UniProt functional annotation for P19120

UniProt code: P19120.

Organism: Bos taurus (Bovine).
Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Function: Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19- CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex (By similarity). Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion (By similarity).
Subunit: Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with PACRG. Interacts with HSPH1/HSP105. Interacts with IRAK1BP1 and BAG1. Interacts with DNAJC7. Interacts with CITED1 (via N-terminus); the interaction suppresses the association of CITED1 to p300/CBP and SMAD-mediated transcription transactivation. Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts with TRIM5 (By similarity). Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3- specific methyltransferase activity (By similarity). Following LPS binding, may form a complex with CXCR4, GDF5 and HSP90AA1 (By similarity). Interacts with PARK2 (By similarity).
Subcellular location: Cytoplasm (By similarity). Melanosome (By similarity). Nucleus, nucleolus (By similarity). Cell membrane (By similarity). Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock (By similarity).
Tissue specificity: Ubiquitous.
Induction: Constitutively synthesized.
Domain: The N-terminal 1-386 residues constitute the ATPase domain, while residues 387-646 form the peptide-binding domain (By similarity).
Ptm: Acetylated (By similarity).
Ptm: ISGylated (By similarity).
Ptm: Trimethylation at Lys-561 reduces fibrillar SNCA binding (By similarity).
Similarity: Belongs to the heat shock protein 70 family.

Annotations taken from UniProtKB at the EBI.