##gff-version 3 Q53ET0 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:22814378;Dbxref=PMID:19413330,PMID:22814378 Q53ET0 UniProtKB Chain 2 693 . . . ID=PRO_0000318528;Note=CREB-regulated transcription coactivator 2 Q53ET0 UniProtKB Region 1 30 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q53ET0 UniProtKB Region 282 306 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q53ET0 UniProtKB Region 328 554 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q53ET0 UniProtKB Motif 271 287 . . . Note=Nuclear export signal;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q53ET0 UniProtKB Compositional bias 1 24 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q53ET0 UniProtKB Compositional bias 338 414 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q53ET0 UniProtKB Compositional bias 447 486 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q53ET0 UniProtKB Compositional bias 493 527 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q53ET0 UniProtKB Site 629 629 . . . Note=Required for ubiquitination and degradation;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q53ET0 UniProtKB Modified residue 2 2 . . . Note=N-acetylalanine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:22814378;Dbxref=PMID:19413330,PMID:22814378 Q53ET0 UniProtKB Modified residue 51 51 . . . Note=Asymmetric dimethylarginine%3B by PRMT6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q3U182 Q53ET0 UniProtKB Modified residue 70 70 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:15454081,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332;Dbxref=PMID:15454081,PMID:18669648,PMID:19690332 Q53ET0 UniProtKB Modified residue 86 86 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332;Dbxref=PMID:18669648,PMID:19690332 Q53ET0 UniProtKB Modified residue 90 90 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:15454081,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:24275569;Dbxref=PMID:15454081,PMID:18669648,PMID:19690332,PMID:24275569 Q53ET0 UniProtKB Modified residue 99 99 . . . Note=Asymmetric dimethylarginine%3B by PRMT6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q3U182 Q53ET0 UniProtKB Modified residue 120 120 . . . Note=Asymmetric dimethylarginine%3B by PRMT6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q3U182 Q53ET0 UniProtKB Modified residue 123 123 . . . Note=Asymmetric dimethylarginine%3B by PRMT6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q3U182 Q53ET0 UniProtKB Modified residue 136 136 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:15454081,ECO:0007744|PubMed:18669648;Dbxref=PMID:15454081,PMID:18669648 Q53ET0 UniProtKB Modified residue 161 161 . . . Note=Asymmetric dimethylarginine%3B by PRMT6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q3U182 Q53ET0 UniProtKB Modified residue 168 168 . . . Note=Asymmetric dimethylarginine%3B by PRMT6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q3U182 Q53ET0 UniProtKB Modified residue 169 169 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q3U182 Q53ET0 UniProtKB Modified residue 171 171 . . . Note=Phosphoserine%3B by AMPK%2C MARK2%2C SIK1 and SIK2;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15454081,ECO:0000269|PubMed:16817901,ECO:0000269|PubMed:17210223,ECO:0000269|PubMed:18626018;Dbxref=PMID:15454081,PMID:16817901,PMID:17210223,PMID:18626018 Q53ET0 UniProtKB Modified residue 192 192 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19690332;Dbxref=PMID:19690332 Q53ET0 UniProtKB Modified residue 274 274 . . . Note=Phosphoserine%3B by MARK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18626018;Dbxref=PMID:18626018 Q53ET0 UniProtKB Modified residue 306 306 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15454081;Dbxref=PMID:15454081 Q53ET0 UniProtKB Modified residue 368 368 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15454081;Dbxref=PMID:15454081 Q53ET0 UniProtKB Modified residue 393 393 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15454081;Dbxref=PMID:15454081 Q53ET0 UniProtKB Modified residue 433 433 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:15454081,ECO:0007744|PubMed:16964243,ECO:0007744|PubMed:18220336,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:23186163;Dbxref=PMID:15454081,PMID:16964243,PMID:18220336,PMID:18669648,PMID:19690332,PMID:23186163 Q53ET0 UniProtKB Modified residue 456 456 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15454081;Dbxref=PMID:15454081 Q53ET0 UniProtKB Modified residue 488 488 . . . Note=Phosphotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19690332;Dbxref=PMID:19690332 Q53ET0 UniProtKB Modified residue 489 489 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15454081;Dbxref=PMID:15454081 Q53ET0 UniProtKB Modified residue 490 490 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19690332;Dbxref=PMID:19690332 Q53ET0 UniProtKB Modified residue 492 492 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15454081;Dbxref=PMID:15454081 Q53ET0 UniProtKB Modified residue 501 501 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231;Dbxref=PMID:18669648,PMID:20068231 Q53ET0 UniProtKB Modified residue 613 613 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:15454081,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:15454081,PMID:18669648,PMID:19690332,PMID:20068231,PMID:23186163,PMID:24275569 Q53ET0 UniProtKB Modified residue 623 623 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q3U182 Q53ET0 UniProtKB Modified residue 624 624 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:19690332,PMID:20068231,PMID:23186163 Q53ET0 UniProtKB Cross-link 234 234 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q53ET0 UniProtKB Natural variant 147 147 . . . ID=VAR_038756;Note=M->V;Dbxref=dbSNP:rs11264680 Q53ET0 UniProtKB Natural variant 379 379 . . . ID=VAR_038757;Note=R->C;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14506290,ECO:0000269|PubMed:17950019;Dbxref=dbSNP:rs150423770,PMID:14506290,PMID:17950019 Q53ET0 UniProtKB Mutagenesis 70 70 . . . Note=No effect on cAMP- and calcium-regulated phosphorylation. S->A Q53ET0 UniProtKB Mutagenesis 171 171 . . . Note=Loss of cAMP- and calcium-regulated phosphorylation. Greatly reduced interaction with 14-3-3 proteins. Impaired phosphorylation under low glucose conditions and impaired interaction with 14-3-3 proteins%3B when associated with A-274. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15454081,ECO:0000269|PubMed:16817901,ECO:0000269|PubMed:18626018;Dbxref=PMID:15454081,PMID:16817901,PMID:18626018 Q53ET0 UniProtKB Mutagenesis 274 274 . . . Note=Impaired phosphorylation under low glucose conditions and impaired interaction with 14-3-3 proteins%3B when associated with A-171. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18626018;Dbxref=PMID:18626018 Q53ET0 UniProtKB Mutagenesis 368 368 . . . Note=Reduced cAMP- and calcium-regulated phosphorylation. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15454081,ECO:0000269|PubMed:18626018;Dbxref=PMID:15454081,PMID:18626018 Q53ET0 UniProtKB Mutagenesis 393 393 . . . Note=No effect on cAMP- and calcium-regulated phosphorylation. S->A Q53ET0 UniProtKB Sequence conflict 323 325 . . . Note=MGL->HGP;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q53ET0 UniProtKB Sequence conflict 499 499 . . . Note=P->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q53ET0 UniProtKB Helix 21 45 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HTM