| IED ID | IndEnz0002001255 |
| Enzyme Type ID | protease001255 |
| Protein Name |
Heterogeneous nuclear ribonucleoprotein A1 hnRNP A1 Helix-destabilizing protein Single-strand RNA-binding protein hnRNP core protein A1 Cleaved into: Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed |
| Gene Name | HNRNPA1 HNRPA1 |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGGYGGGGPGYSGGSRGYGSGGQGYGNQGSGYGGSGSYDSYNNGGGGGFGGGSGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPRNQGGYGGSSSSSSYGSGRRF |
| Enzyme Length | 372 |
| Uniprot Accession Number | P09651 |
| 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 (PubMed:17371836). 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 (PubMed:20010808). Binds to the IRES and thereby inhibits the translation of the apoptosis protease activating factor APAF1 (PubMed:31498791). May bind to specific miRNA hairpins (PubMed:28431233). {ECO:0000269|PubMed:17371836, ECO:0000269|PubMed:20010808, ECO:0000269|PubMed:28431233, ECO:0000269|PubMed:31498791}.; FUNCTION: (Microbial infection) May play a role in HCV RNA replication. {ECO:0000269|PubMed:17229681}.; FUNCTION: (Microbial infection) Cleavage by Enterovirus 71 protease 3C results in increased translation of apoptosis protease activating factor APAF1, leading to apoptosis. {ECO:0000269|PubMed:17229681}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Beta strand (14); Chain (2); Compositional bias (2); Cross-link (7); Domain (2); Helix (8); Initiator methionine (1); Modified residue (33); Mutagenesis (6); Natural variant (6); Region (6); Sequence conflict (3); Turn (5) |
| Keywords | 3D-structure;Acetylation;Alternative splicing;Amyotrophic lateral sclerosis;Cytoplasm;Direct protein sequencing;Disease variant;Host-virus interaction;Isopeptide bond;Methylation;Neurodegeneration;Nucleus;Phosphoprotein;RNA-binding;Reference proteome;Repeat;Ribonucleoprotein;Spliceosome;Transport;Ubl conjugation;mRNA processing;mRNA splicing;mRNA transport |
| Interact With | P22626; P51991; P07910; P31942; Q07666; Q14141; Q9UHD9; P27958; Itself; O00233; Q92973; Q9UHD9 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:27694260}. Cytoplasm {ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles continuously between the nucleus and the cytoplasm along with mRNA. Component of ribonucleosomes (PubMed:17289661). {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:27694260}.; SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17229681}. Note=(Microbial infection) In the course of viral infection, colocalizes with HCV NS5B at speckles in the cytoplasm in a HCV-replication dependent manner. {ECO:0000269|PubMed:17229681}.; SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33360543}. Note=(Microbial infection) SARS coronavirus-2/SARS-CoV-2 ORF6 protein increases accumulation to the nucleus. {ECO:0000269|PubMed:33360543}. |
| Modified Residue | MOD_RES 1; /note="N-acetylmethionine"; /evidence="ECO:0007744|PubMed:22814378"; MOD_RES 2; /note="N-acetylserine; in Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed"; /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22814378"; MOD_RES 2; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"; MOD_RES 3; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 4; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"; MOD_RES 6; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"; MOD_RES 22; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P49312"; MOD_RES 192; /note="Phosphoserine; by MKNK2"; /evidence="ECO:0000269|PubMed:16111636"; MOD_RES 194; /note="Asymmetric dimethylarginine; alternate"; /evidence="ECO:0000250|UniProtKB:P09867"; MOD_RES 194; /note="Dimethylated arginine; alternate"; /evidence="ECO:0007744|PubMed:15782174"; MOD_RES 194; /note="Omega-N-methylarginine; alternate"; /evidence="ECO:0000250|UniProtKB:P49312"; MOD_RES 199; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21406692"; MOD_RES 206; /note="Asymmetric dimethylarginine; alternate"; /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:24129315"; MOD_RES 206; /note="Dimethylated arginine; alternate"; /evidence="ECO:0007744|PubMed:15782174"; MOD_RES 206; /note="Omega-N-methylarginine; alternate"; /evidence="ECO:0000269|Ref.9, 