Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000165 | biological_process | MAPK cascade |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0004707 | molecular_function | MAP kinase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006468 | biological_process | protein phosphorylation |
A | 0006970 | biological_process | response to osmotic stress |
A | 0016310 | biological_process | phosphorylation |
A | 0018105 | biological_process | peptidyl-serine phosphorylation |
A | 0032755 | biological_process | positive regulation of interleukin-6 production |
A | 0033554 | biological_process | cellular response to stress |
A | 0034644 | biological_process | cellular response to UV |
A | 0035556 | biological_process | intracellular signal transduction |
A | 0050729 | biological_process | positive regulation of inflammatory response |
A | 0051403 | biological_process | stress-activated MAPK cascade |
A | 0070301 | biological_process | cellular response to hydrogen peroxide |
A | 0071347 | biological_process | cellular response to interleukin-1 |
A | 0072709 | biological_process | cellular response to sorbitol |
A | 0072740 | biological_process | cellular response to anisomycin |
A | 0106310 | molecular_function | protein serine kinase activity |
A | 1903936 | biological_process | cellular response to sodium arsenite |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 25 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGSGAYGSVCsAidkrsgekv.........AIKK |
Chain | Residue | Details |
A | VAL31-LYS55 |
site_id | PS01351 |
Number of Residues | 103 |
Details | MAPK MAP kinase signature. FqseifakrayREllllkhmqhenviglldvftpasslrnfydfylvmpfmqtdlqkimgmefseekiqylvyqmlkglkyihsagvvh..........RDlKpgnlavnedC |
Chain | Residue | Details |
A | PHE60-CYS162 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | ASP150 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | VAL31 | |
A | LYS54 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18088087 |
Chain | Residue | Details |
A | SER47 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and MAP2K7 => ECO:0000269|PubMed:9374491 |
Chain | Residue | Details |
A | THR180 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and MAP2K7 => ECO:0000269|PubMed:9374491 |
Chain | Residue | Details |
A | TYR182 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195 |
Chain | Residue | Details |
A | SER350 |