7OAT
Structural basis for targeted p97 remodelling by ASPL as prerequisite for p97 trimethylation by METTL21D
Functional Information from GO Data
Chain | GOid | namespace | contents |
B | 0005524 | molecular_function | ATP binding |
B | 0016887 | molecular_function | ATP hydrolysis activity |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006338 | biological_process | chromatin remodeling |
C | 0008168 | molecular_function | methyltransferase activity |
C | 0008276 | molecular_function | protein methyltransferase activity |
C | 0016279 | molecular_function | protein-lysine N-methyltransferase activity |
C | 0018022 | biological_process | peptidyl-lysine methylation |
C | 0018023 | biological_process | peptidyl-lysine trimethylation |
C | 0032259 | biological_process | methylation |
C | 0032780 | biological_process | negative regulation of ATP-dependent activity |
C | 0032991 | cellular_component | protein-containing complex |
C | 0042054 | molecular_function | histone methyltransferase activity |
C | 0051117 | molecular_function | ATPase binding |
Functional Information from PROSITE/UniProt
site_id | PS00674 |
Number of Residues | 19 |
Details | AAA AAA-protein family signature. ViVMaATNrpnsIDpALr.R |
Chain | Residue | Details |
B | VAL341-ARG359 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|Ref.9 |
Chain | Residue | Details |
C | TRP43 | |
C | GLY75 | |
C | ASP96 | |
C | TRP126 | |
C | ALA143 | |
C | TYR148 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
C | SER8 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
B | SER3 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
B | SER7 | |
B | SER13 | |
B | SER462 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195 |
Chain | Residue | Details |
B | SER37 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: N6,N6,N6-trimethyllysine; by VCPKMT => ECO:0000269|PubMed:22948820, ECO:0000269|PubMed:23349634 |
Chain | Residue | Details |
B | M3L315 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976 |
Chain | Residue | Details |
B | THR436 |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
B | LYS8 | |
B | LYS18 |