1IAT
CRYSTAL STRUCTURE OF HUMAN PHOSPHOGLUCOSE ISOMERASE/NEUROLEUKIN/AUTOCRINE MOTILITY FACTOR/MATURATION FACTOR
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001701 | biological_process | in utero embryonic development |
| A | 0001707 | biological_process | mesoderm formation |
| A | 0002639 | biological_process | positive regulation of immunoglobulin production |
| A | 0004347 | molecular_function | glucose-6-phosphate isomerase activity |
| A | 0005125 | molecular_function | cytokine activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006096 | biological_process | glycolytic process |
| A | 0006959 | biological_process | humoral immune response |
| A | 0007165 | biological_process | signal transduction |
| A | 0007599 | biological_process | hemostasis |
| A | 0007611 | biological_process | learning or memory |
| A | 0008083 | molecular_function | growth factor activity |
| A | 0010595 | biological_process | positive regulation of endothelial cell migration |
| A | 0016020 | cellular_component | membrane |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0031625 | molecular_function | ubiquitin protein ligase binding |
| A | 0032355 | biological_process | response to estradiol |
| A | 0032570 | biological_process | response to progesterone |
| A | 0033574 | biological_process | response to testosterone |
| A | 0034101 | biological_process | erythrocyte homeostasis |
| A | 0034774 | cellular_component | secretory granule lumen |
| A | 0035902 | biological_process | response to immobilization stress |
| A | 0035994 | biological_process | response to muscle stretch |
| A | 0042593 | biological_process | glucose homeostasis |
| A | 0043524 | biological_process | negative regulation of neuron apoptotic process |
| A | 0046686 | biological_process | response to cadmium ion |
| A | 0048029 | molecular_function | monosaccharide binding |
| A | 0051156 | biological_process | glucose 6-phosphate metabolic process |
| A | 0060170 | cellular_component | ciliary membrane |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0097367 | molecular_function | carbohydrate derivative binding |
| A | 1901135 | biological_process | carbohydrate derivative metabolic process |
| A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 602 |
| Chain | Residue |
| A | SER159 |
| A | HOH973 |
| A | SER209 |
| A | LYS210 |
| A | THR211 |
| A | THR214 |
| A | BME601 |
| A | HOH627 |
| A | HOH747 |
| A | HOH925 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 603 |
| Chain | Residue |
| A | ARG27 |
| A | ASN46 |
| A | HIS47 |
| A | HOH985 |
| A | HOH1056 |
| A | HOH1070 |
| A | HOH1161 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BME A 601 |
| Chain | Residue |
| A | GLY158 |
| A | GLY271 |
| A | GLN353 |
| A | SO4602 |
| A | HOH710 |
| A | HOH747 |
| A | HOH866 |
| A | HOH973 |
Functional Information from PROSITE/UniProt
| site_id | PS00174 |
| Number of Residues | 18 |
| Details | P_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GiIWdinsFDQwGVElgK |
| Chain | Residue | Details |
| A | GLY501-LYS518 |
| site_id | PS00765 |
| Number of Residues | 14 |
| Details | P_GLUCOSE_ISOMERASE_1 Phosphoglucose isomerase signature 1. DwVGGRYSLwSAIG |
| Chain | Residue | Details |
| A | ASP267-GLY280 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:11371164, ECO:0000269|PubMed:12573240, ECO:0000269|PubMed:12777791 |
| Chain | Residue | Details |
| A | GLU357 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:11371164, ECO:0000269|PubMed:12573240, ECO:0000269|PubMed:12777791 |
| Chain | Residue | Details |
| A | HIS388 | |
| A | LYS518 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P06745 |
| Chain | Residue | Details |
| A | GLY158 | |
| A | SER209 | |
| A | GLN353 | |
| A | GLU357 | |
| A | HIS388 | |
| A | LYS518 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylalanine => ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330 |
| Chain | Residue | Details |
| A | ALA1 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS11 | |
| A | LYS141 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29775581 |
| Chain | Residue | Details |
| A | LYS33 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER106 | |
| A | SER454 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | THR108 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by CK2 => ECO:0000269|PubMed:11004567, ECO:0000269|PubMed:15637053 |
| Chain | Residue | Details |
| A | SER184 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q6P6V0 |
| Chain | Residue | Details |
| A | THR249 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06745 |
| Chain | Residue | Details |
| A | LYS453 |
