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IID00538
 UniprotP10412
ProteinHistone H1.4
GeneH1-4
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
219
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 19-36 Hetero dimer : IID00245Complex
 Evidence X-RAY 3tzd T Reference
       Region 3tzd T 19-29 order
       Region 3tzd T 30-36 disorder
Seq 21-32 Hetero dimer : Q8N8U2
 Evidence X-RAY 5jjz B Reference
       Region 5jjz B 21-24 disorder
       Region 5jjz B 25-28 order
       Region 5jjz B 29-32 disorder
SeqProS possible 19-29 Same region of mouse homolog (P43274, 97%identity) is disordered in the free state (PubMed=11790831). Hetero dimer : Q8N8U2
       Region 5jjz B 25-28 order
SeqProS possible 19-29 Same region of mouse homolog (P43274, 97%identity) is disordered in the free state (PubMed=11790831). Hetero dimer : IID00245Complex
       Region 3tzd T 19-29 order
Seqphosphorylation
    2-2 Phosphoserine
    18-18 Phosphothreonine
    36-36 Phosphoserine
    146-146 Phosphothreonine
    187-187 Phosphoserine
Seqacetylation
    2-2 N-acetylserine
    17-17 N6-acetyllysine
    26-26 N6-acetyllysine; alternate
 
Prediction
NeProc
Disorder 1-40,98-219
Order 41-97
ProS 36-40,98-109
AlphaFold
Disorder 1-5,7-37,110-219
Order 6-6,38-109
Pfam Hmmer
PF00538 36-109 7.7e-32
SEG 5-15 ,21-37 ,59-69 ,109-219
Function
Function in SwissProt
Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity).