Difference between revisions of "Phosphatase Family HP2"
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======[[Phosphatase_Subfamily_ PPIP5K| PPIP5K]] ====== | ======[[Phosphatase_Subfamily_ PPIP5K| PPIP5K]] ====== | ||
| + | PPIP5K has a pseudophosphatase domain which bind to PtdIns(3,4,5)P3 and a kinase domain of RimK superfamily. The proteins therefore show kinase activity which convert InsP6 and 5-InsP7 to 1-InsP7 and InsP8. | ||
===References=== | ===References=== | ||
Revision as of 04:08, 2 January 2015
Phosphatase Classification: Fold HP: Superfamily HP (histidine phosphatase): Family HP, branch 2
Refer to Pfam ID PF00328 for general information.
Contents
Subfamilies
ACP2
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.
MINPP1
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)
PXYLP1 dephosphorylates xylose, a sugar, in the glycosaminoglycan-protein linkage region of proteoglycans [1]. It is widely found in bilateria.
PPIP5K
PPIP5K has a pseudophosphatase domain which bind to PtdIns(3,4,5)P3 and a kinase domain of RimK superfamily. The proteins therefore show kinase activity which convert InsP6 and 5-InsP7 to 1-InsP7 and InsP8.
References
- 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 |
- 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 |
- 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 |
