- INFO: Beginning work on ABCC2... {November 16, 2007 11:27:13 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:27:55 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = ATP-binding cassette, sub-family C (CFTR/MRP), member 2
| HGNCid = 53
| Symbol = ABCC2
| AltSymbols =; ABC30; CMOAT; DJS; KIAA1010; MRP2; cMRP
| OMIM = 601107
| ECnumber =
| Homologene = 68052
| MGIid = 1352447
| GeneAtlas_image1 = PBB_GE_ABCC2_206155_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008514 |text = organic anion transmembrane transporter activity}} {{GNF_GO|id=GO:0016887 |text = ATPase activity}} {{GNF_GO|id=GO:0042626 |text = ATPase activity, coupled to transmembrane movement of substances}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016324 |text = apical plasma membrane}} {{GNF_GO|id=GO:0046581 |text = intercellular canaliculus}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1244
| Hs_Ensembl = ENSG00000023839
| Hs_RefseqProtein = NP_000383
| Hs_RefseqmRNA = NM_000392
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 101532479
| Hs_GenLoc_end = 101601939
| Hs_Uniprot = Q92887
| Mm_EntrezGene = 12780
| Mm_Ensembl = ENSMUSG00000025194
| Mm_RefseqmRNA = NM_013806
| Mm_RefseqProtein = NP_038834
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 43835715
| Mm_GenLoc_end = 43891262
| Mm_Uniprot = Q8VI46
}}
}}
'''ATP-binding cassette, sub-family C (CFTR/MRP), member 2''', also known as '''ABCC2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ABCC2 ATP-binding cassette, sub-family C (CFTR/MRP), member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1244| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the MRP subfamily which is involved in multi-drug resistance. This protein is expressed in the canalicular (apical) part of the hepatocyte and functions in biliary transport. Substrates include anticancer drugs such as vinblastine; therefore, this protein appears to contribute to drug resistance in mammalian cells. Several different mutations in this gene have been observed in patients with Dubin-Johnson syndrome (DJS), an autosomal recessive disorder characterized by conjugated hyperbilirubinemia.<ref name="entrez">{{cite web | title = Entrez Gene: ABCC2 ATP-binding cassette, sub-family C (CFTR/MRP), member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1244| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Keppler D, König J |title=Hepatic secretion of conjugated drugs and endogenous substances. |journal=Semin. Liver Dis. |volume=20 |issue= 3 |pages= 265-72 |year= 2001 |pmid= 11076395 |doi= }}
*{{cite journal | author=Gerk PM, Vore M |title=Regulation of expression of the multidrug resistance-associated protein 2 (MRP2) and its role in drug disposition. |journal=J. Pharmacol. Exp. Ther. |volume=302 |issue= 2 |pages= 407-15 |year= 2002 |pmid= 12130697 |doi= 10.1124/jpet.102.035014 }}
*{{cite journal | author=Mayer R, Kartenbeck J, Büchler M, ''et al.'' |title=Expression of the MRP gene-encoded conjugate export pump in liver and its selective absence from the canalicular membrane in transport-deficient mutant hepatocytes. |journal=J. Cell Biol. |volume=131 |issue= 1 |pages= 137-50 |year= 1995 |pmid= 7559771 |doi= }}
*{{cite journal | author=Büchler M, König J, Brom M, ''et al.'' |title=cDNA cloning of the hepatocyte canalicular isoform of the multidrug resistance protein, cMrp, reveals a novel conjugate export pump deficient in hyperbilirubinemic mutant rats. |journal=J. Biol. Chem. |volume=271 |issue= 25 |pages= 15091-8 |year= 1996 |pmid= 8662992 |doi= }}
*{{cite journal | author=Taniguchi K, Wada M, Kohno K, ''et al.'' |title=A human canalicular multispecific organic anion transporter (cMOAT) gene is overexpressed in cisplatin-resistant human cancer cell lines with decreased drug accumulation. |journal=Cancer Res. |volume=56 |issue= 18 |pages= 4124-9 |year= 1996 |pmid= 8797578 |doi= }}
*{{cite journal | author=Paulusma CC, Kool M, Bosma PJ, ''et al.'' |title=A mutation in the human canalicular multispecific organic anion transporter gene causes the Dubin-Johnson syndrome. |journal=Hepatology |volume=25 |issue= 6 |pages= 1539-42 |year= 1997 |pmid= 9185779 |doi= 10.1002/hep.510250635 }}
*{{cite journal | author=van Kuijck MA, Kool M, Merkx GF, ''et al.'' |title=Assignment of the canalicular multispecific organic anion transporter gene (CMOAT) to human chromosome 10q24 and mouse chromosome 19D2 by fluorescent in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=77 |issue= 3-4 |pages= 285-7 |year= 1997 |pmid= 9284939 |doi= }}
*{{cite journal | author=Wada M, Toh S, Taniguchi K, ''et al.'' |title=Mutations in the canilicular multispecific organic anion transporter (cMOAT) gene, a novel ABC transporter, in patients with hyperbilirubinemia II/Dubin-Johnson syndrome. |journal=Hum. Mol. Genet. |volume=7 |issue= 2 |pages= 203-7 |year= 1998 |pmid= 9425227 |doi= }}
*{{cite journal | author=Evers R, Kool M, van Deemter L, ''et al.'' |title=Drug export activity of the human canalicular multispecific organic anion transporter in polarized kidney MDCK cells expressing cMOAT (MRP2) cDNA. |journal=J. Clin. Invest. |volume=101 |issue= 7 |pages= 1310-9 |year= 1998 |pmid= 9525973 |doi= }}
*{{cite journal | author=Kajihara S, Hisatomi A, Mizuta T, ''et al.'' |title=A splice mutation in the human canalicular multispecific organic anion transporter gene causes Dubin-Johnson syndrome. |journal=Biochem. Biophys. Res. Commun. |volume=253 |issue= 2 |pages= 454-7 |year= 1999 |pmid= 9878557 |doi= 10.1006/bbrc.1998.9780 }}
*{{cite journal | author=Toh S, Wada M, Uchiumi T, ''et al.'' |title=Genomic structure of the canalicular multispecific organic anion-transporter gene (MRP2/cMOAT) and mutations in the ATP-binding-cassette region in Dubin-Johnson syndrome. |journal=Am. J. Hum. Genet. |volume=64 |issue= 3 |pages= 739-46 |year= 1999 |pmid= 10053008 |doi= }}
*{{cite journal | author=Schaub TP, Kartenbeck J, König J, ''et al.'' |title=Expression of the MRP2 gene-encoded conjugate export pump in human kidney proximal tubules and in renal cell carcinoma. |journal=J. Am. Soc. Nephrol. |volume=10 |issue= 6 |pages= 1159-69 |year= 1999 |pmid= 10361853 |doi= }}
*{{cite journal | author=Tsujii H, König J, Rost D, ''et al.'' |title=Exon-intron organization of the human multidrug-resistance protein 2 (MRP2) gene mutated in Dubin-Johnson syndrome. |journal=Gastroenterology |volume=117 |issue= 3 |pages= 653-60 |year= 1999 |pmid= 10464142 |doi= }}
*{{cite journal | author=Kocher O, Comella N, Gilchrist A, ''et al.'' |title=PDZK1, a novel PDZ domain-containing protein up-regulated in carcinomas and mapped to chromosome 1q21, interacts with cMOAT (MRP2), the multidrug resistance-associated protein. |journal=Lab. Invest. |volume=79 |issue= 9 |pages= 1161-70 |year= 1999 |pmid= 10496535 |doi= }}
*{{cite journal | author=Tanaka T, Uchiumi T, Hinoshita E, ''et al.'' |title=The human multidrug resistance protein 2 gene: functional characterization of the 5'-flanking region and expression in hepatic cells. |journal=Hepatology |volume=30 |issue= 6 |pages= 1507-12 |year= 1999 |pmid= 10573531 |doi= 10.1002/hep.510300617 }}
*{{cite journal | author=St-Pierre MV, Serrano MA, Macias RI, ''et al.'' |title=Expression of members of the multidrug resistance protein family in human term placenta. |journal=Am. J. Physiol. Regul. Integr. Comp. Physiol. |volume=279 |issue= 4 |pages= R1495-503 |year= 2000 |pmid= 11004020 |doi= }}
*{{cite journal | author=Keitel V, Kartenbeck J, Nies AT, ''et al.'' |title=Impaired protein maturation of the conjugate export pump multidrug resistance protein 2 as a consequence of a deletion mutation in Dubin-Johnson syndrome. |journal=Hepatology |volume=32 |issue= 6 |pages= 1317-28 |year= 2001 |pmid= 11093739 |doi= 10.1053/jhep.2000.19791 }}
*{{cite journal | author=Ito S, Ieiri I, Tanabe M, ''et al.'' |title=Polymorphism of the ABC transporter genes, MDR1, MRP1 and MRP2/cMOAT, in healthy Japanese subjects. |journal=Pharmacogenetics |volume=11 |issue= 2 |pages= 175-84 |year= 2001 |pmid= 11266082 |doi= }}
*{{cite journal | author=Mor-Cohen R, Zivelin A, Rosenberg N, ''et al.'' |title=Identification and functional analysis of two novel mutations in the multidrug resistance protein 2 gene in Israeli patients with Dubin-Johnson syndrome. |journal=J. Biol. Chem. |volume=276 |issue= 40 |pages= 36923-30 |year= 2001 |pmid= 11477083 |doi= 10.1074/jbc.M105047200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ADAM10... {November 16, 2007 11:24:11 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:24:52 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ADAM10_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2ao7.
| PDB = {{PDB2|2ao7}}
| Name = ADAM metallopeptidase domain 10
| HGNCid = 188
| Symbol = ADAM10
| AltSymbols =; CD156c; HsT18717; MADM; kuz
| OMIM = 602192
| ECnumber =
| Homologene = 865
| MGIid = 109548
| GeneAtlas_image1 = PBB_GE_ADAM10_202603_at_tn.png
| GeneAtlas_image2 = PBB_GE_ADAM10_202604_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_ADAM10_214895_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004222 |text = metalloendopeptidase activity}} {{GNF_GO|id=GO:0005178 |text = integrin binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0019901 |text = protein kinase binding}} {{GNF_GO|id=GO:0042169 |text = SH2 domain binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0005798 |text = Golgi-associated vesicle}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0009986 |text = cell surface}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0001701 |text = in utero embryonic development}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006913 |text = nucleocytoplasmic transport}} {{GNF_GO|id=GO:0007162 |text = negative regulation of cell adhesion}} {{GNF_GO|id=GO:0007220 |text = Notch receptor processing}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0051089 |text = constitutive protein ectodomain proteolysis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 102
| Hs_Ensembl = ENSG00000137845
| Hs_RefseqProtein = NP_001101
| Hs_RefseqmRNA = NM_001110
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 56675802
| Hs_GenLoc_end = 56829469
| Hs_Uniprot = O14672
| Mm_EntrezGene = 11487
| Mm_Ensembl = ENSMUSG00000054693
| Mm_RefseqmRNA = NM_007399
| Mm_RefseqProtein = NP_031425
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 70478203
| Mm_GenLoc_end = 70579439
| Mm_Uniprot = Q6NZC0
}}
}}
'''ADAM metallopeptidase domain 10''', also known as '''ADAM10''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ADAM10 ADAM metallopeptidase domain 10| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=102| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Members of the ADAM family are cell surface proteins with a unique structure possessing both potential adhesion and protease domains. This gene encodes and ADAM family member that cleaves many proteins including TNF-alpha and E-cadherin.<ref name="entrez">{{cite web | title = Entrez Gene: ADAM10 ADAM metallopeptidase domain 10| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=102| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wolfsberg TG, Primakoff P, Myles DG, White JM |title=ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions. |journal=J. Cell Biol. |volume=131 |issue= 2 |pages= 275-8 |year= 1995 |pmid= 7593158 |doi= }}
*{{cite journal | author=O'Bryan JP, Fridell YW, Koski R, ''et al.'' |title=The transforming receptor tyrosine kinase, Axl, is post-translationally regulated by proteolytic cleavage. |journal=J. Biol. Chem. |volume=270 |issue= 2 |pages= 551-7 |year= 1995 |pmid= 7822279 |doi= }}
*{{cite journal | author=Howard L, Lu X, Mitchell S, ''et al.'' |title=Molecular cloning of MADM: a catalytically active mammalian disintegrin-metalloprotease expressed in various cell types. |journal=Biochem. J. |volume=317 ( Pt 1) |issue= |pages= 45-50 |year= 1996 |pmid= 8694785 |doi= }}
*{{cite journal | author=McKie N, Edwards T, Dallas DJ, ''et al.'' |title=Expression of members of a novel membrane linked metalloproteinase family (ADAM) in human articular chondrocytes. |journal=Biochem. Biophys. Res. Commun. |volume=230 |issue= 2 |pages= 335-9 |year= 1997 |pmid= 9016778 |doi= 10.1006/bbrc.1996.5957 }}
*{{cite journal | author=Rosendahl MS, Ko SC, Long DL, ''et al.'' |title=Identification and characterization of a pro-tumor necrosis factor-alpha-processing enzyme from the ADAM family of zinc metalloproteases. |journal=J. Biol. Chem. |volume=272 |issue= 39 |pages= 24588-93 |year= 1997 |pmid= 9305925 |doi= }}
*{{cite journal | author=Yamazaki K, Mizui Y, Tanaka I |title=Radiation hybrid mapping of human ADAM10 gene to chromosome 15. |journal=Genomics |volume=45 |issue= 2 |pages= 457-9 |year= 1998 |pmid= 9344679 |doi= 10.1006/geno.1997.4910 }}
*{{cite journal | author=Yamazaki K, Mizui Y, Sagane K, Tanaka I |title=Assignment of a disintegrin and metalloproteinase domain 10 (Adam10) gene to mouse chromosome 9. |journal=Genomics |volume=46 |issue= 3 |pages= 528-9 |year= 1998 |pmid= 9441766 |doi= 10.1006/geno.1997.5043 }}
*{{cite journal | author=Yavari R, Adida C, Bray-Ward P, ''et al.'' |title=Human metalloprotease-disintegrin Kuzbanian regulates sympathoadrenal cell fate in development and neoplasia. |journal=Hum. Mol. Genet. |volume=7 |issue= 7 |pages= 1161-7 |year= 1999 |pmid= 9618175 |doi= }}
*{{cite journal | author=Dallas DJ, Genever PG, Patton AJ, ''et al.'' |title=Localization of ADAM10 and Notch receptors in bone. |journal=Bone |volume=25 |issue= 1 |pages= 9-15 |year= 1999 |pmid= 10423016 |doi= }}
*{{cite journal | author=Dias Neto E, Correa RG, Verjovski-Almeida S, ''et al.'' |title=Shotgun sequencing of the human transcriptome with ORF expressed sequence tags. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3491-6 |year= 2000 |pmid= 10737800 |doi= }}
*{{cite journal | author=Hattori M, Osterfield M, Flanagan JG |title=Regulated cleavage of a contact-mediated axon repellent. |journal=Science |volume=289 |issue= 5483 |pages= 1360-5 |year= 2000 |pmid= 10958785 |doi= }}
*{{cite journal | author=Vincent B, Paitel E, Saftig P, ''et al.'' |title=The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein. |journal=J. Biol. Chem. |volume=276 |issue= 41 |pages= 37743-6 |year= 2001 |pmid= 11477090 |doi= 10.1074/jbc.M105677200 }}
*{{cite journal | author=Chubinskaya S, Mikhail R, Deutsch A, Tindal MH |title=ADAM-10 protein is present in human articular cartilage primarily in the membrane-bound form and is upregulated in osteoarthritis and in response to IL-1alpha in bovine nasal cartilage. |journal=J. Histochem. Cytochem. |volume=49 |issue= 9 |pages= 1165-76 |year= 2001 |pmid= 11511685 |doi= }}
*{{cite journal | author=Lemjabbar H, Basbaum C |title=Platelet-activating factor receptor and ADAM10 mediate responses to Staphylococcus aureus in epithelial cells. |journal=Nat. Med. |volume=8 |issue= 1 |pages= 41-6 |year= 2002 |pmid= 11786905 |doi= 10.1038/nm0102-41 }}
*{{cite journal | author=Arndt M, Lendeckel U, Röcken C, ''et al.'' |title=Altered expression of ADAMs (A Disintegrin And Metalloproteinase) in fibrillating human atria. |journal=Circulation |volume=105 |issue= 6 |pages= 720-5 |year= 2002 |pmid= 11839628 |doi= }}
*{{cite journal | author=Colciaghi F, Borroni B, Pastorino L, ''et al.'' |title=[alpha]-Secretase ADAM10 as well as [alpha]APPs is reduced in platelets and CSF of Alzheimer disease patients. |journal=Mol. Med. |volume=8 |issue= 2 |pages= 67-74 |year= 2002 |pmid= 12080182 |doi= }}
*{{cite journal | author=Lim R, Winteringham LN, Williams JH, ''et al.'' |title=MADM, a novel adaptor protein that mediates phosphorylation of the 14-3-3 binding site of myeloid leukemia factor 1. |journal=J. Biol. Chem. |volume=277 |issue= 43 |pages= 40997-1008 |year= 2002 |pmid= 12176995 |doi= 10.1074/jbc.M206041200 }}
*{{cite journal | author=Gatta LB, Albertini A, Ravid R, Finazzi D |title=Levels of beta-secretase BACE and alpha-secretase ADAM10 mRNAs in Alzheimer hippocampus. |journal=Neuroreport |volume=13 |issue= 16 |pages= 2031-3 |year= 2003 |pmid= 12438920 |doi= }}
*{{cite journal | author=Gutwein P, Mechtersheimer S, Riedle S, ''et al.'' |title=ADAM10-mediated cleavage of L1 adhesion molecule at the cell surface and in released membrane vesicles. |journal=FASEB J. |volume=17 |issue= 2 |pages= 292-4 |year= 2003 |pmid= 12475894 |doi= 10.1096/fj.02-0430fje }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on APOA2... {November 16, 2007 11:24:52 AM PST}
- SEARCH REDIRECT: Control Box Found: APOA2 {November 16, 2007 11:25:10 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 11:25:11 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 11:25:11 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 11:25:11 AM PST}
- UPDATED: Updated protein page: APOA2 {November 16, 2007 11:25:17 AM PST}
- INFO: Beginning work on BARD1... {November 16, 2007 11:25:17 AM PST}
- SEARCH REDIRECT: Control Box Found: BARD1 {November 16, 2007 11:25:37 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 11:25:38 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 11:25:38 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 11:25:38 AM PST}
