Phosphatase Subfamily MTMR1 - Revision history

Gerard at 23:54, 13 April 2017

2017-04-13T23:54:19Z

2017-04-13T23:54:00Z

‎Evolution

2016-09-09T14:54:03Z

‎Catalytic activity and functions

2016-09-07T16:07:15Z

‎Domain Structure

2016-09-07T15:55:36Z

‎Domain Structure

2016-03-09T06:09:27Z

‎Domain Structure

2016-03-09T06:06:00Z

‎Domain Structure

2016-03-09T06:05:26Z

‎Domain Structure

2016-03-09T06:04:24Z

‎Domain Structure

2016-03-09T06:02:27Z

‎Evolution

@@ Line 20: / Line 20: @@
 ===References===
 <biblio>
 #kim03 pmid=12668758
 #robinson05 pmid=15998640

@@ Line 6: / Line 6: @@
 ===Evolution===
-MTMR1 is found throughout holozoa. It consists of three members in human, MTM1, MTMR1 and MTMR2. In fruit fly and C elegans, a single copy is found. In most vertebrates from fish to human, MTM1 and MTMR1 are adjacent on the X chromosome (see [http://www.genomicus.biologie.ens.fr/genomicus-78.01/cgi-bin/phyloview.pl?root=2198950&amp;id=2199015&amp;xhide=108:107:105:110:69:96:97:63:111:-2198950:94:92:82:115:76:46:48:57:56:67:112:78:61:3:99:52:24:81:58:10:55:83&amp;xcollapse=-2198950&amp; Genomicus]).
+MTMR1 is found throughout holozoa <cite>Chen</cite>. It consists of three members in human, MTM1, MTMR1 and MTMR2. In fruit fly and C elegans, a single copy is found. In most vertebrates from fish to human, MTM1 and MTMR1 are adjacent on the X chromosome (see [http://www.genomicus.biologie.ens.fr/genomicus-78.01/cgi-bin/phyloview.pl?root=2198950&amp;id=2199015&amp;xhide=108:107:105:110:69:96:97:63:111:-2198950:94:92:82:115:76:46:48:57:56:67:112:78:61:3:99:52:24:81:58:10:55:83&amp;xcollapse=-2198950&amp; Genomicus]).
 ===Domain Structure===

@@ Line 12: / Line 12: @@
 ===Catalytic activity and functions===
-Human MTM1 has phosphatase activity towards the second messenger phosphatidylinositol 3-monophosphate [PI(3)P] in vitro and in human, budding yeast, and fission yeast <cite>taylor00, blondeau00</cite>.
+Human MTM1 has phosphatase activity towards the second messenger phosphatidylinositol 3-monophosphate [PI(3)P] in vitro and in human <cite>taylor00, blondeau00</cite>.
 Human MTMR1 and MTMR2 have been shown to dephosphorylate PI(3)P (<cite>bujbello02</cite> and <cite>kim01</cite>, respectively). Although the enzymatic properties of the three human phosphatases are indistinguishable, their functions are not totally redundant. MTM1 and MTMR2 are differentially regulated in the aspects of developmental expression and subcellular localization, resulting in their use of specific cellular pools of PI(3)P <cite>kim01</cite>.

@@ Line 9: / Line 9: @@
 ===Domain Structure===
-MTMR1 has a [http://pfam.xfam.org/family/PF02893.15 GRAM] domain, phosphatase domain and coiled-coil region. The GRAM domain is similar to the PH domain in structure and is found in membrane-associated proteins. As shown in [[Phosphatase_Subfamily_MTMR3|MTMR3 subfamily]], the GRAM domain can bind to phosphoinositide lipids. In Monosiga, the GRAM is replaced by a C1 domain, which is also a lipid-binding domain. The coiled-coil domain has been shown to mediate the interaction between [[Phosphatase_Gene_MTMR2|MTMR2]] and the [[Phosphatase_Subfamily_MTMR5|MTMR5 subfamily]] members MTMR13 and MTMR5 in human <cite>kim03, robinson05</cite>.
+MTMR1 has a [http://pfam.xfam.org/family/PF02893.15 GRAM] domain, phosphatase domain and coiled-coil region. The GRAM domain is similar to the PH domain in structure and is found in membrane-associated proteins. As shown in [[Phosphatase_Subfamily_MTMR3|MTMR3 subfamily]], the GRAM domain can bind to phosphoinositide lipids. The coiled-coil domain has been shown to mediate the interaction between [[Phosphatase_Gene_MTMR2|MTMR2]] and the [[Phosphatase_Subfamily_MTMR5|MTMR5 subfamily]] members MTMR13 and MTMR5 in human <cite>kim03, robinson05</cite>.
 ===Catalytic activity and functions===

@@ Line 9: / Line 9: @@
 ===Domain Structure===
-MTMR1 has a [http://pfam.xfam.org/family/PF02893.15 GRAM] domain, phosphatase domain and coiled-coil region. The GRAM domain is similar to the PH domain in structure and is found in membrane-associated proteins. As shown in [[Phosphatase_Subfamily_MTMR3|MTMR3 subfamily]], PH/GRAM domain can bind to phosphoinositide lipids. In Monosiga, the GRAM is replaced by a C1 domain, which is also a lipid-binding domain. The coiled-coil domain has been shown to mediate the interaction between [[Phosphatase_Gene_MTMR2|MTMR2]] and the [[Phosphatase_Subfamily_MTMR5|MTMR5 subfamily]] members MTMR13 and MTMR5 in human <cite>kim03, robinson05</cite>.
+MTMR1 has a [http://pfam.xfam.org/family/PF02893.15 GRAM] domain, phosphatase domain and coiled-coil region. The GRAM domain is similar to the PH domain in structure and is found in membrane-associated proteins. As shown in [[Phosphatase_Subfamily_MTMR3|MTMR3 subfamily]], the GRAM domain can bind to phosphoinositide lipids. In Monosiga, the GRAM is replaced by a C1 domain, which is also a lipid-binding domain. The coiled-coil domain has been shown to mediate the interaction between [[Phosphatase_Gene_MTMR2|MTMR2]] and the [[Phosphatase_Subfamily_MTMR5|MTMR5 subfamily]] members MTMR13 and MTMR5 in human <cite>kim03, robinson05</cite>.
 ===Catalytic activity and functions===