Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.1.1.320 - type II protein arginine methyltransferase and Organism(s) Arabidopsis thaliana

for references in articles please use BRENDA:EC2.1.1.320
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Arabidopsis thaliana
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform PRMT5
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
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?
A0A5S9XGJ7_ARATH
471
0
51920
TrEMBL
Chloroplast (Reliability: 5)
A0A178VC13_ARATH
476
0
52554
TrEMBL
Chloroplast (Reliability: 5)
A0A5S9SLY2_ARATH
442
0
50663
TrEMBL
Mitochondrion (Reliability: 5)
Q9LJI6_ARATH
378
0
41983
TrEMBL
other Location (Reliability: 2)
A0A178WEZ0_ARATH
442
0
50604
TrEMBL
Mitochondrion (Reliability: 5)
F4J0D4_ARATH
471
0
52234
TrEMBL
Mitochondrion (Reliability: 5)
Q94C90_ARATH
442
0
50604
TrEMBL
Mitochondrion (Reliability: 5)
Q1JPN1_ARATH
471
0
51980
TrEMBL
Mitochondrion (Reliability: 5)
A0A1I9LQL6_ARATH
373
0
41349
TrEMBL
other Location (Reliability: 2)
A0A7G2EU21_ARATH
471
0
51958
TrEMBL
Mitochondrion (Reliability: 5)
A0A654FI28_ARATH
471
0
51980
TrEMBL
Mitochondrion (Reliability: 5)
Q9MAT8_ARATH
479
0
55042
TrEMBL
Mitochondrion (Reliability: 5)
ANM15_ARATH
642
0
71870
Swiss-Prot
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform PRMT5 expression is regulated by the circadian clock and responds to both light and temperature cues
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hernando, C.E.; Sanchez, S.E.; Mancini, E.; Yanovsky, M.J.
Genome wide comparative analysis of the effects of PRMT5 and PRMT4/CARM1 arginine methyltransferases on the Arabidopsis thaliana transcriptome
BMC Genomics
16
192
2015
Arabidopsis thaliana (Q8GWT4), Arabidopsis thaliana
Manually annotated by BRENDA team
Hong, S.; Song, H.R.; Lutz, K.; Kerstetter, R.A.; Michael, T.P.; McClung, C.R.
Type II protein arginine methyltransferase 5 (PRMT5) is required for circadian period determination in Arabidopsis thaliana
Proc. Natl. Acad. Sci. USA
107
21211-21216
2010
Arabidopsis thaliana (Q8GWT4), Arabidopsis thaliana
Manually annotated by BRENDA team