4nnd - Revision history

OCA at 08:36, 11 January 2023

OCA — Wed, 11 Jan 2023 08:36:10 GMT

←Older revision		Revision as of 08:36, 11 January 2023
Line 3:		Line 3:
	<StructureSection load='4nnd' size='340' side='right'caption='[[4nnd]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='4nnd' size='340' side='right'caption='[[4nnd]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4nnd]] is a 8 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NND OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4NND FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4nnd]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NND OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NND FirstGlance]. <br>
-	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PTPN18, BDP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4nnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nnd OCA], [https://pdbe.org/4nnd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nnd RCSB], [https://www.ebi.ac.uk/pdbsum/4nnd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nnd ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></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=4nnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nnd OCA], [~~http~~://pdbe.org/4nnd PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4nnd RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4nnd PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4nnd ProSAT]</span></td></tr>	+
	</table>		</table>
-	== Disease ==
-	[[http://www.uniprot.org/uniprot/ERBB2_HUMAN ERBB2_HUMAN]] Defects in ERBB2 are a cause of hereditary diffuse gastric cancer (HDGC) [MIM:[http://omim.org/entry/137215 137215]]. A cancer predisposition syndrome with increased susceptibility to diffuse gastric cancer. Diffuse gastric cancer is a malignant disease characterized by poorly differentiated infiltrating lesions resulting in thickening of the stomach. Malignant tumors start in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. Defects in ERBB2 are involved in the development of glioma (GLM) [MIM:[http://omim.org/entry/137800 137800]]. Gliomas are central nervous system neoplasms derived from glial cells and comprise astrocytomas, glioblastoma multiforme, oligodendrogliomas, and ependymomas. Defects in ERBB2 are a cause of susceptibility to ovarian cancer (OC) [MIM:[http://omim.org/entry/167000 167000]]. Ovarian cancer common malignancy originating from ovarian tissue. Although many histologic types of ovarian neoplasms have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease. Defects in ERBB2 may be a cause of lung cancer (LNCR) [MIM:[http://omim.org/entry/211980 211980]]. LNCR is a common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis. Defects in ERBB2 are a cause of gastric cancer (GASC) [MIM:[http://omim.org/entry/613659 613659]]. A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease. Note=Chromosomal aberrations involving ERBB2 may be a cause gastric cancer. Deletions within 17q12 region producing fusion transcripts with CDK12, leading to CDK12-ERBB2 fusion leading to truncated CDK12 protein not in-frame with ERBB2.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PTN18_HUMAN PTN18_HUMAN]] Differentially dephosphorylate autophosphorylated tyrosine kinases which are known to be overexpressed in tumor tissues. [[http://www.uniprot.org/uniprot/ERBB2_HUMAN ERBB2_HUMAN]] Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization.<ref>PMID:10358079</ref> <ref>PMID:15380516</ref> <ref>PMID:16794579</ref> <ref>PMID:19372587</ref> <ref>PMID:20937854</ref> <ref>PMID:21555369</ref> In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth.<ref>PMID:10358079</ref> <ref>PMID:15380516</ref> <ref>PMID:16794579</ref> <ref>PMID:19372587</ref> <ref>PMID:20937854</ref> <ref>PMID:21555369</ref>	+	[https://www.uniprot.org/uniprot/PTN18_HUMAN PTN18_HUMAN] Differentially dephosphorylate autophosphorylated tyrosine kinases which are known to be overexpressed in tumor tissues.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Protein tyrosine phosphatases (PTPs) play a critical role in regulating cellular functions by selectively dephosphorylating their substrates. Here we present 22 human PTP crystal structures that, together with prior structural knowledge, enable a comprehensive analysis of the classical PTP family. Despite their largely conserved fold, surface properties of PTPs are strikingly diverse. A potential secondary substrate-binding pocket is frequently found in phosphatases, and this has implications for both substrate recognition and development of selective inhibitors. Structural comparison identified four diverse catalytic loop (WPD) conformations and suggested a mechanism for loop closure. Enzymatic assays revealed vast differences in PTP catalytic activity and identified PTPD1, PTPD2, and HDPTP as catalytically inert protein phosphatases. We propose a "head-to-toe" dimerization model for RPTPgamma/zeta that is distinct from the "inhibitory wedge" model and that provides a molecular basis for inhibitory regulation. This phosphatome resource gives an expanded insight into intrafamily PTP diversity, catalytic activity, substrate recognition, and autoregulatory self-association.	+
-		+
-	Large-scale structural analysis of the classical human protein tyrosine phosphatome.,Barr AJ, Ugochukwu E, Lee WH, King ON, Filippakopoulos P, Alfano I, Savitsky P, Burgess-Brown NA, Muller S, Knapp S Cell. 2009 Jan 23;136(2):352-63. PMID:19167335<ref>PMID:19167335</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4nnd" style="background-color:#fffaf0;"></div>~~	+

	==See Also==		==See Also==
-	*[[Tyrosine phosphatase\|Tyrosine phosphatase]]	+	*[[Tyrosine phosphatase 3D structures\|Tyrosine phosphatase 3D structures]]
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Protein-tyrosine-phosphatase]]~~	+	[[Category: Du Y]]
-	[[Category: Du, Y]]	+	[[Category: Wang H]]
-	[[Category: Wang, H]]	+	[[Category: Yang D]]
-	[[Category: Yang, D]]	+	[[Category: Yang F]]
-	[[Category: Yang, F]]	+
-	~~[[Category: Beta barrel]]~~	+
-	~~[[Category: Beta-propeller]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Kinase binding]]~~	+
-	~~[[Category: Phosphorylation~~]]	+

OCA at 08:55, 10 April 2019

OCA — Wed, 10 Apr 2019 08:55:14 GMT

←Older revision		Revision as of 08:55, 10 April 2019
Line 1:		Line 1:

	==Structural basis of PTPN18 fingerprint on distinct HER2 tyrosine phosphorylation sites==		==Structural basis of PTPN18 fingerprint on distinct HER2 tyrosine phosphorylation sites==
-	<StructureSection load='4nnd' size='340' side='right' caption='[[4nnd]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='4nnd' size='340' side='right'caption='[[4nnd]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4nnd]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NND OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NND FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4nnd]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NND OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NND FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PTPN18, BDP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></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=4nnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nnd OCA], [http://pdbe.org/4nnd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nnd RCSB], [http://www.ebi.ac.uk/pdbsum/4nnd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nnd ProSAT]</span></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=4nnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nnd OCA], [http://pdbe.org/4nnd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nnd RCSB], [http://www.ebi.ac.uk/pdbsum/4nnd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nnd ProSAT]</span></td></tr>
Line 28:		Line 29:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Protein-tyrosine-phosphatase]]		[[Category: Protein-tyrosine-phosphatase]]
	[[Category: Du, Y]]		[[Category: Du, Y]]

OCA at 19:20, 11 August 2016

OCA — Thu, 11 Aug 2016 19:20:01 GMT

←Older revision		Revision as of 19:20, 11 August 2016
Line 1:		Line 1:
		+
	==Structural basis of PTPN18 fingerprint on distinct HER2 tyrosine phosphorylation sites==		==Structural basis of PTPN18 fingerprint on distinct HER2 tyrosine phosphorylation sites==
	<StructureSection load='4nnd' size='340' side='right' caption='[[4nnd]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='4nnd' size='340' side='right' caption='[[4nnd]], [[Resolution\|resolution]] 2.50Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></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=4nnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nnd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nnd RCSB], [http://www.ebi.ac.uk/pdbsum/4nnd PDBsum]</span></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=4nnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nnd OCA], [http://pdbe.org/4nnd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nnd RCSB], [http://www.ebi.ac.uk/pdbsum/4nnd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nnd ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 19:		Line 20:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4nnd" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Tyrosine phosphatase\|Tyrosine phosphatase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:39, 19 November 2014

OCA — Wed, 19 Nov 2014 12:39:58 GMT

←Older revision		Revision as of 12:39, 19 November 2014
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Structural basis of PTPN18 fingerprint on distinct HER2 tyrosine phosphorylation sites==
		+	<StructureSection load='4nnd' size='340' side='right' caption='[[4nnd]], [[Resolution\|resolution]] 2.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4nnd]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NND OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NND FirstGlance]. <br>
		+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></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=4nnd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nnd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nnd RCSB], [http://www.ebi.ac.uk/pdbsum/4nnd PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/ERBB2_HUMAN ERBB2_HUMAN]] Defects in ERBB2 are a cause of hereditary diffuse gastric cancer (HDGC) [MIM:[http://omim.org/entry/137215 137215]]. A cancer predisposition syndrome with increased susceptibility to diffuse gastric cancer. Diffuse gastric cancer is a malignant disease characterized by poorly differentiated infiltrating lesions resulting in thickening of the stomach. Malignant tumors start in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. Defects in ERBB2 are involved in the development of glioma (GLM) [MIM:[http://omim.org/entry/137800 137800]]. Gliomas are central nervous system neoplasms derived from glial cells and comprise astrocytomas, glioblastoma multiforme, oligodendrogliomas, and ependymomas. Defects in ERBB2 are a cause of susceptibility to ovarian cancer (OC) [MIM:[http://omim.org/entry/167000 167000]]. Ovarian cancer common malignancy originating from ovarian tissue. Although many histologic types of ovarian neoplasms have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease. Defects in ERBB2 may be a cause of lung cancer (LNCR) [MIM:[http://omim.org/entry/211980 211980]]. LNCR is a common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis. Defects in ERBB2 are a cause of gastric cancer (GASC) [MIM:[http://omim.org/entry/613659 613659]]. A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease. Note=Chromosomal aberrations involving ERBB2 may be a cause gastric cancer. Deletions within 17q12 region producing fusion transcripts with CDK12, leading to CDK12-ERBB2 fusion leading to truncated CDK12 protein not in-frame with ERBB2.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PTN18_HUMAN PTN18_HUMAN]] Differentially dephosphorylate autophosphorylated tyrosine kinases which are known to be overexpressed in tumor tissues. [[http://www.uniprot.org/uniprot/ERBB2_HUMAN ERBB2_HUMAN]] Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization.<ref>PMID:10358079</ref> <ref>PMID:15380516</ref> <ref>PMID:16794579</ref> <ref>PMID:19372587</ref> <ref>PMID:20937854</ref> <ref>PMID:21555369</ref> In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth.<ref>PMID:10358079</ref> <ref>PMID:15380516</ref> <ref>PMID:16794579</ref> <ref>PMID:19372587</ref> <ref>PMID:20937854</ref> <ref>PMID:21555369</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Protein tyrosine phosphatases (PTPs) play a critical role in regulating cellular functions by selectively dephosphorylating their substrates. Here we present 22 human PTP crystal structures that, together with prior structural knowledge, enable a comprehensive analysis of the classical PTP family. Despite their largely conserved fold, surface properties of PTPs are strikingly diverse. A potential secondary substrate-binding pocket is frequently found in phosphatases, and this has implications for both substrate recognition and development of selective inhibitors. Structural comparison identified four diverse catalytic loop (WPD) conformations and suggested a mechanism for loop closure. Enzymatic assays revealed vast differences in PTP catalytic activity and identified PTPD1, PTPD2, and HDPTP as catalytically inert protein phosphatases. We propose a "head-to-toe" dimerization model for RPTPgamma/zeta that is distinct from the "inhibitory wedge" model and that provides a molecular basis for inhibitory regulation. This phosphatome resource gives an expanded insight into intrafamily PTP diversity, catalytic activity, substrate recognition, and autoregulatory self-association.

-	~~The entry 4nnd is~~ ON ~~HOLD until Nov 17 2015~~	+	Large-scale structural analysis of the classical human protein tyrosine phosphatome.,Barr AJ, Ugochukwu E, Lee WH, King ON, Filippakopoulos P, Alfano I, Savitsky P, Burgess-Brown NA, Muller S, Knapp S Cell. 2009 Jan 23;136(2):352-63. PMID:19167335<ref>PMID:19167335</ref>

-	~~Authors~~: Wang, H., Yang, ~~F.,~~ Yang, ~~D., Du, Y.~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Structural basis of PTPN18 fingerprint on distinct HER2 tyrosine phosphorylation sites~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Protein-tyrosine-phosphatase]]
		+	[[Category: Du, Y]]
		+	[[Category: Wang, H]]
		+	[[Category: Yang, D]]
		+	[[Category: Yang, F]]
		+	[[Category: Beta barrel]]
		+	[[Category: Beta-propeller]]
		+	[[Category: Hydrolase]]
		+	[[Category: Kinase binding]]
		+	[[Category: Phosphorylation]]

OCA at 10:18, 5 February 2014

OCA — Wed, 05 Feb 2014 10:18:31 GMT

←Older revision		Revision as of 10:18, 5 February 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4nnd is ON HOLD	+	The entry 4nnd is ON HOLD until Nov 17 2015

	Authors: Wang, H., Yang, F., Yang, D., Du, Y.		Authors: Wang, H., Yang, F., Yang, D., Du, Y.

	Description: Structural basis of PTPN18 fingerprint on distinct HER2 tyrosine phosphorylation sites		Description: Structural basis of PTPN18 fingerprint on distinct HER2 tyrosine phosphorylation sites

OCA at 09:17, 18 December 2013

OCA — Wed, 18 Dec 2013 09:17:53 GMT

←Older revision		Revision as of 09:17, 18 December 2013
Line 3:		Line 3:
	The entry 4nnd is ON HOLD		The entry 4nnd is ON HOLD

-	Authors: ~~hongmei wang~~, ~~fan yang~~, ~~duxiao yang~~, ~~yujie du~~	+	Authors: Wang, H., Yang, F., Yang, D., Du, Y.

	Description: Structural basis of PTPN18 fingerprint on distinct HER2 tyrosine phosphorylation sites		Description: Structural basis of PTPN18 fingerprint on distinct HER2 tyrosine phosphorylation sites

OCA: Protected "4nnd" [edit=sysop:move=sysop]

OCA — Wed, 27 Nov 2013 09:52:10 GMT

Protected "4nnd" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:52, 27 November 2013

OCA: New page: '''Unreleased structure''' The entry 4nnd is ON HOLD Authors: hongmei wang, fan yang, duxiao yang, yujie du Description: Structural basis of PTPN18 fingerprint on distinct HER2 tyrosin...

OCA — Wed, 27 Nov 2013 09:52:09 GMT

New page: '''Unreleased structure''' The entry 4nnd is ON HOLD Authors: hongmei wang, fan yang, duxiao yang, yujie du Description: Structural basis of PTPN18 fingerprint on distinct HER2 tyrosin...

New page

'''Unreleased structure'''

The entry 4nnd is ON HOLD

Authors: hongmei wang, fan yang, duxiao yang, yujie du

Description: Structural basis of PTPN18 fingerprint on distinct HER2 tyrosine phosphorylation sites