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:0000269|Ref.9, ECO:0007744|PubMed:24129315"; MOD_RES 225; /note="Dimethylated arginine; alternate"; /evidence="ECO:0007744|PubMed:15782174"; MOD_RES 225; /note="Omega-N-methylarginine; alternate"; /evidence="ECO:0000269|Ref.9, 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 336; /note="Omega-N-methylarginine"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 337; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 350; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 352; /note="Omega-N-methylarginine"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 361; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 362; /note="Phosphoserine; by MKNK2"; /evidence="ECO:0000269|PubMed:16111636"; MOD_RES 363; /note="Phosphoserine; by MKNK2"; /evidence="ECO:0000269|PubMed:16111636"; MOD_RES 364; /note="Phosphoserine; by MKNK2"; /evidence="ECO:0000269|PubMed:16111636, ECO:0007744|PubMed:23186163"; MOD_RES 365; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"; MOD_RES 368; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"; MOD_RES 370; /note="Omega-N-methylarginine"; /evidence="ECO:0007744|PubMed:24129315" |
| Post Translational Modification | PTM: Arg-194, Arg-206 and Arg-225 are dimethylated, probably to asymmetric dimethylarginine.; PTM: Sumoylated. {ECO:0000269|PubMed:15161980}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (3); Electron microscopy (2); X-ray crystallography (20) |
| Cross Reference PDB | 1HA1; 1L3K; 1PGZ; 1PO6; 1U1K; 1U1L; 1U1M; 1U1N; 1U1O; 1U1P; 1U1Q; 1U1R; 1UP1; 2H4M; 2LYV; 2UP1; 4YOE; 5MPG; 5MPL; 5ZGD; 5ZGL; 6BXX; 6DCL; 6J60; 7BX7; |
| Mapped Pubmed ID | 10323862; 10938105; 10982855; 11101529; 11118221; 11532962; 11546873; 11779509; 11825891; 11884611; 11893730; 11917013; 12060656; 12176931; 12212851; 12411573; 12414731; 12419255; 12477934; 12577067; 12612063; 12665590; 12799433; 12904298; 12927788; 12945950; 14559993; 14625303; 14633690; 14645369; 14703516; 14730019; 14743216; 14756317; 15024032; 15047060; 15161933; 15166247; 15208309; 15231747; 15342234; 15525641; 15671034; 15703079; 15703818; 15848144; 16169070; 16449636; 16449650; 16600502; 16603717; 16809785; 16901787; 16990281; 17287399; 17332742; 17353911; 17558416; 17620599; 17884807; 17898077; 17932509; 17950949; 17959601; 18322460; 18391021; 18457437; 18562319; 18573884; 18846111; 18850631; 19004954; 1906035; 19103666; 19119138; 19135240; 19262567; 19282454; 19285943; 19339352; 19349988; 19369418; 19430204; 19656952; 19667073; 19703396; 19715280; 19737937; 19808671; 19913121; 19926721; 20000738; 20133837; 20186123; 20360068; 20423332; 20467437; 20562859; 20639884; 20711500; 20716340; 20872967; 20932480; 20974848; 20978194; 20980672; 21120954; 21182205; 21398516; 21399625; 21454539; 21526149; 21548758; 21627027; 21642987; 21849455; 21858080; 21988832; 22110043; 22132154; 22227431; 22285803; 22325350; 22365833; 22419818; 22446626; 22496234; 22522808; 22575643; 22623428; 22628224; 22810585; 22821376; 22863774; 22959432; 22983828; 23035981; 23084401; 23106379; 23247503; 23345524; 23430061; 23455153; 23602568; 23658645; 23827524; 23902751; 23985572; 24001602; 24119545; 24166503; 24189400; 24205981; 24514149; 24530421; 24612671; 24628426; 24635384; 24831962; 25324306; 25338872; 25609649; 25752295; 25920683; 25999341; 26003924; 26011126; 26056150; 26151392; 26247723; 26412307; 26420826; 26494299; 26496610; 26518267; 26581508; 26607354; 26674223; 26757361; 26791953; 26825578; 26869449; 26930004; 27168114; 27211563; 27380775; 27489271; 27595546; 27913144; 27958374; 28000042; 28084329; 28115626; 28193894; 28504207; 28625847; 28650318; 29033165; 29077485; 29229447; 29344170; 29367466; 29396485; 29439243; 29484423; 29625167; 2963332; 29650551; 29762696; 29946118; 29996671; 30042133; 30190085; 30357359; 30368881; 30858544; 30954215; 31002816; 31043593; 31311954; 31868085; 32106859; 32200451; 32417965; 32560659; 32759322; 32800545; 32960212; 33311513; 33319070; 33405298; 33422616; 33441818; 33457194; 33507382; 33545634; 33550645; 33564070; 33573689; 33651408; 33782401; 33809384; 33951764; 33982369; 34071140; 34080184; 6088074; 6206566; 8352591; 8451194; 9271388; 9731529; 9858549; |
| Motif | |
| Gene Encoded By | |
| Mass | 38,747 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |