Difference between revisions of "Phosphatase Family LMWPTP"
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== Function == | == Function == | ||
| − | In eukaryotes, LMWPTP dephosphorylates many receptor tyrosine kinases, such PDGFR, InsR, and Eph <cite>Kikawa02</cite>. It is a substrate for Src and Src phosphorylation creates a Grb2 SH2 domain-binding site. Accordingly it has been implicated in cancer progression <cite>Alho</cite>. Polymorphisms have also been implicated in metabolic and immune diseases. | + | In eukaryotes, LMWPTP dephosphorylates many receptor tyrosine kinases, such [http://kinase.com/wiki/index.php/Kinase_Subfamily_PDGFR PDGFR], [http://kinase.com/wiki/index.php/Kinase_Family_InsR InsR], and [http://kinase.com/wiki/index.php/Kinase_Family_Eph Eph] <cite>Kikawa02</cite>. It is a substrate for Src and Src phosphorylation creates a Grb2 SH2 domain-binding site. Accordingly it has been implicated in cancer progression <cite>Alho</cite>. Polymorphisms have also been implicated in metabolic and immune diseases. |
Human LMWPTP is also known to be a declycating agent, removing ribulose 5-phosphate from proteins <cite>Forpied, Van</cite>, in collaboration with [http://kinase.com/wiki/index.php/Kinase_Family_FruK Fructosamine Kinase]. | Human LMWPTP is also known to be a declycating agent, removing ribulose 5-phosphate from proteins <cite>Forpied, Van</cite>, in collaboration with [http://kinase.com/wiki/index.php/Kinase_Family_FruK Fructosamine Kinase]. | ||
Revision as of 04:12, 1 May 2014
Phosphatase Classification: Superfamily Cys-based III: Family LMWPTP
Evolution
The LMWPTP is present not only in eukaryotes but also prokaryotes. In eukaryotes, it is generally absent from alveolates, trypanosoma, leishmania.
Domain Structure
Most LMWPTP consist almost entirely of a phosphatase domain
Function
In eukaryotes, LMWPTP dephosphorylates many receptor tyrosine kinases, such PDGFR, InsR, and Eph [1]. It is a substrate for Src and Src phosphorylation creates a Grb2 SH2 domain-binding site. Accordingly it has been implicated in cancer progression [2]. Polymorphisms have also been implicated in metabolic and immune diseases.
Human LMWPTP is also known to be a declycating agent, removing ribulose 5-phosphate from proteins [3, 4], in collaboration with Fructosamine Kinase.
Yeast lacks classical TKs but the least homolog (LTP1) is a tyrosine-specific phosphatase and may dephosphorylate the immunophilin Fpr3 in vivo [5], on a residue likely phosphorylated by CK2 [6].
In prokaryotes, the molecular function is not fully understood. It is involved in the syntheisis and translocation of exopolysaccharides (EPS) and capsular polysaccharides (CPS) in E. coli. YwlE also acts as an arginine phosphatase [7]
Reference
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