Arginine/serine-rich (RS) domain-containing proteins and their phosphorylation by specific protein kinases constitute control circuits to regulate both constitutive and alternative pre-mRNA splicing and coordinate splicing with transcription in cells. Two SR protein-specific kinases (SRPK, also designated SFRSK), SRPK1 and SRPK2, are highly specific for the phosphorylation of these RS proteins, thereby contributing to splicing regulation. SRPK1 plays a role in the condensation of sperm chromatin. SRPK2 has a stringent preference for SR dipeptides and contains a proline-rich sequence at its amino terminus. Both SRPK1 and SRPK2 are highly expresed in testes. SRPK1 is found exclusively in pancreas and SRPK2 is found exclusively in brain and lung. SRPK3 is expressed in the heart and in skeletal muscle.
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Arginine/serine-rich (RS) domain-containing proteins and their phosphorylation by specific protein kinases constitute control circuits to regulate both constitutive and alternative pre-mRNA splicing and coordinate splicing with transcription in cells. Two SR protein-specific kinases (SRPK, also designated SFRSK), SRPK1 and SRPK2, are highly specific for the phosphorylation of these RS proteins, thereby contributing to splicing regulation. SRPK1 plays a role in the condensation of sperm chromatin. SRPK2 has a stringent preference for SR dipeptides and contains a proline-rich sequence at its amino terminus. Both SRPK1 and SRPK2 are highly expresed in testes. SRPK1 is found exclusively in pancreas and SRPK2 is found exclusively in brain and lung. SRPK3 is expressed in the heart and in skeletal muscle.
