Phosphatase Subfamily LMWPTP - Revision history

Gerard: /* Catalytic activity and functions */

2015-05-31T04:39:51Z

‎Catalytic activity and functions

Gerard at 04:38, 31 May 2015

2015-05-31T04:38:27Z

Mark: Created page with "NOTOC Phosphatase Classification: Fold CC2: Superfamily CC2: Phosphatase_Family_L..."

2014-12-31T23:01:07Z

Created page with "__NOTOC__ Phosphatase Classification: Fold CC2: Superfamily CC2: Phosphatase_Family_L..."

New page

__NOTOC__
[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC2|Fold CC2]]: [[Phosphatase_Superfamily_CC2|Superfamily CC2]]: [[Phosphatase_Family_LMWPTP|Family LMWPTP]]: [[Phosphatase_Subfamily_LMWPTP|LMWPTP]]

'''L'''ow '''M'''olecular '''W'''eight '''P'''rotein '''T'''yrosine '''P'''hosphatase (LMWPTP) is a small protein (LMW) which dephosphorylates proteins on phospho-tyrosine. Most eukaryotic LMWPTP consist almost entirely of a phosphatase domain. The family has a single subfamily [[Phosphatase_Subfamily_LMWPTP|LMWPTP]].

=== Evolution ===
LMWPTP is present in most eukaryotes, though lost from from alveolates, trypanosoma, leishmania. It is also found in many bacteria and archaea. It is usually a single copy per genome.

=== Domain ===
LMWPTP has a single domain: phosphatase domain.

=== Catalytic activity and functions ===
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]. Yeast lacks classical TKs but the least homolog (LTP1) is a tyrosine-specific phosphatase and may dephosphorylate the immunophilin Fpr3 in vivo <cite>Magherini</cite>, on a residue likely phosphorylated by CK2 <cite>Wilson</cite>.

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 <cite>Fuhrmann</cite>. In many species, the LMWPTP is chromosomally adjacent to a fructosamine kinase, suggesting that it's major role is in protein deglycation <cite>Gemayel</cite>. E. coli Wzb is known to dephosphorylate the atypical tyrosine kinase Wzc <cite>Temel</cite>. YwlE from B. subtilis and CG31469 from Drosophila are LMWPTPs that have been shown to have arginine phosphatase activity <cite>Furhman, Furhman2</cite>.

=== References ===
<biblio>
#Temel pmid=23543749
#Gemayel pmid=17681011
#Van pmid=20967558
#Alho pmid=23584899
#Fuhrmann pmid=23838530
#Fuhrmann pmid=23770242
#Fortpied pmid=17472574
#Kikawa02 pmid=12167657
#Magherini pmid=15358193
#Wilson pmid=9148902
</biblio>

@@ Line 12: / Line 12: @@
 === Catalytic activity and functions ===
-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]. Yeast lacks classical TKs but the least homolog (LTP1) is a tyrosine-specific phosphatase and may dephosphorylate the immunophilin Fpr3 in vivo <cite>Magherini</cite>, on a residue likely phosphorylated by CK2 <cite>Wilson</cite>.
+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 deacylating 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]. Yeast lacks classical TKs but has an LMWPTP (LTP1) which is a tyrosine-specific phosphatase and may dephosphorylate the immunophilin Fpr3 in vivo <cite>Magherini</cite>, on a residue likely phosphorylated by CK2 <cite>Wilson</cite>.
 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 <cite>Fuhrmann</cite>. In many species, the LMWPTP is chromosomally adjacent to a fructosamine kinase, suggesting that it's major role is in protein deglycation <cite>Gemayel</cite>. E. coli Wzb is known to dephosphorylate the atypical tyrosine kinase Wzc <cite>Temel</cite>. YwlE from B. subtilis and CG31469 from Drosophila are LMWPTPs that have been shown to have arginine phosphatase activity <cite>Furhman, Furhman2</cite>.

@@ Line 3: / Line 3: @@
-'''L'''ow '''M'''olecular '''W'''eight '''P'''rotein '''T'''yrosine '''P'''hosphatase (LMWPTP) is a small protein (LMW) which dephosphorylates proteins on phospho-tyrosine. Most eukaryotic LMWPTP consist almost entirely of a phosphatase domain. The family has a single subfamily [[Phosphatase_Subfamily_LMWPTP|LMWPTP]].
+'''L'''ow '''M'''olecular '''W'''eight '''P'''rotein '''T'''yrosine '''P'''hosphatase (LMWPTP) is a small protein (LMW) phosphotyrosine protein phosphatase. Most eukaryotic LMWPTP consist almost entirely of a phosphatase domain. The family has a single subfamily [[Phosphatase_Subfamily_LMWPTP|LMWPTP]].
 === Evolution ===
-LMWPTP is present in most eukaryotes, though lost from from alveolates, trypanosoma, leishmania. It is also found in many bacteria and archaea. It is usually a single copy per genome.
+LMWPTP is present in most eukaryotes, though lost from from alveolates, and kinetoplastids. It is also found in many bacteria and archaea. It is usually a single copy per genome.
 === Domain ===
-LMWPTP has a single domain: phosphatase domain.
+LMWPTP consists almost entirely of a CC2 phosphatase domain.
 === Catalytic activity and functions ===

Phosphatase Subfamily LMWPTP - Revision history

Gerard: /* Catalytic activity and functions */

Gerard at 04:38, 31 May 2015

Mark: Created page with "__NOTOC__ Phosphatase Classification: Fold CC2: Superfamily CC2: Phosphatase_Family_L..."

Mark: Created page with "NOTOC Phosphatase Classification: Fold CC2: Superfamily CC2: Phosphatase_Family_L..."