- UPDATED: Updated protein page: BARD1 {November 16, 2007 11:25:44 AM PST}
- INFO: Beginning work on BCL10... {November 16, 2007 11:36:42 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:37:11 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = B-cell CLL/lymphoma 10
| HGNCid = 989
| Symbol = BCL10
| AltSymbols =; CARMEN; CIPER; CLAP; c-E10; mE10
| OMIM = 603517
| ECnumber =
| Homologene = 2912
| MGIid = 1337994
| Function = {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0008022 |text = protein C-terminus binding}} {{GNF_GO|id=GO:0019209 |text = kinase activator activity}} {{GNF_GO|id=GO:0031625 |text = ubiquitin protein ligase binding}} {{GNF_GO|id=GO:0043130 |text = ubiquitin binding}} {{GNF_GO|id=GO:0043422 |text = protein kinase B binding}} {{GNF_GO|id=GO:0043621 |text = protein self-association}} {{GNF_GO|id=GO:0051059 |text = NF-kappaB binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0032449 |text = CBM complex}} {{GNF_GO|id=GO:0042101 |text = T cell receptor complex}} {{GNF_GO|id=GO:0045121 |text = lipid raft}} {{GNF_GO|id=GO:0046696 |text = lipopolysaccharide receptor complex}} {{GNF_GO|id=GO:0048471 |text = perinuclear region of cytoplasm}}
| Process = {{GNF_GO|id=GO:0002224 |text = toll-like receptor signaling pathway}} {{GNF_GO|id=GO:0002237 |text = response to molecule of bacterial origin}} {{GNF_GO|id=GO:0002250 |text = adaptive immune response}} {{GNF_GO|id=GO:0002906 |text = negative regulation of mature B cell apoptosis}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007249 |text = I-kappaB kinase/NF-kappaB cascade}} {{GNF_GO|id=GO:0008219 |text = cell death}} {{GNF_GO|id=GO:0016064 |text = immunoglobulin mediated immune response}} {{GNF_GO|id=GO:0031398 |text = positive regulation of protein ubiquitination}} {{GNF_GO|id=GO:0032765 |text = positive regulation of mast cell cytokine production}} {{GNF_GO|id=GO:0042109 |text = lymphotoxin A biosynthetic process}} {{GNF_GO|id=GO:0042221 |text = response to chemical stimulus}} {{GNF_GO|id=GO:0042226 |text = interleukin-6 biosynthetic process}} {{GNF_GO|id=GO:0042327 |text = positive regulation of phosphorylation}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}} {{GNF_GO|id=GO:0045087 |text = innate immune response}} {{GNF_GO|id=GO:0045416 |text = positive regulation of interleukin-8 biosynthetic process}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}} {{GNF_GO|id=GO:0045893 |text = positive regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0050852 |text = T cell receptor signaling pathway}} {{GNF_GO|id=GO:0051092 |text = activation of NF-kappaB transcription factor}} {{GNF_GO|id=GO:0051260 |text = protein homooligomerization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8915
| Hs_Ensembl =
| Hs_RefseqProtein = NP_003912
| Hs_RefseqmRNA = NM_003921
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 12042
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_009740
| Mm_RefseqProtein = NP_033870
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''B-cell CLL/lymphoma 10''', also known as '''BCL10''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BCL10 B-cell CLL/lymphoma 10| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8915| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene was identified by its translocation in a case of mucosa-associated lymphoid tissue (MALT) lymphoma. The protein encoded by this gene contains a caspase recruitment domain (CARD), and has been shown to induce apoptosis and to activate NF-kappaB. This protein is reported to interact with other CARD domain containing proteins including CARD9, 10, 11 and 14, which are thought to function as upstream regulators in NF-kappaB signaling. This protein is found to form a complex with MALT1, a protein encoded by another gene known to be translocated in MALT lymphoma. MALT1 and this protein are thought to synergize in the activation of NF-kappaB, and the deregulation of either of them may contribute to the same pathogenetic process that leads to the malignancy.<ref name="entrez">{{cite web | title = Entrez Gene: BCL10 B-cell CLL/lymphoma 10| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8915| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bertoni F, Cavalli F, Cotter FE, Zucca E |title=Genetic alterations underlying the pathogenesis of MALT lymphoma. |journal=Hematol. J. |volume=3 |issue= 1 |pages= 10-3 |year= 2003 |pmid= 11960389 |doi= 10.1038/sj/thj/6200146 }}
*{{cite journal | author=Lee WC, Balsara B, Liu Z, ''et al.'' |title=Loss of heterozygosity analysis defines a critical region in chromosome 1p22 commonly deleted in human malignant mesothelioma. |journal=Cancer Res. |volume=56 |issue= 19 |pages= 4297-301 |year= 1996 |pmid= 8813110 |doi= }}
*{{cite journal | author=Willis TG, Jadayel DM, Du MQ, ''et al.'' |title=Bcl10 is involved in t(1;14)(p22;q32) of MALT B cell lymphoma and mutated in multiple tumor types. |journal=Cell |volume=96 |issue= 1 |pages= 35-45 |year= 1999 |pmid= 9989495 |doi= }}
*{{cite journal | author=Koseki T, Inohara N, Chen S, ''et al.'' |title=CIPER, a novel NF kappaB-activating protein containing a caspase recruitment domain with homology to Herpesvirus-2 protein E10. |journal=J. Biol. Chem. |volume=274 |issue= 15 |pages= 9955-61 |year= 1999 |pmid= 10187770 |doi= }}
*{{cite journal | author=Thome M, Martinon F, Hofmann K, ''et al.'' |title=Equine herpesvirus-2 E10 gene product, but not its cellular homologue, activates NF-kappaB transcription factor and c-Jun N-terminal kinase. |journal=J. Biol. Chem. |volume=274 |issue= 15 |pages= 9962-8 |year= 1999 |pmid= 10187771 |doi= }}
*{{cite journal | author=Yan M, Lee J, Schilbach S, ''et al.'' |title=mE10, a novel caspase recruitment domain-containing proapoptotic molecule. |journal=J. Biol. Chem. |volume=274 |issue= 15 |pages= 10287-92 |year= 1999 |pmid= 10187815 |doi= }}
*{{cite journal | author=Zhang Q, Siebert R, Yan M, ''et al.'' |title=Inactivating mutations and overexpression of BCL10, a caspase recruitment domain-containing gene, in MALT lymphoma with t(1;14)(p22;q32). |journal=Nat. Genet. |volume=22 |issue= 1 |pages= 63-8 |year= 1999 |pmid= 10319863 |doi= 10.1038/8767 }}
*{{cite journal | author=Srinivasula SM, Ahmad M, Lin JH, ''et al.'' |title=CLAP, a novel caspase recruitment domain-containing protein in the tumor necrosis factor receptor pathway, regulates NF-kappaB activation and apoptosis. |journal=J. Biol. Chem. |volume=274 |issue= 25 |pages= 17946-54 |year= 1999 |pmid= 10364242 |doi= }}
*{{cite journal | author=Apostolou S, De Rienzo A, Murthy SS, ''et al.'' |title=Absence of BCL10 mutations in human malignant mesothelioma. |journal=Cell |volume=97 |issue= 6 |pages= 684-6; discussion 686-8 |year= 1999 |pmid= 10380921 |doi= }}
*{{cite journal | author=Costanzo A, Guiet C, Vito P |title=c-E10 is a caspase-recruiting domain-containing protein that interacts with components of death receptors signaling pathway and activates nuclear factor-kappaB. |journal=J. Biol. Chem. |volume=274 |issue= 29 |pages= 20127-32 |year= 1999 |pmid= 10400625 |doi= }}
*{{cite journal | author=Yoneda T, Imaizumi K, Maeda M, ''et al.'' |title=Regulatory mechanisms of TRAF2-mediated signal transduction by Bcl10, a MALT lymphoma-associated protein. |journal=J. Biol. Chem. |volume=275 |issue= 15 |pages= 11114-20 |year= 2000 |pmid= 10753917 |doi= }}
*{{cite journal | author=Ye H, Dogan A, Karran L, ''et al.'' |title=BCL10 expression in normal and neoplastic lymphoid tissue. Nuclear localization in MALT lymphoma. |journal=Am. J. Pathol. |volume=157 |issue= 4 |pages= 1147-54 |year= 2000 |pmid= 11021819 |doi= }}
*{{cite journal | author=Bertin J, Guo Y, Wang L, ''et al.'' |title=CARD9 is a novel caspase recruitment domain-containing protein that interacts with BCL10/CLAP and activates NF-kappa B. |journal=J. Biol. Chem. |volume=275 |issue= 52 |pages= 41082-6 |year= 2001 |pmid= 11053425 |doi= 10.1074/jbc.C000726200 }}
*{{cite journal | author=Uren AG, O'Rourke K, Aravind LA, ''et al.'' |title=Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma. |journal=Mol. Cell |volume=6 |issue= 4 |pages= 961-7 |year= 2000 |pmid= 11090634 |doi= }}
*{{cite journal | author=Poyet JL, Srinivasula SM, Alnemri ES |title=vCLAP, a caspase-recruitment domain-containing protein of equine Herpesvirus-2, persistently activates the Ikappa B kinases through oligomerization of IKKgamma. |journal=J. Biol. Chem. |volume=276 |issue= 5 |pages= 3183-7 |year= 2001 |pmid= 11113112 |doi= 10.1074/jbc.C000792200 }}
*{{cite journal | author=Ruland J, Duncan GS, Elia A, ''et al.'' |title=Bcl10 is a positive regulator of antigen receptor-induced activation of NF-kappaB and neural tube closure. |journal=Cell |volume=104 |issue= 1 |pages= 33-42 |year= 2001 |pmid= 11163238 |doi= }}
*{{cite journal | author=Wang L, Guo Y, Huang WJ, ''et al.'' |title=Card10 is a novel caspase recruitment domain/membrane-associated guanylate kinase family member that interacts with BCL10 and activates NF-kappa B. |journal=J. Biol. Chem. |volume=276 |issue= 24 |pages= 21405-9 |year= 2001 |pmid= 11259443 |doi= 10.1074/jbc.M102488200 }}
*{{cite journal | author=Lucas PC, Yonezumi M, Inohara N, ''et al.'' |title=Bcl10 and MALT1, independent targets of chromosomal translocation in malt lymphoma, cooperate in a novel NF-kappa B signaling pathway. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 19012-9 |year= 2001 |pmid= 11262391 |doi= 10.1074/jbc.M009984200 }}
*{{cite journal | author=Bertin J, Wang L, Guo Y, ''et al.'' |title=CARD11 and CARD14 are novel caspase recruitment domain (CARD)/membrane-associated guanylate kinase (MAGUK) family members that interact with BCL10 and activate NF-kappa B. |journal=J. Biol. Chem. |volume=276 |issue= 15 |pages= 11877-82 |year= 2001 |pmid= 11278692 |doi= 10.1074/jbc.M010512200 }}
*{{cite journal | author=Gaide O, Martinon F, Micheau O, ''et al.'' |title=Carma1, a CARD-containing binding partner of Bcl10, induces Bcl10 phosphorylation and NF-kappaB activation. |journal=FEBS Lett. |volume=496 |issue= 2-3 |pages= 121-7 |year= 2001 |pmid= 11356195 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CA9... {November 16, 2007 11:25:44 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:26:09 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Carbonic anhydrase IX
| HGNCid = 1383
| Symbol = CA9
| AltSymbols =; CAIX; MN
| OMIM = 603179
| ECnumber =
| Homologene = 20325
| MGIid = 2447188
| GeneAtlas_image1 = PBB_GE_CA9_205199_at_tn.png
| Function = {{GNF_GO|id=GO:0004089 |text = carbonate dehydratase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016829 |text = lyase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0002009 |text = morphogenesis of an epithelium}} {{GNF_GO|id=GO:0006730 |text = one-carbon compound metabolic process}} {{GNF_GO|id=GO:0046903 |text = secretion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 768
| Hs_Ensembl = ENSG00000107159
| Hs_RefseqProtein = NP_001207
| Hs_RefseqmRNA = NM_001216
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 35663853
| Hs_GenLoc_end = 35671156
| Hs_Uniprot = Q16790
| Mm_EntrezGene = 230099
| Mm_Ensembl = ENSMUSG00000028463
| Mm_RefseqmRNA = NM_139305
| Mm_RefseqProtein = NP_647466
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 43528107
| Mm_GenLoc_end = 43534829
| Mm_Uniprot = Q3TLN7
}}
}}
'''Carbonic anhydrase IX''', also known as '''CA9''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CA9 carbonic anhydrase IX| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=768| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. They show extensive diversity in tissue distribution and in their subcellular localization. CA IX is a transmembrane protein and the only tumor-associated carbonic anhydrase isoenzyme known. It is expressed in all clear-cell renal cell carcinoma, but is not detected in normal kidney or most other normal tissues. It may be involved in cell proliferation and transformation. This gene was mapped to 17q21.2 by fluorescence in situ hybridization, however, radiation hybrid mapping localized it to 9p13-p12.<ref name="entrez">{{cite web | title = Entrez Gene: CA9 carbonic anhydrase IX| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=768| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nishimori I, Onishi S |title=Carbonic anhydrase isozymes in the human pancreas. |journal=Digestive and liver disease : official journal of the Italian Society of Gastroenterology and the Italian Association for the Study of the Liver |volume=33 |issue= 1 |pages= 68-74 |year= 2001 |pmid= 11303978 |doi= }}
*{{cite journal | author=Pastoreková S, Závadová Z, Kostál M, ''et al.'' |title=A novel quasi-viral agent, MaTu, is a two-component system. |journal=Virology |volume=187 |issue= 2 |pages= 620-6 |year= 1992 |pmid= 1312272 |doi= }}
*{{cite journal | author=Pastorek J, Pastoreková S, Callebaut I, ''et al.'' |title=Cloning and characterization of MN, a human tumor-associated protein with a domain homologous to carbonic anhydrase and a putative helix-loop-helix DNA binding segment. |journal=Oncogene |volume=9 |issue= 10 |pages= 2877-88 |year= 1994 |pmid= 8084592 |doi= }}
*{{cite journal | author=Závada J, Závadová Z, Pastoreková S, ''et al.'' |title=Expression of MaTu-MN protein in human tumor cultures and in clinical specimens. |journal=Int. J. Cancer |volume=54 |issue= 2 |pages= 268-74 |year= 1993 |pmid= 8486430 |doi= }}
*{{cite journal | author=Opavský R, Pastoreková S, Zelník V, ''et al.'' |title=Human MN/CA9 gene, a novel member of the carbonic anhydrase family: structure and exon to protein domain relationships. |journal=Genomics |volume=33 |issue= 3 |pages= 480-7 |year= 1996 |pmid= 8661007 |doi= }}
*{{cite journal | author=Pastoreková S, Parkkila S, Parkkila AK, ''et al.'' |title=Carbonic anhydrase IX, MN/CA IX: analysis of stomach complementary DNA sequence and expression in human and rat alimentary tracts. |journal=Gastroenterology |volume=112 |issue= 2 |pages= 398-408 |year= 1997 |pmid= 9024293 |doi= }}
*{{cite journal | author=Saarnio J, Parkkila S, Parkkila AK, ''et al.'' |title=Immunohistochemistry of carbonic anhydrase isozyme IX (MN/CA IX) in human gut reveals polarized expression in the epithelial cells with the highest proliferative capacity. |journal=J. Histochem. Cytochem. |volume=46 |issue= 4 |pages= 497-504 |year= 1998 |pmid= 9524195 |doi= }}
*{{cite journal | author=Ivanov SV, Kuzmin I, Wei MH, ''et al.'' |title=Down-regulation of transmembrane carbonic anhydrases in renal cell carcinoma cell lines by wild-type von Hippel-Lindau transgenes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 21 |pages= 12596-601 |year= 1998 |pmid= 9770531 |doi= }}
*{{cite journal | author=Nakagawa Y, Uemura H, Hirao Y, ''et al.'' |title=Radiation hybrid mapping of the human MN/CA9 locus to chromosome band 9p12-p13. |journal=Genomics |volume=53 |issue= 1 |pages= 118-9 |year= 1998 |pmid= 9787087 |doi= 10.1006/geno.1998.5483 }}
*{{cite journal | author=Grabmaier K, Vissers JL, De Weijert MC, ''et al.'' |title=Molecular cloning and immunogenicity of renal cell carcinoma-associated antigen G250. |journal=Int. J. Cancer |volume=85 |issue= 6 |pages= 865-70 |year= 2000 |pmid= 10709109 |doi= }}
*{{cite journal | author=Kivelä AJ, Parkkila S, Saarnio J, ''et al.'' |title=Expression of transmembrane carbonic anhydrase isoenzymes IX and XII in normal human pancreas and pancreatic tumours. |journal=Histochem. Cell Biol. |volume=114 |issue= 3 |pages= 197-204 |year= 2001 |pmid= 11083462 |doi= }}
*{{cite journal | author=Wingo T, Tu C, Laipis PJ, Silverman DN |title=The catalytic properties of human carbonic anhydrase IX. |journal=Biochem. Biophys. Res. Commun. |volume=288 |issue= 3 |pages= 666-9 |year= 2001 |pmid= 11676494 |doi= 10.1006/bbrc.2001.5824 }}
*{{cite journal | author=Kivela AJ, Saarnio J, Karttunen TJ, ''et al.'' |title=Differential expression of cytoplasmic carbonic anhydrases, CA I and II, and membrane-associated isozymes, CA IX and XII, in normal mucosa of large intestine and in colorectal tumors. |journal=Dig. Dis. Sci. |volume=46 |issue= 10 |pages= 2179-86 |year= 2001 |pmid= 11680594 |doi= }}
*{{cite journal | author=Koukourakis MI, Giatromanolaki A, Sivridis E, ''et al.'' |title=Hypoxia-regulated carbonic anhydrase-9 (CA9) relates to poor vascularization and resistance of squamous cell head and neck cancer to chemoradiotherapy. |journal=Clin. Cancer Res. |volume=7 |issue= 11 |pages= 3399-403 |year= 2002 |pmid= 11705854 |doi= }}
*{{cite journal | author=Grabmaier K, de Weijert M, Uemura H, ''et al.'' |title=Renal cell carcinoma-associated G250 methylation and expression: in vivo and in vitro studies. |journal=Urology |volume=60 |issue= 2 |pages= 357-62 |year= 2002 |pmid= 12137853 |doi= }}
*{{cite journal | author=Kaluz S, Kaluzová M, Chrastina A, ''et al.'' |title=Lowered oxygen tension induces expression of the hypoxia marker MN/carbonic anhydrase IX in the absence of hypoxia-inducible factor 1 alpha stabilization: a role for phosphatidylinositol 3'-kinase. |journal=Cancer Res. |volume=62 |issue= 15 |pages= 4469-77 |year= 2002 |pmid= 12154057 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Swinson DE, Jones JL, Richardson D, ''et al.'' |title=Carbonic anhydrase IX expression, a novel surrogate marker of tumor hypoxia, is associated with a poor prognosis in non-small-cell lung cancer. |journal=J. Clin. Oncol. |volume=21 |issue= 3 |pages= 473-82 |year= 2003 |pmid= 12560438 |doi= }}
