##gff-version 3 P22893 UniProtKB Chain 1 319 . . . ID=PRO_0000089164;Note=MRNA decay activator protein ZFP36 P22893 UniProtKB Repeat 63 67 . . . Note=P-P-P-P-G P22893 UniProtKB Repeat 190 194 . . . Note=P-P-P-P-G P22893 UniProtKB Repeat 211 215 . . . Note=P-P-P-P-G P22893 UniProtKB Zinc finger 95 123 . . . Note=C3H1-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 P22893 UniProtKB Zinc finger 133 161 . . . Note=C3H1-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 P22893 UniProtKB Region 1 166 . . . Note=Necessary for localization of ARE-containing mRNAs to processing bodies (PBs);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26651 P22893 UniProtKB Region 1 92 . . . Note=Necessary and sufficient for the association with mRNA decay enzymes and mRNA decay activation;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26651 P22893 UniProtKB Region 1 15 . . . Note=Necessary for nuclear export;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47973 P22893 UniProtKB Region 65 95 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P22893 UniProtKB Region 87 160 . . . Note=Necessary for nuclear localization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47973 P22893 UniProtKB Region 89 165 . . . Note=Necessary for RNA-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26651 P22893 UniProtKB Region 92 319 . . . Note=Necessary for localization of ARE-containing mRNAs to processing bodies (PBs);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26651 P22893 UniProtKB Region 95 186 . . . Note=Necessary for interaction with PABPN1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22844456;Dbxref=PMID:22844456 P22893 UniProtKB Region 166 319 . . . Note=Necessary for mRNA decay activation;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26651 P22893 UniProtKB Region 179 309 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P22893 UniProtKB Region 305 319 . . . Note=Interaction with CNOT1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26651 P22893 UniProtKB Compositional bias 65 84 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P22893 UniProtKB Compositional bias 273 287 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P22893 UniProtKB Modified residue 52 52 . . . Note=Phosphoserine%3B by MAPKAPK2;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14688255,ECO:0000269|PubMed:15014438,ECO:0000269|PubMed:20595389;Dbxref=PMID:14688255,PMID:15014438,PMID:20595389 P22893 UniProtKB Modified residue 58 58 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26651 P22893 UniProtKB Modified residue 80 80 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14688255;Dbxref=PMID:14688255 P22893 UniProtKB Modified residue 82 82 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14688255;Dbxref=PMID:14688255 P22893 UniProtKB Modified residue 84 84 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26651 P22893 UniProtKB Modified residue 85 85 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14688255;Dbxref=PMID:14688255 P22893 UniProtKB Modified residue 178 178 . . . Note=Phosphoserine%3B by MAPKAPK2;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14688255,ECO:0000269|PubMed:15014438,ECO:0000269|PubMed:20595389;Dbxref=PMID:14688255,PMID:15014438,PMID:20595389 P22893 UniProtKB Modified residue 189 189 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26651 P22893 UniProtKB Modified residue 210 210 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26651 P22893 UniProtKB Modified residue 220 220 . . . Note=Phosphoserine%3B by MAPK1%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7768935;Dbxref=PMID:7768935 P22893 UniProtKB Modified residue 250 250 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14688255;Dbxref=PMID:14688255 P22893 UniProtKB Modified residue 269 269 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26651 P22893 UniProtKB Modified residue 289 289 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P26651 P22893 UniProtKB Modified residue 316 316 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14688255;Dbxref=PMID:14688255 P22893 UniProtKB Mutagenesis 52 52 . . . Note=Impairs phosphorylation by MAPKAPK2%2C decreases its stability and cytoplasmic localization%2C increases interaction with PPP2CA%2C inhibits binding to 14-3-3 proteins%2C but does not impair binding to ARE-containing transcripts%2C recruitment of mRNA decay factors and ZFP36-mediated deadenylation and decay of ARE-containing transcripts%3B when associated with A-178. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15014438,ECO:0000269|PubMed:16508014,ECO:0000269|PubMed:16508015,ECO:0000269|PubMed:17170118,ECO:0000269|PubMed:20595389,ECO:0000269|PubMed:21078877;Dbxref=PMID:15014438,PMID:16508014,PMID:16508015,PMID:17170118,PMID:20595389,PMID:21078877 P22893 UniProtKB Mutagenesis 64 66 . . . Note=Abolished interaction with GIGYF2 and impaired TTP-mediated mRNA repression%3B when associated with 191-S--S-193. PPP->SSS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26763119;Dbxref=PMID:26763119 P22893 UniProtKB Mutagenesis 178 178 . . . Note=Reduces both interaction with 14-3-3 proteins and YWHAB-induced cytoplasmic localization. Impairs phosphorylation by MAPKAPK2%2C decreases its stability and cytoplasmic localization%2C increases interaction with PPP2CA%2C inhibits binding to 14-3-3 proteins%2C but does not impair binding to ARE-containing transcripts%2C recruitment of mRNA decay factors and ZFP36-mediated deadenylation and decay of ARE-containing transcripts%3B when associated with A-52. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11886850,ECO:0000269|PubMed:15014438,ECO:0000269|PubMed:16508014,ECO:0000269|PubMed:16508015,ECO:0000269|PubMed:17170118,ECO:0000269|PubMed:20595389,ECO:0000269|PubMed:21078877;Dbxref=PMID:11886850,PMID:15014438,PMID:16508014,PMID:16508015,PMID:17170118,PMID:20595389,PMID:21078877 P22893 UniProtKB Mutagenesis 191 193 . . . Note=Abolished interaction with GIGYF2 and impaired TTP-mediated mRNA repression%3B when associated with 64-S--S-66. PPP->SSS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26763119;Dbxref=PMID:26763119 P22893 UniProtKB Mutagenesis 212 214 . . . Note=Does not affect interaction with GIGYF2. PPP->SSS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26763119;Dbxref=PMID:26763119 P22893 UniProtKB Mutagenesis 303 303 . . . Note=Stimulates interaction with SH3KBP1. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20221403;Dbxref=PMID:20221403 P22893 UniProtKB Helix 103 106 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1M9O P22893 UniProtKB Turn 111 115 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1M9O P22893 UniProtKB Beta strand 120 122 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1M9O P22893 UniProtKB Helix 125 127 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1M9O