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IID00963
 UniprotQ01130
ProteinSerine/arginine-rich splicing factor 2
GeneSRSF2
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
221
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-101 Monomer :
 Evidence NMR 2lea A Reference
       Region 2lea A 1-101 order
       Region 2lea A 1-7 high_rmsd
       Region 2lea A 95-101 high_rmsd
 Evidence NMR 2leb A Reference
       Region 2leb A 1-101 order
       Region 2leb A 1-1 high_rmsd
       Region 2leb A 100-101 high_rmsd
 Evidence NMR 2lec A Reference
       Region 2lec A 1-101 order
       Region 2lec A 1-1 high_rmsd
       Region 2lec A 100-101 high_rmsd
Seq 9-101 Hetero dimer : P19909
 Evidence NMR 2kn4 A Reference
       Region 2kn4 A 9-101 order
       Region 2kn4 A 9-12 high_rmsd
       Region 2kn4 A 48-54 high_rmsd
       Region 2kn4 A 92-101 high_rmsd
Seqdisorder 1-8,94-101
 Evidence NMR The remaining parts of the SRSF2 N- and C-termini (aa 1-8 and 94-101, respectively) are flexible as confirmed by relaxation data (1H-15N NOE, Supplementary Figure S1A). Reference
       Region 1-8 disorder
       Region 94-101 disorder
SeqProS verified 2-8,94-99 Contact with RNA; the residues with high_rmsd are excluded from the ProS. :
       Region 2leb A 1-101 order
       Region 2lec A 1-101 order
       Region 1-8 disorder
       Region 94-101 disorder
Seqphosphorylation
    2-2 Phosphoserine
    22-22 Phosphothreonine
    25-25 Phosphothreonine
    26-26 Phosphoserine
    189-189 Phosphoserine
    191-191 Phosphoserine
    204-204 Phosphoserine
    206-206 Phosphoserine
    208-208 Phosphoserine
    212-212 Phosphoserine
    220-220 Phosphoserine
Seqacetylation
    2-2 N-acetylserine
    52-52 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-6,95-221
Order 7-94
ProS 1-6,106-136,142-152,206-216
AlphaFold
Disorder 1-11,52-53,92-221
Order 12-51,54-91
SEG 67-78 ,101-213
Function
Function in SwissProt
Necessary for the splicing of pre-mRNA. It is required for formation of the earliest ATP-dependent splicing complex and interacts with spliceosomal components bound to both the 5'- and 3'-splice sites during spliceosome assembly. It also is required for ATP-dependent interactions of both U1 and U2 snRNPs with pre-mRNA. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Binds to purine-rich RNA sequences, either 5'-AGSAGAGTA-3' (S=C or G) or 5'-GTTCGAGTA-3'. Can bind to beta-globin mRNA and commit it to the splicing pathway. The phosphorylated form (by SRPK2) is required for cellular apoptosis in response to cisplatin treatment.