3qhe - Revision history

OCA at 17:12, 1 November 2023

2023-11-01T17:12:36Z

←Older revision		Revision as of 17:12, 1 November 2023
Line 3:		Line 3:
	<StructureSection load='3qhe' size='340' side='right'caption='[[3qhe]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='3qhe' size='340' side='right'caption='[[3qhe]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3qhe]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QHE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3qhe]] is a 4 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=3QHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QHE FirstGlance]. <br>
-	</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=3qhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qhe OCA], [https://pdbe.org/3qhe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qhe RCSB], [https://www.ebi.ac.uk/pdbsum/3qhe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qhe ProSAT]</span></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]] 2.4Å</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=3qhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qhe OCA], [https://pdbe.org/3qhe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qhe RCSB], [https://www.ebi.ac.uk/pdbsum/3qhe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qhe ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/APC_HUMAN APC_HUMAN]] Defects in APC are a cause of familial adenomatous polyposis (FAP) [MIM:[https://omim.org/entry/175100 175100]]; which includes also Gardner syndrome (GS). FAP and GS contribute to tumor development in patients with uninherited forms of colorectal cancer. FAP is characterized by adenomatous polyps of the colon and rectum, but also of upper gastrointestinal tract (ampullary, duodenal and gastric adenomas). This is a viciously premalignant disease with one or more polyps progressing through dysplasia to malignancy in untreated gene carriers with a median age at diagnosis of 40 years.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> <ref>PMID:1651563</ref> <ref>PMID:1338904</ref> <ref>PMID:1338691</ref> <ref>PMID:1338764</ref> <ref>PMID:7833149</ref> <ref>PMID:7833931</ref> <ref>PMID:8990002</ref> <ref>PMID:10470088</ref> Defects in APC are a cause of hereditary desmoid disease (HDD) [MIM:[https://omim.org/entry/135290 135290]]; also known as familial infiltrative fibromatosis (FIF). HDD is an autosomal dominant trait with 100% penetrance and possible variable expression among affected relatives. HDD patients show multifocal fibromatosis of the paraspinal muscles, breast, occiput, arms, lower ribs, abdominal wall, and mesentery. Desmoid tumors appears also as a complication of familial adenomatous polyposis.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> Defects in APC are a cause of medulloblastoma (MDB) [MIM:[https://omim.org/entry/155255 155255]]. MDB is a malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. Although the majority of medulloblastomas occur sporadically, some manifest within familial cancer syndromes such as Turcot syndrome and basal cell nevus syndrome (Gorlin syndrome).<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> <ref>PMID:10666372</ref> Defects in APC are a cause of mismatch repair cancer syndrome (MMRCS) [MIM:[https://omim.org/entry/276300 276300]]; also known as Turcot syndrome or brain tumor-polyposis syndrome 1 (BTPS1). MMRCS is an autosomal dominant disorder characterized by malignant tumors of the brain associated with multiple colorectal adenomas. Skin features include sebaceous cysts, hyperpigmented and cafe au lait spots.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> <ref>PMID:7661930</ref> Defects in APC are a cause of gastric cancer (GASC) [MIM:[https://omim.org/entry/613659 613659]]; also called gastric cancer intestinal or stomach cancer. Gastric cancer is 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.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> Defects in APC are a cause of hepatocellular carcinoma (HCC) [MIM:[https://omim.org/entry/114550 114550]]. This defect includes also the disease entity termed hepatoblastoma.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref>	+	[https://www.uniprot.org/uniprot/APC_HUMAN APC_HUMAN] Defects in APC are a cause of familial adenomatous polyposis (FAP) [MIM:[https://omim.org/entry/175100 175100]; which includes also Gardner syndrome (GS). FAP and GS contribute to tumor development in patients with uninherited forms of colorectal cancer. FAP is characterized by adenomatous polyps of the colon and rectum, but also of upper gastrointestinal tract (ampullary, duodenal and gastric adenomas). This is a viciously premalignant disease with one or more polyps progressing through dysplasia to malignancy in untreated gene carriers with a median age at diagnosis of 40 years.