##gff-version 3 P20263 UniProtKB Chain 1 352 . . . ID=PRO_0000100749;Note=POU domain%2C class 5%2C transcription factor 1 P20263 UniProtKB Domain 131 205 . . . Note=POU-specific;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00530 P20263 UniProtKB DNA binding 223 282 . . . Note=Homeobox;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00108,ECO:0000269|PubMed:23376973;Dbxref=PMID:23376973 P20263 UniProtKB Region 1 48 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P20263 UniProtKB Region 91 115 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P20263 UniProtKB Region 173 179 . . . Note=DNA-binding;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:23376973,ECO:0007744|PDB:3L1P;Dbxref=PMID:23376973 P20263 UniProtKB Region 186 189 . . . Note=DNA-binding;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:23376973,ECO:0007744|PDB:3L1P;Dbxref=PMID:23376973 P20263 UniProtKB Motif 4 12 . . . Note=9aaTAD;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01860 P20263 UniProtKB Compositional bias 94 109 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P20263 UniProtKB Binding site 150 150 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:23376973,ECO:0007744|PDB:3L1P;Dbxref=PMID:23376973 P20263 UniProtKB Binding site 157 157 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:23376973,ECO:0007744|PDB:3L1P;Dbxref=PMID:23376973 P20263 UniProtKB Modified residue 106 106 . . . Note=Phosphoserine%3B by MAPK;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01860 P20263 UniProtKB Modified residue 228 228 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01860 P20263 UniProtKB Modified residue 229 229 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01860 P20263 UniProtKB Modified residue 282 282 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q01860 P20263 UniProtKB Modified residue 347 347 . . . Note=Phosphoserine%3B by MAPK8 and MAPK9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29153991;Dbxref=PMID:29153991 P20263 UniProtKB Cross-link 118 118 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17097055,ECO:0000269|PubMed:17496161,ECO:0000269|PubMed:17525163;Dbxref=PMID:17097055,PMID:17496161,PMID:17525163 P20263 UniProtKB Mutagenesis 118 118 . . . Note=Absence of sumoylation. Enhanced protein degradation. Reduced self-renewal ability in ES cells. 70%25 lower expression of YES1. Reduced DNA binding. No change in nuclear location. No change in nuclear localization. Absence of sumoylation%3B when associated with R-215 and R-244. K->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17097055,ECO:0000269|PubMed:17496161,ECO:0000269|PubMed:17525163;Dbxref=PMID:17097055,PMID:17496161,PMID:17525163 P20263 UniProtKB Mutagenesis 120 120 . . . Note=Absence of sumoylation. Enhanced protein degradation. Reduced self-renewal ability in ES cells. 55%25 lower expression of YES1. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17496161;Dbxref=PMID:17496161 P20263 UniProtKB Mutagenesis 122 352 . . . Note=Loss of MAPK9 binding. Absence of Ser-347 phosphorylation. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29153991;Dbxref=PMID:29153991 P20263 UniProtKB Mutagenesis 166 166 . . . Note=No change in DNA binding. No loss of self-renewal ability in iPS cells. No change in nuclear location. V->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23376973;Dbxref=PMID:23376973 P20263 UniProtKB Mutagenesis 206 222 . . . Note=Reduced DNA binding. Loss of self-renewal ability in iPS cells. No change in nuclear location. NNENLQEICKSETLVQA->SSSGSPTNLDKIAAQGR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23376973;Dbxref=PMID:23376973 P20263 UniProtKB Mutagenesis 206 210 . . . Note=Loss of self-renewal ability in iPS cells. NNENL->AAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23376973;Dbxref=PMID:23376973 P20263 UniProtKB Mutagenesis 206 206 . . . Note=No change in DNA binding. Reduced self-renewal ability in iPS cells. No change in nuclear location. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23376973;Dbxref=PMID:23376973 P20263 UniProtKB Mutagenesis 207 207 . . . Note=No change in DNA binding. No change in nuclear location. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23376973;Dbxref=PMID:23376973 P20263 UniProtKB Mutagenesis 208 208 . . . Note=No change in DNA binding. No loss of self-renewal ability in iPS cells. No change in nuclear location. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23376973;Dbxref=PMID:23376973 P20263 UniProtKB Mutagenesis 209 209 . . . Note=No change in DNA binding. Reduced self-renewal ability in iPS cells. No change in nuclear location. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23376973;Dbxref=PMID:23376973 P20263 UniProtKB Mutagenesis 210 210 . . . Note=No change in DNA binding. Loss of self-renewal ability in iPS cells. No change in nuclear location. No loss of ability to bind SOX2. Reduced levels of CHD4 and SMARCA4 in a POU5F1 pulldown assay. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23376973;Dbxref=PMID:23376973 P20263 UniProtKB Mutagenesis 211 211 . . . Note=No change in DNA binding. No loss of self-renewal ability in iPS cells. No change in nuclear location. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23376973;Dbxref=PMID:23376973 P20263 UniProtKB Mutagenesis 211 211 . . . Note=No change in DNA binding. Loss of self-renewal ability in iPS cells. No change in nuclear location. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23376973;Dbxref=PMID:23376973 P20263 UniProtKB Mutagenesis 212 212 . . . Note=No change in DNA binding. No loss of self-renewal ability in iPS cells. No change in nuclear location. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23376973;Dbxref=PMID:23376973 P20263 UniProtKB Mutagenesis 215 215 . . . Note=No change in sumoylation%3B when associated with R-244. Loss of sumoylation. No change in nuclear localization%3B when associated with R-118 and R-244. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17496161;Dbxref=PMID:17496161 P20263 UniProtKB Mutagenesis 244 244 . . . Note=No change in sumoylation. No change in sumoylation%3B when associated with R-215. Loss of sumoylation%3B when associated with R-118 and R-215. No change in nuclear localization%3B when associated with R-118 and R-215. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17496161;Dbxref=PMID:17496161 P20263 UniProtKB Mutagenesis 347 347 . . . Note=Absence of phosphorylation. Reduced protein degradation. Reduced self-renewal ability in ES cells. No change in FBXW4 binding. Loss of FBXW8 binding. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29153991;Dbxref=PMID:29153991 P20263 UniProtKB Sequence conflict 1 28 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P20263 UniProtKB Sequence conflict 29 29 . . . Note=V->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 P20263 UniProtKB Sequence conflict 31 31 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 P20263 UniProtKB Helix 132 152 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L1P P20263 UniProtKB Helix 157 168 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L1P P20263 UniProtKB Helix 174 181 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L1P P20263 UniProtKB Helix 187 204 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L1P P20263 UniProtKB Helix 208 212 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L1P P20263 UniProtKB Beta strand 223 225 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1OCP P20263 UniProtKB Helix 232 239 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L1P P20263 UniProtKB Turn 240 244 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L1P P20263 UniProtKB Helix 250 259 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L1P P20263 UniProtKB Helix 264 279 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3L1P