Structure
atLeast majority ProS Experiment
   :order    disorder    conflict    PDB cluster    ProS    Pfam Domain    SEG143 
 order/disorder by at least rule
 
     disorder by at least rule
 
 order/disorder by majority rule
 
Seq  1-143 Hetero octamer : IID00058 Complex ,
IID00062 Complex ,
P06899 
 
       Region 6k1i  G 1-13 disorder 
       Region 6k1i  G 14-123 order 
       Region 6k1i  G 124-143 disorder 
       Region 6k1i  C 1-13 disorder 
       Region 6k1i  C 14-123 order 
       Region 6k1i  C 124-143 disorder 
Seq  1-143 Hetero octamer : IID00058 Complex ,
IID00062 Complex ,
P06899 
 
       Region 6k1j  G 1-13 disorder 
       Region 6k1j  G 14-123 order 
       Region 6k1j  G 124-143 disorder 
       Region 6k1j  C 1-13 disorder 
       Region 6k1j  C 14-125 order 
       Region 6k1j  C 126-143 disorder 
       Region 6k1k  G 1-9 disorder 
       Region 6k1k  G 10-123 order 
       Region 6k1k  G 124-143 disorder 
       Region 6k1k  C 1-14 disorder 
       Region 6k1k  C 15-125 order 
       Region 6k1k  C 126-143 disorder 
Seq  78-86 Hetero dodecamer : P17693 
 
       Region 2d31  F 78-86 order 
       Region 2d31  C 78-86 order 
Seq  78-86 Hetero tetramer : P17693 
 
       Region 2dyp  C 78-86 order 
Seq  78-86 Hetero trimer : P17693 
 
       Region 1ydp  P 78-86 order 
Seq  134-143 Hetero dimer : IID00568 Complex 
 
       Region 2azm  C 134-138 disorder 
       Region 2azm  C 139-143 order 
       Region 2azm  D 134-138 disorder 
       Region 2azm  D 139-143 order 
Seq  134-143 Hetero dimer : IID00516 Complex 
 
       Region 3shv  C 134-137 disorder 
       Region 3shv  C 138-143 order 
       Region 3shv  D 134-137 disorder 
       Region 3shv  D 138-143 order 
       Region 3szm  I 134-137 disorder 
       Region 3szm  I 138-143 order 
       Region 3szm  J 134-137 disorder 
       Region 3szm  J 138-143 order 
       Region 3szm  K 134-138 disorder 
       Region 3szm  K 139-143 order 
       Region 3szm  L 134-137 disorder 
       Region 3szm  L 138-143 order 
       Region 3szm  M 134-137 disorder 
       Region 3szm  M 138-143 order 
       Region 3szm  N 134-137 disorder 
       Region 3szm  N 138-143 order 
       Region 3szm  O 134-137 disorder 
       Region 3szm  O 138-143 order 
       Region 3szm  P 134-138 disorder 
       Region 3szm  P 139-143 order 
       Region 3u3z  B 140-143 order 
Seq  134-143 Hetero dimer : IID00483 Complex 
 
       Region 3sqd  C 134-143 order 
       Region 3sqd  D 134-139 disorder 
       Region 3sqd  D 140-143 order 
Seq  134-143 Hetero dodecamer : 
 
       Region 6zwk  L 134-137 disorder 
       Region 6zwk  L 138-143 order 
       Region 6zwk  K 134-136 disorder 
       Region 6zwk  K 137-143 order 
       Region 6zwk  J 134-136 disorder 
       Region 6zwk  J 137-143 order 
       Region 6zwk  I 134-137 disorder 
       Region 6zwk  I 138-143 order 
       Region 6zwk  H 134-136 disorder 
       Region 6zwk  H 137-143 order 
       Region 6zwk  G 134-137 disorder 
       Region 6zwk  G 138-143 order 
Seq ProS  verified 134-143  Hetero dimer : IID00483 Complex 
 
       Region 3sqd  C 134-143 order 
       Region 3sqd  D 140-143 order 
       Region 6k1i  C 124-143 disorder 
Seq ProS  verified 138-143  Hetero dimer : IID00516 Complex 
 
       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 
       Region 6k1i  C 124-143 disorder 
Seq ProS  verified 139-143  Hetero dimer : IID00568 Complex 
 
       Region 2azm  C 139-143 order 
       Region 2azm  D 139-143 order 
       Region 6k1i  C 124-143 disorder 
     140-140 Phosphoserine; by ATM
 
     143-143 Phosphotyrosine; by WSTF
 
 
 
 
 
 
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/MDC1 Crystal structure of the MDC1 brct repeat in complex with the histone tail of gamma-H2AX H2AX/MCPH1 STRUCTURE OF HUMAN MICROCEPHALIN (MCPH1) TANDEM BRCT DOMAINS IN COMPLEX WITH A GAMMA-H2AX PHOSPHOPEPTIDE H2AX/MCPH1 Structure of human microcephalin (MCPH1) tandem BRCT domains in complex 
with an H2A.X peptide phosphorylated at Ser139 and Tyr142