Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3) (Q24306650)

PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits

GOA release 2020-03-11

author name string

Rafal Swiercz

series ordinal

1

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Maria D Person

series ordinal

2

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Mark T Bedford

series ordinal

3

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language of work or name

English

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publication date

15 February 2005

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published in

Biochemical Journal

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volume

386

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page(s)

85-91

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issue

Pt 1

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cites work

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PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation

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Structure of the Predominant Protein Arginine Methyltransferase PRMT1 and Analysis of Its Binding to Substrate Peptides

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Unusual sites of arginine methylation in Poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3

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Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable

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PRMT5 (Janus Kinase-binding Protein 1) Catalyzes the Formation of Symmetric Dimethylarginine Residues in Proteins

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PubMed

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1 reference

Crossref

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inferred from DOI database lookup

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based on heuristic

Identifiers

DOI

10.1042/BJ20041466

0 references

Fatcat ID

release_ejyweqpp5jfzbjsbnwfhxovk2u

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/ejyweqpp5jfzbjsbnwfhxovk2u