*{{cite journal | author=Bui MH, Seligson D, Han KR, ''et al.'' |title=Carbonic anhydrase IX is an independent predictor of survival in advanced renal clear cell carcinoma: implications for prognosis and therapy. |journal=Clin. Cancer Res. |volume=9 |issue= 2 |pages= 802-11 |year= 2003 |pmid= 12576453 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CCKBR... {November 16, 2007 11:26:09 AM PST}
- SEARCH REDIRECT: Control Box Found: CCKBR {November 16, 2007 11:27:06 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 11:27:07 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 11:27:07 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 11:27:07 AM PST}
- UPDATED: Updated protein page: CCKBR {November 16, 2007 11:27:13 AM PST}
- INFO: Beginning work on DCTN1... {November 16, 2007 11:27:55 AM PST}
- SEARCH REDIRECT: Control Box Found: DCTN1 {November 16, 2007 11:28:20 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 11:28:21 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 11:28:21 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 11:28:21 AM PST}
- UPDATED: Updated protein page: DCTN1 {November 16, 2007 11:28:26 AM PST}
- INFO: Beginning work on GNRHR... {November 16, 2007 11:28:26 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:29:00 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Gonadotropin-releasing hormone receptor
| HGNCid = 4421
| Symbol = GNRHR
| AltSymbols =; GNRHR1; GRHR; LHRHR; LRHR
| OMIM = 138850
| ECnumber =
| Homologene = 350
| MGIid = 95790
| GeneAtlas_image1 = PBB_GE_GNRHR_216341_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_GNRHR_211522_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_GNRHR_211523_at_tn.png
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004968 |text = gonadotropin-releasing hormone receptor activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2798
| Hs_Ensembl = ENSG00000109163
| Hs_RefseqProtein = NP_000397
| Hs_RefseqmRNA = NM_000406
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 68285701
| Hs_GenLoc_end = 68304399
| Hs_Uniprot = P30968
| Mm_EntrezGene = 14715
| Mm_Ensembl = ENSMUSG00000029255
| Mm_RefseqmRNA = NM_010323
| Mm_RefseqProtein = NP_034453
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 87256547
| Mm_GenLoc_end = 87272431
| Mm_Uniprot = Q01776
}}
}}
'''Gonadotropin-releasing hormone receptor''', also known as '''GNRHR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GNRHR gonadotropin-releasing hormone receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2798| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes the receptor for type 1 gonadotropin-releasing hormone. This receptor is a member of the seven-transmembrane, G-protein coupled receptor (GPCR) family. It is expressed on the surface of pituitary gonadotrope cells as well as lymphocytes, breast, ovary, and prostate. Following binding of gonadotropin-releasing hormone, the receptor associates with G-proteins that activate a phosphatidylinositol-calcium second messenger system. Activation of the receptor ultimately causes the release of gonadotropic luteinizing hormone (LH) and follicle stimulating hormone (FSH). Defects in this gene are a cause of hypogonadotropic hypogonadism (HH). Alternative splicing results in multiple transcript variants encoding different isoforms. More than 18 transcription initiation sites in the 5' region and multiple polyA signals in the 3' region have been identified for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: GNRHR gonadotropin-releasing hormone receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2798| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Michel U, Farnworth P, Findlay JK |title=Follistatins: more than follicle-stimulating hormone suppressing proteins. |journal=Mol. Cell. Endocrinol. |volume=91 |issue= 1-2 |pages= 1-11 |year= 1993 |pmid= 8472841 |doi= }}
*{{cite journal | author=Flanagan CA, Millar RP, Illing N |title=Advances in understanding gonadotrophin-releasing hormone receptor structure and ligand interactions. |journal=Rev. Reprod. |volume=2 |issue= 2 |pages= 113-20 |year= 1998 |pmid= 9414473 |doi= }}
*{{cite journal | author=Limonta P, Moretti RM, Marelli MM, Motta M |title=The biology of gonadotropin hormone-releasing hormone: role in the control of tumor growth and progression in humans. |journal=Frontiers in neuroendocrinology |volume=24 |issue= 4 |pages= 279-95 |year= 2004 |pmid= 14726258 |doi= }}
*{{cite journal | author=Bédécarrats GY, Kaiser UB |title=Mutations in the human gonadotropin-releasing hormone receptor: insights into receptor biology and function. |journal=Semin. Reprod. Med. |volume=25 |issue= 5 |pages= 368-78 |year= 2007 |pmid= 17710733 |doi= 10.1055/s-2007-984743 }}
*{{cite journal | author=Kakar SS, Musgrove LC, Devor DC, ''et al.'' |title=Cloning, sequencing, and expression of human gonadotropin releasing hormone (GnRH) receptor. |journal=Biochem. Biophys. Res. Commun. |volume=189 |issue= 1 |pages= 289-95 |year= 1992 |pmid= 1333190 |doi= }}
*{{cite journal | author=Kakar SS, Grizzle WE, Neill JD |title=The nucleotide sequences of human GnRH receptors in breast and ovarian tumors are identical with that found in pituitary. |journal=Mol. Cell. Endocrinol. |volume=106 |issue= 1-2 |pages= 145-9 |year= 1995 |pmid= 7534732 |doi= }}
*{{cite journal | author=Leung PC, Squire J, Peng C, ''et al.'' |title=Mapping of the gonadotropin-releasing hormone (GnRH) receptor gene to human chromosome 4q21.2 by fluorescence in situ hybridization. |journal=Mamm. Genome |volume=6 |issue= 4 |pages= 309-10 |year= 1995 |pmid= 7613048 |doi= }}
*{{cite journal | author=Fan NC, Peng C, Krisinger J, Leung PC |title=The human gonadotropin-releasing hormone receptor gene: complete structure including multiple promoters, transcription initiation sites, and polyadenylation signals. |journal=Mol. Cell. Endocrinol. |volume=107 |issue= 2 |pages= R1-8 |year= 1995 |pmid= 7768323 |doi= }}
*{{cite journal | author=Fan NC, Jeung EB, Peng C, ''et al.'' |title=The human gonadotropin-releasing hormone (GnRH) receptor gene: cloning, genomic organization and chromosomal assignment. |journal=Mol. Cell. Endocrinol. |volume=103 |issue= 1-2 |pages= R1-6 |year= 1994 |pmid= 7958384 |doi= }}
*{{cite journal | author=Chi L, Zhou W, Prikhozhan A, ''et al.'' |title=Cloning and characterization of the human GnRH receptor. |journal=Mol. Cell. Endocrinol. |volume=91 |issue= 1-2 |pages= R1-6 |year= 1993 |pmid= 8386108 |doi= }}
*{{cite journal | author=Grosse R, Schöneberg T, Schultz G, Gudermann T |title=Inhibition of gonadotropin-releasing hormone receptor signaling by expression of a splice variant of the human receptor. |journal=Mol. Endocrinol. |volume=11 |issue= 9 |pages= 1305-18 |year= 1997 |pmid= 9259321 |doi= }}
*{{cite journal | author=Kakar SS |title=Molecular structure of the human gonadotropin-releasing hormone receptor gene. |journal=Eur. J. Endocrinol. |volume=137 |issue= 2 |pages= 183-92 |year= 1997 |pmid= 9272108 |doi= }}
*{{cite journal | author=de Roux N, Young J, Misrahi M, ''et al.'' |title=A family with hypogonadotropic hypogonadism and mutations in the gonadotropin-releasing hormone receptor. |journal=N. Engl. J. Med. |volume=337 |issue= 22 |pages= 1597-602 |year= 1997 |pmid= 9371856 |doi= }}
*{{cite journal | author=Layman LC, Cohen DP, Jin M, ''et al.'' |title=Mutations in gonadotropin-releasing hormone receptor gene cause hypogonadotropic hypogonadism. |journal=Nat. Genet. |volume=18 |issue= 1 |pages= 14-5 |year= 1998 |pmid= 9425890 |doi= 10.1038/ng0198-14 }}
*{{cite journal | author=de Roux N, Young J, Brailly-Tabard S, ''et al.'' |title=The same molecular defects of the gonadotropin-releasing hormone receptor determine a variable degree of hypogonadism in affected kindred. |journal=J. Clin. Endocrinol. Metab. |volume=84 |issue= 2 |pages= 567-72 |year= 1999 |pmid= 10022417 |doi= }}
*{{cite journal | author=Caron P, Chauvin S, Christin-Maitre S, ''et al.'' |title=Resistance of hypogonadic patients with mutated GnRH receptor genes to pulsatile GnRH administration. |journal=J. Clin. Endocrinol. Metab. |volume=84 |issue= 3 |pages= 990-6 |year= 1999 |pmid= 10084584 |doi= }}
*{{cite journal | author=Kottler ML, Bergametti F, Carrë MC, ''et al.'' |title=Tissue-specific pattern of variant transcripts of the human gonadotropin-releasing hormone receptor gene. |journal=Eur. J. Endocrinol. |volume=140 |issue= 6 |pages= 561-9 |year= 1999 |pmid= 10366411 |doi= }}
*{{cite journal | author=Pralong FP, Gomez F, Castillo E, ''et al.'' |title=Complete hypogonadotropic hypogonadism associated with a novel inactivating mutation of the gonadotropin-releasing hormone receptor. |journal=J. Clin. Endocrinol. Metab. |volume=84 |issue= 10 |pages= 3811-6 |year= 1999 |pmid= 10523035 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LAT... {November 16, 2007 11:37:47 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:38:07 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Linker for activation of T cells
| HGNCid = 18874
| Symbol = LAT
| AltSymbols =; LAT1; pp36
| OMIM = 602354
| ECnumber =
| Homologene = 7811
| MGIid = 1342293
| Function = {{GNF_GO|id=GO:0005070 |text = SH3/SH2 adaptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0001772 |text = immunological synapse}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0045121 |text = lipid raft}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0007265 |text = Ras protein signal transduction}} {{GNF_GO|id=GO:0019722 |text = calcium-mediated signaling}} {{GNF_GO|id=GO:0043303 |text = mast cell degranulation}} {{GNF_GO|id=GO:0050863 |text = regulation of T cell activation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 27040
| Hs_Ensembl =
| Hs_RefseqProtein = NP_001014987
| Hs_RefseqmRNA = NM_001014987
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 16797
| Mm_Ensembl = ENSMUSG00000030742
| Mm_RefseqmRNA = NM_010689
| Mm_RefseqProtein = NP_034819
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 126154975
| Mm_GenLoc_end = 126160691
| Mm_Uniprot = Q546H1
}}
}}
'''Linker for activation of T cells''', also known as '''LAT''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LAT linker for activation of T cells| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27040| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is phosphorylated by ZAP-70/Syk protein tyrosine kinases following activation of the T-cell antigen receptor (TCR) signal transduction pathway. This transmembrane protein localizes to lipid rafts and acts as a docking site for SH2 domain-containing proteins. Upon phosphorylation, this protein recruits multiple adaptor proteins and downstream signaling molecules into multimolecular signaling complexes located near the site of TCR engagement. Alternative splicing results in multiple transcript variants encoding different isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: LAT linker for activation of T cells| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27040| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wange RL |title=LAT, the linker for activation of T cells: a bridge between T cell-specific and general signaling pathways. |journal=Sci. STKE |volume=2000 |issue= 63 |pages= RE1 |year= 2002 |pmid= 11752630 |doi= 10.1126/stke.2000.63.re1 }}
*{{cite journal | author=Sommers CL, Samelson LE, Love PE |title=LAT: a T lymphocyte adapter protein that couples the antigen receptor to downstream signaling pathways. |journal=Bioessays |volume=26 |issue= 1 |pages= 61-7 |year= 2004 |pmid= 14696041 |doi= 10.1002/bies.10384 }}
*{{cite journal | author=Rivera J |title=NTAL/LAB and LAT: a balancing act in mast-cell activation and function. |journal=Trends Immunol. |volume=26 |issue= 3 |pages= 119-22 |year= 2005 |pmid= 15745852 |doi= 10.1016/j.it.2005.01.001 }}
*{{cite journal | author=Trüb T, Frantz JD, Miyazaki M, ''et al.'' |title=The role of a lymphoid-restricted, Grb2-like SH3-SH2-SH3 protein in T cell receptor signaling. |journal=J. Biol. Chem. |volume=272 |issue= 2 |pages= 894-902 |year= 1997 |pmid= 8995379 |doi= }}
*{{cite journal | author=Hendricks-Taylor LR, Motto DG, Zhang J, ''et al.'' |title=SLP-76 is a substrate of the high affinity IgE receptor-stimulated protein tyrosine kinases in rat basophilic leukemia cells. |journal=J. Biol. Chem. |volume=272 |issue= 2 |pages= 1363-7 |year= 1997 |pmid= 8995445 |doi= }}
*{{cite journal | author=Zhang W, Sloan-Lancaster J, Kitchen J, ''et al.'' |title=LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. |journal=Cell |volume=92 |issue= 1 |pages= 83-92 |year= 1998 |pmid= 9489702 |doi= }}
*{{cite journal | author=Weber JR, Orstavik S, Torgersen KM, ''et al.'' |title=Molecular cloning of the cDNA encoding pp36, a tyrosine-phosphorylated adaptor protein selectively expressed by T cells and natural killer cells. |journal=J. Exp. Med. |volume=187 |issue= 7 |pages= 1157-61 |year= 1998 |pmid= 9529333 |doi= }}
*{{cite journal | author=Zhang W, Trible RP, Samelson LE |title=LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation. |journal=Immunity |volume=9 |issue= 2 |pages= 239-46 |year= 1998 |pmid= 9729044 |doi= }}
*{{cite journal | author=Finco TS, Kadlecek T, Zhang W, ''et al.'' |title=LAT is required for TCR-mediated activation of PLCgamma1 and the Ras pathway. |journal=Immunity |volume=9 |issue= 5 |pages= 617-26 |year= 1998 |pmid= 9846483 |doi= }}
*{{cite journal | author=Sarkar S |title=Tyrosine phosphorylation and translocation of LAT in platelets. |journal=FEBS Lett. |volume=441 |issue= 3 |pages= 357-60 |year= 1999 |pmid= 9891970 |doi= }}
*{{cite journal | author=Liu SK, Fang N, Koretzky GA, McGlade CJ |title=The hematopoietic-specific adaptor protein gads functions in T-cell signaling via interactions with the SLP-76 and LAT adaptors. |journal=Curr. Biol. |volume=9 |issue= 2 |pages= 67-75 |year= 1999 |pmid= 10021361 |doi= }}
*{{cite journal | author=Jevremovic D, Billadeau DD, Schoon RA, ''et al.'' |title=Cutting edge: a role for the adaptor protein LAT in human NK cell-mediated cytotoxicity. |journal=J. Immunol. |volume=162 |issue= 5 |pages= 2453-6 |year= 1999 |pmid= 10072481 |doi= }}
*{{cite journal | author=Zhang W, Sommers CL, Burshtyn DN, ''et al.'' |title=Essential role of LAT in T cell development. |journal=Immunity |volume=10 |issue= 3 |pages= 323-32 |year= 1999 |pmid= 10204488 |doi= }}
*{{cite journal | author=Tang J, Sawasdikosol S, Chang JH, Burakoff SJ |title=SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 17 |pages= 9775-80 |year= 1999 |pmid= 10449770 |doi= }}
*{{cite journal | author=Gross BS, Melford SK, Watson SP |title=Evidence that phospholipase C-gamma2 interacts with SLP-76, Syk, Lyn, LAT and the Fc receptor gamma-chain after stimulation of the collagen receptor glycoprotein VI in human platelets. |journal=Eur. J. Biochem. |volume=263 |issue= 3 |pages= 612-23 |year= 1999 |pmid= 10469124 |doi= }}
*{{cite journal | author=Lindholm CK, Gylfe E, Zhang W, ''et al.'' |title=Requirement of the Src homology 2 domain protein Shb for T cell receptor-dependent activation of the interleukin-2 gene nuclear factor for activation of T cells element in Jurkat T cells. |journal=J. Biol. Chem. |volume=274 |issue= 39 |pages= 28050-7 |year= 1999 |pmid= 10488157 |doi= }}
*{{cite journal | author=Shan X, Wange RL |title=Itk/Emt/Tsk activation in response to CD3 cross-linking in Jurkat T cells requires ZAP-70 and Lat and is independent of membrane recruitment. |journal=J. Biol. Chem. |volume=274 |issue= 41 |pages= 29323-30 |year= 1999 |pmid= 10506192 |doi= }}
*{{cite journal | author=Bosselut R, Zhang W, Ashe JM, ''et al.'' |title=Association of the adaptor molecule LAT with CD4 and CD8 coreceptors identifies a new coreceptor function in T cell receptor signal transduction. |journal=J. Exp. Med. |volume=190 |issue= 10 |pages= 1517-26 |year= 1999 |pmid= 10562325 |doi= }}
*{{cite journal | author=Tridandapani S, Lyden TW, Smith JL, ''et al.'' |title=The adapter protein LAT enhances fcgamma receptor-mediated signal transduction in myeloid cells. |journal=J. Biol. Chem. |volume=275 |issue= 27 |pages= 20480-7 |year= 2000 |pmid= 10781611 |doi= 10.1074/jbc.M909462199 }}
*{{cite journal | author=Zhang W, Trible RP, Zhu M, ''et al.'' |title=Association of Grb2, Gads, and phospholipase C-gamma 1 with phosphorylated LAT tyrosine residues. Effect of LAT tyrosine mutations on T cell angigen receptor-mediated signaling. |journal=J. Biol. Chem. |volume=275 |issue= 30 |pages= 23355-61 |year= 2000 |pmid= 10811803 |doi= 10.1074/jbc.M000404200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MEF2A... {November 16, 2007 11:29:00 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:29:41 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_MEF2A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1c7u.