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> <ref>PMID:1651563</ref> <ref>PMID:1338904</ref> <ref>PMID:1338691</ref> <ref>PMID:1338764</ref> <ref>PMID:7833149</ref> <ref>PMID:7833931</ref> <ref>PMID:8990002</ref> <ref>PMID:10470088</ref> Defects in APC are a cause of hereditary desmoid disease (HDD) [MIM:[https://omim.org/entry/135290 135290]; also known as familial infiltrative fibromatosis (FIF). HDD is an autosomal dominant trait with 100% penetrance and possible variable expression among affected relatives. HDD patients show multifocal fibromatosis of the paraspinal muscles, breast, occiput, arms, lower ribs, abdominal wall, and mesentery. Desmoid tumors appears also as a complication of familial adenomatous polyposis.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> Defects in APC are a cause of medulloblastoma (MDB) [MIM:[https://omim.org/entry/155255 155255]. MDB is a malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. Although the majority of medulloblastomas occur sporadically, some manifest within familial cancer syndromes such as Turcot syndrome and basal cell nevus syndrome (Gorlin syndrome).<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> <ref>PMID:10666372</ref> Defects in APC are a cause of mismatch repair cancer syndrome (MMRCS) [MIM:[https://omim.org/entry/276300 276300]; also known as Turcot syndrome or brain tumor-polyposis syndrome 1 (BTPS1). MMRCS is an autosomal dominant disorder characterized by malignant tumors of the brain associated with multiple colorectal adenomas. Skin features include sebaceous cysts, hyperpigmented and cafe au lait spots.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> <ref>PMID:7661930</ref> Defects in APC are a cause of gastric cancer (GASC) [MIM:[https://omim.org/entry/613659 613659]; also called gastric cancer intestinal or stomach cancer. Gastric cancer is 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.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> Defects in APC are a cause of hepatocellular carcinoma (HCC) [MIM:[https://omim.org/entry/114550 114550]. This defect includes also the disease entity termed hepatoblastoma.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/APC_HUMAN APC_HUMAN]] Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization.<ref>PMID:10947987</ref> <ref>PMID:17599059</ref> <ref>PMID:19893577</ref> <ref>PMID:19151759</ref> <ref>PMID:20937854</ref> [[https://www.uniprot.org/uniprot/KHDR1_HUMAN KHDR1_HUMAN]] Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export.<ref>PMID:9013542</ref> <ref>PMID:9045636</ref> <ref>PMID:11585385</ref> <ref>PMID:1374686</ref> [UniProtKB:Q60749][UniProtKB:Q8UUW7] Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase.<ref>PMID:9013542</ref> <ref>PMID:9045636</ref> <ref>PMID:11585385</ref>	+	[https://www.uniprot.org/uniprot/APC_HUMAN APC_HUMAN] Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization.<ref>PMID:10947987</ref> <ref>PMID:17599059</ref> <ref>PMID:19893577</ref> <ref>PMID:19151759</ref> <ref>PMID:20937854</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Akiyama, T]]	+	[[Category: Akiyama T]]
-	[[Category: Handa, N]]	+	[[Category: Handa N]]
-	[[Category: Ishizuku-Katsura, Y]]	+	[[Category: Ishizuku-Katsura Y]]
-	[[Category: Kato-Murayama, M]]	+	[[Category: Kato-Murayama M]]
-	[[Category: Morishita~~, E C.J~~]]	+	[[Category: Morishita ECJ]]
-	[[Category: Murayama, K]]	+	[[Category: Murayama K]]
-	~~[[Category: Structural genomic~~]]	+	[[Category: Shirouzu M]]
-	[[Category: Shirouzu, M]]	+	[[Category: Terada T]]
-	[[Category: Terada, T]]	+	[[Category: Tomabechi Y]]
-	[[Category: Tomabechi, Y]]	+	[[Category: Yokoyama S]]
-	[[Category: Yokoyama, S]]	+
-	~~[[Category: Adaptor protein]]~~	+
-	~~[[Category: Armadillo repeat superhelix]]~~	+
-	~~[[Category: National project on protein structural and functional analyse]]~~	+
-	~~[[Category: Nppsfa]]~~	+
-	~~[[Category: Regulation of wnt signaling]]~~	+
-	~~[[Category: Rna-binding protein]]~~	+
-	~~[[Category: Rsgi]]~~	+
-	~~[[Category: Signaling protein-splicing complex]]~~	+
-	~~[[Category: Signaling protein-splicing protein complex]]~~	+
-	~~[[Category: Tumor suppressor protein~~]]	+

