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IID00190
UniprotO75533
ProteinSplicing factor 3B subunit 1
GeneSF3B1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
1304
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-1304 Hetero tetramer : Q15393,Q7RTV0,Q9BWJ5
 Evidence X-RAY 5ife C Reference
       Region 5ife C 1-462 disorder
       Region 5ife C 463-485 order
       Region 5ife C 486-489 disorder
       Region 5ife C 490-1097 order
       Region 5ife C 1098-1106 disorder
       Region 5ife C 1107-1304 order
Seqdisorder 190-344
 Evidence CD Reference
       Region 190-344 disorder
Seq 333-342 Hetero trimer : IID00567Complex
 Evidence X-RAY 4oz1 C Reference
       Region 4oz1 C 333-334 disorder
       Region 4oz1 C 335-342 order
Seq 333-342 Hetero dimer : IID00221Complex
 Evidence X-RAY 2peh D Reference
       Region 2peh D 333-333 disorder
       Region 2peh D 334-342 order
 Evidence X-RAY 2peh C Reference
       Region 2peh C 333-342 order
Seq 373-424 Hetero dimer : IID00229Complex
 Evidence NMR 2fho A Reference
       Region 2fho A 379-424 order
       Region 2fho A 379-398 high_rmsd
       Region 2fho A 423-424 high_rmsd
 Evidence X-RAY 3lqv Q Reference
       Region 3lqv Q 377-378 disorder
       Region 3lqv Q 379-415 order
 Evidence X-RAY 3lqv P Reference
       Region 3lqv P 377-415 order
 Evidence X-RAY 2f9j Q Reference
       Region 2f9j Q 380-388 disorder
       Region 2f9j Q 389-415 order
 Evidence X-RAY 2f9j P Reference
       Region 2f9j P 380-380 disorder
       Region 2f9j P 381-415 order
 Evidence X-RAY 2f9d Q Reference
       Region 2f9d Q 373-376 disorder
       Region 2f9d Q 377-415 order
 Evidence X-RAY 2f9d P Reference
       Region 2f9d P 373-376 disorder
       Region 2f9d P 377-415 order
SeqProS verified 333-342 Hetero dimer : IID00221Complex
       Region 2peh C 333-342 order
       Region 2peh D 334-342 order
       Region 190-344 disorder
SeqProS verified 333-342 Hetero trimer : IID00567Complex
       Region 4oz1 C 335-342 order
       Region 190-344 disorder
Seqphosphorylation
    488-488 Phosphoserine
    436-436 Phosphothreonine
    434-434 Phosphothreonine; by DYRK1A
    426-426 Phosphothreonine
    400-400 Phosphoserine
    354-354 Phosphothreonine
    350-350 Phosphothreonine
    349-349 Phosphoserine
    344-344 Phosphoserine
    341-341 Phosphothreonine
    332-332 Phosphoserine
    328-328 Phosphothreonine
    326-326 Phosphothreonine
    322-322 Phosphoserine
    313-313 Phosphothreonine
    303-303 Phosphothreonine
    299-299 Phosphothreonine
    296-296 Phosphothreonine
    287-287 Phosphoserine
    278-278 Phosphothreonine
    273-273 Phosphothreonine
    267-267 Phosphothreonine
    261-261 Phosphothreonine
    257-257 Phosphothreonine
    248-248 Phosphothreonine
    244-244 Phosphothreonine
    235-235 Phosphothreonine
    229-229 Phosphoserine
    227-227 Phosphothreonine
    223-223 Phosphothreonine
    211-211 Phosphothreonine
    207-207 Phosphothreonine
    203-203 Phosphothreonine
    194-194 Phosphoserine
    142-142 Phosphothreonine
    129-129 Phosphoserine
    125-125 Phosphothreonine
Seqacetylation
    554-554 N6-acetyllysine
    562-562 N6-acetyllysine
    214-214 N6-acetyllysine; alternate
    141-141 N6-acetyllysine
 
Prediction
NeProc
Disorder 29-407,413-417,422-459
Order 1-28,408-412,418-421,460-483,489-1304
ProS 29-63,83-174,196-202,216-223,240-258,266-275,291-296,308-313,321-326,336-344,352-361,385-407,413-417,422-447
AlphaFold
Disorder 1-6,18-110,112-113,115-116,118-119,121-155,179-378,380-380,398-398,414-414,421-462
Order 7-17,111-111,114-114,117-117,120-120,156-178,379-379,381-397,399-413,415-420,463-1304
SEG 65-75 ,706-716 ,1061-1066
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. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA (PubMed:12234937). Together with other U2 snRNP complex components may also play a role in the selective processing of microRNAs (miRNAs) from the long primary miRNA transcript, pri-miR-17-92 (By similarity). May also be involved in the assembly of the 'E' complex (PubMed:10882114). Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron (PubMed:15146077).