| PDB = {{PDB2|1c7u}}, {{PDB2|1egw}}
| Name = MADS box transcription enhancer factor 2, polypeptide A (myocyte enhancer factor 2A)
| HGNCid = 6993
| Symbol = MEF2A
| AltSymbols =; ADCAD1; RSRFC4; RSRFC9
| OMIM = 600660
| ECnumber =
| Homologene = 4080
| MGIid = 99532
| GeneAtlas_image1 = PBB_GE_MEF2A_214684_at_tn.png
| GeneAtlas_image2 = PBB_GE_MEF2A_208328_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_MEF2A_212535_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0007517 |text = muscle development}} {{GNF_GO|id=GO:0045941 |text = positive regulation of transcription}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4205
| Hs_Ensembl = ENSG00000068305
| Hs_RefseqProtein = NP_005578
| Hs_RefseqmRNA = NM_005587
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 97923712
| Hs_GenLoc_end = 98074131
| Hs_Uniprot = Q02078
| Mm_EntrezGene = 17258
| Mm_Ensembl = ENSMUSG00000030557
| Mm_RefseqmRNA = XM_975927
| Mm_RefseqProtein = XP_981021
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 67113818
| Mm_GenLoc_end = 67174528
| Mm_Uniprot = Q6P8Q3
}}
}}
'''MADS box transcription enhancer factor 2, polypeptide A (myocyte enhancer factor 2A)''', also known as '''MEF2A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MEF2A MADS box transcription enhancer factor 2, polypeptide A (myocyte enhancer factor 2A)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4205| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The process of differentiation from mesodermal precursor cells to myoblasts has led to the discovery of a variety of tissue-specific factors that regulate muscle gene expression. The myogenic basic helix-loop-helix proteins, including myoD (MIM 159970), myogenin (MIM 159980), MYF5 (MIM 159990), and MRF4 (MIM 159991) are 1 class of identified factors. A second family of DNA binding regulatory proteins is the myocyte-specific enhancer factor-2 (MEF2) family. Each of these proteins binds to the MEF2 target DNA sequence present in the regulatory regions of many, if not all, muscle-specific genes. The MEF2 genes are members of the MADS gene family (named for the yeast mating type-specific transcription factor MCM1, the plant homeotic genes 'agamous' and 'deficiens' and the human serum response factor SRF (MIM 600589)), a family that also includes several homeotic genes and other transcription factors, all of which share a conserved DNA-binding domain.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: MEF2A MADS box transcription enhancer factor 2, polypeptide A (myocyte enhancer factor 2A)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4205| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wang Q |title=Advances in the genetic basis of coronary artery disease. |journal=Current atherosclerosis reports |volume=7 |issue= 3 |pages= 235-41 |year= 2005 |pmid= 15811259 |doi= }}
*{{cite journal | author=Wang Q |title=Molecular genetics of coronary artery disease. |journal=Curr. Opin. Cardiol. |volume=20 |issue= 3 |pages= 182-8 |year= 2005 |pmid= 15861005 |doi= }}
*{{cite journal | author=Funk WD, Wright WE |title=Cyclic amplification and selection of targets for multicomponent complexes: myogenin interacts with factors recognizing binding sites for basic helix-loop-helix, nuclear factor 1, myocyte-specific enhancer-binding factor 2, and COMP1 factor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 20 |pages= 9484-8 |year= 1992 |pmid= 1329097 |doi= }}
*{{cite journal | author=Yu YT, Breitbart RE, Smoot LB, ''et al.'' |title=Human myocyte-specific enhancer factor 2 comprises a group of tissue-restricted MADS box transcription factors. |journal=Genes Dev. |volume=6 |issue= 9 |pages= 1783-98 |year= 1992 |pmid= 1516833 |doi= }}
*{{cite journal | author=Pollock R, Treisman R |title=Human SRF-related proteins: DNA-binding properties and potential regulatory targets. |journal=Genes Dev. |volume=5 |issue= 12A |pages= 2327-41 |year= 1992 |pmid= 1748287 |doi= }}
*{{cite journal | author=Molkentin JD, Black BL, Martin JF, Olson EN |title=Cooperative activation of muscle gene expression by MEF2 and myogenic bHLH proteins. |journal=Cell |volume=83 |issue= 7 |pages= 1125-36 |year= 1996 |pmid= 8548800 |doi= }}
*{{cite journal | author=Hobson GM, Krahe R, Garcia E, ''et al.'' |title=Regional chromosomal assignments for four members of the MADS domain transcription enhancer factor 2 (MEF2) gene family to human chromosomes 15q26, 19p12, 5q14, and 1q12-q23. |journal=Genomics |volume=29 |issue= 3 |pages= 704-11 |year= 1996 |pmid= 8575763 |doi= 10.1006/geno.1995.9007 }}
*{{cite journal | author=Mao Z, Nadal-Ginard B |title=Functional and physical interactions between mammalian achaete-scute homolog 1 and myocyte enhancer factor 2A. |journal=J. Biol. Chem. |volume=271 |issue= 24 |pages= 14371-5 |year= 1996 |pmid= 8662987 |doi= }}
*{{cite journal | author=Suzuki E, Lowry J, Sonoda G, ''et al.'' |title=Structures and chromosome locations of the human MEF2A gene and a pseudogene MEF2AP. |journal=Cytogenet. Cell Genet. |volume=73 |issue= 3 |pages= 244-9 |year= 1996 |pmid= 8697817 |doi= }}
*{{cite journal | author=Ornatsky OI, McDermott JC |title=MEF2 protein expression, DNA binding specificity and complex composition, and transcriptional activity in muscle and non-muscle cells. |journal=J. Biol. Chem. |volume=271 |issue= 40 |pages= 24927-33 |year= 1996 |pmid= 8798771 |doi= }}
*{{cite journal | author=Black BL, Molkentin JD, Olson EN |title=Multiple roles for the MyoD basic region in transmission of transcriptional activation signals and interaction with MEF2. |journal=Mol. Cell. Biol. |volume=18 |issue= 1 |pages= 69-77 |year= 1998 |pmid= 9418854 |doi= }}
*{{cite journal | author=Yang CC, Ornatsky OI, McDermott JC, ''et al.'' |title=Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1. |journal=Nucleic Acids Res. |volume=26 |issue= 20 |pages= 4771-7 |year= 1998 |pmid= 9753748 |doi= }}
*{{cite journal | author=Zhao M, New L, Kravchenko VV, ''et al.'' |title=Regulation of the MEF2 family of transcription factors by p38. |journal=Mol. Cell. Biol. |volume=19 |issue= 1 |pages= 21-30 |year= 1999 |pmid= 9858528 |doi= }}
*{{cite journal | author=Yang SH, Galanis A, Sharrocks AD |title=Targeting of p38 mitogen-activated protein kinases to MEF2 transcription factors. |journal=Mol. Cell. Biol. |volume=19 |issue= 6 |pages= 4028-38 |year= 1999 |pmid= 10330143 |doi= }}
*{{cite journal | author=Iida K, Hidaka K, Takeuchi M, ''et al.'' |title=Expression of MEF2 genes during human cardiac development. |journal=Tohoku J. Exp. Med. |volume=187 |issue= 1 |pages= 15-23 |year= 1999 |pmid= 10458488 |doi= }}
*{{cite journal | author=Miska EA, Karlsson C, Langley E, ''et al.'' |title=HDAC4 deacetylase associates with and represses the MEF2 transcription factor. |journal=EMBO J. |volume=18 |issue= 18 |pages= 5099-107 |year= 1999 |pmid= 10487761 |doi= 10.1093/emboj/18.18.5099 }}
*{{cite journal | author=Mao Z, Bonni A, Xia F, ''et al.'' |title=Neuronal activity-dependent cell survival mediated by transcription factor MEF2. |journal=Science |volume=286 |issue= 5440 |pages= 785-90 |year= 1999 |pmid= 10531066 |doi= }}
*{{cite journal | author=Lu J, McKinsey TA, Nicol RL, Olson EN |title=Signal-dependent activation of the MEF2 transcription factor by dissociation from histone deacetylases. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 8 |pages= 4070-5 |year= 2000 |pmid= 10737771 |doi= 10.1073/pnas.080064097 }}
*{{cite journal | author=Lemercier C, Verdel A, Galloo B, ''et al.'' |title=mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity. |journal=J. Biol. Chem. |volume=275 |issue= 20 |pages= 15594-9 |year= 2000 |pmid= 10748098 |doi= 10.1074/jbc.M908437199 }}
*{{cite journal | author=Youn HD, Grozinger CM, Liu JO |title=Calcium regulates transcriptional repression of myocyte enhancer factor 2 by histone deacetylase 4. |journal=J. Biol. Chem. |volume=275 |issue= 29 |pages= 22563-7 |year= 2000 |pmid= 10825153 |doi= 10.1074/jbc.C000304200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MUTYH... {November 16, 2007 11:30:24 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:31:13 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_MUTYH_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1x51.
| PDB = {{PDB2|1x51}}
| Name = MutY homolog (E. coli)
| HGNCid = 7527
| Symbol = MUTYH
| AltSymbols =; MGC4416; MYH
| OMIM = 604933
| ECnumber =
| Homologene = 8156
| MGIid = 1917853
| GeneAtlas_image1 = PBB_GE_MUTYH_207727_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0004519 |text = endonuclease activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016798 |text = hydrolase activity, acting on glycosyl bonds}} {{GNF_GO|id=GO:0019104 |text = DNA N-glycosylase activity}} {{GNF_GO|id=GO:0032405 |text = MutLalpha complex binding}} {{GNF_GO|id=GO:0032406 |text = MutLbeta complex binding}} {{GNF_GO|id=GO:0032407 |text = MutSalpha complex binding}} {{GNF_GO|id=GO:0032408 |text = MutSbeta complex binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0051539 |text = 4 iron, 4 sulfur cluster binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006284 |text = base-excision repair}} {{GNF_GO|id=GO:0006298 |text = mismatch repair}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4595
| Hs_Ensembl = ENSG00000132781
| Hs_RefseqProtein = NP_001041636
| Hs_RefseqmRNA = NM_001048171
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 45567501
| Hs_GenLoc_end = 45578729
| Hs_Uniprot = Q9UIF7
| Mm_EntrezGene = 70603
| Mm_Ensembl = ENSMUSG00000028687
| Mm_RefseqmRNA = NM_133250
| Mm_RefseqProtein = NP_573513
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 116305655
| Mm_GenLoc_end = 116317370
| Mm_Uniprot = Q762C9
}}
}}
'''MutY homolog (E. coli)''', also known as '''MUTYH''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MUTYH mutY homolog (E. coli)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4595| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a DNA glycosylase involved in oxidative DNA damage repair. The enzyme excises adenine bases from the DNA backbone at sites where adenine is inappropriately paired with guanine, cytosine, or 8-oxo-7,8-dihydroguanine, a major oxidatively damaged DNA lesion. The protein is localized to the nucleus and mitochondria. Mutations in this gene result in heritable predisposition to colon and stomach cancer. Multiple transcript variants encoding different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: MUTYH mutY homolog (E. coli)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4595| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lindahl T, Wood RD |title=Quality control by DNA repair. |journal=Science |volume=286 |issue= 5446 |pages= 1897-905 |year= 1999 |pmid= 10583946 |doi= }}
*{{cite journal | author=Nakabeppu Y |title=Regulation of intracellular localization of human MTH1, OGG1, and MYH proteins for repair of oxidative DNA damage. |journal=Prog. Nucleic Acid Res. Mol. Biol. |volume=68 |issue= |pages= 75-94 |year= 2001 |pmid= 11554314 |doi= }}
*{{cite journal | author=Lipton L, Tomlinson I |title=The multiple colorectal adenoma phenotype and MYH, a base excision repair gene. |journal=Clin. Gastroenterol. Hepatol. |volume=2 |issue= 8 |pages= 633-8 |year= 2004 |pmid= 15290654 |doi= }}
*{{cite journal | author=Sampson JR, Jones S, Dolwani S, Cheadle JP |title=MutYH (MYH) and colorectal cancer. |journal=Biochem. Soc. Trans. |volume=33 |issue= Pt 4 |pages= 679-83 |year= 2005 |pmid= 16042573 |doi= 10.1042/BST0330679 }}
*{{cite journal | author=Castellví-Bel S, Balaguer F, Castells A |title=[MYH and colorectal cancer. A significant advance?] |journal=Gastroenterología y hepatología |volume=29 |issue= 7 |pages= 409-13 |year= 2006 |pmid= 16938257 |doi= }}
*{{cite journal | author=McGoldrick JP, Yeh YC, Solomon M, ''et al.'' |title=Characterization of a mammalian homolog of the Escherichia coli MutY mismatch repair protein. |journal=Mol. Cell. Biol. |volume=15 |issue= 2 |pages= 989-96 |year= 1995 |pmid= 7823963 |doi= }}
*{{cite journal | author=Slupska MM, Baikalov C, Luther WM, ''et al.'' |title=Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY gene whose function is required for the repair of oxidative DNA damage. |journal=J. Bacteriol. |volume=178 |issue= 13 |pages= 3885-92 |year= 1996 |pmid= 8682794 |doi= }}
*{{cite journal | author=Takao M, Aburatani H, Kobayashi K, Yasui A |title=Mitochondrial targeting of human DNA glycosylases for repair of oxidative DNA damage. |journal=Nucleic Acids Res. |volume=26 |issue= 12 |pages= 2917-22 |year= 1998 |pmid= 9611236 |doi= }}
*{{cite journal | author=Takao M, Zhang QM, Yonei S, Yasui A |title=Differential subcellular localization of human MutY homolog (hMYH) and the functional activity of adenine:8-oxoguanine DNA glycosylase. |journal=Nucleic Acids Res. |volume=27 |issue= 18 |pages= 3638-44 |year= 1999 |pmid= 10471731 |doi= }}
*{{cite journal | author=Ohtsubo T, Nishioka K, Imaiso Y, ''et al.'' |title=Identification of human MutY homolog (hMYH) as a repair enzyme for 2-hydroxyadenine in DNA and detection of multiple forms of hMYH located in nuclei and mitochondria. |journal=Nucleic Acids Res. |volume=28 |issue= 6 |pages= 1355-64 |year= 2000 |pmid= 10684930 |doi= }}
*{{cite journal | author=Parker A, Gu Y, Mahoney W, ''et al.'' |title=Human homolog of the MutY repair protein (hMYH) physically interacts with proteins involved in long patch DNA base excision repair. |journal=J. Biol. Chem. |volume=276 |issue= 8 |pages= 5547-55 |year= 2001 |pmid= 11092888 |doi= 10.1074/jbc.M008463200 }}
*{{cite journal | author=Gu Y, Parker A, Wilson TM, ''et al.'' |title=Human MutY homolog, a DNA glycosylase involved in base excision repair, physically and functionally interacts with mismatch repair proteins human MutS homolog 2/human MutS homolog 6. |journal=J. Biol. Chem. |volume=277 |issue= 13 |pages= 11135-42 |year= 2002 |pmid= 11801590 |doi= 10.1074/jbc.M108618200 }}
*{{cite journal | author=Chang DY, Lu AL |title=Functional interaction of MutY homolog with proliferating cell nuclear antigen in fission yeast, Schizosaccharomyces pombe. |journal=J. Biol. Chem. |volume=277 |issue= 14 |pages= 11853-8 |year= 2002 |pmid= 11805113 |doi= 10.1074/jbc.M111739200 }}
*{{cite journal | author=Al-Tassan N, Chmiel NH, Maynard J, ''et al.'' |title=Inherited variants of MYH associated with somatic G:C-->T:A mutations in colorectal tumors. |journal=Nat. Genet. |volume=30 |issue= 2 |pages= 227-32 |year= 2002 |pmid= 11818965 |doi= 10.1038/ng828 }}
*{{cite journal | author=Yamaguchi S, Shinmura K, Saitoh T, ''et al.'' |title=A single nucleotide polymorphism at the splice donor site of the human MYH base excision repair genes results in reduced translation efficiency of its transcripts. |journal=Genes Cells |volume=7 |issue= 5 |pages= 461-74 |year= 2002 |pmid= 12056405 |doi= }}
*{{cite journal | author=Jones S, Emmerson P, Maynard J, ''et al.'' |title=Biallelic germline mutations in MYH predispose to multiple colorectal adenoma and somatic G:C-->T:A mutations. |journal=Hum. Mol. Genet. |volume=11 |issue= 23 |pages= 2961-7 |year= 2003 |pmid= 12393807 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Sieber OM, Lipton L, Crabtree M, ''et al.'' |title=Multiple colorectal adenomas, classic adenomatous polyposis, and germ-line mutations in MYH. |journal=N. Engl. J. Med. |volume=348 |issue= 9 |pages= 791-9 |year= 2003 |pmid= 12606733 |doi= 10.1056/NEJMoa025283 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NCF1C... {November 16, 2007 11:38:07 AM PST}
- SEARCH REDIRECT: Control Box Found: NCF1C {November 16, 2007 1:09:23 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 1:09:25 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 1:09:25 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 1:09:25 PM PST}
- UPDATED: Updated protein page: NCF1C {November 16, 2007 1:09:29 PM PST}
- INFO: Beginning work on ND2... {November 16, 2007 11:29:41 AM PST}
- SEARCH REDIRECT: Control Box Found: ND2 {November 16, 2007 11:30:15 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 11:30:18 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 11:30:18 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 11:30:18 AM PST}
- UPDATED: Updated protein page: ND2 {November 16, 2007 11:30:23 AM PST}
- INFO: Beginning work on PLD2... {November 16, 2007 11:31:13 AM PST}
- SEARCH REDIRECT: Control Box Found: PLD2 {November 16, 2007 11:31:40 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 11:31:42 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 11:31:42 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 11:31:42 AM PST}
- UPDATED: Updated protein page: PLD2 {November 16, 2007 11:31:48 AM PST}
- INFO: Beginning work on PRKG1... {November 16, 2007 11:31:48 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:32:30 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Protein kinase, cGMP-dependent, type I
| HGNCid = 9414
| Symbol = PRKG1
| AltSymbols =; CGKI; FLJ36117; MGC71944; PGK; PRKG1B; PRKGR1B; cGKI-BETA; cGKI-alpha
| OMIM = 176894
| ECnumber =
| Homologene = 55964
| MGIid = 108174
| GeneAtlas_image1 = PBB_GE_PRKG1_211380_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PRKG1_207119_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004692 |text = cGMP-dependent protein kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008603 |text = cAMP-dependent protein kinase regulator activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0030553 |text = cGMP binding}}
| Component = {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0005952 |text = cAMP-dependent protein kinase complex}}
| Process = {{GNF_GO|id=GO:0001764 |text = neuron migration}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006940 |text = regulation of smooth muscle contraction}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0016358 |text = dendrite development}} {{GNF_GO|id=GO:0030036 |text = actin cytoskeleton organization and biogenesis}} {{GNF_GO|id=GO:0030900 |text = forebrain development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5592
| Hs_Ensembl = ENSG00000185532
| Hs_RefseqProtein = NP_006249
| Hs_RefseqmRNA = NM_006258
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 52421124
| Hs_GenLoc_end = 53728116
| Hs_Uniprot = Q13976
| Mm_EntrezGene = 19091
| Mm_Ensembl = ENSMUSG00000052920
| Mm_RefseqmRNA = XM_993724
| Mm_RefseqProtein = XP_998818
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 30635235
| Mm_GenLoc_end = 31830819
| Mm_Uniprot = Q14DK6
}}
}}
'''Protein kinase, cGMP-dependent, type I''', also known as '''PRKG1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRKG1 protein kinase, cGMP-dependent, type I| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5592| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Picciotto MR, Cohn JA, Bertuzzi G, ''et al.'' |title=Phosphorylation of the cystic fibrosis transmembrane conductance regulator. |journal=J. Biol. Chem. |volume=267 |issue= 18 |pages= 12742-52 |year= 1992 |pmid= 1377674 |doi= }}
*{{cite journal | author=Orstavik S, Sandberg M, Bérubé D, ''et al.'' |title=Localization of the human gene for the type I cyclic GMP-dependent protein kinase to chromosome 10. |journal=Cytogenet. Cell Genet. |volume=59 |issue= 4 |pages= 270-3 |year= 1992 |pmid= 1544322 |doi= }}
*{{cite journal | author=Thomas MK, Francis SH, Corbin JD |title=Substrate- and kinase-directed regulation of phosphorylation of a cGMP-binding phosphodiesterase by cGMP. |journal=J. Biol. Chem. |volume=265 |issue= 25 |pages= 14971-8 |year= 1990 |pmid= 2168396 |doi= }}
*{{cite journal | author=Sandberg M, Natarajan V, Ronander I, ''et al.'' |title=Molecular cloning and predicted full-length amino acid sequence of the type I beta isozyme of cGMP-dependent protein kinase from human placenta. Tissue distribution and developmental changes in rat. |journal=FEBS Lett. |volume=255 |issue= 2 |pages= 321-9 |year= 1989 |pmid= 2792381 |doi= }}
*{{cite journal | author=Pöhler D, Butt E, Meissner J, ''et al.'' |title=Expression, purification, and characterization of the cGMP-dependent protein kinases I beta and II using the baculovirus system. |journal=FEBS Lett. |volume=374 |issue= 3 |pages= 419-25 |year= 1995 |pmid= 7589584 |doi= }}
*{{cite journal | author=Komalavilas P, Lincoln TM |title=Phosphorylation of the inositol 1,4,5-trisphosphate receptor by cyclic GMP-dependent protein kinase. |journal=J. Biol. Chem. |volume=269 |issue= 12 |pages= 8701-7 |year= 1994 |pmid= 8132598 |doi= }}
*{{cite journal | author=Butt E, Abel K, Krieger M, ''et al.'' |title=cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets. |journal=J. Biol. Chem. |volume=269 |issue= 20 |pages= 14509-17 |year= 1994 |pmid= 8182057 |doi= }}
*{{cite journal | author=Suko J, Maurer-Fogy I, Plank B, ''et al.'' |title=Phosphorylation of serine 2843 in ryanodine receptor-calcium release channel of skeletal muscle by cAMP-, cGMP- and CaM-dependent protein kinase. |journal=Biochim. Biophys. Acta |volume=1175 |issue= 2 |pages= 193-206 |year= 1993 |pmid= 8380342 |doi= }}
*{{cite journal | author=Tamura N, Itoh H, Ogawa Y, ''et al.'' |title=cDNA cloning and gene expression of human type Ialpha cGMP-dependent protein kinase. |journal=Hypertension |volume=27 |issue= 3 Pt 2 |pages= 552-7 |year= 1996 |pmid= 8613202 |doi= }}
*{{cite journal | author=Salih E, Zhou HY, Glimcher MJ |title=Phosphorylation of purified bovine bone sialoprotein and osteopontin by protein kinases. |journal=J. Biol. Chem. |volume=271 |issue= 28 |pages= 16897-905 |year= 1996 |pmid= 8663267 |doi= }}
*{{cite journal | author=Xing J, Ginty DD, Greenberg ME |title=Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase. |journal=Science |volume=273 |issue= 5277 |pages= 959-63 |year= 1996 |pmid= 8688081 |doi= }}
*{{cite journal | author=Orstavik S, Natarajan V, Taskén K, ''et al.'' |title=Characterization of the human gene encoding the type I alpha and type I beta cGMP-dependent protein kinase (PRKG1). |journal=Genomics |volume=42 |issue= 2 |pages= 311-8 |year= 1997 |pmid= 9192852 |doi= 10.1006/geno.1997.4743 }}
*{{cite journal | author=Deak M, Clifton AD, Lucocq LM, Alessi DR |title=Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB. |journal=EMBO J. |volume=17 |issue= 15 |pages= 4426-41 |year= 1998 |pmid= 9687510 |doi= 10.1093/emboj/17.15.4426 }}
*{{cite journal | author=Du K, Montminy M |title=CREB is a regulatory target for the protein kinase Akt/PKB. |journal=J. Biol. Chem. |volume=273 |issue= 49 |pages= 32377-9 |year= 1999 |pmid= 9829964 |doi= }}
*{{cite journal | author=Endo S, Suzuki M, Sumi M, ''et al.'' |title=Molecular identification of human G-substrate, a possible downstream component of the cGMP-dependent protein kinase cascade in cerebellar Purkinje cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 5 |pages= 2467-72 |year= 1999 |pmid= 10051666 |doi= }}
*{{cite journal | author=Wang X, Bruderer S, Rafi Z, ''et al.'' |title=Phosphorylation of splicing factor SF1 on Ser20 by cGMP-dependent protein kinase regulates spliceosome assembly. |journal=EMBO J. |volume=18 |issue= 16 |pages= 4549-59 |year= 1999 |pmid= 10449420 |doi= 10.1093/emboj/18.16.4549 }}
*{{cite journal | author=Surks HK, Mochizuki N, Kasai Y, ''et al.'' |title=Regulation of myosin phosphatase by a specific interaction with cGMP- dependent protein kinase Ialpha. |journal=Science |volume=286 |issue= 5444 |pages= 1583-7 |year= 1999 |pmid= 10567269 |doi= }}
*{{cite journal | author=Yuasa K, Michibata H, Omori K, Yanaka N |title=A novel interaction of cGMP-dependent protein kinase I with troponin T. |journal=J. Biol. Chem. |volume=274 |issue= 52 |pages= 37429-34 |year= 2000 |pmid= 10601315 |doi= }}
*{{cite journal | author=Yuasa K, Omori K, Yanaka N |title=Binding and phosphorylation of a novel male germ cell-specific cGMP-dependent protein kinase-anchoring protein by cGMP-dependent protein kinase Ialpha. |journal=J. Biol. Chem. |volume=275 |issue= 7 |pages= 4897-905 |year= 2000 |pmid= 10671526 |doi= }}
*{{cite journal | author=Huber A, Neuhuber WL, Klugbauer N, ''et al.'' |title=Cysteine-rich protein 2, a novel substrate for cGMP kinase I in enteric neurons and intestinal smooth muscle. |journal=J. Biol. Chem. |volume=275 |issue= 8 |pages= 5504-11 |year= 2000 |pmid= 10681529 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PTTG1... {November 16, 2007 11:37:11 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:37:47 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Pituitary tumor-transforming 1
| HGNCid = 9690
| Symbol = PTTG1
| AltSymbols =; EAP1; HPTTG; MGC126883; MGC138276; PTTG; SECURIN; TUTR1
| OMIM = 604147
| ECnumber =
| Homologene = 3110
| MGIid = 1353578
| GeneAtlas_image1 = PBB_GE_PTTG1_203554_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0004869 |text = cysteine protease inhibitor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006259 |text = DNA metabolic process}} {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007059 |text = chromosome segregation}} {{GNF_GO|id=GO:0007067 |text = mitosis}} {{GNF_GO|id=GO:0007283 |text = spermatogenesis}} {{GNF_GO|id=GO:0051276 |text = chromosome organization and biogenesis}} {{GNF_GO|id=GO:0051301 |text = cell division}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 9232
| Hs_Ensembl = ENSG00000164611
| Hs_RefseqProtein = NP_004210
| Hs_RefseqmRNA = NM_004219
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 159781418
| Hs_GenLoc_end = 159788323
| Hs_Uniprot = O95997
| Mm_EntrezGene = 30939
| Mm_Ensembl = ENSMUSG00000020415
| Mm_RefseqmRNA = NM_013917
| Mm_RefseqProtein = NP_038945
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 43263685
| Mm_GenLoc_end = 43269674
| Mm_Uniprot = Q3Y5K4
}}
}}
'''Pituitary tumor-transforming 1''', also known as '''PTTG1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTTG1 pituitary tumor-transforming 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9232| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The encoded protein is a homolog of yeast securin proteins, which prevent separins from promoting sister chromatid separation. It is an anaphase-promoting complex (APC) substrate that associates with a separin until activation of the APC. The gene product has transforming activity in vitro and tumorigenic activity in vivo, and the gene is highly expressed in various tumors. The gene product contains 2 PXXP motifs, which are required for its transforming and tumorigenic activities, as well as for its stimulation of basic fibroblast growth factor expression. It also contains a destruction box (D box) that is required for its degradation by the APC. The acidic C-terminal region of the encoded protein can act as a transactivation domain. The gene product is mainly a cytosolic protein, although it partially localizes in the nucleus.<ref name="entrez">{{cite web | title = Entrez Gene: PTTG1 pituitary tumor-transforming 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9232| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Yu R, Melmed S |title=Pituitary tumor transforming gene: an update. |journal=Frontiers of hormone research |volume=32 |issue= |pages= 175-85 |year= 2004 |pmid= 15281346 |doi= }}
*{{cite journal | author=Tfelt-Hansen J, Kanuparthi D, Chattopadhyay N |title=The emerging role of pituitary tumor transforming gene in tumorigenesis. |journal=Clinical medicine & research |volume=4 |issue= 2 |pages= 130-7 |year= 2006 |pmid= 16809406 |doi= }}
*{{cite journal | author=Domínguez A, Ramos-Morales F, Romero F, ''et al.'' |title=hpttg, a human homologue of rat pttg, is overexpressed in hematopoietic neoplasms. Evidence for a transcriptional activation function of hPTTG. |journal=Oncogene |volume=17 |issue= 17 |pages= 2187-93 |year= 1998 |pmid= 9811450 |doi= 10.1038/sj.onc.1202140 }}
*{{cite journal | author=Zhang X, Horwitz GA, Prezant TR, ''et al.'' |title=Structure, expression, and function of human pituitary tumor-transforming gene (PTTG). |journal=Mol. Endocrinol. |volume=13 |issue= 1 |pages= 156-66 |year= 1999 |pmid= 9892021 |doi= }}
*{{cite journal | author=Pei L |title=Pituitary tumor-transforming gene protein associates with ribosomal protein S10 and a novel human homologue of DnaJ in testicular cells. |journal=J. Biol. Chem. |volume=274 |issue= 5 |pages= 3151-8 |year= 1999 |pmid= 9915854 |doi= }}
*{{cite journal | author=Kakar SS |title=Assignment of the human tumor transforming gene TUTR1 to chromosome band 5q35.1 by fluorescence in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=83 |issue= 1-2 |pages= 93-5 |year= 1999 |pmid= 9925941 |doi= }}
*{{cite journal | author=Zhang X, Horwitz GA, Heaney AP, ''et al.'' |title=Pituitary tumor transforming gene (PTTG) expression in pituitary adenomas. |journal=J. Clin. Endocrinol. Metab. |volume=84 |issue= 2 |pages= 761-7 |year= 1999 |pmid= 10022450 |doi= }}
*{{cite journal | author=Lee IA, Seong C, Choe IS |title=Cloning and expression of human cDNA encoding human homologue of pituitary tumor transforming gene. |journal=Biochem. Mol. Biol. Int. |volume=47 |issue= 5 |pages= 891-7 |year= 1999 |pmid= 10365261 |doi= }}
*{{cite journal | author=Kakar SS, Jennes L |title=Molecular cloning and characterization of the tumor transforming gene (TUTR1): a novel gene in human tumorigenesis. |journal=Cytogenet. Cell Genet. |volume=84 |issue= 3-4 |pages= 211-6 |year= 1999 |pmid= 10393434 |doi= }}
*{{cite journal | author=Zou H, McGarry TJ, Bernal T, Kirschner MW |title=Identification of a vertebrate sister-chromatid separation inhibitor involved in transformation and tumorigenesis. |journal=Science |volume=285 |issue= 5426 |pages= 418-22 |year= 1999 |pmid= 10411507 |doi= }}
*{{cite journal | author=Kakar SS |title=Molecular cloning, genomic organization, and identification of the promoter for the human pituitary tumor transforming gene (PTTG). |journal=Gene |volume=240 |issue= 2 |pages= 317-24 |year= 2000 |pmid= 10580151 |doi= }}
*{{cite journal | author=Ramos-Morales F, Domínguez A, Romero F, ''et al.'' |title=Cell cycle regulated expression and phosphorylation of hpttg proto-oncogene product. |journal=Oncogene |volume=19 |issue= 3 |pages= 403-9 |year= 2000 |pmid= 10656688 |doi= 10.1038/sj.onc.1203320 }}
*{{cite journal | author=Chien W, Pei L |title=A novel binding factor facilitates nuclear translocation and transcriptional activation function of the pituitary tumor-transforming gene product. |journal=J. Biol. Chem. |volume=275 |issue= 25 |pages= 19422-7 |year= 2000 |pmid= 10781616 |doi= 10.1074/jbc.M910105199 }}
*{{cite journal | author=Ishikawa H, Heaney AP, Yu R, ''et al.'' |title=Human pituitary tumor-transforming gene induces angiogenesis. |journal=J. Clin. Endocrinol. Metab. |volume=86 |issue= 2 |pages= 867-74 |year= 2001 |pmid= 11158059 |doi= }}
*{{cite journal | author=Zur A, Brandeis M |title=Securin degradation is mediated by fzy and fzr, and is required for complete chromatid separation but not for cytokinesis. |journal=EMBO J. |volume=20 |issue= 4 |pages= 792-801 |year= 2001 |pmid= 11179223 |doi= 10.1093/emboj/20.4.792 }}
*{{cite journal | author=Romero F, Multon MC, Ramos-Morales F, ''et al.'' |title=Human securin, hPTTG, is associated with Ku heterodimer, the regulatory subunit of the DNA-dependent protein kinase. |journal=Nucleic Acids Res. |volume=29 |issue= 6 |pages= 1300-7 |year= 2001 |pmid= 11238996 |doi= }}
*{{cite journal | author=Jallepalli PV, Waizenegger IC, Bunz F, ''et al.'' |title=Securin is required for chromosomal stability in human cells. |journal=Cell |volume=105 |issue= 4 |pages= 445-57 |year= 2001 |pmid= 11371342 |doi= }}
*{{cite journal | author=Hilioti Z, Chung YS, Mochizuki Y, ''et al.'' |title=The anaphase inhibitor Pds1 binds to the APC/C-associated protein Cdc20 in a destruction box-dependent manner. |journal=Curr. Biol. |volume=11 |issue= 17 |pages= 1347-52 |year= 2001 |pmid= 11553328 |doi= }}
*{{cite journal | author=Waizenegger I, Giménez-Abián JF, Wernic D, Peters JM |title=Regulation of human separase by securin binding and autocleavage. |journal=Curr. Biol. |volume=12 |issue= 16 |pages= 1368-78 |year= 2003 |pmid= 12194817 |doi= }}
*{{cite journal | author=McCabe CJ, Boelaert K, Tannahill LA, ''et al.'' |title=Vascular endothelial growth factor, its receptor KDR/Flk-1, and pituitary tumor transforming gene in pituitary tumors. |journal=J. Clin. Endocrinol. Metab. |volume=87 |issue= 9 |pages= 4238-44 |year= 2002 |pmid= 12213878 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RGS4... {November 16, 2007 11:32:30 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:33:34 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_RGS4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1agr.
