2WZJ
Catalytic and UBA domain of kinase MARK2/(Par-1) K82R, T208E double mutant
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004674 | molecular_function | protein serine/threonine kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
C | 0004672 | molecular_function | protein kinase activity |
C | 0004674 | molecular_function | protein serine/threonine kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006468 | biological_process | protein phosphorylation |
D | 0004672 | molecular_function | protein kinase activity |
D | 0004674 | molecular_function | protein serine/threonine kinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006468 | biological_process | protein phosphorylation |
E | 0004672 | molecular_function | protein kinase activity |
E | 0004674 | molecular_function | protein serine/threonine kinase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0006468 | biological_process | protein phosphorylation |
F | 0004672 | molecular_function | protein kinase activity |
F | 0004674 | molecular_function | protein serine/threonine kinase activity |
F | 0005524 | molecular_function | ATP binding |
F | 0006468 | biological_process | protein phosphorylation |
Functional Information from PROSITE/UniProt
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKaeNLLL |
Chain | Residue | Details |
A | ILE171-LEU183 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 234 |
Details | Domain: {"description":"UBA","evidences":[{"source":"PROSITE-ProRule","id":"PRU00212","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q9H0K1","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O08678","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"14517247","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 18 |
Details | Modified residue: {"description":"Phosphoserine; by CaMK1","evidences":[{"source":"PubMed","id":"17442826","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | Modified residue: {"description":"Phosphothreonine; by LKB1 and TAOK1","evidences":[{"source":"PubMed","id":"14517247","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
Details | Modified residue: {"description":"Phosphoserine; by GSK3-beta","evidences":[{"source":"PubMed","id":"14517247","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16257959","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18424437","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"14517247","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 6 |
Details | Modified residue: {"description":"Phosphothreonine; by CaMK1","evidences":[{"source":"PubMed","id":"17442826","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP175 | |
A | GLU179 |
site_id | CSA10 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
D | ASP175 | |
D | LYS177 |
site_id | CSA11 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
E | ASP175 | |
E | LYS177 |
site_id | CSA12 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
F | ASP175 | |
F | LYS177 |
site_id | CSA13 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | SER212 | |
A | ASP175 | |
A | LYS177 |
site_id | CSA14 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | SER212 | |
B | ASP175 | |
B | LYS177 |
site_id | CSA15 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
C | SER212 | |
C | ASP175 | |
C | LYS177 |
site_id | CSA16 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
D | SER212 | |
D | ASP175 | |
D | LYS177 |
site_id | CSA17 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
E | SER212 | |
E | ASP175 | |
E | LYS177 |
site_id | CSA18 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
F | SER212 | |
F | ASP175 | |
F | LYS177 |
site_id | CSA19 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP175 | |
A | ASN180 | |
A | LYS177 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP175 | |
B | GLU179 |
site_id | CSA20 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP175 | |
B | ASN180 | |
B | LYS177 |
site_id | CSA21 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
C | ASP175 | |
C | ASN180 | |
C | LYS177 |
site_id | CSA22 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
D | ASP175 | |
D | ASN180 | |
D | LYS177 |
site_id | CSA23 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
E | ASP175 | |
E | ASN180 | |
E | LYS177 |
site_id | CSA24 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
F | ASP175 | |
F | ASN180 | |
F | LYS177 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
C | ASP175 | |
C | GLU179 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
D | ASP175 | |
D | GLU179 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
E | ASP175 | |
E | GLU179 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
F | ASP175 | |
F | GLU179 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP175 | |
A | LYS177 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP175 | |
B | LYS177 |
site_id | CSA9 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
C | ASP175 | |
C | LYS177 |