Difference between revisions of "Phosphatase Family PHP"
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Several substrates have been reported, including ''beta'' subunit of heterotrimeric G proteins <cite>Maurer04</cite>, the metabolic enzyme adenosine 5’-triphosphate-citrate lyase (ACL) <cite>Klumpp03</cite>, and the Ca2+-activated K+ channel KCa3.1 <cite>Skolnik08</cite>. These are known or suspected substrates of the nucleoside diphosphate kinases ([http://kinase.com/wiki/index.php/Kinase_Group_NDK NDK]). | Several substrates have been reported, including ''beta'' subunit of heterotrimeric G proteins <cite>Maurer04</cite>, the metabolic enzyme adenosine 5’-triphosphate-citrate lyase (ACL) <cite>Klumpp03</cite>, and the Ca2+-activated K+ channel KCa3.1 <cite>Skolnik08</cite>. These are known or suspected substrates of the nucleoside diphosphate kinases ([http://kinase.com/wiki/index.php/Kinase_Group_NDK NDK]). | ||
| − | Its role in neuronal cells is particularly interesting. In ''C. elegans'', PHP is expressed exclusively in neurons <cite>Klumpp02</cite>. In human cells, the overexpression of PHPT1 decreases the activity of adenosine 5’-triphosphate-citrate lyase (ACL) and reduces the viability of neuronal cells <cite>Klumpp09</cite>. | + | Its role in neuronal cells is particularly interesting. Human PHP (PHPT1) is widely expressed across different tissues, most abundantly in cerebellum and pituitary, according to RNA-seq data from [http://www.gtexportal.org/home/gene/PHPT1 GTEx]. In ''C. elegans'', PHP is expressed exclusively in neurons <cite>Klumpp02</cite>. In human cells, the overexpression of PHPT1 decreases the activity of adenosine 5’-triphosphate-citrate lyase (ACL) and reduces the viability of neuronal cells <cite>Klumpp09</cite>. |
=== References === | === References === | ||
Revision as of 23:38, 1 June 2015
Phosphatase Classification: PHP Fold: PHP Superfamily: PHP Family
PHP is the only phosphatase known to be histidine-specific.
Evolution
PHP is found throughout eukaryotes, though lost from fungi. It is usually single copy per genome, but four are found in fruit fly.
Domain
PHP has a single domain: catalytic domain. The structure of the domain has been solved and a potential enzymatic mechanism proposed [1].
Functions
Several substrates have been reported, including beta subunit of heterotrimeric G proteins [2], the metabolic enzyme adenosine 5’-triphosphate-citrate lyase (ACL) [3], and the Ca2+-activated K+ channel KCa3.1 [4]. These are known or suspected substrates of the nucleoside diphosphate kinases (NDK).
Its role in neuronal cells is particularly interesting. Human PHP (PHPT1) is widely expressed across different tissues, most abundantly in cerebellum and pituitary, according to RNA-seq data from GTEx. In C. elegans, PHP is expressed exclusively in neurons [5]. In human cells, the overexpression of PHPT1 decreases the activity of adenosine 5’-triphosphate-citrate lyase (ACL) and reduces the viability of neuronal cells [6].
References
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