2.1.1.320: type II protein arginine methyltransferase
This is an abbreviated version!
For detailed information about type II protein arginine methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.320
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2.1.1.320
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histone
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methyltransferases
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chromatin
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prmts
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dimethylarginine
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tumorigenesis
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h4r3me2s
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monomethylation
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spliceosomal
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mep50
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methylosome
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ribonucleoproteins
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non-histone
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pre-mrna
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snrnps
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picln
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monomethylarginine
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methylthioadenosine
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tudor
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menin
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protein-arginine
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medicine
- 2.1.1.320
- histone
- methyltransferases
- chromatin
-
prmts
- dimethylarginine
- tumorigenesis
-
h4r3me2s
-
monomethylation
-
spliceosomal
- mep50
-
methylosome
- ribonucleoproteins
-
non-histone
- pre-mrna
-
snrnps
-
picln
-
monomethylarginine
- methylthioadenosine
-
tudor
-
menin
- protein-arginine
- medicine
Reaction
2 S-adenosyl-L-methionine + = 2 S-adenosyl-L-homocysteine +
Synonyms
At4g31120, EC 2.1.1.124, EC 2.1.1.125, EC 2.1.1.126, EC 2.1.1.23, Hsl7, Jak-binding protein 1, Janus kinase-binding protein 1, JBP1, PRMT-5, PRMT-9, PRMT15, PRMT5, PRMT7, PRMT9, protein arginine methyltransferase 5, Skb1
ECTree
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medicine
abundant expression of isoform PRMT5 and its symmetric methylation mark H4R3 in lung carcinoma but not in non-neoplastic human pulmonary alveolar and bronchial epithelial cell lines. More than two thirds of lung tumors express PRMT5. High levels of cytoplasmic PRMT5 are detected in 20.5% of non-small cell lung carcinomas and in 16.5% of pulmonary neuroendocrine tumors. High levels of nuclear PRMT5 are detected in 38.0% of non-small cell lung carcinomas and 24.0% of pulmonary neuroendocrine tumors. Cytoplasmic PRMT5 is associated with high grade in both non-small cell lung carcinomas and pulmonary pulmonary neuroendocrine tumors, while nuclear PRMT5 is more frequent in carcinoid tumors
medicine
knockdown of isoform PRMT5 results in more paralysis in a Caenorhabditis elegans model of Alzheimer's disease
medicine
PRMT5 localizes in the nucleus in benign prostate epithelium, whereas it localizes in the cytoplasm in prostate premalignant and cancer tissues
medicine
PRMT1 and PRMT5 have opposing effects on chemotherapeutic agent-mediated apoptosis in lung cancer cells. The identification of PRMT5 and PRMT1 as CFLARL regulators involved in cellular apoptosis may help in developing new strategies to increase the sensitivity of cancer cells to chemotherapy, which may eventually benefit lung cancer treatments