Phosphatase Family HP2

Phosphatase Classification: Fold HP: Superfamily HP (histidine phosphatase): Family HP, branch 2 (HP2)

The histidine phosphatase, branch 2 (HP2) family is found throughout eukaryotes. It has subfamilies of protein phosphatases, non-protein phosphatases and pseudophosphatases. See also Pfam PF00328.

Subfamilies

• ACP2 is a protein phosphatase subfamily that usually has multiple copies per genome. Human has three copies with different tissue specificity. It is found in holozoa, ameobozoa, and some protists.

• ACP6

• MINPP1 is a non-protein phosphatase found in a broad of eukaryotes, including most metazoan and amoebazoan. Known substrates include InsP6 and 2,3-BPG.

• PXYLP1 (ACPL2) dephosphorylates xylose, a sugar, in the glycosaminoglycan-protein linkage region of proteoglycans [1]. It is widely found in bilateria.

• PPIP5K has a pseudophosphatase domain which bind to PtdIns(3,4,5)P3. It also has a kinase domain of RimK superfamily, which converts InsP6 and 5-InsP7 to 1-InsP7 and InsP8. PPIP5K is found throughout eukaryotes; vertebrates usually have two copies per genome.

• Cf60 is cellular slime mold specific pseudophosphatase. It encodes a secreted 450-kDa complex of proteins called counting factor (CF), through which Dictyostelium discoideum cells sense and regulate the size of groups and fruiting bodies using.

References

1. Koike T, Izumikawa T, Sato B, and Kitagawa H. Identification of phosphatase that dephosphorylates xylose in the glycosaminoglycan-protein linkage region of proteoglycans. J Biol Chem. 2014 Mar 7;289(10):6695-6708. DOI:10.1074/jbc.M113.520536 |
2. Zhang XQ, Lee MS, Zelivianski S, and Lin MF. Characterization of a prostate-specific tyrosine phosphatase by mutagenesis and expression in human prostate cancer cells. J Biol Chem. 2001 Jan 26;276(4):2544-50. DOI:10.1074/jbc.M006661200 |
3. Meng TC and Lin MF. Tyrosine phosphorylation of c-ErbB-2 is regulated by the cellular form of prostatic acid phosphatase in human prostate cancer cells. J Biol Chem. 1998 Aug 21;273(34):22096-104. DOI:10.1074/jbc.273.34.22096 |