This entry represents the single helix domain of RNA-binding protein 48 (RBM48), located adjacent to the N-terminal RRM domain. RBM48 is a component of the minor spliceosome involved in the splicing of U12-type introns in pre-mRNAs []. The protein interacts with ARMC7 and PRPF8 within the spliceosomal complex. RBM48 contains an RRM domain at its N-terminal region and shows alternative splicing. The protein belongs to the RBM48 family and is found across vertebrates.In the structure of human minor spliceosome (), this domain is involved in interaction with the ARMC7 []. The RBM48-ARMC7 complex binds the ��-monomethyl phosphate cap of the guanine nucleotide at the 5' end of U6atac snRNA through extensive interactions.
This family includes animal Pre-mRNA-processing factor 19 (Prp19) and its homologues.Prp19, also known as DNA repair protein Pso4 (psoralen-sensitive mutant 4), is a ubiquitously expressed multifunctional E3 ubiquitin ligase with pleiotropic activities in DNA damage signalling, repair, and replicative senescence. It functions as a critical component of DNA repair and DNA damage checkpoint complexes. It senses DNA damage, binds double-stranded DNA in a sequence-independent manner, facilitates processing of damaged DNA, promotes DNA end joining, regulates replication protein A (RPA2) phosphorylation and ubiquitination at damaged DNA, and regulates RNA splicing and mitotic spindle formation in its integral capacity as a scaffold for a multimeric core complex [, , , , ].Prp19 is essential for spliceosome assembly and stability. It is a core component of the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome and participates in its assembly, its remodelling and is required for its activity. During assembly of the spliceosome, it mediates Lys-63-linked polyubiquitination of the U4 spliceosomal protein PRPF3. Ubiquitination of PRPF3 allows its recognition by the U5 component PRPF8 and stabilises the U4/U5/U6 tri-snRNP spliceosomal complex [].Prp19 contains an N-terminal E3 ubiquitin ligase U-box domain with E2 recruitment function that facilitates dimerisation and is essential for its auto-ubiquitination activity in vitro or when overexpressed [], a coiled-coil Prp19 homology region that mediates its tetramerisation and interaction with CDC5L and SPF27 [, , ]and a C-terminal seven-bladed WD40 ��-propeller that forms an asymmetrical barrel-shaped structure important for substrate recognition and recruitment [, ].
This entry represents the U-box domain of Prp19.Prp19, also known as DNA repair protein Pso4 (psoralen-sensitive mutant 4), is a ubiquitously expressed multifunctional E3 ubiquitin ligase with pleiotropic activities in DNA damage signalling, repair, and replicative senescence. It functions as a critical component of DNA repair and DNA damage checkpoint complexes. It senses DNA damage, binds double-stranded DNA in a sequence-independent manner, facilitates processing of damaged DNA, promotes DNA end joining, regulates replication protein A (RPA2) phosphorylation and ubiquitination at damaged DNA, and regulates RNA splicing and mitotic spindle formation in its integral capacity as a scaffold for a multimeric core complex [, , , , ].Prp19 is essential for spliceosome assembly and stability. It is a core component of the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome and participates in its assembly, its remodelling and is required for its activity. During assembly of the spliceosome, it mediates Lys-63-linked polyubiquitination of the U4 spliceosomal protein PRPF3. Ubiquitination of PRPF3 allows its recognition by the U5 component PRPF8 and stabilises the U4/U5/U6 tri-snRNP spliceosomal complex [].Prp19 contains an N-terminal E3 ubiquitin ligase U-box domain with E2 recruitment function that facilitates dimerisation and is essential for its auto-ubiquitination activity in vitro or when overexpressed [], a coiled-coil Prp19 homology region that mediates its tetramerisation and interaction with CDC5L and SPF27 [, , ]and a C-terminal seven-bladed WD40 ��-propeller that forms an asymmetrical barrel-shaped structure important for substrate recognition and recruitment [, ].
This entry represents the coiled-coil region of Prp19.Prp19, also known as DNA repair protein Pso4 (psoralen-sensitive mutant 4), is a ubiquitously expressed multifunctional E3 ubiquitin ligase with pleiotropic activities in DNA damage signalling, repair, and replicative senescence. It functions as a critical component of DNA repair and DNA damage checkpoint complexes. It senses DNA damage, binds double-stranded DNA in a sequence-independent manner, facilitates processing of damaged DNA, promotes DNA end joining, regulates replication protein A (RPA2) phosphorylation and ubiquitination at damaged DNA, and regulates RNA splicing and mitotic spindle formation in its integral capacity as a scaffold for a multimeric core complex [, , , , ].Prp19 is essential for spliceosome assembly and stability. It is a core component of the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome and participates in its assembly, its remodelling and is required for its activity. During assembly of the spliceosome, it mediates Lys-63-linked polyubiquitination of the U4 spliceosomal protein PRPF3. Ubiquitination of PRPF3 allows its recognition by the U5 component PRPF8 and stabilises the U4/U5/U6 tri-snRNP spliceosomal complex [].Prp19 contains an N-terminal E3 ubiquitin ligase U-box domain with E2 recruitment function that facilitates dimerisation and is essential for its auto-ubiquitination activity in vitro or when overexpressed [], a coiled-coil Prp19 homology region that mediates its tetramerisation and interaction with CDC5L and SPF27 [, , ]and a C-terminal seven-bladed WD40 ��-propeller that forms an asymmetrical barrel-shaped structure important for substrate recognition and recruitment [, ].
