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IID00221
 UniprotQ96I25
ProteinSplicing factor 45
GeneRBM17
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
401
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 301-400 Hetero dimer :
 Evidence X-RAY 5lso A Reference
       Region 5lso A 301-400 order
Seq 301-400 Hetero dimer :
 Evidence X-RAY 5lso B Reference
       Region 5lso B 301-400 order
Seq 301-401 Monomer :
 Evidence X-RAY 2pe8 A Reference
       Region 2pe8 A 301-318 order
       Region 2pe8 A 319-321 disorder
       Region 2pe8 A 322-401 order
Seq 301-401 Hetero dimer : IID00190Complex
 Evidence X-RAY 2peh A Reference
       Region 2peh A 301-401 order
 Evidence X-RAY 2peh B Reference
       Region 2peh B 301-401 order
Seqphosphorylation
    222-222 Phosphoserine
    2-2 Phosphoserine
    71-71 Phosphothreonine
    155-155 Phosphoserine
    169-169 Phosphoserine
    237-237 Phosphothreonine
    266-266 Phosphoserine
    291-291 Phosphoserine
    293-293 Phosphoserine
Seqacetylation
    2-2 N-acetylserine
    21-21 N6-acetyllysine
    41-41 N6-acetyllysine; alternate
 
Prediction
NeProc
Disorder 1-107,143-299
Order 108-142,300-401
ProS 1-9,19-32,91-107,237-280
AlphaFold
Disorder 1-27,29-99,142-176,179-235,280-296
Order 28-28,100-141,177-178,236-279,297-401
Pfam Hmmer
PF01585 235-279 4.4e-13
SEG 109-139 ,149-166
Function
Function in SwissProt
Splice factor that binds to the single-stranded 3'AG at the exon/intron border and promotes its utilization in the second catalytic step. Involved in the regulation of alternative splicing and the utilization of cryptic splice sites. Promotes the utilization of a cryptic splice site created by the beta-110 mutation in the HBB gene. The resulting frameshift leads to sickle cell anemia.