CATH Classification

Domain Context

CATH Clusters

Superfamily Protein tyrosine phosphatase superfamily
Functional Family Dual specificity phosphatase 13, isoform CRA_b

Enzyme Information

3.1.3.48
Protein-tyrosine-phosphatase.
based on mapping to UniProt Q9UII6
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 Q9UII6
[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)

Q9UII6
DS13B_HUMAN
Homo sapiens
Dual specificity protein phosphatase 13 isoform B

PDB Structure

PDB 2PQ5
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structure of Dual specificity protein phosphatase 13 (DUSP13).
Ugochukwu, E., Salah, E., Savitsky, P., Barr, A., Pantic, N., Niesen, F., Burgess-Brown, N., Berridge, G., Bunkoczi, G., Uppenberg, J., Pike, A.C.W., Sundstrom, M., Arrowsmith, C.H., Weigelt, J., Edwards, A., von Delft, F., Knapp, S.
To be Published