Difference between revisions of "Phosphatase Family HP2"

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(Created page with "Phosphatase Classification: Histidine phosphatase superfamily: Phosphatase_Family_Histidin...")
 
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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]]
  
One subfamily in this family has been reported as protein phosphatases. See Pfam ID [http://pfam.xfam.org/family/PF00328 PF00328] for general information.
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Refer to Pfam ID [http://pfam.xfam.org/family/PF00328 PF00328] for general information.
  
======ACPP======
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====== 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.
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====== PXYLP1 ======
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[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
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#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

  1. 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 | PubMed ID:9705354 | HubMed [ACPP_2]
  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 | PubMed ID:11067847 | HubMed [ACPP_1]
  3. 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 | PubMed ID:24425863 | HubMed [koike14]
All Medline abstracts: PubMed | HubMed