863 UniProtKB Mutagenesis 232 235 . . . Note=Does not affect binding to KPNB1%2C KPNA2%2C IPO7 or TNPO1. DVKK->KVEE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19386897;Dbxref=PMID:19386897 O95863 UniProtKB Mutagenesis 238 238 . . . Note=Impairs binding to KPNB1 and IPO7 and abolishes binding to KPNA2 and TNPO1 and nuclear localization. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19386897;Dbxref=PMID:19386897 O95863 UniProtKB Mutagenesis 239 239 . . . Note=Does not affect binding to KPNB1%2C KPNA2%2C IPO7%2C TNPO1 or DNA. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19386897;Dbxref=PMID:19386897 O95863 UniProtKB Mutagenesis 246 246 . . . Note=Decreases repression activity on E-cadherin/CDH1%2C occludin and aromatase promoters. Preferentially localizes to the cytoplasm. Abolishes phosphorylation by PAK1. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15833848;Dbxref=PMID:15833848 O95863 UniProtKB Mutagenesis 247 247 . . . Note=Mildly reduces binding to KPNB1 and nuclear import. R->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24699649;Dbxref=PMID:24699649 O95863 UniProtKB Sequence conflict 46 46 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 O95863 UniProtKB Sequence conflict 154 154 . . . Note=F->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 O95863 UniProtKB Helix 3 5 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2Y48 O95863 UniProtKB Turn 157 159 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3W5K O95863 UniProtKB Beta strand 163 165 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3W5K O95863 UniProtKB Helix 166 173 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3W5K O95863 UniProtKB Helix 174 176 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3W5K O95863 UniProtKB Beta strand 183 185 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3W5K O95863 UniProtKB Beta strand 188 191 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3W5K O95863 UniProtKB Helix 192 200 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3W5K O95863 UniProtKB Turn 211 213 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3W5K O95863 UniProtKB Beta strand 216 219 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3W5K O95863 UniProtKB Helix 220 227 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3W5K O95863 UniProtKB Turn 239 241 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3W5K O95863 UniProtKB Beta strand 244 247 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3W5K O95863 UniProtKB Helix 248 256 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3W5K