OCA at 06:09, 8 June 2022

2022-06-08T06:09:01Z

←Older revision		Revision as of 06:09, 8 June 2022
Line 1:		Line 1:

	==Crystal structure of the complex between the armadillo repeat domain of adenomatous polyposis coli and the tyrosine-rich domain of Sam68==		==Crystal structure of the complex between the armadillo repeat domain of adenomatous polyposis coli and the tyrosine-rich domain of Sam68==
-	<StructureSection load='3qhe' size='340' side='right' caption='[[3qhe]], [[Resolution\|resolution]] 2.40Å' scene=''>	+	<StructureSection load='3qhe' size='340' side='right'caption='[[3qhe]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3qhe]] is a 4 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=3QHE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3QHE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3qhe]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QHE 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=3qhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qhe OCA], [~~http~~://pdbe.org/3qhe PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3qhe RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3qhe PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3qhe ProSAT]</span></td></tr>	+	</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=3qhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qhe OCA], [https://pdbe.org/3qhe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qhe RCSB], [https://www.ebi.ac.uk/pdbsum/3qhe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qhe ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/APC_HUMAN APC_HUMAN]] Defects in APC are a cause of familial adenomatous polyposis (FAP) [MIM:[~~http~~://omim.org/entry/175100 175100]]; which includes also Gardner syndrome (GS). FAP and GS contribute to tumor development in patients with uninherited forms of colorectal cancer. FAP is characterized by adenomatous polyps of the colon and rectum, but also of upper gastrointestinal tract (ampullary, duodenal and gastric adenomas). This is a viciously premalignant disease with one or more polyps progressing through dysplasia to malignancy in untreated gene carriers with a median age at diagnosis of 40 years.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> <ref>PMID:1651563</ref> <ref>PMID:1338904</ref> <ref>PMID:1338691</ref> <ref>PMID:1338764</ref> <ref>PMID:7833149</ref> <ref>PMID:7833931</ref> <ref>PMID:8990002</ref> <ref>PMID:10470088</ref> Defects in APC are a cause of hereditary desmoid disease (HDD) [MIM:[~~http~~://omim.org/entry/135290 135290]]; also known as familial infiltrative fibromatosis (FIF). HDD is an autosomal dominant trait with 100% penetrance and possible variable expression among affected relatives. HDD patients show multifocal fibromatosis of the paraspinal muscles, breast, occiput, arms, lower ribs, abdominal wall, and mesentery. Desmoid tumors appears also as a complication of familial adenomatous polyposis.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> Defects in APC are a cause of medulloblastoma (MDB) [MIM:[~~http~~://omim.org/entry/155255 155255]]. MDB is a malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. Although the majority of medulloblastomas occur sporadically, some manifest within familial cancer syndromes such as Turcot syndrome and basal cell nevus syndrome (Gorlin syndrome).<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> <ref>PMID:10666372</ref> Defects in APC are a cause of mismatch repair cancer syndrome (MMRCS) [MIM:[~~http~~://omim.org/entry/276300 276300]]; also known as Turcot syndrome or brain tumor-polyposis syndrome 1 (BTPS1). MMRCS is an autosomal dominant disorder characterized by malignant tumors of the brain associated with multiple colorectal adenomas. Skin features include sebaceous cysts, hyperpigmented and cafe au lait spots.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> <ref>PMID:7661930</ref> Defects in APC are a cause of gastric cancer (GASC) [MIM:[~~http~~://omim.org/entry/613659 613659]]; also called gastric cancer intestinal or stomach cancer. Gastric cancer is 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.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> Defects in APC are a cause of hepatocellular carcinoma (HCC) [MIM:[~~http~~://omim.org/entry/114550 114550]]. This defect includes also the disease entity termed hepatoblastoma.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref>	+	[[https://www.uniprot.org/uniprot/APC_HUMAN APC_HUMAN]] Defects in APC are a cause of familial adenomatous polyposis (FAP) [MIM:[https://omim.org/entry/175100 175100]]; which includes also Gardner syndrome (GS). FAP and GS contribute to tumor development in patients with uninherited forms of colorectal cancer. FAP is characterized by adenomatous polyps of the colon and rectum, but also of upper gastrointestinal tract (ampullary, duodenal and gastric adenomas). This is a viciously premalignant disease with one or more polyps progressing through dysplasia to malignancy in untreated gene carriers with a median age at diagnosis of 40 years.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> <ref>PMID:1651563</ref> <ref>PMID:1338904</ref> <ref>PMID:1338691</ref> <ref>PMID:1338764</ref> <ref>PMID:7833149</ref> <ref>PMID:7833931</ref> <ref>PMID:8990002</ref> <ref>PMID:10470088</ref> Defects in APC are a cause of hereditary desmoid disease (HDD) [MIM:[https://omim.org/entry/135290 135290]]; also known as familial infiltrative fibromatosis (FIF). HDD is an autosomal dominant trait with 100% penetrance and possible variable expression among affected relatives. HDD patients show multifocal fibromatosis of the paraspinal muscles, breast, occiput, arms, lower ribs, abdominal wall, and mesentery. Desmoid tumors appears also as a complication of familial adenomatous polyposis.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> Defects in APC are a cause of medulloblastoma (MDB) [MIM:[https://omim.org/entry/155255 155255]]. MDB is a malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. Although the majority of medulloblastomas occur sporadically, some manifest within familial cancer syndromes such as Turcot syndrome and basal cell nevus syndrome (Gorlin syndrome).<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> <ref>PMID:10666372</ref> Defects in APC are a cause of mismatch repair cancer syndrome (MMRCS) [MIM:[https://omim.org/entry/276300 276300]]; also known as Turcot syndrome or brain tumor-polyposis syndrome 1 (BTPS1). MMRCS is an autosomal dominant disorder characterized by malignant tumors of the brain associated with multiple colorectal adenomas. Skin features include sebaceous cysts, hyperpigmented and cafe au lait spots.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> <ref>PMID:7661930</ref> Defects in APC are a cause of gastric cancer (GASC) [MIM:[https://omim.org/entry/613659 613659]]; also called gastric cancer intestinal or stomach cancer. Gastric cancer is 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.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> Defects in APC are a cause of hepatocellular carcinoma (HCC) [MIM:[https://omim.org/entry/114550 114550]]. This defect includes also the disease entity termed hepatoblastoma.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/APC_HUMAN APC_HUMAN]] Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization.<ref>PMID:10947987</ref> <ref>PMID:17599059</ref> <ref>PMID:19893577</ref> <ref>PMID:19151759</ref> <ref>PMID:20937854</ref> [[~~http~~://www.uniprot.org/uniprot/KHDR1_HUMAN KHDR1_HUMAN]] Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export.<ref>PMID:9013542</ref> <ref>PMID:9045636</ref> <ref>PMID:11585385</ref> <ref>PMID:1374686</ref> [UniProtKB:Q60749][UniProtKB:Q8UUW7] Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase.<ref>PMID:9013542</ref> <ref>PMID:9045636</ref> <ref>PMID:11585385</ref>	+	[[https://www.uniprot.org/uniprot/APC_HUMAN APC_HUMAN]] Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization.<ref>PMID:10947987</ref> <ref>PMID:17599059</ref> <ref>PMID:19893577</ref> <ref>PMID:19151759</ref> <ref>PMID:20937854</ref> [[https://www.uniprot.org/uniprot/KHDR1_HUMAN KHDR1_HUMAN]] Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export.<ref>PMID:9013542</ref> <ref>PMID:9045636</ref> <ref>PMID:11585385</ref> <ref>PMID:1374686</ref> [UniProtKB:Q60749][UniProtKB:Q8UUW7] Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase.<ref>PMID:9013542</ref> <ref>PMID:9045636</ref> <ref>PMID:11585385</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 21:

	==See Also==		==See Also==
-	*[[~~Armadillo repeats~~\|~~Armadillo repeats~~]]	+	*[[Adenomatous polyposis coli\|Adenomatous polyposis coli]]
	== References ==		== References ==
	<references/>		<references/>
Line 27:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Akiyama, T]]		[[Category: Akiyama, T]]
	[[Category: Handa, N]]		[[Category: Handa, N]]

OCA at 10:06, 13 February 2019

2019-02-13T10:06:50Z

←Older revision		Revision as of 10:06, 13 February 2019
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 3qhe" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3qhe" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Armadillo repeats\|Armadillo repeats]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 02:37, 5 August 2016

2016-08-05T02:37:39Z

←Older revision		Revision as of 02:37, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the complex between the armadillo repeat domain of adenomatous polyposis coli and the tyrosine-rich domain of Sam68==		==Crystal structure of the complex between the armadillo repeat domain of adenomatous polyposis coli and the tyrosine-rich domain of Sam68==
	<StructureSection load='3qhe' size='340' side='right' caption='[[3qhe]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='3qhe' size='340' side='right' caption='[[3qhe]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3qhe]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QHE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QHE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3qhe]] is a 4 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=3QHE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QHE 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=3qhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qhe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qhe RCSB], [http://www.ebi.ac.uk/pdbsum/3qhe PDBsum]</span></td></tr>	+	</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=3qhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qhe OCA], [http://pdbe.org/3qhe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3qhe RCSB], [http://www.ebi.ac.uk/pdbsum/3qhe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3qhe ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 17:		Line 18:
	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 3qhe" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Akiyama, T]]		[[Category: Akiyama, T]]
	[[Category: Handa, N]]		[[Category: Handa, N]]

