##gff-version 3 P26651 UniProtKB Chain 1 326 . . . ID=PRO_0000089163;Note=MRNA decay activator protein ZFP36 P26651 UniProtKB Repeat 71 75 . . . Note=P-P-P-P-G P26651 UniProtKB Repeat 198 202 . . . Note=P-P-P-P-G P26651 UniProtKB Repeat 219 223 . . . Note=P-P-P-P-G P26651 UniProtKB Zinc finger 103 131 . . . Note=C3H1-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 P26651 UniProtKB Zinc finger 141 169 . . . Note=C3H1-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00723 P26651 UniProtKB Region 1 174 . . . Note=Necessary for localization of ARE-containing mRNAs to processing bodies (PBs);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17369404;Dbxref=PMID:17369404 P26651 UniProtKB Region 1 100 . . . Note=Necessary and sufficient for the association with mRNA decay enzymes and mRNA decay activation;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15687258;Dbxref=PMID:15687258 P26651 UniProtKB Region 1 15 . . . Note=Necessary for nuclear export;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47973 P26651 UniProtKB Region 13 66 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P26651 UniProtKB Region 78 102 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P26651 UniProtKB Region 95 168 . . . Note=Necessary for nuclear localization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47973 P26651 UniProtKB Region 97 173 . . . Note=Necessary for RNA-binding;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10751406,ECO:0000269|PubMed:12748283;Dbxref=PMID:10751406,PMID:12748283 P26651 UniProtKB Region 100 326 . . . Note=Necessary for localization of ARE-containing mRNAs to processing bodies (PBs);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17369404;Dbxref=PMID:17369404 P26651 UniProtKB Region 103 194 . . . Note=Necessary for interaction with PABPN1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22893 P26651 UniProtKB Region 174 326 . . . Note=Necessary for mRNA decay activation;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15687258;Dbxref=PMID:15687258 P26651 UniProtKB Region 175 245 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P26651 UniProtKB Region 273 292 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P26651 UniProtKB Region 312 326 . . . Note=Interaction with CNOT1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23644599;Dbxref=PMID:23644599 P26651 UniProtKB Compositional bias 27 59 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P26651 UniProtKB Modified residue 60 60 . . . Note=Phosphoserine%3B by MAPKAPK2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22893 P26651 UniProtKB Modified residue 66 66 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16262601,ECO:0000269|PubMed:20221403;Dbxref=PMID:16262601,PMID:20221403 P26651 UniProtKB Modified residue 88 88 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16262601;Dbxref=PMID:16262601 P26651 UniProtKB Modified residue 90 90 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22893 P26651 UniProtKB Modified residue 92 92 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16262601;Dbxref=PMID:16262601 P26651 UniProtKB Modified residue 93 93 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:20221403,ECO:0007744|PubMed:23186163;Dbxref=PMID:20221403,PMID:23186163 P26651 UniProtKB Modified residue 169 169 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16262601;Dbxref=PMID:16262601 P26651 UniProtKB Modified residue 186 186 . . . Note=Phosphoserine%3B by MAPKAPK2;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:16262601,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:16262601,PMID:18669648,PMID:23186163 P26651 UniProtKB Modified residue 197 197 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16262601;Dbxref=PMID:16262601 P26651 UniProtKB Modified residue 218 218 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16262601;Dbxref=PMID:16262601 P26651 UniProtKB Modified residue 228 228 . . . Note=Phosphoserine%3B by MAPK1%3B in vitro;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16262601;Dbxref=PMID:16262601 P26651 UniProtKB Modified residue 276 276 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16262601;Dbxref=PMID:16262601 P26651 UniProtKB Modified residue 296 296 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16262601;Dbxref=PMID:16262601 P26651 UniProtKB Modified residue 323 323 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P26651 UniProtKB Natural variant 37 37 . . . ID=VAR_021064;Note=P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs17878633 P26651 UniProtKB Natural variant 55 55 . . . ID=VAR_052324;Note=P->S;Dbxref=dbSNP:rs2229272 P26651 UniProtKB Natural variant 259 259 . . . ID=VAR_021065;Note=I->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs17886974 P26651 UniProtKB Natural variant 324 324 . . . ID=VAR_021066;Note=V->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.3;Dbxref=dbSNP:rs17884899 P26651 UniProtKB Mutagenesis 60 60 . . . Note=Inhibits PKM-induced ZFP36 degradation through a p38 MAPK signaling pathway. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26926077;Dbxref=PMID:26926077 P26651 UniProtKB Mutagenesis 124 124 . . . Note=Inhibits binding to ARE-containing transcripts. Inhibits binding to and deadenylation activities of ARE-containing mRNAs. Inhibits localization of ARE-containing mRNAs to processing bodies (PBs). C->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10330172,ECO:0000269|PubMed:12748283,ECO:0000269|PubMed:17030620,ECO:0000269|PubMed:17369404,ECO:0000269|PubMed:19188452;Dbxref=PMID:10330172,PMID:12748283,PMID:17030620,PMID:17369404,PMID:19188452 P26651 UniProtKB Mutagenesis 126 126 . . . Note=Inhibits ARE-containing RNA-binding%2C deadenylation and RNA decapping activities. F->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16364915,ECO:0000269|PubMed:21078877,ECO:0000269|PubMed:25815583;Dbxref=PMID:16364915,PMID:21078877,PMID:25815583 P26651 UniProtKB Mutagenesis 147 147 . . . Note=Inhibits both ARE-binding and mRNA deadenylation activities. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10330172;Dbxref=PMID:10330172 P26651 UniProtKB Mutagenesis 309 309 . . . Note=Inhibits interaction with SH3KBP1. P->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20221403;Dbxref=PMID:20221403 P26651 UniProtKB Mutagenesis 315 315 . . . Note=Abolishes interaction with CNOT1. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23644599;Dbxref=PMID:23644599 P26651 UniProtKB Mutagenesis 319 319 . . . Note=Abolishes interaction with CNOT1 and impairs TNF mRNA deadenylation. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23644599;Dbxref=PMID:23644599 P26651 UniProtKB Helix 317 322 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4J8S