UniProt acc. | Start of exon skipping (AA) | End of exon skipping (AA) | Protein feature start (AA) | Protein feature end (AA) | Category of protein feature | Description of feature |
P22626 | 2 | 13 | 3 | 14 | Alternative sequence | ID=VSP_005830;Note=In isoform A2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:2557628;Dbxref=PMID:2557628 |
P22626 | 2 | 13 | 1 | 353 | Chain | ID=PRO_0000081836;Note=Heterogeneous nuclear ribonucleoproteins A2/B1 |
P22626 | 2 | 13 | 4 | 4 | Modified residue | Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:23186163;Dbxref=PMID:23186163 |
P22626 | 2 | 13 | 9 | 15 | Motif | Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 |
P22626 | 51 | 99 | 47 | 54 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HO4 |
P22626 | 51 | 99 | 61 | 71 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HO4 |
P22626 | 51 | 99 | 83 | 86 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X4B |
P22626 | 51 | 99 | 92 | 95 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HO4 |
P22626 | 51 | 99 | 1 | 353 | Chain | ID=PRO_0000081836;Note=Heterogeneous nuclear ribonucleoproteins A2/B1 |
P22626 | 51 | 99 | 21 | 104 | Domain | Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 |
P22626 | 51 | 99 | 72 | 80 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HO4 |
P22626 | 51 | 99 | 99 | 101 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HO4 |
P22626 | 51 | 99 | 85 | 85 | Modified residue | Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:19690332,ECO:0000244|PubMed:20068231,ECO:0000244|PubMed:24275569;Dbxref=PMID:19690332,PMID:20068231,PMID:24275569 |
P22626 | 51 | 99 | 56 | 58 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HO4 |
P22626 | 170 | 204 | 174 | 177 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HO4 |
P22626 | 170 | 204 | 180 | 186 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HO4 |
P22626 | 170 | 204 | 1 | 353 | Chain | ID=PRO_0000081836;Note=Heterogeneous nuclear ribonucleoproteins A2/B1 |
P22626 | 170 | 204 | 202 | 353 | Compositional bias | Note=Gly-rich |
P22626 | 170 | 204 | 173 | 173 | Cross-link | Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:28112733;Dbxref=PMID:28112733 |
P22626 | 170 | 204 | 186 | 186 | Cross-link | Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:25218447;Dbxref=PMID:25218447 |
P22626 | 170 | 204 | 112 | 191 | Domain | Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 |
P22626 | 170 | 204 | 173 | 173 | Modified residue | Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19608861;Dbxref=PMID:19608861 |
P22626 | 170 | 204 | 176 | 176 | Modified residue | Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:23186163;Dbxref=PMID:23186163 |
P22626 | 170 | 204 | 189 | 189 | Modified residue | Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:23186163;Dbxref=PMID:23186163 |
P22626 | 170 | 204 | 201 | 201 | Modified residue | Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:23186163;Dbxref=PMID:23186163 |
P22626 | 170 | 204 | 203 | 203 | Modified residue | Note=Asymmetric dimethylarginine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88569 |
P22626 | 170 | 204 | 203 | 203 | Modified residue | Note=Dimethylated arginine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6 |
P22626 | 170 | 204 | 203 | 203 | Modified residue | Note=Omega-N-methylarginine%3B alternate;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:15782174,ECO:0000244|PubMed:24129315,ECO:0000269|Ref.6;Dbxref=PMID:15782174,PMID:24129315 |
P22626 | 170 | 204 | 193 | 353 | Region | Note=Low complexity (LC) region;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 170 | 204 | 190 | 192 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HO4 |
P22626 | 204 | 231 | 1 | 353 | Chain | ID=PRO_0000081836;Note=Heterogeneous nuclear ribonucleoproteins A2/B1 |
P22626 | 204 | 231 | 202 | 353 | Compositional bias | Note=Gly-rich |
P22626 | 204 | 231 | 212 | 212 | Modified residue | Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:19690332,ECO:0000244|PubMed:20068231,ECO:0000244|PubMed:21406692,ECO:0000244|PubMed:23186163,ECO:0000244|PubMed:24275569;Dbxref=PMID:1 |