OCA at 10:12, 19 December 2014

2014-12-19T10:12:04Z

←Older revision		Revision as of 10:12, 19 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3qhe\| PDB=3qhe \| SCENE= }}~~	+	==Crystal structure of the complex between the armadillo repeat domain of adenomatous polyposis coli and the tyrosine-rich domain of Sam68==
-	===Crystal structure of the complex between the armadillo repeat domain of adenomatous polyposis coli and the tyrosine-rich domain of Sam68===	+	<StructureSection load='3qhe' size='340' side='right' caption='[[3qhe]], [[Resolution\|resolution]] 2.40Å' scene=''>
-	~~{{ABSTRACT_PUBMED_22000517}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3qhe]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QHE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QHE 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=3qhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qhe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qhe RCSB], [http://www.ebi.ac.uk/pdbsum/3qhe PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/APC_HUMAN APC_HUMAN]] Defects in APC are a cause of familial adenomatous polyposis (FAP) [MIM:[http://omim.org/entry/175100 175100]]; which includes also Gardner syndrome (GS). FAP and GS contribute to tumor development in patients with uninherited forms of colorectal cancer. FAP is characterized by adenomatous polyps of the colon and rectum, but also of upper gastrointestinal tract (ampullary, duodenal and gastric adenomas). This is a viciously premalignant disease with one or more polyps progressing through dysplasia to malignancy in untreated gene carriers with a median age at diagnosis of 40 years.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> <ref>PMID:1651563</ref> <ref>PMID:1338904</ref> <ref>PMID:1338691</ref> <ref>PMID:1338764</ref> <ref>PMID:7833149</ref> <ref>PMID:7833931</ref> <ref>PMID:8990002</ref> <ref>PMID:10470088</ref> Defects in APC are a cause of hereditary desmoid disease (HDD) [MIM:[http://omim.org/entry/135290 135290]]; also known as familial infiltrative fibromatosis (FIF). HDD is an autosomal dominant trait with 100% penetrance and possible variable expression among affected relatives. HDD patients show multifocal fibromatosis of the paraspinal muscles, breast, occiput, arms, lower ribs, abdominal wall, and mesentery. Desmoid tumors appears also as a complication of familial adenomatous polyposis.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> Defects in APC are a cause of medulloblastoma (MDB) [MIM:[http://omim.org/entry/155255 155255]]. MDB is a malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. Although the majority of medulloblastomas occur sporadically, some manifest within familial cancer syndromes such as Turcot syndrome and basal cell nevus syndrome (Gorlin syndrome).<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> <ref>PMID:10666372</ref> Defects in APC are a cause of mismatch repair cancer syndrome (MMRCS) [MIM:[http://omim.org/entry/276300 276300]]; also known as Turcot syndrome or brain tumor-polyposis syndrome 1 (BTPS1). MMRCS is an autosomal dominant disorder characterized by malignant tumors of the brain associated with multiple colorectal adenomas. Skin features include sebaceous cysts, hyperpigmented and cafe au lait spots.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> <ref>PMID:7661930</ref> Defects in APC are a cause of gastric cancer (GASC) [MIM:[http://omim.org/entry/613659 613659]]; also called gastric cancer intestinal or stomach cancer. Gastric cancer is 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.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref> Defects in APC are a cause of hepatocellular carcinoma (HCC) [MIM:[http://omim.org/entry/114550 114550]]. This defect includes also the disease entity termed hepatoblastoma.<ref>PMID:8940264</ref> <ref>PMID:10782927</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/APC_HUMAN APC_HUMAN]] Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization.<ref>PMID:10947987</ref> <ref>PMID:17599059</ref> <ref>PMID:19893577</ref> <ref>PMID:19151759</ref> <ref>PMID:20937854</ref> [[http://www.uniprot.org/uniprot/KHDR1_HUMAN KHDR1_HUMAN]] Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export.<ref>PMID:9013542</ref> <ref>PMID:9045636</ref> <ref>PMID:11585385</ref> <ref>PMID:1374686</ref> [UniProtKB:Q60749][UniProtKB:Q8UUW7] Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase.<ref>PMID:9013542</ref> <ref>PMID:9045636</ref> <ref>PMID:11585385</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Adenomatous polyposis coli (APC) is a tumor suppressor protein commonly mutated in colorectal tumors. APC plays important roles in Wnt signaling and other cellular processes. Here, we present the crystal structure of the armadillo repeat (Arm) domain of APC, which facilitates the binding of APC to various proteins. APC-Arm forms a superhelix with a positively charged groove. We also determined the structure of the complex of APC-Arm with the tyrosine-rich (YY) domain of the Src-associated in mitosis, 68 kDa protein (Sam68), which regulates TCF-1 alternative splicing. Sam68-YY forms numerous interactions with the residues on the groove and is thereby fixed in a bent conformation. We assessed the effects of mutations and phosphorylation on complex formation between APC-Arm and Sam68-YY. Structural comparisons revealed different modes of ligand recognition between the Arm domains of APC and other Arm-containing proteins.

