##gff-version 3 P05412 UniProtKB Chain 1 331 . . . ID=PRO_0000076429;Note=Transcription factor Jun P05412 UniProtKB Domain 252 315 . . . Note=BZIP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 P05412 UniProtKB Region 150 223 . . . Note=Interaction with PAGE4;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26242913;Dbxref=PMID:26242913 P05412 UniProtKB Region 252 279 . . . Note=Basic motif;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 P05412 UniProtKB Region 280 308 . . . Note=Leucine-zipper;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00978 P05412 UniProtKB Site 272 272 . . . Note=Necessary for synergistic transcriptional activity with SMAD3 P05412 UniProtKB Modified residue 2 2 . . . Note=Phosphothreonine%3B by PAK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21177766;Dbxref=PMID:21177766 P05412 UniProtKB Modified residue 8 8 . . . Note=Phosphothreonine%3B by PAK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21177766;Dbxref=PMID:21177766 P05412 UniProtKB Modified residue 56 56 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P05627 P05412 UniProtKB Modified residue 58 58 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:21406692;Dbxref=PMID:18669648,PMID:21406692 P05412 UniProtKB Modified residue 63 63 . . . Note=Phosphoserine%3B by MAPK8 and PLK3;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:14739463,ECO:0000269|PubMed:17804415,ECO:0000269|PubMed:18650425,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:14739463,PMID:17804415,PMID:18650425,PMID:18669648,PMID:19690332,PMID:20068231,PMID:21406692,PMID:23186163 P05412 UniProtKB Modified residue 73 73 . . . Note=Phosphoserine%3B by MAPK8 and PLK3;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14739463,ECO:0000269|PubMed:17804415,ECO:0000269|PubMed:18650425;Dbxref=PMID:14739463,PMID:17804415,PMID:18650425 P05412 UniProtKB Modified residue 89 89 . . . Note=Phosphothreonine%3B by PAK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21177766;Dbxref=PMID:21177766 P05412 UniProtKB Modified residue 91 91 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14739463;Dbxref=PMID:14739463 P05412 UniProtKB Modified residue 93 93 . . . Note=Phosphothreonine%3B by PAK2;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14739463,ECO:0000269|PubMed:21177766;Dbxref=PMID:14739463,PMID:21177766 P05412 UniProtKB Modified residue 239 239 . . . Note=Phosphothreonine%3B by GSK3-beta;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:1846781,ECO:0007744|PubMed:18669648;Dbxref=PMID:1846781,PMID:18669648 P05412 UniProtKB Modified residue 243 243 . . . Note=Phosphoserine%3B by DYRK2 and GSK3-beta;Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:1846781,ECO:0000269|PubMed:22307329,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:23186163;Dbxref=PMID:1846781,PMID:18669648,PMID:19690332,PMID:22307329,PMID:23186163 P05412 UniProtKB Modified residue 249 249 . . . Note=Phosphoserine%3B by GSK3-beta;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1846781,ECO:0000269|PubMed:8464713;Dbxref=PMID:1846781,PMID:8464713 P05412 UniProtKB Modified residue 271 271 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11689449;Dbxref=PMID:11689449 P05412 UniProtKB Modified residue 286 286 . . . Note=Phosphothreonine%3B by PAK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21177766;Dbxref=PMID:21177766 P05412 UniProtKB Cross-link 35 35 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 P05412 UniProtKB Cross-link 50 50 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 P05412 UniProtKB Cross-link 56 56 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 P05412 UniProtKB Cross-link 70 70 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 P05412 UniProtKB Cross-link 226 226 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 P05412 UniProtKB Natural variant 297 297 . . . ID=VAR_012070;Note=T->M;Dbxref=dbSNP:rs9989 P05412 UniProtKB Mutagenesis 2 2 . . . Note=Complete loss of PAK2-mediated phosphorylation%3B when associated with A-8%3B A-89%3B A-93%3B and A-286. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21177766;Dbxref=PMID:21177766 P05412 UniProtKB Mutagenesis 6 194 . . . Note=Abolishes activation of FASLG/CD95L transcription. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12618758;Dbxref=PMID:12618758 P05412 UniProtKB Mutagenesis 8 8 . . . Note=Complete loss of PAK2-mediated phosphorylation%3B when associated with A-2%3B A-89%3B A-93%3B and A-286. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21177766;Dbxref=PMID:21177766 P05412 UniProtKB Mutagenesis 63 63 . . . Note=Greatly reduced ATF7-mediated transcriptional activity%3B when associated with A-73. Abolishes interaction with FBXW7%3B when associated with A-73%3B A-91 and A-93. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10376527,ECO:0000269|PubMed:14739463;Dbxref=PMID:10376527,PMID:14739463 P05412 UniProtKB Mutagenesis 73 73 . . . Note=Greatly reduced ATF7-mediated transcriptional activity%3B when associated with A-63. Abolishes interaction with FBXW7%3B when associated with A-63%3B A-91 and A-93. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10376527,ECO:0000269|PubMed:14739463;Dbxref=PMID:10376527,PMID:14739463 P05412 UniProtKB Mutagenesis 89 89 . . . Note=Complete loss of PAK2-mediated phosphorylation%3B when associated with A-2%3B A-8%3B A-93%3B and A-286. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21177766;Dbxref=PMID:21177766 P05412 UniProtKB Mutagenesis 91 91 . . . Note=Abolishes interaction with FBXW7%3B when associated with A-63%3B A-73 and A-93. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14739463;Dbxref=PMID:14739463 P05412 UniProtKB Mutagenesis 93 93 . . . Note=Abolishes interaction with FBXW7%3B when associated with A-63%3B A-73 and A-91. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14739463;Dbxref=PMID:14739463 P05412 UniProtKB Mutagenesis 93 93 . . . Note=Complete loss of PAK2-mediated phosphorylation%3B when associated with A-2%3B A-8%3B A-89%3B and A-286. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21177766;Dbxref=PMID:21177766 P05412 UniProtKB Mutagenesis 243 243 . . . Note=Abolishes phosphorylation by DYRK2. Abolishes phosphorylation by GSK3B at Thr-239. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22307329;Dbxref=PMID:22307329 P05412 UniProtKB Mutagenesis 272 272 . . . Note=Abolishes the synergistic activity with SMAD3 to activate TGF-beta-mediated transcription. R->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10995748;Dbxref=PMID:10995748 P05412 UniProtKB Mutagenesis 286 286 . . . Note=Complete loss of PAK2-mediated phosphorylation%3B when associated with A-2%3B A-8%3B A-89%3B and A-93. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21177766;Dbxref=PMID:21177766 P05412 UniProtKB Sequence conflict 11 11 . . . Note=D->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 P05412 UniProtKB Sequence conflict 14 14 . . . Note=L->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 P05412 UniProtKB Sequence conflict 80 80 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 P05412 UniProtKB Sequence conflict 151 151 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 P05412 UniProtKB Helix 255 310 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5T01