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
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prmts
- dimethylarginine
- tumorigenesis
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h4r3me2s
-
monomethylation
-
spliceosomal
- mep50
-
methylosome
- ribonucleoproteins
-
non-histone
- pre-mrna
-
snrnps
-
picln
-
monomethylarginine
- methylthioadenosine
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tudor
-
menin
- protein-arginine
- medicine
Reaction
2 S-adenosyl-L-methionine
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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
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2.1.1.320 type II protein arginine methyltransferaseAdvanced search results
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results (Localization
Localization on EC 2.1.1.320 - type II protein arginine methyltransferase
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LOCALIZATION 
ORGANISM
UNIPROT
COMMENTARY 
GeneOntology No.
LITERATURE
SOURCE
PRMT5 enzyme localization is concentrated in the cytosolic, membrane, and myonuclear compartments of mature myofibers
coexpression of candidate tumor suppressor gene RASSF1A and PRMT5 leads to a redistribution of PRMT5 from the cytosol to stabilized microtubules
additional information
high levels of cytoplasmic PRMT5 are detected in 20.5% of non-small cell lung carcinomas and in 16.5% of pulmonary neuroendocrine tumors
isoform PRMT5 and p44/MED50/WD45/WDR77 colocalize in the cytoplasm, and both are required for the growth of prostate cancer cells in an PRMT5 methyltransferase activity-dependent manner
PRMT5 enzyme localization is concentrated in the cytosolic, membrane, and myonuclear compartments of mature myofibers
isoform PRMT5 localizes to the Golgi apparatus and forms complexes with several components involved in Golgi apparatus ribbon formation and vesicle tethering. PRMT5 interacts with the golgin GM130
original isoform PRMT5L mainly colocalizes with Giantin, a Golgi marker
high levels of nuclear PRMT5 are detected in 38.0% of non-small cell lung carcinomas and 24.0% of pulmonary neuroendocrine tumors
isoform PRMT5 in the nucleus inhibits cell growth in a methyltransferase activity-independent manner
additional information
evolutionarily emerged splice variant PRMT5S is distributed all over the cell. The isoforms are differentially expressed during neuronal or dendritic cell differentiation, and their ectopic expression shows an opposite effect on dendritic cell differentiation
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additional information
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evolutionarily emerged splice variant PRMT5S is distributed all over the cell. The isoforms are differentially expressed during neuronal or dendritic cell differentiation, and their ectopic expression shows an opposite effect on dendritic cell differentiation
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additional information
presence of three nuclear exclusion signals in the PRMT5 protein
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