-	~~==Disease==~~	+	Crystal structures of the armadillo repeat domain of adenomatous polyposis coli and its complex with the tyrosine-rich domain of sam68.,Morishita EC, Murayama K, Kato-Murayama M, Ishizuka-Katsura Y, Tomabechi Y, Hayashi T, Terada T, Handa N, Shirouzu M, Akiyama T, Yokoyama S Structure. 2011 Oct 12;19(10):1496-508. PMID:22000517<ref>PMID:22000517</ref>
-	~~[[http://www.uniprot.org/uniprot/APC_HUMAN APC_HUMAN]] Defects in APC are a cause~~ of ~~familial~~ adenomatous polyposis ~~(FAP) [MIM:[http://omim.org/entry/175100 175100]]; which includes also Gardner syndrome (GS). FAP~~ and ~~GS contribute to tumor development in patients~~ with ~~uninherited forms of colorectal cancer. FAP is characterized by adenomatous polyps of~~ the ~~colon and rectum, but also~~ of ~~upper gastrointestinal tract (ampullary, duodenal and gastric adenomas)~~. This is a viciously premalignant disease with one or more polyps progressing through dysplasia to malignancy in untreated gene carriers with a median age at diagnosis of 40 years.<ref>PMID:8940264</ref><ref>PMID:10782927</ref><ref>PMID:1651563</ref><ref>PMID:1338904</ref><ref>PMID:1338691</ref><ref>PMID:1338764</ref><ref>PMID:7833149</ref><ref>PMID:7833931</ref><ref>PMID:8990002</ref><ref>PMID:10470088</ref> Defects in APC are a cause of hereditary desmoid disease (HDD) [MIM:[http://omim.org/entry/135290 135290]]; also known as familial infiltrative fibromatosis (FIF). HDD is an autosomal dominant trait with 100% penetrance and possible variable expression among affected relatives. HDD patients show multifocal fibromatosis of the paraspinal muscles, ~~breast~~, ~~occiput~~, ~~arms~~, lower ribs, abdominal wall, and mesentery. Desmoid tumors appears also as a complication of familial adenomatous polyposis.<ref>PMID:8940264</ref><ref>PMID:10782927</ref> Defects in APC are a cause of medulloblastoma (MDB) [MIM:[http://omim.org/entry/155255 155255]]. MDB is a malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. Although the majority of medulloblastomas occur sporadically, some manifest within familial cancer syndromes such as Turcot syndrome and basal cell nevus syndrome (Gorlin syndrome).<ref>PMID:8940264</ref><ref>PMID:10782927</ref><ref>PMID:10666372</ref> Defects in APC are a cause of mismatch repair cancer syndrome (MMRCS) [MIM:[http://omim.org/entry/276300 276300]]; also known as Turcot syndrome or brain tumor-~~polyposis syndrome 1 (BTPS1). MMRCS is an autosomal dominant disorder characterized by malignant tumors of the brain associated with multiple colorectal adenomas. Skin features include sebaceous cysts~~, hyperpigmented and cafe au lait spots.<ref>PMID:8940264</ref><ref>PMID:10782927</ref><ref>PMID:7661930</ref> Defects in APC are a cause of gastric cancer (GASC) [MIM:[http://omim.org/entry/613659 613659]]; also called gastric cancer intestinal or stomach cancer. Gastric cancer is 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~~.~~<ref>PMID:8940264</ref><ref>PMID:10782927</ref> Defects in APC are a cause of hepatocellular carcinoma~~ (~~HCC~~) ~~[MIM~~:~~[http://omim~~.~~org/entry/114550 114550]]. This defect includes also the disease entity termed hepatoblastoma.<ref>~~PMID:~~8940264</ref>~~<ref>PMID:~~10782927~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/APC_HUMAN APC_HUMAN]] Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as~~ a ~~negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity~~ of ~~SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via~~ the ~~JNK signaling pathway in colorectal tumor cells~~. ~~Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex~~. ~~It is required for the localization of MACF1 to the cell membrane and this localization~~ of ~~MACF1 is critical for its function in microtubule stabilization~~.<~~ref~~>~~PMID:10947987~~</~~ref~~><ref>PMID:17599059</ref><ref>PMID:19893577</ref><ref>PMID:19151759</ref><ref>PMID:20937854</ref> [[http://www.uniprot.org/uniprot/KHDR1_HUMAN KHDR1_HUMAN]] Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export.<ref>PMID:9013542</ref><ref>PMID:9045636</ref><ref>PMID:11585385</ref><ref>PMID:1374686</ref>[UniProtKB:Q60749][UniProtKB:Q8UUW7] Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase.<ref>PMID:9013542</ref><ref>PMID:9045636</ref><ref>PMID:11585385</ref>	+	</div>
-		+	== References ==
-	==~~About this Structure==~~	+	<references/>
-	[[3qhe]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QHE OCA].	+	__TOC__
-		+	</StructureSection>
-	~~==Reference~~==	+
-	~~<ref group="xtra">PMID:022000517</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Akiyama, T.]]	+	[[Category: Akiyama, T]]
-	[[Category: Handa, N.]]	+	[[Category: Handa, N]]
-	[[Category: Ishizuku-Katsura, Y.]]	+	[[Category: Ishizuku-Katsura, Y]]
-	[[Category: Kato-Murayama, M.]]	+	[[Category: Kato-Murayama, M]]
-	[[Category: Morishita, E C.J.]]	+	[[Category: Morishita, E C.J]]
-	[[Category: Murayama, K.]]	+	[[Category: Murayama, K]]
-	[[Category: ~~RSGI, RIKEN~~ Structural ~~Genomics/Proteomics Initiative.~~]]	+	[[Category: Structural genomic]]
-	[[Category: Shirouzu, M.]]	+	[[Category: Shirouzu, M]]
-	[[Category: Terada, T.]]	+	[[Category: Terada, T]]
-	[[Category: Tomabechi, Y.]]	+	[[Category: Tomabechi, Y]]
-	[[Category: Yokoyama, S.]]	+	[[Category: Yokoyama, S]]
	[[Category: Adaptor protein]]		[[Category: Adaptor protein]]
	[[Category: Armadillo repeat superhelix]]		[[Category: Armadillo repeat superhelix]]
Line 31:		Line 38:
	[[Category: Nppsfa]]		[[Category: Nppsfa]]
	[[Category: Regulation of wnt signaling]]		[[Category: Regulation of wnt signaling]]
-	[[Category: Riken structural genomics/proteomics initiative]]
	[[Category: Rna-binding protein]]		[[Category: Rna-binding protein]]
	[[Category: Rsgi]]		[[Category: Rsgi]]
	[[Category: Signaling protein-splicing complex]]		[[Category: Signaling protein-splicing complex]]
	[[Category: Signaling protein-splicing protein complex]]		[[Category: Signaling protein-splicing protein complex]]
-	[[Category: Structural genomic]]
	[[Category: Tumor suppressor protein]]		[[Category: Tumor suppressor protein]]

