Pseudophosphatases (obsolete) - Revision history

Gerard at 00:36, 14 April 2017

2017-04-14T00:36:00Z

2017-04-14T00:33:20Z

‎Auxilin subfamily

2017-04-14T00:33:07Z

‎References

2016-02-11T23:19:06Z

2015-12-08T20:17:27Z

2015-12-08T20:14:50Z

2015-10-02T17:50:15Z

2015-10-02T17:16:08Z

‎PTPRN subfamily

2015-10-02T16:44:07Z

‎PTPN14 subfamily

2015-10-02T16:36:43Z

‎References

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 ==== DSP3 subfamily: DUSP27 (1 out 5 members) ====
 The function of [[Phosphatase_Subfamily_DSP3#DUSP27|DUSP27]] is unknown, so is its catalytically inactive phosphatase domain.
 === Myotubularins ===
@@ Line 59: / Line 55: @@
 #Caromile10 pmid=20097759
 #denHertog02 pmid=12376545
 #Gingras09 pmid=19340315
 #Gokhale11 pmid=21222653
@@ Line 66: / Line 61: @@
 #Kharitidi13 pmid=24064037
 #Kim03 pmid=12668758
 #Lin11 pmid=21724833
 #Lu07 pmid=17560374

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 === PTEN-like phosphatases ===
 ==== Tensin subfamily: TNS1 and TNS2 (2 out of 3 members) ====
 The [[Phosphatase_Subfamily_Tensin|tensin subfamily]] has 3 members containing phosphatase domains, TNS1-3. TNS1 and TNS2 are predicted to be catalytically inactive, given the arginine residue is replaced by asparagine and lysine at CX<sub>5</sub>R motif, respectively. However, TNS2 has been reported to dephosphorylate IRS-1 <cite> Koh13 </cite>. The phosphatase domain of TNS1 mediates its interaction with PPP1CA in focal adhesions <cite>Eto07</cite>. TNS3 is predicted to be active as it has CX<sub>5</sub>R motif.

@@ Line 67: / Line 67: @@
 #Gross02 pmid=12364328
 #Guo04 pmid=15044455
 #Kharitidi13 pmid=24064037
 #Kim03 pmid=12668758
 #Koh13 pmid=23401856
 #Lin11 pmid=21724833
 #Lu07 pmid=17560374

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-{{TOC limit|4}}
+__TOC__
 == Human pseudophosphatases ==
 === PTPs ===

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+{{TOC limit|4}}
 == Human pseudophosphatases ==
 === PTPs ===

← Older revision	Revision as of 23:19, 11 February 2016
(No difference)

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 ==== PTPRN subfamily ====
-The [[Phosphatase_Subfamily_PTPRN|PTPRN subfamily]] has two members in human, PTPRN and PTPRN2. They have single phosphatase domain rather than two phosphatase domains as the members of PTPRA, PTPRC, PTPRD, PTPRK subfamilies. Their phosphatase domains mediate the interactions between them to form homo- and hetero-dimers <cite> Gross02</cite>. PTPRN2 also functions as a phosphatidylinositol phosphatase to regulate insulin secretion in mouse <cite> Caromile11 </cite>.
+The [[Phosphatase_Subfamily_PTPRN|PTPRN subfamily]] has two members in human, PTPRN and PTPRN2. They have single phosphatase domain rather than two phosphatase domains as the members of PTPRA, PTPRC, PTPRD, PTPRK subfamilies. Their phosphatase domains mediate the interactions between them to form homo- and hetero-dimers <cite> Gross02</cite>. PTPRN2 also functions as a phosphatidylinositol phosphatase to regulate insulin secretion in mouse <cite> Caromile10 </cite>.
 ==== PTPN14 subfamily ====
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 === Other families ===
 ==== TIM50 subfamily of HAD family ====
 ==== PPIP5K subfamily of HP2 family ====
 ==== TAB1 subfamily of PPM family ====
 == References ==
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 #Eto07 pmid=17435217
 #Gingras09 pmid=19340315
 #Kalli pmid=23823232
 #Kharitidi13 pmid=24064037
@@ Line 66: / Line 72: @@
 #Lee pmid=16895969
 #Lin11 pmid=21724833
 #marie10 pmid=21076391
 #Mariotti09 pmid=18762272

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 ==== PTPN14 subfamily ====
-The [[Phosphatase_Subfamily_PTPN14|PTPN14 subfamily]] has two members in human, PTPN14 and PTPN21. PTPN14 was shown to dephosphorylate p130Cas on Y128, a Src phosphorylation site <cite>Zhang13</cite>
+The [[Phosphatase_Subfamily_PTPN14|PTPN14 subfamily]] has two members in human, PTPN14 and PTPN21. Although PTPN14 and PTPN21 are supposed to lack enzymatic activity, PTPN14 has been shown to dephosphorylate p130Cas on Y128, a Src phosphorylation site <cite>Zhang13</cite>. It is worthy pointing out that the substitutions are found around WPD loop but not CX<sub>5</sub>R motif.
 ==== PTPN23 subfamily ====

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 #Reiterer13 pmid=23847209
 #Wishart98 pmid=9757831
 #zou09 pmid=19038970
 #zou12 pmid=22647598
 </biblio>