5TOS
Botrytis-induced kinase 1 (BIK1) from Arabidopsis thaliana
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002221 | biological_process | pattern recognition receptor signaling pathway |
| A | 0002237 | biological_process | response to molecule of bacterial origin |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005730 | cellular_component | nucleolus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005768 | cellular_component | endosome |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0009620 | biological_process | response to fungus |
| A | 0010008 | cellular_component | endosome membrane |
| A | 0010119 | biological_process | regulation of stomatal movement |
| A | 0012505 | cellular_component | endomembrane system |
| A | 0016301 | molecular_function | kinase activity |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0045087 | biological_process | innate immune response |
| A | 0046777 | biological_process | protein autophosphorylation |
| A | 0050832 | biological_process | defense response to fungus |
| A | 0080141 | biological_process | regulation of jasmonic acid biosynthetic process |
| A | 0080142 | biological_process | regulation of salicylic acid biosynthetic process |
| A | 0106310 | molecular_function | protein serine kinase activity |
| A | 1900424 | biological_process | regulation of defense response to bacterium |
| B | 0002221 | biological_process | pattern recognition receptor signaling pathway |
| B | 0002237 | biological_process | response to molecule of bacterial origin |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005730 | cellular_component | nucleolus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005768 | cellular_component | endosome |
| B | 0005794 | cellular_component | Golgi apparatus |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0009620 | biological_process | response to fungus |
| B | 0010008 | cellular_component | endosome membrane |
| B | 0010119 | biological_process | regulation of stomatal movement |
| B | 0012505 | cellular_component | endomembrane system |
| B | 0016301 | molecular_function | kinase activity |
| B | 0042742 | biological_process | defense response to bacterium |
| B | 0045087 | biological_process | innate immune response |
| B | 0046777 | biological_process | protein autophosphorylation |
| B | 0050832 | biological_process | defense response to fungus |
| B | 0080141 | biological_process | regulation of jasmonic acid biosynthetic process |
| B | 0080142 | biological_process | regulation of salicylic acid biosynthetic process |
| B | 0106310 | molecular_function | protein serine kinase activity |
| B | 1900424 | biological_process | regulation of defense response to bacterium |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 34 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGGFGCVFkGwldestltptkpgtglviAVKK |
| Chain | Residue | Details |
| A | ILE73-LYS106 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViYrDIKasNILL |
| Chain | Residue | Details |
| A | VAL198-LEU210 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | ASP202 | |
| B | ASP202 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | ILE73 | |
| A | LYS105 | |
| B | ILE73 | |
| B | LYS105 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:30212650 |
| Chain | Residue | Details |
| A | SER26 | |
| B | SER34 | |
| B | SER193 | |
| B | SER219 | |
| A | SER32 | |
| A | SER33 | |
| A | SER34 | |
| A | SER193 | |
| A | SER219 | |
| B | SER26 | |
| B | SER32 | |
| B | SER33 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:30212650 |
| Chain | Residue | Details |
| A | THR35 | |
| B | THR50 | |
| B | THR64 | |
| B | THR341 | |
| B | THR375 | |
| B | THR377 | |
| A | THR42 | |
| A | THR50 | |
| A | THR64 | |
| A | THR341 | |
| A | THR375 | |
| A | THR377 | |
| B | THR35 | |
| B | THR42 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by autocatalysis and BAK1 => ECO:0000269|PubMed:24104392 |
| Chain | Residue | Details |
| A | SER48 | |
| B | SER48 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:24104392, ECO:0000269|PubMed:30212650 |
| Chain | Residue | Details |
| A | SER54 | |
| B | SER54 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:24104392, ECO:0000269|PubMed:30212650 |
| Chain | Residue | Details |
| A | THR56 | |
| A | THR314 | |
| B | THR56 | |
| B | THR314 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine; by autocatalysis and BAK1 => ECO:0000269|PubMed:24104392, ECO:0000269|PubMed:30212650 |
| Chain | Residue | Details |
| A | SER71 | |
| A | SER206 | |
| A | SER360 | |
| B | SER71 | |
| B | SER206 | |
| B | SER360 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by EFR => ECO:0000269|PubMed:29649442 |
| Chain | Residue | Details |
| A | SER89 | |
| A | SER129 | |
| B | SER89 | |
| B | SER129 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by EFR => ECO:0000269|PubMed:29649442 |
| Chain | Residue | Details |
| A | THR90 | |
| B | THR90 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by EFR => ECO:0000269|PubMed:29649442, ECO:0000269|PubMed:30212650 |
| Chain | Residue | Details |
| A | THR120 | |
| B | THR120 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:24532660 |
| Chain | Residue | Details |
| A | TYR150 | |
| A | TYR243 | |
| B | TYR150 | |
| B | TYR243 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:24104392, ECO:0000269|PubMed:30212650 |
| Chain | Residue | Details |
| A | TYR168 | |
| B | TYR168 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:24104392 |
| Chain | Residue | Details |
| A | TYR214 | |
| B | TYR214 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:23431184, ECO:0000269|PubMed:24104392, ECO:0000269|PubMed:30212650 |
| Chain | Residue | Details |
| A | SER233 | |
| B | SER233 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by autocatalysis and BAK1; alternate => ECO:0000269|PubMed:20413097, ECO:0000269|PubMed:23431184, ECO:0000269|PubMed:24104392, ECO:0000269|PubMed:30212650 |
| Chain | Residue | Details |
| A | SER236 | |
| B | SER236 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by autocatalysis and BAK1; alternate => ECO:0000269|PubMed:20404519, ECO:0000269|PubMed:23431184, ECO:0000269|PubMed:24104392 |
| Chain | Residue | Details |
| A | THR237 | |
| B | THR237 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by autocatalysis and BAK1 => ECO:0000269|PubMed:24104392 |
| Chain | Residue | Details |
| A | THR242 | |
| B | THR242 |
| site_id | SWS_FT_FI19 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:24104392, ECO:0000269|PubMed:24532660 |
| Chain | Residue | Details |
| A | TYR250 | |
| B | TYR250 |
| site_id | SWS_FT_FI20 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:24104392 |
| Chain | Residue | Details |
| A | SER252 | |
| A | SEP253 | |
| B | SER252 | |
| B | SEP253 |
| site_id | SWS_FT_FI21 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine; by autocatalysis and BAK1 => ECO:0000269|PubMed:24104392, ECO:0000269|PubMed:30212650 |
| Chain | Residue | Details |
| A | THR362 | |
| A | THR368 | |
| B | THR362 | |
| B | THR368 |
| site_id | SWS_FT_FI22 |
| Number of Residues | 2 |
| Details | LIPID: N-myristoyl glycine => ECO:0000305|PubMed:26021844 |
| Chain | Residue | Details |
| A | GLY2 | |
| B | GLY2 |
| site_id | SWS_FT_FI23 |
| Number of Residues | 2 |
| Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q9FE20 |
| Chain | Residue | Details |
| A | CYS4 | |
| B | CYS4 |
| site_id | SWS_FT_FI24 |
| Number of Residues | 20 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|DOI:10.1038/s41586-020-2210-3 |
| Chain | Residue | Details |
| A | LYS31 | |
| A | LYS366 | |
| B | LYS31 | |
| B | LYS41 | |
| B | LYS95 | |
| B | LYS170 | |
| B | LYS186 | |
| B | LYS286 | |
| B | LYS337 | |
| B | LYS358 | |
| B | LYS366 | |
| A | LYS41 | |
| A | LYS95 | |
| A | LYS170 | |
| A | LYS186 | |
| A | LYS286 | |
| A | LYS337 | |
| A | LYS358 |
