Any feedback?
Information on EC 2.1.1.320 - type II protein arginine methyltransferase and Organism(s) Mus musculus and UniProt Accession Q8CIG8
for references in articles please use BRENDA:EC2.1.1.320Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.1.1.320 type II protein arginine methyltransferaseIUBMB 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.
Specify your search results
Word Map
- 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
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + [histone H3R2]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R2]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + [histone H3R2]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3R2]-Nomega,Nomega'-dimethyl-L-arginine
-
-
-
?
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
PRMT5 enzyme localization is concentrated in the cytosolic, membrane, and myonuclear compartments of mature myofibers
-
isoform PRMT5 is abundantly expressed in the germ cells of both male and female gonads
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PRMT5 enzyme localization is concentrated in the cytosolic, membrane, and myonuclear compartments of mature myofibers
PRMT5 enzyme localization is concentrated in the cytosolic, membrane, and myonuclear compartments of mature myofibers
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
physiological function
inactivation of isoform Prmt5 in skeletal muscle stem cells of adult mice prevents expansion of skeletal muscle stem cells, abolishes long-term skeletal muscle stem cells maintenance and abrogates skeletal muscle regeneration. Prmt5 is dispensable for proliferation and differentiation of Pax7+ myogenic progenitor cells during mouse embryonic development. Prmt5 controls proliferation of adult skeletal muscle stem cells by direct epigenetic silencing of the cell cycle inhibitor p21
physiological function
Loss of PRMT5 in conditional KO mice triggers an initial but transient expansion of hematopoietic stem cells. Prmt5 deletion results in a concurrent loss of hematopoietic progenitor cells, leading to fatal bone marrow aplasia. PRMT5-specific effects on hematopoiesis are cell intrinsic and depend on PRMT5 methyltransferase activity. PRMT5-deficient hematopoietic stem and progenitor cells exhibit severely impaired cytokine signaling as well as upregulation of p53 and expression of its downstream targets
physiological function
PRMT5 expression, localization, and activity are altered following denervation-induced inactivity
physiological function
PRMT5 inhibition induces mouse primary lymphoma cell death through inactivation of AKT/GSK3x02 and WNT/beta-CATENIN proliferative signaling
physiological function
the enzyme (PRMT5) is essential for IFN-gamma induced, CIITA-dependent MHC II transactivation by promoting histone H3R2 methylation in macrophages. Over-expression of PRMT5 potentiates IFN-gamma induced activation of MHC II transcription in an enzyme activity-dependent manner. Pathophysiologically relevant role for PRMT5 in MHC II transactivation in macrophages
physiological function
-
deletion of Prmt5 results in germ cell depletion in adult mice. Germ cell loss is first observed between embryonic days 12.5 and 13.5, and very few of these cells remain at birth. Oct4, Sox2, and Nanog are abundantly expressed in Prmt5-deficient germ cells, whereas their expression is dramatically decreased in control germ cells. The expression of meiosis-associated genes is virtually absent in Prmt5-deficient female germ cells at embryonic day 13.5 , whereas the expression of other germ cell-specific genes is not changed. Methylation of histine H4R3 is completely absent after Prmt5 inactivation, whereas the level of histone H3R2 is not changed
physiological function
-
siRNA-mediated depletion of PRMT5 primary oligodendrocyte progenitor cells abrogates oligodendrocyte differentiation. PRMT5-depleted oligodendrocyte progenitor and C6 glioma cells express high levels of the inhibitors of differentiation/DNA binding, Id2 and Id4, known repressors of glial cell differentiation. CpG-rich islands within the Id2 and Id4 genes are bound by PRMT5 and are hypomethylated in PRMT5-deficient cells
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ANM5_MOUSE
637
0
72680
Swiss-Prot
other Location (Reliability: 4)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
PRMT5 expression is down-regulated in senescent and H2O2-treated macrophages rendering ineffectual induction of MHC II transcription by IFN-gamma
PRMT5 protein expression is elevated by 1.8-2.9fold in the denervated tibialis anterior muscle, as compared with the control tibialis anterior muscle
relative to the control muscle PRMT5 mRNA expression levels in the denervated soleus muscle is decreased by 26% after 12 h
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, Y.; Li, Q.; Liu, C.; Han, F.; Chen, M.; Zhang, L.; Cui, X.; Qin, Y.; Bao, S.; Gao, F.
Protein arginine methyltransferase 5 (Prmt5) is required for germ cell survival during mouse embryonic development
Biol. Reprod.
92
104
2015
Mus musculus
Huang, J.; Vogel, G.; Yu, Z.; Almazan, G.; Richard, S.
Type II arginine methyltransferase PRMT5 regulates gene expression of inhibitors of differentiation/DNA binding Id2 and Id4 during glial cell differentiation
J. Biol. Chem.
286
44424-44432
2011
Mus musculus, Rattus norvegicus (D4A0E8)
Liu, F.; Cheng, G.; Hamard, P.J.; Greenblatt, S.; Wang, L.; Man, N.; Perna, F.; Xu, H.; Tadi, M.; Luciani, L.; Nimer, S.D.
Arginine methyltransferase PRMT5 is essential for sustaining normal adult hematopoiesis
J. Clin. Invest.
125
3532-3544
2015
Mus musculus (Q8CIG8)
Zhang, T.; Guenther, S.; Looso, M.; Kuenne, C.; Krueger, M.; Kim, J.; Zhou, Y.; Braun, T.
Prmt5 is a regulator of muscle stem cell expansion in adult mice
Nat. Commun.
6
7140
2015
Mus musculus (Q8CIG8), Mus musculus
Stouth, D.W.; Manta, A.; Ljubicic, V.
Protein arginine methyltransferase expression, localization, and activity during disuse-induced skeletal muscle plasticity
Am. J. Physiol. Cell Physiol.
314
C177-C190
2018
Mus musculus (Q8CIG8)
Fan, Z.; Kong, X.; Xia, J.; Wu, X.; Li, H.; Xu, H.; Fang, M.; Xu, Y.
The arginine methyltransferase PRMT5 regulates CIITA-dependent MHC II transcription
Biochim. Biophys. Acta
1859
687-696
2016
Homo sapiens (O14744), Mus musculus (Q8CIG8)
Chung, J.; Karkhanis, V.; Baiocchi, R.A.; Sif, S.
Protein arginine methyltransferase 5 (PRMT5) promotes survival of lymphoma cells via activation of WNT/?-catenin and AKT/GSK3? proliferative signaling
J. Biol. Chem.
294
7692-7710
2019
Homo sapiens (O14744), Mus musculus (Q8CIG8), Mus musculus
EXTERNAL LINKS (specific for EC-Number 2.1.1.320)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
