Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 19:56, 18 November 2007 (UTC)
[edit]Proteins without matches (7)
[edit]Proteins with a High Potential Match (7)
[edit]Redirected Proteins (11)
[edit]Manual Inspection (Page not found) (14)
[edit]
Protein Status Grid - Date: 19:56, 18 November 2007 (UTC)
[edit]Vebose Log - Date: 19:56, 18 November 2007 (UTC)
[edit]- INFO: Beginning work on ABCG1... {November 18, 2007 11:41:26 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:42:15 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = ATP-binding cassette, sub-family G (WHITE), member 1
| HGNCid = 73
| Symbol = ABCG1
| AltSymbols =; ABC8; MGC34313; WHITE1
| OMIM = 603076
| ECnumber =
| Homologene = 21022
| MGIid = 107704
| GeneAtlas_image1 = PBB_GE_ABCG1_204567_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ABCG1_211113_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0015196 |text = L-tryptophan transmembrane transporter activity}} {{GNF_GO|id=GO:0015216 |text = purine nucleotide transmembrane transporter activity}} {{GNF_GO|id=GO:0015646 |text = transmembrane transporter activity}} {{GNF_GO|id=GO:0016887 |text = ATPase activity}} {{GNF_GO|id=GO:0042626 |text = ATPase activity, coupled to transmembrane movement of substances}} {{GNF_GO|id=GO:0046983 |text = protein dimerization activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006869 |text = lipid transport}} {{GNF_GO|id=GO:0008203 |text = cholesterol metabolic process}} {{GNF_GO|id=GO:0009720 |text = detection of hormone stimulus}} {{GNF_GO|id=GO:0010033 |text = response to organic substance}} {{GNF_GO|id=GO:0042632 |text = cholesterol homeostasis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 9619
| Hs_Ensembl = ENSG00000160179
| Hs_RefseqProtein = NP_004906
| Hs_RefseqmRNA = NM_004915
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 21
| Hs_GenLoc_start = 42509335
| Hs_GenLoc_end = 42590421
| Hs_Uniprot = P45844
| Mm_EntrezGene = 11307
| Mm_Ensembl = ENSMUSG00000024030
| Mm_RefseqmRNA = NM_009593
| Mm_RefseqProtein = NP_033723
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 30784710
| Mm_GenLoc_end = 30842784
| Mm_Uniprot = Q0VDW9
}}
}}
'''ATP-binding cassette, sub-family G (WHITE), member 1''', also known as '''ABCG1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ABCG1 ATP-binding cassette, sub-family G (WHITE), member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9619| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the White subfamily. It is involved in macrophage cholesterol and phospholipids transport, and may regulate cellular lipid homeostasis in other cell types. Several alternative splice variants have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: ABCG1 ATP-binding cassette, sub-family G (WHITE), member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9619| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schmitz G, Langmann T, Heimerl S |title=Role of ABCG1 and other ABCG family members in lipid metabolism. |journal=J. Lipid Res. |volume=42 |issue= 10 |pages= 1513-20 |year= 2002 |pmid= 11590207 |doi= }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal | author=Chen H, Rossier C, Lalioti MD, ''et al.'' |title=Cloning of the cDNA for a human homologue of the Drosophila white gene and mapping to chromosome 21q22.3. |journal=Am. J. Hum. Genet. |volume=59 |issue= 1 |pages= 66-75 |year= 1996 |pmid= 8659545 |doi= }}
*{{cite journal | author=Savary S, Denizot F, Luciani M, ''et al.'' |title=Molecular cloning of a mammalian ABC transporter homologous to Drosophila white gene. |journal=Mamm. Genome |volume=7 |issue= 9 |pages= 673-6 |year= 1996 |pmid= 8703120 |doi= }}
*{{cite journal | author=Croop JM, Tiller GE, Fletcher JA, ''et al.'' |title=Isolation and characterization of a mammalian homolog of the Drosophila white gene. |journal=Gene |volume=185 |issue= 1 |pages= 77-85 |year= 1997 |pmid= 9034316 |doi= }}
*{{cite journal | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi= }}
*{{cite journal | author=Klucken J, Büchler C, Orsó E, ''et al.'' |title=ABCG1 (ABC8), the human homolog of the Drosophila white gene, is a regulator of macrophage cholesterol and phospholipid transport. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 2 |pages= 817-22 |year= 2000 |pmid= 10639163 |doi= }}
*{{cite journal | author=Venkateswaran A, Repa JJ, Lobaccaro JM, ''et al.'' |title=Human white/murine ABC8 mRNA levels are highly induced in lipid-loaded macrophages. A transcriptional role for specific oxysterols. |journal=J. Biol. Chem. |volume=275 |issue= 19 |pages= 14700-7 |year= 2000 |pmid= 10799558 |doi= }}
*{{cite journal | author=Hattori M, Fujiyama A, Taylor TD, ''et al.'' |title=The DNA sequence of human chromosome 21. |journal=Nature |volume=405 |issue= 6784 |pages= 311-9 |year= 2000 |pmid= 10830953 |doi= 10.1038/35012518 }}
*{{cite journal | author=Berry A, Scott HS, Kudoh J, ''et al.'' |title=Refined localization of autosomal recessive nonsyndromic deafness DFNB10 locus using 34 novel microsatellite markers, genomic structure, and exclusion of six known genes in the region. |journal=Genomics |volume=68 |issue= 1 |pages= 22-9 |year= 2001 |pmid= 10950923 |doi= 10.1006/geno.2000.6253 }}
*{{cite journal | author=Langmann T, Porsch-Ozcürümez M, Unkelbach U, ''et al.'' |title=Genomic organization and characterization of the promoter of the human ATP-binding cassette transporter-G1 (ABCG1) gene. |journal=Biochim. Biophys. Acta |volume=1494 |issue= 1-2 |pages= 175-80 |year= 2000 |pmid= 11072082 |doi= }}
*{{cite journal | author=Lorkowski S, Rust S, Engel T, ''et al.'' |title=Genomic sequence and structure of the human ABCG1 (ABC8) gene. |journal=Biochem. Biophys. Res. Commun. |volume=280 |issue= 1 |pages= 121-31 |year= 2001 |pmid= 11162488 |doi= 10.1006/bbrc.2000.4089 }}
*{{cite journal | author=Porsch-Ozcurumez M, Langmann T, Heimerl S, ''et al.'' |title=The zinc finger protein 202 (ZNF202) is a transcriptional repressor of ATP binding cassette transporter A1 (ABCA1) and ABCG1 gene expression and a modulator of cellular lipid efflux. |journal=J. Biol. Chem. |volume=276 |issue= 15 |pages= 12427-33 |year= 2001 |pmid= 11279031 |doi= 10.1074/jbc.M100218200 }}
*{{cite journal | author=Lorkowski S, Kratz M, Wenner C, ''et al.'' |title=Expression of the ATP-binding cassette transporter gene ABCG1 (ABC8) in Tangier disease. |journal=Biochem. Biophys. Res. Commun. |volume=283 |issue= 4 |pages= 821-30 |year= 2001 |pmid= 11350058 |doi= 10.1006/bbrc.2001.4863 }}
*{{cite journal | author=Kennedy MA, Venkateswaran A, Tarr PT, ''et al.'' |title=Characterization of the human ABCG1 gene: liver X receptor activates an internal promoter that produces a novel transcript encoding an alternative form of the protein. |journal=J. Biol. Chem. |volume=276 |issue= 42 |pages= 39438-47 |year= 2001 |pmid= 11500512 |doi= 10.1074/jbc.M105863200 }}
*{{cite journal | author=Kaplan R, Gan X, Menke JG, ''et al.'' |title=Bacterial lipopolysaccharide induces expression of ABCA1 but not ABCG1 via an LXR-independent pathway. |journal=J. Lipid Res. |volume=43 |issue= 6 |pages= 952-9 |year= 2003 |pmid= 12032171 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Cserepes J, Szentpétery Z, Seres L, ''et al.'' |title=Functional expression and characterization of the human ABCG1 and ABCG4 proteins: indications for heterodimerization. |journal=Biochem. Biophys. Res. Commun. |volume=320 |issue= 3 |pages= 860-7 |year= 2004 |pmid= 15240127 |doi= 10.1016/j.bbrc.2004.06.037 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on BUB1B... {November 18, 2007 11:21:50 AM PST}
- SEARCH REDIRECT: Control Box Found: BUB1B {November 18, 2007 11:22:40 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:22:48 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:22:48 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:22:48 AM PST}
- UPDATED: Updated protein page: BUB1B {November 18, 2007 11:23:02 AM PST}
- INFO: Beginning work on CCL7... {November 18, 2007 11:30:47 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:31:51 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CCL7_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bo0.