OCA at 08:56, 24 March 2013

2013-03-24T08:56:55Z

←Older revision		Revision as of 08:56, 24 March 2013
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-	[[Image:3qhe.jpg\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_3qhe", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3qhe\| PDB=3qhe \| SCENE= }}		{{STRUCTURE_3qhe\| PDB=3qhe \| SCENE= }}
-
	===Crystal structure of the complex between the armadillo repeat domain of adenomatous polyposis coli and the tyrosine-rich domain of Sam68===		===Crystal structure of the complex between the armadillo repeat domain of adenomatous polyposis coli and the tyrosine-rich domain of Sam68===
		+	{{ABSTRACT_PUBMED_22000517}}

		+	==Disease==
		+	[[http://www.uniprot.org/uniprot/APC_HUMAN APC_HUMAN]] Defects in APC are a cause of familial adenomatous polyposis (FAP) [MIM:[http://omim.org/entry/175100 175100]]; which includes also Gardner syndrome (GS). FAP and GS contribute to tumor development in patients with uninherited forms of colorectal cancer. FAP is characterized by adenomatous polyps of the colon and rectum, but also of upper gastrointestinal tract (ampullary, duodenal and gastric adenomas). This is a viciously premalignant disease with one or more polyps progressing through dysplasia to malignancy in untreated gene carriers with a median age at diagnosis of 40 years.<ref>PMID:8940264</ref><ref>PMID:10782927</ref><ref>PMID:1651563</ref><ref>PMID:1338904</ref><ref>PMID:1338691</ref><ref>PMID:1338764</ref><ref>PMID:7833149</ref><ref>PMID:7833931</ref><ref>PMID:8990002</ref><ref>PMID:10470088</ref> Defects in APC are a cause of hereditary desmoid disease (HDD) [MIM:[http://omim.org/entry/135290 135290]]; also known as familial infiltrative fibromatosis (FIF). HDD is an autosomal dominant trait with 100% penetrance and possible variable expression among affected relatives. HDD patients show multifocal fibromatosis of the paraspinal muscles, breast, occiput, arms, lower ribs, abdominal wall, and mesentery. Desmoid tumors appears also as a complication of familial adenomatous polyposis.<ref>PMID:8940264</ref><ref>PMID:10782927</ref> Defects in APC are a cause of medulloblastoma (MDB) [MIM:[http://omim.org/entry/155255 155255]]. MDB is a malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. Although the majority of medulloblastomas occur sporadically, some manifest within familial cancer syndromes such as Turcot syndrome and basal cell nevus syndrome (Gorlin syndrome).<ref>PMID:8940264</ref><ref>PMID:10782927</ref><ref>PMID:10666372</ref> Defects in APC are a cause of mismatch repair cancer syndrome (MMRCS) [MIM:[http://omim.org/entry/276300 276300]]; also known as Turcot syndrome or brain tumor-polyposis syndrome 1 (BTPS1). MMRCS is an autosomal dominant disorder characterized by malignant tumors of the brain associated with multiple colorectal adenomas. Skin features include sebaceous cysts, hyperpigmented and cafe au lait spots.<ref>PMID:8940264</ref><ref>PMID:10782927</ref><ref>PMID:7661930</ref> Defects in APC are a cause of gastric cancer (GASC) [MIM:[http://omim.org/entry/613659 613659]]; also called gastric cancer intestinal or stomach cancer. Gastric cancer is 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.<ref>PMID:8940264</ref><ref>PMID:10782927</ref> Defects in APC are a cause of hepatocellular carcinoma (HCC) [MIM:[http://omim.org/entry/114550 114550]]. This defect includes also the disease entity termed hepatoblastoma.<ref>PMID:8940264</ref><ref>PMID:10782927</ref>

