Phosphatase Family FCP - Revision history

Gerard at 04:43, 9 May 2016

2016-05-09T04:43:39Z

Mark at 03:58, 1 January 2015

2015-01-01T03:58:19Z

Mark at 03:52, 1 January 2015

2015-01-01T03:52:58Z

Gerard at 06:56, 30 December 2014

2014-12-30T06:56:27Z

Gerard at 05:29, 29 December 2014

2014-12-29T05:29:40Z

Gerard at 05:10, 29 December 2014

2014-12-29T05:10:02Z

Mark at 00:25, 7 May 2014

2014-05-07T00:25:17Z

Mark at 00:24, 7 May 2014

2014-05-07T00:24:22Z

Mark: Created page with "==Phosphatase Classification: FCP== The FCP family is named after subfamily FCP1. It contains five catalytically acti..."

2014-03-14T18:09:08Z

Created page with "==Phosphatase Classification: FCP== The FCP family is named after subfamily FCP1. It contains five catalytically acti..."

New page

==[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Family_FCP|FCP]]==
The FCP family is named after subfamily FCP1. It contains five catalytically active families, and one inactive one (TIMM50). Four of the five catalytically active families show phosphatase activity toward the C-terminal domain (CTD) of RNA polymerase II (Pol II). The CTD, found only in eukaryotes, consists of tandem repeated heptapeptide segments usually of a consensus sequence YSPTSPS, and the different phosphorylation patterns that predominate at each stage of transcription recruit the appropriate set of mRNA-processing and histone-modifying factors. FCP1 and SCP have different preference over pSer2 and pSer5, which may be important for regulating phosphorylation patterns. See [[CTD_Phosphorylation|Phosphorylation of RNA polymerase II C-terminal domain]].

===[[FCP1]]===
F-cell production 1 (FCP1) also called TFIIF-stimulated CTD phosphatase 1, prefers to dephosphorylate pSer2 of heptapeptide repeats at CTD of RNA polymerase II.

===[[SCP]]===
SCP is named after Small CTD (carboxy-terminal domain, RNA polymerase II, polypeptide A) phosphatase. This subfamily has three members in human, SCP1 (or CTDSP1), SCP2 (or CTDSP2), and SCP3 (or CTDSPL). The SCP1 prefers to dephosphorylate pSer5 at CTD, while FCP1 prefers pSer2.

===[[Dullard]]===
Dullard, is also known as CTDNEP1 (CTD nuclear envelope phosphatase 1). However, its known substrate is lipin rather than RNA polymerase II CTD. The kinase of yeast lipin, SMP2, is Cdc28/cdk1.

===[[HSPC129]]===
HSPC129 is also known as HSPC058, and CTDSPL2 (CTD small phosphatase like 2). It has not been well characterized, though in vitro assay showed its phosphatase activity toward CTD.

===[[UBLCP1]]===
UBLCP1 is named after Ubiquitin-like domain containing CTD phosphatase 1. It has not been well characterized. It has a N-terminal domain similar to ubiquitin. Its putative substrate is RNA polymerase II C-terminal domain.

===[[TIMM50]]===
TIMM50, translocase of inner mitochondrial membrane 50 homolog. Catalytically inactive.

== DxDxT motif ==
The pattern of DxDxT motif are obtained from eight organisms, yeast, Monosiga, sponge, anemone, worm, fly, sea urchin, and human.

{| class="wikitable" border="2" style="background: #ffffff; border: 1px #000000 solid; border-collapse: collapse; font-size: 100%;" cellpadding="5" cellspacing="10"
|-
!bgcolor="#ffffff" rowspan="1" align="center" |Subfamily|| bgcolor="#ffffff" colspan="1" align="center" |Motif pattern|| bgcolor="#ffffff" colspan="1" align="left"| Note
|-
!bgcolor="#ffffff" rowspan="1" align="center" |FCP1|| bgcolor="#ffffff" colspan="1" align="center" |DLDQT|| bgcolor="#ffffff" colspan="1" align="center"|
|-
!bgcolor="#ffffff" rowspan="1" align="center" |SCP|| bgcolor="#ffffff" colspan="1" align="center" |DLDET|| bgcolor="#ffffff" colspan="1" align="center"|
|-
!bgcolor="#ffffff" rowspan="1" align="center" |Dullard|| bgcolor="#ffffff" colspan="1" align="center" |DLDET|| bgcolor="#ffffff" colspan="1" align="center"| Exceptionally, one of the three fly Dullards has DMDNT.
|-
!bgcolor="#ffffff" rowspan="1" align="center" |HSPC129|| bgcolor="#ffffff" colspan="1" align="center" |DLDET|| bgcolor="#ffffff" colspan="1" align="center"|
|-
!bgcolor="#ffffff" rowspan="1" align="center" |UBLCP1|| bgcolor="#ffffff" colspan="1" align="center" |D[I|V]DYT|| bgcolor="#ffffff" colspan="1" align="center"|
|-
!bgcolor="#ffffff" rowspan="1" align="center" |TIMM50|| bgcolor="#ffffff" colspan="1" align="center" |-|| bgcolor="#ffffff" colspan="1" align="left"| Not very conserved.
|-
}

@@ Line 2: / Line 2: @@
 __NOTOC__
-FCP contains five catalytically active families, and one inactive one (TIMM50). Four of the five catalytically active families show phosphatase activity toward the C-terminal domain (CTD) of RNA polymerase II (Pol II). The CTD consists of tandem repeated heptapeptide segments usually of a consensus sequence YSPTSPS, and the different phosphorylation patterns that predominate at each stage of transcription recruit the appropriate set of mRNA-processing and histone-modifying factors. FCP1 and SCP have different preference over pSer2 and pSer5, which may be important for regulating phosphorylation patterns. See [[CTD_Phosphorylation|Phosphorylation of RNA polymerase II C-terminal domain]].
+FCP contains five catalytically active subfamilies, and one inactive one (TIMM50). Four of the five catalytically active subfamilies act on the C-terminal domain (CTD) of RNA polymerase II (Pol II). The CTD consists of tandem repeated heptapeptide segments of a consensus YSPTSPS sequence, and the different phosphorylation patterns that predominate at each stage of transcription recruit the appropriate set of mRNA-processing and histone-modifying factors. FCP1 and SCP have different preference over pSer2 and pSer5. See [[CTD_Phosphorylation|Phosphorylation of RNA polymerase II C-terminal domain]].
 ===[[Phosphatase_Subfamily_FCP1|FCP1]]===

@@ Line 1: / Line 1: @@
-[[Phosphatase classification|Phosphatase Classification]]:  [[Phosphatase_Superfamily_HAD|Superfamily HAD]]: [[Phosphatase_Family_FCP|Family FCP]]
+[[Phosphatase classification|Phosphatase Classification]]:  [[Phosphatase_Fold_HAD|Fold HAD]]: [[Phosphatase_Superfamily_HAD|Superfamily HAD]]: [[Phosphatase_Family_FCP|Family FCP]]
 __NOTOC__
 FCP contains five catalytically active families, and one inactive one (TIMM50). Four of the five catalytically active families show phosphatase activity toward the C-terminal domain (CTD) of RNA polymerase II (Pol II). The CTD consists of tandem repeated heptapeptide segments usually of a consensus sequence YSPTSPS, and the different phosphorylation patterns that predominate at each stage of transcription recruit the appropriate set of mRNA-processing and histone-modifying factors. FCP1 and SCP have different preference over pSer2 and pSer5, which may be important for regulating phosphorylation patterns. See [[CTD_Phosphorylation|Phosphorylation of RNA polymerase II C-terminal domain]].

@@ Line 1: / Line 1: @@
-[[Phosphatase classification|Phosphatase Classification]]:  [[Phosphatase_Group_HAD|Superfamily HAD]]: [[Phosphatase_Family_FCP|Family FCP]]
+[[Phosphatase classification|Phosphatase Classification]]:  [[Phosphatase_Superfamily_HAD|Superfamily HAD]]: [[Phosphatase_Family_FCP|Family FCP]]
 __NOTOC__
 FCP contains five catalytically active families, and one inactive one (TIMM50). Four of the five catalytically active families show phosphatase activity toward the C-terminal domain (CTD) of RNA polymerase II (Pol II). The CTD consists of tandem repeated heptapeptide segments usually of a consensus sequence YSPTSPS, and the different phosphorylation patterns that predominate at each stage of transcription recruit the appropriate set of mRNA-processing and histone-modifying factors. FCP1 and SCP have different preference over pSer2 and pSer5, which may be important for regulating phosphorylation patterns. See [[CTD_Phosphorylation|Phosphorylation of RNA polymerase II C-terminal domain]].

@@ Line 12: / Line 12: @@
 Dullard, is also known as CTDNEP1 (CTD nuclear envelope phosphatase 1). However, its known substrate is lipin rather than RNA polymerase II CTD. The kinase of yeast lipin, SMP2, is Cdc28/cdk1.
-===[[Phosphatase_Subfamily_HSPC129|HSPC129]]===
+===[[Phosphatase_Subfamily_CTDSPL2|CTDSPL2]]===
-HSPC129 is also known as HSPC058, and CTDSPL2 (CTD small phosphatase like 2). It has not been well characterized, though in vitro assay showed its phosphatase activity on the CTD.
+A poorly-described but almost pan-eukaryotic CTD phosphatase.
 ===[[Phosphatase_Subfamily_UBLCP1|UBLCP1]]===

@@ Line 3: / Line 3: @@
 FCP contains five catalytically active families, and one inactive one (TIMM50). Four of the five catalytically active families show phosphatase activity toward the C-terminal domain (CTD) of RNA polymerase II (Pol II). The CTD consists of tandem repeated heptapeptide segments usually of a consensus sequence YSPTSPS, and the different phosphorylation patterns that predominate at each stage of transcription recruit the appropriate set of mRNA-processing and histone-modifying factors. FCP1 and SCP have different preference over pSer2 and pSer5, which may be important for regulating phosphorylation patterns. See [[CTD_Phosphorylation|Phosphorylation of RNA polymerase II C-terminal domain]].
-===[[FCP1]]===
+===[[Phosphatase_Subfamily_FCP1|FCP1]]===
 F-cell production 1 (FCP1) also called TFIIF-stimulated CTD phosphatase 1, prefers to dephosphorylate pSer2 of the CTD
-===[[SCP]]===
+===[[Phosphatase_Subfamily_SCP|SCP]]===
 SCP is named after Small CTD (carboxy-terminal domain, RNA polymerase II, polypeptide A) phosphatase. This subfamily has three members in human, SCP1 (or CTDSP1), SCP2 (or CTDSP2), and SCP3 (or CTDSPL). SCP1 prefers to dephosphorylate pSer5.
-===[[Dullard]]===
+===[[Phosphatase_Subfamily_Dullard|Dullard]]===
 Dullard, is also known as CTDNEP1 (CTD nuclear envelope phosphatase 1). However, its known substrate is lipin rather than RNA polymerase II CTD. The kinase of yeast lipin, SMP2, is Cdc28/cdk1.
-===[[HSPC129]]===
+===[[Phosphatase_Subfamily_HSPC129|HSPC129]]===
 HSPC129 is also known as HSPC058, and CTDSPL2 (CTD small phosphatase like 2). It has not been well characterized, though in vitro assay showed its phosphatase activity on the CTD.
-===[[UBLCP1]]===
+===[[Phosphatase_Subfamily_UBLCP1|UBLCP1]]===
 UBLCP1 is named after Ubiquitin-like domain containing CTD phosphatase 1. It has not been well characterized. It has a N-terminal domain similar to ubiquitin. Its putative substrate is the CTD.
-===[[TIMM50]]===
+===[[Phosphatase_Subfamily_TIMM50|TIMM50]]===
 TIMM50, translocase of inner mitochondrial membrane 50 homolog. Catalytically inactive.

← Older revision		Revision as of 00:25, 7 May 2014
Line 1:		Line 1:
−	[[Phosphatase classification\|Phosphatase Classification]]: [[Phosphatase_Group_HAD\|Superfamily HAD]]: [[Phosphatase_Family_FCP\|FCP]]	+	[[Phosphatase classification\|Phosphatase Classification]]: [[Phosphatase_Group_HAD\|Superfamily HAD]]: [[Phosphatase_Family_FCP\|Family FCP]]

	The FCP family is named after subfamily FCP1. It contains five catalytically active families, and one inactive one (TIMM50). Four of the five catalytically active families show phosphatase activity toward the C-terminal domain (CTD) of RNA polymerase II (Pol II). The CTD, found only in eukaryotes, consists of tandem repeated heptapeptide segments usually of a consensus sequence YSPTSPS, and the different phosphorylation patterns that predominate at each stage of transcription recruit the appropriate set of mRNA-processing and histone-modifying factors. FCP1 and SCP have different preference over pSer2 and pSer5, which may be important for regulating phosphorylation patterns. See [[CTD_Phosphorylation\|Phosphorylation of RNA polymerase II C-terminal domain]].		The FCP family is named after subfamily FCP1. It contains five catalytically active families, and one inactive one (TIMM50). Four of the five catalytically active families show phosphatase activity toward the C-terminal domain (CTD) of RNA polymerase II (Pol II). The CTD, found only in eukaryotes, consists of tandem repeated heptapeptide segments usually of a consensus sequence YSPTSPS, and the different phosphorylation patterns that predominate at each stage of transcription recruit the appropriate set of mRNA-processing and histone-modifying factors. FCP1 and SCP have different preference over pSer2 and pSer5, which may be important for regulating phosphorylation patterns. See [[CTD_Phosphorylation\|Phosphorylation of RNA polymerase II C-terminal domain]].

← Older revision		Revision as of 00:24, 7 May 2014
Line 1:		Line 1:
−	==[[Phosphatase classification\|Phosphatase Classification]]: [[Phosphatase_Family_FCP\|FCP]]==	+	[[Phosphatase classification\|Phosphatase Classification]]: [[Phosphatase_Group_HAD\|Superfamily HAD]]: [[Phosphatase_Family_FCP\|FCP]]
		+
	The FCP family is named after subfamily FCP1. It contains five catalytically active families, and one inactive one (TIMM50). Four of the five catalytically active families show phosphatase activity toward the C-terminal domain (CTD) of RNA polymerase II (Pol II). The CTD, found only in eukaryotes, consists of tandem repeated heptapeptide segments usually of a consensus sequence YSPTSPS, and the different phosphorylation patterns that predominate at each stage of transcription recruit the appropriate set of mRNA-processing and histone-modifying factors. FCP1 and SCP have different preference over pSer2 and pSer5, which may be important for regulating phosphorylation patterns. See [[CTD_Phosphorylation\|Phosphorylation of RNA polymerase II C-terminal domain]].		The FCP family is named after subfamily FCP1. It contains five catalytically active families, and one inactive one (TIMM50). Four of the five catalytically active families show phosphatase activity toward the C-terminal domain (CTD) of RNA polymerase II (Pol II). The CTD, found only in eukaryotes, consists of tandem repeated heptapeptide segments usually of a consensus sequence YSPTSPS, and the different phosphorylation patterns that predominate at each stage of transcription recruit the appropriate set of mRNA-processing and histone-modifying factors. FCP1 and SCP have different preference over pSer2 and pSer5, which may be important for regulating phosphorylation patterns. See [[CTD_Phosphorylation\|Phosphorylation of RNA polymerase II C-terminal domain]].