UniProt functional annotation for F1LQ48



	UniProt functional annotation for F1LQ48

UniProt code: F1LQ48.

Organism: Rattus norvegicus (Rat).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.

Function: Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements. Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts. Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter. {ECO:0000250|UniProtKB:P14866}.

Subunit: Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with HNRNPLL. Interacts with APEX1; the interaction is DNA-dependent. Component of a complex with SETD2 (By similarity). Interacts with ELAVL1 (PubMed:18161049). {ECO:0000250|UniProtKB:P14866, ECO:0000269|PubMed:18161049}.

Subcellular location: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P14866}. Cytoplasm {ECO:0000269|PubMed:18161049}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. These granules are not identical with P bodies or stress granules. {ECO:0000250|UniProtKB:P14866}.

Domain: RRM domain 2 has moderate RNA-binding affinity. RRM domains 3 and 4 may facilitate RNA looping when binding to two appropriately separated binding sites within the same target pre-mRNA. {ECO:0000250|UniProtKB:P14866}.

Ptm: Several isoelectric forms of the L protein are probably the results of post-translational modifications. {ECO:0000250|UniProtKB:P14866}.

Ptm: Phosphorylation at Ser-578 by CaMK4 enhances interaction with a CaMK4-responsive RNA element (CaRRE1), and prevents inclusion of the stress axis-regulated exon (STREX) of the KCNMA1 potassium channel transcripts upon membrane depolarization. {ECO:0000250|UniProtKB:P14866}.

Annotations taken from UniProtKB at the EBI.


Organism:		Rattus norvegicus (Rat).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.



Function:		Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements. Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts. Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter. {ECO:0000250\|UniProtKB:P14866}.


Subunit:		Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with HNRNPLL. Interacts with APEX1; the interaction is DNA-dependent. Component of a complex with SETD2 (By similarity). Interacts with ELAVL1 (PubMed:18161049). {ECO:0000250\|UniProtKB:P14866, ECO:0000269\|PubMed:18161049}.
Subcellular location:		Nucleus, nucleoplasm {ECO:0000250\|UniProtKB:P14866}. Cytoplasm {ECO:0000269\|PubMed:18161049}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. These granules are not identical with P bodies or stress granules. {ECO:0000250\|UniProtKB:P14866}.
Domain:		RRM domain 2 has moderate RNA-binding affinity. RRM domains 3 and 4 may facilitate RNA looping when binding to two appropriately separated binding sites within the same target pre-mRNA. {ECO:0000250\|UniProtKB:P14866}.
Ptm:		Several isoelectric forms of the L protein are probably the results of post-translational modifications. {ECO:0000250\|UniProtKB:P14866}.
Ptm:		Phosphorylation at Ser-578 by CaMK4 enhances interaction with a CaMK4-responsive RNA element (CaRRE1), and prevents inclusion of the stress axis-regulated exon (STREX) of the KCNMA1 potassium channel transcripts upon membrane depolarization. {ECO:0000250\|UniProtKB:P14866}.