| PDB = {{PDB2|1bo0}}, {{PDB2|1ncv}}
| Name = Chemokine (C-C motif) ligand 7
| HGNCid = 10634
| Symbol = CCL7
| AltSymbols =; FIC; MARC; MCP-3; MCP3; MGC138463; MGC138465; NC28; SCYA6; SCYA7
| OMIM = 158106
| ECnumber =
| Homologene = 4568
| MGIid = 99512
| GeneAtlas_image1 = PBB_GE_CCL7_208075_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008009 |text = chemokine activity}} {{GNF_GO|id=GO:0008201 |text = heparin binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006874 |text = cellular calcium ion homeostasis}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0019735 |text = antimicrobial humoral response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6354
| Hs_Ensembl = ENSG00000108688
| Hs_RefseqProtein = NP_006264
| Hs_RefseqmRNA = NM_006273
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 29621354
| Hs_GenLoc_end = 29623373
| Hs_Uniprot = P80098
| Mm_EntrezGene = 20306
| Mm_Ensembl = ENSMUSG00000035373
| Mm_RefseqmRNA = NM_013654
| Mm_RefseqProtein = NP_038682
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 81861909
| Mm_GenLoc_end = 81863714
| Mm_Uniprot = Q5SVU0
}}
}}
'''Chemokine (C-C motif) ligand 7''', also known as '''CCL7''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CCL7 chemokine (C-C motif) ligand 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6354| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes monocyte chemotactic protein 3, a secreted chemokine which attracts macrophages during inflammation and metastasis. It is a member of the C-C subfamily of chemokines which are characterized by having two adjacent cysteine residues. The protein is an in vivo substrate of matrix metalloproteinase 2, an enzyme which degrades components of the extracellular matrix. This gene is part of a cluster of C-C chemokine family members on chromosome 17q.<ref name="entrez">{{cite web | title = Entrez Gene: CCL7 chemokine (C-C motif) ligand 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6354| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Menten P, Wuyts A, Van Damme J |title=Monocyte chemotactic protein-3. |journal=Eur. Cytokine Netw. |volume=12 |issue= 4 |pages= 554-60 |year= 2002 |pmid= 11781181 |doi= }}
*{{cite journal | author=Van Damme J, Proost P, Lenaerts JP, Opdenakker G |title=Structural and functional identification of two human, tumor-derived monocyte chemotactic proteins (MCP-2 and MCP-3) belonging to the chemokine family. |journal=J. Exp. Med. |volume=176 |issue= 1 |pages= 59-65 |year= 1992 |pmid= 1613466 |doi= }}
*{{cite journal | author=Ben-Baruch A, Xu L, Young PR, ''et al.'' |title=Monocyte chemotactic protein-3 (MCP3) interacts with multiple leukocyte receptors. C-C CKR1, a receptor for macrophage inflammatory protein-1 alpha/Rantes, is also a functional receptor for MCP3. |journal=J. Biol. Chem. |volume=270 |issue= 38 |pages= 22123-8 |year= 1995 |pmid= 7545673 |doi= }}
*{{cite journal | author=Opdenakker G, Fiten P, Nys G, ''et al.'' |title=The human MCP-3 gene (SCYA7): cloning, sequence analysis, and assignment to the C-C chemokine gene cluster on chromosome 17q11.2-q12. |journal=Genomics |volume=21 |issue= 2 |pages= 403-8 |year= 1994 |pmid= 7916328 |doi= 10.1006/geno.1994.1283 }}
*{{cite journal | author=Minty A, Chalon P, Guillemot JC, ''et al.'' |title=Molecular cloning of the MCP-3 chemokine gene and regulation of its expression. |journal=Eur. Cytokine Netw. |volume=4 |issue= 2 |pages= 99-110 |year= 1993 |pmid= 8318676 |doi= }}
*{{cite journal | author=Opdenakker G, Froyen G, Fiten P, ''et al.'' |title=Human monocyte chemotactic protein-3 (MCP-3): molecular cloning of the cDNA and comparison with other chemokines. |journal=Biochem. Biophys. Res. Commun. |volume=191 |issue= 2 |pages= 535-42 |year= 1993 |pmid= 8461011 |doi= }}
