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IID00229
 UniprotQ9Y3B4
ProteinSplicing factor 3B subunit 6
GeneSF3B6
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
125
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-125 Hetero dimer : IID00190Complex
 Evidence X-RAY 2f9d A Reference
       Region 2f9d A 1-11 disorder
       Region 2f9d A 12-125 order
 Evidence X-RAY 2f9d B Reference
       Region 2f9d B 1-11 disorder
       Region 2f9d B 12-125 order
 Evidence X-RAY 2f9j A Reference
       Region 2f9j A 1-11 disorder
       Region 2f9j A 12-125 order
 Evidence X-RAY 2f9j B Reference
       Region 2f9j B 1-11 disorder
       Region 2f9j B 12-125 order
 Evidence NMR 2fho B Reference
       Region 2fho B 8-93 order
       Region 2fho B 8-12 high_rmsd
 Evidence X-RAY 3lqv A Reference
       Region 3lqv A 11-12 disorder
       Region 3lqv A 13-125 order
 Evidence X-RAY 3lqv B Reference
       Region 3lqv B 11-125 order
Seqacetylation
    41-41 N6-acetyllysine
    29-29 N6-acetyllysine; alternate
 
Prediction
NeProc
Disorder 1-13,99-125
Order 14-98
ProS 13-13,99-125
AlphaFold
Disorder 1-10
Order 11-125
Pfam Hmmer
PF00076 21-89 1.9e-14
SEG 104-116
Function
Function in SwissProt
Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex (PubMed:27720643). SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA (PubMed:12234937). Directly contacts the pre-mRNA branch site adenosine for the first catalytic step of splicing (PubMed:16432215). Enters the spliceosome and associates with the pre-mRNA branch site as part of the 17S U2 or, in the case of the minor spliceosome, as part of the 18S U11/U12 snRNP complex, and thus may facilitate the interaction of these snRNP with the branch sites of U2 and U12 respectively (PubMed:16432215).