Phosphatase Subfamily DSP3 - Revision history

Mark: /* DUSP27 */

2015-12-07T20:36:52Z

‎DUSP27

Mark: /* Function */

2015-12-07T20:00:41Z

‎Function

Mark at 00:50, 2 October 2015

2015-10-02T00:50:06Z

Mark: /* References */

2015-04-17T18:47:28Z

‎References

Mark: /* DUSP3 (VHR, vaccinia H1-related) */

2015-04-17T18:47:04Z

‎DUSP3 (VHR, vaccinia H1-related)

Mark: /* References */

2015-04-09T16:39:09Z

‎References

Mark: /* DUSP3 (VHR, vaccinia H1-related) */

2015-04-09T16:38:49Z

‎DUSP3 (VHR, vaccinia H1-related)

Mark at 01:01, 9 March 2015

2015-03-09T01:01:15Z

Mark at 16:37, 8 March 2015

2015-03-08T16:37:39Z

Mark at 02:40, 8 March 2015

2015-03-08T02:40:21Z

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 ====== DUSP27 ======
-DUSP27 function is unknown, but it is predicted to be catalytically inactive due to the cysteine was replaced by serine at the Cx5R catalytic motif. DUSP27 orthologs are found from fish to human, and all of them are predicted to be catalytically inactive due to the substitution at cysteine by serine/aspartic acid/valine (not arginine) at the catalytic motif (internal data). According to [http://www.gtexportal.org/home/gene/DUSP27 GTEx] data, DUSP27 is abundantly expressed in skeletal muscle and heart. It is also expressed artery but almost not expressed in other tissues.
+DUSP27 function is unknown. According to [http://www.gtexportal.org/home/gene/DUSP27 GTEx] data, DUSP27 is abundantly expressed in skeletal muscle and heart. It is also expressed artery but almost not expressed in other tissues.
 ====== DUPD1 ======

@@ Line 48: / Line 48: @@
 ====== DUSP27 ======
-DUSP27 function is unknown, though its crystal structure has been solved <cite>Lountos11</cite>. According to [http://www.gtexportal.org/home/gene/DUSP27 GTEx] data, DUSP27 is abundantly expressed in skeletal muscle and heart. It is also expressed artery but almost not expressed in other tissues.
+DUSP27 function is unknown, but it is predicted to be catalytically inactive due to the cysteine was replaced by serine at the Cx5R catalytic motif. DUSP27 orthologs are found from fish to human, and all of them are predicted to be catalytically inactive due to the substitution at cysteine by serine/aspartic acid/valine (not arginine) at the catalytic motif (internal data). According to [http://www.gtexportal.org/home/gene/DUSP27 GTEx] data, DUSP27 is abundantly expressed in skeletal muscle and heart. It is also expressed artery but almost not expressed in other tissues.
 ====== DUPD1 ======
-DUPD1 is strictly expressed in skeletal muscle according to [http://www.gtexportal.org/home/gene/DUPD1 GTEx]. It is a cytosolic enzyme. Besides skeletal muscle, it has been shown to be expressed in liver and adipose tissue <cite>Friedberg07</cite>. DUPD1 has an alias of  DUSP27, which is misleading since there is a gene whose official symbol is DUSP27.
+DUPD1 is strictly expressed in skeletal muscle according to [http://www.gtexportal.org/home/gene/DUPD1 GTEx]. It is a cytosolic enzyme. Besides skeletal muscle, it has been shown to be expressed in liver and adipose tissue <cite>Friedberg07</cite>. DUPD1 has an alias of  DUSP27, which is misleading since there is a gene whose official symbol is DUSP27. Its physiological substrate is unclear, though its crystal structure has been solved <cite>Lountos11</cite>.
 === References ===

