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{
"metadata": {
"accession": "IPR035075",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF05185": "PRMT5 arginine-N-methyltransferase"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR035075",
"name": "PRMT5 arginine-N-methyltransferase",
"type": "Domain",
"children": []
},
"name": {
"name": "PRMT5 arginine-N-methyltransferase",
"short": "PRMT5"
},
"description": [
{
"text": "<p>This entry represents a domain found in arginine-N-methyltransferase PRMT5. Proteins containing this domain include Skb1 from S. pombe [[cite:PUB00073546]], Hsl7 from S. cerevisiae [[cite:PUB00073547]] and their homologues PRMT5 from animals [[cite:PUB00010228], [cite:PUB00020182], [cite:PUB00058186]] and plants [[cite:PUB00073549]].</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>Skb1 is a mediator of hyperosmotic stress response in Schizosaccharomyces pombe [[cite:PUB00073546]]. Plant PMRT15 is involved in the post-transcriptional regulation of the circadian clock [[cite:PUB00073550]]. Human PRMT5 is a component of multiple protein complexes and contributes to essential cellular processes, such as RNA transport and splicing, cell cycle regulation, tumour growth, and chromatin remodelling, leading to either gene silencing or activation [[cite:PUB00073551]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00073551": {
"PMID": 22269951,
"ISBN": null,
"volume": "32",
"issue": "7",
"year": 2012,
"title": "HOXA9 methylation by PRMT5 is essential for endothelial cell expression of leukocyte adhesion molecules.",
"URL": null,
"raw_pages": "1202-13",
"medline_journal": "Mol Cell Biol",
"ISO_journal": "Mol. Cell. Biol.",
"authors": [
"Bandyopadhyay S",
"Harris DP",
"Adams GN",
"Lause GE",
"McHugh A",
"Tillmaand EG",
"Money A",
"Willard B",
"Fox PL",
"Dicorleto PE."
],
"DOI_URL": "http://dx.doi.org/10.1128/MCB.05977-11"
},
"PUB00058186": {
"PMID": 17709427,
"ISBN": null,
"volume": "178",
"issue": "5",
"year": 2007,
"title": "Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins.",
"URL": null,
"raw_pages": "733-40",
"medline_journal": "J Cell Biol",
"ISO_journal": "J. Cell Biol.",
"authors": [
"Gonsalvez GB",
"Tian L",
"Ospina JK",
"Boisvert FM",
"Lamond AI",
"Matera AG."
],
"DOI_URL": "http://dx.doi.org/10.1083/jcb.200702147"
},
"PUB00073550": {
"PMID": 20962777,
"ISBN": null,
"volume": "468",
"issue": "7320",
"year": 2010,
"title": "A methyl transferase links the circadian clock to the regulation of alternative splicing.",
"URL": null,
"raw_pages": "112-6",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Sanchez SE",
"Petrillo E",
"Beckwith EJ",
"Zhang X",
"Rugnone ML",
"Hernando CE",
"Cuevas JC",
"Godoy Herz MA",
"Depetris-Chauvin A",
"Simpson CG",
"Brown JW",
"Cerdan PD",
"Borevitz JO",
"Mas P",
"Ceriani MF",
"Kornblihtt AR",
"Yanovsky MJ."
],
"DOI_URL": "http://dx.doi.org/10.1038/nature09470"
},
"PUB00073549": {
"PMID": 17363895,
"ISBN": null,
"volume": "26",
"issue": "7",
"year": 2007,
"title": "SKB1-mediated symmetric dimethylation of histone H4R3 controls flowering time in Arabidopsis.",
"URL": null,
"raw_pages": "1934-41",
"medline_journal": "EMBO J",
"ISO_journal": "EMBO J.",
"authors": [
"Wang X",
"Zhang Y",
"Ma Q",
"Zhang Z",
"Xue Y",
"Bao S",
"Chong K."
],
"DOI_URL": "http://dx.doi.org/10.1038/sj.emboj.7601647"
},
"PUB00073546": {
"PMID": 11278267,
"ISBN": null,
"volume": "276",
"issue": "18",
"year": 2001,
"title": "The highly conserved protein methyltransferase, Skb1, is a mediator of hyperosmotic stress response in the fission yeast Schizosaccharomyces pombe.",
"URL": null,
"raw_pages": "14549-52",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Bao S",
"Qyang Y",
"Yang P",
"Kim H",
"Du H",
"Bartholomeusz G",
"Henkel J",
"Pimental R",
"Verde F",
"Marcus S."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.C100096200"
},
"PUB00073547": {
"PMID": 10903903,
"ISBN": null,
"volume": "274",
"issue": "1",
"year": 2000,
"title": "Hsl7p, the yeast homologue of human JBP1, is a protein methyltransferase.",
"URL": null,
"raw_pages": "105-11",
"medline_journal": "Biochem Biophys Res Commun",
"ISO_journal": "Biochem. Biophys. Res. Commun.",
"authors": [
"Lee JH",
"Cook JR",
"Pollack BP",
"Kinzy TG",
"Norris D",
"Pestka S."
],
"DOI_URL": "http://dx.doi.org/10.1006/bbrc.2000.3049"
},
"PUB00010228": {
"PMID": 10531356,
"ISBN": null,
"volume": "274",
"issue": "44",
"year": 1999,
"title": "The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity.",
"URL": null,
"raw_pages": "31531-42",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Pollack BP",
"Kotenko SV",
"He W",
"Izotova LS",
"Barnoski BL",
"Pestka S."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.274.44.31531"
},
"PUB00020182": {
"PMID": 11152681,
"ISBN": null,
"volume": "276",
"issue": "14",
"year": 2001,
"title": "Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family.",
"URL": null,
"raw_pages": "11393-401",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Rho J",
"Choi S",
"Seong YR",
"Cho WK",
"Kim SH",
"Im DS."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M008660200"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR029063",
"name": "S-adenosyl-L-methionine-dependent methyltransferase superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 145,
"interactions": 0,
"matches": 5212,
"pathways": 9,
"proteins": 5091,
"proteomes": 2915,
"sets": 0,
"structural_models": {
"alphafold": 4481,
"bfvd": 0
},
"structures": 86,
"taxa": 8380
},
"entry_annotations": {
"alignment:seed": 28,
"alignment:full": 3296
},
"cross_references": {
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "2.1.1.320",
"url": "https://enzyme.expasy.org/EC/2.1.1.320"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
