Description: Homo sapiens protein arginine methyltransferase 7 (PRMT7), transcript variant 1, mRNA. RefSeq Summary (NM_019023): This gene encodes a member of the protein arginine N-methyltransferase family of proteins. The encoded enzyme transfers single methyl groups to arginine residues to generate monomethylarginines on histone proteins as well as other protein substrates. This enzyme plays a role in a wide range of biological processes, including neuronal differentiation, male germ line imprinting, small nuclear ribonucleoprotein biogenesis, and regulation of the Wnt signaling pathway. Mutations in this gene underlie multiple related syndromes in human patients characterized by intellectual disability, short stature and other features. The encoded protein may promote breast cancer cell invasion and metastasis in human patients. [provided by RefSeq, May 2017]. Transcript (Including UTRs) Position: hg19 chr16:68,344,877-68,391,169 Size: 46,293 Total Exon Count: 19 Strand: + Coding Region Position: hg19 chr16:68,349,883-68,391,127 Size: 41,245 Coding Exon Count: 17
ID:ANM7_HUMAN DESCRIPTION: RecName: Full=Protein arginine N-methyltransferase 7; EC=2.1.1.-; AltName: Full=Histone-arginine N-methyltransferase PRMT7; EC=2.1.1.125; AltName: Full=[Myelin basic protein]-arginine N-methyltransferase PRMT7; EC=2.1.1.126; FUNCTION: 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. CATALYTIC ACTIVITY: S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone]. CATALYTIC ACTIVITY: S-adenosyl-L-methionine + [myelin basic protein]-arginine = S-adenosyl-L-homocysteine + [myelin basic protein]-N(omega)-methyl-arginine. SUBUNIT: Homodimer and heterodimer (By similarity). Interacts with CTCFL (By similarity). Interacts with PRMT5 and SNRPD3. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. MISCELLANEOUS: May be involved in etoposide-induced cytotoxicity, a chemotherapeutic agent frequently used for testicular cancer and small-cell lung cancer that can cause cytotoxicity in the treatment of other cancers. Down-regulation confers increased sensitivity to the Top1 inhibitor camptothecin (CPT). SIMILARITY: Belongs to the protein arginine N-methyltransferase family. PRMT7 subfamily. SEQUENCE CAUTION: Sequence=BAB14215.1; Type=Erroneous initiation;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9NVM4
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
US Server