← Older revision		Revision as of 00:50, 2 October 2015
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−	~~__NOTOC__~~
	[[Phosphatase classification\|Phosphatase Classification]]: [[Phosphatase_Fold_CC1\|Fold CC1]]: [[Phosphatase_Superfamily_CC1\|Superfamily CC1]]: [[Phosphatase_Family_DSP\|Family DSP]]: [[Phosphatase_Subfamily_DSP3\|Subfamily DSP3]]		[[Phosphatase classification\|Phosphatase Classification]]: [[Phosphatase_Fold_CC1\|Fold CC1]]: [[Phosphatase_Superfamily_CC1\|Superfamily CC1]]: [[Phosphatase_Family_DSP\|Family DSP]]: [[Phosphatase_Subfamily_DSP3\|Subfamily DSP3]]

@@ Line 78: / Line 78: @@
 #Schumacher02 pmid=11863439
 #Shang10 pmid=20562916
 #Takagaki07 pmid=17001450
 #Tanuma05 pmid=19043453

← Older revision		Revision as of 18:47, 17 April 2015
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	DUSP3 is implicated in human cancer, but it has been alternatively described as having tumor suppressive and oncogenic properties. DUSP3 is upregulated in (pre) neoplastic lesions (squamous intraepithelial lesions; SILs) of the uterine cervix mainly in high grade SIL (H-SIL) compared to normal exocervix. In the invasive cancer, it is also highly expressed with nuclear localization in the majority of cells compared to normal tissue where it is always in the cytoplasm. DUSP3 is highly expressed in several cervix cancer cell lines such as HeLa, SiHa, CaSki, C33 and HT3 compared to primary keratinocytes <cite>Henkens08</cite>. DUSP3 inhibits apoptosis in prostate cancer cells and is overexpressed in prostate cancer. DUSP3 may therefore have a role in prostate cancer progression <cite>Arnoldussen08</cite>. Expression of DUSP3 suppressed tumor formation in a mouse xenograft model. Its expression was significantly lower in non-small cell lung cancer tissues in comparison to that in normal lung tissues <cite>Wang11</cite>. In addition, DUSP3 is a pro-angiogenic <cite>Amand14</cite>.		DUSP3 is implicated in human cancer, but it has been alternatively described as having tumor suppressive and oncogenic properties. DUSP3 is upregulated in (pre) neoplastic lesions (squamous intraepithelial lesions; SILs) of the uterine cervix mainly in high grade SIL (H-SIL) compared to normal exocervix. In the invasive cancer, it is also highly expressed with nuclear localization in the majority of cells compared to normal tissue where it is always in the cytoplasm. DUSP3 is highly expressed in several cervix cancer cell lines such as HeLa, SiHa, CaSki, C33 and HT3 compared to primary keratinocytes <cite>Henkens08</cite>. DUSP3 inhibits apoptosis in prostate cancer cells and is overexpressed in prostate cancer. DUSP3 may therefore have a role in prostate cancer progression <cite>Arnoldussen08</cite>. Expression of DUSP3 suppressed tumor formation in a mouse xenograft model. Its expression was significantly lower in non-small cell lung cancer tissues in comparison to that in normal lung tissues <cite>Wang11</cite>. In addition, DUSP3 is a pro-angiogenic <cite>Amand14</cite>.
		+
		+	DUSP3 is involved in innate immune system. It is strongly expressed in human and mouse monocytes and macrophages, and that its deficiency in mice promotes tolerance to LPS-induced endotoxin shock and to polymicrobial septic shock after cecal ligation and puncture <cite>Singh15</cite>.

	DUSP3 was one of the first phosphatases whose crystal structure was solved <cite>Yuvaniyama96, Schumacher02</cite>.		DUSP3 was one of the first phosphatases whose crystal structure was solved <cite>Yuvaniyama96, Schumacher02</cite>.