| PDB = {{PDB2|1agr}}, {{PDB2|1ezt}}, {{PDB2|1ezy}}
| Name = Regulator of G-protein signalling 4
| HGNCid = 10000
| Symbol = RGS4
| AltSymbols =; MGC2124; MGC60244; RGP4; SCZD9
| OMIM = 602516
| ECnumber =
| Homologene = 4100
| MGIid = 108409
| GeneAtlas_image1 = PBB_GE_RGS4_204337_at_tn.png
| GeneAtlas_image2 = PBB_GE_RGS4_204338_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_RGS4_204339_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005096 |text = GTPase activator activity}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}}
| Component =
| Process = {{GNF_GO|id=GO:0000188 |text = inactivation of MAPK activity}} {{GNF_GO|id=GO:0008277 |text = regulation of G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0009968 |text = negative regulation of signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5999
| Hs_Ensembl = ENSG00000117152
| Hs_RefseqProtein = NP_005604
| Hs_RefseqmRNA = NM_005613
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 161305673
| Hs_GenLoc_end = 161313006
| Hs_Uniprot = P49798
| Mm_EntrezGene = 19736
| Mm_Ensembl = ENSMUSG00000038530
| Mm_RefseqmRNA = NM_009062
| Mm_RefseqProtein = NP_033088
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 171578985
| Mm_GenLoc_end = 171584317
| Mm_Uniprot = Q5D078
}}
}}
'''Regulator of G-protein signalling 4''', also known as '''RGS4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RGS4 regulator of G-protein signalling 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5999| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Regulator of G protein signaling (RGS) family members are regulatory molecules that act as GTPase activating proteins (GAPs) for G alpha subunits of heterotrimeric G proteins. RGS proteins are able to deactivate G protein subunits of the Gi alpha, Go alpha and Gq alpha subtypes. They drive G proteins into their inactive GDP-bound forms. Regulator of G protein signaling 4 belongs to this family. All RGS proteins share a conserved 120-amino acid sequence termed the RGS domain. Regulator of G protein signaling 4 protein is 37% identical to RGS1 and 97% identical to rat Rgs4. This protein negatively regulate signaling upstream or at the level of the heterotrimeric G protein and is localized in the cytoplasm.<ref name="entrez">{{cite web | title = Entrez Gene: RGS4 regulator of G-protein signalling 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5999| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Levitt P, Ebert P, Mirnics K, ''et al.'' |title=Making the case for a candidate vulnerability gene in schizophrenia: Convergent evidence for regulator of G-protein signaling 4 (RGS4). |journal=Biol. Psychiatry |volume=60 |issue= 6 |pages= 534-7 |year= 2006 |pmid= 16860780 |doi= 10.1016/j.biopsych.2006.04.028 }}
*{{cite journal | author=Druey KM, Blumer KJ, Kang VH, Kehrl JH |title=Inhibition of G-protein-mediated MAP kinase activation by a new mammalian gene family. |journal=Nature |volume=379 |issue= 6567 |pages= 742-6 |year= 1996 |pmid= 8602223 |doi= 10.1038/379742a0 }}
*{{cite journal | author=Berman DM, Wilkie TM, Gilman AG |title=GAIP and RGS4 are GTPase-activating proteins for the Gi subfamily of G protein alpha subunits. |journal=Cell |volume=86 |issue= 3 |pages= 445-52 |year= 1996 |pmid= 8756726 |doi= }}
*{{cite journal | author=Heximer SP, Watson N, Linder ME, ''et al.'' |title=RGS2/G0S8 is a selective inhibitor of Gqalpha function. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 26 |pages= 14389-93 |year= 1998 |pmid= 9405622 |doi= }}
*{{cite journal | author=Srinivasa SP, Bernstein LS, Blumer KJ, Linder ME |title=Plasma membrane localization is required for RGS4 function in Saccharomyces cerevisiae. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 10 |pages= 5584-9 |year= 1998 |pmid= 9576926 |doi= }}
*{{cite journal | author=Druey KM, Sullivan BM, Brown D, ''et al.'' |title=Expression of GTPase-deficient Gialpha2 results in translocation of cytoplasmic RGS4 to the plasma membrane. |journal=J. Biol. Chem. |volume=273 |issue= 29 |pages= 18405-10 |year= 1998 |pmid= 9660808 |doi= }}
*{{cite journal | author=Faraone SV, Matise T, Svrakic D, ''et al.'' |title=Genome scan of European-American schizophrenia pedigrees: results of the NIMH Genetics Initiative and Millennium Consortium. |journal=Am. J. Med. Genet. |volume=81 |issue= 4 |pages= 290-5 |year= 1998 |pmid= 9674973 |doi= }}
*{{cite journal | author=Wang J, Ducret A, Tu Y, ''et al.'' |title=RGSZ1, a Gz-selective RGS protein in brain. Structure, membrane association, regulation by Galphaz phosphorylation, and relationship to a Gz gtpase-activating protein subfamily. |journal=J. Biol. Chem. |volume=273 |issue= 40 |pages= 26014-25 |year= 1998 |pmid= 9748280 |doi= }}
*{{cite journal | author=Shaw SH, Kelly M, Smith AB, ''et al.'' |title=A genome-wide search for schizophrenia susceptibility genes. |journal=Am. J. Med. Genet. |volume=81 |issue= 5 |pages= 364-76 |year= 1998 |pmid= 9754621 |doi= }}
*{{cite journal | author=Posner BA, Mukhopadhyay S, Tesmer JJ, ''et al.'' |title=Modulation of the affinity and selectivity of RGS protein interaction with G alpha subunits by a conserved asparagine/serine residue. |journal=Biochemistry |volume=38 |issue= 24 |pages= 7773-9 |year= 1999 |pmid= 10387017 |doi= 10.1021/bi9906367 }}
*{{cite journal | author=Tu Y, Popov S, Slaughter C, Ross EM |title=Palmitoylation of a conserved cysteine in the regulator of G protein signaling (RGS) domain modulates the GTPase-activating activity of RGS4 and RGS10. |journal=J. Biol. Chem. |volume=274 |issue= 53 |pages= 38260-7 |year= 2000 |pmid= 10608901 |doi= }}
*{{cite journal | author=Moy FJ, Chanda PK, Cockett MI, ''et al.'' |title=1H, 15N, 13C, and 13CO assignments and secondary structure determination of RGS4. |journal=J. Biomol. NMR |volume=15 |issue= 4 |pages= 339-40 |year= 2000 |pmid= 10685342 |doi= }}
*{{cite journal | author=Popov SG, Krishna UM, Falck JR, Wilkie TM |title=Ca2+/Calmodulin reverses phosphatidylinositol 3,4, 5-trisphosphate-dependent inhibition of regulators of G protein-signaling GTPase-activating protein activity. |journal=J. Biol. Chem. |volume=275 |issue= 25 |pages= 18962-8 |year= 2000 |pmid= 10747990 |doi= 10.1074/jbc.M001128200 }}
*{{cite journal | author=Ekelund J, Lichtermann D, Hovatta I, ''et al.'' |title=Genome-wide scan for schizophrenia in the Finnish population: evidence for a locus on chromosome 7q22. |journal=Hum. Mol. Genet. |volume=9 |issue= 7 |pages= 1049-57 |year= 2000 |pmid= 10767329 |doi= }}
*{{cite journal | author=Brzustowicz LM, Hodgkinson KA, Chow EW, ''et al.'' |title=Location of a major susceptibility locus for familial schizophrenia on chromosome 1q21-q22. |journal=Science |volume=288 |issue= 5466 |pages= 678-82 |year= 2000 |pmid= 10784452 |doi= }}
*{{cite journal | author=Chatterjee TK, Fisher RA |title=Cytoplasmic, nuclear, and golgi localization of RGS proteins. Evidence for N-terminal and RGS domain sequences as intracellular targeting motifs. |journal=J. Biol. Chem. |volume=275 |issue= 31 |pages= 24013-21 |year= 2000 |pmid= 10791963 |doi= 10.1074/jbc.M002082200 }}
*{{cite journal | author=Chatterjee TK, Fisher RA |title=Novel alternative splicing and nuclear localization of human RGS12 gene products. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29660-71 |year= 2000 |pmid= 10869340 |doi= 10.1074/jbc.M000330200 }}
*{{cite journal | author=Sullivan BM, Harrison-Lavoie KJ, Marshansky V, ''et al.'' |title=RGS4 and RGS2 bind coatomer and inhibit COPI association with Golgi membranes and intracellular transport. |journal=Mol. Biol. Cell |volume=11 |issue= 9 |pages= 3155-68 |year= 2000 |pmid= 10982407 |doi= }}
*{{cite journal | author=Dowal L, Elliott J, Popov S, ''et al.'' |title=Determination of the contact energies between a regulator of G protein signaling and G protein subunits and phospholipase C beta 1. |journal=Biochemistry |volume=40 |issue= 2 |pages= 414-21 |year= 2001 |pmid= 11148035 |doi= }}
*{{cite journal | author=Richardson RM, Marjoram RJ, Barr AJ, Snyderman R |title=RGS4 inhibits platelet-activating factor receptor phosphorylation and cellular responses. |journal=Biochemistry |volume=40 |issue= 12 |pages= 3583-8 |year= 2001 |pmid= 11297424 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SLC2A4... {November 16, 2007 11:33:34 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:33:57 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Solute carrier family 2 (facilitated glucose transporter), member 4
| HGNCid = 11009
| Symbol = SLC2A4
| AltSymbols =; GLUT4
| OMIM = 138190
| ECnumber =
| Homologene = 74381
| MGIid = 95758
| GeneAtlas_image1 = PBB_GE_SLC2A4_206603_at_tn.png
| Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005351 |text = sugar:hydrogen ion symporter activity}} {{GNF_GO|id=GO:0005355 |text = glucose transmembrane transporter activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0009897 |text = external side of plasma membrane}} {{GNF_GO|id=GO:0012506 |text = vesicle membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0048471 |text = perinuclear region of cytoplasm}}
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0008643 |text = carbohydrate transport}} {{GNF_GO|id=GO:0015758 |text = glucose transport}} {{GNF_GO|id=GO:0042593 |text = glucose homeostasis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6517
| Hs_Ensembl = ENSG00000181856
| Hs_RefseqProtein = NP_001033
| Hs_RefseqmRNA = NM_001042
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 7125777
| Hs_GenLoc_end = 7132300
| Hs_Uniprot = P14672
| Mm_EntrezGene = 20528
| Mm_Ensembl = ENSMUSG00000018566
| Mm_RefseqmRNA = NM_009204
| Mm_RefseqProtein = NP_033230
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 69758738
| Mm_GenLoc_end = 69764344
| Mm_Uniprot = Q5NCW7
}}
}}
'''Solute carrier family 2 (facilitated glucose transporter), member 4''', also known as '''SLC2A4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SLC2A4 solute carrier family 2 (facilitated glucose transporter), member 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6517| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is a member of the solute carrier family 2 (facilitated glucose transporter) family and encodes a protein that functions as an insulin-regulated facilitative glucose transporter. In the absence of insulin, this integral membrane protein is sequestered within the cells of muscle and adipose tissue. Within minutes of insulin stimulation, the protein moves to the cell surface and begins to transport glucose across the cell membrane. Mutations in this gene have been associated with noninsulin-dependent diabetes mellitus (NIDDM).<ref name="entrez">{{cite web | title = Entrez Gene: SLC2A4 solute carrier family 2 (facilitated glucose transporter), member 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6517| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Foster LJ, Klip A |title=Mechanism and regulation of GLUT-4 vesicle fusion in muscle and fat cells. |journal=Am. J. Physiol., Cell Physiol. |volume=279 |issue= 4 |pages= C877-90 |year= 2000 |pmid= 11003568 |doi= }}
*{{cite journal | author=Bryant NJ, Govers R, James DE |title=Regulated transport of the glucose transporter GLUT4. |journal=Nat. Rev. Mol. Cell Biol. |volume=3 |issue= 4 |pages= 267-77 |year= 2002 |pmid= 11994746 |doi= 10.1038/nrm782 }}
*{{cite journal | author=Baumann MU, Deborde S, Illsley NP |title=Placental glucose transfer and fetal growth. |journal=Endocrine |volume=19 |issue= 1 |pages= 13-22 |year= 2003 |pmid= 12583599 |doi= }}
*{{cite journal | author=Olson AL, Knight JB |title=Regulation of GLUT4 expression in vivo and in vitro. |journal=Front. Biosci. |volume=8 |issue= |pages= s401-9 |year= 2004 |pmid= 12700047 |doi= }}
*{{cite journal | author=McCarthy AM, Elmendorf JS |title=GLUT4's itinerary in health & disease. |journal=Indian J. Med. Res. |volume=125 |issue= 3 |pages= 373-88 |year= 2007 |pmid= 17496362 |doi= }}
*{{cite journal | author=Buse JB, Yasuda K, Lay TP, ''et al.'' |title=Human GLUT4/muscle-fat glucose-transporter gene. Characterization and genetic variation. |journal=Diabetes |volume=41 |issue= 11 |pages= 1436-45 |year= 1992 |pmid= 1397719 |doi= }}
*{{cite journal | author=O'Rahilly S, Krook A, Morgan R, ''et al.'' |title=Insulin receptor and insulin-responsive glucose transporter (GLUT 4) mutations and polymorphisms in a Welsh type 2 (non-insulin-dependent) diabetic population. |journal=Diabetologia |volume=35 |issue= 5 |pages= 486-9 |year= 1992 |pmid= 1521731 |doi= }}
*{{cite journal | author=Liu ML, Olson AL, Moye-Rowley WS, ''et al.'' |title=Expression and regulation of the human GLUT4/muscle-fat facilitative glucose transporter gene in transgenic mice. |journal=J. Biol. Chem. |volume=267 |issue= 17 |pages= 11673-6 |year= 1992 |pmid= 1601840 |doi= }}
*{{cite journal | author=Choi WH, O'Rahilly S, Buse JB, ''et al.'' |title=Molecular scanning of insulin-responsive glucose transporter (GLUT4) gene in NIDDM subjects. |journal=Diabetes |volume=40 |issue= 12 |pages= 1712-8 |year= 1992 |pmid= 1756912 |doi= }}
*{{cite journal | author=Kusari J, Verma US, Buse JB, ''et al.'' |title=Analysis of the gene sequences of the insulin receptor and the insulin-sensitive glucose transporter (GLUT-4) in patients with common-type non-insulin-dependent diabetes mellitus. |journal=J. Clin. Invest. |volume=88 |issue= 4 |pages= 1323-30 |year= 1991 |pmid= 1918382 |doi= }}
*{{cite journal | author=Bell GI, Murray JC, Nakamura Y, ''et al.'' |title=Polymorphic human insulin-responsive glucose-transporter gene on chromosome 17p13. |journal=Diabetes |volume=38 |issue= 8 |pages= 1072-5 |year= 1989 |pmid= 2568955 |doi= }}
*{{cite journal | author=Birnbaum MJ |title=Identification of a novel gene encoding an insulin-responsive glucose transporter protein. |journal=Cell |volume=57 |issue= 2 |pages= 305-15 |year= 1989 |pmid= 2649253 |doi= }}
*{{cite journal | author=Fukumoto H, Kayano T, Buse JB, ''et al.'' |title=Cloning and characterization of the major insulin-responsive glucose transporter expressed in human skeletal muscle and other insulin-responsive tissues. |journal=J. Biol. Chem. |volume=264 |issue= 14 |pages= 7776-9 |year= 1989 |pmid= 2656669 |doi= }}
*{{cite journal | author=Chiaramonte R, Martini R, Taramelli R, Comi P |title=Identification of the 5' end of the gene encoding a human insulin-responsive glucose transporter. |journal=Gene |volume=130 |issue= 2 |pages= 307-8 |year= 1993 |pmid= 7916714 |doi= }}
*{{cite journal | author=Verhey KJ, Birnbaum MJ |title=A Leu-Leu sequence is essential for COOH-terminal targeting signal of GLUT4 glucose transporter in fibroblasts. |journal=J. Biol. Chem. |volume=269 |issue= 4 |pages= 2353-6 |year= 1994 |pmid= 8300557 |doi= }}
*{{cite journal | author=Lee W, Samuel J, Zhang W, ''et al.'' |title=A myosin-derived peptide C109 binds to GLUT4-vesicles and inhibits the insulin-induced glucose transport stimulation and GLUT4 recruitment in rat adipocytes. |journal=Biochem. Biophys. Res. Commun. |volume=240 |issue= 2 |pages= 409-14 |year= 1997 |pmid= 9388492 |doi= 10.1006/bbrc.1997.7671 }}
*{{cite journal | author=Shi Y, Samuel SJ, Lee W, ''et al.'' |title=Cloning of an L-3-hydroxyacyl-CoA dehydrogenase that interacts with the GLUT4 C-terminus. |journal=Arch. Biochem. Biophys. |volume=363 |issue= 2 |pages= 323-32 |year= 1999 |pmid= 10068455 |doi= }}
*{{cite journal | author=Abel ED, Kaulbach HC, Tian R, ''et al.'' |title=Cardiac hypertrophy with preserved contractile function after selective deletion of GLUT4 from the heart. |journal=J. Clin. Invest. |volume=104 |issue= 12 |pages= 1703-14 |year= 2000 |pmid= 10606624 |doi= }}
