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Information on EC 2.1.1.320 - type II protein arginine methyltransferase and Organism(s) Caenorhabditis elegans

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EC Tree
IUBMB Comments
The enzyme catalyses the methylation of one of the terminal guanidino nitrogen atoms in arginine residues within proteins, forming monomethylarginine, followed by the methylation of the second terminal nitrogen atom to form a symmetrical dimethylarginine. The mammalian enzyme is active in both the nucleus and the cytoplasm, and plays a role in the assembly of snRNP core particles by methylating certain small nuclear ribonucleoproteins. cf. EC 2.1.1.319, type I protein arginine methyltransferase, EC 2.1.1.321, type III protein arginine methyltransferase, and EC 2.1.1.322, type IV protein arginine methyltransferase.
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Caenorhabditis elegans
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The taxonomic range for the selected organisms is: Caenorhabditis elegans
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
prmt5, prmt7, protein arginine methyltransferase 5, prmt9, type ii protein arginine methyltransferase, prmt-5, prmt-9, jak-binding protein 1, janus kinase-binding protein 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PRMT5
PRMT9
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-Nomega,Nomega'-dimethyl-L-arginine-forming)
The enzyme catalyses the methylation of one of the terminal guanidino nitrogen atoms in arginine residues within proteins, forming monomethylarginine, followed by the methylation of the second terminal nitrogen atom to form a symmetrical dimethylarginine. The mammalian enzyme is active in both the nucleus and the cytoplasm, and plays a role in the assembly of snRNP core particles by methylating certain small nuclear ribonucleoproteins. cf. EC 2.1.1.319, type I protein arginine methyltransferase, EC 2.1.1.321, type III protein arginine methyltransferase, and EC 2.1.1.322, type IV protein arginine methyltransferase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + [protein]-L-arginine
2 S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
-
-
-
?
2 S-adenosyl-L-methionine + [SER-2 tyramine receptor]-L-arginine
2 S-adenosyl-L-homocysteine + [SER-2 tyramine receptor]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
2 S-adenosyl-L-methionine + [splicing factor SF3B2]-L-arginine
2 S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
S-adenosyl-L-methionine + [splicing factor SF3B2]-L-arginine
S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega-methyl-L-arginine
show the reaction diagram
the enzyme methylates the R508 residue
-
-
?
S-adenosyl-L-methionine + [splicing factor SF3B2]-Nomega-L-arginine
S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
the enzyme methylates the R508 residue
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + [SER-2 tyramine receptor]-L-arginine
2 S-adenosyl-L-homocysteine + [SER-2 tyramine receptor]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
the enzyme (PRMT-5) regulates SER-2 tyramine receptor-mediated behaviors in Caenorhabditis elegans
-
-
?
2 S-adenosyl-L-methionine + [splicing factor SF3B2]-L-arginine
2 S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NDUF7_CAEEL
426
0
48107
Swiss-Prot
Mitochondrion (Reliability: 4)
ANM5_CAEEL
734
0
83292
Swiss-Prot
other Location (Reliability: 2)
O02325_CAEEL
680
0
77765
TrEMBL
Secretory Pathway (Reliability: 4)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in BL21 DE3 cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
knockdown of isoform PRMT5 results in more paralysis in a Caenorhabditis elegans model of Alzheimer's disease
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Quan, X.; Yue, W.; Luo, Y.; Cao, J.; Wang, H.; Wang, Y.; Lu, Z.
The protein arginine methyltransferase PRMT5 regulates Abeta-induced toxicity in human cells and Caenorhabditis elegans models of Alzheimers disease
J. Neurochem.
134
969-977
2015
Homo sapiens (O14744), Homo sapiens, Caenorhabditis elegans (P46580), Caenorhabditis elegans
Manually annotated by BRENDA team
Likhite, N.; Jackson, C.A.; Liang, M.S.; Krzyzanowski, M.C.; Lei, P.; Wood, J.F.; Birkaya, B.; Michaels, K.L.; Andreadis, S.T.; Clark, S.D.; Yu, M.C.; Ferkey, D.M.
The protein arginine methyltransferase PRMT5 promotes D2-like dopamine receptor signaling
Sci. Signal.
8
ra115
2015
Homo sapiens (O14744), Homo sapiens, Caenorhabditis elegans (P46580), Caenorhabditis elegans
Manually annotated by BRENDA team
Hadjikyriacou, A.; Clarke, S.G.
Caenorhabditis elegans PRMT-7 and PRMT-9 are evolutionarily conserved protein arginine methyltransferases with distinct substrate specificities
Biochemistry
56
2612-2626
2017
Caenorhabditis elegans (O02325), Caenorhabditis elegans
Manually annotated by BRENDA team
Stopa, N.; Krebs, J.E.; Shechter, D.
The PRMT5 arginine methyltransferase many roles in development, cancer and beyond
Cell. Mol. Life Sci.
72
2041-2059
2015
Homo sapiens (O14744), Homo sapiens, Caenorhabditis elegans (P46580), Caenorhabditis elegans, Xenopus laevis (Q6NUA1)
Manually annotated by BRENDA team
Bowitch, A.; Michaels, K.; Yu, M.; Ferkey, D.
The protein arginine methyltransferase PRMT-5 regulates SER-2 tyramine receptor-mediated behaviors in Caenorhabditis elegans
G3 (Bethesda)
8
2389-2398
2018
Caenorhabditis elegans (P46580), Caenorhabditis elegans
Manually annotated by BRENDA team