P22626 | 204 | 231 | 213 | 213 | Modified residue | Note=Asymmetric dimethylarginine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88569 |
P22626 | 204 | 231 | 213 | 213 | Modified residue | Note=Dimethylated arginine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6 |
P22626 | 204 | 231 | 213 | 213 | Modified residue | Note=Omega-N-methylarginine%3B alternate;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:24129315,ECO:0000269|Ref.6;Dbxref=PMID:24129315 |
P22626 | 204 | 231 | 225 | 225 | Modified residue | Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:20068231,ECO:0000244|PubMed:21406692,ECO:0000244|PubMed:23186163,ECO:0000244|PubMed:24275569;Dbxref=PMID:20068231,PMID:21406692,PMID:23186163,PMID |
P22626 | 204 | 231 | 228 | 228 | Modified residue | Note=Omega-N-methylarginine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:24129315;Dbxref=PMID:24129315 |
P22626 | 204 | 231 | 231 | 231 | Modified residue | Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:20068231,ECO:0000244|PubMed:21406692,ECO:0000244|PubMed:24275569;Dbxref=PMID:20068231,PMID:21406692,PMID:24275569 |
P22626 | 204 | 231 | 207 | 207 | Mutagenesis | Note=Does not affect hydrogel-binding. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 204 | 231 | 209 | 209 | Mutagenesis | Note=Does not affect hydrogel-binding. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 204 | 231 | 219 | 219 | Mutagenesis | Note=Does not affect hydrogel-binding. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 204 | 231 | 227 | 227 | Mutagenesis | Note=Does not affect hydrogel-binding. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 204 | 231 | 193 | 353 | Region | Note=Low complexity (LC) region;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 204 | 231 | 205 | 205 | Sequence conflict | Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
P22626 | 252 | 292 | 1 | 353 | Chain | ID=PRO_0000081836;Note=Heterogeneous nuclear ribonucleoproteins A2/B1 |
P22626 | 252 | 292 | 202 | 353 | Compositional bias | Note=Gly-rich |
P22626 | 252 | 292 | 259 | 259 | Modified residue | Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17924679,ECO:0000244|PubMed:18220336,ECO:0000244|PubMed:18669648,ECO:0000244|PubMed:18 |
P22626 | 252 | 292 | 266 | 266 | Modified residue | Note=Asymmetric dimethylarginine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:A7VJC2 |
P22626 | 252 | 292 | 266 | 266 | Modified residue | Note=Omega-N-methylarginine%3B alternate;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:24129315;Dbxref=PMID:24129315 |
P22626 | 252 | 292 | 256 | 256 | Mutagenesis | Note=Does not affect hydrogel-binding. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 252 | 292 | 262 | 262 | Mutagenesis | Note=Slightly affects hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 252 | 292 | 269 | 269 | Mutagenesis | Note=Does not affect hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 252 | 292 | 276 | 276 | Mutagenesis | Note=Impairs hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 252 | 292 | 283 | 283 | Mutagenesis | Note=Slightly affects hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 252 | 292 | 287 | 287 | Mutagenesis | Note=Does not affect hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 252 | 292 | 290 | 290 | Mutagenesis | Note=Impairs hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 252 | 292 | 193 | 353 | Region | Note=Low complexity (LC) region;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 292 | 333 | 1 | 353 | Chain | ID=PRO_0000081836;Note=Heterogeneous nuclear ribonucleoproteins A2/B1 |
P22626 | 292 | 333 | 202 | 353 | Compositional bias | Note=Gly-rich |
P22626 | 292 | 333 | 324 | 324 | Modified residue | Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:21406692,ECO:0000244|PubMed:23186163;Dbxref=PMID:21406692,PMID:23186163 |
P22626 | 292 | 333 | 325 | 325 | Modified residue | Note=Omega-N-methylarginine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:24129315;Dbxref=PMID:24129315 |
P22626 | 292 | 333 | 331 | 331 | Modified residue | Note=Phosphotyrosine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:21406692,ECO:0000244|PubMed:23186163;Dbxref=PMID:21406692,PMID:23186163 |
