7UXV
human triosephosphate isomerase mutant G122R
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004807 | molecular_function | triose-phosphate isomerase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005615 | cellular_component | extracellular space |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006006 | biological_process | glucose metabolic process |
A | 0006094 | biological_process | gluconeogenesis |
A | 0006096 | biological_process | glycolytic process |
A | 0008929 | molecular_function | methylglyoxal synthase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0019242 | biological_process | methylglyoxal biosynthetic process |
A | 0019563 | biological_process | glycerol catabolic process |
A | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
A | 0031625 | molecular_function | ubiquitin protein ligase binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
A | 0061621 | biological_process | canonical glycolysis |
A | 0070062 | cellular_component | extracellular exosome |
B | 0004807 | molecular_function | triose-phosphate isomerase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005615 | cellular_component | extracellular space |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006006 | biological_process | glucose metabolic process |
B | 0006094 | biological_process | gluconeogenesis |
B | 0006096 | biological_process | glycolytic process |
B | 0008929 | molecular_function | methylglyoxal synthase activity |
B | 0016829 | molecular_function | lyase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0019242 | biological_process | methylglyoxal biosynthetic process |
B | 0019563 | biological_process | glycerol catabolic process |
B | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
B | 0031625 | molecular_function | ubiquitin protein ligase binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
B | 0061621 | biological_process | canonical glycolysis |
B | 0070062 | cellular_component | extracellular exosome |
Functional Information from PROSITE/UniProt
site_id | PS00171 |
Number of Residues | 11 |
Details | TIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG |
Chain | Residue | Details |
A | ALA163-GLY173 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Electrophile => ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000269|PubMed:8061610 |
Chain | Residue | Details |
A | HIS95 | |
B | HIS95 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000269|PubMed:8061610 |
Chain | Residue | Details |
A | GLU165 | |
B | GLU165 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10127, ECO:0000269|PubMed:8061610 |
Chain | Residue | Details |
A | ASN11 | |
A | LYS13 | |
B | ASN11 | |
B | LYS13 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS13 | |
A | LYS237 | |
B | LYS13 | |
B | LYS237 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:16807684, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER20 | |
B | SER20 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P17751 |
Chain | Residue | Details |
A | TYR67 | |
A | TYR208 | |
B | TYR67 | |
B | TYR208 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER79 | |
B | SER79 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P48500 |
Chain | Residue | Details |
A | SER105 | |
A | SER197 | |
B | SER105 | |
B | SER197 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P17751 |
Chain | Residue | Details |
A | LYS148 | |
B | LYS148 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17751 |
Chain | Residue | Details |
A | LYS155 | |
A | LYS193 | |
B | LYS155 | |
B | LYS193 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P17751 |
Chain | Residue | Details |
A | SER158 | |
B | SER158 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P17751 |
Chain | Residue | Details |
A | THR172 | |
B | THR172 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER211 | |
B | SER211 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | THR213 | |
B | THR213 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER222 | |
B | SER222 |
site_id | SWS_FT_FI16 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211 |
Chain | Residue | Details |
A | LYS141 | |
B | LYS141 |