8XY7
hPhK alpha-gamma subcomplex in active state
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004689 | molecular_function | phosphorylase kinase activity |
A | 0005516 | molecular_function | calmodulin binding |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0005964 | cellular_component | phosphorylase kinase complex |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0005977 | biological_process | glycogen metabolic process |
A | 0006091 | biological_process | generation of precursor metabolites and energy |
A | 0045819 | biological_process | positive regulation of glycogen catabolic process |
C | 0004672 | molecular_function | protein kinase activity |
C | 0004674 | molecular_function | protein serine/threonine kinase activity |
C | 0004689 | molecular_function | phosphorylase kinase activity |
C | 0005516 | molecular_function | calmodulin binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005829 | cellular_component | cytosol |
C | 0005964 | cellular_component | phosphorylase kinase complex |
C | 0005975 | biological_process | carbohydrate metabolic process |
C | 0005977 | biological_process | glycogen metabolic process |
C | 0006338 | biological_process | chromatin remodeling |
C | 0006468 | biological_process | protein phosphorylation |
C | 0016310 | biological_process | phosphorylation |
C | 0019899 | molecular_function | enzyme binding |
C | 0044024 | molecular_function | histone H2AS1 kinase activity |
C | 0050321 | molecular_function | tau-protein kinase activity |
C | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGVSSVVRrCihkptsqe..........YAVK |
Chain | Residue | Details |
C | LEU26-LYS49 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNILL |
Chain | Residue | Details |
C | ILE146-LEU158 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
Chain | Residue | Details |
C | ASP150 | |
A | SER1113 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
C | LEU26 | |
C | LYS49 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976 |
Chain | Residue | Details |
A | SER735 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
A | SER758 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER972 | |
A | SER985 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P18688 |
Chain | Residue | Details |
A | SER1007 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PKA => ECO:0000250|UniProtKB:P18688 |
Chain | Residue | Details |
A | SER1018 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P18688 |
Chain | Residue | Details |
A | SER1020 | |
A | SER1023 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | LIPID: S-farnesyl cysteine => ECO:0000250|UniProtKB:P18688 |
Chain | Residue | Details |
A | CYS1220 |