Pseudophosphatases - Revision history

Gerard: /* HP fold */

2017-04-14T00:38:49Z

‎HP fold

Gerard at 00:38, 14 April 2017

2017-04-14T00:38:11Z

Gerard: /* Specifics */

2017-04-14T00:36:53Z

‎Specifics

Gerard: /* References */

2017-04-14T00:34:31Z

‎References

Gerard: /* List of pseudophosphatases */

2017-04-14T00:34:21Z

‎List of pseudophosphatases

Gerard at 00:31, 14 April 2017

2017-04-14T00:31:47Z

Gerard: /* Other folds */

2017-04-12T18:02:46Z

‎Other folds

Gerard: /* Other folds */

2017-04-12T18:01:58Z

‎Other folds

Gerard: /* List of pseudophosphatases */

2017-04-11T16:54:45Z

‎List of pseudophosphatases

Gerard: /* List of pseudophosphatases */

2017-04-11T16:53:39Z

‎List of pseudophosphatases

@@ Line 34: / Line 34: @@
-=== HP fold ===
+=== HP fold: HP1 family ===
-==== HP1 family ====
-−
 ===== PFKFB subfamily =====
 PFKFB has two enzymatic domains:  6-phosphofructo-2-kinase domain and fructose-2,6-bisphosphatase domain.

@@ Line 8: / Line 8: @@
 ===CC1 fold===
-CC1 fold phosphatases have an active site of CxxxxxR, and pseudophosphatases are computationally defined by loss of the C or R, which largely correlates with experimental evidence. Some CC1 phosphatases have dual domains, with one active and one an inactive pseudophosphatase domain. Subfamilies that have pseudophosphatase domains in human include:
+CC1 fold phosphatases have an active site of CxxxxxR, and pseudophosphatases are computationally defined by loss of the C or R, which largely correlates with experimental evidence <cite>Chen</cite>. Some CC1 phosphatases have dual domains, with one active and one an inactive pseudophosphatase domain. Subfamilies that have pseudophosphatase domains in human include:
 * [[Phosphatase_Subfamily_CDC14|CDC14]] subfamily, where CDC14A and CDC14B have dual phosphatase domains, with the first being a pseudophosphatase.
@@ Line 18: / Line 18: @@
 ===Other folds===
 (draft)
-* TIMM50 from the TIM50 subfamily (HAD/FCP) - predicted to be inactive, but shown experimentally to be a phosphatase
+* TIMM50 from the TIM50 subfamily (HAD/FCP) is predicted to be inactive, but shown experimentally to be a phosphatase
 * PFKFB3 from the HP fold (HP1/PFKFB)
-* PPIP5K1 and PPIP5K2 from HP fold (HP2/[[Phosphatase_Subfamily_PPIP5K|PPIP5K]] subfamily) - predicted to be active, but shown experimentally to be inactive
+* PPIP5K1 and PPIP5K2 from HP fold (HP2/[[Phosphatase_Subfamily_PPIP5K|PPIP5K]] subfamily) are predicted to be active, but shown experimentally to be inactive
 * PHLPP1 and PHLPP2 from the [[Phosphatase_Family_PPM|PPM]] fold/family are predicted computationally to be inactive, but shown experimentally to be active.
 * PPM fold phosphatases PP2D1 ([[Phosphatase_Subfamily_PP2D1|PP2D1]] subfamily) and TAB1 ([[Phosphatase_Subfamily_TAB1|TAB1]] subfamily).
@@ Line 31: / Line 31: @@
 ==== Auxilin subfamily ====
-There are two members of [[Phosphatase_Subfamily_Auxilin|auxilin subfamily]] in human, GAK and DNAJC6. Both GAK and DNAJC6 phosphatase domains have been shown to bind to phospholipids <cite>Lee, Kalli</cite>. The phosphatase domains of both are predicted to be inactive due to arginine in catalytic motif Cx5R is replaced by alanine.
+There are two human members of the [[Phosphatase_Subfamily_Auxilin|auxilin subfamily]], GAK and DNAJC6. Both GAK and DNAJC6 phosphatase domains have been shown to bind to phospholipids <cite>Lee, Kalli</cite>. The phosphatase domains of both are predicted to be inactive due to arginine in catalytic motif Cx5R is replaced by alanine.
@@ Line 57: / Line 57: @@
 #Lee pmid=16895969
 #Kalli pmid=23823232
 </biblio>

@@ Line 25: / Line 25: @@
 ==Specifics==
 ==== Auxilin subfamily ====
 There are two members of [[Phosphatase_Subfamily_Auxilin|auxilin subfamily]] in human, GAK and DNAJC6. Both GAK and DNAJC6 phosphatase domains have been shown to bind to phospholipids <cite>Lee, Kalli</cite>. The phosphatase domains of both are predicted to be inactive due to arginine in catalytic motif Cx5R is replaced by alanine.

@@ Line 50: / Line 50: @@
 #Manes05 pmid=15896703
 #Kretschmer93 pmid=8218176
 </biblio>

@@ Line 5: / Line 5: @@
-== List of pseudophosphatases ==
+== Pseudophosphatase Overview ==
 ===CC1 fold===
@@ Line 23: / Line 23: @@
 * PHLPP1 and PHLPP2 from the [[Phosphatase_Family_PPM|PPM]] fold/family are predicted computationally to be inactive, but shown experimentally to be active.
 * PPM fold phosphatases PP2D1 ([[Phosphatase_Subfamily_PP2D1|PP2D1]] subfamily) and TAB1 ([[Phosphatase_Subfamily_TAB1|TAB1]] subfamily).
 === HP fold ===

@@ Line 2: / Line 2: @@
   The page is incomplete.
-Pseudophosphatases are proteins with strong structural and sequence similarity to active phosphatases, but that have sequence changes to the active site that make them catalytically inactive. They are found in all eukaryotes and tend to be deeply conserved, suggesting that they continue to have important biological functions.
+Pseudophosphatases are proteins with strong structural and sequence similarity to active phosphatases, but that have sequence changes to the active site that make them catalytically inactive. They are found in all eukaryotes and tend to be deeply conserved <cite>Chen</cite>, suggesting that they continue to have important biological functions.
@@ Line 41: / Line 41: @@
 == References ==
 <biblio>
 #Cavalier12 pmid=22275052
 #Manes05 pmid=15896703
 #Kretschmer93 pmid=8218176
 </biblio>

@@ Line 16: / Line 16: @@
 * The [[Phosphatase_Family_PTP|PTP]] family contains several subfamilies of receptor PTPs with dual phosphatase domains. In all cases, the second (D2) domain is believed to be inactive. The Cx5R motif is lost in many (PTPRC, PTPRG, PTPRZ in human), and others have modifications to the conserved knrY domain that make them likely unable to bind phosphotyrosine substrates.
+===Other folds=== (draft)
-Other human pseudophosphatase domains (draft)
 * TIMM50 from the TIM50 subfamily (HAD/FCP) - predicted to be inactive, but shown experimentally to be a phosphatase
 * PFKFB3 from the HP fold (HP1/PFKFB)