Phosphatase Subfamily PTPN5 RR - Revision history

Gerard: /* Domains */

2017-04-03T04:23:01Z

‎Domains

Gerard: /* Domains */

2017-04-03T04:21:03Z

‎Domains

Gerard at 04:17, 3 April 2017

2017-04-03T04:17:29Z

Gerard: /* Domains */

2017-04-03T04:12:28Z

‎Domains

Gerard: /* Evolution */

2017-04-03T04:11:59Z

‎Evolution

Gerard at 23:40, 17 May 2016

2016-05-17T23:40:58Z

Gerard at 00:14, 19 March 2016

2016-03-19T00:14:06Z

Mark: /* PTPN7 (HePTP/LC-PTP) */

2016-03-12T20:28:57Z

‎PTPN7 (HePTP/LC-PTP)

Mark: /* Domains */

2015-11-03T18:42:21Z

‎Domains

Mark: /* References */

2015-05-11T00:44:26Z

‎References

@@ Line 11: / Line 11: @@
 PTPN5_RR members have an N-terminal kinase interaction motif (KIM) (~16 aa) <cite>Francis</cite> and a C-terminal phosphatase domain. Vertebrate PTP5RR has a signal peptide and TM region upstream from these domains, while PTPN7 has a TM but no signal peptide. Some but not all invertebrate homologs contain a SigP.
-KIM mediates an interaction with ERK MAP kinases and with p53. The KIM is a serine that can be phosphorylated by PKA. The phosphorylation state of this serine affects the binding between phosphatases to MAP kinases ERK and p53, therefore rapidly change the response to external stimuli.
+KIM mediates an interaction with ERK MAP kinases and with p53. The KIM contains a serine that can be phosphorylated by PKA. The phosphorylation state of this serine affects the binding between phosphatases to ERK MAP kinases ERK and to p53.
-Several PTPN5 crystal structures have been solved <cite>Eswaran06, Mustelin05, Critton08, Szedlacsek01</cite>. An additional helix H0 was found in mouse PTPRR and human PTPN7. The H0 of mouse PTPRR supports the site of phosphorylation at Thr253 when PTP-SL/BR7 interacts with ERK2 or p38. But, the H0 of PTPRR and PTPN7 do not align with each other in structure, and PTPN5 does not have H0.
+Several PTPN5 crystal structures have been solved <cite>Eswaran06, Mustelin05, Critton08, Szedlacsek01</cite>. An additional helix H0 was found in mouse PTPRR and human PTPN7. The H0 of mouse PTPRR supports the site of phosphorylation at Thr253 when PTPRR interacts with ERK2 or p38. The H0 of PTPRR and PTPN7 do not align with each other in structure, and PTPN5 does not have H0.
-Besides KIM and phosphatase domain, the longest isoform of human PTPN5 has two proline-rich regions <cite>Nguyen02</cite>.
+The longest isoform of human PTPN5 has two proline-rich regions <cite>Nguyen02</cite>.
 ===Functions===

@@ Line 9: / Line 9: @@
 ===Domains===
-PTPN5_RR members have an N-terminal kinase interaction motif (KIM) (~16 aa) <cite>Francis</cite> and a C-terminal phosphatase domain.
+PTPN5_RR members have an N-terminal kinase interaction motif (KIM) (~16 aa) <cite>Francis</cite> and a C-terminal phosphatase domain. Vertebrate PTP5RR has a signal peptide and TM region upstream from these domains, while PTPN7 has a TM but no signal peptide. Some but not all invertebrate homologs contain a SigP.
 KIM mediates an interaction with ERK MAP kinases and with p53. The KIM is a serine that can be phosphorylated by PKA. The phosphorylation state of this serine affects the binding between phosphatases to MAP kinases ERK and p53, therefore rapidly change the response to external stimuli.

@@ Line 9: / Line 9: @@
 ===Domains===
-PTPN5_RR members have an N-terminal kinase interaction motif (KIM) (~16 aa) and a C-terminal phosphatase domain.
+PTPN5_RR members have an N-terminal kinase interaction motif (KIM) (~16 aa) <cite>Francis</cite> and a C-terminal phosphatase domain.
 KIM mediates an interaction with ERK MAP kinases and with p53. The KIM is a serine that can be phosphorylated by PKA. The phosphorylation state of this serine affects the binding between phosphatases to MAP kinases ERK and p53, therefore rapidly change the response to external stimuli.
@@ Line 63: / Line 63: @@
 #Critton08 pmid=19053285
 #Eswaran06 pmid=16441242
 #Gronda01 pmid=11564869
 #Kurup10 pmid=20427654

@@ Line 9: / Line 9: @@
 ===Domains===
-PTPN5_RR members have an N-terminal kinase interaction motif (KIM) (~16 aa) ('''note: is is the same with MKP's KIM?''') and a C-terminal phosphatase domain.
+PTPN5_RR members have an N-terminal kinase interaction motif (KIM) (~16 aa) and a C-terminal phosphatase domain.
 KIM mediates an interaction with ERK MAP kinases and with p53. The KIM is a serine that can be phosphorylated by PKA. The phosphorylation state of this serine affects the binding between phosphatases to MAP kinases ERK and p53, therefore rapidly change the response to external stimuli.

@@ Line 6: / Line 6: @@
 ===Evolution===
-The PTPN5_RR subfamily emerged in eumetazoa and duplicated in vertebrates but is lost in nematodes. Human has three members: PTPN5/STEP, PTPN7/HePTP, PTPRR/PTP-SL.
+The PTPN5_RR subfamily emerged in eumetazoa and duplicated in vertebrates but is lost in nematodes. Human has three members: PTPN5 (STEP), PTPN7 (HePTP), and PTPRR (PTP-SL).
 ===Domains===

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 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_PTP|Family PTP]]: [[Phosphatase_Subfamily_PTPN5_RR|Subfamily PTPN5_RR]]
-PTPN5 is a tyrosine-specific phosphatase subfamily. It is characterized by a kinase interaction motif (KIM), which is regulated by the phosphorylation state of a serine within the motif. Human has three members: PTPN5/STEP, PTPN7/HePTP, PTPRR/PTP-SL. They all regulate the ERK pathway, but may have specific substrates. They are expressed in different tissues, particularly, abundant in spleen, thymus, and different parts of the brain.
+PTPN5_RR is a tyrosine-specific phosphatase subfamily. Uniquely, some members are non-receptors, while others have receptor and non-receptor isoforms. It is characterized by a kinase interaction motif (KIM), which is regulated by the phosphorylation state of a serine within the motif. Human has three members: PTPN5/STEP, PTPN7/HePTP, PTPRR/PTP-SL. They all regulate the ERK pathway, but may have specific substrates. They are expressed in different tissues, particularly, abundant in spleen, thymus, and different parts of the brain.
 ===Evolution===
-PTPN5 subfamily emerged in eumetazoan and duplicated in vertebrates but lost in nematode.
+The PTPN5_RR subfamily emerged in eumetazoa and duplicated in vertebrates but is lost in nematodes.
 ===Domains===
-PTPN5 members have an N-terminal kinase interaction motif (KIM) (~16 aa) ('''note: is is the same with MKP's KIM?''') and a C-terminal phosphatase domain.
+PTPN5_RR members have an N-terminal kinase interaction motif (KIM) (~16 aa) ('''note: is is the same with MKP's KIM?''') and a C-terminal phosphatase domain.
 KIM mediates an interaction with ERK MAP kinases and with p53. The KIM is a serine that can be phosphorylated by PKA. The phosphorylation state of this serine affects the binding between phosphatases to MAP kinases ERK and p53, therefore rapidly change the response to external stimuli.

← Older revision		Revision as of 20:28, 12 March 2016
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	PTPN7 is amplified and overexpressed in myeloid malignancies, which implies it may promote abnormal myeloid cell growth <cite>Zanke94</cite>.		PTPN7 is amplified and overexpressed in myeloid malignancies, which implies it may promote abnormal myeloid cell growth <cite>Zanke94</cite>.
		+
		+	It is worthy pointing out that PTPN7 has PTP activity, although it has substitution at N replaced by D at KNRY motif.

	====== PTPRR (EC-PTP/PTP-SL/PTPBR7) ======		====== PTPRR (EC-PTP/PTP-SL/PTPBR7) ======

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 #Swieter95 pmid=7545170
 #Szedlacsek01 pmid=11493009
 #Yang12 pmid=22649233
 #Zanke92 pmid=1530918