Difference between revisions of "Phosphatase Family HP2"
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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_Histidine_Phosphatase|Histidine phosphatase superfamily]]: [[Phosphatase_Family_Histidine_Phosphatase_Branch2|HP, branch2 family]] | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_Histidine_Phosphatase|Histidine phosphatase superfamily]]: [[Phosphatase_Family_Histidine_Phosphatase_Branch2|HP, branch2 family]] | ||
− | + | Refer to Pfam ID [http://pfam.xfam.org/family/PF00328 PF00328] for general information. | |
− | ======ACPP====== | + | ====== ACPP ====== |
[http://www.ncbi.nlm.nih.gov/gene/55 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 <cite>ACPP_2</cite>. His-12 and Asp-258 of ACPP, but not Cys-183 or Cys-281, are required for the phosphatase activity <cite>ACPP_1</cite>. ACPP and its paralog [http://www.ncbi.nlm.nih.gov/gene/53 ACP2] is found in metazoan, choanoflagellida, amoebozoa and some protists, but is absent from fungi and plants. | [http://www.ncbi.nlm.nih.gov/gene/55 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 <cite>ACPP_2</cite>. His-12 and Asp-258 of ACPP, but not Cys-183 or Cys-281, are required for the phosphatase activity <cite>ACPP_1</cite>. ACPP and its paralog [http://www.ncbi.nlm.nih.gov/gene/53 ACP2] is found in metazoan, choanoflagellida, amoebozoa and some protists, but is absent from fungi and plants. | ||
+ | |||
+ | ====== PXYLP1 ====== | ||
+ | [http://www.ncbi.nlm.nih.gov/gene/?term=92370 PXYLP1] dephosphorylates [http://en.wikipedia.org/wiki/Xylose xylose], a sugar, in the glycosaminoglycan-protein linkage region of proteoglycans <cite>koike14</cite>. It is found in most metazoan, absent from fungi, plants and most protists, but ''Entamoeba histolytica'' and ''Emiliania huxleyi'' have PXYLP1 like genes. | ||
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#ACPP_1 pmid=11067847 | #ACPP_1 pmid=11067847 | ||
#ACPP_2 pmid=9705354 | #ACPP_2 pmid=9705354 | ||
+ | #koike14 pmid=24425863 | ||
</biblio> | </biblio> |
Revision as of 16:49, 17 June 2014
Phosphatase Classification: Histidine phosphatase superfamily: 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 |