PRMT7
{{Short description|Protein-coding gene in the species Homo sapiens}}
Protein arginine methyltransferase 7 (PRMT7) is a protein that in humans is encoded by the PRMT7 gene.{{cite web | title = Protein arginine methyltransferase 7| url = https://www.ncbi.nlm.nih.gov/gene/54496| access-date = 2011-12-06}} Arginine methylation is an apparently irreversible protein modification catalyzed by arginine methyltransferases, such as PRMT7, using S-adenosylmethionine (AdoMet) as the methyl donor. Arginine methylation is implicated in signal transduction, RNA transport, and RNA splicing.{{Cite journal
| last1 = Miranda | first1 = T. B.
| last2 = Miranda | first2 = M.
| last3 = Frankel | first3 = A.
| last4 = Clarke | first4 = S.
| title = PRMT7 is a Member of the Protein Arginine Methyltransferase Family with a Distinct Substrate Specificity
| doi = 10.1074/jbc.M312904200
| journal = Journal of Biological Chemistry
| volume = 279
| issue = 22
| pages = 22902–22907
| year = 2004
| pmid = 15044439
| pmc =
| doi-access = free
}}
PRMT7 was initially identified as a Type II protein lysine methyltransferase, indicating its role in the symmetric dimethylation of arginine residues. However, it was later reclassified as a Type III protein lysine methyltransferase, meaning it facilitates the mono-methylation of arginine residues. As of 2023, PRMT7 remains the sole member of the Type III PRMT category.{{Cite book |title=Handbook of epigenetics: the new molecular and medical genetics |date=2023 |publisher=Academic Press, an imprint of Elseiver |isbn=978-0-323-91909-8 |editor-last=Tollefsbol |editor-first=Trygve O. |edition=Third |location=London, United Kingdom; San Diego, CA |pages=36}}
References
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Further reading
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- {{Cite journal
| last1 = Jelinic | first1 = P.
| last2 = Stehle | first2 = J. C.
| last3 = Shaw | first3 = P.
| doi = 10.1371/journal.pbio.0040355
| title = The Testis-Specific Factor CTCFL Cooperates with the Protein Methyltransferase PRMT7 in H19 Imprinting Control Region Methylation
| journal = PLOS Biology
| volume = 4
| issue = 11
| pages = e355
| year = 2006
| pmid = 17048991
| pmc =1609128
| doi-access = free
}}
- {{Cite journal
| last1 = Lee | first1 = J. -H.
| last2 = Cook | first2 = J. R.
| last3 = Yang | first3 = Z. H.
| last4 = Mirochnitchenko | first4 = O.
| last5 = Gunderson | first5 = S. I.
| last6 = Felix | first6 = A. M.
| last7 = Herth | first7 = N.
| last8 = Hoffmann | first8 = R.
| last9 = Pestka | first9 = S.
| title = PRMT7, a New Protein Arginine Methyltransferase That Synthesizes Symmetric Dimethylarginine
| doi = 10.1074/jbc.M405295200
| journal = Journal of Biological Chemistry
| volume = 280
| issue = 5
| pages = 3656–3664
| year = 2004
| pmid = 15494416
| pmc =
| doi-access = free
}}
- {{Cite journal
| last1 = Gonsalvez | first1 = G. B.
| last2 = Tian | first2 = L.
| last3 = Ospina | first3 = J. K.
| last4 = Boisvert | first4 = F. -M.
| last5 = Lamond | first5 = A. I.
| last6 = Matera | first6 = A. G.
| doi = 10.1083/jcb.200702147
| title = Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins
| journal = The Journal of Cell Biology
| volume = 178
| issue = 5
| pages = 733–740
| year = 2007
| pmid = 17709427
| pmc =2064538
}}
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Category:Genes mutated in mice
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