1CM8
PHOSPHORYLATED MAP KINASE P38-GAMMA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000165 | biological_process | MAPK cascade |
A | 0000287 | molecular_function | magnesium ion binding |
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 | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005829 | cellular_component | cytosol |
A | 0006468 | biological_process | protein phosphorylation |
A | 0007165 | biological_process | signal transduction |
A | 0007517 | biological_process | muscle organ development |
A | 0010952 | biological_process | positive regulation of peptidase activity |
A | 0018105 | biological_process | peptidyl-serine phosphorylation |
A | 0035556 | biological_process | intracellular signal transduction |
A | 0042770 | biological_process | signal transduction in response to DNA damage |
A | 0045445 | biological_process | myoblast differentiation |
A | 0045786 | biological_process | negative regulation of cell cycle |
A | 0046872 | molecular_function | metal ion binding |
A | 0051149 | biological_process | positive regulation of muscle cell differentiation |
A | 0051726 | biological_process | regulation of cell cycle |
A | 0106310 | molecular_function | protein serine kinase activity |
B | 0000165 | biological_process | MAPK cascade |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004674 | molecular_function | protein serine/threonine kinase activity |
B | 0004707 | molecular_function | MAP kinase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005829 | cellular_component | cytosol |
B | 0006468 | biological_process | protein phosphorylation |
B | 0007165 | biological_process | signal transduction |
B | 0007517 | biological_process | muscle organ development |
B | 0010952 | biological_process | positive regulation of peptidase activity |
B | 0018105 | biological_process | peptidyl-serine phosphorylation |
B | 0035556 | biological_process | intracellular signal transduction |
B | 0042770 | biological_process | signal transduction in response to DNA damage |
B | 0045445 | biological_process | myoblast differentiation |
B | 0045786 | biological_process | negative regulation of cell cycle |
B | 0046872 | molecular_function | metal ion binding |
B | 0051149 | biological_process | positive regulation of muscle cell differentiation |
B | 0051726 | biological_process | regulation of cell cycle |
B | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 401 |
Chain | Residue |
A | ASN158 |
A | ASP171 |
A | ANP400 |
A | HOH2039 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 402 |
Chain | Residue |
A | ASP171 |
A | ANP400 |
A | HOH2152 |
A | HOH2153 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG B 1401 |
Chain | Residue |
B | ASP1171 |
B | ANP1400 |
B | ASN1158 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG B 1402 |
Chain | Residue |
B | ASP1171 |
B | ANP1400 |
B | HOH2118 |
site_id | AC5 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE ANP A 400 |
Chain | Residue |
A | VAL41 |
A | ALA54 |
A | LYS56 |
A | ILE87 |
A | MET109 |
A | PRO110 |
A | MET112 |
A | ASP115 |
A | LYS155 |
A | GLY157 |
A | ASN158 |
A | LEU170 |
A | ASP171 |
A | MG401 |
A | MG402 |
A | HOH2039 |
A | HOH2111 |
A | HOH2152 |
site_id | AC6 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE ANP B 1400 |
Chain | Residue |
B | VAL1041 |
B | ALA1054 |
B | LYS1056 |
B | ILE1087 |
B | MET1109 |
B | PRO1110 |
B | MET1112 |
B | ASP1115 |
B | LYS1155 |
B | GLY1157 |
B | ASN1158 |
B | LEU1170 |
B | ASP1171 |
B | MG1401 |
B | MG1402 |
B | HOH2002 |
B | HOH2037 |
B | HOH2053 |
B | HOH2185 |
B | HOH2186 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 25 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGSGAYGAVCsAvdgrtgakv.........AIKK |
Chain | Residue | Details |
A | VAL33-LYS57 |
site_id | PS01351 |
Number of Residues | 104 |
Details | MAPK MAP kinase signature. FqselfakrayRElrllkhmrhenviglldvftpdetlddftdfylvmpfmgtdlgklmkheklgedriqflvyqmlkglryihaagiih.........RDlKpgnlavnedC |
Chain | Residue | Details |
A | PHE62-CYS165 |
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 | ASP153 | |
B | ASP1153 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | VAL33 | |
A | LYS56 | |
B | VAL1033 | |
B | LYS1056 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by MAP2K3 and MAP2K6 => ECO:0000250|UniProtKB:Q63538 |
Chain | Residue | Details |
A | TPO183 | |
B | TPO1183 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | PTR185 | |
B | PTR1185 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | GLY157 | |
A | ASP153 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | GLY1157 | |
B | ASP1153 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | LYS155 | |
A | ASP153 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | LYS1155 | |
B | ASP1153 |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | LYS155 | |
A | THR188 | |
A | ASP153 |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | THR1188 | |
B | LYS1155 | |
B | ASP1153 |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | LYS155 | |
A | ASN158 | |
A | ASP153 |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | LYS1155 | |
B | ASN1158 | |
B | ASP1153 |