*{{cite journal | author=Combadiere C, Ahuja SK, Van Damme J, ''et al.'' |title=Monocyte chemoattractant protein-3 is a functional ligand for CC chemokine receptors 1 and 2B. |journal=J. Biol. Chem. |volume=270 |issue= 50 |pages= 29671-5 |year= 1996 |pmid= 8530354 |doi= }}
*{{cite journal | author=Power CA, Clemetson JM, Clemetson KJ, Wells TN |title=Chemokine and chemokine receptor mRNA expression in human platelets. |journal=Cytokine |volume=7 |issue= 6 |pages= 479-82 |year= 1996 |pmid= 8580362 |doi= 10.1006/cyto.1995.0065 }}
*{{cite journal | author=Daugherty BL, Siciliano SJ, DeMartino JA, ''et al.'' |title=Cloning, expression, and characterization of the human eosinophil eotaxin receptor. |journal=J. Exp. Med. |volume=183 |issue= 5 |pages= 2349-54 |year= 1996 |pmid= 8642344 |doi= }}
*{{cite journal | author=Kim KS, Rajarathnam K, Clark-Lewis I, Sykes BD |title=Structural characterization of a monomeric chemokine: monocyte chemoattractant protein-3. |journal=FEBS Lett. |volume=395 |issue= 2-3 |pages= 277-82 |year= 1996 |pmid= 8898111 |doi= }}
*{{cite journal | author=Meunier S, Bernassau JM, Guillemot JC, ''et al.'' |title=Determination of the three-dimensional structure of CC chemokine monocyte chemoattractant protein 3 by 1H two-dimensional NMR spectroscopy. |journal=Biochemistry |volume=36 |issue= 15 |pages= 4412-22 |year= 1997 |pmid= 9109648 |doi= 10.1021/bi9627929 }}
*{{cite journal | author=Polentarutti N, Introna M, Sozzani S, ''et al.'' |title=Expression of monocyte chemotactic protein-3 in human monocytes and endothelial cells. |journal=Eur. Cytokine Netw. |volume=8 |issue= 3 |pages= 271-4 |year= 1997 |pmid= 9346360 |doi= }}
*{{cite journal | author=Bonini JA, Martin SK, Dralyuk F, ''et al.'' |title=Cloning, expression, and chromosomal mapping of a novel human CC-chemokine receptor (CCR10) that displays high-affinity binding for MCP-1 and MCP-3. |journal=DNA Cell Biol. |volume=16 |issue= 10 |pages= 1249-56 |year= 1997 |pmid= 9364936 |doi= }}
*{{cite journal | author=Nibbs RJ, Wylie SM, Yang J, ''et al.'' |title=Cloning and characterization of a novel promiscuous human beta-chemokine receptor D6. |journal=J. Biol. Chem. |volume=272 |issue= 51 |pages= 32078-83 |year= 1998 |pmid= 9405404 |doi= }}
*{{cite journal | author=Wang JM, Ueda H, Howard OM, ''et al.'' |title=HIV-1 envelope gp120 inhibits the monocyte response to chemokines through CD4 signal-dependent chemokine receptor down-regulation. |journal=J. Immunol. |volume=161 |issue= 8 |pages= 4309-17 |year= 1998 |pmid= 9780207 |doi= }}
*{{cite journal | author=Albini A, Ferrini S, Benelli R, ''et al.'' |title=HIV-1 Tat protein mimicry of chemokines. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 22 |pages= 13153-8 |year= 1998 |pmid= 9789057 |doi= }}
*{{cite journal | author=Rabin RL, Park MK, Liao F, ''et al.'' |title=Chemokine receptor responses on T cells are achieved through regulation of both receptor expression and signaling. |journal=J. Immunol. |volume=162 |issue= 7 |pages= 3840-50 |year= 1999 |pmid= 10201901 |doi= }}
*{{cite journal | author=Wedemeyer J, Lorentz A, Göke M, ''et al.'' |title=Enhanced production of monocyte chemotactic protein 3 in inflammatory bowel disease mucosa. |journal=Gut |volume=44 |issue= 5 |pages= 629-35 |year= 1999 |pmid= 10205198 |doi= }}
*{{cite journal | author=Blanpain C, Migeotte I, Lee B, ''et al.'' |title=CCR5 binds multiple CC-chemokines: MCP-3 acts as a natural antagonist. |journal=Blood |volume=94 |issue= 6 |pages= 1899-905 |year= 1999 |pmid= 10477718 |doi= }}
