5zrx - Revision history

OCA at 09:05, 22 November 2023

2023-11-22T09:05:23Z

←Older revision		Revision as of 09:05, 22 November 2023
Line 3:		Line 3:
	<StructureSection load='5zrx' size='340' side='right'caption='[[5zrx]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='5zrx' size='340' side='right'caption='[[5zrx]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5zrx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZRX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5zrx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZRX FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~Epha2~~, ~~Eck, Myk2, Sek2 (~~[~~https://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=~~5&~~id=10090 LK3 transgenic mice])~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.5Å</td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5zrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zrx OCA], [https://pdbe.org/5zrx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zrx RCSB], [https://www.ebi.ac.uk/pdbsum/5zrx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zrx ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5zrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zrx OCA], [https://pdbe.org/5zrx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zrx RCSB], [https://www.ebi.ac.uk/pdbsum/5zrx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zrx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/SHIP2_MOUSE SHIP2_MOUSE]] Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling (By similarity). Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification (By similarity).[UniProtKB:O15357]<ref>PMID:10958682</ref> <ref>PMID:11343120</ref> <ref>PMID:14744864</ref> <ref>PMID:15557176</ref> <ref>PMID:15654325</ref> <ref>PMID:16179375</ref>	+	[https://www.uniprot.org/uniprot/SHIP2_MOUSE SHIP2_MOUSE] Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling (By similarity). Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification (By similarity).[UniProtKB:O15357]<ref>PMID:10958682</ref> <ref>PMID:11343120</ref> <ref>PMID:14744864</ref> <ref>PMID:15557176</ref> <ref>PMID:15654325</ref> <ref>PMID:16179375</ref> [https://www.uniprot.org/uniprot/EPHA2_MOUSE EPHA2_MOUSE] Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Activated by the ligand ephrin-A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells (PubMed:29749928). Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 signaling pathway. May also participate in UV radiation-induced apoptosis and have a ligand-independent stimulatory effect on chemotactic cell migration. During development, may function in distinctive aspects of pattern formation and subsequently in development of several fetal tissues. Involved for instance in angiogenesis, in early hindbrain development and epithelial proliferation and branching morphogenesis during mammary gland development. Engaged by the ligand ephrin-A5/EFNA5 may regulate lens fiber cells shape and interactions and be important for lens transparency development and maintenance. With ephrin-A2/EFNA2 may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis.<ref>PMID:15054110</ref> <ref>PMID:16782872</ref> <ref>PMID:16849550</ref> <ref>PMID:18387945</ref> <ref>PMID:18948590</ref> <ref>PMID:19299512</ref> <ref>PMID:19321667</ref> <ref>PMID:29749928</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lk3 transgenic mice~~]]	+	[[Category: Mus musculus]]
-	[[Category: Chen, W]]	+	[[Category: Chen W]]
-	[[Category: Li, G]]	+	[[Category: Li G]]
-	[[Category: Li, J]]	+	[[Category: Li J]]
-	[[Category: Liu, W]]	+	[[Category: Liu W]]
-	[[Category: Shang, Y]]	+	[[Category: Shang Y]]
-	[[Category: Wan, J]]	+	[[Category: Wan J]]
-	[[Category: Wang, Y]]	+	[[Category: Wang Y]]
-	[[Category: Zhang, M]]	+	[[Category: Zhang M]]
-	~~[[Category: Cell adhesion]]~~	+
-	~~[[Category: Cell signaling]]~~	+
-	~~[[Category: Heterodimer]]~~	+
-	~~[[Category: Protein binding]]~~	+
-	~~[[Category: Receptor]]~~	+
-	~~[[Category: Sam domain]]~~	+
-	~~[[Category: Signaling protein]]~~	+
-	~~[[Category: Transmembrane]]~~	+
-	~~[[Category: Tyrosine-protein kinase~~]]	+

OCA at 09:31, 15 September 2021

2021-09-15T09:31:56Z

←Older revision		Revision as of 09:31, 15 September 2021
Line 3:		Line 3:
	<StructureSection load='5zrx' size='340' side='right'caption='[[5zrx]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='5zrx' size='340' side='right'caption='[[5zrx]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5zrx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZRX OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5ZRX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5zrx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZRX FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5zrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zrx OCA], [~~http~~://pdbe.org/5zrx PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5zrx RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5zrx PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5zrx ProSAT]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Epha2, Eck, Myk2, Sek2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5zrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zrx OCA], [https://pdbe.org/5zrx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zrx RCSB], [https://www.ebi.ac.uk/pdbsum/5zrx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zrx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/SHIP2_MOUSE SHIP2_MOUSE]] Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling (By similarity). Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification (By similarity).[UniProtKB:O15357]<ref>PMID:10958682</ref> <ref>PMID:11343120</ref> <ref>PMID:14744864</ref> <ref>PMID:15557176</ref> <ref>PMID:15654325</ref> <ref>PMID:16179375</ref>	+	[[https://www.uniprot.org/uniprot/SHIP2_MOUSE SHIP2_MOUSE]] Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling (By similarity). Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification (By similarity).[UniProtKB:O15357]<ref>PMID:10958682</ref> <ref>PMID:11343120</ref> <ref>PMID:14744864</ref> <ref>PMID:15557176</ref> <ref>PMID:15654325</ref> <ref>PMID:16179375</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
		+	[[Category: Lk3 transgenic mice]]
	[[Category: Chen, W]]		[[Category: Chen, W]]
	[[Category: Li, G]]		[[Category: Li, G]]

OCA at 21:23, 28 October 2020

2020-10-28T21:23:52Z

←Older revision		Revision as of 21:23, 28 October 2020
Line 1:		Line 1:

	==Crystal Structure of EphA2/SHIP2 Complex==		==Crystal Structure of EphA2/SHIP2 Complex==
-	<StructureSection load='5zrx' size='340' side='right' caption='[[5zrx]], [[Resolution\|resolution]] 1.50Å' scene=''>	+	<StructureSection load='5zrx' size='340' side='right'caption='[[5zrx]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5zrx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZRX OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5ZRX FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5zrx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZRX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZRX FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5zrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zrx OCA], [http://pdbe.org/5zrx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zrx RCSB], [http://www.ebi.ac.uk/pdbsum/5zrx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zrx ProSAT]</span></td></tr>	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5zrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zrx OCA], [http://pdbe.org/5zrx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zrx RCSB], [http://www.ebi.ac.uk/pdbsum/5zrx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zrx ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 21:		Line 21:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Chen, W]]		[[Category: Chen, W]]
	[[Category: Li, G]]		[[Category: Li, G]]

OCA at 05:30, 30 May 2018

2018-05-30T05:30:41Z

←Older revision		Revision as of 05:30, 30 May 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5zrx is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Crystal Structure of EphA2/SHIP2 Complex==
		+	<StructureSection load='5zrx' size='340' side='right' caption='[[5zrx]], [[Resolution\|resolution]] 1.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5zrx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZRX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZRX FirstGlance]. <br>
		+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5zrx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zrx OCA], [http://pdbe.org/5zrx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zrx RCSB], [http://www.ebi.ac.uk/pdbsum/5zrx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zrx ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SHIP2_MOUSE SHIP2_MOUSE]] Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling (By similarity). Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification (By similarity).[UniProtKB:O15357]<ref>PMID:10958682</ref> <ref>PMID:11343120</ref> <ref>PMID:14744864</ref> <ref>PMID:15557176</ref> <ref>PMID:15654325</ref> <ref>PMID:16179375</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The Eph receptor tyrosine kinase (RTK) family is the largest subfamily of RTKs playing critical roles in many developmental processes such as tissue patterning, neurogenesis and neuronal circuit formation, angiogenesis, etc. How the 14 Eph proteins, via their highly similar cytoplasmic domains, can transmit diverse and sometimes opposite cellular signals upon engaging ephrins is a major unresolved question. Here we systematically investigated the bindings of each SAM domain of Eph receptors to the SAM domains from SHIP2 and Odin, and uncover a highly specific SAM-SAM interaction-mediated cytoplasmic Eph-effector binding pattern. Comparative X-ray crystallographic studies of several SAM-SAM heterodimer complexes, together with biochemical and cell biology experiments, not only revealed the exquisite specificity code governing Eph/effector interactions but also allowed us to identify SAMD5 as a new Eph binding partner. Finally, these Eph/effector SAM heterodimer structures can explain many Eph SAM mutations identified in patients suffering from cancers and other diseases.

-	~~Authors~~:	+	Specific Eph receptor-cytoplasmic effector signaling mediated by SAM-SAM domain interactions.,Wang Y, Shang Y, Li J, Chen W, Li G, Wan J, Liu W, Zhang M Elife. 2018 May 11;7. pii: 35677. doi: 10.7554/eLife.35677. PMID:29749928<ref>PMID:29749928</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5zrx" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Chen, W]]
		+	[[Category: Li, G]]
		+	[[Category: Li, J]]
		+	[[Category: Liu, W]]
		+	[[Category: Shang, Y]]
		+	[[Category: Wan, J]]
		+	[[Category: Wang, Y]]
		+	[[Category: Zhang, M]]
		+	[[Category: Cell adhesion]]
		+	[[Category: Cell signaling]]
		+	[[Category: Heterodimer]]
		+	[[Category: Protein binding]]
		+	[[Category: Receptor]]
		+	[[Category: Sam domain]]
		+	[[Category: Signaling protein]]
		+	[[Category: Transmembrane]]
		+	[[Category: Tyrosine-protein kinase]]

OCA at 05:49, 23 May 2018

2018-05-23T05:49:02Z

←Older revision		Revision as of 05:49, 23 May 2018
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5zrx is ON HOLD	+	The entry 5zrx is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "5zrx" [edit=sysop:move=sysop]

2018-05-02T06:35:53Z

Protected "5zrx" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:35, 2 May 2018

OCA: New page: '''Unreleased structure''' The entry 5zrx is ON HOLD Authors: Description: Category: Unreleased Structures

2018-05-02T06:35:51Z

New page: '''Unreleased structure''' The entry 5zrx is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5zrx is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]