Tbio | Protein arginine N-methyltransferase 7 |
Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo.
Arginine methylation is an apparently irreversible protein modification catalyzed by arginine methyltransferases, such as PMT7, using S-adenosylmethionine (AdoMet) as the methyl donor. Arginine methylation is implicated in signal transduction, RNA transport, and RNA splicing (Miranda et al., 2004 [PubMed 15044439]).[supplied by OMIM, Mar 2008]
Arginine methylation is an apparently irreversible protein modification catalyzed by arginine methyltransferases, such as PMT7, using S-adenosylmethionine (AdoMet) as the methyl donor. Arginine methylation is implicated in signal transduction, RNA transport, and RNA splicing (Miranda et al., 2004 [PubMed 15044439]).[supplied by OMIM, Mar 2008]
Comments
Disease | Target Count | P-value |
---|---|---|
intraductal papillary-mucinous adenoma (IPMA) | 2956 | 1.28896529079578E-4 |
Disease | Target Count | Z-score | Confidence |
---|---|---|---|
Intellectual disability | 573 | 0.0 | 4.0 |
Disease | Target Count | Z-score | Confidence |
---|---|---|---|
Syndromic intellectual disability | 9 | 3.576 | 1.8 |
Disease | log2 FC | p |
---|---|---|
intraductal papillary-mucinous adenoma (... | 1.300 | 0.000 |
Species | Source |
---|---|
Macaque | OMA Inparanoid |
Mouse | OMA EggNOG Inparanoid |
Rat | OMA EggNOG Inparanoid |
Dog | OMA EggNOG Inparanoid |
Cow | OMA Inparanoid |
Platypus | OMA Inparanoid |
Anole lizard | OMA Inparanoid |
Xenopus | OMA Inparanoid |
C. elegans | OMA Inparanoid |
Fruitfly | OMA Inparanoid |
PMID | Text |
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25605249 | Upregulation of PRMT7 in breast cancer may have a significant role in promoting cell invasion through the regulation of MMP9. |
25294873 | Data indicate that two acidic residues within the double E loop, Asp-147 and Glu-149, confer specificity to protein arginine methyltransferase 7 (PRMT7. |
25136067 | results define PRMT7 as an inducer of breast cancer metastasis and present the opportunity for applying PRMT7-targeted therapeutics to treat highly invasive breast cancers |
22761421 | reducing expression of individual PRMT7 target DNA repair genes showed that only the catalytic subunit of DNA polymerase, POLD1, was able to resensitize PRMT7 knock-down cells to DNA-damaging agents. |
22241471 | Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming omega-NG-monomethylated arginine residues. |
22231400 | Here the authors report that H3R2 is also symmetrically dimethylated (H3R2me2s) by PRMT5 and PRMT7 and present in euchromatic regions. |
17709427 | that in human cells, PRMT5 and PRMT7 are required for Sm protein sDMA modification, and that Sm protein symmetric dimethylarginine modification is required for snRNP biogenesis in human cells. |
15494416 | PRMT7 (like PRMT5) is a Type II methyltransferase capable of producing symmetric dimethylarginine modifications in proteins. |
15044439 | both domains are required for functionality |
MKIFCSRANPTTGSVEWLEEDEHYDYHQEIARSSYADMLHDKDRNVKYYQGIRAAVSRVKDRGQKALVLD 1 - 70 IGTGTGLLSMMAVTAGADFCYAIEVFKPMADAAVKIVEKNGFSDKIKVINKHSTEVTVGPEGDMPCRANI 71 - 140 LVTELFDTELIGEGALPSYEHAHRHLVEENCEAVPHRATVYAQLVESGRMWSWNKLFPIHVQTSLGEQVI 141 - 210 VPPVDVESCPGAPSVCDIQLNQVSPADFTVLSDVLPMFSIDFSKQVSSSAACHSRRFEPLTSGRAQVVLS 211 - 280 WWDIEMDPEGKIKCTMAPFWAHSDPEEMQWRDHWMQCVYFLPQEEPVVQGSALYLVAHHDDYCVWYSLQR 281 - 350 TSPEKNERVRQMRPVCDCQAHLLWNRPRFGEINDQDRTDRYVQALRTVLKPDSVCLCVSDGSLLSVLAHH 351 - 420 LGVEQVFTVESSAASHKLLRKIFKANHLEDKINIIEKRPELLTNEDLQGRKVSLLLGEPFFTTSLLPWHN 421 - 490 LYFWYVRTAVDQHLGPGAMVMPQAASLHAVVVEFRDLWRIRSPCGDCEGFDVHIMDDMIKRALDFRESRE 491 - 560 AEPHPLWEYPCRSLSEPWQILTFDFQQPVPLQPLCAEGTVELRRPGQSHAAVLWMEYHLTPECTLSTGLL 561 - 630 EPADPEGGCCWNPHCKQAVYFFSPAPDPRALLGGPRTVSYAVEFHPDTGDIIMEFRHADTPD 631 - 692 //
PMID | Year | Title |
---|---|---|
26429889 | 2015 | A human laterality disorder caused by a homozygous deleterious mutation in MMP21. |
25605249 | 2015 | Protein arginine methyltransferase 7 promotes breast cancer cell invasion through the induction of MMP9 expression. |
25294873 | 2014 | Substrate specificity of human protein arginine methyltransferase 7 (PRMT7): the importance of acidic residues in the double E loop. |
25136067 | 2014 | PRMT7 induces epithelial-to-mesenchymal transition and promotes metastasis in breast cancer. |
22814378 | 2012 | N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. |
22761421 | 2012 | Protein arginine methyltransferase 7 regulates cellular response to DNA damage by methylating promoter histones H2A and H4 of the polymerase ? catalytic subunit gene, POLD1. |
22241471 | 2012 | Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming ?-NG-monomethylated arginine residues. |
22231400 | 2012 | Symmetric dimethylation of H3R2 is a newly identified histone mark that supports euchromatin maintenance. |
20700443 | 2010 | Genome-wide association studies of serum magnesium, potassium, and sodium concentrations identify six Loci influencing serum magnesium levels. |
19110445 | 2009 | Accurate localization and relative quantification of arginine methylation using nanoflow liquid chromatography coupled to electron transfer dissociation and orbitrap mass spectrometry. |
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