*{{cite journal | author=Jordan NJ, Kolios G, Abbot SE, ''et al.'' |title=Expression of functional CXCR4 chemokine receptors on human colonic epithelial cells. |journal=J. Clin. Invest. |volume=104 |issue= 8 |pages= 1061-9 |year= 1999 |pmid= 10525044 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CD163... {November 18, 2007 11:40:01 AM PST}
- SEARCH REDIRECT: Control Box Found: CD163 {November 18, 2007 11:41:06 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:41:13 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:41:13 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:41:13 AM PST}
- UPDATED: Updated protein page: CD163 {November 18, 2007 11:41:25 AM PST}
- INFO: Beginning work on CFB... {November 18, 2007 11:20:50 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:21:49 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CFB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dle.
| PDB = {{PDB2|1dle}}, {{PDB2|1q0p}}, {{PDB2|1rrk}}, {{PDB2|1rs0}}, {{PDB2|1rtk}}, {{PDB2|2ok5}}
| Name = Complement factor B
| HGNCid = 1037
| Symbol = CFB
| AltSymbols =; BF; BFD; CFAB; GBG; H2-Bf; PBF2
| OMIM = 138470
| ECnumber =
| Homologene = 1292
| MGIid = 105975
| GeneAtlas_image1 = PBB_GE_CFB_202357_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CFB_211920_at_tn.png
| Function = {{GNF_GO|id=GO:0001848 |text = complement binding}} {{GNF_GO|id=GO:0003812 |text = alternative-complement-pathway C3/C5 convertase activity}} {{GNF_GO|id=GO:0004252 |text = serine-type endopeptidase activity}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006956 |text = complement activation}} {{GNF_GO|id=GO:0006957 |text = complement activation, alternative pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 629
| Hs_Ensembl = ENSG00000166285
| Hs_RefseqProtein = NP_001701
| Hs_RefseqmRNA = NM_001710
| Hs_GenLoc_db =
| Hs_GenLoc_chr = c6_COX
| Hs_GenLoc_start = 32048579
| Hs_GenLoc_end = 32054666
| Hs_Uniprot = P00751
| Mm_EntrezGene = 14962
| Mm_Ensembl = ENSMUSG00000024371
| Mm_RefseqmRNA = NM_008198
| Mm_RefseqProtein = NP_032224
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 34464437
| Mm_GenLoc_end = 34470273
| Mm_Uniprot = Q3U925
}}
}}
'''Complement factor B''', also known as '''CFB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CFB complement factor B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=629| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes complement factor B, a component of the alternative pathway of complement activation. Factor B circulates in the blood as a single chain polypeptide. Upon activation of the alternative pathway, it is cleaved by complement factor D yielding the noncatalytic chain Ba and the catalytic subunit Bb. The active subunit Bb is a serine protease which associates with C3b to form the alternative pathway C3 convertase. Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation. This gene localizes to the major histocompatibility complex (MHC) class III region on chromosome 6. This cluster includes several genes involved in regulation of the immune reaction. The polyadenylation site of this gene is 421 bp from the 5' end of the gene for complement component 2.<ref name="entrez">{{cite web | title = Entrez Gene: CFB complement factor B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=629| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Campbell RD |title=The molecular genetics and polymorphism of C2 and factor B. |journal=Br. Med. Bull. |volume=43 |issue= 1 |pages= 37-49 |year= 1988 |pmid= 3315100 |doi= }}
