##gff-version 3 P25293 UniProtKB Chain 1 417 . . . ID=PRO_0000185659;Note=Nucleosome assembly protein P25293 UniProtKB DNA binding 330 356 . . . Note=H-T-H motif;Ontology_term=ECO:0000255;evidence=ECO:0000255 P25293 UniProtKB Region 1 47 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P25293 UniProtKB Region 143 362 . . . Note=Interaction with NBA1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 P25293 UniProtKB Region 364 417 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P25293 UniProtKB Compositional bias 1 43 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P25293 UniProtKB Compositional bias 365 400 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P25293 UniProtKB Modified residue 20 20 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17330950,ECO:0007744|PubMed:18407956,ECO:0007744|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 P25293 UniProtKB Modified residue 24 24 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17330950,ECO:0007744|PubMed:18407956,ECO:0007744|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 P25293 UniProtKB Modified residue 27 27 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17330950,ECO:0007744|PubMed:18407956,ECO:0007744|PubMed:19779198;Dbxref=PMID:17330950,PMID:18407956,PMID:19779198 P25293 UniProtKB Modified residue 53 53 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19779198;Dbxref=PMID:19779198 P25293 UniProtKB Modified residue 69 69 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19779198;Dbxref=PMID:19779198 P25293 UniProtKB Modified residue 76 76 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:15665377,ECO:0007744|PubMed:17330950,ECO:0007744|PubMed:18407956,ECO:0007744|PubMed:19779198;Dbxref=PMID:15665377,PMID:17330950,PMID:18407956,PMID:19779198 P25293 UniProtKB Modified residue 82 82 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:18086883,ECO:0007744|PubMed:19779198;Dbxref=PMID:18086883,PMID:19779198 P25293 UniProtKB Modified residue 98 98 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 P25293 UniProtKB Modified residue 104 104 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 P25293 UniProtKB Modified residue 140 140 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:18086883,ECO:0007744|PubMed:18407956;Dbxref=PMID:18086883,PMID:18407956 P25293 UniProtKB Modified residue 159 159 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 P25293 UniProtKB Modified residue 177 177 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:18086883,ECO:0007744|PubMed:17330950,ECO:0007744|PubMed:18407956,ECO:0007744|PubMed:19779198;Dbxref=PMID:17330950,PMID:18086883,PMID:18407956,PMID:19779198 P25293 UniProtKB Modified residue 397 397 . . . Note=Phosphoserine%3B by CK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 P25293 UniProtKB Cross-link 50 50 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22106047;Dbxref=PMID:22106047 P25293 UniProtKB Mutagenesis 99 99 . . . Note=Predominantly cytoplasmic%3B when associated with A-159%2C A-177 and S-397. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 P25293 UniProtKB Mutagenesis 159 159 . . . Note=Significant reduction in phosphorylation%3B when associated with A-397. Complete inhibition of phosphorylation%3B when associated with A-177 and A-397. Leads to a prolonged S phase and a shortened passage through G1%3B when associated with A-177 and A-397. Predominantly cytoplasmic%3B when associated with S-99%2C A-177 and A-397. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 P25293 UniProtKB Mutagenesis 159 159 . . . Note=Leads to a prolonged S phase and a shortened passage through G1%3B when associated with A-177 and A-397. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 P25293 UniProtKB Mutagenesis 177 177 . . . Note=Significant reduction in phosphorylation%3B when associated with A-397. Complete inhibition of phosphorylation%3B when associated with A-159 and A-397. Leads to a prolonged S phase and a shortened passage through G1%3B when associated with A-159 and A-397. Predominantly cytoplasmic%3B when associated with S-99%2C A-159 and A-397. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 P25293 UniProtKB Mutagenesis 177 177 . . . Note=Leads to a prolonged S phase and a shortened passage through G1%3B when associated with A-159 and A-397. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 P25293 UniProtKB Mutagenesis 397 397 . . . Note=Significant reduction in phosphorylation%3B when associated with either A-159 or A-177. Complete inhibition of phosphorylation%3B when associated with A-159 and A-177. Leads to a prolonged S phase and a shortened passage through G1%3B when associated with A-159 and A-177. Predominantly cytoplasmic%3B when associated with S-99%3B A-159 and A-177. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 P25293 UniProtKB Mutagenesis 397 397 . . . Note=Leads to a prolonged S phase and a shortened passage through G1%3B when associated with A-159 and A-177. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18086883;Dbxref=PMID:18086883 P25293 UniProtKB Sequence conflict 2 2 . . . Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 P25293 UniProtKB Sequence conflict 103 104 . . . Note=QS->LC;Ontology_term=ECO:0000305;evidence=ECO:0000305 P25293 UniProtKB Sequence conflict 137 138 . . . Note=RI->TM;Ontology_term=ECO:0000305;evidence=ECO:0000305 P25293 UniProtKB Sequence conflict 384 384 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 P25293 UniProtKB Turn 73 75 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Helix 77 87 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Helix 90 140 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Beta strand 141 143 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Helix 147 159 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Helix 163 165 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Helix 188 194 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Helix 199 201 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Helix 205 208 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Helix 210 213 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Beta strand 214 218 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Beta strand 224 226 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Beta strand 228 235 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Turn 237 239 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Beta strand 241 243 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Beta strand 246 257 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Beta strand 260 263 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Beta strand 265 271 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Turn 279 281 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Beta strand 285 289 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Turn 295 297 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2Z2R P25293 UniProtKB Beta strand 304 308 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Helix 312 316 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Beta strand 327 329 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Helix 332 350 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Turn 351 355 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Helix 356 361 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU P25293 UniProtKB Helix 363 369 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2AYU