×

Network disruptions

We have been experiencing disruptions on our local network which has affected the stability of these web pages. We have been working with IT support team to get this fixed as a matter of urgency and apologise for any inconvenience.

CATH Classification

Domain Context

CATH Clusters

Superfamily Protein tyrosine phosphatase superfamily
Functional Family Dual specificity phosphatase 10

Enzyme Information

3.1.3.48
Protein-tyrosine-phosphatase.
based on mapping to UniProt Q9Y6W6
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 Q9Y6W6
[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)

Q9Y6W6
DUS10_HUMAN
Homo sapiens
Dual specificity protein phosphatase 10

PDB Structure

PDB 1ZZW
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal Structure of the Catalytic Domain of Human MAP Kinase Phosphatase 5: Structural Insight into Constitutively Active Phosphatase.
Jeong, D.G., Yoon, T.S., Kim, J.H., Shim, M.Y., Jeong, S.K., Son, J.H., Ryu, S.E., Kim, S.J.
J.Mol.Biol.
CATH-Gene3D is a Global Biodata Core Resource Learn more...