##gff-version 3 P52597 UniProtKB Chain 1 415 . . . ID=PRO_0000367114;Note=Heterogeneous nuclear ribonucleoprotein F P52597 UniProtKB Initiator methionine 1 1 . . . Note=Removed%3B alternate;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|Ref.8,ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:22223895,ECO:0007744|PubMed:22814378;Dbxref=PMID:19413330,PMID:22223895,PMID:22814378 P52597 UniProtKB Chain 2 415 . . . ID=PRO_0000081852;Note=Heterogeneous nuclear ribonucleoprotein F%2C N-terminally processed P52597 UniProtKB Domain 13 85 . . . Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 P52597 UniProtKB Domain 111 188 . . . Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 P52597 UniProtKB Domain 289 366 . . . Note=RRM 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 P52597 UniProtKB Region 81 86 . . . Note=Interaction with RNA P52597 UniProtKB Region 179 184 . . . Note=Interaction with RNA P52597 UniProtKB Region 355 360 . . . Note=Interaction with RNA P52597 UniProtKB Site 16 16 . . . Note=Interaction with RNA P52597 UniProtKB Site 20 20 . . . Note=Interaction with RNA P52597 UniProtKB Site 52 52 . . . Note=Interaction with RNA P52597 UniProtKB Site 75 75 . . . Note=Interaction with RNA P52597 UniProtKB Site 116 116 . . . Note=Interaction with RNA P52597 UniProtKB Site 120 120 . . . Note=Interaction with RNA P52597 UniProtKB Site 150 150 . . . Note=Interaction with RNA P52597 UniProtKB Site 173 173 . . . Note=Interaction with RNA P52597 UniProtKB Site 294 294 . . . Note=Interaction with RNA P52597 UniProtKB Site 298 298 . . . Note=Interaction with RNA P52597 UniProtKB Site 326 326 . . . Note=Interaction with RNA P52597 UniProtKB Site 349 349 . . . Note=Interaction with RNA P52597 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine%3B in Heterogeneous nuclear ribonucleoprotein F%3B alternate;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|Ref.8,ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:22814378;Dbxref=PMID:19413330,PMID:22814378 P52597 UniProtKB Modified residue 2 2 . . . Note=N-acetylmethionine%3B in Heterogeneous nuclear ribonucleoprotein F%2C N-terminally processed;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|Ref.8,ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:22223895,ECO:0007744|PubMed:22814378;Dbxref=PMID:19413330,PMID:22223895,PMID:22814378 P52597 UniProtKB Modified residue 104 104 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19369195,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:19369195,PMID:20068231,PMID:21406692,PMID:23186163,PMID:24275569 P52597 UniProtKB Modified residue 107 107 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P52597 UniProtKB Modified residue 161 161 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:17525332;Dbxref=PMID:17525332 P52597 UniProtKB Modified residue 187 187 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:20068231;Dbxref=PMID:20068231 P52597 UniProtKB Modified residue 193 193 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P52597 UniProtKB Modified residue 195 195 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q794E4 P52597 UniProtKB Modified residue 200 200 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Z2X1 P52597 UniProtKB Modified residue 215 215 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P52597 UniProtKB Modified residue 224 224 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P52597 UniProtKB Modified residue 265 265 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P52597 UniProtKB Cross-link 72 72 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15161980;Dbxref=PMID:15161980 P52597 UniProtKB Cross-link 87 87 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 P52597 UniProtKB Cross-link 167 167 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 P52597 UniProtKB Cross-link 185 185 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 P52597 UniProtKB Cross-link 200 200 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25772364,ECO:0007744|PubMed:28112733;Dbxref=PMID:25772364,PMID:28112733 P52597 UniProtKB Cross-link 224 224 . . . 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 P52597 UniProtKB Natural variant 87 87 . . . ID=VAR_027999;Note=K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=dbSNP:rs17851426,PMID:15489334 P52597 UniProtKB Mutagenesis 20 20 . . . Note=Loss of RNA-binding. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20526337;Dbxref=PMID:20526337 P52597 UniProtKB Mutagenesis 84 84 . . . Note=Loss of RNA-binding. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20526337;Dbxref=PMID:20526337 P52597 UniProtKB Mutagenesis 116 116 . . . Note=Decreases affinity for RNA oligonucleotide 100-fold. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20526337;Dbxref=PMID:20526337 P52597 UniProtKB Mutagenesis 120 120 . . . Note=Little disruption of binding RNA. Decreases affinity for RNA oligonucleotide 100-fold. Abrogates RNA-binding%3B when associated with A-180. F->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16885237,ECO:0000269|PubMed:20526337;Dbxref=PMID:16885237,PMID:20526337 P52597 UniProtKB Mutagenesis 150 150 . . . Note=No effect on affinity for RNA oligonucleotide. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20526337;Dbxref=PMID:20526337 P52597 UniProtKB Mutagenesis 156 156 . . . Note=Drastically effects folding of RRM2. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16885237;Dbxref=PMID:16885237 P52597 UniProtKB Mutagenesis 173 173 . . . Note=Minimal effect on affinity for RNA oligonucleotide. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20526337;Dbxref=PMID:20526337 P52597 UniProtKB Mutagenesis 178 178 . . . Note=Little disruption of binding RNA. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16885237;Dbxref=PMID:16885237 P52597 UniProtKB Mutagenesis 179 179 . . . Note=Decreases affinity for RNA oligonucleotide 100-fold. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20526337;Dbxref=PMID:20526337 P52597 UniProtKB Mutagenesis 180 180 . . . Note=Decreases affinity for RNA oligonucleotide 10-fold. Abrogates RNA-binding%3B when associated with A-120. Y->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16885237,ECO:0000269|PubMed:20526337;Dbxref=PMID:16885237,PMID:20526337 P52597 UniProtKB Mutagenesis 182 182 . . . Note=Decreases affinity for RNA oligonucleotide 100-fold. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20526337;Dbxref=PMID:20526337 P52597 UniProtKB Mutagenesis 184 184 . . . Note=Minimal effect on affinity for RNA oligonucleotide. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20526337;Dbxref=PMID:20526337 P52597 UniProtKB Beta strand 12 17 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGL P52597 UniProtKB Helix 24 30 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGL P52597 UniProtKB Turn 31 33 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGL P52597 UniProtKB Beta strand 37 40 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGL P52597 UniProtKB Beta strand 43 47 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGL P52597 UniProtKB Beta strand 49 51 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGL P52597 UniProtKB Beta strand 53 60 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGL P52597 UniProtKB Helix 64 71 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGL P52597 UniProtKB Turn 72 74 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGL P52597 UniProtKB Beta strand 75 87 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGL P52597 UniProtKB Helix 90 97 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGL P52597 UniProtKB Beta strand 107 109 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGM P52597 UniProtKB Beta strand 112 116 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGM P52597 UniProtKB Helix 124 130 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGM P52597 UniProtKB Turn 131 133 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGM P52597 UniProtKB Beta strand 136 142 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGM P52597 UniProtKB Beta strand 147 151 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGM P52597 UniProtKB Beta strand 153 161 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGM P52597 UniProtKB Helix 164 169 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGM P52597 UniProtKB Turn 170 173 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGM P52597 UniProtKB Beta strand 175 180 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KG0 P52597 UniProtKB Beta strand 184 186 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGM P52597 UniProtKB Helix 188 191 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGM P52597 UniProtKB Beta strand 284 294 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KG1 P52597 UniProtKB Helix 302 309 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGN P52597 UniProtKB Beta strand 315 318 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGN P52597 UniProtKB Beta strand 322 325 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGN P52597 UniProtKB Beta strand 332 334 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGN P52597 UniProtKB Helix 337 344 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGN P52597 UniProtKB Beta strand 351 354 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2HGN P52597 UniProtKB Beta strand 358 362 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KG1 P52597 UniProtKB Beta strand 368 371 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KG1 P52597 UniProtKB Beta strand 377 379 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KG1