Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0004672 | molecular_function | protein kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
C | 0004672 | molecular_function | protein kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006468 | biological_process | protein phosphorylation |
D | 0004672 | molecular_function | protein kinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006468 | biological_process | protein phosphorylation |
E | 0004672 | molecular_function | protein kinase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0006468 | biological_process | protein phosphorylation |
F | 0004672 | molecular_function | protein kinase activity |
F | 0005524 | molecular_function | ATP binding |
F | 0006468 | biological_process | protein phosphorylation |
G | 0004672 | molecular_function | protein kinase activity |
G | 0005524 | molecular_function | ATP binding |
G | 0006468 | biological_process | protein phosphorylation |
H | 0004672 | molecular_function | protein kinase activity |
H | 0005524 | molecular_function | ATP binding |
H | 0006468 | biological_process | protein phosphorylation |
I | 0004672 | molecular_function | protein kinase activity |
I | 0005524 | molecular_function | ATP binding |
I | 0006468 | biological_process | protein phosphorylation |
J | 0004672 | molecular_function | protein kinase activity |
J | 0005524 | molecular_function | ATP binding |
J | 0006468 | biological_process | protein phosphorylation |
K | 0004672 | molecular_function | protein kinase activity |
K | 0005524 | molecular_function | ATP binding |
K | 0006468 | biological_process | protein phosphorylation |
L | 0004672 | molecular_function | protein kinase activity |
L | 0005524 | molecular_function | ATP binding |
L | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE MK2 A 500 |
Chain | Residue |
A | LEU70 |
A | THR206 |
A | ASP207 |
A | VAL78 |
A | LYS93 |
A | HIS108 |
A | MET138 |
A | GLU139 |
A | LEU141 |
A | ASP142 |
A | LEU193 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE MK2 B 500 |
Chain | Residue |
B | LEU70 |
B | VAL78 |
B | ALA91 |
B | LYS93 |
B | MET138 |
B | GLU139 |
B | LEU141 |
B | GLY144 |
B | LEU193 |
B | THR206 |
B | ASP207 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MK2 C 500 |
Chain | Residue |
C | LEU70 |
C | ALA91 |
C | LYS93 |
C | MET138 |
C | GLU139 |
C | LEU141 |
C | LEU193 |
C | THR206 |
C | ASP207 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE MK2 D 500 |
Chain | Residue |
D | LEU70 |
D | VAL78 |
D | LYS93 |
D | MET138 |
D | GLU139 |
D | LEU141 |
D | ASP142 |
D | LEU193 |
D | THR206 |
D | ASP207 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE MK2 E 500 |
Chain | Residue |
E | ALA91 |
E | LYS93 |
E | MET138 |
E | GLU139 |
E | CYS140 |
E | LEU141 |
E | ASP142 |
E | GLU145 |
E | LEU193 |
E | THR206 |
E | ASP207 |
site_id | AC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE MK2 F 500 |
Chain | Residue |
F | LEU70 |
F | VAL78 |
F | ALA91 |
F | LYS93 |
F | HIS108 |
F | MET138 |
F | GLU139 |
F | LEU141 |
F | ASP142 |
F | LEU193 |
F | THR206 |
F | ASP207 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE MK2 H 500 |
Chain | Residue |
H | LEU70 |
H | VAL78 |
H | LYS93 |
H | MET138 |
H | GLU139 |
H | LEU141 |
H | ASP142 |
H | LEU193 |
H | THR206 |
H | ASP207 |