-	~~<!--~~	+	==Function==
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_22000517}}, adds~~ the ~~Publication Abstract to the page~~	+	[[http://www.uniprot.org/uniprot/APC_HUMAN APC_HUMAN]] Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization.<ref>PMID:10947987</ref><ref>PMID:17599059</ref><ref>PMID:19893577</ref><ref>PMID:19151759</ref><ref>PMID:20937854</ref> [[http://www.uniprot.org/uniprot/KHDR1_HUMAN KHDR1_HUMAN]] Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export.<ref>PMID:9013542</ref><ref>PMID:9045636</ref><ref>PMID:11585385</ref><ref>PMID:1374686</ref>[UniProtKB:Q60749][UniProtKB:Q8UUW7] Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase.<ref>PMID:9013542</ref><ref>PMID:9045636</ref><ref>PMID:11585385</ref>
-	(as ~~it appears on PubMed~~ at http://www.~~pubmed~~.~~gov)~~, ~~where 22000517 is~~ the ~~PubMed ID number~~.	+
-	-->	+
-	~~{{ABSTRACT_PUBMED_22000517}}~~	+

	==About this Structure==		==About this Structure==
Line 22:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:022000517</ref><references group="xtra"/>	+	<ref group="xtra">PMID:022000517</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Akiyama, T.]]		[[Category: Akiyama, T.]]

OCA at 08:19, 2 November 2011

2011-11-02T08:19:43Z

←Older revision		Revision as of 08:19, 2 November 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3qhe.jpg\|left\|200px]]

-	The ~~entry 3qhe~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3qhe", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3qhe\| PDB=3qhe \| SCENE= }}

-	~~Authors: Morishita, E.C.J., Murayama, K., Kato~~-~~Murayama, M., Ishizuku-Katsura, Y., Tomabechi, Y., Terada, T., Handa, N., Shirouzu, M., Akiyama, T., Yokoyama, S., RIKEN Structural Genomics/Proteomics Initiative (RSGI)~~	+	===Crystal structure of the complex between the armadillo repeat domain of adenomatous polyposis coli and the tyrosine-rich domain of Sam68===

-	~~Description~~:	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_22000517}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 22000517 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_22000517}}
		+
		+	==About this Structure==
		+	[[3qhe]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QHE OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:022000517</ref><references group="xtra"/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Akiyama, T.]]
		+	[[Category: Handa, N.]]
		+	[[Category: Ishizuku-Katsura, Y.]]
		+	[[Category: Kato-Murayama, M.]]
		+	[[Category: Morishita, E C.J.]]
		+	[[Category: Murayama, K.]]
		+	[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
		+	[[Category: Shirouzu, M.]]
		+	[[Category: Terada, T.]]
		+	[[Category: Tomabechi, Y.]]
		+	[[Category: Yokoyama, S.]]
		+	[[Category: Adaptor protein]]
		+	[[Category: Armadillo repeat superhelix]]
		+	[[Category: National project on protein structural and functional analyse]]
		+	[[Category: Nppsfa]]
		+	[[Category: Regulation of wnt signaling]]
		+	[[Category: Riken structural genomics/proteomics initiative]]
		+	[[Category: Rna-binding protein]]
		+	[[Category: Rsgi]]
		+	[[Category: Signaling protein-splicing complex]]
		+	[[Category: Signaling protein-splicing protein complex]]
		+	[[Category: Structural genomic]]
		+	[[Category: Tumor suppressor protein]]

OCA at 05:49, 9 February 2011

2011-02-09T05:49:46Z

←Older revision		Revision as of 05:49, 9 February 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3qhe is ON HOLD	+	The entry 3qhe is ON HOLD until Paper Publication

	Authors: Morishita, E.C.J., Murayama, K., Kato-Murayama, M., Ishizuku-Katsura, Y., Tomabechi, Y., Terada, T., Handa, N., Shirouzu, M., Akiyama, T., Yokoyama, S., RIKEN Structural Genomics/Proteomics Initiative (RSGI)		Authors: Morishita, E.C.J., Murayama, K., Kato-Murayama, M., Ishizuku-Katsura, Y., Tomabechi, Y., Terada, T., Handa, N., Shirouzu, M., Akiyama, T., Yokoyama, S., RIKEN Structural Genomics/Proteomics Initiative (RSGI)

	Description:		Description:

OCA: Protected "3qhe" [edit=sysop:move=sysop]

2011-02-02T06:12:46Z

Protected "3qhe" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:12, 2 February 2011

OCA: New page: '''Unreleased structure''' The entry 3qhe is ON HOLD Authors: Morishita, E.C.J., Murayama, K., Kato-Murayama, M., Ishizuku-Katsura, Y., Tomabechi, Y., Terada, T., Handa, N., Shirouzu, M...

2011-02-02T06:12:45Z

New page: '''Unreleased structure''' The entry 3qhe is ON HOLD Authors: Morishita, E.C.J., Murayama, K., Kato-Murayama, M., Ishizuku-Katsura, Y., Tomabechi, Y., Terada, T., Handa, N., Shirouzu, M...

New page

'''Unreleased structure'''

The entry 3qhe is ON HOLD

Authors: Morishita, E.C.J., Murayama, K., Kato-Murayama, M., Ishizuku-Katsura, Y., Tomabechi, Y., Terada, T., Handa, N., Shirouzu, M., Akiyama, T., Yokoyama, S., RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Description: