##gff-version 3 P28033 UniProtKB Chain 1 296 . . . ID=PRO_0000076618;Note=CCAAT/enhancer-binding protein beta P28033 UniProtKB Domain 222 285 . . . Note=BZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 P28033 UniProtKB Region 1 22 . . . Note=Required for Lys-133 sumoylation;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P17676 P28033 UniProtKB Region 22 104 . . . Note=Required for MYC transcriptional repression;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16585579;Dbxref=PMID:16585579 P28033 UniProtKB Region 171 199 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P28033 UniProtKB Region 226 246 . . . Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 P28033 UniProtKB Region 248 255 . . . Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 P28033 UniProtKB Compositional bias 171 189 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P28033 UniProtKB Modified residue 3 3 . . . Note=Asymmetric dimethylarginine%3B by CARM1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20111005;Dbxref=PMID:20111005 P28033 UniProtKB Modified residue 39 39 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18486321;Dbxref=PMID:18486321 P28033 UniProtKB Modified residue 39 39 . . . Note=N6-methylated lysine%3B alternate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:18647749;Dbxref=PMID:18647749 P28033 UniProtKB Modified residue 98 98 . . . Note=N6-acetyllysine%3B by KAT2A and KAT2B;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:17301242;Dbxref=PMID:17301242 P28033 UniProtKB Modified residue 101 101 . . . Note=N6-acetyllysine%3B by KAT2A and KAT2B;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:17301242;Dbxref=PMID:17301242 P28033 UniProtKB Modified residue 102 102 . . . Note=N6-acetyllysine%3B by KAT2A and KAT2B%3B alternate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:17301242;Dbxref=PMID:17301242 P28033 UniProtKB Modified residue 179 179 . . . Note=Phosphothreonine%3B by GSK3-beta;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15985551,ECO:0000269|PubMed:17601773,ECO:0000269|PubMed:19478079;Dbxref=PMID:15985551,PMID:17601773,PMID:19478079 P28033 UniProtKB Modified residue 184 184 . . . Note=Phosphoserine%3B by GSK3-beta;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:15985551,ECO:0000269|PubMed:17601773,ECO:0000269|PubMed:19478079,ECO:0007744|PubMed:21183079;Dbxref=PMID:15985551,PMID:17601773,PMID:19478079,PMID:21183079 P28033 UniProtKB Modified residue 188 188 . . . Note=Phosphothreonine%3B by RPS6KA1%2C CDK2 and MAPK;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:15985551,ECO:0000269|PubMed:17601773,ECO:0000269|PubMed:19324970,ECO:0000269|PubMed:19478079,ECO:0007744|PubMed:21183079;Dbxref=PMID:15985551,PMID:17601773,PMID:19324970,PMID:19478079,PMID:21183079 P28033 UniProtKB Modified residue 217 217 . . . Note=Phosphothreonine%3B by RPS6KA1 and PKC/PRKCA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10635333;Dbxref=PMID:10635333 P28033 UniProtKB Modified residue 239 239 . . . Note=Phosphoserine%3B by PKC/PRKCA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P17676 P28033 UniProtKB Modified residue 276 276 . . . Note=Phosphoserine%3B by CaMK2;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:1314426;Dbxref=PMID:1314426 P28033 UniProtKB Glycosylation 180 180 . . . Note=O-linked (GlcNAc) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19478079;Dbxref=PMID:19478079 P28033 UniProtKB Glycosylation 181 181 . . . Note=O-linked (GlcNAc) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19478079;Dbxref=PMID:19478079 P28033 UniProtKB Cross-link 102 102 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P17676 P28033 UniProtKB Cross-link 133 133 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16585579,ECO:0000269|PubMed:20194620,ECO:0000269|PubMed:24061474;Dbxref=PMID:16585579,PMID:20194620,PMID:24061474 P28033 UniProtKB Cross-link 133 133 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P17676 P28033 UniProtKB Cross-link 144 144 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P17676 P28033 UniProtKB Cross-link 211 211 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P17676 P28033 UniProtKB Cross-link 213 213 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P17676 P28033 UniProtKB Cross-link 283 283 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P17676 P28033 UniProtKB Alternative sequence 1 151 . . . ID=VSP_053976;Note=In isoform 3. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P28033 UniProtKB Alternative sequence 1 21 . . . ID=VSP_053977;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P28033 UniProtKB Mutagenesis 39 39 . . . Note=No effect on interaction with EP300. K->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18486321;Dbxref=PMID:18486321 P28033 UniProtKB Mutagenesis 39 39 . . . Note=Dominant negative. Loss of transactivation activity. No effect on interaction with EP300. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18486321;Dbxref=PMID:18486321 P28033 UniProtKB Mutagenesis 98 98 . . . Note=No effect on transactivation activity. Not acetylated after glucocorticoid-stimulation and no increase of transactivation activity%3B when associated with R-101 and R-102. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17301242,ECO:0000269|PubMed:18486321;Dbxref=PMID:17301242,PMID:18486321 P28033 UniProtKB Mutagenesis 101 101 . . . Note=Not acetylated after glucocorticoid-stimulation and no increase of transactivation activity%3B when associated with R-98 and R-102. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17301242;Dbxref=PMID:17301242 P28033 UniProtKB Mutagenesis 102 102 . . . Note=Not acetylated and no increase of transactivation activity after glucocorticoid-stimulation%3B when associated with R-98 and R-101. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17301242;Dbxref=PMID:17301242 P28033 UniProtKB Mutagenesis 133 133 . . . Note=Not sumoylated. Decreases ubiquitination and increases stability. Loss of proliferation inhibition in T cells. No effect on transactivation activity. K->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16585579,ECO:0000269|PubMed:20194620,ECO:0000269|PubMed:24061474;Dbxref=PMID:16585579,PMID:20194620,PMID:24061474 P28033 UniProtKB Mutagenesis 135 135 . . . Note=Not sumoylated and not ubiquitinated. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20194620;Dbxref=PMID:20194620 P28033 UniProtKB Mutagenesis 179 179 . . . Note=Disruption of phosphorylation by MAPK and GSK3B%2C acquisition of DNA-binding activity and transactivation function%3B when associated with A-184 and A-188. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15985551;Dbxref=PMID:15985551 P28033 UniProtKB Mutagenesis 180 180 . . . Note=Highly increases transactivation activity%3B when associated with A-181. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19478079;Dbxref=PMID:19478079 P28033 UniProtKB Mutagenesis 181 181 . . . Note=Highly increases transactivation activity%3B when associated with A-180. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19478079;Dbxref=PMID:19478079 P28033 UniProtKB Mutagenesis 184 184 . . . Note=Disruption of phosphorylation by MAPK and GSK3B%2C acquisition of DNA-binding activity and transactivation function%3B when associated with A-179 and A-188. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15985551;Dbxref=PMID:15985551 P28033 UniProtKB Mutagenesis 188 188 . . . Note=Disruption of phosphorylation by MAPK and GSK3B%2C acquisition of DNA-binding activity and transactivation function%3B when associated with A-179 and A-184. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15985551;Dbxref=PMID:15985551 P28033 UniProtKB Mutagenesis 215 215 . . . Note=No effect on transactivation activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18486321;Dbxref=PMID:18486321 P28033 UniProtKB Mutagenesis 217 217 . . . Note=Loss of hepatocyte proliferation induction by TGFA. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10635333;Dbxref=PMID:10635333 P28033 UniProtKB Mutagenesis 217 217 . . . Note=Induces hepatocyte proliferation. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10635333;Dbxref=PMID:10635333 P28033 UniProtKB Mutagenesis 276 276 . . . Note=Reduces phosphorylation in response to calcium. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1314426;Dbxref=PMID:1314426 P28033 UniProtKB Helix 240 282 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1CI6