7T7T
Structure of TSK/BRU1 bound to histone H3.1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005634 | cellular_component | nucleus |
A | 0006325 | biological_process | chromatin organization |
A | 0009933 | biological_process | meristem structural organization |
A | 0040029 | biological_process | epigenetic regulation of gene expression |
A | 0072423 | biological_process | response to DNA damage checkpoint signaling |
B | 0005634 | cellular_component | nucleus |
B | 0006325 | biological_process | chromatin organization |
B | 0009933 | biological_process | meristem structural organization |
B | 0040029 | biological_process | epigenetic regulation of gene expression |
B | 0072423 | biological_process | response to DNA damage checkpoint signaling |
W | 0000786 | cellular_component | nucleosome |
W | 0003677 | molecular_function | DNA binding |
W | 0030527 | molecular_function | structural constituent of chromatin |
W | 0046982 | molecular_function | protein heterodimerization activity |
X | 0000786 | cellular_component | nucleosome |
X | 0003677 | molecular_function | DNA binding |
X | 0030527 | molecular_function | structural constituent of chromatin |
X | 0046982 | molecular_function | protein heterodimerization activity |
Functional Information from PROSITE/UniProt
site_id | PS00322 |
Number of Residues | 7 |
Details | HISTONE_H3_1 Histone H3 signature 1. KAPRKQL |
Chain | Residue | Details |
X | LYS14-LEU20 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | SITE: Not N6-methylated => ECO:0000269|PubMed:15598823 |
Chain | Residue | Details |
X | LYS14 | |
W | LYS14 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | SITE: Not N6-acetylated => ECO:0000269|PubMed:15598823 |
Chain | Residue | Details |
X | LYS27 | |
X | LYS36 | |
W | LYS27 | |
W | LYS36 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Required for interaction with TSK => ECO:0000269|PubMed:35298257 |
Chain | Residue | Details |
X | ALA31 | |
W | ALA31 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12581305, ECO:0000269|PubMed:14712277, ECO:0000269|PubMed:15598823, ECO:0000269|PubMed:16258034 |
Chain | Residue | Details |
X | LYS4 | |
W | LYS4 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12456661, ECO:0000269|PubMed:12581305, ECO:0000269|PubMed:14712277, ECO:0000269|PubMed:15014946, ECO:0000269|PubMed:15598823 |
Chain | Residue | Details |
X | LYS9 | |
W | LYS9 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:14610360, ECO:0000269|PubMed:15753571 |
Chain | Residue | Details |
X | SER10 | |
X | SER28 | |
W | SER10 | |
W | SER28 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:15753571 |
Chain | Residue | Details |
X | THR11 | |
W | THR11 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:15598823, ECO:0000269|PubMed:16648464, ECO:0000269|PubMed:17174094, ECO:0000269|PubMed:17363895 |
Chain | Residue | Details |
X | LYS14 | |
W | LYS14 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:15598823 |
Chain | Residue | Details |
X | LYS18 | |
X | LYS23 | |
W | LYS18 | |
W | LYS23 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:14712277, ECO:0000269|PubMed:15598823, ECO:0000269|PubMed:17174094, ECO:0000269|PubMed:17439305, ECO:0000269|PubMed:19503079, ECO:0000269|PubMed:24626927, ECO:0000269|PubMed:35298257 |
Chain | Residue | Details |
X | LYS27 | |
W | LYS27 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:15598823, ECO:0000269|PubMed:16299497 |
Chain | Residue | Details |
X | LYS36 | |
W | LYS36 |