| IED ID | IndEnz0002011611 |
| Enzyme Type ID | protease011611 |
| Protein Name |
Heterogeneous nuclear ribonucleoprotein A1 hnRNP A1 HDP-1 Helix-destabilizing protein Single-strand-binding protein Topoisomerase-inhibitor suppressed hnRNP core protein A1 Cleaved into: Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed |
| Gene Name | Hnrnpa1 Fli-2 Hnrpa1 Tis |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPRNQGGYGGSSSSSSYGSGRRF |
| Enzyme Length | 320 |
| Uniprot Accession Number | P49312 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and modulation of splice site selection. Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform. Binds to the IRES and thereby inhibits the translation of the apoptosis protease activating factor APAF1. May bind to specific miRNA hairpins. {ECO:0000250|UniProtKB:P09651}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Chain (2); Compositional bias (2); Cross-link (7); Domain (2); Initiator methionine (1); Modified residue (33); Region (6) |
| Keywords | Acetylation;Alternative splicing;Cytoplasm;Direct protein sequencing;Isopeptide bond;Methylation;Nucleus;Phosphoprotein;RNA-binding;Reference proteome;Repeat;Ribonucleoprotein;Spliceosome;Transport;Ubl conjugation;mRNA processing;mRNA splicing;mRNA transport |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09651}. Cytoplasm {ECO:0000250|UniProtKB:P09651}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles continuously between the nucleus and the cytoplasm along with mRNA. Component of ribonucleosomes. {ECO:0000250|UniProtKB:P09651}. |
| Modified Residue | MOD_RES 1; /note="N-acetylmethionine"; /evidence="ECO:0000250|UniProtKB:P09651"; MOD_RES 2; /note="N-acetylserine; in Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed"; /evidence="ECO:0000250|UniProtKB:P09651"; MOD_RES 2; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P09651"; MOD_RES 3; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P09651"; MOD_RES 4; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P09651"; MOD_RES 6; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"; MOD_RES 22; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 192; /note="Phosphoserine; by MKNK2"; /evidence="ECO:0000250|UniProtKB:P09651"; MOD_RES 194; /note="Asymmetric dimethylarginine; alternate"; /evidence="ECO:0000250|UniProtKB:P09867"; MOD_RES 194; /note="Dimethylated arginine; alternate"; /evidence="ECO:0000250|UniProtKB:P09651"; MOD_RES 194; /note="Omega-N-methylarginine; alternate"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 199; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P09651"; MOD_RES 206; /note="Asymmetric dimethylarginine; alternate"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 206; /note="Dimethylated arginine; alternate"; /evidence="ECO:0000250|UniProtKB:P09651"; MOD_RES 206; /note="Omega-N-methylarginine; alternate"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 218; /note="Asymmetric dimethylarginine; alternate"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 218; /note="Omega-N-methylarginine; alternate"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 225; /note="Asymmetric dimethylarginine; alternate"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 225; /note="Dimethylated arginine; alternate"; /evidence="ECO:0000250|UniProtKB:P09651"; MOD_RES 225; /note="Omega-N-methylarginine; alternate"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 232; /note="Asymmetric dimethylarginine; alternate"; /evidence="ECO:0000250|UniProtKB:P04256"; MOD_RES 232; /note="Omega-N-methylarginine; alternate"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 284; /note="Omega-N-methylarginine"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 285; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P09651"; MOD_RES 298; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:23806337"; MOD_RES 300; /note="Omega-N-methylarginine"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 309; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P09651"; MOD_RES 310; /note="Phosphoserine; by MKNK2"; /evidence="ECO:0000250|UniProtKB:P09651"; MOD_RES 311; /note="Phosphoserine; by MKNK2"; /evidence="ECO:0000250|UniProtKB:P09651"; MOD_RES 312; /note="Phosphoserine; by MKNK2"; /evidence="ECO:0000250|UniProtKB:P09651"; MOD_RES 313; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P09651"; MOD_RES 316; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P09651"; MOD_RES 318; /note="Omega-N-methylarginine"; /evidence="ECO:0000250|UniProtKB:P09651" |
| Post Translational Modification | PTM: Sumoylated. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10215609; 10725249; 11217851; 11774503; 11774505; 12107167; 12560094; 12904583; 14610273; 14611647; 14654002; 1497882; 15102471; 15390079; 15582152; 15615787; 15703188; 15798186; 16033648; 16110338; 16236758; 16602821; 16604525; 16615898; 18562319; 18799693; 18809582; 19834914; 20133837; 20338999; 20537373; 21253564; 21454539; 21677750; 21984414; 22345078; 22740652; 23704325; 23946460; 24152440; 24553115; 24607481; 25901972; 26435271; 27151978; 28024152; 28077597; 28088441; 28115626; 28220845; 28671691; 28912364; 29077485; 29367466; 32086392; 32960212; 33115498; 33692334; 33951764; 34630013; 34944075; 7768196; 7832805; |
| Motif | |
| Gene Encoded By | |
| Mass | 34,196 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |