CATH Classification

Domain Context

CATH Clusters

Superfamily Protein tyrosine phosphatase superfamily
Functional Family Dual specificity protein phosphatase 14

Enzyme Information

3.1.3.16
Protein-serine/threonine phosphatase.
based on mapping to UniProt Q8NEJ0
[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).
3.1.3.48
Protein-tyrosine-phosphatase.
based on mapping to UniProt Q8NEJ0
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.

UniProtKB Entries (1)

Q8NEJ0
DUS18_HUMAN
Homo sapiens
Dual specificity protein phosphatase 18

PDB Structure

PDB 2ESB
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structure of human DSP18, a member of the dual-specificity protein tyrosine phosphatase family.
Jeong, D.G., Cho, Y.H., Yoon, T.S., Kim, J.H., Son, J.H., Ryu, S.E., Kim, S.J.
Acta Crystallogr.,Sect.D