*{{cite journal | author=Campbell RD, Bentley DR, Morley BJ |title=The factor B and C2 genes. |journal=Philos. Trans. R. Soc. Lond., B, Biol. Sci. |volume=306 |issue= 1129 |pages= 367-78 |year= 1984 |pmid= 6149579 |doi= }}
*{{cite journal | author=Yu CY |title=Molecular genetics of the human MHC complement gene cluster. |journal=Exp. Clin. Immunogenet. |volume=15 |issue= 4 |pages= 213-30 |year= 1999 |pmid= 10072631 |doi= }}
*{{cite journal | author=Rawal N, Pangburn MK |title=Structure/function of C5 convertases of complement. |journal=Int. Immunopharmacol. |volume=1 |issue= 3 |pages= 415-22 |year= 2001 |pmid= 11367526 |doi= }}
*{{cite journal | author=Arnason A, Larsen B, Marshall WH, ''et al.'' |title=Very close linkage between HLA-B and Bf inferred from allelic association. |journal=Nature |volume=268 |issue= 5620 |pages= 527-8 |year= 1977 |pmid= 889587 |doi= }}
*{{cite journal | author=Barnum SR, Ishii Y, Agrawal A, Volanakis JE |title=Production and interferon-gamma-mediated regulation of complement component C2 and factors B and D by the astroglioma cell line U105-MG. |journal=Biochem. J. |volume=287 ( Pt 2) |issue= |pages= 595-601 |year= 1992 |pmid= 1445220 |doi= }}
*{{cite journal | author=Yancey KB, Overholser O, Domloge-Hultsch N, ''et al.'' |title=Human keratinocytes and A-431 cells synthesize and secrete factor B, the major zymogen protease of the alternative complement pathway. |journal=J. Invest. Dermatol. |volume=98 |issue= 3 |pages= 379-83 |year= 1992 |pmid= 1545147 |doi= }}
*{{cite journal | author=Niemann MA, Bhown AS, Miller EJ |title=The principal site of glycation of human complement factor B. |journal=Biochem. J. |volume=274 ( Pt 2) |issue= |pages= 473-80 |year= 1991 |pmid= 2006911 |doi= }}
*{{cite journal | author=Davrinche C, Abbal M, Clerc A |title=Molecular characterization of human complement factor B subtypes. |journal=Immunogenetics |volume=32 |issue= 5 |pages= 309-12 |year= 1991 |pmid= 2249879 |doi= }}
*{{cite journal | author=Farries TC, Lachmann PJ, Harrison RA |title=Analysis of the interaction between properdin and factor B, components of the alternative-pathway C3 convertase of complement. |journal=Biochem. J. |volume=253 |issue= 3 |pages= 667-75 |year= 1988 |pmid= 3140783 |doi= }}
*{{cite journal | author=Wu LC, Morley BJ, Campbell RD |title=Cell-specific expression of the human complement protein factor B gene: evidence for the role of two distinct 5'-flanking elements. |journal=Cell |volume=48 |issue= 2 |pages= 331-42 |year= 1987 |pmid= 3643061 |doi= }}
*{{cite journal | author=Campbell RD, Porter RR |title=Molecular cloning and characterization of the gene coding for human complement protein factor B. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=80 |issue= 14 |pages= 4464-8 |year= 1983 |pmid= 6308626 |doi= }}
*{{cite journal | author=Morley BJ, Campbell RD |title=Internal homologies of the Ba fragment from human complement component Factor B, a class III MHC antigen. |journal=EMBO J. |volume=3 |issue= 1 |pages= 153-7 |year= 1984 |pmid= 6323161 |doi= }}
*{{cite journal | author=Christie DL, Gagnon J |title=Amino acid sequence of the Bb fragment from complement Factor B. Sequence of the major cyanogen bromide-cleavage peptide (CB-II) and completion of the sequence of the Bb fragment. |journal=Biochem. J. |volume=209 |issue= 1 |pages= 61-70 |year= 1983 |pmid= 6342610 |doi= }}
*{{cite journal | author=Mole JE, Anderson JK, Davison EA, Woods DE |title=Complete primary structure for the zymogen of human complement factor B. |journal=J. Biol. Chem. |volume=259 |issue= 6 |pages= 3407-12 |year= 1984 |pmid= 6546754 |doi= }}
