Structure
atLeast majority ProS Experiment
:order disorder conflict PDB cluster ProS Pfam Domain SEG
136
order/disorder by at least rule
disorder by at least rule
order/disorder by majority rule
Seq 1-136 Hetero octamer : IID00016 Complex ,
IID00058 Complex
Region 3a6n E 1-38 disorder
Region 3a6n E 39-136 order
Region 3a6n A 1-38 disorder
Region 3a6n A 39-135 order
Region 3a6n A 136-136 disorder
Seq 2-8 Hetero trimer : IID00327 Complex
Region 3t6r D 7-8 disorder
Seq 2-22 Hetero trimer : IID00009 Complex
Region 2v1d C 18-22 disorder
Seq 17-36 Hetero trimer : IID00360 Complex
Region 4v2w C 17-25 disorder
Region 4v2w C 26-29 order
Region 4v2w C 30-36 disorder
Seq 26-30 Hetero dimer : IID00360 Complex
Region 4v2v C 26-30 order
Region 4v2v D 26-30 order
Seq 31-42 Hetero dimer : IID00360 Complex
Region 2ybs D 31-42 order
Region 2ybs C 31-42 order
Region 2ybp D 31-42 order
Region 2ybp C 31-42 order
Seq ProS verified 2-6 Hetero trimer : IID00327 Complex
Region 3a6n A 1-38 disorder
Seq ProS verified 2-17 Hetero trimer : IID00009 Complex
Region 3a6n A 1-38 disorder
Seq ProS verified 26-30 Hetero trimer : IID00360 Complex
Region 4v2w C 26-29 order
Region 3a6n A 1-38 disorder
Seq ProS verified 26-30 Hetero dimer : IID00360 Complex
Region 4v2v C 26-30 order
Region 4v2v D 26-30 order
Region 3a6n A 1-38 disorder
Seq ProS verified 31-38 Hetero dimer : IID00360 Complex
Region 2ybp C 31-42 order
Region 2ybp D 31-42 order
Region 2ybs C 31-42 order
Region 2ybs D 31-42 order
Region 3a6n A 1-38 disorder
4-4 Phosphothreonine; by HASPIN
7-7 Phosphothreonine; by PKC
11-11 Phosphoserine; alternate; by AURKB
12-12 Phosphothreonine; by PKC
29-29 Phosphoserine; alternate; by AURKB
5-5 N6-acetyllysine; alternate
10-10 N6-acetyllysine; alternate
15-15 N6-acetyllysine; alternate
19-19 N6-acetyllysine; alternate
24-24 N6-acetyllysine; alternate
28-28 N6-acetyllysine; alternate
37-37 N6-acetyllysine; alternate
57-57 N6-acetyllysine; alternate
80-80 N6-acetyllysine; alternate
116-116 N6-acetyllysine; alternate
123-123 N6-acetyllysine; alternate
Prediction
Disorder 1-3,7-35,135-136
Function
Function in SwissProt
Core component of nucleosome. 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.