site_id | AC8 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE MK2 I 500 |
Chain | Residue |
I | LEU70 |
I | GLY71 |
I | GLY73 |
I | VAL78 |
I | LYS93 |
I | MET138 |
I | GLU139 |
I | LEU141 |
I | ASP142 |
I | GLY144 |
I | LEU193 |
I | THR206 |
I | ASP207 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MK2 J 500 |
Chain | Residue |
J | LEU70 |
J | VAL78 |
J | LYS93 |
J | MET138 |
J | LEU141 |
J | ASP142 |
J | LEU193 |
J | THR206 |
J | ASP207 |
site_id | BC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE MK2 K 500 |
Chain | Residue |
K | LYS93 |
K | MET138 |
K | GLU139 |
K | LEU141 |
K | ASP142 |
K | GLY144 |
K | LEU193 |
K | THR206 |
K | ASP207 |
K | LEU70 |
K | GLY71 |
K | ALA91 |
site_id | BC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE MK2 L 500 |
Chain | Residue |
L | LEU70 |
L | VAL78 |
L | LYS93 |
L | HIS108 |
L | MET138 |
L | GLU139 |
L | LEU141 |
L | GLY144 |
L | THR206 |
L | ASP207 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGLGINGKVLqIfnkrtqek..........FALK |
Chain | Residue | Details |
A | LEU70-LYS93 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHrDVKpeNLLY |
Chain | Residue | Details |
A | ILE182-TYR194 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | ASP186 | |
J | ASP186 | |
K | ASP186 | |
L | ASP186 | |
B | ASP186 | |
C | ASP186 | |
D | ASP186 | |
E | ASP186 | |
F | ASP186 | |
G | ASP186 | |
H | ASP186 | |
I | ASP186 | |
Chain | Residue | Details |
A | LEU70 | |
E | LYS93 | |
F | LEU70 | |
F | LYS93 | |
G | LEU70 | |
G | LYS93 | |
H | LEU70 | |
H | LYS93 | |
I | LEU70 | |
I | LYS93 | |
J | LEU70 | |
A | LYS93 | |
J | LYS93 | |
K | LEU70 | |
K | LYS93 | |
L | LEU70 | |
L | LYS93 | |
B | LEU70 | |
B | LYS93 | |
C | LEU70 | |
C | LYS93 | |
D | LEU70 | |
D | LYS93 | |
E | LEU70 | |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: |
Chain | Residue | Details |
A | GLU139 | |
J | GLU139 | |
K | GLU139 | |
L | GLU139 | |
B | GLU139 | |
C | GLU139 | |
D | GLU139 | |
E | GLU139 | |
F | GLU139 | |
G | GLU139 | |
H | GLU139 | |
I | GLU139 | |
Chain | Residue | Details |
A | THR222 | |
J | THR222 | |
K | THR222 | |
L | THR222 | |
B | THR222 | |
C | THR222 | |
D | THR222 | |
E | THR222 | |
F | THR222 | |
G | THR222 | |
H | THR222 | |
I | THR222 | |
Chain | Residue | Details |
A | SER272 | |
J | SER272 | |
K | SER272 | |
L | SER272 | |
B | SER272 | |
C | SER272 | |
D | SER272 | |
E | SER272 | |
F | SER272 | |
G | SER272 | |
H | SER272 | |
I | SER272 | |
site_id | SWS_FT_FI6 |
Number of Residues | 12 |
Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000250 |
Chain | Residue | Details |
A | SER328 | |
J | SER328 | |
K | SER328 | |
L | SER328 | |
B | SER328 | |
C | SER328 | |
D | SER328 | |
E | SER328 | |
F | SER328 | |
G | SER328 | |
H | SER328 | |
I | SER328 | |
Chain | Residue | Details |
A | THR334 | |
J | THR334 | |
K | THR334 | |
L | THR334 | |
B | THR334 | |
C | THR334 | |
D | THR334 | |
E | THR334 | |
F | THR334 | |
G | THR334 | |
H | THR334 | |
I | THR334 | |
site_id | SWS_FT_FI8 |
Number of Residues | 24 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000269|PubMed:21131586 |
Chain | Residue | Details |
A | LYS353 | |
F | LYS353 | |
G | LYS353 | |
H | LYS353 | |
I | LYS353 | |
J | LYS353 | |
K | LYS353 | |
L | LYS353 | |
B | LYS353 | |
C | LYS353 | |
D | LYS353 | |
E | LYS353 | |