P22626 | 292 | 333 | 295 | 295 | Mutagenesis | Note=Impairs hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 292 | 333 | 300 | 300 | Mutagenesis | Note=Slightly affects hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 292 | 333 | 303 | 303 | Mutagenesis | Note=Impairs hydrogel-binding. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 292 | 333 | 306 | 306 | Mutagenesis | Note=Slightly affects hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 292 | 333 | 313 | 313 | Mutagenesis | Note=Slightly affects hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 292 | 333 | 321 | 321 | Mutagenesis | Note=Impairs hydrogel-binding. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 292 | 333 | 331 | 331 | Mutagenesis | Note=Impairs hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 292 | 333 | 302 | 302 | Natural variant | ID=VAR_070591;Note=In IBMPFD2. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23455423;Dbxref=dbSNP:rs397515326,PMID:23455423 |
P22626 | 292 | 333 | 193 | 353 | Region | Note=Low complexity (LC) region;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 292 | 333 | 308 | 347 | Region | Note=Nuclear targeting sequence;Ontology_term=ECO:0000250;evidence=ECO:0000250 |
UniProt acc. | Start of exon skipping (AA) | End of exon skipping (AA) | Protein feature start (AA) | Protein feature end (AA) | Category of protein feature | Description of feature |
P22626 | 2 | 13 | 3 | 14 | Alternative sequence | ID=VSP_005830;Note=In isoform A2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:2557628;Dbxref=PMID:2557628 |
P22626 | 2 | 13 | 1 | 353 | Chain | ID=PRO_0000081836;Note=Heterogeneous nuclear ribonucleoproteins A2/B1 |
P22626 | 2 | 13 | 4 | 4 | Modified residue | Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:23186163;Dbxref=PMID:23186163 |
P22626 | 2 | 13 | 9 | 15 | Motif | Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 |
P22626 | 51 | 99 | 47 | 54 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HO4 |
P22626 | 51 | 99 | 61 | 71 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HO4 |
P22626 | 51 | 99 | 83 | 86 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:1X4B |
P22626 | 51 | 99 | 92 | 95 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HO4 |
P22626 | 51 | 99 | 1 | 353 | Chain | ID=PRO_0000081836;Note=Heterogeneous nuclear ribonucleoproteins A2/B1 |
P22626 | 51 | 99 | 21 | 104 | Domain | Note=RRM 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 |
P22626 | 51 | 99 | 72 | 80 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HO4 |
P22626 | 51 | 99 | 99 | 101 | Helix | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HO4 |
P22626 | 51 | 99 | 85 | 85 | Modified residue | Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:19690332,ECO:0000244|PubMed:20068231,ECO:0000244|PubMed:24275569;Dbxref=PMID:19690332,PMID:20068231,PMID:24275569 |
P22626 | 51 | 99 | 56 | 58 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HO4 |
P22626 | 170 | 204 | 174 | 177 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HO4 |
P22626 | 170 | 204 | 180 | 186 | Beta strand | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HO4 |
P22626 | 170 | 204 | 1 | 353 | Chain | ID=PRO_0000081836;Note=Heterogeneous nuclear ribonucleoproteins A2/B1 |
P22626 | 170 | 204 | 202 | 353 | Compositional bias | Note=Gly-rich |
P22626 | 170 | 204 | 173 | 173 | Cross-link | Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:28112733;Dbxref=PMID:28112733 |
P22626 | 170 | 204 | 186 | 186 | Cross-link | Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:25218447;Dbxref=PMID:25218447 |
P22626 | 170 | 204 | 112 | 191 | Domain | Note=RRM 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00176 |
P22626 | 170 | 204 | 173 | 173 | Modified residue | Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:19608861;Dbxref=PMID:19608861 |
P22626 | 170 | 204 | 176 | 176 | Modified residue | Note=Phosphothreonine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:23186163;Dbxref=PMID:23186163 |
