Splicing factor 3 subunit 1 is a
protein that in humans is encoded by the SF3A1gene.[5][6]
This gene encodes subunit 1 of the splicing factor 3a protein complex. The splicing factor 3a heterotrimer includes subunits 1, 2 and 3 and is necessary for the in vitro conversion of 15S U2 snRNP into an active 17S particle that performs pre-mRNA splicing. Subunit 1 belongs to the SURP protein family; named for the SURP (also called SWAP or Suppressor-of-White-APricot) motifs that are thought to mediate RNA binding. Subunit 1 has tandemly repeated SURP motifs in its amino-terminal half while its carboxy-terminal half contains a proline-rich region and a ubiquitin-like domain. Binding studies with truncated subunit 1 derivatives demonstrated that the two SURP motifs are necessary for binding to subunit 3 while contacts with subunit 2 may occur through sequences carboxy-terminal to the SURP motifs. Alternative splicing results in multiple transcript variants encoding different isoforms.[6]
Neubauer G, King A, Rappsilber J, et al. (1998). "Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex". Nat. Genet. 20 (1): 46–50.
doi:
10.1038/1700.
PMID9731529.
S2CID585778.
Gunther M; Laithier M; Brison O (2000). "A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening". Mol. Cell. Biochem. 210 (1–2): 131–42.
doi:
10.1023/A:1007177623283.
PMID10976766.
S2CID1339642.
Splicing factor 3 subunit 1 is a
protein that in humans is encoded by the SF3A1gene.[5][6]
This gene encodes subunit 1 of the splicing factor 3a protein complex. The splicing factor 3a heterotrimer includes subunits 1, 2 and 3 and is necessary for the in vitro conversion of 15S U2 snRNP into an active 17S particle that performs pre-mRNA splicing. Subunit 1 belongs to the SURP protein family; named for the SURP (also called SWAP or Suppressor-of-White-APricot) motifs that are thought to mediate RNA binding. Subunit 1 has tandemly repeated SURP motifs in its amino-terminal half while its carboxy-terminal half contains a proline-rich region and a ubiquitin-like domain. Binding studies with truncated subunit 1 derivatives demonstrated that the two SURP motifs are necessary for binding to subunit 3 while contacts with subunit 2 may occur through sequences carboxy-terminal to the SURP motifs. Alternative splicing results in multiple transcript variants encoding different isoforms.[6]
Neubauer G, King A, Rappsilber J, et al. (1998). "Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex". Nat. Genet. 20 (1): 46–50.
doi:
10.1038/1700.
PMID9731529.
S2CID585778.
Gunther M; Laithier M; Brison O (2000). "A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening". Mol. Cell. Biochem. 210 (1–2): 131–42.
doi:
10.1023/A:1007177623283.
PMID10976766.
S2CID1339642.