Summary: PRMT5 arginine-N-methyltransferase
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PRMT5 arginine-N-methyltransferase Provide feedback
The human homologue of yeast Skb1 (Shk1 kinase-binding protein 1) is PRMT5, an arginine-N-methyltransferase . These proteins appear to be key mitotic regulators. They play a role in Jak signalling in higher eukaryotes.
Gilbreth M, Yang P, Wang D, Frost J, Polverino A, Cobb MH, Marcus S; , Proc Natl Acad Sci U S A 1996;93:13802-13807.: The highly conserved skb1 gene encodes a protein that interacts with Shk1, a fission yeast Ste20/PAK homolog. PUBMED:8943016 EPMC:8943016
Gilbreth M, Yang P, Bartholomeusz G, Pimental RA, Kansra S, Gadiraju R, Marcus S; , Proc Natl Acad Sci U S A 1998;95:14781-14786.: Negative regulation of mitosis in fission yeast by the shk1 interacting protein skb1 and its human homolog, Skb1Hs. PUBMED:9843966 EPMC:9843966
Pollack BP, Kotenko SV, He W, Izotova LS, Barnoski BL, Pestka S; , J Biol Chem 1999;274:31531-31542.: The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity. PUBMED:10531356 EPMC:10531356
Rho J, Choi S, Seong YR, Cho WK, Kim SH, Im DS; , J Biol Chem 2001;276:11393-11401.: Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family. PUBMED:11152681 EPMC:11152681
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR025799This entry includes different protein arginine-N-methyltransferases, including PRMT2, PRMT5, and others. S-Adenosyl methionine (SAM) serves as a cofactor and methyl donor group for this enzymes [PUBMED:11413150]. Methyltransferases (EC 2.1.1.-) constitute an important class of enzymes present in every life form. They transfer a methyl group most frequently from S-adenosyl L-methionine (SAM or AdoMet) to a nucleophilic acceptor such as oxygen leading to S-adenosyl-L-homocysteine (AdoHcy) and a methylated molecule [PUBMED:16225687, PUBMED:21858014, PUBMED:12826405]. All these enzymes have in common a conserved region of about 130 amino acid residues that allow them to bind SAM [PUBMED:7897657]. The substrates that are methylated by these enzymes cover virtually every kind of biomolecules ranging from small molecules, to lipids, proteins and nucleic acids [PUBMED:16225687, PUBMED:21858014, PUBMED:7897657]. Methyltransferase are therefore involved in many essential cellular processes including biosynthesis, signal transduction, protein repair, chromatin regulation and gene silencing [PUBMED:16225687, PUBMED:21858014, PUBMED:12826405]. More than 230 families of methyltransferases have been described so far, of which more than 220 use SAM as the methyl donor.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||methyltransferase activity (GO:0008168)|
|Biological process||protein methylation (GO:0006479)|
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Curation and family details
|Seed source:||Pfam-B_4050 (release 7.7)|
|Author:||Wood V, Mistry J|
|Number in seed:||35|
|Number in full:||750|
|Average length of the domain:||345.80 aa|
|Average identity of full alignment:||25 %|
|Average coverage of the sequence by the domain:||63.15 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||11|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the PRMT5 domain has been found. There are 29 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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