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IID01009
UniprotQ96ST2
ProteinProtein IWS1 homolog
GeneIWS1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
819
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seqdisorder 352-548
 Evidence CD¸ NMR The unstructured character of the fragment was verified experimentally using CD spectroscopy, DSF and 1D 1H and 2D 15N/1H HSQC NMR spectra. Reference
       Region 352-548 disorder
Seq 447-471 Hetero dimer : P23193
 Evidence NMR 6zv4 A Reference
       Region 6zv4 A 447-471 order
       Region 6zv4 A 447-447 high_rmsd
       Region 6zv4 A 463-471 high_rmsd
Seq 447-548 Hetero dimer : IID00408Complex
 Evidence NMR 6emr A Reference
       Region 6emr A 447-548 order
       Region 6emr A 447-465 high_rmsd
       Region 6emr A 483-484 high_rmsd
       Region 6emr A 499-548 high_rmsd
Seq 550-692 Monomer :
 Evidence NMR 6zv1 A Reference
       Region 6zv1 A 550-692 order
       Region 6zv1 A 550-552 high_rmsd
       Region 6zv1 A 688-692 high_rmsd
SeqProS verified 448-462 The residues with high_rmsd are excluded from the ProS; TND (TFIIS N-terminal domain) binding Hetero dimer : P23193
       Region 6zv4 A 447-471 order
       Region 352-548 disorder
SeqProS verified 466-498 The N- and C-terminal residues with high_rmsd are excluded from the ProS; IBD (Integrase-binding domain) binding Hetero dimer : IID00408Complex
       Region 6emr A 447-548 order
       Region 352-548 disorder
Seqphosphorylation
    248-248 Phosphoserine
    513-513 Phosphoserine
    725-725 Phosphothreonine
    263-263 Phosphoserine
    261-261 Phosphoserine
    250-250 Phosphoserine
    511-511 Phosphoserine
    237-237 Phosphoserine
    235-235 Phosphoserine
    209-209 Phosphoserine
    198-198 Phosphoserine
    196-196 Phosphoserine
    183-183 Phosphoserine
    159-159 Phosphoserine
    157-157 Phosphoserine
    69-69 Phosphoserine
    54-54 Phosphoserine
    27-27 Phosphoserine
    377-377 Phosphoserine
    276-276 Phosphoserine
    287-287 Phosphoserine
    289-289 Phosphoserine
    300-300 Phosphoserine
    302-302 Phosphoserine
    304-304 Phosphoserine
    313-313 Phosphoserine
    315-315 Phosphoserine
    329-329 Phosphoserine
    333-333 Phosphoserine
    351-351 Phosphoserine
    362-362 Phosphoserine
    363-363 Phosphoserine
    365-365 Phosphoserine
    274-274 Phosphoserine
    398-398 Phosphoserine
    400-400 Phosphoserine
    415-415 Phosphoserine
    420-420 Phosphoserine
    422-422 Phosphoserine
    426-426 Phosphoserine
    435-435 Phosphothreonine
    438-438 Phosphoserine
    440-440 Phosphoserine
    461-461 Phosphoserine
    463-463 Phosphoserine
    465-465 Phosphoserine
    480-480 Phosphoserine
    489-489 Phosphothreonine
Seqacetylation
    1-1 N-acetylmethionine
 
Prediction
NeProc
Disorder 1-553,703-754,761-764,773-819
Order 554-702,755-760,765-772
ProS 1-27,49-58,472-498,507-533,547-553,703-710,729-734,742-754,761-764,784-796,807-819
AlphaFold
Disorder 1-526,539-553,693-701,709-709,711-740,759-759,761-763,770-785,802-812,814-814,816-817,819-819
Order 527-538,554-692,702-708,710-710,741-758,760-760,764-769,786-801,813-813,815-815,818-818
SEG 21-32 ,92-109 ,358-372 ,374-395 ,409-429 ,460-471 ,475-495 ,581-593
Function
Function in SwissProt
Transcription factor which plays a key role in defining the composition of the RNA polymerase II (RNAPII) elongation complex and in modulating the production of mature mRNA transcripts. Acts as an assembly factor to recruit various factors to the RNAPII elongation complex and is recruited to the complex via binding to the transcription elongation factor SUPT6H bound to the C-terminal domain (CTD) of the RNAPII subunit RPB1 (POLR2A). The SUPT6H:IWS1:CTD complex recruits mRNA export factors (ALYREF/THOC4, EXOSC10) as well as histone modifying enzymes (such as SETD2) to ensure proper mRNA splicing, efficient mRNA export and elongation-coupled H3K36 methylation, a signature chromatin mark of active transcription.