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IID00027
 UniprotP16104
ProteinHistone H2AX
GeneH2AX
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
143
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 78-86 Hetero trimer : P17693
 Evidence X-RAY 1ydp P Reference
       Region 1ydp P 78-86 order
Seq 78-86 Hetero tetramer : P17693
 Evidence X-RAY 2dyp C Reference
       Region 2dyp C 78-86 order
Seq 78-86 Hetero dodecamer : P17693
 Evidence X-RAY 2d31 F Reference
       Region 2d31 F 78-86 order
 Evidence X-RAY 2d31 C Reference
       Region 2d31 C 78-86 order
Seq 134-143 Hetero dimer : IID00568Complex
 Evidence X-RAY 2azm D Reference
       Region 2azm D 134-138 disorder
       Region 2azm D 139-143 order
 Evidence X-RAY 2azm C Reference
       Region 2azm C 134-138 disorder
       Region 2azm C 139-143 order
Seq 134-143 Hetero dimer : IID00516Complex
 Evidence X-RAY 3u3z B Reference
       Region 3u3z B 140-143 order
 Evidence X-RAY 3szm P Reference
       Region 3szm P 134-138 disorder
       Region 3szm P 139-143 order
 Evidence X-RAY 3szm O Reference
       Region 3szm O 134-137 disorder
       Region 3szm O 138-143 order
 Evidence X-RAY 3szm N Reference
       Region 3szm N 134-137 disorder
       Region 3szm N 138-143 order
 Evidence X-RAY 3szm M Reference
       Region 3szm M 134-137 disorder
       Region 3szm M 138-143 order
 Evidence X-RAY 3szm L Reference
       Region 3szm L 134-137 disorder
       Region 3szm L 138-143 order
 Evidence X-RAY 3szm K Reference
       Region 3szm K 134-138 disorder
       Region 3szm K 139-143 order
 Evidence X-RAY 3szm J Reference
       Region 3szm J 134-137 disorder
       Region 3szm J 138-143 order
 Evidence X-RAY 3szm I Reference
       Region 3szm I 134-137 disorder
       Region 3szm I 138-143 order
 Evidence X-RAY 3shv D Reference
       Region 3shv D 134-137 disorder
       Region 3shv D 138-143 order
 Evidence X-RAY 3shv C Reference
       Region 3shv C 134-137 disorder
       Region 3shv C 138-143 order
Seq 134-143 Hetero dimer : IID00483Complex
 Evidence X-RAY 3sqd D Reference
       Region 3sqd D 134-139 disorder
       Region 3sqd D 140-143 order
 Evidence X-RAY 3sqd C Reference
       Region 3sqd C 134-143 order
SeqProS possible 134-143 Same region of Saccharomyces homolog (P04908, 94%identity) is disordered in the free state. Hetero dimer : IID00483Complex
       Region 3sqd C 134-143 order
       Region 3sqd D 140-143 order
SeqProS possible 138-143 Same region of Saccharomyces homolog (P04908, 94%identity) is disordered in the free state. Hetero dimer : IID00516Complex
       Region 3shv C 138-143 order
       Region 3shv D 138-143 order
       Region 3szm I 138-143 order
       Region 3szm J 138-143 order
       Region 3szm K 139-143 order
       Region 3szm L 138-143 order
       Region 3szm M 138-143 order
       Region 3szm N 138-143 order
       Region 3szm O 138-143 order
       Region 3szm P 139-143 order
       Region 3u3z B 140-143 order
SeqProS possible 139-143 Same region of Saccharomyces homolog (P04908, 94%identity) is disordered in the free state. Hetero dimer : IID00568Complex
       Region 2azm C 139-143 order
       Region 2azm D 139-143 order
Seqphosphorylation
    2-2 Phosphoserine
    122-122 Phosphoserine
    140-140 Phosphoserine; by ATM
    143-143 Phosphotyrosine; by WSTF
Seqacetylation
    2-2 N-acetylserine
    6-6 N6-acetyllysine
    10-10 N6-acetyllysine
    37-37 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-22,118-143
Order 23-117
ProS 1-7,19-22
AlphaFold
Disorder 1-12,121-143
Order 13-120
Pfam Hmmer
PF00125 18-91 2.4e-32
SEG 2-22
Function
Function in SwissProt
Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C-terminal phosphorylation.
Biological Process
Diagram with PDB data
H2AX/MDC1Crystal structure of the MDC1 brct repeat in complex with the histone tail of gamma-H2AX
H2AX/MCPH1STRUCTURE OF HUMAN MICROCEPHALIN (MCPH1) TANDEM BRCT DOMAINS IN COMPLEX WITH A GAMMA-H2AX PHOSPHOPEPTIDE
H2AX/MCPH1Structure of human microcephalin (MCPH1) tandem BRCT domains in complex with an H2A.X peptide phosphorylated at Ser139 and Tyr142