P22626 | 170 | 204 | 189 | 189 | Modified residue | Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:23186163;Dbxref=PMID:23186163 |
P22626 | 170 | 204 | 201 | 201 | Modified residue | Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:23186163;Dbxref=PMID:23186163 |
P22626 | 170 | 204 | 203 | 203 | Modified residue | Note=Asymmetric dimethylarginine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88569 |
P22626 | 170 | 204 | 203 | 203 | Modified residue | Note=Dimethylated arginine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6 |
P22626 | 170 | 204 | 203 | 203 | Modified residue | Note=Omega-N-methylarginine%3B alternate;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:15782174,ECO:0000244|PubMed:24129315,ECO:0000269|Ref.6;Dbxref=PMID:15782174,PMID:24129315 |
P22626 | 170 | 204 | 193 | 353 | Region | Note=Low complexity (LC) region;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 170 | 204 | 190 | 192 | Turn | Ontology_term=ECO:0000244;evidence=ECO:0000244|PDB:5HO4 |
P22626 | 204 | 231 | 1 | 353 | Chain | ID=PRO_0000081836;Note=Heterogeneous nuclear ribonucleoproteins A2/B1 |
P22626 | 204 | 231 | 202 | 353 | Compositional bias | Note=Gly-rich |
P22626 | 204 | 231 | 212 | 212 | Modified residue | Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:19690332,ECO:0000244|PubMed:20068231,ECO:0000244|PubMed:21406692,ECO:0000244|PubMed:23186163,ECO:0000244|PubMed:24275569;Dbxref=PMID:1 |
P22626 | 204 | 231 | 213 | 213 | Modified residue | Note=Asymmetric dimethylarginine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88569 |
P22626 | 204 | 231 | 213 | 213 | Modified residue | Note=Dimethylated arginine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.6 |
P22626 | 204 | 231 | 213 | 213 | Modified residue | Note=Omega-N-methylarginine%3B alternate;Ontology_term=ECO:0000244,ECO:0000269;evidence=ECO:0000244|PubMed:24129315,ECO:0000269|Ref.6;Dbxref=PMID:24129315 |
P22626 | 204 | 231 | 225 | 225 | Modified residue | Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:20068231,ECO:0000244|PubMed:21406692,ECO:0000244|PubMed:23186163,ECO:0000244|PubMed:24275569;Dbxref=PMID:20068231,PMID:21406692,PMID:23186163,PMID |
P22626 | 204 | 231 | 228 | 228 | Modified residue | Note=Omega-N-methylarginine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:24129315;Dbxref=PMID:24129315 |
P22626 | 204 | 231 | 231 | 231 | Modified residue | Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:20068231,ECO:0000244|PubMed:21406692,ECO:0000244|PubMed:24275569;Dbxref=PMID:20068231,PMID:21406692,PMID:24275569 |
P22626 | 204 | 231 | 207 | 207 | Mutagenesis | Note=Does not affect hydrogel-binding. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 204 | 231 | 209 | 209 | Mutagenesis | Note=Does not affect hydrogel-binding. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 204 | 231 | 219 | 219 | Mutagenesis | Note=Does not affect hydrogel-binding. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 204 | 231 | 227 | 227 | Mutagenesis | Note=Does not affect hydrogel-binding. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 204 | 231 | 193 | 353 | Region | Note=Low complexity (LC) region;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 204 | 231 | 205 | 205 | Sequence conflict | Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 |
P22626 | 231 | 252 | 1 | 353 | Chain | ID=PRO_0000081836;Note=Heterogeneous nuclear ribonucleoproteins A2/B1 |
P22626 | 231 | 252 | 202 | 353 | Compositional bias | Note=Gly-rich |
P22626 | 231 | 252 | 231 | 231 | Modified residue | Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:20068231,ECO:0000244|PubMed:21406692,ECO:0000244|PubMed:24275569;Dbxref=PMID:20068231,PMID:21406692,PMID:24275569 |
P22626 | 231 | 252 | 236 | 236 | Modified residue | Note=Phosphoserine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:21406692;Dbxref=PMID:21406692 |
P22626 | 231 | 252 | 238 | 238 | Modified residue | Note=Omega-N-methylarginine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:24129315;Dbxref=PMID:24129315 |
P22626 | 231 | 252 | 234 | 234 | Mutagenesis | Note=Does not affect hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 231 | 252 | 240 | 240 | Mutagenesis | Note=Does not affect hydrogel-binding. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 231 | 252 | 244 | 244 | Mutagenesis | Note=Does not affect hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 231 | 252 | 247 | 247 | Mutagenesis | Note=Slightly affects hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 231 | 252 | 193 | 353 | Region | Note=Low complexity (LC) region;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 252 | 292 | 1 | 353 | Chain | ID=PRO_0000081836;Note=Heterogeneous nuclear ribonucleoproteins A2/B1 |
P22626 | 252 | 292 | 202 | 353 | Compositional bias | Note=Gly-rich |
P22626 | 252 | 292 | 259 | 259 | Modified residue | Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:17924679,ECO:0000244|PubMed:18220336,ECO:0000244|PubMed:18669648,ECO:0000244|PubMed:18 |
P22626 | 252 | 292 | 266 | 266 | Modified residue | Note=Asymmetric dimethylarginine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:A7VJC2 |
P22626 | 252 | 292 | 266 | 266 | Modified residue | Note=Omega-N-methylarginine%3B alternate;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:24129315;Dbxref=PMID:24129315 |
P22626 | 252 | 292 | 256 | 256 | Mutagenesis | Note=Does not affect hydrogel-binding. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 252 | 292 | 262 | 262 | Mutagenesis | Note=Slightly affects hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 252 | 292 | 269 | 269 | Mutagenesis | Note=Does not affect hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 252 | 292 | 276 | 276 | Mutagenesis | Note=Impairs hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 252 | 292 | 283 | 283 | Mutagenesis | Note=Slightly affects hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 252 | 292 | 287 | 287 | Mutagenesis | Note=Does not affect hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 252 | 292 | 290 | 290 | Mutagenesis | Note=Impairs hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 252 | 292 | 193 | 353 | Region | Note=Low complexity (LC) region;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 292 | 333 | 1 | 353 | Chain | ID=PRO_0000081836;Note=Heterogeneous nuclear ribonucleoproteins A2/B1 |
P22626 | 292 | 333 | 202 | 353 | Compositional bias | Note=Gly-rich |
P22626 | 292 | 333 | 324 | 324 | Modified residue | Note=Phosphoserine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:21406692,ECO:0000244|PubMed:23186163;Dbxref=PMID:21406692,PMID:23186163 |
P22626 | 292 | 333 | 325 | 325 | Modified residue | Note=Omega-N-methylarginine;Ontology_term=ECO:0000244;evidence=ECO:0000244|PubMed:24129315;Dbxref=PMID:24129315 |
P22626 | 292 | 333 | 331 | 331 | Modified residue | Note=Phosphotyrosine;Ontology_term=ECO:0000244,ECO:0000244;evidence=ECO:0000244|PubMed:21406692,ECO:0000244|PubMed:23186163;Dbxref=PMID:21406692,PMID:23186163 |
P22626 | 292 | 333 | 295 | 295 | Mutagenesis | Note=Impairs hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 292 | 333 | 300 | 300 | Mutagenesis | Note=Slightly affects hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 292 | 333 | 303 | 303 | Mutagenesis | Note=Impairs hydrogel-binding. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 292 | 333 | 306 | 306 | Mutagenesis | Note=Slightly affects hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 292 | 333 | 313 | 313 | Mutagenesis | Note=Slightly affects hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 292 | 333 | 321 | 321 | Mutagenesis | Note=Impairs hydrogel-binding. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 292 | 333 | 331 | 331 | Mutagenesis | Note=Impairs hydrogel-binding. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 292 | 333 | 302 | 302 | Natural variant | ID=VAR_070591;Note=In IBMPFD2. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23455423;Dbxref=dbSNP:rs397515326,PMID:23455423 |
P22626 | 292 | 333 | 193 | 353 | Region | Note=Low complexity (LC) region;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26544936;Dbxref=PMID:26544936 |
P22626 | 292 | 333 | 308 | 347 | Region | Note=Nuclear targeting sequence;Ontology_term=ECO:0000250;evidence=ECO:0000250 |