*{{cite journal | author=Abel ED, Peroni O, Kim JK, ''et al.'' |title=Adipose-selective targeting of the GLUT4 gene impairs insulin action in muscle and liver. |journal=Nature |volume=409 |issue= 6821 |pages= 729-33 |year= 2001 |pmid= 11217863 |doi= 10.1038/35055575 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SOX9... {November 16, 2007 11:33:57 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:34:23 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = SRY (sex determining region Y)-box 9 (campomelic dysplasia, autosomal sex-reversal)
| HGNCid = 11204
| Symbol = SOX9
| AltSymbols =; CMPD1; CMD1; SRA1
| OMIM = 608160
| ECnumber =
| Homologene = 294
| MGIid = 98371
| GeneAtlas_image1 = PBB_GE_SOX9_202936_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SOX9_202935_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003704 |text = specific RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016563 |text = transcription activator activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0001502 |text = cartilage condensation}} {{GNF_GO|id=GO:0001708 |text = cell fate specification}} {{GNF_GO|id=GO:0001837 |text = epithelial to mesenchymal transition}} {{GNF_GO|id=GO:0001942 |text = hair follicle development}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0008584 |text = male gonad development}} {{GNF_GO|id=GO:0014032 |text = neural crest cell development}} {{GNF_GO|id=GO:0019100 |text = male germ-line sex determination}} {{GNF_GO|id=GO:0042127 |text = regulation of cell proliferation}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}} {{GNF_GO|id=GO:0045892 |text = negative regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6662
| Hs_Ensembl = ENSG00000125398
| Hs_RefseqProtein = NP_000337
| Hs_RefseqmRNA = NM_000346
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 67628756
| Hs_GenLoc_end = 67634147
| Hs_Uniprot = P48436
| Mm_EntrezGene = 20682
| Mm_Ensembl = ENSMUSG00000000567
| Mm_RefseqmRNA = NM_011448
| Mm_RefseqProtein = NP_035578
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 112598314
| Mm_GenLoc_end = 112603839
| Mm_Uniprot = Q571J2
}}
}}
'''SRY (sex determining region Y)-box 9 (campomelic dysplasia, autosomal sex-reversal)''', also known as '''SOX9''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SOX9 SRY (sex determining region Y)-box 9 (campomelic dysplasia, autosomal sex-reversal)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6662| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene recognizes the sequence CCTTGAG along with other members of the HMG-box class DNA-binding proteins. It acts during chondrocyte differentiation and, with steroidogenic factor 1, regulates transcription of the anti-Muellerian hormone (AMH) gene. Deficiencies lead to the skeletal malformation syndrome campomelic dysplasia, frequently with sex reversal.<ref name="entrez">{{cite web | title = Entrez Gene: SOX9 SRY (sex determining region Y)-box 9 (campomelic dysplasia, autosomal sex-reversal)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6662| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ninomiya S, Narahara K, Tsuji K, ''et al.'' |title=Acampomelic campomelic syndrome and sex reversal associated with de novo t(12;17) translocation. |journal=Am. J. Med. Genet. |volume=56 |issue= 1 |pages= 31-4 |year= 1995 |pmid= 7747782 |doi= 10.1002/ajmg.1320560109 }}
*{{cite journal | author=Lefebvre V, de Crombrugghe B |title=Toward understanding SOX9 function in chondrocyte differentiation. |journal=Matrix Biol. |volume=16 |issue= 9 |pages= 529-40 |year= 1998 |pmid= 9569122 |doi= }}
*{{cite journal | author=Harley VR |title=The molecular action of testis-determining factors SRY and SOX9. |journal=Novartis Found. Symp. |volume=244 |issue= |pages= 57-66; discussion 66-7, 79-85, 253-7 |year= 2002 |pmid= 11990798 |doi= }}
*{{cite journal | author=Kwok C, Weller PA, Guioli S, ''et al.'' |title=Mutations in SOX9, the gene responsible for Campomelic dysplasia and autosomal sex reversal. |journal=Am. J. Hum. Genet. |volume=57 |issue= 5 |pages= 1028-36 |year= 1995 |pmid= 7485151 |doi= }}
*{{cite journal | author=Foster JW, Dominguez-Steglich MA, Guioli S, ''et al.'' |title=Campomelic dysplasia and autosomal sex reversal caused by mutations in an SRY-related gene. |journal=Nature |volume=372 |issue= 6506 |pages= 525-30 |year= 1995 |pmid= 7990924 |doi= 10.1038/372525a0 }}
*{{cite journal | author=Wagner T, Wirth J, Meyer J, ''et al.'' |title=Autosomal sex reversal and campomelic dysplasia are caused by mutations in and around the SRY-related gene SOX9. |journal=Cell |volume=79 |issue= 6 |pages= 1111-20 |year= 1995 |pmid= 8001137 |doi= }}
*{{cite journal | author=Tommerup N, Schempp W, Meinecke P, ''et al.'' |title=Assignment of an autosomal sex reversal locus (SRA1) and campomelic dysplasia (CMPD1) to 17q24.3-q25.1. |journal=Nat. Genet. |volume=4 |issue= 2 |pages= 170-4 |year= 1993 |pmid= 8348155 |doi= 10.1038/ng0693-170 }}
*{{cite journal | author=Südbeck P, Schmitz ML, Baeuerle PA, Scherer G |title=Sex reversal by loss of the C-terminal transactivation domain of human SOX9. |journal=Nat. Genet. |volume=13 |issue= 2 |pages= 230-2 |year= 1996 |pmid= 8640233 |doi= 10.1038/ng0696-230 }}
*{{cite journal | author=Cameron FJ, Hageman RM, Cooke-Yarborough C, ''et al.'' |title=A novel germ line mutation in SOX9 causes familial campomelic dysplasia and sex reversal. |journal=Hum. Mol. Genet. |volume=5 |issue= 10 |pages= 1625-30 |year= 1997 |pmid= 8894698 |doi= }}
*{{cite journal | author=Meyer J, Südbeck P, Held M, ''et al.'' |title=Mutational analysis of the SOX9 gene in campomelic dysplasia and autosomal sex reversal: lack of genotype/phenotype correlations. |journal=Hum. Mol. Genet. |volume=6 |issue= 1 |pages= 91-8 |year= 1997 |pmid= 9002675 |doi= }}
*{{cite journal | author=Cameron FJ, Sinclair AH |title=Mutations in SRY and SOX9: testis-determining genes. |journal=Hum. Mutat. |volume=9 |issue= 5 |pages= 388-95 |year= 1997 |pmid= 9143916 |doi= 10.1002/(SICI)1098-1004(1997)9:5<388::AID-HUMU2>3.0.CO;2-0 }}
*{{cite journal | author=Wunderle VM, Critcher R, Hastie N, ''et al.'' |title=Deletion of long-range regulatory elements upstream of SOX9 causes campomelic dysplasia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 18 |pages= 10649-54 |year= 1998 |pmid= 9724758 |doi= }}
*{{cite journal | author=De Santa Barbara P, Bonneaud N, Boizet B, ''et al.'' |title=Direct interaction of SRY-related protein SOX9 and steroidogenic factor 1 regulates transcription of the human anti-Müllerian hormone gene. |journal=Mol. Cell. Biol. |volume=18 |issue= 11 |pages= 6653-65 |year= 1998 |pmid= 9774680 |doi= }}
*{{cite journal | author=McDowall S, Argentaro A, Ranganathan S, ''et al.'' |title=Functional and structural studies of wild type SOX9 and mutations causing campomelic dysplasia. |journal=J. Biol. Chem. |volume=274 |issue= 34 |pages= 24023-30 |year= 1999 |pmid= 10446171 |doi= }}
*{{cite journal | author=Huang W, Zhou X, Lefebvre V, de Crombrugghe B |title=Phosphorylation of SOX9 by cyclic AMP-dependent protein kinase A enhances SOX9's ability to transactivate a Col2a1 chondrocyte-specific enhancer. |journal=Mol. Cell. Biol. |volume=20 |issue= 11 |pages= 4149-58 |year= 2000 |pmid= 10805756 |doi= }}
*{{cite journal | author=Thong MK, Scherer G, Kozlowski K, ''et al.'' |title=Acampomelic campomelic dysplasia with SOX9 mutation. |journal=Am. J. Med. Genet. |volume=93 |issue= 5 |pages= 421-5 |year= 2000 |pmid= 10951468 |doi= }}
*{{cite journal | author=Ninomiya S, Yokoyama Y, Teraoka M, ''et al.'' |title=A novel mutation (296 del G) of the SOX90 gene in a patient with campomelic syndrome and sex reversal. |journal=Clin. Genet. |volume=58 |issue= 3 |pages= 224-7 |year= 2001 |pmid= 11076045 |doi= }}
*{{cite journal | author=Preiss S, Argentaro A, Clayton A, ''et al.'' |title=Compound effects of point mutations causing campomelic dysplasia/autosomal sex reversal upon SOX9 structure, nuclear transport, DNA binding, and transcriptional activation. |journal=J. Biol. Chem. |volume=276 |issue= 30 |pages= 27864-72 |year= 2001 |pmid= 11323423 |doi= 10.1074/jbc.M101278200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TITF1... {November 16, 2007 11:34:24 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:35:05 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_TITF1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ftt.
| PDB = {{PDB2|1ftt}}
| Name = Thyroid transcription factor 1
| HGNCid = 11825
| Symbol = TITF1
| AltSymbols =; BCH; BHC; NK-2; NKX2.1; NKX2A; TEBP; TTF-1; TTF1
| OMIM = 600635
| ECnumber =
| Homologene = 2488
| MGIid = 108067
| GeneAtlas_image1 = PBB_GE_TITF1_210673_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_TITF1_211024_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016563 |text = transcription activator activity}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005654 |text = nucleoplasm}} {{GNF_GO|id=GO:0005667 |text = transcription factor complex}}
| Process = {{GNF_GO|id=GO:0001764 |text = neuron migration}} {{GNF_GO|id=GO:0007389 |text = pattern specification process}} {{GNF_GO|id=GO:0007420 |text = brain development}} {{GNF_GO|id=GO:0007492 |text = endoderm development}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0030324 |text = lung development}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7080
| Hs_Ensembl = ENSG00000136352
| Hs_RefseqProtein = NP_001073136
| Hs_RefseqmRNA = NM_001079668
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 36055357
| Hs_GenLoc_end = 36059167
| Hs_Uniprot = P43699
| Mm_EntrezGene = 21869
| Mm_Ensembl = ENSMUSG00000001496
| Mm_RefseqmRNA = NM_009385
| Mm_RefseqProtein = NP_033411
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 57449968
| Mm_GenLoc_end = 57454920
| Mm_Uniprot = Q6PFE0
}}
}}
'''Thyroid transcription factor 1''', also known as '''TITF1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TITF1 thyroid transcription factor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7080| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lau SK, Luthringer DJ, Eisen RN |title=Thyroid transcription factor-1: a review. |journal=Appl. Immunohistochem. Mol. Morphol. |volume=10 |issue= 2 |pages= 97-102 |year= 2002 |pmid= 12051643 |doi= }}
*{{cite journal | author=Guazzi S, Price M, De Felice M, ''et al.'' |title=Thyroid nuclear factor 1 (TTF-1) contains a homeodomain and displays a novel DNA binding specificity. |journal=EMBO J. |volume=9 |issue= 11 |pages= 3631-9 |year= 1990 |pmid= 1976511 |doi= }}
*{{cite journal | author=Oguchi H, Pan YT, Kimura S |title=The complete nucleotide sequence of the mouse thyroid-specific enhancer-binding protein (T/EBP) gene: extensive identity of the deduced amino acid sequence with the human protein. |journal=Biochim. Biophys. Acta |volume=1261 |issue= 2 |pages= 304-6 |year= 1995 |pmid= 7711079 |doi= }}
*{{cite journal | author=Saiardi A, Tassi V, De Filippis V, Civitareale D |title=Cloning and sequence analysis of human thyroid transcription factor 1. |journal=Biochim. Biophys. Acta |volume=1261 |issue= 2 |pages= 307-10 |year= 1995 |pmid= 7711080 |doi= }}
*{{cite journal | author=Ikeda K, Clark JC, Shaw-White JR, ''et al.'' |title=Gene structure and expression of human thyroid transcription factor-1 in respiratory epithelial cells. |journal=J. Biol. Chem. |volume=270 |issue= 14 |pages= 8108-14 |year= 1995 |pmid= 7713914 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Ghaffari M, Zeng X, Whitsett JA, Yan C |title=Nuclear localization domain of thyroid transcription factor-1 in respiratory epithelial cells. |journal=Biochem. J. |volume=328 ( Pt 3) |issue= |pages= 757-61 |year= 1998 |pmid= 9396717 |doi= }}
*{{cite journal | author=Hamdan H, Liu H, Li C, ''et al.'' |title=Structure of the human Nkx2.1 gene. |journal=Biochim. Biophys. Acta |volume=1396 |issue= 3 |pages= 336-48 |year= 1998 |pmid= 9545595 |doi= }}
*{{cite journal | author=Perrone L, Tell G, Di Lauro R |title=Calreticulin enhances the transcriptional activity of thyroid transcription factor-1 by binding to its homeodomain. |journal=J. Biol. Chem. |volume=274 |issue= 8 |pages= 4640-5 |year= 1999 |pmid= 9988700 |doi= }}
*{{cite journal | author=Naltner A, Ghaffari M, Whitsett JA, Yan C |title=Retinoic acid stimulation of the human surfactant protein B promoter is thyroid transcription factor 1 site-dependent. |journal=J. Biol. Chem. |volume=275 |issue= 1 |pages= 56-62 |year= 2000 |pmid= 10617585 |doi= }}
*{{cite journal | author=Missero C, Pirro MT, Di Lauro R |title=Multiple ras downstream pathways mediate functional repression of the homeobox gene product TTF-1. |journal=Mol. Cell. Biol. |volume=20 |issue= 8 |pages= 2783-93 |year= 2000 |pmid= 10733581 |doi= }}
*{{cite journal | author=Naltner A, Wert S, Whitsett JA, Yan C |title=Temporal/spatial expression of nuclear receptor coactivators in the mouse lung. |journal=Am. J. Physiol. Lung Cell Mol. Physiol. |volume=279 |issue= 6 |pages= L1066-74 |year= 2000 |pmid= 11076796 |doi= }}
*{{cite journal | author=Yan C, Naltner A, Conkright J, Ghaffari M |title=Protein-protein interaction of retinoic acid receptor alpha and thyroid transcription factor-1 in respiratory epithelial cells. |journal=J. Biol. Chem. |volume=276 |issue= 24 |pages= 21686-91 |year= 2001 |pmid= 11274148 |doi= 10.1074/jbc.M011378200 }}
*{{cite journal | author=Missero C, Pirro MT, Simeone S, ''et al.'' |title=The DNA glycosylase T:G mismatch-specific thymine DNA glycosylase represses thyroid transcription factor-1-activated transcription. |journal=J. Biol. Chem. |volume=276 |issue= 36 |pages= 33569-75 |year= 2001 |pmid= 11438542 |doi= 10.1074/jbc.M104963200 }}
*{{cite journal | author=Yi M, Tong GX, Murry B, Mendelson CR |title=Role of CBP/p300 and SRC-1 in transcriptional regulation of the pulmonary surfactant protein-A (SP-A) gene by thyroid transcription factor-1 (TTF-1). |journal=J. Biol. Chem. |volume=277 |issue= 4 |pages= 2997-3005 |year= 2002 |pmid= 11713256 |doi= 10.1074/jbc.M109793200 }}
*{{cite journal | author=Liu C, Glasser SW, Wan H, Whitsett JA |title=GATA-6 and thyroid transcription factor-1 directly interact and regulate surfactant protein-C gene expression. |journal=J. Biol. Chem. |volume=277 |issue= 6 |pages= 4519-25 |year= 2002 |pmid= 11733512 |doi= 10.1074/jbc.M107585200 }}
*{{cite journal | author=Ng WK, Chow JC, Ng PK |title=Thyroid transcription factor-1 is highly sensitive and specific in differentiating metastatic pulmonary from extrapulmonary adenocarcinoma in effusion fluid cytology specimens. |journal=Cancer |volume=96 |issue= 1 |pages= 43-8 |year= 2002 |pmid= 11836702 |doi= }}
*{{cite journal | author=Pohlenz J, Dumitrescu A, Zundel D, ''et al.'' |title=Partial deficiency of thyroid transcription factor 1 produces predominantly neurological defects in humans and mice. |journal=J. Clin. Invest. |volume=109 |issue= 4 |pages= 469-73 |year= 2002 |pmid= 11854318 |doi= }}
*{{cite journal | author=Krude H, Schütz B, Biebermann H, ''et al.'' |title=Choreoathetosis, hypothyroidism, and pulmonary alterations due to human NKX2-1 haploinsufficiency. |journal=J. Clin. Invest. |volume=109 |issue= 4 |pages= 475-80 |year= 2002 |pmid= 11854319 |doi= }}
*{{cite journal | author=Miccadei S, De Leo R, Zammarchi E, ''et al.'' |title=The synergistic activity of thyroid transcription factor 1 and Pax 8 relies on the promoter/enhancer interplay. |journal=Mol. Endocrinol. |volume=16 |issue= 4 |pages= 837-46 |year= 2002 |pmid= 11923479 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on UCP3... {November 16, 2007 11:35:05 AM PST}
- SEARCH REDIRECT: Control Box Found: UCP3 {November 16, 2007 11:35:33 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 11:35:35 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 11:35:35 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 11:35:35 AM PST}
- UPDATED: Updated protein page: UCP3 {November 16, 2007 11:35:43 AM PST}
- INFO: Beginning work on USF1... {November 16, 2007 11:35:43 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:36:15 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_USF1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1an4.