*{{cite journal | author=Woods DE, Markham AF, Ricker AT, ''et al.'' |title=Isolation of cDNA clones for the human complement protein factor B, a class III major histocompatibility complex gene product. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=79 |issue= 18 |pages= 5661-5 |year= 1982 |pmid= 6957884 |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=Mejía JE, Jahn I, de la Salle H, Hauptmann G |title=Human factor B. Complete cDNA sequence of the BF*S allele. |journal=Hum. Immunol. |volume=39 |issue= 1 |pages= 49-53 |year= 1994 |pmid= 8181962 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DIO2... {November 18, 2007 11:23:58 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:24:39 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Deiodinase, iodothyronine, type II
| HGNCid = 2884
| Symbol = DIO2
| AltSymbols =; 5DII; D2; SelY; TXDI2
| OMIM = 601413
| ECnumber =
| Homologene = 621
| MGIid = 1338833
| Function = {{GNF_GO|id=GO:0004800 |text = thyroxine 5'-deiodinase activity}} {{GNF_GO|id=GO:0008430 |text = selenium binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0001514 |text = selenocysteine incorporation}} {{GNF_GO|id=GO:0006590 |text = thyroid hormone generation}} {{GNF_GO|id=GO:0042446 |text = hormone biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1734
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000784
| Hs_RefseqmRNA = NM_000793
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 13371
| Mm_Ensembl = ENSMUSG00000007682
| Mm_RefseqmRNA = NM_010050
| Mm_RefseqProtein = NP_034180
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 91134815
| Mm_GenLoc_end = 91143674
| Mm_Uniprot = Q05A70
}}
}}
'''Deiodinase, iodothyronine, type II''', also known as '''DIO2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DIO2 deiodinase, iodothyronine, type II| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1734| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene belongs to the iodothyronine deiodinase family. It activates thyroid hormone by converting the prohormone thyroxine (T4) by outer ring deiodination (ORD) to bioactive 3,3',5-triiodothyronine (T3). It is highly expressed in the thyroid, and may contribute significantly to the relative increase in thyroidal T3 production in patients with Graves disease and thyroid adenomas. This protein contains selenocysteine (Sec) residues encoded by the UGA codon, which normally signals translation termination. The 3' UTR of Sec-containing genes have a common stem-loop structure, the sec insertion sequence (SECIS), which is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Alternative splicing results in multiple transcript variants encoding different isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: DIO2 deiodinase, iodothyronine, type II| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1734| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Gereben B, Salvatore D |title=Pretranslational regulation of type 2 deiodinase. |journal=Thyroid |volume=15 |issue= 8 |pages= 855-64 |year= 2006 |pmid= 16131328 |doi= 10.1089/thy.2005.15.855 }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal | author=Croteau W, Davey JC, Galton VA, St Germain DL |title=Cloning of the mammalian type II iodothyronine deiodinase. A selenoprotein differentially expressed and regulated in human and rat brain and other tissues. |journal=J. Clin. Invest. |volume=98 |issue= 2 |pages= 405-17 |year= 1996 |pmid= 8755651 |doi= }}
*{{cite journal | author=Salvatore D, Tu H, Harney JW, Larsen PR |title=Type 2 iodothyronine deiodinase is highly expressed in human thyroid. |journal=J. Clin. Invest. |volume=98 |issue= 4 |pages= 962-8 |year= 1996 |pmid= 8770868 |doi= }}
