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IID00901
 UniprotQ7Z3B3
ProteinKAT8 regulatory NSL complex subunit 1
GeneKANSL1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
1105
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 585-598 Hetero trimer : IID00377Complex
 Evidence X-RAY 4cy2 D Reference
       Region 4cy2 D 585-596 order
       Region 4cy2 D 597-598 disorder
Seq 585-598 Hetero dimer : IID00377Complex
 Evidence X-RAY 4cy1 D Reference
       Region 4cy1 D 585-585 disorder
       Region 4cy1 D 586-598 order
 Evidence X-RAY 4cy1 C Reference
       Region 4cy1 C 585-585 disorder
       Region 4cy1 C 586-598 order
SeqProS predicted 585-598 This region is predicted to be disordered by AlphaFold and NeProc. Hetero trimer : IID00377Complex
       Region 4cy2 D 585-596 order
SeqProS predicted 585-598 This region is predicted to be disordered by AlphaFold and NeProc. Hetero dimer : IID00377Complex
       Region 4cy1 C 586-598 order
       Region 4cy1 D 586-598 order
Seqphosphorylation
    994-994 Phosphoserine
    249-249 Phosphoserine
    268-268 Phosphoserine
    991-991 Phosphoserine
    1003-1003 Phosphothreonine
    1045-1045 Phosphoserine
Seqacetylation
    104-104 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-68,119-283,331-420,486-663,683-862,872-876,899-1105
Order 70-88,95-118,284-330,421-485,664-682,863-871,877-898
ProS 1-20,37-68,119-139,153-160,169-181,208-218,280-283,350-356,361-401,486-510,516-522,542-555,587-638,653-663,683-698,704-708,720-725,736-749,786-792,850-862,905-939,946-969,1002-1009,1030-1053,1065-1075
AlphaFold
Disorder 1-278,329-374,400-427,478-478,484-591,597-649,686-858,860-860,869-877,880-880,885-885,887-887,890-890,892-909,937-1105
Order 279-328,375-399,428-477,479-483,592-596,650-685,859-859,861-868,878-879,881-884,886-886,888-889,891-891,910-936
SEG 2-15 ,34-48 ,164-175 ,404-417 ,827-850 ,942-954 ,975-988
Function
Function in SwissProt
As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription.