Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 22:18, 14 November 2007 (UTC)[edit]
Proteins without matches (10)[edit]
Proteins with a High Potential Match (12)[edit]
Redirected Proteins (3)[edit]
Manual Inspection (Page not found) (22)[edit]
Updated (3)[edit]
Protein Status Grid - Date: 22:18, 14 November 2007 (UTC)[edit]
Vebose Log - Date: 22:18, 14 November 2007 (UTC)[edit]
- INFO: Beginning work on ALOX5... {November 14, 2007 1:45:24 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 1:45:58 PM 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 = Arachidonate 5-lipoxygenase
| HGNCid = 435
| Symbol = ALOX5
| AltSymbols =; 5-LO; 5LPG; LOG5; MGC163204
| OMIM = 152390
| ECnumber =
| Homologene = 561
| MGIid = 87999
| GeneAtlas_image1 = PBB_GE_ALOX5_204446_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ALOX5_204445_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_ALOX5_214366_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004051 |text = arachidonate 5-lipoxygenase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016165 |text = lipoxygenase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006691 |text = leukotriene metabolic process}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0019370 |text = leukotriene biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 240
| Hs_Ensembl = ENSG00000012779
| Hs_RefseqProtein = XP_001127464
| Hs_RefseqmRNA = XM_001127464
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 45189635
| Hs_GenLoc_end = 45261567
| Hs_Uniprot = P09917
| Mm_EntrezGene = 11689
| Mm_Ensembl = ENSMUSG00000025701
| Mm_RefseqmRNA = NM_009662
| Mm_RefseqProtein = NP_033792
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 116375696
| Mm_GenLoc_end = 116426797
| Mm_Uniprot = Q3TB75
}}
}}
'''Arachidonate 5-lipoxygenase''', also known as '''ALOX5''', is a human [[gene]].
<!-- 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 lipoxygenase gene family and plays a dual role in the synthesis of leukotrienes from arachidonic acid. The encoded protein, which is expressed specifically in bone marrow-derived cells, catalyzes the conversion of arachidonic acid to 5(S)-hydroperoxy-6-trans-8,11,14-cis-eicosatetraenoic acid, and further to the allylic epoxide 5(S)-trans-7,9-trans-11,14-cis-eicosatetrenoic acid (leukotriene A4). Leukotrienes are important mediators of a number of inflammatory and allergic conditions. Mutations in the promoter region of this gene lead to a diminished response to antileukotriene drugs used in the treatment of asthma and may also be associated with atherosclerosis and several cancers. Alternatively spliced transcript variants have been observed, but their full-length nature has not been determined.<ref>{{cite web | title = Entrez Gene: ALOX5 arachidonate 5-lipoxygenase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=240| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Rådmark OP |title=The molecular biology and regulation of 5-lipoxygenase. |journal=Am. J. Respir. Crit. Care Med. |volume=161 |issue= 2 Pt 2 |pages= S11-5 |year= 2000 |pmid= 10673219 |doi= }}
*{{cite journal | author=Hammarberg T, Reddy KV, Persson B, Rådmark O |title=Calcium binding to 5-lipoxygenase. |journal=Adv. Exp. Med. Biol. |volume=507 |issue= |pages= 117-21 |year= 2003 |pmid= 12664574 |doi= }}
*{{cite journal | author=Ishii S, Noguchi M, Miyano M, ''et al.'' |title=Mutagenesis studies on the amino acid residues involved in the iron-binding and the activity of human 5-lipoxygenase. |journal=Biochem. Biophys. Res. Commun. |volume=182 |issue= 3 |pages= 1482-90 |year= 1992 |pmid= 1540191 |doi= }}
*{{cite journal | author=Nguyen T, Falgueyret JP, Abramovitz M, Riendeau D |title=Evaluation of the role of conserved His and Met residues among lipoxygenases by site-directed mutagenesis of recombinant human 5-lipoxygenase. |journal=J. Biol. Chem. |volume=266 |issue= 32 |pages= 22057-62 |year= 1991 |pmid= 1939225 |doi= }}
*{{cite journal | author=Hoshiko S, Rådmark O, Samuelsson B |title=Characterization of the human 5-lipoxygenase gene promoter. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 23 |pages= 9073-7 |year= 1991 |pmid= 2251250 |doi= }}
*{{cite journal | author=Funk CD, Hoshiko S, Matsumoto T, ''et al.'' |title=Characterization of the human 5-lipoxygenase gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 8 |pages= 2587-91 |year= 1989 |pmid= 2565035 |doi= }}
*{{cite journal | author=Matsumoto T, Funk CD, Rådmark O, ''et al.'' |title=Molecular cloning and amino acid sequence of human 5-lipoxygenase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 1 |pages= 26-30 |year= 1988 |pmid= 2829172 |doi= }}
*{{cite journal | author=Rouzer CA, Kargman S |title=Translocation of 5-lipoxygenase to the membrane in human leukocytes challenged with ionophore A23187. |journal=J. Biol. Chem. |volume=263 |issue= 22 |pages= 10980-8 |year= 1988 |pmid= 3134355 |doi= }}
*{{cite journal | author=Dixon RA, Jones RE, Diehl RE, ''et al.'' |title=Cloning of the cDNA for human 5-lipoxygenase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 2 |pages= 416-20 |year= 1988 |pmid= 3422434 |doi= }}
*{{cite journal | author=Jakobsson PJ, Shaskin P, Larsson P, ''et al.'' |title=Studies on the regulation and localization of 5-lipoxygenase in human B-lymphocytes. |journal=Eur. J. Biochem. |volume=232 |issue= 1 |pages= 37-46 |year= 1995 |pmid= 7556168 |doi= }}
*{{cite journal | author=Janssen-Timmen U, Vickers PJ, Wittig U, ''et al.'' |title=Expression of 5-lipoxygenase in differentiating human skin keratinocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 15 |pages= 6966-70 |year= 1995 |pmid= 7624354 |doi= }}
*{{cite journal | author=Lepley RA, Fitzpatrick FA |title=5-Lipoxygenase contains a functional Src homology 3-binding motif that interacts with the Src homology 3 domain of Grb2 and cytoskeletal proteins. |journal=J. Biol. Chem. |volume=269 |issue= 39 |pages= 24163-8 |year= 1994 |pmid= 7929073 |doi= }}
*{{cite journal | author=Shaw KJ, Ng C, Kovacs BW |title=Cyclooxygenase gene expression in human endometrium and decidua. |journal=Prostaglandins Leukot. Essent. Fatty Acids |volume=50 |issue= 5 |pages= 239-43 |year= 1994 |pmid= 8066098 |doi= }}
*{{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=Woods JW, Evans JF, Ethier D, ''et al.'' |title=5-lipoxygenase and 5-lipoxygenase-activating protein are localized in the nuclear envelope of activated human leukocytes. |journal=J. Exp. Med. |volume=178 |issue= 6 |pages= 1935-46 |year= 1993 |pmid= 8245774 |doi= }}
*{{cite journal | author=Mancini JA, Li C, Vickers PJ |title=5-Lipoxygenase activity in the human pancreas. |journal=Journal of lipid mediators |volume=8 |issue= 3 |pages= 145-50 |year= 1994 |pmid= 8268460 |doi= }}
*{{cite journal | author=VanderNoot VA, Fitzpatrick FA |title=Competitive binding assay of src homology domain 3 interactions between 5-lipoxygenase and growth factor receptor binding protein 2. |journal=Anal. Biochem. |volume=230 |issue= 1 |pages= 108-14 |year= 1996 |pmid= 8585605 |doi= 10.1006/abio.1995.1444 }}
*{{cite journal | author=Brock TG, McNish RW, Bailie MB, Peters-Golden M |title=Rapid import of cytosolic 5-lipoxygenase into the nucleus of neutrophils after in vivo recruitment and in vitro adherence. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8276-80 |year= 1997 |pmid= 9079648 |doi= }}
*{{cite journal | author=Nassar GM, Montero A, Fukunaga M, Badr KF |title=Contrasting effects of proinflammatory and T-helper lymphocyte subset-2 cytokines on the 5-lipoxygenase pathway in monocytes. |journal=Kidney Int. |volume=51 |issue= 5 |pages= 1520-8 |year= 1997 |pmid= 9150468 |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= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ARF1... {November 14, 2007 1:45:58 PM PST}
- SEARCH REDIRECT: Control Box Found: ARF1 {November 14, 2007 1:47:30 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 1:47:31 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 1:47:31 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 1:47:31 PM PST}
- UPDATED: Updated protein page: ARF1 {November 14, 2007 1:47:39 PM PST}
- INFO: Beginning work on CD59... {November 14, 2007 1:49:31 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 1:50:50 PM 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_CD59_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cdq.
| PDB = {{PDB2|1cdq}}, {{PDB2|1cdr}}, {{PDB2|1cds}}, {{PDB2|1erg}}, {{PDB2|1erh}}, {{PDB2|2ofs}}
| Name = CD59 molecule, complement regulatory protein
| HGNCid = 1689
| Symbol = CD59
| AltSymbols =; 16.3A5; EJ16; EJ30; EL32; G344; MGC2354; MIC11; MIN1; MIN2; MIN3; MSK21; PROTECTIN; p18-20
| OMIM = 107271
| ECnumber =
| Homologene = 56386
| MGIid = 1888996
| GeneAtlas_image1 = PBB_GE_CD59_200984_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CD59_200983_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_CD59_200985_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0048503 |text = GPI anchor binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}}
| Process = {{GNF_GO|id=GO:0006952 |text = defense response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 966
| Hs_Ensembl = ENSG00000085063
| Hs_RefseqProtein = NP_000602
| Hs_RefseqmRNA = NM_000611
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 33681134
| Hs_GenLoc_end = 33714600
| Hs_Uniprot = P13987
| Mm_EntrezGene = 333883
| Mm_Ensembl = ENSMUSG00000068686
| Mm_RefseqmRNA = NM_181858
| Mm_RefseqProtein = NP_862906
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 103871849
| Mm_GenLoc_end = 103885796
| Mm_Uniprot = Q6PBG1
}}
}}
'''CD59 molecule, complement regulatory protein''', also known as '''CD59''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tandon N, Morgan BP, Weetman AP |title=Expression and function of membrane attack complex inhibitory proteins on thyroid follicular cells. |journal=Immunology |volume=75 |issue= 2 |pages= 372-7 |year= 1992 |pmid= 1372592 |doi= }}
*{{cite journal | author=Holmes CH, Simpson KL, Okada H, ''et al.'' |title=Complement regulatory proteins at the feto-maternal interface during human placental development: distribution of CD59 by comparison with membrane cofactor protein (CD46) and decay accelerating factor (CD55). |journal=Eur. J. Immunol. |volume=22 |issue= 6 |pages= 1579-85 |year= 1992 |pmid= 1376264 |doi= }}
*{{cite journal | author=Hahn WC, Menu E, Bothwell AL, ''et al.'' |title=Overlapping but nonidentical binding sites on CD2 for CD58 and a second ligand CD59. |journal=Science |volume=256 |issue= 5065 |pages= 1805-7 |year= 1992 |pmid= 1377404 |doi= }}
*{{cite journal | author=Ninomiya H, Sims PJ |title=The human complement regulatory protein CD59 binds to the alpha-chain of C8 and to the "b"domain of C9. |journal=J. Biol. Chem. |volume=267 |issue= 19 |pages= 13675-80 |year= 1992 |pmid= 1377690 |doi= }}
*{{cite journal | author=Petranka JG, Fleenor DE, Sykes K, ''et al.'' |title=Structure of the CD59-encoding gene: further evidence of a relationship to murine lymphocyte antigen Ly-6 protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 17 |pages= 7876-9 |year= 1992 |pmid= 1381503 |doi= }}
*{{cite journal | author=Motoyama N, Okada N, Yamashina M, Okada H |title=Paroxysmal nocturnal hemoglobinuria due to hereditary nucleotide deletion in the HRF20 (CD59) gene. |journal=Eur. J. Immunol. |volume=22 |issue= 10 |pages= 2669-73 |year= 1992 |pmid= 1382994 |doi= }}
*{{cite journal | author=Rooney IA, Morgan BP |title=Characterization of the membrane attack complex inhibitory protein CD59 antigen on human amniotic cells and in amniotic fluid. |journal=Immunology |volume=76 |issue= 4 |pages= 541-7 |year= 1992 |pmid= 1383132 |doi= }}
*{{cite journal | author=Tone M, Walsh LA, Waldmann H |title=Gene structure of human CD59 and demonstration that discrete mRNAs are generated by alternative polyadenylation. |journal=J. Mol. Biol. |volume=227 |issue= 3 |pages= 971-6 |year= 1992 |pmid= 1383553 |doi= }}
*{{cite journal | author=Philbrick WM, Palfree RG, Maher SE, ''et al.'' |title=The CD59 antigen is a structural homologue of murine Ly-6 antigens but lacks interferon inducibility. |journal=Eur. J. Immunol. |volume=20 |issue= 1 |pages= 87-92 |year= 1990 |pmid= 1689664 |doi= }}
*{{cite journal | author=Sawada R, Ohashi K, Anaguchi H, ''et al.'' |title=Isolation and expression of the full-length cDNA encoding CD59 antigen of human lymphocytes. |journal=DNA Cell Biol. |volume=9 |issue= 3 |pages= 213-20 |year= 1990 |pmid= 1692709 |doi= }}
*{{cite journal | author=Yamashina M, Ueda E, Kinoshita T, ''et al.'' |title=Inherited complete deficiency of 20-kilodalton homologous restriction factor (CD59) as a cause of paroxysmal nocturnal hemoglobinuria. |journal=N. Engl. J. Med. |volume=323 |issue= 17 |pages= 1184-9 |year= 1990 |pmid= 1699124 |doi= }}
*{{cite journal | author=Rooney IA, Morgan BP |title=Protection of human amniotic epithelial cells (HAEC) from complement-mediated lysis: expression on the cells of three complement inhibitory membrane proteins. |journal=Immunology |volume=71 |issue= 3 |pages= 308-11 |year= 1991 |pmid= 1702747 |doi= }}
*{{cite journal | author=Watts MJ, Dankert JR, Morgan EP |title=Isolation and characterization of a membrane-attack-complex-inhibiting protein present in human serum and other biological fluids. |journal=Biochem. J. |volume=265 |issue= 2 |pages= 471-7 |year= 1990 |pmid= 2302178 |doi= }}
*{{cite journal | author=Okada H, Nagami Y, Takahashi K, ''et al.'' |title=20 KDa homologous restriction factor of complement resembles T cell activating protein. |journal=Biochem. Biophys. Res. Commun. |volume=162 |issue= 3 |pages= 1553-9 |year= 1989 |pmid= 2475111 |doi= }}
*{{cite journal | author=Davies A, Simmons DL, Hale G, ''et al.'' |title=CD59, an LY-6-like protein expressed in human lymphoid cells, regulates the action of the complement membrane attack complex on homologous cells. |journal=J. Exp. Med. |volume=170 |issue= 3 |pages= 637-54 |year= 1989 |pmid= 2475570 |doi= }}
*{{cite journal | author=Sawada R, Ohashi K, Okano K, ''et al.'' |title=Complementary DNA sequence and deduced peptide sequence for CD59/MEM-43 antigen, the human homologue of murine lymphocyte antigen Ly-6C. |journal=Nucleic Acids Res. |volume=17 |issue= 16 |pages= 6728 |year= 1989 |pmid= 2476718 |doi= }}
*{{cite journal | author=Sugita Y, Tobe T, Oda E, ''et al.'' |title=Molecular cloning and characterization of MACIF, an inhibitor of membrane channel formation of complement. |journal=J. Biochem. |volume=106 |issue= 4 |pages= 555-7 |year= 1990 |pmid= 2606909 |doi= }}
*{{cite journal | author=Bora NS, Gobleman CL, Atkinson JP, ''et al.'' |title=Differential expression of the complement regulatory proteins in the human eye. |journal=Invest. Ophthalmol. Vis. Sci. |volume=34 |issue= 13 |pages= 3579-84 |year= 1994 |pmid= 7505007 |doi= }}
*{{cite journal | author=Kieffer B, Driscoll PC, Campbell ID, ''et al.'' |title=Three-dimensional solution structure of the extracellular region of the complement regulatory protein CD59, a new cell-surface protein domain related to snake venom neurotoxins. |journal=Biochemistry |volume=33 |issue= 15 |pages= 4471-82 |year= 1994 |pmid= 7512825 |doi= }}
*{{cite journal | author=Kennedy SP, Rollins SA, Burton WV, ''et al.'' |title=Protection of porcine aortic endothelial cells from complement-mediated cell lysis and activation by recombinant human CD59. |journal=Transplantation |volume=57 |issue= 10 |pages= 1494-501 |year= 1994 |pmid= 7515200 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CD80... {November 14, 2007 1:47:39 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 1:49:31 PM 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_CD80_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dr9.
| PDB = {{PDB2|1dr9}}, {{PDB2|1i8l}}
| Name = CD80 molecule
| HGNCid = 1700
| Symbol = CD80
| AltSymbols =; CD28LG; CD28LG1; LAB7
| OMIM = 112203
| ECnumber =
| Homologene = 3804
| MGIid = 101775
| Function = {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0015026 |text = coreceptor activity}} {{GNF_GO|id=GO:0016563 |text = transcription activator activity}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0009967 |text = positive regulation of signal transduction}} {{GNF_GO|id=GO:0042110 |text = T cell activation}} {{GNF_GO|id=GO:0045086 |text = positive regulation of interleukin-2 biosynthetic process}} {{GNF_GO|id=GO:0045425 |text = positive regulation of granulocyte macrophage colony-stimulating factor biosynthetic process}} {{GNF_GO|id=GO:0045627 |text = positive regulation of T-helper 1 cell differentiation}} {{GNF_GO|id=GO:0045941 |text = positive regulation of transcription}} {{GNF_GO|id=GO:0050731 |text = positive regulation of peptidyl-tyrosine phosphorylation}} {{GNF_GO|id=GO:0050798 |text = activated T cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 941
| Hs_Ensembl = ENSG00000121594
| Hs_RefseqProtein = NP_005182
| Hs_RefseqmRNA = NM_005191
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 120725835
| Hs_GenLoc_end = 120761139
| Hs_Uniprot = P33681
| Mm_EntrezGene = 12519
| Mm_Ensembl = ENSMUSG00000075122
| Mm_RefseqmRNA = NM_009855
| Mm_RefseqProtein = NP_033985
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 38378357
| Mm_GenLoc_end = 38405776
| Mm_Uniprot = Q3U4B5
}}
}}
'''CD80 molecule''', also known as '''CD80''', is a human [[gene]].
<!-- 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 B-lymphocyte activation antigen B7-1 (formerly referred to as B7) provides regulatory signals for T lymphocytes as a consequence of binding to the CD28 (MIM 186760) and CTLA4 (MIM 123890) ligands of T cells.[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: CD80 CD80 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=941| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Knolle PA, Gerken G |title=Local control of the immune response in the liver. |journal=Immunol. Rev. |volume=174 |issue= |pages= 21-34 |year= 2000 |pmid= 10807504 |doi= }}
*{{cite journal | author=Henz BM, Maurer M, Lippert U, ''et al.'' |title=Mast cells as initiators of immunity and host defense. |journal=Exp. Dermatol. |volume=10 |issue= 1 |pages= 1-10 |year= 2001 |pmid= 11168574 |doi= }}
*{{cite journal | author=Chang TT, Kuchroo VK, Sharpe AH |title=Role of the B7-CD28/CTLA-4 pathway in autoimmune disease. |journal=Curr. Dir. Autoimmun. |volume=5 |issue= |pages= 113-30 |year= 2002 |pmid= 11826754 |doi= }}
*{{cite journal | author=Stove V, Verhasselt B |title=Modelling thymic HIV-1 Nef effects. |journal=Curr. HIV Res. |volume=4 |issue= 1 |pages= 57-64 |year= 2006 |pmid= 16454711 |doi= }}
*{{cite journal | author=Quaranta MG, Mattioli B, Giordani L, Viora M |title=The immunoregulatory effects of HIV-1 Nef on dendritic cells and the pathogenesis of AIDS. |journal=FASEB J. |volume=20 |issue= 13 |pages= 2198-208 |year= 2006 |pmid= 17077296 |doi= 10.1096/fj.06-6260rev }}
*{{cite journal | author=Freeman GJ, Disteche CM, Gribben JG, ''et al.'' |title=The gene for B7, a costimulatory signal for T-cell activation, maps to chromosomal region 3q13.3-3q21. |journal=Blood |volume=79 |issue= 2 |pages= 489-94 |year= 1992 |pmid= 1370389 |doi= }}
*{{cite journal | author=Selvakumar A, Mohanraj BK, Eddy RL, ''et al.'' |title=Genomic organization and chromosomal location of the human gene encoding the B-lymphocyte activation antigen B7. |journal=Immunogenetics |volume=36 |issue= 3 |pages= 175-81 |year= 1992 |pmid= 1377173 |doi= }}
*{{cite journal | author=Freeman GJ, Gray GS, Gimmi CD, ''et al.'' |title=Structure, expression, and T cell costimulatory activity of the murine homologue of the human B lymphocyte activation antigen B7. |journal=J. Exp. Med. |volume=174 |issue= 3 |pages= 625-31 |year= 1991 |pmid= 1714935 |doi= }}
*{{cite journal | author=Freeman GJ, Freedman AS, Segil JM, ''et al.'' |title=B7, a new member of the Ig superfamily with unique expression on activated and neoplastic B cells. |journal=J. Immunol. |volume=143 |issue= 8 |pages= 2714-22 |year= 1989 |pmid= 2794510 |doi= }}
*{{cite journal | author=Weiskirchen R, Pino JD, Macalma T, ''et al.'' |title=The cysteine-rich protein family of highly related LIM domain proteins. |journal=J. Biol. Chem. |volume=270 |issue= 48 |pages= 28946-54 |year= 1996 |pmid= 7499425 |doi= }}
*{{cite journal | author=Lanier LL, O'Fallon S, Somoza C, ''et al.'' |title=CD80 (B7) and CD86 (B70) provide similar costimulatory signals for T cell proliferation, cytokine production, and generation of CTL. |journal=J. Immunol. |volume=154 |issue= 1 |pages= 97-105 |year= 1995 |pmid= 7527824 |doi= }}
*{{cite journal | author=Chirmule N, McCloskey TW, Hu R, ''et al.'' |title=HIV gp120 inhibits T cell activation by interfering with expression of costimulatory molecules CD40 ligand and CD80 (B71). |journal=J. Immunol. |volume=155 |issue= 2 |pages= 917-24 |year= 1995 |pmid= 7541827 |doi= }}
*{{cite journal | author=Peach RJ, Bajorath J, Naemura J, ''et al.'' |title=Both extracellular immunoglobin-like domains of CD80 contain residues critical for binding T cell surface receptors CTLA-4 and CD28. |journal=J. Biol. Chem. |volume=270 |issue= 36 |pages= 21181-7 |year= 1995 |pmid= 7545666 |doi= }}
*{{cite journal | author=Tuosto L, Piazza C, Moretti S, ''et al.'' |title=Ligation of either CD2 or CD28 rescues CD4+ T cells from HIV-gp120-induced apoptosis. |journal=Eur. J. Immunol. |volume=25 |issue= 10 |pages= 2917-22 |year= 1995 |pmid= 7589092 |doi= }}
*{{cite journal | author=Chirmule N, Oyaizu N, Saxinger C, Pahwa S |title=Nef protein of HIV-1 has B-cell stimulatory activity. |journal=AIDS |volume=8 |issue= 6 |pages= 733-4 |year= 1994 |pmid= 8086129 |doi= }}
*{{cite journal | author=Weiskirchen R, Bister K |title=Suppression in transformed avian fibroblasts of a gene (crp) encoding a cysteine-rich protein containing LIM domains. |journal=Oncogene |volume=8 |issue= 9 |pages= 2317-24 |year= 1993 |pmid= 8361751 |doi= }}
*{{cite journal | author=Dono M, Zupo S, Augliera A, ''et al.'' |title=Subepithelial B cells in the human palatine tonsil. II. Functional characterization. |journal=Eur. J. Immunol. |volume=26 |issue= 9 |pages= 2043-9 |year= 1996 |pmid= 8814244 |doi= }}
*{{cite journal | author=Reeves RH, Patch D, Sharpe AH, ''et al.'' |title=The costimulatory genes Cd80 and Cd86 are linked on mouse chromosome 16 and human chromosome 3. |journal=Mamm. Genome |volume=8 |issue= 8 |pages= 581-2 |year= 1997 |pmid= 9250865 |doi= }}
*{{cite journal | author=Olivares EG, Montes MJ, Oliver C, ''et al.'' |title=Cultured human decidual stromal cells express B7-1 (CD80) and B7-2 (CD86) and stimulate allogeneic T cells. |journal=Biol. Reprod. |volume=57 |issue= 3 |pages= 609-15 |year= 1997 |pmid= 9282998 |doi= }}
*{{cite journal | author=Weiskirchen R, Erdel M, Utermann G, Bister K |title=Cloning, structural analysis, and chromosomal localization of the human CSRP2 gene encoding the LIM domain protein CRP2. |journal=Genomics |volume=44 |issue= 1 |pages= 83-93 |year= 1997 |pmid= 9286703 |doi= 10.1006/geno.1997.4855 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DCN... {November 14, 2007 1:50:50 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 1:51:37 PM 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_DCN_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1xcd.
| PDB = {{PDB2|1xcd}}, {{PDB2|1xec}}, {{PDB2|1xku}}
| Name = Decorin
| HGNCid = 2705
| Symbol = DCN
| AltSymbols =; CSCD; DSPG2; PG40; PGII; PGS2; SLRR1B
| OMIM = 125255
| ECnumber =
| Homologene = 22430
| MGIid = 94872
| GeneAtlas_image1 = PBB_GE_DCN_201893_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_DCN_209335_at_tn.png
| GeneAtlas_image3 = PBB_GE_DCN_211813_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}}
| Process = {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1634
| Hs_Ensembl = ENSG00000011465
| Hs_RefseqProtein = NP_001911
| Hs_RefseqmRNA = NM_001920
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 90063167
| Hs_GenLoc_end = 90100937
| Hs_Uniprot = P07585
| Mm_EntrezGene = 13179
| Mm_Ensembl = ENSMUSG00000019929
| Mm_RefseqmRNA = NM_007833
| Mm_RefseqProtein = NP_031859
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 96912055
| Mm_GenLoc_end = 96947839
| Mm_Uniprot = Q3TSV1
}}
}}
'''Decorin''', also known as '''DCN''', is a human [[gene]].
<!-- 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 small cellular or pericellular matrix proteoglycan that is closely related in structure to biglycan protein. The encoded protein and biglycan are thought to be the result of a gene duplication. This protein is a component of connective tissue, binds to type I collagen fibrils, and plays a role in matrix assembly. It contains one attached glycosaminoglycan chain. This protein is capable of suppressing the growth of various tumor cell lines. There are multiple alternatively spliced transcript variants known for this gene. This gene is a candidate gene for Marfan syndrome.<ref>{{cite web | title = Entrez Gene: DCN decorin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1634| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ständer M, Naumann U, Wick W, Weller M |title=Transforming growth factor-beta and p-21: multiple molecular targets of decorin-mediated suppression of neoplastic growth. |journal=Cell Tissue Res. |volume=296 |issue= 2 |pages= 221-7 |year= 1999 |pmid= 10382266 |doi= }}
*{{cite journal | author=Fujisawa R |title=[Recent advances in research on bone matrix proteins] |journal=Nippon Rinsho |volume=60 Suppl 3 |issue= |pages= 72-8 |year= 2002 |pmid= 11979972 |doi= }}
*{{cite journal | author=Krumdieck R, Höök M, Rosenberg LC, Volanakis JE |title=The proteoglycan decorin binds C1q and inhibits the activity of the C1 complex. |journal=J. Immunol. |volume=149 |issue= 11 |pages= 3695-701 |year= 1992 |pmid= 1431141 |doi= }}
*{{cite journal | author=Winnemöller M, Schön P, Vischer P, Kresse H |title=Interactions between thrombospondin and the small proteoglycan decorin: interference with cell attachment. |journal=Eur. J. Cell Biol. |volume=59 |issue= 1 |pages= 47-55 |year= 1993 |pmid= 1468447 |doi= }}
*{{cite journal | author=Murphy-Ullrich JE, Schultz-Cherry S, Höök M |title=Transforming growth factor-beta complexes with thrombospondin. |journal=Mol. Biol. Cell |volume=3 |issue= 2 |pages= 181-8 |year= 1992 |pmid= 1550960 |doi= }}
*{{cite journal | author=Pulkkinen L, Alitalo T, Krusius T, Peltonen L |title=Expression of decorin in human tissues and cell lines and defined chromosomal assignment of the gene locus (DCN). |journal=Cytogenet. Cell Genet. |volume=60 |issue= 2 |pages= 107-11 |year= 1992 |pmid= 1611907 |doi= }}
*{{cite journal | author=McBride OW, Fisher LW, Young MF |title=Localization of PGI (biglycan, BGN) and PGII (decorin, DCN, PG-40) genes on human chromosomes Xq13-qter and 12q, respectively. |journal=Genomics |volume=6 |issue= 2 |pages= 219-25 |year= 1990 |pmid= 1968422 |doi= }}
*{{cite journal | author=Fleischmajer R, Fisher LW, MacDonald ED, ''et al.'' |title=Decorin interacts with fibrillar collagen of embryonic and adult human skin. |journal=J. Struct. Biol. |volume=106 |issue= 1 |pages= 82-90 |year= 1991 |pmid= 2059554 |doi= }}
*{{cite journal | author=Pulkkinen L, Kainulainen K, Krusius T, ''et al.'' |title=Deficient expression of the gene coding for decorin in a lethal form of Marfan syndrome. |journal=J. Biol. Chem. |volume=265 |issue= 29 |pages= 17780-5 |year= 1990 |pmid= 2211661 |doi= }}
*{{cite journal | author=Yamaguchi Y, Mann DM, Ruoslahti E |title=Negative regulation of transforming growth factor-beta by the proteoglycan decorin. |journal=Nature |volume=346 |issue= 6281 |pages= 281-4 |year= 1990 |pmid= 2374594 |doi= 10.1038/346281a0 }}
*{{cite journal | author=Greve H, Blumberg P, Schmidt G, ''et al.'' |title=Influence of collagen lattice on the metabolism of small proteoglycan II by cultured fibroblasts. |journal=Biochem. J. |volume=269 |issue= 1 |pages= 149-55 |year= 1990 |pmid= 2375748 |doi= }}
*{{cite journal | author=Roughley PJ, White RJ |title=Dermatan sulphate proteoglycans of human articular cartilage. The properties of dermatan sulphate proteoglycans I and II. |journal=Biochem. J. |volume=262 |issue= 3 |pages= 823-7 |year= 1990 |pmid= 2590169 |doi= }}
*{{cite journal | author=Fisher LW, Termine JD, Young MF |title=Deduced protein sequence of bone small proteoglycan I (biglycan) shows homology with proteoglycan II (decorin) and several nonconnective tissue proteins in a variety of species. |journal=J. Biol. Chem. |volume=264 |issue= 8 |pages= 4571-6 |year= 1989 |pmid= 2647739 |doi= }}
*{{cite journal | author=Yamaguchi Y, Ruoslahti E |title=Expression of human proteoglycan in Chinese hamster ovary cells inhibits cell proliferation. |journal=Nature |volume=336 |issue= 6196 |pages= 244-6 |year= 1988 |pmid= 3194009 |doi= 10.1038/336244a0 }}
*{{cite journal | author=Krusius T, Ruoslahti E |title=Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 20 |pages= 7683-7 |year= 1986 |pmid= 3484330 |doi= }}
*{{cite journal | author=Fisher LW, Hawkins GR, Tuross N, Termine JD |title=Purification and partial characterization of small proteoglycans I and II, bone sialoproteins I and II, and osteonectin from the mineral compartment of developing human bone. |journal=J. Biol. Chem. |volume=262 |issue= 20 |pages= 9702-8 |year= 1987 |pmid= 3597437 |doi= }}
*{{cite journal | author=Lysiak JJ, Hunt J, Pringle GA, Lala PK |title=Localization of transforming growth factor beta and its natural inhibitor decorin in the human placenta and decidua throughout gestation. |journal=Placenta |volume=16 |issue= 3 |pages= 221-31 |year= 1995 |pmid= 7638106 |doi= }}
*{{cite journal | author=Takeuchi Y, Kodama Y, Matsumoto T |title=Bone matrix decorin binds transforming growth factor-beta and enhances its bioactivity. |journal=J. Biol. Chem. |volume=269 |issue= 51 |pages= 32634-8 |year= 1995 |pmid= 7798269 |doi= }}
*{{cite journal | author=Scholzen T, Solursh M, Suzuki S, ''et al.'' |title=The murine decorin. Complete cDNA cloning, genomic organization, chromosomal assignment, and expression during organogenesis and tissue differentiation. |journal=J. Biol. Chem. |volume=269 |issue= 45 |pages= 28270-81 |year= 1994 |pmid= 7961765 |doi= }}
*{{cite journal | author=Danielson KG, Fazzio A, Cohen I, ''et al.'' |title=The human decorin gene: intron-exon organization, discovery of two alternatively spliced exons in the 5' untranslated region, and mapping of the gene to chromosome 12q23. |journal=Genomics |volume=15 |issue= 1 |pages= 146-60 |year= 1993 |pmid= 8432526 |doi= 10.1006/geno.1993.1022 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ERBB4... {November 14, 2007 1:51:37 PM PST}
- SEARCH REDIRECT: Control Box Found: ERBB4 {November 14, 2007 1:52:15 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 1:52:16 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 1:52:16 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 1:52:16 PM PST}
- UPDATED: Updated protein page: ERBB4 {November 14, 2007 1:52:24 PM PST}
- INFO: Beginning work on FSHR... {November 14, 2007 1:52:25 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 1:54:35 PM 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_FSHR_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1xwd.
| PDB = {{PDB2|1xwd}}
| Name = Follicle stimulating hormone receptor
| HGNCid = 3969
| Symbol = FSHR
| AltSymbols =; FSHRO; LGR1; MGC141667; MGC141668; ODG1
| OMIM = 136435
| ECnumber =
| Homologene = 117
| MGIid = 95583
| GeneAtlas_image1 = PBB_GE_FSHR_211201_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004963 |text = follicle-stimulating hormone receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to 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:0007283 |text = spermatogenesis}} {{GNF_GO|id=GO:0007292 |text = female gamete generation}} {{GNF_GO|id=GO:0008585 |text = female gonad development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2492
| Hs_Ensembl = ENSG00000170820
| Hs_RefseqProtein = NP_000136
| Hs_RefseqmRNA = NM_000145
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 49043156
| Hs_GenLoc_end = 49235134
| Hs_Uniprot = P23945
| Mm_EntrezGene = 14309
| Mm_Ensembl = ENSMUSG00000032937
| Mm_RefseqmRNA = NM_013523
| Mm_RefseqProtein = NP_038551
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 88893278
| Mm_GenLoc_end = 89109001
| Mm_Uniprot = P35378
}}
}}
'''Follicle stimulating hormone receptor''', also known as '''FSHR''', is a human [[gene]].
<!-- 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 belongs to family 1 of G-protein coupled receptors. It is the receptor for follicle stimulating hormone and functions in gonad development. Alternative splicing occurs at this locus and two transcript variants encoding distinct isoforms have been identified.<ref>{{cite web | title = Entrez Gene: FSHR follicle stimulating hormone receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2492| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=de la Chapelle A |title=Disease gene mapping in isolated human populations: the example of Finland. |journal=J. Med. Genet. |volume=30 |issue= 10 |pages= 857-65 |year= 1993 |pmid= 8230163 |doi= }}
*{{cite journal | author=Simoni M, Gromoll J, Nieschlag E |title=The follicle-stimulating hormone receptor: biochemistry, molecular biology, physiology, and pathophysiology. |journal=Endocr. Rev. |volume=18 |issue= 6 |pages= 739-73 |year= 1998 |pmid= 9408742 |doi= }}
*{{cite journal | author=Amsterdam A, Hanoch T, Dantes A, ''et al.'' |title=Mechanisms of gonadotropin desensitization. |journal=Mol. Cell. Endocrinol. |volume=187 |issue= 1-2 |pages= 69-74 |year= 2003 |pmid= 11988313 |doi= }}
*{{cite journal | author=Simoni M, Nieschlag E, Gromoll J |title=Isoforms and single nucleotide polymorphisms of the FSH receptor gene: implications for human reproduction. |journal=Hum. Reprod. Update |volume=8 |issue= 5 |pages= 413-21 |year= 2003 |pmid= 12398222 |doi= }}
*{{cite journal | author=Delbaere A, Smits G, Olatunbosun O, ''et al.'' |title=New insights into the pathophysiology of ovarian hyperstimulation syndrome. What makes the difference between spontaneous and iatrogenic syndrome? |journal=Hum. Reprod. |volume=19 |issue= 3 |pages= 486-9 |year= 2004 |pmid= 14998941 |doi= 10.1093/humrep/deh124 }}
*{{cite journal | author=Bose CK |title=Role of nerve growth factor and FSH receptor in epithelial ovarian cancer. |journal=Reprod. Biomed. Online |volume=11 |issue= 2 |pages= 194-7 |year= 2005 |pmid= 16168216 |doi= }}
*{{cite journal | author=Wunsch A, Sonntag B, Simoni M |title=Polymorphism of the FSH receptor and ovarian response to FSH. |journal=Ann. Endocrinol. (Paris) |volume=68 |issue= 2-3 |pages= 160-6 |year= 2007 |pmid= 17544358 |doi= 10.1016/j.ando.2007.04.006 }}
*{{cite journal | author=Kelton CA, Cheng SV, Nugent NP, ''et al.'' |title=The cloning of the human follicle stimulating hormone receptor and its expression in COS-7, CHO, and Y-1 cells. |journal=Mol. Cell. Endocrinol. |volume=89 |issue= 1-2 |pages= 141-51 |year= 1993 |pmid= 1301382 |doi= }}
*{{cite journal | author=Tilly JL, Aihara T, Nishimori K, ''et al.'' |title=Expression of recombinant human follicle-stimulating hormone receptor: species-specific ligand binding, signal transduction, and identification of multiple ovarian messenger ribonucleic acid transcripts. |journal=Endocrinology |volume=131 |issue= 2 |pages= 799-806 |year= 1992 |pmid= 1322283 |doi= }}
*{{cite journal | author=Gromoll J, Gudermann T, Nieschlag E |title=Molecular cloning of a truncated isoform of the human follicle stimulating hormone receptor. |journal=Biochem. Biophys. Res. Commun. |volume=188 |issue= 3 |pages= 1077-83 |year= 1992 |pmid= 1359889 |doi= }}
*{{cite journal | author=Minegishi T, Nakamura K, Takakura Y, ''et al.'' |title=Cloning and sequencing of human FSH receptor cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=175 |issue= 3 |pages= 1125-30 |year= 1991 |pmid= 1709010 |doi= }}
*{{cite journal | author=Aittomäki K, Lucena JL, Pakarinen P, ''et al.'' |title=Mutation in the follicle-stimulating hormone receptor gene causes hereditary hypergonadotropic ovarian failure. |journal=Cell |volume=82 |issue= 6 |pages= 959-68 |year= 1995 |pmid= 7553856 |doi= }}
*{{cite journal | author=Gromoll J, Ried T, Holtgreve-Grez H, ''et al.'' |title=Localization of the human FSH receptor to chromosome 2 p21 using a genomic probe comprising exon 10. |journal=J. Mol. Endocrinol. |volume=12 |issue= 3 |pages= 265-71 |year= 1994 |pmid= 7916967 |doi= }}
*{{cite journal | author=Gromoll J, Dankbar B, Gudermann T |title=Characterization of the 5' flanking region of the human follicle-stimulating hormone receptor gene. |journal=Mol. Cell. Endocrinol. |volume=102 |issue= 1-2 |pages= 93-102 |year= 1994 |pmid= 7926278 |doi= }}
*{{cite journal | author=Rousseau-Merck MF, Atger M, Loosfelt H, ''et al.'' |title=The chromosomal localization of the human follicle-stimulating hormone receptor gene (FSHR) on 2p21-p16 is similar to that of the luteinizing hormone receptor gene. |journal=Genomics |volume=15 |issue= 1 |pages= 222-4 |year= 1993 |pmid= 8432542 |doi= 10.1006/geno.1993.1041 }}
*{{cite journal | author=Jiang X, Dreano M, Buckler DR, ''et al.'' |title=Structural predictions for the ligand-binding region of glycoprotein hormone receptors and the nature of hormone-receptor interactions. |journal=Structure |volume=3 |issue= 12 |pages= 1341-53 |year= 1996 |pmid= 8747461 |doi= }}
*{{cite journal | author=Aittomäki K, Herva R, Stenman UH, ''et al.'' |title=Clinical features of primary ovarian failure caused by a point mutation in the follicle-stimulating hormone receptor gene. |journal=J. Clin. Endocrinol. Metab. |volume=81 |issue= 10 |pages= 3722-6 |year= 1996 |pmid= 8855829 |doi= }}
*{{cite journal | author=Tapanainen JS, Aittomäki K, Min J, ''et al.'' |title=Men homozygous for an inactivating mutation of the follicle-stimulating hormone (FSH) receptor gene present variable suppression of spermatogenesis and fertility. |journal=Nat. Genet. |volume=15 |issue= 2 |pages= 205-6 |year= 1997 |pmid= 9020851 |doi= 10.1038/ng0297-205 }}
*{{cite journal | author=Kotlar TJ, Young RH, Albanese C, ''et al.'' |title=A mutation in the follicle-stimulating hormone receptor occurs frequently in human ovarian sex cord tumors. |journal=J. Clin. Endocrinol. Metab. |volume=82 |issue= 4 |pages= 1020-6 |year= 1997 |pmid= 9100567 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GTF2B... {November 14, 2007 1:54:35 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 1:55:51 PM 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_GTF2B_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1c9b.
| PDB = {{PDB2|1c9b}}, {{PDB2|1dl6}}, {{PDB2|1rly}}, {{PDB2|1ro4}}, {{PDB2|1tfb}}, {{PDB2|1vol}}, {{PDB2|2phg}}
| Name = General transcription factor IIB
| HGNCid = 4648
| Symbol = GTF2B
| AltSymbols =; TF2B; TFIIB
| OMIM = 189963
| ECnumber =
| Homologene = 1158
| MGIid = 2385191
| GeneAtlas_image1 = PBB_GE_GTF2B_208066_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016251 |text = general RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0030528 |text = transcription regulator activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005667 |text = transcription factor complex}}
| Process = {{GNF_GO|id=GO:0006352 |text = transcription initiation}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2959
| Hs_Ensembl = ENSG00000137947
| Hs_RefseqProtein = NP_001505
| Hs_RefseqmRNA = NM_001514
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 89091203
| Hs_GenLoc_end = 89129889
| Hs_Uniprot = Q00403
| Mm_EntrezGene = 229906
| Mm_Ensembl = ENSMUSG00000028271
| Mm_RefseqmRNA = NM_145546
| Mm_RefseqProtein = NP_663521
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 142702633
| Mm_GenLoc_end = 142720992
| Mm_Uniprot = Q3ULN2
}}
}}
'''General transcription factor IIB''', also known as '''GTF2B''', is a human [[gene]].
<!-- 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 general transcription factor IIB, one of the ubiquitous factors required for transcription initiation by RNA polymerase II. The protein localizes to the nucleus where it forms a complex (the DAB complex) with transcription factors IID and IIA. Transcription factor IIB serves as a bridge between IID, the factor which initially recognizes the promoter sequence, and RNA polymerase II.<ref>{{cite web | title = Entrez Gene: GTF2B general transcription factor IIB| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2959| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Roeder RG |title=The role of general initiation factors in transcription by RNA polymerase II. |journal=Trends Biochem. Sci. |volume=21 |issue= 9 |pages= 327-35 |year= 1996 |pmid= 8870495 |doi= }}
*{{cite journal | author=Kino T, Pavlakis GN |title=Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1. |journal=DNA Cell Biol. |volume=23 |issue= 4 |pages= 193-205 |year= 2004 |pmid= 15142377 |doi= 10.1089/104454904773819789 }}
*{{cite journal | author=Kino T, Chrousos GP |title=Human immunodeficiency virus type-1 accessory protein Vpr: a causative agent of the AIDS-related insulin resistance/lipodystrophy syndrome? |journal=Ann. N. Y. Acad. Sci. |volume=1024 |issue= |pages= 153-67 |year= 2004 |pmid= 15265780 |doi= 10.1196/annals.1321.013 }}
*{{cite journal | author=Seelamgari A, Maddukuri A, Berro R, ''et al.'' |title=Role of viral regulatory and accessory proteins in HIV-1 replication. |journal=Front. Biosci. |volume=9 |issue= |pages= 2388-413 |year= 2006 |pmid= 15353294 |doi= }}
*{{cite journal | author=Ing NH, Beekman JM, Tsai SY, ''et al.'' |title=Members of the steroid hormone receptor superfamily interact with TFIIB (S300-II). |journal=J. Biol. Chem. |volume=267 |issue= 25 |pages= 17617-23 |year= 1992 |pmid= 1517211 |doi= }}
*{{cite journal | author=Ha I, Lane WS, Reinberg D |title=Cloning of a human gene encoding the general transcription initiation factor IIB. |journal=Nature |volume=352 |issue= 6337 |pages= 689-95 |year= 1991 |pmid= 1876184 |doi= 10.1038/352689a0 }}
*{{cite journal | author=Malik S, Hisatake K, Sumimoto H, ''et al.'' |title=Sequence of general transcription factor TFIIB and relationships to other initiation factors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 21 |pages= 9553-7 |year= 1991 |pmid= 1946368 |doi= }}
*{{cite journal | author=Klemm RD, Goodrich JA, Zhou S, Tjian R |title=Molecular cloning and expression of the 32-kDa subunit of human TFIID reveals interactions with VP16 and TFIIB that mediate transcriptional activation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 13 |pages= 5788-92 |year= 1995 |pmid= 7597030 |doi= }}
*{{cite journal | author=Veschambre P, Simard P, Jalinot P |title=Evidence for functional interaction between the HIV-1 Tat transactivator and the TATA box binding protein in vivo. |journal=J. Mol. Biol. |volume=250 |issue= 2 |pages= 169-80 |year= 1995 |pmid= 7608968 |doi= 10.1006/jmbi.1995.0368 }}
*{{cite journal | author=Desai-Yajnik V, Hadzic E, Modlinger P, ''et al.'' |title=Interactions of thyroid hormone receptor with the human immunodeficiency virus type 1 (HIV-1) long terminal repeat and the HIV-1 Tat transactivator. |journal=J. Virol. |volume=69 |issue= 8 |pages= 5103-12 |year= 1995 |pmid= 7609079 |doi= }}
*{{cite journal | author=Cavaillès V, Dauvois S, L'Horset F, ''et al.'' |title=Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor. |journal=EMBO J. |volume=14 |issue= 15 |pages= 3741-51 |year= 1995 |pmid= 7641693 |doi= }}
*{{cite journal | author=Nakshatri H, Nakshatri P, Currie RA |title=Interaction of Oct-1 with TFIIB. Implications for a novel response elicited through the proximal octamer site of the lipoprotein lipase promoter. |journal=J. Biol. Chem. |volume=270 |issue= 33 |pages= 19613-23 |year= 1995 |pmid= 7642649 |doi= }}
*{{cite journal | author=Abendroth FD, Peterson SR, Galman M, ''et al.'' |title=Identification of human autoantibodies to transcription factor IIB. |journal=Nucleic Acids Res. |volume=23 |issue= 14 |pages= 2770-4 |year= 1995 |pmid= 7651839 |doi= }}
*{{cite journal | author=Bagby S, Kim S, Maldonado E, ''et al.'' |title=Solution structure of the C-terminal core domain of human TFIIB: similarity to cyclin A and interaction with TATA-binding protein. |journal=Cell |volume=82 |issue= 5 |pages= 857-67 |year= 1995 |pmid= 7671313 |doi= }}
*{{cite journal | author=Nikolov DB, Chen H, Halay ED, ''et al.'' |title=Crystal structure of a TFIIB-TBP-TATA-element ternary complex. |journal=Nature |volume=377 |issue= 6545 |pages= 119-28 |year= 1995 |pmid= 7675079 |doi= 10.1038/377119a0 }}
*{{cite journal | author=Schmitz ML, Stelzer G, Altmann H, ''et al.'' |title=Interaction of the COOH-terminal transactivation domain of p65 NF-kappa B with TATA-binding protein, transcription factor IIB, and coactivators. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7219-26 |year= 1995 |pmid= 7706261 |doi= }}
*{{cite journal | author=Yu L, Zhang Z, Loewenstein PM, ''et al.'' |title=Molecular cloning and characterization of a cellular protein that interacts with the human immunodeficiency virus type 1 Tat transactivator and encodes a strong transcriptional activation domain. |journal=J. Virol. |volume=69 |issue= 5 |pages= 3007-16 |year= 1995 |pmid= 7707527 |doi= }}
*{{cite journal | author=Yu L, Loewenstein PM, Zhang Z, Green M |title=In vitro interaction of the human immunodeficiency virus type 1 Tat transactivator and the general transcription factor TFIIB with the cellular protein TAP. |journal=J. Virol. |volume=69 |issue= 5 |pages= 3017-23 |year= 1995 |pmid= 7707528 |doi= }}
*{{cite journal | author=Auffray C, Behar G, Bois F, ''et al.'' |title=[IMAGE: molecular integration of the analysis of the human genome and its expression] |journal=C. R. Acad. Sci. III, Sci. Vie |volume=318 |issue= 2 |pages= 263-72 |year= 1995 |pmid= 7757816 |doi= }}
*{{cite journal | author=Franklin CC, McCulloch AV, Kraft AS |title=In vitro association between the Jun protein family and the general transcription factors, TBP and TFIIB. |journal=Biochem. J. |volume=305 ( Pt 3) |issue= |pages= 967-74 |year= 1995 |pmid= 7848298 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HPRT1... {November 14, 2007 1:55:51 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 1:56:56 PM 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
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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_HPRT1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bzy.
| PDB = {{PDB2|1bzy}}, {{PDB2|1d6n}}, {{PDB2|1hmp}}, {{PDB2|1z7g}}
| Name = Hypoxanthine phosphoribosyltransferase 1 (Lesch-Nyhan syndrome)
| HGNCid = 5157
| Symbol = HPRT1
| AltSymbols =; HGPRT; HPRT
| OMIM = 308000
| ECnumber =
| Homologene = 56590
| MGIid = 96217
| GeneAtlas_image1 = PBB_GE_HPRT1_202854_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004422 |text = hypoxanthine phosphoribosyltransferase activity}} {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0001975 |text = response to amphetamine}} {{GNF_GO|id=GO:0006164 |text = purine nucleotide biosynthetic process}} {{GNF_GO|id=GO:0006166 |text = purine ribonucleoside salvage}} {{GNF_GO|id=GO:0006168 |text = adenine salvage}} {{GNF_GO|id=GO:0006178 |text = guanine salvage}} {{GNF_GO|id=GO:0007625 |text = grooming behavior}} {{GNF_GO|id=GO:0009116 |text = nucleoside metabolic process}} {{GNF_GO|id=GO:0019835 |text = cytolysis}} {{GNF_GO|id=GO:0021756 |text = striatum development}} {{GNF_GO|id=GO:0021895 |text = cerebral cortex neuron differentiation}} {{GNF_GO|id=GO:0021954 |text = central nervous system neuron development}} {{GNF_GO|id=GO:0042417 |text = dopamine metabolic process}} {{GNF_GO|id=GO:0045964 |text = positive regulation of dopamine metabolic process}} {{GNF_GO|id=GO:0046100 |text = hypoxanthine metabolic process}} {{GNF_GO|id=GO:0046651 |text = lymphocyte proliferation}} {{GNF_GO|id=GO:0048813 |text = dendrite morphogenesis}} {{GNF_GO|id=GO:0051289 |text = protein homotetramerization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3251
| Hs_Ensembl = ENSG00000165704
| Hs_RefseqProtein = NP_000185
| Hs_RefseqmRNA = NM_000194
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 133421849
| Hs_GenLoc_end = 133462364
| Hs_Uniprot = P00492
| Mm_EntrezGene = 15452
| Mm_Ensembl = ENSMUSG00000025630
| Mm_RefseqmRNA = NM_013556
| Mm_RefseqProtein = NP_038584
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 49232760
| Mm_GenLoc_end = 49266287
| Mm_Uniprot = Q6TDG6
}}
}}
'''Hypoxanthine phosphoribosyltransferase 1 (Lesch-Nyhan syndrome)''', also known as '''HPRT1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Sculley DG, Dawson PA, Emmerson BT, Gordon RB |title=A review of the molecular basis of hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency. |journal=Hum. Genet. |volume=90 |issue= 3 |pages= 195-207 |year= 1993 |pmid= 1487231 |doi= }}
*{{cite journal | author=Davidson BL, Tarlé SA, Van Antwerp M, ''et al.'' |title=Identification of 17 independent mutations responsible for human hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency. |journal=Am. J. Hum. Genet. |volume=48 |issue= 5 |pages= 951-8 |year= 1991 |pmid= 2018042 |doi= }}
*{{cite journal | author=Stout JT, Caskey CT |title=HPRT: gene structure, expression, and mutation. |journal=Annu. Rev. Genet. |volume=19 |issue= |pages= 127-48 |year= 1986 |pmid= 3909940 |doi= 10.1146/annurev.ge.19.120185.001015 }}
*{{cite journal | author=Sege-Peterson K, Chambers J, Page T, ''et al.'' |title=Characterization of mutations in phenotypic variants of hypoxanthine phosphoribosyltransferase deficiency. |journal=Hum. Mol. Genet. |volume=1 |issue= 6 |pages= 427-32 |year= 1993 |pmid= 1301916 |doi= }}
*{{cite journal | author=Lightfoot T, Joshi R, Nuki G, Snyder FF |title=The point mutation of hypoxanthine-guanine phosphoribosyltransferase (HPRTEdinburgh) and detection by allele-specific polymerase chain reaction. |journal=Hum. Genet. |volume=88 |issue= 6 |pages= 695-6 |year= 1992 |pmid= 1551676 |doi= }}
*{{cite journal | author=Yamada Y, Goto H, Ogasawara N |title=Identification of two independent Japanese mutant HPRT genes using the PCR technique. |journal=Adv. Exp. Med. Biol. |volume=309B |issue= |pages= 121-4 |year= 1992 |pmid= 1840476 |doi= }}
*{{cite journal | author=Sculley DG, Dawson PA, Beacham IR, ''et al.'' |title=Hypoxanthine-guanine phosphoribosyltransferase deficiency: analysis of HPRT mutations by direct sequencing and allele-specific amplification. |journal=Hum. Genet. |volume=87 |issue= 6 |pages= 688-92 |year= 1991 |pmid= 1937471 |doi= }}
*{{cite journal | author=Tarlé SA, Davidson BL, Wu VC, ''et al.'' |title=Determination of the mutations responsible for the Lesch-Nyhan syndrome in 17 subjects. |journal=Genomics |volume=10 |issue= 2 |pages= 499-501 |year= 1991 |pmid= 2071157 |doi= }}
*{{cite journal | author=Gordon RB, Sculley DG, Dawson PA, ''et al.'' |title=Identification of a single nucleotide substitution in the coding sequence of in vitro amplified cDNA from a patient with partial HPRT deficiency (HPRTBRISBANE). |journal=J. Inherit. Metab. Dis. |volume=13 |issue= 5 |pages= 692-700 |year= 1991 |pmid= 2246854 |doi= }}
*{{cite journal | author=Edwards A, Voss H, Rice P, ''et al.'' |title=Automated DNA sequencing of the human HPRT locus. |journal=Genomics |volume=6 |issue= 4 |pages= 593-608 |year= 1990 |pmid= 2341149 |doi= }}
*{{cite journal | author=Gibbs RA, Nguyen PN, Edwards A, ''et al.'' |title=Multiplex DNA deletion detection and exon sequencing of the hypoxanthine phosphoribosyltransferase gene in Lesch-Nyhan families. |journal=Genomics |volume=7 |issue= 2 |pages= 235-44 |year= 1990 |pmid= 2347587 |doi= }}
*{{cite journal | author=Skopek TR, Recio L, Simpson D, ''et al.'' |title=Molecular analyses of a Lesch-Nyhan syndrome mutation (hprtMontreal) by use of T-lymphocyte cultures. |journal=Hum. Genet. |volume=85 |issue= 1 |pages= 111-6 |year= 1990 |pmid= 2358296 |doi= }}
*{{cite journal | author=Davidson BL, Tarlé SA, Palella TD, Kelley WN |title=Molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in ten subjects determined by direct sequencing of amplified transcripts. |journal=J. Clin. Invest. |volume=84 |issue= 1 |pages= 342-6 |year= 1989 |pmid= 2738157 |doi= }}
*{{cite journal | author=Ogasawara N, Stout JT, Goto H, ''et al.'' |title=Molecular analysis of a female Lesch-Nyhan patient. |journal=J. Clin. Invest. |volume=84 |issue= 3 |pages= 1024-7 |year= 1989 |pmid= 2760209 |doi= }}
*{{cite journal | author=Yang TP, Stout JT, Konecki DS, ''et al.'' |title=Spontaneous reversion of novel Lesch-Nyhan mutation by HPRT gene rearrangement. |journal=Somat. Cell Mol. Genet. |volume=14 |issue= 3 |pages= 293-303 |year= 1988 |pmid= 2835825 |doi= }}
*{{cite journal | author=Fujimori S, Hidaka Y, Davidson BL, ''et al.'' |title=Identification of a single nucleotide change in a mutant gene for hypoxanthine-guanine phosphoribosyltransferase (HPRT Ann Arbor). |journal=Hum. Genet. |volume=79 |issue= 1 |pages= 39-43 |year= 1988 |pmid= 2896620 |doi= }}
*{{cite journal | author=Davidson BL, Pashmforoush M, Kelley WN, Palella TD |title=Human hypoxanthine-guanine phosphoribosyltransferase deficiency. The molecular defect in a patient with gout (HPRTAshville). |journal=J. Biol. Chem. |volume=264 |issue= 1 |pages= 520-5 |year= 1989 |pmid= 2909537 |doi= }}
*{{cite journal | author=Fujimori S, Davidson BL, Kelley WN, Palella TD |title=Identification of a single nucleotide change in the hypoxanthine-guanine phosphoribosyltransferase gene (HPRTYale) responsible for Lesch-Nyhan syndrome. |journal=J. Clin. Invest. |volume=83 |issue= 1 |pages= 11-3 |year= 1989 |pmid= 2910902 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KRT18... {November 14, 2007 1:56:56 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 1:58:34 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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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 = Keratin 18
| HGNCid = 6430
| Symbol = KRT18
| AltSymbols =; CYK18; K18
| OMIM = 148070
| ECnumber =
| Homologene = 55448
| MGIid = 96692
| GeneAtlas_image1 = PBB_GE_KRT18_201596_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005882 |text = intermediate filament}}
| Process = {{GNF_GO|id=GO:0009653 |text = anatomical structure morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3875
| Hs_Ensembl = ENSG00000111057
| Hs_RefseqProtein = NP_000215
| Hs_RefseqmRNA = NM_000224
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 51629225
| Hs_GenLoc_end = 51632951
| Hs_Uniprot = P05783
| Mm_EntrezGene = 16668
| Mm_Ensembl = ENSMUSG00000023043
| Mm_RefseqmRNA = NM_010664
| Mm_RefseqProtein = NP_034794
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 101856259
| Mm_GenLoc_end = 101860055
| Mm_Uniprot = Q3TIX1
}}
}}
'''Keratin 18''', also known as '''KRT18''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = KRT18 encodes the type I intermediate filament chain keratin 18. Keratin 18, together with its filament partner keratin 8, are perhaps the most commonly found members of the intermediate filament gene family. They are expressed in single layer epithelial tissues of the body. Mutations in this gene have been linked to cryptogenic cirrhosis. Two transcript variants encoding the same protein have been found for this gene.<ref>{{cite web | title = Entrez Gene: KRT18 keratin 18| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3875| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Roland FP |title=Management of atypical pneumonias in view of the new entity "Legionnaire's disease". |journal=Rhode Island medical journal |volume=61 |issue= 7 |pages= 270-2 |year= 1978 |pmid= 276901 |doi= }}
*{{cite journal | author=Omary MB, Baxter GT, Chou CF, ''et al.'' |title=PKC epsilon-related kinase associates with and phosphorylates cytokeratin 8 and 18. |journal=J. Cell Biol. |volume=117 |issue= 3 |pages= 583-93 |year= 1992 |pmid= 1374067 |doi= }}
*{{cite journal | author=Waseem A, Gough AC, Spurr NK, Lane EB |title=Localization of the gene for human simple epithelial keratin 18 to chromosome 12 using polymerase chain reaction. |journal=Genomics |volume=7 |issue= 2 |pages= 188-94 |year= 1990 |pmid= 1693358 |doi= }}
*{{cite journal | author=Heath P, Elvin P, Jenner D, ''et al.'' |title=Localisation of a cDNA clone for human cytokeratin 18 to chromosome 17p11-p12 by in situ hybridisation. |journal=Hum. Genet. |volume=85 |issue= 6 |pages= 669-70 |year= 1990 |pmid= 1699878 |doi= }}
*{{cite journal | author=Waseem A, Alexander CM, Steel JB, Lane EB |title=Embryonic simple epithelial keratins 8 and 18: chromosomal location emphasizes difference from other keratin pairs. |journal=New Biol. |volume=2 |issue= 5 |pages= 464-78 |year= 1991 |pmid= 1705144 |doi= }}
*{{cite journal | author=Romano V, Hatzfeld M, Magin TM, ''et al.'' |title=Cytokeratin expression in simple epithelia. I. Identification of mRNA coding for human cytokeratin no. 18 by a cDNA clone. |journal=Differentiation |volume=30 |issue= 3 |pages= 244-53 |year= 1986 |pmid= 2422083 |doi= }}
*{{cite journal | author=Oshima RG, Millán JL, Ceceña G |title=Comparison of mouse and human keratin 18: a component of intermediate filaments expressed prior to implantation. |journal=Differentiation |volume=33 |issue= 1 |pages= 61-8 |year= 1987 |pmid= 2434380 |doi= }}
*{{cite journal | author=Leube RE, Bosch FX, Romano V, ''et al.'' |title=Cytokeratin expression in simple epithelia. III. Detection of mRNAs encoding human cytokeratins nos. 8 and 18 in normal and tumor cells by hybridization with cDNA sequences in vitro and in situ. |journal=Differentiation |volume=33 |issue= 1 |pages= 69-85 |year= 1987 |pmid= 2434381 |doi= }}
*{{cite journal | author=Kulesh DA, Oshima RG |title=Cloning of the human keratin 18 gene and its expression in nonepithelial mouse cells. |journal=Mol. Cell. Biol. |volume=8 |issue= 4 |pages= 1540-50 |year= 1988 |pmid= 2454392 |doi= }}
*{{cite journal | author=Sémat A, Vasseur M, Maillet L, ''et al.'' |title=Sequence analysis of murine cytokeratin endo A (no. 8) cDNA. Evidence for mRNA species initiated upstream of the normal 5' end in PCC4 cells. |journal=Differentiation |volume=37 |issue= 1 |pages= 40-6 |year= 1988 |pmid= 2454862 |doi= }}
*{{cite journal | author=Kulesh DA, Oshima RG |title=Complete structure of the gene for human keratin 18. |journal=Genomics |volume=4 |issue= 3 |pages= 339-47 |year= 1989 |pmid= 2469635 |doi= }}
*{{cite journal | author=Ku NO, Omary MB |title=Identification of the major physiologic phosphorylation site of human keratin 18: potential kinases and a role in filament reorganization. |journal=J. Cell Biol. |volume=127 |issue= 1 |pages= 161-71 |year= 1994 |pmid= 7523419 |doi= }}
*{{cite journal | author=Liao J, Lowthert LA, Ghori N, Omary MB |title=The 70-kDa heat shock proteins associate with glandular intermediate filaments in an ATP-dependent manner. |journal=J. Biol. Chem. |volume=270 |issue= 2 |pages= 915-22 |year= 1995 |pmid= 7529764 |doi= }}
*{{cite journal | author=Yoon SJ, LeBlanc-Straceski J, Ward D, ''et al.'' |title=Organization of the human keratin type II gene cluster at 12q13. |journal=Genomics |volume=24 |issue= 3 |pages= 502-8 |year= 1995 |pmid= 7536183 |doi= 10.1006/geno.1994.1659 }}
*{{cite journal | author=Ku NO, Omary MB |title=Identification and mutational analysis of the glycosylation sites of human keratin 18. |journal=J. Biol. Chem. |volume=270 |issue= 20 |pages= 11820-7 |year= 1995 |pmid= 7538124 |doi= }}
*{{cite journal | author=Neumaier M, Gerhard M, Wagener C |title=Diagnosis of micrometastases by the amplification of tissue-specific genes. |journal=Gene |volume=159 |issue= 1 |pages= 43-7 |year= 1995 |pmid= 7541767 |doi= }}
*{{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=Liao J, Lowthert LA, Ku NO, ''et al.'' |title=Dynamics of human keratin 18 phosphorylation: polarized distribution of phosphorylated keratins in simple epithelial tissues. |journal=J. Cell Biol. |volume=131 |issue= 5 |pages= 1291-301 |year= 1996 |pmid= 8522590 |doi= }}
*{{cite journal | author=Ku NO, Wright TL, Terrault NA, ''et al.'' |title=Mutation of human keratin 18 in association with cryptogenic cirrhosis. |journal=J. Clin. Invest. |volume=99 |issue= 1 |pages= 19-23 |year= 1997 |pmid= 9011570 |doi= }}
*{{cite journal | author=Ji H, Reid GE, Moritz RL, ''et al.'' |title=A two-dimensional gel database of human colon carcinoma proteins. |journal=Electrophoresis |volume=18 |issue= 3-4 |pages= 605-13 |year= 1997 |pmid= 9150948 |doi= 10.1002/elps.1150180344 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MAP3K5... {November 14, 2007 1:58:34 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:00:44 PM 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_MAP3K5_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2clq.
| PDB = {{PDB2|2clq}}
| Name = Mitogen-activated protein kinase kinase kinase 5
| HGNCid = 6857
| Symbol = MAP3K5
| AltSymbols =; ASK1; MAPKKK5; MEKK5
| OMIM = 602448
| ECnumber =
| Homologene = 38114
| MGIid = 1346876
| GeneAtlas_image1 = PBB_GE_MAP3K5_203837_at_tn.png
| GeneAtlas_image2 = PBB_GE_MAP3K5_203836_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004709 |text = MAP kinase kinase kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008656 |text = caspase activator activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component =
| Process = {{GNF_GO|id=GO:0000165 |text = MAPKKK cascade}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006950 |text = response to stress}} {{GNF_GO|id=GO:0007257 |text = activation of JNK activity}} {{GNF_GO|id=GO:0008624 |text = induction of apoptosis by extracellular signals}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4217
| Hs_Ensembl = ENSG00000197442
| Hs_RefseqProtein = NP_005914
| Hs_RefseqmRNA = NM_005923
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 136919878
| Hs_GenLoc_end = 137155349
| Hs_Uniprot = Q99683
| Mm_EntrezGene = 26408
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_001006040
| Mm_RefseqProtein = XP_001006040
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Mitogen-activated protein kinase kinase kinase 5''', also known as '''MAP3K5''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Mitogen-activated protein kinase (MAPK) signaling cascades include MAPK or extracellular signal-regulated kinase (ERK), MAPK kinase (MKK or MEK), and MAPK kinase kinase (MAPKKK or MEKK). MAPKK kinase/MEKK phosphorylates and activates its downstream protein kinase, MAPK kinase/MEK, which in turn activates MAPK. The kinases of these signaling cascades are highly conserved, and homologs exist in yeast, Drosophila, and mammalian cells. MAPKKK5 contains 1,374 amino acids with all 11 kinase subdomains. Northern blot analysis shows that MAPKKK5 transcript is abundantly expressed in human heart and pancreas. The MAPKKK5 protein phosphorylates and activates MKK4 (aliases SERK1, MAPKK4) in vitro, and activates c-Jun N-terminal kinase (JNK)/stress-activated protein kinase (SAPK) during transient expression in COS and 293 cells; MAPKKK5 does not activate MAPK/ERK.<ref>{{cite web | title = Entrez Gene: MAP3K5 mitogen-activated protein kinase kinase kinase 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4217| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nagai H, Noguchi T, Takeda K, Ichijo H |title=Pathophysiological roles of ASK1-MAP kinase signaling pathways. |journal=J. Biochem. Mol. Biol. |volume=40 |issue= 1 |pages= 1-6 |year= 2007 |pmid= 17244475 |doi= }}
*{{cite journal | author=Wang XS, Diener K, Jannuzzi D, ''et al.'' |title=Molecular cloning and characterization of a novel protein kinase with a catalytic domain homologous to mitogen-activated protein kinase kinase kinase. |journal=J. Biol. Chem. |volume=271 |issue= 49 |pages= 31607-11 |year= 1997 |pmid= 8940179 |doi= }}
*{{cite journal | author=Ichijo H, Nishida E, Irie K, ''et al.'' |title=Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways. |journal=Science |volume=275 |issue= 5296 |pages= 90-4 |year= 1997 |pmid= 8974401 |doi= }}
*{{cite journal | author=Rampoldi L, Zimbello R, Bortoluzzi S, ''et al.'' |title=Chromosomal localization of four MAPK signaling cascade genes: MEK1, MEK3, MEK4 and MEKK5. |journal=Cytogenet. Cell Genet. |volume=78 |issue= 3-4 |pages= 301-3 |year= 1998 |pmid= 9465908 |doi= }}
*{{cite journal | author=Saitoh M, Nishitoh H, Fujii M, ''et al.'' |title=Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. |journal=EMBO J. |volume=17 |issue= 9 |pages= 2596-606 |year= 1998 |pmid= 9564042 |doi= 10.1093/emboj/17.9.2596 }}
*{{cite journal | author=Gotoh Y, Cooper JA |title=Reactive oxygen species- and dimerization-induced activation of apoptosis signal-regulating kinase 1 in tumor necrosis factor-alpha signal transduction. |journal=J. Biol. Chem. |volume=273 |issue= 28 |pages= 17477-82 |year= 1998 |pmid= 9651337 |doi= }}
*{{cite journal | author=Chang HY, Nishitoh H, Yang X, ''et al.'' |title=Activation of apoptosis signal-regulating kinase 1 (ASK1) by the adapter protein Daxx. |journal=Science |volume=281 |issue= 5384 |pages= 1860-3 |year= 1998 |pmid= 9743501 |doi= }}
*{{cite journal | author=Nishitoh H, Saitoh M, Mochida Y, ''et al.'' |title=ASK1 is essential for JNK/SAPK activation by TRAF2. |journal=Mol. Cell |volume=2 |issue= 3 |pages= 389-95 |year= 1998 |pmid= 9774977 |doi= }}
*{{cite journal | author=Wang XS, Diener K, Tan TH, Yao Z |title=MAPKKK6, a novel mitogen-activated protein kinase kinase kinase, that associates with MAPKKK5. |journal=Biochem. Biophys. Res. Commun. |volume=253 |issue= 1 |pages= 33-7 |year= 1999 |pmid= 9875215 |doi= 10.1006/bbrc.1998.9749 }}
*{{cite journal | author=Zhang L, Chen J, Fu H |title=Suppression of apoptosis signal-regulating kinase 1-induced cell death by 14-3-3 proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 15 |pages= 8511-5 |year= 1999 |pmid= 10411906 |doi= }}
*{{cite journal | author=Hoeflich KP, Yeh WC, Yao Z, ''et al.'' |title=Mediation of TNF receptor-associated factor effector functions by apoptosis signal-regulating kinase-1 (ASK1). |journal=Oncogene |volume=18 |issue= 42 |pages= 5814-20 |year= 1999 |pmid= 10523862 |doi= 10.1038/sj.onc.1202975 }}
*{{cite journal | author=Takeda K, Hatai T, Hamazaki TS, ''et al.'' |title=Apoptosis signal-regulating kinase 1 (ASK1) induces neuronal differentiation and survival of PC12 cells. |journal=J. Biol. Chem. |volume=275 |issue= 13 |pages= 9805-13 |year= 2000 |pmid= 10734135 |doi= }}
*{{cite journal | author=Mochida Y, Takeda K, Saitoh M, ''et al.'' |title=ASK1 inhibits interleukin-1-induced NF-kappa B activity through disruption of TRAF6-TAK1 interaction. |journal=J. Biol. Chem. |volume=275 |issue= 42 |pages= 32747-52 |year= 2000 |pmid= 10921914 |doi= 10.1074/jbc.M003042200 }}
*{{cite journal | author=Charette SJ, Lavoie JN, Lambert H, Landry J |title=Inhibition of Daxx-mediated apoptosis by heat shock protein 27. |journal=Mol. Cell. Biol. |volume=20 |issue= 20 |pages= 7602-12 |year= 2000 |pmid= 11003656 |doi= }}
*{{cite journal | author=McDonald PH, Chow CW, Miller WE, ''et al.'' |title=Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3. |journal=Science |volume=290 |issue= 5496 |pages= 1574-7 |year= 2000 |pmid= 11090355 |doi= }}
*{{cite journal | author=Ko YG, Kim EY, Kim T, ''et al.'' |title=Glutamine-dependent antiapoptotic interaction of human glutaminyl-tRNA synthetase with apoptosis signal-regulating kinase 1. |journal=J. Biol. Chem. |volume=276 |issue= 8 |pages= 6030-6 |year= 2001 |pmid= 11096076 |doi= 10.1074/jbc.M006189200 }}
*{{cite journal | author=Kim AH, Khursigara G, Sun X, ''et al.'' |title=Akt phosphorylates and negatively regulates apoptosis signal-regulating kinase 1. |journal=Mol. Cell. Biol. |volume=21 |issue= 3 |pages= 893-901 |year= 2001 |pmid= 11154276 |doi= 10.1128/MCB.21.3.893-901.2001 }}
*{{cite journal | author=Cho SG, Lee YH, Park HS, ''et al.'' |title=Glutathione S-transferase mu modulates the stress-activated signals by suppressing apoptosis signal-regulating kinase 1. |journal=J. Biol. Chem. |volume=276 |issue= 16 |pages= 12749-55 |year= 2001 |pmid= 11278289 |doi= 10.1074/jbc.M005561200 }}
*{{cite journal | author=Geleziunas R, Xu W, Takeda K, ''et al.'' |title=HIV-1 Nef inhibits ASK1-dependent death signalling providing a potential mechanism for protecting the infected host cell. |journal=Nature |volume=410 |issue= 6830 |pages= 834-8 |year= 2001 |pmid= 11298454 |doi= 10.1038/35071111 }}
*{{cite journal | author=Xu XN, Screaton G |title=HIV-1 Nef: negative effector of Fas? |journal=Nat. Immunol. |volume=2 |issue= 5 |pages= 384-5 |year= 2001 |pmid= 11323689 |doi= 10.1038/87682 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MYOD1... {November 14, 2007 2:00:44 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:01:42 PM 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_MYOD1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1mdy.
| PDB = {{PDB2|1mdy}}
| Name = Myogenic differentiation 1
| HGNCid = 7611
| Symbol = MYOD1
| AltSymbols =; PUM; MYF3; MYOD
| OMIM = 159970
| ECnumber =
| Homologene = 7857
| MGIid = 97275
| GeneAtlas_image1 = PBB_GE_MYOD1_206657_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003705 |text = RNA polymerase II transcription factor activity, enhancer binding}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006357 |text = regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007518 |text = myoblast cell fate determination}} {{GNF_GO|id=GO:0007519 |text = striated muscle development}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0045445 |text = myoblast differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4654
| Hs_Ensembl = ENSG00000129152
| Hs_RefseqProtein = NP_002469
| Hs_RefseqmRNA = NM_002478
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 17697686
| Hs_GenLoc_end = 17700251
| Hs_Uniprot = P15172
| Mm_EntrezGene = 17927
| Mm_Ensembl = ENSMUSG00000009471
| Mm_RefseqmRNA = NM_010866
| Mm_RefseqProtein = NP_034996
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 46244516
| Mm_GenLoc_end = 46247134
| Mm_Uniprot = Q8C6B1
}}
}}
'''Myogenic differentiation 1''', also known as '''MYOD1''', is a human [[gene]].
<!-- 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 nuclear protein that belongs to the basic helix-loop-helix family of transcription factors and the myogenic factors subfamily. It regulates muscle cell differentiation by inducing cell cycle arrest, a prerequisite for myogenic initiation. The protein is also involved in muscle regeneration. It activates its own transcription which may stabilize commitment to myogenesis.<ref>{{cite web | title = Entrez Gene: MYOD1 myogenic differentiation 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4654| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Weintraub H, Davis R, Tapscott S, ''et al.'' |title=The myoD gene family: nodal point during specification of the muscle cell lineage. |journal=Science |volume=251 |issue= 4995 |pages= 761-6 |year= 1991 |pmid= 1846704 |doi= }}
*{{cite journal | author=Tapscott SJ, Weintraub H |title=MyoD and the regulation of myogenesis by helix-loop-helix proteins. |journal=J. Clin. Invest. |volume=87 |issue= 4 |pages= 1133-8 |year= 1991 |pmid= 1849142 |doi= }}
*{{cite journal | author=Olson EN |title=MyoD family: a paradigm for development? |journal=Genes Dev. |volume=4 |issue= 9 |pages= 1454-61 |year= 1991 |pmid= 2253873 |doi= }}
*{{cite journal | author=Goldman PS, Tran VK, Goodman RH |title=The multifunctional role of the co-activator CBP in transcriptional regulation. |journal=Recent Prog. Horm. Res. |volume=52 |issue= |pages= 103-19; discussion 119-20 |year= 1997 |pmid= 9238849 |doi= }}
*{{cite journal | author=Puri PL, Sartorelli V |title=Regulation of muscle regulatory factors by DNA-binding, interacting proteins, and post-transcriptional modifications. |journal=J. Cell. Physiol. |volume=185 |issue= 2 |pages= 155-73 |year= 2000 |pmid= 11025438 |doi= 10.1002/1097-4652(200011)185:2<155::AID-JCP1>3.0.CO;2-Z }}
*{{cite journal | author=McKinsey TA, Zhang CL, Olson EN |title=Control of muscle development by dueling HATs and HDACs. |journal=Curr. Opin. Genet. Dev. |volume=11 |issue= 5 |pages= 497-504 |year= 2001 |pmid= 11532390 |doi= }}
*{{cite journal | author=Berkes CA, Tapscott SJ |title=MyoD and the transcriptional control of myogenesis. |journal=Semin. Cell Dev. Biol. |volume=16 |issue= 4-5 |pages= 585-95 |year= 2006 |pmid= 16099183 |doi= 10.1016/j.semcdb.2005.07.006 }}
*{{cite journal | author=Bengal E, Ransone L, Scharfmann R, ''et al.'' |title=Functional antagonism between c-Jun and MyoD proteins: a direct physical association. |journal=Cell |volume=68 |issue= 3 |pages= 507-19 |year= 1992 |pmid= 1310896 |doi= }}
*{{cite journal | author=Walsh K, Gualberto A |title=MyoD binds to the guanine tetrad nucleic acid structure. |journal=J. Biol. Chem. |volume=267 |issue= 19 |pages= 13714-8 |year= 1992 |pmid= 1320026 |doi= }}
*{{cite journal | author=Li L, Zhou J, James G, ''et al.'' |title=FGF inactivates myogenic helix-loop-helix proteins through phosphorylation of a conserved protein kinase C site in their DNA-binding domains. |journal=Cell |volume=71 |issue= 7 |pages= 1181-94 |year= 1993 |pmid= 1335366 |doi= }}
*{{cite journal | author=Shaknovich R, Shue G, Kohtz DS |title=Conformational activation of a basic helix-loop-helix protein (MyoD1) by the C-terminal region of murine HSP90 (HSP84). |journal=Mol. Cell. Biol. |volume=12 |issue= 11 |pages= 5059-68 |year= 1992 |pmid= 1406681 |doi= }}
*{{cite journal | author=Lassar AB, Davis RL, Wright WE, ''et al.'' |title=Functional activity of myogenic HLH proteins requires hetero-oligomerization with E12/E47-like proteins in vivo. |journal=Cell |volume=66 |issue= 2 |pages= 305-15 |year= 1991 |pmid= 1649701 |doi= }}
*{{cite journal | author=Pearson-White SH |title=Human MyoD: cDNA and deduced amino acid sequence. |journal=Nucleic Acids Res. |volume=19 |issue= 5 |pages= 1148 |year= 1991 |pmid= 1850513 |doi= }}
*{{cite journal | author=Gessler M, Hameister H, Henry I, ''et al.'' |title=The human MyoD1 (MYF3) gene maps on the short arm of chromosome 11 but is not associated with the WAGR locus or the region for the Beckwith-Wiedemann syndrome. |journal=Hum. Genet. |volume=86 |issue= 2 |pages= 135-8 |year= 1991 |pmid= 2176177 |doi= }}
*{{cite journal | author=Scrable HJ, Johnson DK, Rinchik EM, Cavenee WK |title=Rhabdomyosarcoma-associated locus and MYOD1 are syntenic but separate loci on the short arm of human chromosome 11. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 6 |pages= 2182-6 |year= 1990 |pmid= 2315312 |doi= }}
*{{cite journal | author=Lassar AB, Buskin JN, Lockshon D, ''et al.'' |title=MyoD is a sequence-specific DNA binding protein requiring a region of myc homology to bind to the muscle creatine kinase enhancer. |journal=Cell |volume=58 |issue= 5 |pages= 823-31 |year= 1989 |pmid= 2550138 |doi= }}
*{{cite journal | author=Braun T, Bober E, Buschhausen-Denker G, ''et al.'' |title=Differential expression of myogenic determination genes in muscle cells: possible autoactivation by the Myf gene products. |journal=EMBO J. |volume=8 |issue= 12 |pages= 3617-25 |year= 1990 |pmid= 2583111 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NPY... {November 14, 2007 2:01:42 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:02:08 PM 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_NPY_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1f8p.
| PDB = {{PDB2|1f8p}}, {{PDB2|1fvn}}, {{PDB2|1icy}}, {{PDB2|1ron}}
| Name = Neuropeptide Y
| HGNCid = 7955
| Symbol = NPY
| AltSymbols =; PYY4
| OMIM = 162640
| ECnumber =
| Homologene = 697
| MGIid = 97374
| GeneAtlas_image1 = PBB_GE_NPY_206001_at_tn.png
| Function = {{GNF_GO|id=GO:0001664 |text = G-protein-coupled receptor binding}} {{GNF_GO|id=GO:0004930 |text = G-protein coupled receptor activity}} {{GNF_GO|id=GO:0005184 |text = neuropeptide hormone activity}} {{GNF_GO|id=GO:0005246 |text = calcium channel regulator activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005623 |text = cell}}
| Process = {{GNF_GO|id=GO:0006816 |text = calcium ion transport}} {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0007187 |text = G-protein signaling, coupled to cyclic nucleotide second messenger}} {{GNF_GO|id=GO:0007218 |text = neuropeptide signaling pathway}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007586 |text = digestion}} {{GNF_GO|id=GO:0008217 |text = blood pressure regulation}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008343 |text = adult feeding behavior}} {{GNF_GO|id=GO:0032100 |text = positive regulation of appetite}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4852
| Hs_Ensembl = ENSG00000122585
| Hs_RefseqProtein = NP_000896
| Hs_RefseqmRNA = NM_000905
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 24290332
| Hs_GenLoc_end = 24298002
| Hs_Uniprot = P01303
| Mm_EntrezGene = 109648
| Mm_Ensembl = ENSMUSG00000029819
| Mm_RefseqmRNA = NM_023456
| Mm_RefseqProtein = NP_075945
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 49753184
| Mm_GenLoc_end = 49758913
| Mm_Uniprot = P57774
}}
}}
'''Neuropeptide Y''', also known as '''NPY''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wan CP, Lau BH |title=Neuropeptide Y receptor subtypes. |journal=Life Sci. |volume=56 |issue= 13 |pages= 1055-64 |year= 1997 |pmid= 9001438 |doi= }}
*{{cite journal | author=Parker E, Van Heek M, Stamford A |title=Neuropeptide Y receptors as targets for anti-obesity drug development: perspective and current status. |journal=Eur. J. Pharmacol. |volume=440 |issue= 2-3 |pages= 173-87 |year= 2002 |pmid= 12007534 |doi= }}
*{{cite journal | author=Kask A, Harro J, von Hörsten S, ''et al.'' |title=The neurocircuitry and receptor subtypes mediating anxiolytic-like effects of neuropeptide Y. |journal=Neuroscience and biobehavioral reviews |volume=26 |issue= 3 |pages= 259-83 |year= 2002 |pmid= 12034130 |doi= }}
*{{cite journal | author=Bettio A, Beck-Sickinger AG |title=Biophysical methods to study ligand-receptor interactions of neuropeptide Y. |journal=Biopolymers |volume=60 |issue= 6 |pages= 420-37 |year= 2002 |pmid= 12209475 |doi= 10.1002/1097-0282(2001)60:6<420::AID-BIP10183>3.0.CO;2-W }}
*{{cite journal | author=Donoso MV, Delpiano AM, Huidobro-Toro JP |title=Modulator role of neuropeptide Y in human vascular sympathetic neuroeffector junctions. |journal=EXS |volume= |issue= 95 |pages= 65-76 |year= 2006 |pmid= 16382997 |doi= }}
*{{cite journal | author=Westfall TC |title=Neuropeptide Y and sympathetic control of vascular tone in hypertension. |journal=EXS |volume= |issue= 95 |pages= 89-103 |year= 2006 |pmid= 16382999 |doi= }}
*{{cite journal | author=Edvinsson L |title=Neuropeptide Y and the cerebral circulation. |journal=EXS |volume= |issue= 95 |pages= 105-12 |year= 2006 |pmid= 16383000 |doi= }}
*{{cite journal | author=Feuerstein GZ, Lee EW |title=Neuropeptide Y and the heart: implication for myocardial infarction and heart failure. |journal=EXS |volume= |issue= 95 |pages= 113-22 |year= 2006 |pmid= 16383001 |doi= }}
*{{cite journal | author=Dutton MA, Lee EW, Zukowska Z |title=NPY and extreme stress: lessons learned from posttraumatic stress disorder. |journal=EXS |volume= |issue= 95 |pages= 213-22 |year= 2006 |pmid= 16383009 |doi= }}
*{{cite journal | author=Colton CA, Vitek MP |title=NPY and chronic neurodegenerative disease. |journal=EXS |volume= |issue= 95 |pages= 223-44 |year= 2006 |pmid= 16383010 |doi= }}
*{{cite journal | author=Ruscica M, Dozio E, Motta M, Magni P |title=Modulatory actions of neuropeptide Y on prostate cancer growth: role of MAP kinase/ERK 1/2 activation. |journal=Adv. Exp. Med. Biol. |volume=604 |issue= |pages= 96-100 |year= 2007 |pmid= 17695723 |doi= }}
*{{cite journal | author=Herzog H, Hort YJ, Ball HJ, ''et al.'' |title=Cloned human neuropeptide Y receptor couples to two different second messenger systems. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 13 |pages= 5794-8 |year= 1992 |pmid= 1321422 |doi= }}
*{{cite journal | author=Darbon H, Bernassau JM, Deleuze C, ''et al.'' |title=Solution conformation of human neuropeptide Y by 1H nuclear magnetic resonance and restrained molecular dynamics. |journal=Eur. J. Biochem. |volume=209 |issue= 2 |pages= 765-71 |year= 1992 |pmid= 1425680 |doi= }}
*{{cite journal | author=Minth CD, Andrews PC, Dixon JE |title=Characterization, sequence, and expression of the cloned human neuropeptide Y gene. |journal=J. Biol. Chem. |volume=261 |issue= 26 |pages= 11974-9 |year= 1986 |pmid= 2427515 |doi= }}
*{{cite journal | author=Terenghi G, Polak JM, Hamid Q, ''et al.'' |title=Localization of neuropeptide Y mRNA in neurons of human cerebral cortex by means of in situ hybridization with a complementary RNA probe. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 20 |pages= 7315-8 |year= 1987 |pmid= 2444979 |doi= }}
*{{cite journal | author=Takeuchi T, Gumucio DL, Yamada T, ''et al.'' |title=Genes encoding pancreatic polypeptide and neuropeptide Y are on human chromosomes 17 and 7. |journal=J. Clin. Invest. |volume=77 |issue= 3 |pages= 1038-41 |year= 1986 |pmid= 3753985 |doi= }}
*{{cite journal | author=Allen JM, Polak JM, Bloom SR |title=Presence of the predicted C-flanking peptide of neuropeptide Y (CPON) in tissue extracts. |journal=Neuropeptides |volume=6 |issue= 2 |pages= 95-100 |year= 1985 |pmid= 3839058 |doi= }}
*{{cite journal | author=Minth CD, Bloom SR, Polak JM, Dixon JE |title=Cloning, characterization, and DNA sequence of a human cDNA encoding neuropeptide tyrosine. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=81 |issue= 14 |pages= 4577-81 |year= 1984 |pmid= 6589611 |doi= }}
*{{cite journal | author=Rose PM, Fernandes P, Lynch JS, ''et al.'' |title=Cloning and functional expression of a cDNA encoding a human type 2 neuropeptide Y receptor. |journal=J. Biol. Chem. |volume=270 |issue= 39 |pages= 22661-4 |year= 1995 |pmid= 7559383 |doi= }}
*{{cite journal | author=Baker E, Hort YJ, Ball H, ''et al.'' |title=Assignment of the human neuropeptide Y gene to chromosome 7p15.1 by nonisotopic in situ hybridization. |journal=Genomics |volume=26 |issue= 1 |pages= 163-4 |year= 1995 |pmid= 7782078 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on OPRM1... {November 14, 2007 2:02:08 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:02:45 PM 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 = Opioid receptor, mu 1
| HGNCid = 8156
| Symbol = OPRM1
| AltSymbols =; MOR1; KIAA0403; OPRM
| OMIM = 600018
| ECnumber =
| Homologene = 37368
| MGIid = 97441
| GeneAtlas_image1 = PBB_GE_OPRM1_211359_s_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:0004988 |text = mu-opioid receptor activity}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to 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:0007187 |text = G-protein signaling, coupled to cyclic nucleotide second messenger}} {{GNF_GO|id=GO:0007600 |text = sensory perception}} {{GNF_GO|id=GO:0007610 |text = behavior}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4988
| Hs_Ensembl = ENSG00000112038
| Hs_RefseqProtein = NP_000905
| Hs_RefseqmRNA = NM_000914
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 154402136
| Hs_GenLoc_end = 154609693
| Hs_Uniprot = P35372
| Mm_EntrezGene = 18390
| Mm_Ensembl = ENSMUSG00000000766
| Mm_RefseqmRNA = XM_001052051
| Mm_RefseqProtein = XP_001052051
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 3332431
| Mm_GenLoc_end = 3588035
| Mm_Uniprot = Q8CH75
}}
}}
'''Opioid receptor, mu 1''', also known as '''OPRM1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Uhl GR, Sora I, Wang Z |title=The mu opiate receptor as a candidate gene for pain: polymorphisms, variations in expression, nociception, and opiate responses. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 14 |pages= 7752-5 |year= 1999 |pmid= 10393893 |doi= }}
*{{cite journal | author=Christie MJ, Connor M, Vaughan CW, ''et al.'' |title=Cellular actions of opioids and other analgesics: implications for synergism in pain relief. |journal=Clin. Exp. Pharmacol. Physiol. |volume=27 |issue= 7 |pages= 520-3 |year= 2000 |pmid= 10874510 |doi= }}
*{{cite journal | author=Maneckjee R, Minna JD |title=Opioid and nicotine receptors affect growth regulation of human lung cancer cell lines. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 9 |pages= 3294-8 |year= 1990 |pmid= 2159143 |doi= }}
*{{cite journal | author=Chuang TK, Killam KF, Chuang LF, ''et al.'' |title=Mu opioid receptor gene expression in immune cells. |journal=Biochem. Biophys. Res. Commun. |volume=216 |issue= 3 |pages= 922-30 |year= 1995 |pmid= 7488213 |doi= 10.1006/bbrc.1995.2709 }}
*{{cite journal | author=Mestek A, Hurley JH, Bye LS, ''et al.'' |title=The human mu opioid receptor: modulation of functional desensitization by calcium/calmodulin-dependent protein kinase and protein kinase C. |journal=J. Neurosci. |volume=15 |issue= 3 Pt 2 |pages= 2396-406 |year= 1995 |pmid= 7891175 |doi= }}
*{{cite journal | author=Wang JB, Johnson PS, Persico AM, ''et al.'' |title=Human mu opiate receptor. cDNA and genomic clones, pharmacologic characterization and chromosomal assignment. |journal=FEBS Lett. |volume=338 |issue= 2 |pages= 217-22 |year= 1994 |pmid= 7905839 |doi= }}
*{{cite journal | author=Bare LA, Mansson E, Yang D |title=Expression of two variants of the human mu opioid receptor mRNA in SK-N-SH cells and human brain. |journal=FEBS Lett. |volume=354 |issue= 2 |pages= 213-6 |year= 1994 |pmid= 7957926 |doi= }}
*{{cite journal | author=Georgoussi Z, Carr C, Milligan G |title=Direct measurements of in situ interactions of rat brain opioid receptors with the guanine nucleotide-binding protein Go. |journal=Mol. Pharmacol. |volume=44 |issue= 1 |pages= 62-9 |year= 1993 |pmid= 8393523 |doi= }}
*{{cite journal | author=Massotte D, Baroche L, Simonin F, ''et al.'' |title=Characterization of delta, kappa, and mu human opioid receptors overexpressed in baculovirus-infected insect cells. |journal=J. Biol. Chem. |volume=272 |issue= 32 |pages= 19987-92 |year= 1997 |pmid= 9242668 |doi= }}
*{{cite journal | author=Pak Y, O'Dowd BF, George SR |title=Agonist-induced desensitization of the mu opioid receptor is determined by threonine 394 preceded by acidic amino acids in the COOH-terminal tail. |journal=J. Biol. Chem. |volume=272 |issue= 40 |pages= 24961-5 |year= 1997 |pmid= 9312100 |doi= }}
*{{cite journal | author=Koch T, Kroslak T, Mayer P, ''et al.'' |title=Site mutation in the rat mu-opioid receptor demonstrates the involvement of calcium/calmodulin-dependent protein kinase II in agonist-mediated desensitization. |journal=J. Neurochem. |volume=69 |issue= 4 |pages= 1767-70 |year= 1997 |pmid= 9326307 |doi= }}
*{{cite journal | author=Bergen AW, Kokoszka J, Peterson R, ''et al.'' |title=Mu opioid receptor gene variants: lack of association with alcohol dependence. |journal=Mol. Psychiatry |volume=2 |issue= 6 |pages= 490-4 |year= 1998 |pmid= 9399694 |doi= }}
*{{cite journal | author=Lee JW, Joshi S, Chan JS, Wong YH |title=Differential coupling of mu-, delta-, and kappa-opioid receptors to G alpha16-mediated stimulation of phospholipase C. |journal=J. Neurochem. |volume=70 |issue= 5 |pages= 2203-11 |year= 1998 |pmid= 9572309 |doi= }}
*{{cite journal | author=Bond C, LaForge KS, Tian M, ''et al.'' |title=Single-nucleotide polymorphism in the human mu opioid receptor gene alters beta-endorphin binding and activity: possible implications for opiate addiction. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 16 |pages= 9608-13 |year= 1998 |pmid= 9689128 |doi= }}
*{{cite journal | author=Peckys D, Landwehrmeyer GB |title=Expression of mu, kappa, and delta opioid receptor messenger RNA in the human CNS: a 33P in situ hybridization study. |journal=Neuroscience |volume=88 |issue= 4 |pages= 1093-135 |year= 1999 |pmid= 10336124 |doi= }}
*{{cite journal | author=Fimiani C, Arcuri E, Santoni A, ''et al.'' |title=Mu3 opiate receptor expression in lung and lung carcinoma: ligand binding and coupling to nitric oxide release. |journal=Cancer Lett. |volume=146 |issue= 1 |pages= 45-51 |year= 2000 |pmid= 10656608 |doi= }}
*{{cite journal | author=Pan YX, Xu J, Bolan E, ''et al.'' |title=Isolation and expression of a novel alternatively spliced mu opioid receptor isoform, MOR-1F. |journal=FEBS Lett. |volume=466 |issue= 2-3 |pages= 337-40 |year= 2000 |pmid= 10682855 |doi= }}
*{{cite journal | author=Sander T, Berlin W, Gscheidel N, ''et al.'' |title=Genetic variation of the human mu-opioid receptor and susceptibility to idiopathic absence epilepsy. |journal=Epilepsy Res. |volume=39 |issue= 1 |pages= 57-61 |year= 2000 |pmid= 10690754 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PAX3... {November 14, 2007 2:02:45 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:03:55 PM 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 = Paired box gene 3 (Waardenburg syndrome 1)
| HGNCid = 8617
| Symbol = PAX3
| AltSymbols =; CDHS; HUP2; MGC120381; MGC120382; MGC120383; MGC120384; MGC134778; WS1
| OMIM = 606597
| ECnumber =
| Homologene = 22494
| MGIid = 97487
| GeneAtlas_image1 = PBB_GE_PAX3_207680_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_PAX3_216059_at_tn.png
| Function = {{GNF_GO|id=GO:0003682 |text = chromatin binding}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003705 |text = RNA polymerase II transcription factor activity, enhancer binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016563 |text = transcription activator activity}} {{GNF_GO|id=GO:0016566 |text = specific transcriptional repressor activity}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0001755 |text = neural crest cell migration}} {{GNF_GO|id=GO:0001843 |text = neural tube closure}} {{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:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007367 |text = segment polarity determination}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0007517 |text = muscle development}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0048066 |text = pigmentation during development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5077
| Hs_Ensembl = ENSG00000135903
| Hs_RefseqProtein = NP_000429
| Hs_RefseqmRNA = NM_000438
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 222772851
| Hs_GenLoc_end = 222871944
| Hs_Uniprot = P23760
| Mm_EntrezGene = 18505
| Mm_Ensembl = ENSMUSG00000004872
| Mm_RefseqmRNA = XM_986648
| Mm_RefseqProtein = XP_991742
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 77985839
| Mm_GenLoc_end = 78080283
| Mm_Uniprot = Q3UGH9
}}
}}
'''Paired box gene 3 (Waardenburg syndrome 1)''', also known as '''PAX3''', is a human [[gene]].
<!-- 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 paired box (PAX) family of transcription factors. Members of the PAX family typically contain a paired box domain and a paired-type homeodomain. These genes play critical roles during fetal development. Mutations in paired box gene 3 are associated with Waardenburg syndrome, craniofacial-deafness-hand syndrome, and alveolar rhabdomyosarcoma. The translocation t(2;13)(q35;q14), which represents a fusion between PAX3 and the forkhead gene, is a frequent finding in alveolar rhabdomyosarcoma. Alternative splicing results in transcripts encoding isoforms with different C-termini.<ref>{{cite web | title = Entrez Gene: PAX3 paired box gene 3 (Waardenburg syndrome 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5077| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Moase CE, Trasler DG |title=Splotch locus mouse mutants: models for neural tube defects and Waardenburg syndrome type I in humans. |journal=J. Med. Genet. |volume=29 |issue= 3 |pages= 145-51 |year= 1992 |pmid= 1552554 |doi= }}
*{{cite journal | author=Baldwin CT, Hoth CF, Macina RA, Milunsky A |title=Mutations in PAX3 that cause Waardenburg syndrome type I: ten new mutations and review of the literature. |journal=Am. J. Med. Genet. |volume=58 |issue= 2 |pages= 115-22 |year= 1996 |pmid= 8533800 |doi= 10.1002/ajmg.1320580205 }}
*{{cite journal | author=Blake J, Ziman MR |title=Aberrant PAX3 and PAX7 expression. A link to the metastatic potential of embryonal rhabdomyosarcoma and cutaneous malignant melanoma? |journal=Histol. Histopathol. |volume=18 |issue= 2 |pages= 529-39 |year= 2003 |pmid= 12647804 |doi= }}
*{{cite journal | author=Reddi KK |title=Human granulocyte ribonuclease. |journal=Biochem. Biophys. Res. Commun. |volume=68 |issue= 4 |pages= 1119-25 |year= 1976 |pmid= 5077 |doi= }}
*{{cite journal | author=Morell R, Friedman TB, Moeljopawiro S, ''et al.'' |title=A frameshift mutation in the HuP2 paired domain of the probable human homolog of murine Pax-3 is responsible for Waardenburg syndrome type 1 in an Indonesian family. |journal=Hum. Mol. Genet. |volume=1 |issue= 4 |pages= 243-7 |year= 1993 |pmid= 1303193 |doi= }}
*{{cite journal | author=Carezani-Gavin M, Clarren SK, Steege T |title=Waardenburg syndrome associated with meningomyelocele. |journal=Am. J. Med. Genet. |volume=42 |issue= 1 |pages= 135-6 |year= 1993 |pmid= 1308353 |doi= 10.1002/ajmg.1320420127 }}
*{{cite journal | author=Tassabehji M, Read AP, Newton VE, ''et al.'' |title=Waardenburg's syndrome patients have mutations in the human homologue of the Pax-3 paired box gene. |journal=Nature |volume=355 |issue= 6361 |pages= 635-6 |year= 1992 |pmid= 1347148 |doi= 10.1038/355635a0 }}
*{{cite journal | author=Baldwin CT, Hoth CF, Amos JA, ''et al.'' |title=An exonic mutation in the HuP2 paired domain gene causes Waardenburg's syndrome. |journal=Nature |volume=355 |issue= 6361 |pages= 637-8 |year= 1992 |pmid= 1347149 |doi= 10.1038/355637a0 }}
*{{cite journal | author=Farrer LA, Grundfast KM, Amos J, ''et al.'' |title=Waardenburg syndrome (WS) type I is caused by defects at multiple loci, one of which is near ALPP on chromosome 2: first report of the WS consortium. |journal=Am. J. Hum. Genet. |volume=50 |issue= 5 |pages= 902-13 |year= 1992 |pmid= 1349198 |doi= }}
*{{cite journal | author=Sheffer R, Zlotogora J |title=Autosomal dominant inheritance of Klein-Waardenburg syndrome. |journal=Am. J. Med. Genet. |volume=42 |issue= 3 |pages= 320-2 |year= 1992 |pmid= 1536170 |doi= 10.1002/ajmg.1320420312 }}
*{{cite journal | author=Burri M, Tromvoukis Y, Bopp D, ''et al.'' |title=Conservation of the paired domain in metazoans and its structure in three isolated human genes. |journal=EMBO J. |volume=8 |issue= 4 |pages= 1183-90 |year= 1989 |pmid= 2501086 |doi= }}
*{{cite journal | author=Newton VE |title=Waardenburg's syndrome: a comparison of biometric indices used to diagnose lateral displacement of the inner canthi. |journal=Scandinavian audiology |volume=18 |issue= 4 |pages= 221-3 |year= 1990 |pmid= 2609099 |doi= }}
*{{cite journal | author=Newton CR, Graham A, Heptinstall LE, ''et al.'' |title=Analysis of any point mutation in DNA. The amplification refractory mutation system (ARMS). |journal=Nucleic Acids Res. |volume=17 |issue= 7 |pages= 2503-16 |year= 1989 |pmid= 2785681 |doi= }}
*{{cite journal | author=Sommer A, Young-Wee T, Frye T |title=Previously undescribed syndrome of craniofacial, hand anomalies, and sensorineural deafness. |journal=Am. J. Med. Genet. |volume=15 |issue= 1 |pages= 71-7 |year= 1983 |pmid= 6859126 |doi= 10.1002/ajmg.1320150109 }}
*{{cite journal | author=Goodman RM, Lewithal I, Solomon A, Klein D |title=Upper limb involvement in the Klein-Waardenburg syndrome. |journal=Am. J. Med. Genet. |volume=11 |issue= 4 |pages= 425-33 |year= 1982 |pmid= 7091186 |doi= 10.1002/ajmg.1320110407 }}
*{{cite journal | author=Tsukamoto K, Nakamura Y, Niikawa N |title=Isolation of two isoforms of the PAX3 gene transcripts and their tissue-specific alternative expression in human adult tissues. |journal=Hum. Genet. |volume=93 |issue= 3 |pages= 270-4 |year= 1994 |pmid= 7545913 |doi= }}
*{{cite journal | author=Zlotogora J, Lerer I, Bar-David S, ''et al.'' |title=Homozygosity for Waardenburg syndrome. |journal=Am. J. Hum. Genet. |volume=56 |issue= 5 |pages= 1173-8 |year= 1995 |pmid= 7726174 |doi= }}
*{{cite journal | author=Macina RA, Barr FG, Galili N, Riethman HC |title=Genomic organization of the human PAX3 gene: DNA sequence analysis of the region disrupted in alveolar rhabdomyosarcoma. |journal=Genomics |volume=26 |issue= 1 |pages= 1-8 |year= 1995 |pmid= 7782066 |doi= }}
*{{cite journal | author=Lalwani AK, Brister JR, Fex J, ''et al.'' |title=Further elucidation of the genomic structure of PAX3, and identification of two different point mutations within the PAX3 homeobox that cause Waardenburg syndrome type 1 in two families. |journal=Am. J. Hum. Genet. |volume=56 |issue= 1 |pages= 75-83 |year= 1995 |pmid= 7825605 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PDPK1... {November 14, 2007 2:03:55 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:04:39 PM 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_PDPK1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1h1w.
| PDB = {{PDB2|1h1w}}, {{PDB2|1oky}}, {{PDB2|1okz}}, {{PDB2|1uu3}}, {{PDB2|1uu7}}, {{PDB2|1uu8}}, {{PDB2|1uu9}}, {{PDB2|1uvr}}, {{PDB2|1w1d}}, {{PDB2|1w1g}}, {{PDB2|1w1h}}, {{PDB2|1z5m}}, {{PDB2|2biy}}
| Name = 3-phosphoinositide dependent protein kinase-1
| HGNCid = 8816
| Symbol = PDPK1
| AltSymbols =; PDK1; MGC20087; MGC35290; PRO0461; PkB-like; PkB-like 1
| OMIM = 605213
| ECnumber =
| Homologene = 37643
| MGIid = 1338068
| GeneAtlas_image1 = PBB_GE_PDPK1_32029_at_tn.png
| GeneAtlas_image2 = PBB_GE_PDPK1_204524_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:0004676 |text = 3-phosphoinositide-dependent protein kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016023 |text = cytoplasmic membrane-bound vesicle}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006972 |text = hyperosmotic response}} {{GNF_GO|id=GO:0008286 |text = insulin receptor signaling pathway}} {{GNF_GO|id=GO:0030036 |text = actin cytoskeleton organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5170
| Hs_Ensembl = ENSG00000140992
| Hs_RefseqProtein = XP_001130789
| Hs_RefseqmRNA = XM_001130789
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 2527971
| Hs_GenLoc_end = 2593189
| Hs_Uniprot = O15530
| Mm_EntrezGene = 18607
| Mm_Ensembl = ENSMUSG00000024122
| Mm_RefseqmRNA = NM_001080773
| Mm_RefseqProtein = NP_001074242
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 23803292
| Mm_GenLoc_end = 23869207
| Mm_Uniprot = Q810Z4
}}
}}
'''3-phosphoinositide dependent protein kinase-1''', also known as '''PDPK1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Vanhaesebroeck B, Alessi DR |title=The PI3K-PDK1 connection: more than just a road to PKB. |journal=Biochem. J. |volume=346 Pt 3 |issue= |pages= 561-76 |year= 2000 |pmid= 10698680 |doi= }}
*{{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=Alessi DR, James SR, Downes CP, ''et al.'' |title=Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha. |journal=Curr. Biol. |volume=7 |issue= 4 |pages= 261-9 |year= 1997 |pmid= 9094314 |doi= }}
*{{cite journal | author=Moser BA, Dennis PB, Pullen N, ''et al.'' |title=Dual requirement for a newly identified phosphorylation site in p70s6k. |journal=Mol. Cell. Biol. |volume=17 |issue= 9 |pages= 5648-55 |year= 1997 |pmid= 9271440 |doi= }}
*{{cite journal | author=Alessi DR, Deak M, Casamayor A, ''et al.'' |title=3-Phosphoinositide-dependent protein kinase-1 (PDK1): structural and functional homology with the Drosophila DSTPK61 kinase. |journal=Curr. Biol. |volume=7 |issue= 10 |pages= 776-89 |year= 1998 |pmid= 9368760 |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=Meier R, Alessi DR, Cron P, ''et al.'' |title=Mitogenic activation, phosphorylation, and nuclear translocation of protein kinase Bbeta. |journal=J. Biol. Chem. |volume=272 |issue= 48 |pages= 30491-7 |year= 1997 |pmid= 9374542 |doi= }}
*{{cite journal | author=Alessi DR, Kozlowski MT, Weng QP, ''et al.'' |title=3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro. |journal=Curr. Biol. |volume=8 |issue= 2 |pages= 69-81 |year= 1998 |pmid= 9427642 |doi= }}
*{{cite journal | author=Dalby KN, Morrice N, Caudwell FB, ''et al.'' |title=Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK. |journal=J. Biol. Chem. |volume=273 |issue= 3 |pages= 1496-505 |year= 1998 |pmid= 9430688 |doi= }}
*{{cite journal | author=Pullen N, Dennis PB, Andjelkovic M, ''et al.'' |title=Phosphorylation and activation of p70s6k by PDK1. |journal=Science |volume=279 |issue= 5351 |pages= 707-10 |year= 1998 |pmid= 9445476 |doi= }}
*{{cite journal | author=Stephens L, Anderson K, Stokoe D, ''et al.'' |title=Protein kinase B kinases that mediate phosphatidylinositol 3,4,5-trisphosphate-dependent activation of protein kinase B. |journal=Science |volume=279 |issue= 5351 |pages= 710-4 |year= 1998 |pmid= 9445477 |doi= }}
*{{cite journal | author=Walker KS, Deak M, Paterson A, ''et al.'' |title=Activation of protein kinase B beta and gamma isoforms by insulin in vivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro: comparison with protein kinase B alpha. |journal=Biochem. J. |volume=331 ( Pt 1) |issue= |pages= 299-308 |year= 1998 |pmid= 9512493 |doi= }}
*{{cite journal | author=Anderson KE, Coadwell J, Stephens LR, Hawkins PT |title=Translocation of PDK-1 to the plasma membrane is important in allowing PDK-1 to activate protein kinase B. |journal=Curr. Biol. |volume=8 |issue= 12 |pages= 684-91 |year= 1998 |pmid= 9637919 |doi= }}
*{{cite journal | author=Le Good JA, Ziegler WH, Parekh DB, ''et al.'' |title=Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1. |journal=Science |volume=281 |issue= 5385 |pages= 2042-5 |year= 1998 |pmid= 9748166 |doi= }}
*{{cite journal | author=Currie RA, Walker KS, Gray A, ''et al.'' |title=Role of phosphatidylinositol 3,4,5-trisphosphate in regulating the activity and localization of 3-phosphoinositide-dependent protein kinase-1. |journal=Biochem. J. |volume=337 ( Pt 3) |issue= |pages= 575-83 |year= 1999 |pmid= 9895304 |doi= }}
*{{cite journal | author=Kobayashi T, Cohen P |title=Activation of serum- and glucocorticoid-regulated protein kinase by agonists that activate phosphatidylinositide 3-kinase is mediated by 3-phosphoinositide-dependent protein kinase-1 (PDK1) and PDK2. |journal=Biochem. J. |volume=339 ( Pt 2) |issue= |pages= 319-28 |year= 1999 |pmid= 10191262 |doi= }}
*{{cite journal | author=Balendran A, Casamayor A, Deak M, ''et al.'' |title=PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2. |journal=Curr. Biol. |volume=9 |issue= 8 |pages= 393-404 |year= 1999 |pmid= 10226025 |doi= }}
*{{cite journal | author=Park J, Leong ML, Buse P, ''et al.'' |title=Serum and glucocorticoid-inducible kinase (SGK) is a target of the PI 3-kinase-stimulated signaling pathway. |journal=EMBO J. |volume=18 |issue= 11 |pages= 3024-33 |year= 1999 |pmid= 10357815 |doi= 10.1093/emboj/18.11.3024 }}
*{{cite journal | author=Paradis S, Ailion M, Toker A, ''et al.'' |title=A PDK1 homolog is necessary and sufficient to transduce AGE-1 PI3 kinase signals that regulate diapause in Caenorhabditis elegans. |journal=Genes Dev. |volume=13 |issue= 11 |pages= 1438-52 |year= 1999 |pmid= 10364160 |doi= }}
*{{cite journal | author=Casamayor A, Morrice NA, Alessi DR |title=Phosphorylation of Ser-241 is essential for the activity of 3-phosphoinositide-dependent protein kinase-1: identification of five sites of phosphorylation in vivo. |journal=Biochem. J. |volume=342 ( Pt 2) |issue= |pages= 287-92 |year= 1999 |pmid= 10455013 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PPP2CA... {November 14, 2007 2:04:39 PM PST}
- SEARCH REDIRECT: Control Box Found: PPP2CA {November 14, 2007 2:05:14 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 2:05:15 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 2:05:15 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 2:05:15 PM PST}
- UPDATED: Updated protein page: PPP2CA {November 14, 2007 2:05:22 PM PST}
- INFO: Beginning work on PRKAR1A... {November 14, 2007 2:05:22 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:06:15 PM 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_PRKAR1A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ne4.
| PDB = {{PDB2|1ne4}}, {{PDB2|1ne6}}, {{PDB2|1rgs}}, {{PDB2|1rl3}}, {{PDB2|1u7e}}, {{PDB2|2ezw}}
| Name = Protein kinase, cAMP-dependent, regulatory, type I, alpha (tissue specific extinguisher 1)
| HGNCid = 9388
| Symbol = PRKAR1A
| AltSymbols =; CAR; CNC; CNC1; DKFZp779L0468; MGC17251; PKR1; PRKAR1; TSE1
| OMIM = 188830
| ECnumber =
| Homologene = 37664
| MGIid = 104878
| GeneAtlas_image1 = PBB_GE_PRKAR1A_200603_at_tn.png
| GeneAtlas_image2 = PBB_GE_PRKAR1A_200604_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_PRKAR1A_200605_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008603 |text = cAMP-dependent protein kinase regulator activity}} {{GNF_GO|id=GO:0016301 |text = kinase activity}} {{GNF_GO|id=GO:0030552 |text = cAMP binding}}
| Component = {{GNF_GO|id=GO:0005952 |text = cAMP-dependent protein kinase complex}} {{GNF_GO|id=GO:0031594 |text = neuromuscular junction}}
| Process = {{GNF_GO|id=GO:0001707 |text = mesoderm formation}} {{GNF_GO|id=GO:0006357 |text = regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5573
| Hs_Ensembl = ENSG00000108946
| Hs_RefseqProtein = NP_002725
| Hs_RefseqmRNA = NM_002734
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 64019705
| Hs_GenLoc_end = 64040503
| Hs_Uniprot = P10644
| Mm_EntrezGene = 19084
| Mm_Ensembl = ENSMUSG00000020612
| Mm_RefseqmRNA = NM_021880
| Mm_RefseqProtein = NP_068680
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 109466334
| Mm_GenLoc_end = 109485746
| Mm_Uniprot = Q3UBA7
}}
}}
'''Protein kinase, cAMP-dependent, regulatory, type I, alpha (tissue specific extinguisher 1)''', also known as '''PRKAR1A''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase (AMPK), which transduces the signal through phosphorylation of different target proteins. The inactive holoenzyme of AMPK is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits of AMPK have been identified in humans. The protein encoded by this gene is one of the regulatory subunits. This protein was found to be a tissue-specific extinguisher that down-regulates the expression of seven liver genes in hepatoma x fibroblast hybrids. Functional null mutations in this gene cause Carney complex (CNC), an autosomal dominant multiple neoplasia syndrome. This gene can fuse to the RET protooncogene by gene rearrangement and form the thyroid tumor-specific chimeric oncogene known as PTC2. Three alternatively spliced transcript variants encoding the same protein have been observed.<ref>{{cite web | title = Entrez Gene: PRKAR1A protein kinase, cAMP-dependent, regulatory, type I, alpha (tissue specific extinguisher 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5573| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Stratakis CA |title=Mutations of the gene encoding the protein kinase A type I-alpha regulatory subunit (PRKAR1A) in patients with the "complex of spotty skin pigmentation, myxomas, endocrine overactivity, and schwannomas" (Carney complex). |journal=Ann. N. Y. Acad. Sci. |volume=968 |issue= |pages= 3-21 |year= 2002 |pmid= 12119264 |doi= }}
*{{cite journal | author=Bourdeau I, Stratakis CA |title=Cyclic AMP-dependent signaling aberrations in macronodular adrenal disease. |journal=Ann. N. Y. Acad. Sci. |volume=968 |issue= |pages= 240-55 |year= 2002 |pmid= 12119280 |doi= }}
*{{cite journal | author=Alto N, Carlisle Michel JJ, Dodge KL, ''et al.'' |title=Intracellular targeting of protein kinases and phosphatases. |journal=Diabetes |volume=51 Suppl 3 |issue= |pages= S385-8 |year= 2003 |pmid= 12475780 |doi= }}
*{{cite journal | author=Stergiopoulos SG, Stratakis CA |title=Human tumors associated with Carney complex and germline PRKAR1A mutations: a protein kinase A disease! |journal=FEBS Lett. |volume=546 |issue= 1 |pages= 59-64 |year= 2003 |pmid= 12829237 |doi= }}
*{{cite journal | author=Bossis I, Stratakis CA |title=Minireview: PRKAR1A: normal and abnormal functions. |journal=Endocrinology |volume=145 |issue= 12 |pages= 5452-8 |year= 2004 |pmid= 15331577 |doi= 10.1210/en.2004-0900 }}
*{{cite journal | author=Cho-Chung YS, Nesterova MV |title=Tumor reversion: protein kinase A isozyme switching. |journal=Ann. N. Y. Acad. Sci. |volume=1058 |issue= |pages= 76-86 |year= 2006 |pmid= 16394127 |doi= 10.1196/annals.1359.014 }}
*{{cite journal | author=Lytras A, Tolis G |title=Growth hormone-secreting tumors: genetic aspects and data from animal models. |journal=Neuroendocrinology |volume=83 |issue= 3-4 |pages= 166-78 |year= 2006 |pmid= 17047380 |doi= 10.1159/000095525 }}
*{{cite journal | author=Harrich D, McMillan N, Munoz L, ''et al.'' |title=Will diverse Tat interactions lead to novel antiretroviral drug targets? |journal=Current drug targets |volume=7 |issue= 12 |pages= 1595-606 |year= 2007 |pmid= 17168834 |doi= }}
*{{cite journal | author=Boshart M, Weih F, Nichols M, Schütz G |title=The tissue-specific extinguisher locus TSE1 encodes a regulatory subunit of cAMP-dependent protein kinase. |journal=Cell |volume=66 |issue= 5 |pages= 849-59 |year= 1991 |pmid= 1832337 |doi= }}
*{{cite journal | author=Jones KW, Shapero MH, Chevrette M, Fournier RE |title=Subtractive hybridization cloning of a tissue-specific extinguisher: TSE1 encodes a regulatory subunit of protein kinase A. |journal=Cell |volume=66 |issue= 5 |pages= 861-72 |year= 1991 |pmid= 1889088 |doi= }}
*{{cite journal | author=Hofmann B, Nishanian P, Baldwin RL, ''et al.'' |title=HIV inhibits the early steps of lymphocyte activation, including initiation of inositol phospholipid metabolism. |journal=J. Immunol. |volume=145 |issue= 11 |pages= 3699-705 |year= 1991 |pmid= 1978848 |doi= }}
*{{cite journal | author=Sandberg M, Skålhegg B, Jahnsen T |title=The two mRNA forms for the type I alpha regulatory subunit of cAMP-dependent protein kinase from human testis are due to the use of different polyadenylation site signals. |journal=Biochem. Biophys. Res. Commun. |volume=167 |issue= 1 |pages= 323-30 |year= 1990 |pmid= 2310396 |doi= }}
*{{cite journal | author=Lem J, Chin AC, Thayer MJ, ''et al.'' |title=Coordinate regulation of two genes encoding gluconeogenic enzymes by the trans-dominant locus Tse-1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 19 |pages= 7302-6 |year= 1988 |pmid= 2902627 |doi= }}
*{{cite journal | author=Sandberg M, Taskén K, Oyen O, ''et al.'' |title=Molecular cloning, cDNA structure and deduced amino acid sequence for a type I regulatory subunit of cAMP-dependent protein kinase from human testis. |journal=Biochem. Biophys. Res. Commun. |volume=149 |issue= 3 |pages= 939-45 |year= 1988 |pmid= 3426618 |doi= }}
*{{cite journal | author=Scambler P, Oyen O, Wainwright B, ''et al.'' |title=Exclusion of catalytic and regulatory subunits of cAMP-dependent protein kinase as candidate genes for the defect causing cystic fibrosis. |journal=Am. J. Hum. Genet. |volume=41 |issue= 5 |pages= 925-32 |year= 1987 |pmid= 3479018 |doi= }}
*{{cite journal | author=Geahlen RL, Carmichael DF, Hashimoto E, Krebs EG |title=Phosphorylation of cAMP-dependent protein kinase subunits. |journal=Adv. Enzyme Regul. |volume=20 |issue= |pages= 195-209 |year= 1982 |pmid= 6287816 |doi= }}
*{{cite journal | author=Guild BC, Strominger JL |title=HLA-A2 antigen phosphorylation in vitro by cyclic AMP-dependent protein kinase. Sites of phosphorylation and segmentation in class i major histocompatibility complex gene structure. |journal=J. Biol. Chem. |volume=259 |issue= 21 |pages= 13504-10 |year= 1984 |pmid= 6333425 |doi= }}
*{{cite journal | author=Bongarzone I, Monzini N, Borrello MG, ''et al.'' |title=Molecular characterization of a thyroid tumor-specific transforming sequence formed by the fusion of ret tyrosine kinase and the regulatory subunit RI alpha of cyclic AMP-dependent protein kinase A. |journal=Mol. Cell. Biol. |volume=13 |issue= 1 |pages= 358-66 |year= 1993 |pmid= 7678053 |doi= }}
*{{cite journal | author=Hofmann B, Nishanian P, Nguyen T, ''et al.'' |title=Human immunodeficiency virus proteins induce the inhibitory cAMP/protein kinase A pathway in normal lymphocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 14 |pages= 6676-80 |year= 1993 |pmid= 7688126 |doi= }}
*{{cite journal | author=Hofmann B, Nishanian P, Fan J, ''et al.'' |title=HIV Gag p17 protein impairs proliferation of normal lymphocytes in vitro. |journal=AIDS |volume=8 |issue= 7 |pages= 1016-7 |year= 1994 |pmid= 7946090 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PTHLH... {November 14, 2007 2:06:15 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:07:01 PM 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_PTHLH_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bzg.
| PDB = {{PDB2|1bzg}}, {{PDB2|1m5n}}
| Name = Parathyroid hormone-like hormone
| HGNCid = 9607
| Symbol = PTHLH
| AltSymbols =; PLP; HHM; MGC14611; PTHR; PTHRP
| OMIM = 168470
| ECnumber =
| Homologene = 2113
| MGIid = 97800
| GeneAtlas_image1 = PBB_GE_PTHLH_206300_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PTHLH_211756_at_tn.png
| Function = {{GNF_GO|id=GO:0005179 |text = hormone activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0002076 |text = osteoblast development}} {{GNF_GO|id=GO:0007189 |text = G-protein signaling, adenylate cyclase activating pathway}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007565 |text = female pregnancy}} {{GNF_GO|id=GO:0007595 |text = lactation}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0008544 |text = epidermis development}} {{GNF_GO|id=GO:0030855 |text = epithelial cell differentiation}} {{GNF_GO|id=GO:0043129 |text = surfactant homeostasis}} {{GNF_GO|id=GO:0046058 |text = cAMP metabolic process}} {{GNF_GO|id=GO:0048286 |text = alveolus development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5744
| Hs_Ensembl = ENSG00000087494
| Hs_RefseqProtein = NP_002811
| Hs_RefseqmRNA = NM_002820
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 28006092
| Hs_GenLoc_end = 28015124
| Hs_Uniprot = P12272
| Mm_EntrezGene = 19227
| Mm_Ensembl = ENSMUSG00000048776
| Mm_RefseqmRNA = NM_008970
| Mm_RefseqProtein = NP_032996
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 147214106
| Mm_GenLoc_end = 147220540
| Mm_Uniprot = Q540C1
}}
}}
'''Parathyroid hormone-like hormone''', also known as '''PTHLH''', is a human [[gene]].
<!-- 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 parathyroid hormone family. This hormone regulates endochondral bone development and epithelial-mesenchymal interactions during the formation of the mammary glands and teeth. This hormone is involved in lactation possibly by regulating the mobilization and transfer of calcium to the milk. The receptor of this hormone, PTHR1, is responsible for most cases of humoral hypercalcemia of malignancy. Four alternatively spliced transcript variants encoding two distinct isoforms have been observed. There is also evidence for alternative translation initiation from non-AUG (CUG and GUG) start sites, in-frame and downstream of the initiator AUG codon, to give rise to nuclear forms of this hormone.<ref>{{cite web | title = Entrez Gene: PTHLH parathyroid hormone-like hormone| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5744| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Casey ML, MacDonald PC |title=The endothelin-parathyroid hormone-related protein vasoactive peptide system in human endometrium: modulation by transforming growth factor-beta. |journal=Hum. Reprod. |volume=11 Suppl 2 |issue= |pages= 62-82 |year= 1997 |pmid= 8982748 |doi= }}
*{{cite journal | author=Lam MH, Thomas RJ, Martin TJ, ''et al.'' |title=Nuclear and nucleolar localization of parathyroid hormone-related protein. |journal=Immunol. Cell Biol. |volume=78 |issue= 4 |pages= 395-402 |year= 2000 |pmid= 10947864 |doi= }}
*{{cite journal | author=Fiaschi-Taesch NM, Stewart AF |title=Minireview: parathyroid hormone-related protein as an intracrine factor--trafficking mechanisms and functional consequences. |journal=Endocrinology |volume=144 |issue= 2 |pages= 407-11 |year= 2003 |pmid= 12538599 |doi= }}
*{{cite journal | author=Jans DA, Thomas RJ, Gillespie MT |title=Parathyroid hormone-related protein (PTHrP): a nucleocytoplasmic shuttling protein with distinct paracrine and intracrine roles. |journal=Vitam. Horm. |volume=66 |issue= |pages= 345-84 |year= 2003 |pmid= 12852260 |doi= }}
*{{cite journal | author=Maioli E, Fortino V, Pacini A |title=Parathyroid hormone-related protein in preeclampsia: a linkage between maternal and fetal failures. |journal=Biol. Reprod. |volume=71 |issue= 6 |pages= 1779-84 |year= 2005 |pmid= 15286039 |doi= 10.1095/biolreprod.104.030932 }}
*{{cite journal | author=Fenton AJ, Kemp BE, Kent GN, ''et al.'' |title=A carboxyl-terminal peptide from the parathyroid hormone-related protein inhibits bone resorption by osteoclasts. |journal=Endocrinology |volume=129 |issue= 4 |pages= 1762-8 |year= 1991 |pmid= 1915066 |doi= }}
*{{cite journal | author=Fenton AJ, Kemp BE, Hammonds RG, ''et al.'' |title=A potent inhibitor of osteoclastic bone resorption within a highly conserved pentapeptide region of parathyroid hormone-related protein; PTHrP[107-111] |journal=Endocrinology |volume=129 |issue= 6 |pages= 3424-6 |year= 1991 |pmid= 1954916 |doi= }}
*{{cite journal | author=Moniz C, Burton PB, Malik AN, ''et al.'' |title=Parathyroid hormone-related peptide in normal human fetal development. |journal=J. Mol. Endocrinol. |volume=5 |issue= 3 |pages= 259-66 |year= 1991 |pmid= 2288637 |doi= }}
*{{cite journal | author=Hammonds RG, McKay P, Winslow GA, ''et al.'' |title=Purification and characterization of recombinant human parathyroid hormone-related protein. |journal=J. Biol. Chem. |volume=264 |issue= 25 |pages= 14806-11 |year= 1989 |pmid= 2549037 |doi= }}
*{{cite journal | author=Yasuda T, Banville D, Hendy GN, Goltzman D |title=Characterization of the human parathyroid hormone-like peptide gene. Functional and evolutionary aspects. |journal=J. Biol. Chem. |volume=264 |issue= 13 |pages= 7720-5 |year= 1989 |pmid= 2708388 |doi= }}
*{{cite journal | author=Suva LJ, Mather KA, Gillespie MT, ''et al.'' |title=Structure of the 5' flanking region of the gene encoding human parathyroid-hormone-related protein (PTHrP). |journal=Gene |volume=77 |issue= 1 |pages= 95-105 |year= 1989 |pmid= 2744490 |doi= }}
*{{cite journal | author=Mangin M, Webb AC, Dreyer BE, ''et al.'' |title=Identification of a cDNA encoding a parathyroid hormone-like peptide from a human tumor associated with humoral hypercalcemia of malignancy. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 2 |pages= 597-601 |year= 1988 |pmid= 2829195 |doi= }}
*{{cite journal | author=Moseley JM, Kubota M, Diefenbach-Jagger H, ''et al.'' |title=Parathyroid hormone-related protein purified from a human lung cancer cell line. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 14 |pages= 5048-52 |year= 1987 |pmid= 2885845 |doi= }}
*{{cite journal | author=Mangin M, Ikeda K, Dreyer BE, Broadus AE |title=Isolation and characterization of the human parathyroid hormone-like peptide gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 7 |pages= 2408-12 |year= 1989 |pmid= 2928340 |doi= }}
*{{cite journal | author=Thiede MA, Strewler GJ, Nissenson RA, ''et al.'' |title=Human renal carcinoma expresses two messages encoding a parathyroid hormone-like peptide: evidence for the alternative splicing of a single-copy gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 13 |pages= 4605-9 |year= 1988 |pmid= 3290897 |doi= }}
*{{cite journal | author=Suva LJ, Winslow GA, Wettenhall RE, ''et al.'' |title=A parathyroid hormone-related protein implicated in malignant hypercalcemia: cloning and expression. |journal=Science |volume=237 |issue= 4817 |pages= 893-6 |year= 1987 |pmid= 3616618 |doi= }}
*{{cite journal | author=Campos RV, Zhang L, Drucker DJ |title=Differential expression of RNA transcripts encoding unique carboxy-terminal sequences of human parathyroid hormone-related peptide. |journal=Mol. Endocrinol. |volume=8 |issue= 12 |pages= 1656-66 |year= 1995 |pmid= 7708054 |doi= }}
*{{cite journal | author=Holick MF, Ray S, Chen TC, ''et al.'' |title=A parathyroid hormone antagonist stimulates epidermal proliferation and hair growth in mice. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 17 |pages= 8014-6 |year= 1994 |pmid= 8058749 |doi= }}
*{{cite journal | author=Seitz PK, Cooper KM, Ives KL, ''et al.'' |title=Parathyroid hormone-related peptide production and action in a myoepithelial cell line derived from normal human breast. |journal=Endocrinology |volume=133 |issue= 3 |pages= 1116-24 |year= 1993 |pmid= 8396010 |doi= }}
*{{cite journal | author=Li H, Seitz PK, Selvanayagam P, ''et al.'' |title=Effect of endogenously produced parathyroid hormone-related peptide on growth of a human hepatoma cell line (Hep G2). |journal=Endocrinology |volume=137 |issue= 6 |pages= 2367-74 |year= 1996 |pmid= 8641188 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on S100B... {November 14, 2007 2:07:01 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:07:32 PM 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_S100B_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1b4c.
| PDB = {{PDB2|1b4c}}, {{PDB2|1cfp}}, {{PDB2|1dt7}}, {{PDB2|1mho}}, {{PDB2|1mq1}}, {{PDB2|1mwn}}, {{PDB2|1psb}}, {{PDB2|1qlk}}, {{PDB2|1sym}}, {{PDB2|1uwo}}, {{PDB2|1xyd}}, {{PDB2|2h61}}
| Name = S100 calcium binding protein B
| HGNCid = 10500
| Symbol = S100B
| AltSymbols =; S100; NEF; S100beta
| OMIM = 176990
| ECnumber =
| Homologene = 4567
| MGIid = 98217
| GeneAtlas_image1 = PBB_GE_S100B_209686_at_tn.png
| Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0019210 |text = kinase inhibitor activity}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0048154 |text = S100 beta binding}} {{GNF_GO|id=GO:0048156 |text = tau protein binding}} {{GNF_GO|id=GO:0048306 |text = calcium-dependent protein binding}}
| Component = {{GNF_GO|id=GO:0001726 |text = ruffle}} {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0043025 |text = cell soma}}
| Process = {{GNF_GO|id=GO:0006112 |text = energy reserve metabolic process}} {{GNF_GO|id=GO:0006874 |text = cellular calcium ion homeostasis}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0007409 |text = axonogenesis}} {{GNF_GO|id=GO:0007417 |text = central nervous system development}} {{GNF_GO|id=GO:0007613 |text = memory}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0042035 |text = regulation of cytokine biosynthetic process}} {{GNF_GO|id=GO:0045917 |text = positive regulation of complement activation}} {{GNF_GO|id=GO:0048143 |text = astrocyte activation}} {{GNF_GO|id=GO:0048151 |text = hyperphosphorylation}} {{GNF_GO|id=GO:0048169 |text = regulation of long-term neuronal synaptic plasticity}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6285
| Hs_Ensembl = ENSG00000160307
| Hs_RefseqProtein = NP_006263
| Hs_RefseqmRNA = NM_006272
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 21
| Hs_GenLoc_start = 46842968
| Hs_GenLoc_end = 46849424
| Hs_Uniprot = P04271
| Mm_EntrezGene = 20203
| Mm_Ensembl = ENSMUSG00000033208
| Mm_RefseqmRNA = NM_009115
| Mm_RefseqProtein = NP_033141
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 75697569
| Mm_GenLoc_end = 75703788
| Mm_Uniprot = Q3UY00
}}
}}
'''S100 calcium binding protein B''', also known as '''S100B''', is a human [[gene]].
<!-- 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 S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21; however, this gene is located at 21q22.3. This protein may function in Neurite extension, proliferation of melanoma cells, stimulation of Ca2+ fluxes, inhibition of PKC-mediated phosphorylation, astrocytosis and axonal proliferation, and inhibition of microtubule assembly. Chromosomal rearrangements and altered expression of this gene have been implicated in several neurological, neoplastic, and other types of diseases, including Alzheimer's disease, Down's syndrome, epilepsy, amyotrophic lateral sclerosis, melanoma, and type I diabetes.<ref>{{cite web | title = Entrez Gene: S100B S100 calcium binding protein B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6285| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schäfer BW, Heizmann CW |title=The S100 family of EF-hand calcium-binding proteins: functions and pathology. |journal=Trends Biochem. Sci. |volume=21 |issue= 4 |pages= 134-40 |year= 1996 |pmid= 8701470 |doi= }}
*{{cite journal | author=Garbuglia M, Verzini M, Sorci G, ''et al.'' |title=The calcium-modulated proteins, S100A1 and S100B, as potential regulators of the dynamics of type III intermediate filaments. |journal=Braz. J. Med. Biol. Res. |volume=32 |issue= 10 |pages= 1177-85 |year= 2000 |pmid= 10510252 |doi= }}
*{{cite journal | author=Rothermundt M, Peters M, Prehn JH, Arolt V |title=S100B in brain damage and neurodegeneration. |journal=Microsc. Res. Tech. |volume=60 |issue= 6 |pages= 614-32 |year= 2003 |pmid= 12645009 |doi= 10.1002/jemt.10303 }}
*{{cite journal | author=Michetti F, Gazzolo D |title=S100B testing in pregnancy. |journal=Clin. Chim. Acta |volume=335 |issue= 1-2 |pages= 1-7 |year= 2004 |pmid= 12927678 |doi= }}
*{{cite journal | author=Raabe A, Kopetsch O, Woszczyk A, ''et al.'' |title=Serum S-100B protein as a molecular marker in severe traumatic brain injury. |journal=Restor. Neurol. Neurosci. |volume=21 |issue= 3-4 |pages= 159-69 |year= 2004 |pmid= 14530578 |doi= }}
*{{cite journal | author=Sen J, Belli A |title=S100B in neuropathologic states: the CRP of the brain? |journal=J. Neurosci. Res. |volume=85 |issue= 7 |pages= 1373-80 |year= 2007 |pmid= 17348038 |doi= 10.1002/jnr.21211 }}
*{{cite journal | author=Morii K, Tanaka R, Takahashi Y, ''et al.'' |title=Structure and chromosome assignment of human S100 alpha and beta subunit genes. |journal=Biochem. Biophys. Res. Commun. |volume=175 |issue= 1 |pages= 185-91 |year= 1991 |pmid= 1998503 |doi= }}
*{{cite journal | author=Allore RJ, Friend WC, O'Hanlon D, ''et al.'' |title=Cloning and expression of the human S100 beta gene. |journal=J. Biol. Chem. |volume=265 |issue= 26 |pages= 15537-43 |year= 1990 |pmid= 2394738 |doi= }}
*{{cite journal | author=Duncan AM, Higgins J, Dunn RJ, ''et al.'' |title=Refined sublocalization of the human gene encoding the beta subunit of the S100 protein (S100B) and confirmation of a subtle t(9;21) translocation using in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=50 |issue= 4 |pages= 234-5 |year= 1989 |pmid= 2530061 |doi= }}
*{{cite journal | author=Baudier J, Cole RD |title=Interactions between the microtubule-associated tau proteins and S100b regulate tau phosphorylation by the Ca2+/calmodulin-dependent protein kinase II. |journal=J. Biol. Chem. |volume=263 |issue= 12 |pages= 5876-83 |year= 1988 |pmid= 2833519 |doi= }}
*{{cite journal | author=Allore R, O'Hanlon D, Price R, ''et al.'' |title=Gene encoding the beta subunit of S100 protein is on chromosome 21: implications for Down syndrome. |journal=Science |volume=239 |issue= 4845 |pages= 1311-3 |year= 1988 |pmid= 2964086 |doi= }}
*{{cite journal | author=Jensen R, Marshak DR, Anderson C, ''et al.'' |title=Characterization of human brain S100 protein fraction: amino acid sequence of S100 beta. |journal=J. Neurochem. |volume=45 |issue= 3 |pages= 700-5 |year= 1985 |pmid= 4031854 |doi= }}
*{{cite journal | author=Baudier J, Glasser N, Haglid K, Gerard D |title=Purification, characterization and ion binding properties of human brain S100b protein. |journal=Biochim. Biophys. Acta |volume=790 |issue= 2 |pages= 164-73 |year= 1984 |pmid= 6487634 |doi= }}
*{{cite journal | author=Adams MD, Kerlavage AR, Fleischmann RD, ''et al.'' |title=Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. |journal=Nature |volume=377 |issue= 6547 Suppl |pages= 3-174 |year= 1995 |pmid= 7566098 |doi= }}
*{{cite journal | author=Schäfer BW, Wicki R, Engelkamp D, ''et al.'' |title=Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21: rationale for a new nomenclature of the S100 calcium-binding protein family. |journal=Genomics |volume=25 |issue= 3 |pages= 638-43 |year= 1995 |pmid= 7759097 |doi= }}
*{{cite journal | author=Reeves RH, Yao J, Crowley MR, ''et al.'' |title=Astrocytosis and axonal proliferation in the hippocampus of S100b transgenic mice. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 12 |pages= 5359-63 |year= 1994 |pmid= 8202493 |doi= }}
*{{cite journal | author=Engelkamp D, Schäfer BW, Mattei MG, ''et al.'' |title=Six S100 genes are clustered on human chromosome 1q21: identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 14 |pages= 6547-51 |year= 1993 |pmid= 8341667 |doi= }}
*{{cite journal | author=Peña LA, Brecher CW, Marshak DR |title=beta-Amyloid regulates gene expression of glial trophic substance S100 beta in C6 glioma and primary astrocyte cultures. |journal=Brain Res. Mol. Brain Res. |volume=34 |issue= 1 |pages= 118-26 |year= 1997 |pmid= 8750867 |doi= }}
*{{cite journal | author=Landar A, Caddell G, Chessher J, Zimmer DB |title=Identification of an S100A1/S100B target protein: phosphoglucomutase. |journal=Cell Calcium |volume=20 |issue= 3 |pages= 279-85 |year= 1997 |pmid= 8894274 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SOCS1... {November 14, 2007 2:08:52 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:09:42 PM 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 = Suppressor of cytokine signaling 1
| HGNCid = 19383
| Symbol = SOCS1
| AltSymbols =; CIS1; CISH1; JAB; SOCS-1; SSI-1; SSI1; TIP3
| OMIM = 603597
| ECnumber =
| Homologene = 2776
| MGIid = 1354910
| GeneAtlas_image1 = PBB_GE_SOCS1_210001_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SOCS1_209999_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004860 |text = protein kinase inhibitor activity}} {{GNF_GO|id=GO:0005159 |text = insulin-like growth factor receptor binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0019901 |text = protein kinase binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0001558 |text = regulation of cell growth}} {{GNF_GO|id=GO:0001932 |text = regulation of protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0007259 |text = JAK-STAT cascade}} {{GNF_GO|id=GO:0019221 |text = cytokine and chemokine mediated signaling pathway}} {{GNF_GO|id=GO:0042518 |text = negative regulation of tyrosine phosphorylation of Stat3 protein}} {{GNF_GO|id=GO:0045444 |text = fat cell differentiation}} {{GNF_GO|id=GO:0046426 |text = negative regulation of JAK-STAT cascade}} {{GNF_GO|id=GO:0046627 |text = negative regulation of insulin receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8651
| Hs_Ensembl = ENSG00000185338
| Hs_RefseqProtein = NP_003736
| Hs_RefseqmRNA = NM_003745
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 11255775
| Hs_GenLoc_end = 11257540
| Hs_Uniprot = O15524
| Mm_EntrezGene = 12703
| Mm_Ensembl = ENSMUSG00000038037
| Mm_RefseqmRNA = NM_009896
| Mm_RefseqProtein = NP_034026
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 10695821
| Mm_GenLoc_end = 10699114
| Mm_Uniprot = O35716
}}
}}
'''Suppressor of cytokine signaling 1''', also known as '''SOCS1''', is a human [[gene]].
<!-- 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 STAT-induced STAT inhibitor (SSI), also known as suppressor of cytokine signaling (SOCS), family. SSI family members are cytokine-inducible negative regulators of cytokine signaling. The expression of this gene can be induced by a subset of cytokines, including IL2, IL3 erythropoietin (EPO), CSF2/GM-CSF, and interferon (IFN)-gamma. The protein encoded by this gene functions downstream of cytokine receptors, and takes part in a negative feedback loop to attenuate cytokine signaling. Knockout studies in mice suggested the role of this gene as a modulator of IFN-gamma action, which is required for normal postnatal growth and survival.<ref>{{cite web | title = Entrez Gene: SOCS1 suppressor of cytokine signaling 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8651| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Krebs DL, Hilton DJ |title=SOCS proteins: negative regulators of cytokine signaling. |journal=Stem Cells |volume=19 |issue= 5 |pages= 378-87 |year= 2001 |pmid= 11553846 |doi= }}
*{{cite journal | author=Wang J, Campbell IL |title=Cytokine signaling in the brain: putting a SOCS in it? |journal=J. Neurosci. Res. |volume=67 |issue= 4 |pages= 423-7 |year= 2002 |pmid= 11835308 |doi= }}
*{{cite journal | author=Kile BT, Schulman BA, Alexander WS, ''et al.'' |title=The SOCS box: a tale of destruction and degradation. |journal=Trends Biochem. Sci. |volume=27 |issue= 5 |pages= 235-41 |year= 2002 |pmid= 12076535 |doi= }}
*{{cite journal | author=Yoshimura A, Ohkubo T, Kiguchi T, ''et al.'' |title=A novel cytokine-inducible gene CIS encodes an SH2-containing protein that binds to tyrosine-phosphorylated interleukin 3 and erythropoietin receptors. |journal=EMBO J. |volume=14 |issue= 12 |pages= 2816-26 |year= 1995 |pmid= 7796808 |doi= }}
*{{cite journal | author=Starr R, Willson TA, Viney EM, ''et al.'' |title=A family of cytokine-inducible inhibitors of signalling. |journal=Nature |volume=387 |issue= 6636 |pages= 917-21 |year= 1997 |pmid= 9202125 |doi= 10.1038/43206 }}
*{{cite journal | author=Endo TA, Masuhara M, Yokouchi M, ''et al.'' |title=A new protein containing an SH2 domain that inhibits JAK kinases. |journal=Nature |volume=387 |issue= 6636 |pages= 921-4 |year= 1997 |pmid= 9202126 |doi= 10.1038/43213 }}
*{{cite journal | author=Minamoto S, Ikegame K, Ueno K, ''et al.'' |title=Cloning and functional analysis of new members of STAT induced STAT inhibitor (SSI) family: SSI-2 and SSI-3. |journal=Biochem. Biophys. Res. Commun. |volume=237 |issue= 1 |pages= 79-83 |year= 1997 |pmid= 9266833 |doi= 10.1006/bbrc.1997.7080 }}
*{{cite journal | author=Ohya K, Kajigaya S, Yamashita Y, ''et al.'' |title=SOCS-1/JAB/SSI-1 can bind to and suppress Tec protein-tyrosine kinase. |journal=J. Biol. Chem. |volume=272 |issue= 43 |pages= 27178-82 |year= 1997 |pmid= 9341160 |doi= }}
*{{cite journal | author=Dey BR, Spence SL, Nissley P, Furlanetto RW |title=Interaction of human suppressor of cytokine signaling (SOCS)-2 with the insulin-like growth factor-I receptor. |journal=J. Biol. Chem. |volume=273 |issue= 37 |pages= 24095-101 |year= 1998 |pmid= 9727029 |doi= }}
*{{cite journal | author=De Sepulveda P, Okkenhaug K, Rose JL, ''et al.'' |title=Socs1 binds to multiple signalling proteins and suppresses steel factor-dependent proliferation. |journal=EMBO J. |volume=18 |issue= 4 |pages= 904-15 |year= 1999 |pmid= 10022833 |doi= 10.1093/emboj/18.4.904 }}
*{{cite journal | author=Zhang JG, Farley A, Nicholson SE, ''et al.'' |title=The conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 5 |pages= 2071-6 |year= 1999 |pmid= 10051596 |doi= }}
*{{cite journal | author=Yasukawa H, Misawa H, Sakamoto H, ''et al.'' |title=The JAK-binding protein JAB inhibits Janus tyrosine kinase activity through binding in the activation loop. |journal=EMBO J. |volume=18 |issue= 5 |pages= 1309-20 |year= 1999 |pmid= 10064597 |doi= 10.1093/emboj/18.5.1309 }}
*{{cite journal | author=Marine JC, Topham DJ, McKay C, ''et al.'' |title=SOCS1 deficiency causes a lymphocyte-dependent perinatal lethality. |journal=Cell |volume=98 |issue= 5 |pages= 609-16 |year= 1999 |pmid= 10490100 |doi= }}
*{{cite journal | author=Yandava CN, Pillari A, Drazen JM |title=Radiation hybrid and cytogenetic mapping of SOCS1 and SOCS2 to chromosomes 16p13 and 12q, respectively. |journal=Genomics |volume=61 |issue= 1 |pages= 108-11 |year= 1999 |pmid= 10512686 |doi= 10.1006/geno.1999.5937 }}
*{{cite journal | author=Okabe S, Tauchi T, Morita H, ''et al.'' |title=Thrombopoietin induces an SH2-containing protein, CIS1, which binds to Mpl: involvement of the ubiquitin proteosome pathway. |journal=Exp. Hematol. |volume=27 |issue= 10 |pages= 1542-7 |year= 1999 |pmid= 10517496 |doi= }}
*{{cite journal | author=Ram PA, Waxman DJ |title=SOCS/CIS protein inhibition of growth hormone-stimulated STAT5 signaling by multiple mechanisms. |journal=J. Biol. Chem. |volume=274 |issue= 50 |pages= 35553-61 |year= 2000 |pmid= 10585430 |doi= }}
*{{cite journal | author=Sporri B, Kovanen PE, Sasaki A, ''et al.'' |title=JAB/SOCS1/SSI-1 is an interleukin-2-induced inhibitor of IL-2 signaling. |journal=Blood |volume=97 |issue= 1 |pages= 221-6 |year= 2001 |pmid= 11133764 |doi= }}
*{{cite journal | author=Kawazoe Y, Naka T, Fujimoto M, ''et al.'' |title=Signal transducer and activator of transcription (STAT)-induced STAT inhibitor 1 (SSI-1)/suppressor of cytokine signaling 1 (SOCS1) inhibits insulin signal transduction pathway through modulating insulin receptor substrate 1 (IRS-1) phosphorylation. |journal=J. Exp. Med. |volume=193 |issue= 2 |pages= 263-9 |year= 2001 |pmid= 11208867 |doi= }}
*{{cite journal | author=Bourette RP, De Sepulveda P, Arnaud S, ''et al.'' |title=Suppressor of cytokine signaling 1 interacts with the macrophage colony-stimulating factor receptor and negatively regulates its proliferation signal. |journal=J. Biol. Chem. |volume=276 |issue= 25 |pages= 22133-9 |year= 2001 |pmid= 11297560 |doi= 10.1074/jbc.M101878200 }}
*{{cite journal | author=Mooney RA, Senn J, Cameron S, ''et al.'' |title=Suppressors of cytokine signaling-1 and -6 associate with and inhibit the insulin receptor. A potential mechanism for cytokine-mediated insulin resistance. |journal=J. Biol. Chem. |volume=276 |issue= 28 |pages= 25889-93 |year= 2001 |pmid= 11342531 |doi= 10.1074/jbc.M010579200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on STK11... {November 14, 2007 2:07:32 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:08:07 PM 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 = Serine/threonine kinase 11
| HGNCid = 11389
| Symbol = STK11
| AltSymbols =; LKB1; PJS
| OMIM = 602216
| ECnumber =
| Homologene = 393
| MGIid = 1341870
| GeneAtlas_image1 = PBB_GE_STK11_41657_at_tn.png
| GeneAtlas_image2 = PBB_GE_STK11_204292_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0030145 |text = manganese ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007050 |text = cell cycle arrest}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6794
| Hs_Ensembl = ENSG00000118046
| Hs_RefseqProtein = NP_000446
| Hs_RefseqmRNA = NM_000455
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 1156798
| Hs_GenLoc_end = 1179434
| Hs_Uniprot = Q15831
| Mm_EntrezGene = 20869
| Mm_Ensembl = ENSMUSG00000003068
| Mm_RefseqmRNA = NM_011492
| Mm_RefseqProtein = NP_035622
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 79519331
| Mm_GenLoc_end = 79533808
| Mm_Uniprot = Q3V4A1
}}
}}
'''Serine/threonine kinase 11''', also known as '''STK11''', is a human [[gene]].
<!-- 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, which encodes a member of the serine/threonine kinase family, regulates cell polarity and functions as a tumor suppressor. Mutations in this gene have been associated with Peutz-Jeghers syndrome, an autosomal dominant disorder characterized by the growth of polyps in the gastrointestinal tract, pigmented macules on the skin and mouth, and other neoplasms. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.<ref>{{cite web | title = Entrez Gene: STK11 serine/threonine kinase 11| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6794| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Yoo LI, Chung DC, Yuan J |title=LKB1--a master tumour suppressor of the small intestine and beyond. |journal=Nat. Rev. Cancer |volume=2 |issue= 7 |pages= 529-35 |year= 2002 |pmid= 12094239 |doi= 10.1038/nrc843 }}
*{{cite journal | author=Baas AF, Smit L, Clevers H |title=LKB1 tumor suppressor protein: PARtaker in cell polarity. |journal=Trends Cell Biol. |volume=14 |issue= 6 |pages= 312-9 |year= 2004 |pmid= 15183188 |doi= 10.1016/j.tcb.2004.04.001 }}
*{{cite journal | author=Katajisto P, Vallenius T, Vaahtomeri K, ''et al.'' |title=The LKB1 tumor suppressor kinase in human disease. |journal=Biochim. Biophys. Acta |volume=1775 |issue= 1 |pages= 63-75 |year= 2007 |pmid= 17010524 |doi= 10.1016/j.bbcan.2006.08.003 }}
*{{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=Hemminki A, Tomlinson I, Markie D, ''et al.'' |title=Localization of a susceptibility locus for Peutz-Jeghers syndrome to 19p using comparative genomic hybridization and targeted linkage analysis. |journal=Nat. Genet. |volume=15 |issue= 1 |pages= 87-90 |year= 1997 |pmid= 8988175 |doi= 10.1038/ng0197-87 }}
*{{cite journal | author=Jenne DE, Reimann H, Nezu J, ''et al.'' |title=Peutz-Jeghers syndrome is caused by mutations in a novel serine threonine kinase. |journal=Nat. Genet. |volume=18 |issue= 1 |pages= 38-43 |year= 1998 |pmid= 9425897 |doi= 10.1038/ng0198-38 }}
*{{cite journal | author=Hemminki A, Markie D, Tomlinson I, ''et al.'' |title=A serine/threonine kinase gene defective in Peutz-Jeghers syndrome. |journal=Nature |volume=391 |issue= 6663 |pages= 184-7 |year= 1998 |pmid= 9428765 |doi= 10.1038/34432 }}
*{{cite journal | author=Bignell GR, Barfoot R, Seal S, ''et al.'' |title=Low frequency of somatic mutations in the LKB1/Peutz-Jeghers syndrome gene in sporadic breast cancer. |journal=Cancer Res. |volume=58 |issue= 7 |pages= 1384-6 |year= 1998 |pmid= 9537235 |doi= }}
*{{cite journal | author=Nakagawa H, Koyama K, Miyoshi Y, ''et al.'' |title=Nine novel germline mutations of STK11 in ten families with Peutz-Jeghers syndrome. |journal=Hum. Genet. |volume=103 |issue= 2 |pages= 168-72 |year= 1998 |pmid= 9760200 |doi= }}
*{{cite journal | author=Mehenni H, Gehrig C, Nezu J, ''et al.'' |title=Loss of LKB1 kinase activity in Peutz-Jeghers syndrome, and evidence for allelic and locus heterogeneity. |journal=Am. J. Hum. Genet. |volume=63 |issue= 6 |pages= 1641-50 |year= 1999 |pmid= 9837816 |doi= }}
*{{cite journal | author=Guldberg P, thor Straten P, Ahrenkiel V, ''et al.'' |title=Somatic mutation of the Peutz-Jeghers syndrome gene, LKB1/STK11, in malignant melanoma. |journal=Oncogene |volume=18 |issue= 9 |pages= 1777-80 |year= 1999 |pmid= 10208439 |doi= 10.1038/sj.onc.1202486 }}
*{{cite journal | author=Su GH, Hruban RH, Bansal RK, ''et al.'' |title=Germline and somatic mutations of the STK11/LKB1 Peutz-Jeghers gene in pancreatic and biliary cancers. |journal=Am. J. Pathol. |volume=154 |issue= 6 |pages= 1835-40 |year= 1999 |pmid= 10362809 |doi= }}
*{{cite journal | author=Westerman AM, Entius MM, Boor PP, ''et al.'' |title=Novel mutations in the LKB1/STK11 gene in Dutch Peutz-Jeghers families. |journal=Hum. Mutat. |volume=13 |issue= 6 |pages= 476-81 |year= 1999 |pmid= 10408777 |doi= 10.1002/(SICI)1098-1004(1999)13:6<476::AID-HUMU7>3.0.CO;2-2 }}
*{{cite journal | author=Scanlan MJ, Gordan JD, Williamson B, ''et al.'' |title=Antigens recognized by autologous antibody in patients with renal-cell carcinoma. |journal=Int. J. Cancer |volume=83 |issue= 4 |pages= 456-64 |year= 1999 |pmid= 10508479 |doi= }}
*{{cite journal | author=Collins SP, Reoma JL, Gamm DM, Uhler MD |title=LKB1, a novel serine/threonine protein kinase and potential tumour suppressor, is phosphorylated by cAMP-dependent protein kinase (PKA) and prenylated in vivo. |journal=Biochem. J. |volume=345 Pt 3 |issue= |pages= 673-80 |year= 2000 |pmid= 10642527 |doi= }}
*{{cite journal | author=Sapkota GP, Kieloch A, Lizcano JM, ''et al.'' |title=Phosphorylation of the protein kinase mutated in Peutz-Jeghers cancer syndrome, LKB1/STK11, at Ser431 by p90(RSK) and cAMP-dependent protein kinase, but not its farnesylation at Cys(433), is essential for LKB1 to suppress cell vrowth. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 19469-82 |year= 2001 |pmid= 11297520 |doi= 10.1074/jbc.M009953200 }}
*{{cite journal | author=Karuman P, Gozani O, Odze RD, ''et al.'' |title=The Peutz-Jegher gene product LKB1 is a mediator of p53-dependent cell death. |journal=Mol. Cell |volume=7 |issue= 6 |pages= 1307-19 |year= 2001 |pmid= 11430832 |doi= }}
*{{cite journal | author=Marignani PA, Kanai F, Carpenter CL |title=LKB1 associates with Brg1 and is necessary for Brg1-induced growth arrest. |journal=J. Biol. Chem. |volume=276 |issue= 35 |pages= 32415-8 |year= 2001 |pmid= 11445556 |doi= 10.1074/jbc.C100207200 }}
*{{cite journal | author=Abed AA, Günther K, Kraus C, ''et al.'' |title=Mutation screening at the RNA level of the STK11/LKB1 gene in Peutz-Jeghers syndrome reveals complex splicing abnormalities and a novel mRNA isoform (STK11 c.597(insertion mark)598insIVS4). |journal=Hum. Mutat. |volume=18 |issue= 5 |pages= 397-410 |year= 2002 |pmid= 11668633 |doi= 10.1002/humu.1211 }}
*{{cite journal | author=Sato N, Rosty C, Jansen M, ''et al.'' |title=STK11/LKB1 Peutz-Jeghers gene inactivation in intraductal papillary-mucinous neoplasms of the pancreas. |journal=Am. J. Pathol. |volume=159 |issue= 6 |pages= 2017-22 |year= 2001 |pmid= 11733352 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TAF1... {November 14, 2007 2:08:07 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:08:52 PM 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_TAF1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1eqf.
| PDB = {{PDB2|1eqf}}
| Name = TAF1 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 250kDa
| HGNCid = 11535
| Symbol = TAF1
| AltSymbols =; NSCL2; OF; BA2R; CCG1; CCGS; P250; TAF2A; TAFII250
| OMIM = 313650
| ECnumber =
| Homologene = 37942
| MGIid = 1336878
| GeneAtlas_image1 = PBB_GE_TAF1_216711_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0004402 |text = histone acetyltransferase activity}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016301 |text = kinase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005669 |text = transcription factor TFIID complex}}
| Process = {{GNF_GO|id=GO:0000080 |text = G1 phase of mitotic cell cycle}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006352 |text = transcription initiation}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0046777 |text = protein amino acid autophosphorylation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6872
| Hs_Ensembl = ENSG00000147133
| Hs_RefseqProtein = NP_004597
| Hs_RefseqmRNA = NM_004606
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 70502839
| Hs_GenLoc_end = 70667100
| Hs_Uniprot = P21675
| Mm_EntrezGene = 270627
| Mm_Ensembl = ENSMUSG00000031314
| Mm_RefseqmRNA = XM_001000569
| Mm_RefseqProtein = XP_001000569
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 97735541
| Mm_GenLoc_end = 97802241
| Mm_Uniprot =
}}
}}
'''TAF1 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 250kDa''', also known as '''TAF1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein that coordinates these activities is the basal transcription factor TFIID, which binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes the largest subunit of TFIID. This subunit binds to core promoter sequences encompassing the transcription start site. It also binds to activators and other transcriptional regulators, and these interactions affect the rate of transcription initiation. This subunit contains two independent protein kinase domains at the N and C-terminals, but also possesses acetyltransferase activity and can act as a ubiquitin-activating/conjugating enzyme. Two transcripts encoding different isoforms have been identified for this gene.<ref>{{cite web | title = Entrez Gene: TAF1 TAF1 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 250kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6872| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wassarman DA, Sauer F |title=TAF(II)250: a transcription toolbox. |journal=J. Cell. Sci. |volume=114 |issue= Pt 16 |pages= 2895-902 |year= 2002 |pmid= 11686293 |doi= }}
*{{cite journal | author=Ha I, Lane WS, Reinberg D |title=Cloning of a human gene encoding the general transcription initiation factor IIB. |journal=Nature |volume=352 |issue= 6337 |pages= 689-95 |year= 1991 |pmid= 1876184 |doi= 10.1038/352689a0 }}
*{{cite journal | author=Sekiguchi T, Nohiro Y, Nakamura Y, ''et al.'' |title=The human CCG1 gene, essential for progression of the G1 phase, encodes a 210-kilodalton nuclear DNA-binding protein. |journal=Mol. Cell. Biol. |volume=11 |issue= 6 |pages= 3317-25 |year= 1991 |pmid= 2038334 |doi= }}
*{{cite journal | author=Sekiguchi T, Miyata T, Nishimoto T |title=Molecular cloning of the cDNA of human X chromosomal gene (CCG1) which complements the temperature-sensitive G1 mutants, tsBN462 and ts13, of the BHK cell line. |journal=EMBO J. |volume=7 |issue= 6 |pages= 1683-7 |year= 1988 |pmid= 3169001 |doi= }}
*{{cite journal | author=Sekiguchi T, Yoshida MC, Sekiguchi M, Nishimoto T |title=Isolation of a human X chromosome-linked gene essential for progression from G1 to S phase of the cell cycle. |journal=Exp. Cell Res. |volume=169 |issue= 2 |pages= 395-407 |year= 1987 |pmid= 3556424 |doi= }}
*{{cite journal | author=Ruppert S, Tjian R |title=Human TAFII250 interacts with RAP74: implications for RNA polymerase II initiation. |journal=Genes Dev. |volume=9 |issue= 22 |pages= 2747-55 |year= 1995 |pmid= 7590250 |doi= }}
*{{cite journal | author=Hisatake K, Ohta T, Takada R, ''et al.'' |title=Evolutionary conservation of human TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and with general transcription factors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 18 |pages= 8195-9 |year= 1995 |pmid= 7667268 |doi= }}
*{{cite journal | author=Ruppert S, Wang EH, Tjian R |title=Cloning and expression of human TAFII250: a TBP-associated factor implicated in cell-cycle regulation. |journal=Nature |volume=362 |issue= 6416 |pages= 175-9 |year= 1993 |pmid= 7680771 |doi= 10.1038/362175a0 }}
*{{cite journal | author=Shao Z, Ruppert S, Robbins PD |title=The retinoblastoma-susceptibility gene product binds directly to the human TATA-binding protein-associated factor TAFII250. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 8 |pages= 3115-9 |year= 1995 |pmid= 7724524 |doi= }}
*{{cite journal | author=DeJong J, Bernstein R, Roeder RG |title=Human general transcription factor TFIIA: characterization of a cDNA encoding the small subunit and requirement for basal and activated transcription. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 8 |pages= 3313-7 |year= 1995 |pmid= 7724559 |doi= }}
*{{cite journal | author=Thut CJ, Chen JL, Klemm R, Tjian R |title=p53 transcriptional activation mediated by coactivators TAFII40 and TAFII60. |journal=Science |volume=267 |issue= 5194 |pages= 100-4 |year= 1995 |pmid= 7809597 |doi= }}
*{{cite journal | author=Zhou Q, Sharp PA |title=Novel mechanism and factor for regulation by HIV-1 Tat. |journal=EMBO J. |volume=14 |issue= 2 |pages= 321-8 |year= 1995 |pmid= 7835343 |doi= }}
*{{cite journal | author=Parada CA, Yoon JB, Roeder RG |title=A novel LBP-1-mediated restriction of HIV-1 transcription at the level of elongation in vitro. |journal=J. Biol. Chem. |volume=270 |issue= 5 |pages= 2274-83 |year= 1995 |pmid= 7836461 |doi= }}
*{{cite journal | author=Jacq X, Brou C, Lutz Y, ''et al.'' |title=Human TAFII30 is present in a distinct TFIID complex and is required for transcriptional activation by the estrogen receptor. |journal=Cell |volume=79 |issue= 1 |pages= 107-17 |year= 1994 |pmid= 7923369 |doi= }}
*{{cite journal | author=Ou SH, Garcia-Martínez LF, Paulssen EJ, Gaynor RB |title=Role of flanking E box motifs in human immunodeficiency virus type 1 TATA element function. |journal=J. Virol. |volume=68 |issue= 11 |pages= 7188-99 |year= 1994 |pmid= 7933101 |doi= }}
*{{cite journal | author=Sun X, Ma D, Sheldon M, ''et al.'' |title=Reconstitution of human TFIIA activity from recombinant polypeptides: a role in TFIID-mediated transcription. |journal=Genes Dev. |volume=8 |issue= 19 |pages= 2336-48 |year= 1994 |pmid= 7958900 |doi= }}
*{{cite journal | author=Metz R, Bannister AJ, Sutherland JA, ''et al.'' |title=c-Fos-induced activation of a TATA-box-containing promoter involves direct contact with TATA-box-binding protein. |journal=Mol. Cell. Biol. |volume=14 |issue= 9 |pages= 6021-9 |year= 1994 |pmid= 8065335 |doi= }}
*{{cite journal | author=Kashanchi F, Piras G, Radonovich MF, ''et al.'' |title=Direct interaction of human TFIID with the HIV-1 transactivator tat. |journal=Nature |volume=367 |issue= 6460 |pages= 295-9 |year= 1994 |pmid= 8121496 |doi= 10.1038/367295a0 }}
*{{cite journal | author=Nakashima T, Sekiguchi T, Sunamoto H, ''et al.'' |title=Structure of the human CCG1 gene: relationship between the exons/introns and functional domain/modules of the protein. |journal=Gene |volume=141 |issue= 2 |pages= 193-200 |year= 1994 |pmid= 8163188 |doi= }}
*{{cite journal | author=Ma D, Watanabe H, Mermelstein F, ''et al.'' |title=Isolation of a cDNA encoding the largest subunit of TFIIA reveals functions important for activated transcription. |journal=Genes Dev. |volume=7 |issue= 11 |pages= 2246-57 |year= 1993 |pmid= 8224850 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TNFRSF10B... {November 14, 2007 2:09:42 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:10:35 PM 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_TNFRSF10B_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1d0g.
| PDB = {{PDB2|1d0g}}, {{PDB2|1d4v}}, {{PDB2|1du3}}, {{PDB2|1za3}}, {{PDB2|2h9g}}
| Name = Tumor necrosis factor receptor superfamily, member 10b
| HGNCid = 11905
| Symbol = TNFRSF10B
| AltSymbols =; CD262; DR5; KILLER; KILLER/DR5; TRAIL-R2; TRAILR2; TRICK2; TRICK2A; TRICK2B; TRICKB; ZTNFR9
| OMIM = 603612
| ECnumber =
| Homologene = 88698
| MGIid =
| GeneAtlas_image1 = PBB_GE_TNFRSF10B_209295_at_tn.png
| GeneAtlas_image2 = PBB_GE_TNFRSF10B_209294_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_TNFRSF10B_210405_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008656 |text = caspase activator activity}} {{GNF_GO|id=GO:0045569 |text = TRAIL binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006919 |text = caspase activation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0007250 |text = activation of NF-kappaB-inducing kinase}} {{GNF_GO|id=GO:0008625 |text = induction of apoptosis via death domain receptors}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8795
| Hs_Ensembl = ENSG00000120889
| Hs_RefseqProtein = NP_003833
| Hs_RefseqmRNA = NM_003842
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 22933598
| Hs_GenLoc_end = 22982637
| Hs_Uniprot = O14763
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Tumor necrosis factor receptor superfamily, member 10b''', also known as '''TNFRSF10B''', is a human [[gene]].
<!-- 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 TNF-receptor superfamily, and contains an intracelluar death domain. This receptor can be activated by tumor necrosis factor-related apoptosis inducing ligand (TNFSF10/TRAIL/APO-2L), and transduces apoptosis signal. Studies with FADD-deficient mice suggested that FADD, a death domain containing adaptor protein, is required for the apoptosis mediated by this protein.<ref>{{cite web | title = Entrez Gene: TNFRSF10B tumor necrosis factor receptor superfamily, member 10b| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8795| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Abe K, Kurakin A, Mohseni-Maybodi M, ''et al.'' |title=The complexity of TNF-related apoptosis-inducing ligand. |journal=Ann. N. Y. Acad. Sci. |volume=926 |issue= |pages= 52-63 |year= 2001 |pmid= 11193041 |doi= }}
*{{cite journal | author=Cha SS, Song YL, Oh BH |title=Specificity of molecular recognition learned from the crystal structures of TRAIL and the TRAIL:sDR5 complex. |journal=Vitam. Horm. |volume=67 |issue= |pages= 1-17 |year= 2004 |pmid= 15110168 |doi= 10.1016/S0083-6729(04)67001-4 }}
*{{cite journal | author=Kimberley FC, Screaton GR |title=Following a TRAIL: update on a ligand and its five receptors. |journal=Cell Res. |volume=14 |issue= 5 |pages= 359-72 |year= 2005 |pmid= 15538968 |doi= 10.1038/sj.cr.7290236 }}
*{{cite journal | author=Pan G, Ni J, Wei YF, ''et al.'' |title=An antagonist decoy receptor and a death domain-containing receptor for TRAIL. |journal=Science |volume=277 |issue= 5327 |pages= 815-8 |year= 1997 |pmid= 9242610 |doi= }}
*{{cite journal | author=Sheridan JP, Marsters SA, Pitti RM, ''et al.'' |title=Control of TRAIL-induced apoptosis by a family of signaling and decoy receptors. |journal=Science |volume=277 |issue= 5327 |pages= 818-21 |year= 1997 |pmid= 9242611 |doi= }}
*{{cite journal | author=Screaton GR, Mongkolsapaya J, Xu XN, ''et al.'' |title=TRICK2, a new alternatively spliced receptor that transduces the cytotoxic signal from TRAIL. |journal=Curr. Biol. |volume=7 |issue= 9 |pages= 693-6 |year= 1998 |pmid= 9285725 |doi= }}
*{{cite journal | author=Walczak H, Degli-Esposti MA, Johnson RS, ''et al.'' |title=TRAIL-R2: a novel apoptosis-mediating receptor for TRAIL. |journal=EMBO J. |volume=16 |issue= 17 |pages= 5386-97 |year= 1997 |pmid= 9311998 |doi= 10.1093/emboj/16.17.5386 }}
*{{cite journal | author=MacFarlane M, Ahmad M, Srinivasula SM, ''et al.'' |title=Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL. |journal=J. Biol. Chem. |volume=272 |issue= 41 |pages= 25417-20 |year= 1997 |pmid= 9325248 |doi= }}
*{{cite journal | author=Wu GS, Burns TF, McDonald ER, ''et al.'' |title=KILLER/DR5 is a DNA damage-inducible p53-regulated death receptor gene. |journal=Nat. Genet. |volume=17 |issue= 2 |pages= 141-3 |year= 1997 |pmid= 9326928 |doi= 10.1038/ng1097-141 }}
*{{cite journal | author=Schneider P, Bodmer JL, Thome M, ''et al.'' |title=Characterization of two receptors for TRAIL. |journal=FEBS Lett. |volume=416 |issue= 3 |pages= 329-34 |year= 1997 |pmid= 9373179 |doi= }}
*{{cite journal | author=Marsters SA, Sheridan JP, Pitti RM, ''et al.'' |title=A novel receptor for Apo2L/TRAIL contains a truncated death domain. |journal=Curr. Biol. |volume=7 |issue= 12 |pages= 1003-6 |year= 1998 |pmid= 9382840 |doi= }}
*{{cite journal | author=Chaudhary PM, Eby M, Jasmin A, ''et al.'' |title=Death receptor 5, a new member of the TNFR family, and DR4 induce FADD-dependent apoptosis and activate the NF-kappaB pathway. |journal=Immunity |volume=7 |issue= 6 |pages= 821-30 |year= 1998 |pmid= 9430227 |doi= }}
*{{cite journal | author=Schneider P, Thome M, Burns K, ''et al.'' |title=TRAIL receptors 1 (DR4) and 2 (DR5) signal FADD-dependent apoptosis and activate NF-kappaB. |journal=Immunity |volume=7 |issue= 6 |pages= 831-6 |year= 1998 |pmid= 9430228 |doi= }}
*{{cite journal | author=Pai SI, Wu GS, Ozören N, ''et al.'' |title=Rare loss-of-function mutation of a death receptor gene in head and neck cancer. |journal=Cancer Res. |volume=58 |issue= 16 |pages= 3513-8 |year= 1998 |pmid= 9721851 |doi= }}
*{{cite journal | author=Arai T, Akiyama Y, Okabe S, ''et al.'' |title=Genomic organization and mutation analyses of the DR5/TRAIL receptor 2 gene in colorectal carcinomas. |journal=Cancer Lett. |volume=133 |issue= 2 |pages= 197-204 |year= 1999 |pmid= 10072170 |doi= }}
*{{cite journal | author=Mongkolsapaya J, Grimes JM, Chen N, ''et al.'' |title=Structure of the TRAIL-DR5 complex reveals mechanisms conferring specificity in apoptotic initiation. |journal=Nat. Struct. Biol. |volume=6 |issue= 11 |pages= 1048-53 |year= 2002 |pmid= 10542098 |doi= 10.1038/14935 }}
*{{cite journal | author=Hymowitz SG, Christinger HW, Fuh G, ''et al.'' |title=Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex with death receptor 5. |journal=Mol. Cell |volume=4 |issue= 4 |pages= 563-71 |year= 1999 |pmid= 10549288 |doi= }}
*{{cite journal | author=Kuang AA, Diehl GE, Zhang J, Winoto A |title=FADD is required for DR4- and DR5-mediated apoptosis: lack of trail-induced apoptosis in FADD-deficient mouse embryonic fibroblasts. |journal=J. Biol. Chem. |volume=275 |issue= 33 |pages= 25065-8 |year= 2000 |pmid= 10862756 |doi= 10.1074/jbc.C000284200 }}
*{{cite journal | author=Trauzold A, Wermann H, Arlt A, ''et al.'' |title=CD95 and TRAIL receptor-mediated activation of protein kinase C and NF-kappaB contributes to apoptosis resistance in ductal pancreatic adenocarcinoma cells. |journal=Oncogene |volume=20 |issue= 31 |pages= 4258-69 |year= 2001 |pmid= 11464292 |doi= 10.1038/sj.onc.1204559 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TNFSF13B... {November 14, 2007 2:10:35 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:11:38 PM 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_TNFSF13B_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1jh5.
| PDB = {{PDB2|1jh5}}, {{PDB2|1kd7}}, {{PDB2|1kxg}}, {{PDB2|1oqd}}, {{PDB2|1oqe}}, {{PDB2|1osg}}, {{PDB2|1otz}}
| Name = Tumor necrosis factor (ligand) superfamily, member 13b
| HGNCid = 11929
| Symbol = TNFSF13B
| AltSymbols =; BAFF; BLYS; CD257; TALL-1; TALL1; THANK; TNFSF20; ZTNF4; delta BAFF
| OMIM = 603969
| ECnumber =
| Homologene = 48443
| MGIid = 1344376
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005164 |text = tumor necrosis factor receptor binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0001782 |text = B cell homeostasis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0030890 |text = positive regulation of B cell proliferation}} {{GNF_GO|id=GO:0031295 |text = T cell costimulation}} {{GNF_GO|id=GO:0031296 |text = B cell costimulation}} {{GNF_GO|id=GO:0042102 |text = positive regulation of T cell proliferation}} {{GNF_GO|id=GO:0045885 |text = positive regulation of survival gene product activity}} {{GNF_GO|id=GO:0048305 |text = immunoglobulin secretion}} {{GNF_GO|id=GO:0050776 |text = regulation of immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10673
| Hs_Ensembl = ENSG00000102524
| Hs_RefseqProtein = NP_006564
| Hs_RefseqmRNA = NM_006573
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 13
| Hs_GenLoc_start = 107720067
| Hs_GenLoc_end = 107758826
| Hs_Uniprot = Q9Y275
| Mm_EntrezGene = 24099
| Mm_Ensembl = ENSMUSG00000031497
| Mm_RefseqmRNA = NM_033622
| Mm_RefseqProtein = NP_296371
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 10006815
| Mm_GenLoc_end = 10035413
| Mm_Uniprot = Q3KP92
}}
}}
'''Tumor necrosis factor (ligand) superfamily, member 13b''', also known as '''TNFSF13B''', is a human [[gene]].
<!-- 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 cytokine that belongs to the tumor necrosis factor (TNF) ligand family. This cytokine is a ligand for receptors TNFRSF13B/TACI, TNFRSF17/BCMA, and TNFRSF13C/BAFFR. This cytokine is expressed in B cell lineage cells, and acts as a potent B cell activator. It has been also shown to play an important role in the proliferation and differentiation of B cells.<ref>{{cite web | title = Entrez Gene: TNFSF13B tumor necrosis factor (ligand) superfamily, member 13b| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10673| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nardelli B, Moore PA, Li Y, Hilbert DM |title=B lymphocyte stimulator (BLyS): a therapeutic trichotomy for the treatment of B lymphocyte diseases. |journal=Leuk. Lymphoma |volume=43 |issue= 7 |pages= 1367-73 |year= 2003 |pmid= 12389615 |doi= }}
*{{cite journal | author=Zhou T, Zhang J, Carter R, Kimberly R |title=BLyS and B cell autoimmunity. |journal=Curr. Dir. Autoimmun. |volume=6 |issue= |pages= 21-37 |year= 2003 |pmid= 12408045 |doi= }}
*{{cite journal | author=Stohl W |title=A therapeutic role for BLyS antagonists. |journal=Lupus |volume=13 |issue= 5 |pages= 317-22 |year= 2005 |pmid= 15230285 |doi= }}
*{{cite journal | author=Quartuccio L, Fabris M, Ferraccioli G |title=[B lymphocyte stimulator (BLyS) and monocytes: possible role in autoimmune diseases with a particular reference to rheumatoid arthritis] |journal=Reumatismo |volume=56 |issue= 3 |pages= 143-6 |year= 2004 |pmid= 15470519 |doi= }}
*{{cite journal | author=Sutherland AP, Mackay F, Mackay CR |title=Targeting BAFF: immunomodulation for autoimmune diseases and lymphomas. |journal=Pharmacol. Ther. |volume=112 |issue= 3 |pages= 774-86 |year= 2007 |pmid= 16863659 |doi= 10.1016/j.pharmthera.2006.06.002 }}
*{{cite journal | author=Bossen C, Schneider P |title=BAFF, APRIL and their receptors: structure, function and signaling. |journal=Semin. Immunol. |volume=18 |issue= 5 |pages= 263-75 |year= 2007 |pmid= 16914324 |doi= 10.1016/j.smim.2006.04.006 }}
*{{cite journal | author=Brink R |title=Regulation of B cell self-tolerance by BAFF. |journal=Semin. Immunol. |volume=18 |issue= 5 |pages= 276-83 |year= 2007 |pmid= 16916609 |doi= 10.1016/j.smim.2006.04.003 }}
*{{cite journal | author=Tangye SG, Bryant VL, Cuss AK, Good KL |title=BAFF, APRIL and human B cell disorders. |journal=Semin. Immunol. |volume=18 |issue= 5 |pages= 305-17 |year= 2007 |pmid= 16916610 |doi= 10.1016/j.smim.2006.04.004 }}
*{{cite journal | author=Treml LS, Crowley JE, Cancro MP |title=BLyS receptor signatures resolve homeostatically independent compartments among naïve and antigen-experienced B cells. |journal=Semin. Immunol. |volume=18 |issue= 5 |pages= 297-304 |year= 2007 |pmid= 16919470 |doi= 10.1016/j.smim.2006.07.001 }}
*{{cite journal | author=Woodland RT, Schmidt MR, Thompson CB |title=BLyS and B cell homeostasis. |journal=Semin. Immunol. |volume=18 |issue= 5 |pages= 318-26 |year= 2007 |pmid= 16931037 |doi= 10.1016/j.smim.2006.06.001 }}
*{{cite journal | author=Kalled SL |title=Impact of the BAFF/BR3 axis on B cell survival, germinal center maintenance and antibody production. |journal=Semin. Immunol. |volume=18 |issue= 5 |pages= 290-6 |year= 2007 |pmid= 16931038 |doi= 10.1016/j.smim.2006.06.002 }}
*{{cite journal | author=Mackay F, Leung H |title=The role of the BAFF/APRIL system on T cell function. |journal=Semin. Immunol. |volume=18 |issue= 5 |pages= 284-9 |year= 2007 |pmid= 16931039 |doi= 10.1016/j.smim.2006.04.005 }}
*{{cite journal | author=Bosello S, Pers JO, Rochas C, ''et al.'' |title=BAFF and rheumatic autoimmune disorders: implications for disease management and therapy. |journal=International journal of immunopathology and pharmacology |volume=20 |issue= 1 |pages= 1-8 |year= 2007 |pmid= 17346422 |doi= }}
*{{cite journal | author=Shu HB, Hu WH, Johnson H |title=TALL-1 is a novel member of the TNF family that is down-regulated by mitogens. |journal=J. Leukoc. Biol. |volume=65 |issue= 5 |pages= 680-3 |year= 1999 |pmid= 10331498 |doi= }}
*{{cite journal | author=Mukhopadhyay A, Ni J, Zhai Y, ''et al.'' |title=Identification and characterization of a novel cytokine, THANK, a TNF homologue that activates apoptosis, nuclear factor-kappaB, and c-Jun NH2-terminal kinase. |journal=J. Biol. Chem. |volume=274 |issue= 23 |pages= 15978-81 |year= 1999 |pmid= 10347144 |doi= }}
*{{cite journal | author=Schneider P, MacKay F, Steiner V, ''et al.'' |title=BAFF, a novel ligand of the tumor necrosis factor family, stimulates B cell growth. |journal=J. Exp. Med. |volume=189 |issue= 11 |pages= 1747-56 |year= 1999 |pmid= 10359578 |doi= }}
*{{cite journal | author=Moore PA, Belvedere O, Orr A, ''et al.'' |title=BLyS: member of the tumor necrosis factor family and B lymphocyte stimulator. |journal=Science |volume=285 |issue= 5425 |pages= 260-3 |year= 1999 |pmid= 10398604 |doi= }}
*{{cite journal | author=Tribouley C, Wallroth M, Chan V, ''et al.'' |title=Characterization of a new member of the TNF family expressed on antigen presenting cells. |journal=Biol. Chem. |volume=380 |issue= 12 |pages= 1443-7 |year= 2000 |pmid= 10661873 |doi= }}
*{{cite journal | author=Gross JA, Johnston J, Mudri S, ''et al.'' |title=TACI and BCMA are receptors for a TNF homologue implicated in B-cell autoimmune disease. |journal=Nature |volume=404 |issue= 6781 |pages= 995-9 |year= 2000 |pmid= 10801128 |doi= 10.1038/35010115 }}
*{{cite journal | author=Shu HB, Johnson H |title=B cell maturation protein is a receptor for the tumor necrosis factor family member TALL-1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 16 |pages= 9156-61 |year= 2000 |pmid= 10908663 |doi= 10.1073/pnas.160213497 }}
}}
{{refend}}
{{protein-stub}}
end log.