| PDB = {{PDB2|1an4}}
| Name = Upstream transcription factor 1
| HGNCid = 12593
| Symbol = USF1
| AltSymbols =; FCHL; FCHL1; HYPLIP1; MLTF; MLTFI; UEF
| OMIM = 191523
| ECnumber =
| Homologene = 31426
| MGIid = 99542
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003704 |text = specific RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0030528 |text = transcription regulator activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0045449 |text = regulation of transcription}} {{GNF_GO|id=GO:0045893 |text = positive regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7391
| Hs_Ensembl = ENSG00000158773
| Hs_RefseqProtein = NP_009053
| Hs_RefseqmRNA = NM_007122
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 159275665
| Hs_GenLoc_end = 159282391
| Hs_Uniprot = P22415
| Mm_EntrezGene = 22278
| Mm_Ensembl = ENSMUSG00000026641
| Mm_RefseqmRNA = NM_009480
| Mm_RefseqProtein = NP_033506
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 173248059
| Mm_GenLoc_end = 173254796
| Mm_Uniprot = O09135
}}
}}
'''Upstream transcription factor 1''', also known as '''USF1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: USF1 upstream transcription factor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7391| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the basic helix-loop-helix leucine zipper family, and can function as a cellular transcription factor. The encoded protein can activate transcription through pyrimidine-rich initiator (Inr) elements and E-box motifs. This gene has been linked to familial combined hyperlipidemia (FCHL). Two transcript variants encoding distinct isoforms have been identified for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: USF1 upstream transcription factor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7391| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Corre S, Galibert MD |title=[USF as a key regulatory element of gene expression] |journal=Med Sci (Paris) |volume=22 |issue= 1 |pages= 62-7 |year= 2006 |pmid= 16386222 |doi= }}
*{{cite journal | author=Lee JC, Lusis AJ, Pajukanta P |title=Familial combined hyperlipidemia: upstream transcription factor 1 and beyond. |journal=Curr. Opin. Lipidol. |volume=17 |issue= 2 |pages= 101-9 |year= 2007 |pmid= 16531745 |doi= 10.1097/01.mol.0000217890.54875.13 }}
*{{cite journal | author=Roy AL, Meisterernst M, Pognonec P, Roeder RG |title=Cooperative interaction of an initiator-binding transcription initiation factor and the helix-loop-helix activator USF. |journal=Nature |volume=354 |issue= 6350 |pages= 245-8 |year= 1992 |pmid= 1961251 |doi= 10.1038/354245a0 }}
*{{cite journal | author=Gregor PD, Sawadogo M, Roeder RG |title=The adenovirus major late transcription factor USF is a member of the helix-loop-helix group of regulatory proteins and binds to DNA as a dimer. |journal=Genes Dev. |volume=4 |issue= 10 |pages= 1730-40 |year= 1991 |pmid= 2249772 |doi= }}
*{{cite journal | author=Henrion AA, Martinez A, Mattei MG, ''et al.'' |title=Structure, sequence, and chromosomal location of the gene for USF2 transcription factors in mouse. |journal=Genomics |volume=25 |issue= 1 |pages= 36-43 |year= 1995 |pmid= 7774954 |doi= }}
*{{cite journal | author=Ferré-D'Amaré AR, Pognonec P, Roeder RG, Burley SK |title=Structure and function of the b/HLH/Z domain of USF. |journal=EMBO J. |volume=13 |issue= 1 |pages= 180-9 |year= 1994 |pmid= 8306960 |doi= }}
*{{cite journal | author=Shieh BH, Sparkes RS, Gaynor RB, Lusis AJ |title=Localization of the gene-encoding upstream stimulatory factor (USF) to human chromosome 1q22-q23. |journal=Genomics |volume=16 |issue= 1 |pages= 266-8 |year= 1993 |pmid= 8486371 |doi= 10.1006/geno.1993.1174 }}
*{{cite journal | author=Viollet B, Lefrançois-Martinez AM, Henrion A, ''et al.'' |title=Immunochemical characterization and transacting properties of upstream stimulatory factor isoforms. |journal=J. Biol. Chem. |volume=271 |issue= 3 |pages= 1405-15 |year= 1996 |pmid= 8576131 |doi= }}
*{{cite journal | author=Ghosh AK, Datta PK, Jacob ST |title=The dual role of helix-loop--helix-zipper protein USF in ribosomal RNA gene transcription in vivo. |journal=Oncogene |volume=14 |issue= 5 |pages= 589-94 |year= 1997 |pmid= 9053857 |doi= 10.1038/sj.onc.1200866 }}
*{{cite journal | author=Pognonec P, Boulukos KE, Aperlo C, ''et al.'' |title=Cross-family interaction between the bHLHZip USF and bZip Fra1 proteins results in down-regulation of AP1 activity. |journal=Oncogene |volume=14 |issue= 17 |pages= 2091-8 |year= 1997 |pmid= 9160889 |doi= 10.1038/sj.onc.1201046 }}
*{{cite journal | author=Roy AL, Du H, Gregor PD, ''et al.'' |title=Cloning of an inr- and E-box-binding protein, TFII-I, that interacts physically and functionally with USF1. |journal=EMBO J. |volume=16 |issue= 23 |pages= 7091-104 |year= 1998 |pmid= 9384587 |doi= 10.1093/emboj/16.23.7091 }}
*{{cite journal | author=Pajukanta P, Nuotio I, Terwilliger JD, ''et al.'' |title=Linkage of familial combined hyperlipidaemia to chromosome 1q21-q23. |journal=Nat. Genet. |volume=18 |issue= 4 |pages= 369-73 |year= 1998 |pmid= 9537421 |doi= 10.1038/ng0498-369 }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
*{{cite journal | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
*{{cite journal | author=Bengtsson SH, Madeyski-Bengtson K, Nilsson J, Bjursell G |title=Transcriptional regulation of the human carboxyl ester lipase gene in THP-1 monocytes: an E-box required for activation binds upstream stimulatory factors 1 and 2. |journal=Biochem. J. |volume=365 |issue= Pt 2 |pages= 481-8 |year= 2002 |pmid= 11945176 |doi= 10.1042/BJ20020223 }}
*{{cite journal | author=Villavicencio EH, Yoon JW, Frank DJ, ''et al.'' |title=Cooperative E-box regulation of human GLI1 by TWIST and USF. |journal=Genesis |volume=32 |issue= 4 |pages= 247-58 |year= 2002 |pmid= 11948912 |doi= }}
*{{cite journal | author=Coulson JM, Edgson JL, Marshall-Jones ZV, ''et al.'' |title=Upstream stimulatory factor activates the vasopressin promoter via multiple motifs, including a non-canonical E-box. |journal=Biochem. J. |volume=369 |issue= Pt 3 |pages= 549-61 |year= 2003 |pmid= 12403649 |doi= 10.1042/BJ20021176 }}
*{{cite journal | author=Salero E, Giménez C, Zafra F |title=Identification of a non-canonical E-box motif as a regulatory element in the proximal promoter region of the apolipoprotein E gene. |journal=Biochem. J. |volume=370 |issue= Pt 3 |pages= 979-86 |year= 2003 |pmid= 12444925 |doi= 10.1042/BJ20021142 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Pickwell GV, Shih H, Quattrochi LC |title=Interaction of upstream stimulatory factor proteins with an E-box located within the human CYP1A2 5'-flanking gene contributes to basal transcriptional gene activation. |journal=Biochem. Pharmacol. |volume=65 |issue= 7 |pages= 1087-96 |year= 2003 |pmid= 12663044 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on XPC... {November 16, 2007 11:36:15 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:36:42 AM PST}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Xeroderma pigmentosum, complementation group C
| HGNCid = 12816
| Symbol = XPC
| AltSymbols =; XP3; XPCC
| OMIM = 278720
| ECnumber =
| Homologene = 3401
| MGIid = 103557
| GeneAtlas_image1 = PBB_GE_XPC_209375_at_tn.png
| Function = {{GNF_GO|id=GO:0003684 |text = damaged DNA binding}} {{GNF_GO|id=GO:0003697 |text = single-stranded DNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006289 |text = nucleotide-excision repair}} {{GNF_GO|id=GO:0031573 |text = intra-S DNA damage checkpoint}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7508
| Hs_Ensembl = ENSG00000154767
| Hs_RefseqProtein = NP_004619
| Hs_RefseqmRNA = NM_004628
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 14161651
| Hs_GenLoc_end = 14195143
| Hs_Uniprot = Q01831
| Mm_EntrezGene = 22591
| Mm_Ensembl = ENSMUSG00000030094
| Mm_RefseqmRNA = NM_009531
| Mm_RefseqProtein = NP_033557
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 91454814
| Mm_GenLoc_end = 91481329
| Mm_Uniprot = Q7TSZ1
}}
}}
'''Xeroderma pigmentosum, complementation group C''', also known as '''XPC''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: XPC xeroderma pigmentosum, complementation group C| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7508| accessdate = }}</ref>
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{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Cleaver JE, Thompson LH, Richardson AS, States JC |title=A summary of mutations in the UV-sensitive disorders: xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy. |journal=Hum. Mutat. |volume=14 |issue= 1 |pages= 9-22 |year= 1999 |pmid= 10447254 |doi= 10.1002/(SICI)1098-1004(1999)14:1<9::AID-HUMU2>3.0.CO;2-6 }}
*{{cite journal | author=El-Deiry WS |title=Transactivation of repair genes by BRCA1. |journal=Cancer Biol. Ther. |volume=1 |issue= 5 |pages= 490-1 |year= 2003 |pmid= 12496474 |doi= }}
*{{cite journal | author=Sugasawa K |title=UV-induced ubiquitylation of XPC complex, the UV-DDB-ubiquitin ligase complex, and DNA repair. |journal=J. Mol. Histol. |volume=37 |issue= 5-7 |pages= 189-202 |year= 2007 |pmid= 16858626 |doi= 10.1007/s10735-006-9044-7 }}
*{{cite journal | author=Legerski R, Peterson C |title=Expression cloning of a human DNA repair gene involved in xeroderma pigmentosum group C. |journal=Nature |volume=360 |issue= 6404 |pages= 610 |year= 1993 |pmid= 1461286 |doi= 10.1038/360610b0 }}
*{{cite journal | author=Legerski R, Peterson C |title=Expression cloning of a human DNA repair gene involved in xeroderma pigmentosum group C. |journal=Nature |volume=359 |issue= 6390 |pages= 70-3 |year= 1992 |pmid= 1522891 |doi= 10.1038/359070a0 }}
*{{cite journal | author=Legerski RJ, Liu P, Li L, ''et al.'' |title=Assignment of xeroderma pigmentosum group C (XPC) gene to chromosome 3p25. |journal=Genomics |volume=21 |issue= 1 |pages= 266-9 |year= 1994 |pmid= 8088800 |doi= 10.1006/geno.1994.1256 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Masutani C, Sugasawa K, Yanagisawa J, ''et al.'' |title=Purification and cloning of a nucleotide excision repair complex involving the xeroderma pigmentosum group C protein and a human homologue of yeast RAD23. |journal=EMBO J. |volume=13 |issue= 8 |pages= 1831-43 |year= 1994 |pmid= 8168482 |doi= }}
*{{cite journal | author=Li L, Bales ES, Peterson CA, Legerski RJ |title=Characterization of molecular defects in xeroderma pigmentosum group C. |journal=Nat. Genet. |volume=5 |issue= 4 |pages= 413-7 |year= 1994 |pmid= 8298653 |doi= 10.1038/ng1293-413 }}
*{{cite journal | author=Li L, Peterson C, Legerski R |title=Sequence of the mouse XPC cDNA and genomic structure of the human XPC gene. |journal=Nucleic Acids Res. |volume=24 |issue= 6 |pages= 1026-8 |year= 1996 |pmid= 8604333 |doi= }}
*{{cite journal | author=van der Spek PJ, Eker A, Rademakers S, ''et al.'' |title=XPC and human homologs of RAD23: intracellular localization and relationship to other nucleotide excision repair complexes. |journal=Nucleic Acids Res. |volume=24 |issue= 13 |pages= 2551-9 |year= 1996 |pmid= 8692695 |doi= }}
*{{cite journal | author=Li L, Lu X, Peterson C, Legerski R |title=XPC interacts with both HHR23B and HHR23A in vivo. |journal=Mutat. Res. |volume=383 |issue= 3 |pages= 197-203 |year= 1997 |pmid= 9164480 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Zeng L, Quilliet X, Chevallier-Lagente O, ''et al.'' |title=Retrovirus-mediated gene transfer corrects DNA repair defect of xeroderma pigmentosum cells of complementation groups A, B and C. |journal=Gene Ther. |volume=4 |issue= 10 |pages= 1077-84 |year= 1998 |pmid= 9415314 |doi= 10.1038/sj.gt.3300495 }}
*{{cite journal | author=Khan SG, Levy HL, Legerski R, ''et al.'' |title=Xeroderma pigmentosum group C splice mutation associated with autism and hypoglycinemia. |journal=J. Invest. Dermatol. |volume=111 |issue= 5 |pages= 791-6 |year= 1998 |pmid= 9804340 |doi= 10.1046/j.1523-1747.1998.00391.x }}
*{{cite journal | author=Yokoi M, Masutani C, Maekawa T, ''et al.'' |title=The xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNA. |journal=J. Biol. Chem. |volume=275 |issue= 13 |pages= 9870-5 |year= 2000 |pmid= 10734143 |doi= }}
*{{cite journal | author=Batty D, Rapic'-Otrin V, Levine AS, Wood RD |title=Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites. |journal=J. Mol. Biol. |volume=300 |issue= 2 |pages= 275-90 |year= 2000 |pmid= 10873465 |doi= 10.1006/jmbi.2000.3857 }}
*{{cite journal | author=Araújo SJ, Nigg EA, Wood RD |title=Strong functional interactions of TFIIH with XPC and XPG in human DNA nucleotide excision repair, without a preassembled repairosome. |journal=Mol. Cell. Biol. |volume=21 |issue= 7 |pages= 2281-91 |year= 2001 |pmid= 11259578 |doi= 10.1128/MCB.21.7.2281-2291.2001 }}
*{{cite journal | author=Araki M, Masutani C, Takemura M, ''et al.'' |title=Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 18665-72 |year= 2001 |pmid= 11279143 |doi= 10.1074/jbc.M100855200 }}
}}
{{refend}}
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