Phosphatase Subfamily STYX - Revision history

Mark at 00:55, 2 October 2015

2015-10-02T00:55:09Z

Mark: /* Function */

2015-10-02T00:54:04Z

‎Function

Mark at 22:10, 2 March 2015

2015-03-02T22:10:53Z

Mark: /* Domain */

2015-03-02T22:10:37Z

‎Domain

Mark at 22:03, 2 March 2015

2015-03-02T22:03:39Z

Mark: Created page with "is a pseudophosphatase subfamily with a single human member. STYX localizes to the nucleus, competes with DUSP4 for binding to ERK, and acts as a nuclear anchor that regulates..."

2015-03-02T21:52:29Z

Created page with "is a pseudophosphatase subfamily with a single human member. STYX localizes to the nucleus, competes with DUSP4 for binding to ERK, and acts as a nuclear anchor that regulates..."

New page

is a pseudophosphatase subfamily with a single human member. STYX localizes to the nucleus, competes with DUSP4 for binding to ERK, and acts as a nuclear anchor that regulates ERK nuclear export <cite>farhan13</cite>. The subfamily is found in most opisthokonts but lost in nematodes. Although It is not found in Drosophila and budding yeast, it is found in other arthropoda and fungi ([http://resdev.gene.com/gOrtholog/view/cluster/MC0005385/overview unpublished data from gOrtholog]).

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 === Function ===
-STYX is catalytically inactive (pseudophosphatase) <cite>Wishart95</cite>. STYX localizes to the nucleus, competes with DUSP4 for binding to ERK, and acts as a nuclear anchor that regulates ERK nuclear export <cite>Reiterer13</cite>.
+STYX is catalytically inactive (pseudophosphatase) <cite>Wishart95</cite>. It binds to phosphorylated tyrosine to module signaling <cite>Wishart98</cite>. STYX localizes to the nucleus, competes with DUSP4 for binding to ERK, and acts as a nuclear anchor that regulates ERK nuclear export <cite>Reiterer13</cite>. STYX also binds to a testicular RNA-binding protein Crhsp-24. This complex is essential for normal spermiogenesis <cite>Wishart02</cite>.
 STYX also binds to a testicular RNA-binding protein Crhsp-24. This complex is essential for normal spermiogenesis <cite>Wishart02</cite>.
 === References ===
@@ Line 18: / Line 17: @@
 #Reiterer13 pmid=23847209
 #Wishart95 pmid=7592916
 #Wishart02 pmid=11842224
 </biblio>

@@ Line 11: / Line 11: @@
 === Function ===
-STYX is catalytically inactive (pseudophosphatase) <cite>Wishart95</cite>. Little is known about its function.
+STYX is catalytically inactive (pseudophosphatase) <cite>Wishart95</cite>. STYX localizes to the nucleus, competes with DUSP4 for binding to ERK, and acts as a nuclear anchor that regulates ERK nuclear export <cite>Reiterer13</cite>.
 STYX localizes to the nucleus, competes with DUSP4 for binding to ERK, and acts as a nuclear anchor that regulates ERK nuclear export <cite>Reiterer13</cite>.
 STYX also binds to a testicular RNA-binding protein Crhsp-24. This complex is essential for normal spermiogenesis <cite>Wishart02</cite>.

@@ Line 6: / Line 6: @@
 === Evolution ===
 STYX is found in most opisthokonts but lost in nematodes. Although STYX is not found in Drosophila and budding yeast, it is found in other arthropoda and fungi ([http://resdev.gene.com/gOrtholog/view/cluster/MC0005385/overview unpublished data from gOrtholog]).
 === Domain ===

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 === Domain ===
-DSP23 has a single domain, the phosphatase domain. Actually, it is the shortest within DSP family <cite>Alonso04</cite>.
+STYX has a single domain, (inactive) phosphatase domain.
 === Function ===

← Older revision		Revision as of 22:03, 2 March 2015
Line 1:		Line 1:
−	is a ~~pseudophosphatase subfamily with a single human member~~. STYX ~~localizes to the nucleus, competes with DUSP4 for binding to ERK, and acts as a nuclear anchor that regulates ERK nuclear export <cite>farhan13</cite>. The subfamily~~ is found in most opisthokonts but lost in nematodes. Although It is not found in Drosophila and budding yeast, it is found in other arthropoda and fungi ([http://resdev.gene.com/gOrtholog/view/cluster/MC0005385/overview unpublished data from gOrtholog]).	+	__NOTOC__
		+	[[Phosphatase classification\|Phosphatase Classification]]: [[Phosphatase_Fold_CC1\|Fold CC1]]: [[Phosphatase_Superfamily_CC1\|Superfamily CC1]]: [[Phosphatase_Family_DSP\|Family DSP]]: [[Phosphatase_Subfamily_STYX\|Subfamily STYX]]
		+
		+	STYX is a catalytically inactive phosphatase found in most opisthokonts but lost in nematodes.
		+
		+	=== Evolution ===
		+	STYX is found in most opisthokonts but lost in nematodes. Although STYX is not found in Drosophila and budding yeast, it is found in other arthropoda and fungi ([http://resdev.gene.com/gOrtholog/view/cluster/MC0005385/overview unpublished data from gOrtholog]).
		+
		+
		+	=== Domain ===
		+	DSP23 has a single domain, the phosphatase domain. Actually, it is the shortest within DSP family <cite>Alonso04</cite>.
		+
		+	=== Function ===
		+	STYX is catalytically inactive (pseudophosphatase) <cite>Wishart95</cite>. Little is known about its function.
		+	STYX localizes to the nucleus, competes with DUSP4 for binding to ERK, and acts as a nuclear anchor that regulates ERK nuclear export <cite>Reiterer13</cite>.
		+	STYX also binds to a testicular RNA-binding protein Crhsp-24. This complex is essential for normal spermiogenesis <cite>Wishart02</cite>.
		+
		+	=== References ===
		+	<biblio>
		+	#Reiterer13 pmid=23847209
		+	#Wishart95 pmid=7592916
		+	#Wishart02 pmid=11842224
		+	</biblio>