Title : Partitioning RS domain phosphorylation in an SR protein through the CLK and SRPK protein kinases.

Pub. Date : 2013 Aug 23

PMID : 23707382






3 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 While SRPK1 rapidly phosphorylates N-terminal serines, SRPK1 and CLK1 display similar activities toward Arg-Ser repeats in the C-terminus, suggesting that these kinases may not separate function in a strict linear manner along the RS domain. Arginine CDC like kinase 1 Homo sapiens
2 CLK1 induces a unique gel shift in SRSF1 that is not the result of enhanced Arg-Ser phosphorylation but rather is the direct result of the phosphorylation of several Ser-Pro dipeptides. Arginine CDC like kinase 1 Homo sapiens
3 The data establish a new view of SR protein regulation in which SRPK1 and CLK1 partition activities based on Ser-Pro versus Arg-Ser placement rather than on N- and C-terminal preferences along the RS domain. Arginine CDC like kinase 1 Homo sapiens