@@ Line 72: / Line 72: @@
 #Patterson10 pmid=20347885
 #Pavic14 pmid=24798147
 #Rahmouni03 pmid=16604064
 #Schumacher02 pmid=11863439

← Older revision		Revision as of 16:38, 9 April 2015
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	DUSP3 was one of the first phosphatases whose crystal structure was solved <cite>Yuvaniyama96, Schumacher02</cite>.		DUSP3 was one of the first phosphatases whose crystal structure was solved <cite>Yuvaniyama96, Schumacher02</cite>.
		+
		+	In sum, DUSP3/VHR plays important roles in cell-cycle regulation, DNA damage response, angiogenesis, platelet activation and MAPK signaling. Its involvement in different pathways appears to be highly cell-type specific <cite>Pavic15</cite>.

	====== DUSP13 (BEDP/TMDP/MDSP/SKRP4) ======		====== DUSP13 (BEDP/TMDP/MDSP/SKRP4) ======

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 __NOTOC__
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]:  [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_DSP3|Subfamily DSP3]]
-summary
+DSP3 is a subfamily abundantly expressed in skeletal muscle and heart. It emerged in eumetazoan, lost in nematodes and duplicated in deuterostomia and vertebrates. Human has five members: DUSP3 (VHR), DUSP13 (BEDP/TMDP/MDSP/SKRP4), DUSP26 (MKP8), DUSP27, DUPD1.
 === Evolution ===
+DSP3 is conserved in eumetazoan but lost in nematodes. It duplicated in deuterostomia and vertebrates. Human has five members: DUSP3, DUSP13, DUSP26, DUSP27 and DUPD1. DUSP13 and DUPD1 are neighboring genes in most vertebrate genomes, implies one of them (probably DUPD1) emerged by duplication (see [http://www.genomicus.biologie.ens.fr/genomicus-78.01/cgi-bin/phyloview.pl?root=2286690&amp;id=2286830&amp;xhide=133:109:19:44:143:45:91:95:141:21:97:23:43:1:134:111:80:87:34:24:120:25:90:78:7:108:20:101:53:35:83:85:118:102:-2286690:124:98:137:32:22:122:18:33:57:4:17:125:144:114:52&amp;xcollapse=-2286690&amp; Genomicus] or UCSC genome browser).
 === Domain ===
+DSP3 subfamily has a single domain: phosphatase domain.
 === Function ===
 ====== DUSP3 (VHR, vaccinia H1-related) ======
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 DUSP3 was one of the first phosphatases whose crystal structure was solved <cite>Yuvaniyama96, Schumacher02</cite>.
 === References ===
@@ Line 33: / Line 56: @@
 #Amand14 pmid=24886454
 #Arnoldussen08 pmid=19010898
 #Henkens08 pmid=18505570
 #Hoyt07 pmid=17785772
 #Ishibashi92 pmid=1281549
 #Pavic14 pmid=24798147
 #Rahmouni03 pmid=16604064
 #Schumacher02 pmid=11863439
 #Todd99 pmid=10224087
 #Wang11 pmid=21262974
 #Yuvaniyama96 pmid=8650541
 </biblio>

@@ Line 7: / Line 7: @@
 === Evolution ===
-DSP14 subfamily emerged in eumetazoan and duplicated in vertebrates.
 === Domain ===
-DSP14 subfamily has a single phosphatase domain.
 === Function ===
-DUSP18 interacts with and dephosphorylates SAPK/JNK in vitro and in vivo. It does not dephosphorylate p38 or ERK1 <cite>Wu06</cite>. USP18 was widely expressed in different tissues as evidenced by RT-PCR <cite>Wu03</cite>. RNA-seq from [http://www.gtexportal.org/home/gene/DUSP18 GTEx] shows a high expression in testis and pituitary, and a low expression in skeleton.
+====== DUSP3 (VHR, vaccinia H1-related) ======
-DUSP21 plays an important role in sustaining human hepatocellular carcinoma cell proliferation <cite>Deng14</cite>.
+DUSP3 selectively dephosphorylates IFN-alpha- and beta-activated, tyrosine-phosphorylated STAT5, leading to the subsequent inhibition of STAT5 function. DUSP3 activity towards STAT5 is also dependent on phosphorylation at Tyr138, but by tyrosine kinase Tyk2 of Jak family, which mediates the phosphorylation of STAT5. Besides phosphorylation at Tyr138 of DUSP3, Src homology 2 domain of STAT5 was required for the effective dephosphorylation of STAT5 <cite>Hoyt07</cite> (note: SH2 domain of STAT5 binds to Tyr138 of DUSP3?).
-DUSP28 (VHP) is widely expressed in different tissues according to RNA-seq data from [http://www.gtexportal.org/home/gene/DUSP28 GTEx], but its function is unknown.
+DUSP3 dephosphorylates EGFR/ERBB1 and ERBB2. In particular, it probably dephosphorylates Tyr-992 <cite>Wang11</cite>. DUSP3 dephosphorylated several activated growth factor receptors, as well as serine-phosphorylated casein, in vitro <cite>Ishibashi92</cite>.
 === References ===
 <biblio>
+#Alonso01 pmid=11085983
 </biblio>

