CATH Classification

Domain Context

CATH Clusters

Superfamily Rhodanese-like domain
Functional Family Dual specificity phosphatase 7

Enzyme Information

3.1.3.48
Protein-tyrosine-phosphatase.
based on mapping to UniProt Q16828
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.
-!- Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2.
3.1.3.16
Protein-serine/threonine phosphatase.
based on mapping to UniProt Q16828
[a protein]-serine/threonine phosphate + H(2)O = [a protein]- serine/threonine + phosphate.
-!- A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48). -!- The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1).

UniProtKB Entries (1)

Q16828
DUS6_HUMAN
Homo sapiens
Dual specificity protein phosphatase 6

PDB Structure

PDB 1HZM
External Links
Method SOLUTION NMR
Organism Escherichia
Primary Citation
Solution structure of ERK2 binding domain of MAPK phosphatase MKP-3: structural insights into MKP-3 activation by ERK2.
Farooq, A., Chaturvedi, G., Mujtaba, S., Plotnikova, O., Zeng, L., Dhalluin, C., Ashton, R., Zhou, M.M.
Mol.Cell
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