Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003729 | molecular_function | mRNA binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0004713 | molecular_function | protein tyrosine kinase activity |
| A | 0004715 | molecular_function | non-membrane spanning protein tyrosine kinase activity |
| A | 0004743 | molecular_function | pyruvate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005791 | cellular_component | rough endoplasmic reticulum |
| A | 0006096 | biological_process | glycolytic process |
| A | 0006417 | biological_process | regulation of translation |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030955 | molecular_function | potassium ion binding |
| A | 0032869 | biological_process | cellular response to insulin stimulus |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| A | 2000767 | biological_process | positive regulation of cytoplasmic translation |
Functional Information from PROSITE/UniProt
| site_id | PS00110 |
| Number of Residues | 13 |
| Details | PYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV |
| Chain | Residue | Details |
| A | ILE264-VAL276 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 224 |
| Details | Region: {"description":"Interaction with POU5F1","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 25 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P30613","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P00549","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P11980","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI16 |
| Number of Residues | 1 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI17 |
| Number of Residues | 3 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI18 |
| Number of Residues | 1 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| A | LYS269 | |
| A | SER361 | |
| A | ARG119 | |
| A | GLU363 | |
| A | ARG72 | |
| A | THR327 | |
