Phosphatase Family LMWPTP - Revision history

Mark: /* Catalytic activity and functions */

2015-03-31T22:31:28Z

‎Catalytic activity and functions

Mark at 23:00, 31 December 2014

2014-12-31T23:00:49Z

Mark at 23:00, 31 December 2014

2014-12-31T23:00:30Z

Mark at 22:59, 31 December 2014

2014-12-31T22:59:17Z

Mark at 22:58, 31 December 2014

2014-12-31T22:58:08Z

Gerard at 20:24, 6 December 2014

2014-12-06T20:24:35Z

Mark at 01:11, 16 June 2014

2014-06-16T01:11:38Z

Mark at 04:44, 27 May 2014

2014-05-27T04:44:00Z

Gerard at 07:48, 1 May 2014

2014-05-01T07:48:25Z

Gerard at 05:01, 1 May 2014

2014-05-01T05:01:13Z

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 === 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 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 yeast 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>.

← Older revision		Revision as of 23:00, 31 December 2014
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	__NOTOC__		__NOTOC__
−	[[Phosphatase classification\|Phosphatase Classification]]: [[Phosphatase_Fold_CC2\|Fold CC2]] [[Phosphatase_Superfamily_CC2\|Superfamily CC2]]: [[Phosphatase_Family_LMWPTP\|Family LMWPTP]]	+	[[Phosphatase classification\|Phosphatase Classification]]: [[Phosphatase_Fold_CC2\|Fold CC2]]: [[Phosphatase_Superfamily_CC2\|Superfamily CC2]]: [[Phosphatase_Family_LMWPTP\|Family LMWPTP]]

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-'''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.
+'''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 ===
@@ Line 16: / Line 15: @@
 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 ===

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 __NOTOC__
-[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_CC2|Superfamily CC2]]: [[Phosphatase_Family_LMWPTP|Family LMWPTP]]
+[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC2|Fold CC2]] [[Phosphatase_Superfamily_CC2|Superfamily CC2]]: [[Phosphatase_Family_LMWPTP|Family 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.
@@ Line 17: / Line 18: @@
-== Reference ==
+=== References ===
 <biblio>
 #Temel pmid=23543749

← Older revision		Revision as of 22:58, 31 December 2014
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	'''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.		'''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.

−	~~LMWPTP is present in most eukaryotes, though lost from from alveolates, trypanosoma, leishmania. It is also found in many bacteria and archaea.~~

		+	=== 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 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>.

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 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>.
@@ Line 27: / Line 29: @@
 #Alho pmid=23584899
 #Fuhrmann pmid=23838530
 #Fortpied pmid=17472574
 #Kikawa02 pmid=12167657

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 __NOTOC__
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_Cys-based_III|Superfamily Cys-based III]]: [[Phosphatase_Family_LMWPTP|Family LMWPTP]]
 == Evolution ==
-The LMWPTP is present not only in eukaryotes but also prokaryotes. In eukaryotes, it is generally absent from alveolates, trypanosoma, leishmania.
+LMWPTP is present in most eukaryotes, though lost from from alveolates, trypanosoma, leishmania. It is also found in many bacteria and archaea.
 == Domain Structure ==
-Most LMWPTP consist almost entirely of a phosphatase domain
+Most eukaryotic LMWPTP consist almost entirely of a phosphatase domain.
 == Function ==