7QRD
Crystal structure of mouse CARM1 in complex with histone H3_10-25
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016274 | molecular_function | protein-arginine N-methyltransferase activity |
A | 0018216 | biological_process | peptidyl-arginine methylation |
B | 0016274 | molecular_function | protein-arginine N-methyltransferase activity |
B | 0018216 | biological_process | peptidyl-arginine methylation |
C | 0016274 | molecular_function | protein-arginine N-methyltransferase activity |
C | 0018216 | biological_process | peptidyl-arginine methylation |
D | 0016274 | molecular_function | protein-arginine N-methyltransferase activity |
D | 0018216 | biological_process | peptidyl-arginine methylation |
L | 0000786 | cellular_component | nucleosome |
L | 0003677 | molecular_function | DNA binding |
L | 0030527 | molecular_function | structural constituent of chromatin |
M | 0000786 | cellular_component | nucleosome |
M | 0003677 | molecular_function | DNA binding |
M | 0030527 | molecular_function | structural constituent of chromatin |
Functional Information from PROSITE/UniProt
site_id | PS00322 |
Number of Residues | 7 |
Details | HISTONE_H3_1 Histone H3 signature 1. KAPRKQL |
Chain | Residue | Details |
L | LYS14-LEU20 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:15735677, ECO:0000269|PubMed:15870105 |
Chain | Residue | Details |
L | SER10 | |
B | GLU215 | |
B | GLU244 | |
B | SER272 | |
C | GLN160 | |
C | ARG169 | |
C | GLY193 | |
C | GLU215 | |
C | GLU244 | |
C | SER272 | |
D | GLN160 | |
M | SER10 | |
D | ARG169 | |
D | GLY193 | |
D | GLU215 | |
D | GLU244 | |
D | SER272 | |
A | GLY193 | |
A | GLU215 | |
A | GLU244 | |
A | SER272 | |
B | GLN160 | |
B | ARG169 | |
B | GLY193 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by PKC and CHEK1 => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
L | THR11 | |
M | THR11 | |
C | SER217 | |
D | SER217 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
L | LYS14 | |
M | LYS14 | |
B | LYS228 | |
C | LYS228 | |
D | LYS228 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Citrulline; alternate => ECO:0000269|PubMed:15339660 |
Chain | Residue | Details |
L | ARG17 | |
M | ARG17 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:17194708 |
Chain | Residue | Details |
L | LYS18 | |
L | LYS23 | |
M | LYS18 | |
M | LYS23 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | LIPID: N6-decanoyllysine => ECO:0000250|UniProtKB:P68431 |
Chain | Residue | Details |
L | LYS18 | |
M | LYS18 |