Difference between revisions of "Phosphatase Subfamily PXYLP1"

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(Functions)
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=== Functions ===
 
=== Functions ===
[http://www.ncbi.nlm.nih.gov/gene/?term=92370 Human PXYLP1] dephosphorylates [http://en.wikipedia.org/wiki/Xylose xylose], a sugar, in the glycosaminoglycan-protein linkage region of proteoglycans . In collaboration with kinase FAM20B, it regulates the transient phosphorylation of the Xyl residue in the glycosaminoglycan-protein linkage region, which controls the formation of glycosaminoglycan chains of proteoglycans <cite>koike14</cite>.  
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[http://www.ncbi.nlm.nih.gov/gene/?term=92370 Human PXYLP1] dephosphorylates [http://en.wikipedia.org/wiki/Xylose xylose], a sugar, in the glycosaminoglycan-protein linkage region of proteoglycans . In collaboration with kinase FAM20B, it regulates the transient phosphorylation of the Xyl residue in the glycosaminoglycan-protein linkage region, which controls the formation of glycosaminoglycan chains of proteoglycans <cite>koike14</cite>.
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=== Related kinase ===
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[http://kinase.com/wiki/index.php/FAM20B FAM20B].
  
 
=== References ===
 
=== References ===

Revision as of 22:00, 1 January 2015

Phosphatase Classification: Fold HP: Superfamily HP (histidine phosphatase): Family HP, branch 2: Subfamily PXYLP1

Evolution

PXYLP1 is found in bilateria, but Entamoeba histolytica and Emiliania huxleyi have PXYLP1 like genes.

Domain

PXYLP1 has a N-terminal transmembrane region and C-terminal phosphatase domain.

Functions

Human PXYLP1 dephosphorylates xylose, a sugar, in the glycosaminoglycan-protein linkage region of proteoglycans . In collaboration with kinase FAM20B, it regulates the transient phosphorylation of the Xyl residue in the glycosaminoglycan-protein linkage region, which controls the formation of glycosaminoglycan chains of proteoglycans [1].


Related kinase

FAM20B.

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 | PubMed ID:24425863 | HubMed [koike14]