← Older revision		Revision as of 02:40, 8 March 2015
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−	~~===== [[Phosphatase_Subfamily_DSP3\|DSP3 subfamily]] =====~~
−
	The subfamily DSP3 consists of five genes in human, [[Phosphatase_Gene_DUSP3\|DUSP3]], DUSP13, [[Phosphatase_Gene_DUSP26\|DUSP26]] (chr 8, also called MKP8, DUSP24), DUSP27 (chr 1), [[Phosphatase_Gene_DUPD1\|DUPD1]] (chr 10, it has an alias of DUSP27). It is found in eumetazoan but lost in nematodes.		The subfamily DSP3 consists of five genes in human, [[Phosphatase_Gene_DUSP3\|DUSP3]], DUSP13, [[Phosphatase_Gene_DUSP26\|DUSP26]] (chr 8, also called MKP8, DUSP24), DUSP27 (chr 1), [[Phosphatase_Gene_DUPD1\|DUPD1]] (chr 10, it has an alias of DUSP27). It is found in eumetazoan but lost in nematodes.
		+
		+	__NOTOC__
		+	[[Phosphatase classification\|Phosphatase Classification]]: [[Phosphatase_Fold_CC1\|Fold CC1]]: [[Phosphatase_Superfamily_CC1\|Superfamily CC1]]: [[Phosphatase_Family_DSP\|Family DSP]]: [[Phosphatase_Subfamily_DSP3\|Subfamily DSP3]]
		+
		+	summary
		+
		+	=== Evolution ===
		+	DSP14 subfamily emerged in eumetazoan and duplicated in vertebrates.
		+
		+	=== Domain ===
		+	DSP14 subfamily has a single phosphatase domain.
		+
		+	=== Function ===
		+	DUSP14 (MKP6) dephosphorylates TGF-beta-activated kinase 1 (TAK1), a member of MAPKKK, at Thr-187 within its kinase activation loop. Thus, DUSP14 negatively regulates TNF- or IL-1-induced NF-kappaB activation <cite>Zheng13</cite>. DUSP14 is widely expressed in different tissues with highest expression in skin tissues (see [http://www.gtexportal.org/home/gene/DUSP14 GTEx]).
		+
		+	DUSP18 interacts with and dephosphorylates SAPK/JNK in vitro and in vivo. It does not dephosphorylate p38 or ERK1 <cite>Wu06</cite>. USP18 was widely expressed in different tissues as evidenced by RT-PCR <cite>Wu03</cite>. RNA-seq from [http://www.gtexportal.org/home/gene/DUSP18 GTEx] shows a high expression in testis and pituitary, and a low expression in skeleton.
		+
		+	DUSP21 plays an important role in sustaining human hepatocellular carcinoma cell proliferation <cite>Deng14</cite>.
		+
		+	DUSP28 (VHP) is widely expressed in different tissues according to RNA-seq data from [http://www.gtexportal.org/home/gene/DUSP28 GTEx], but its function is unknown.
		+
		+	=== References ===
		+	<biblio>
		+
		+	</biblio>