Difference between revisions of "Phosphatase Family HP2"
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| − | [[Phosphatase classification|Phosphatase Classification]]: | + | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_PGM|Fold PGM]]: [[Phosphatase_Superfamily_HP|Superfamily HP]] (histidine phosphatase): [[Phosphatase_Family_HP2|HP, branch2 family]] |
Refer to Pfam ID [http://pfam.xfam.org/family/PF00328 PF00328] for general information. | Refer to Pfam ID [http://pfam.xfam.org/family/PF00328 PF00328] for general information. | ||
Revision as of 21:11, 30 December 2014
Phosphatase Classification: Fold PGM: Superfamily HP (histidine phosphatase): HP, branch2 family
Refer to Pfam ID PF00328 for general information.
ACPP
ACPP (acid phosphatase, prostate) is a prostate epithelium-specific differentiation antigen, and is decreased in prostate carcinomas. It has been show to downregulate prostate cell growth by dephosphorylating phosphotyrosine on c-ErbB-2, an oncoprotein in prostate cells [1]. His-12 and Asp-258 of ACPP, but not Cys-183 or Cys-281, are required for the phosphatase activity [2]. ACPP and its paralog ACP2 is found in metazoan, choanoflagellida, amoebozoa and some protists, but is absent from fungi and plants.
PXYLP1
PXYLP1 dephosphorylates xylose, a sugar, in the glycosaminoglycan-protein linkage region of proteoglycans [3]. It is found in most metazoan, absent from fungi, plants and most protists, but Entamoeba histolytica and Emiliania huxleyi have PXYLP1 like genes.
References
- 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 |
- 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 |
- 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 |
