##gff-version 3 Q9Y6M1 UniProtKB Chain 1 599 . . . ID=PRO_0000244496;Note=Insulin-like growth factor 2 mRNA-binding protein 2 Q9Y6M1 UniProtKB Domain 3 76 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 Q9Y6M1 UniProtKB Domain 82 157 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 Q9Y6M1 UniProtKB Domain 193 258 . . . Note=KH 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117 Q9Y6M1 UniProtKB Domain 274 341 . . . Note=KH 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117 Q9Y6M1 UniProtKB Domain 427 492 . . . Note=KH 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117 Q9Y6M1 UniProtKB Domain 509 575 . . . Note=KH 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00117 Q9Y6M1 UniProtKB Region 157 188 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Y6M1 UniProtKB Modified residue 11 11 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q9Y6M1 UniProtKB Modified residue 162 162 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:21406692;Dbxref=PMID:18669648,PMID:21406692 Q9Y6M1 UniProtKB Modified residue 164 164 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:19690332,PMID:21406692,PMID:23186163 Q9Y6M1 UniProtKB Modified residue 550 550 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SF07 Q9Y6M1 UniProtKB Alternative sequence 1 80 . . . ID=VSP_036550;Note=In isoform 3%2C isoform 4 and isoform 5. MMNKLYIGNLSPAVTADDLRQLFGDRKLPLAGQVLLKSGYAFVDYPDQNWAIRAIETLSGKVELHGKIMEVDYSVSKKLR->MFSCPGHYHVDGFLNPG;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.2 Q9Y6M1 UniProtKB Alternative sequence 1 68 . . . ID=VSP_043699;Note=In isoform 6. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Y6M1 UniProtKB Alternative sequence 113 113 . . . ID=VSP_036552;Note=In isoform 4. Q->QVFAFSL;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.2 Q9Y6M1 UniProtKB Alternative sequence 358 400 . . . ID=VSP_036553;Note=In isoform 2 and isoform 5. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:10190901,ECO:0000303|Ref.2;Dbxref=PMID:10190901 Q9Y6M1 UniProtKB Mutagenesis 211 211 . . . Note=Significantly impaired binding to ACTB transcript but little effect on MYC transcript binding%2C accumulation in the nucleus and partial reduction in interaction with m6A-modified mRNA%3B when associated with E-292. Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2%2C almost complete loss of ACTB and MYC transcript binding%2C almost complete loss of ELAVL1-%2C DHX9- and HNRNPU-binding and perturbed subcellular location%2C including accumulation in the nucleus and loss of localization to stress granules%3B when associated with E-292%3B 445-E-E-446 and 526-E-E-527. K->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23640942,ECO:0000269|PubMed:29476152;Dbxref=PMID:23640942,PMID:29476152 Q9Y6M1 UniProtKB Mutagenesis 292 292 . . . Note=Significantly impaired binding to ACTB transcript but little effect on MYC transcript binding%2C accumulation in the nucleus and partial reduction in interaction with m6A-modified mRNA%3B when associated with E-211. Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2%2C almost complete loss of ACTB and MYC transcript binding%2C almost complete loss of ELAVL1-%2C DHX9- and HNRNPU-binding and perturbed subcellular location%2C including accumulation in the nucleus and loss of localization to stress granules%3B when associated with E-211%3B 445-E-E-445 and 526-E-E-527. K->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23640942,ECO:0000269|PubMed:29476152;Dbxref=PMID:23640942,PMID:29476152 Q9Y6M1 UniProtKB Mutagenesis 445 446 . . . Note=Significantly impaired binding to ACTB and MYC transcripts and loss of interaction with m6A-modified mRNA%3B when associated with 527-E-E-528. Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2%2C almost complete loss of ACTB and MYC transcript binding%2C almost complete loss of ELAVL1-%2C DHX9- and HNRNPU-binding and perturbed subcellular location%2C including accumulation in the nucleus and loss of localization to stress granules%3B when associated with E-211%3B E-292 and 527-E-E-528. KK->EE;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23640942,ECO:0000269|PubMed:29476152;Dbxref=PMID:23640942,PMID:29476152 Q9Y6M1 UniProtKB Mutagenesis 527 528 . . . Note=Significantly impaired binding to ACTB and MYC transcripts and loss of interaction with m6A-modified mRNA%3B when associated with 445-E-E-446. Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2%2C almost complete loss of ACTB and MYC transcript binding%2C almost complete loss of ELAVL1-%2C DHX9- and HNRNPU-binding and perturbed subcellular location%2C including accumulation in the nucleus and loss of localization to stress granules%3B when associated with E-211%3B E-292 and 445-E-E-446. KG->EE;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23640942,ECO:0000269|PubMed:29476152;Dbxref=PMID:23640942,PMID:29476152 Q9Y6M1 UniProtKB Beta strand 5 8 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CQH Q9Y6M1 UniProtKB Helix 16 25 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CQH Q9Y6M1 UniProtKB Beta strand 34 37 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CQH Q9Y6M1 UniProtKB Beta strand 40 43 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CQH Q9Y6M1 UniProtKB Helix 48 58 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CQH Q9Y6M1 UniProtKB Turn 59 61 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CQH Q9Y6M1 UniProtKB Beta strand 70 73 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2CQH Q9Y6M1 UniProtKB Beta strand 370 372 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7Q98 Q9Y6M1 UniProtKB Beta strand 428 435 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ROL Q9Y6M1 UniProtKB Helix 436 438 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ROL Q9Y6M1 UniProtKB Helix 439 443 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ROL Q9Y6M1 UniProtKB Helix 445 447 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ROL Q9Y6M1 UniProtKB Helix 448 457 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ROL Q9Y6M1 UniProtKB Beta strand 459 463 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ROL Q9Y6M1 UniProtKB Beta strand 472 480 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ROL Q9Y6M1 UniProtKB Helix 482 498 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ROL Q9Y6M1 UniProtKB Beta strand 510 517 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ROL Q9Y6M1 UniProtKB Helix 518 520 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ROL Q9Y6M1 UniProtKB Helix 521 525 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ROL Q9Y6M1 UniProtKB Helix 527 529 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ROL Q9Y6M1 UniProtKB Helix 530 539 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ROL Q9Y6M1 UniProtKB Beta strand 542 544 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ROL Q9Y6M1 UniProtKB Beta strand 555 563 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ROL Q9Y6M1 UniProtKB Helix 565 584 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6ROL Q9Y6M1 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:22223895,ECO:0007744|PubMed:22814378;Dbxref=PMID:22223895,PMID:22814378