*{{cite journal | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi= }}
*{{cite journal | author=Buettner C, Harney JW, Larsen PR |title=The 3'-untranslated region of human type 2 iodothyronine deiodinase mRNA contains a functional selenocysteine insertion sequence element. |journal=J. Biol. Chem. |volume=273 |issue= 50 |pages= 33374-8 |year= 1999 |pmid= 9837913 |doi= }}
*{{cite journal | author=Araki O, Murakami M, Morimura T, ''et al.'' |title=Assignment of type II iodothyronine deiodinase gene (DIO2) to human chromosome band 14q24.2-->q24.3 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=84 |issue= 1-2 |pages= 73-4 |year= 1999 |pmid= 10343107 |doi= }}
*{{cite journal | author=Bartha T, Kim SW, Salvatore D, ''et al.'' |title=Characterization of the 5'-flanking and 5'-untranslated regions of the cyclic adenosine 3',5'-monophosphate-responsive human type 2 iodothyronine deiodinase gene. |journal=Endocrinology |volume=141 |issue= 1 |pages= 229-37 |year= 2000 |pmid= 10614643 |doi= }}
*{{cite journal | author=Baqui MM, Gereben B, Harney JW, ''et al.'' |title=Distinct subcellular localization of transiently expressed types 1 and 2 iodothyronine deiodinases as determined by immunofluorescence confocal microscopy. |journal=Endocrinology |volume=141 |issue= 11 |pages= 4309-12 |year= 2000 |pmid= 11089566 |doi= }}
*{{cite journal | author=Ohba K, Yoshioka T, Muraki T |title=Identification of two novel splicing variants of human type II iodothyronine deiodinase mRNA. |journal=Mol. Cell. Endocrinol. |volume=172 |issue= 1-2 |pages= 169-75 |year= 2001 |pmid= 11165050 |doi= }}
*{{cite journal | author=Imai Y, Toyoda N, Maeda A, ''et al.'' |title=Type 2 iodothyronine deiodinase expression is upregulated by the protein kinase A-dependent pathway and is downregulated by the protein kinase C-dependent pathway in cultured human thyroid cells. |journal=Thyroid |volume=11 |issue= 10 |pages= 899-907 |year= 2002 |pmid= 11716036 |doi= 10.1089/105072501753210957 }}
*{{cite journal | author=Molnár I, Balázs C, Szegedi G, Sipka S |title=Inhibition of type 2,5'-deiodinase by tumor necrosis factor alpha, interleukin-6 and interferon gamma in human thyroid tissue. |journal=Immunol. Lett. |volume=80 |issue= 1 |pages= 3-7 |year= 2002 |pmid= 11716958 |doi= }}
*{{cite journal | author=Kuiper GG, Klootwijk W, Visser TJ |title=Substitution of cysteine for a conserved alanine residue in the catalytic center of type II iodothyronine deiodinase alters interaction with reducing cofactor. |journal=Endocrinology |volume=143 |issue= 4 |pages= 1190-8 |year= 2002 |pmid= 11897672 |doi= }}
*{{cite journal | author=Gereben B, Kollár A, Harney JW, Larsen PR |title=The mRNA structure has potent regulatory effects on type 2 iodothyronine deiodinase expression. |journal=Mol. Endocrinol. |volume=16 |issue= 7 |pages= 1667-79 |year= 2003 |pmid= 12089359 |doi= }}
*{{cite journal | author=Baur A, Buchfelder M, Köhrle J |title=Expression of 5'-deiodinase enzymes in normal pituitaries and in various human pituitary adenomas. |journal=Eur. J. Endocrinol. |volume=147 |issue= 2 |pages= 263-8 |year= 2002 |pmid= 12153750 |doi= }}
*{{cite journal | author=Botero D, Gereben B, Goncalves C, ''et al.'' |title=Ubc6p and ubc7p are required for normal and substrate-induced endoplasmic reticulum-associated degradation of the human selenoprotein type 2 iodothyronine monodeiodinase. |journal=Mol. Endocrinol. |volume=16 |issue= 9 |pages= 1999-2007 |year= 2003 |pmid= 12198238 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Curcio-Morelli C, Gereben B, Zavacki AM, ''et al.'' |title=In vivo dimerization of types 1, 2, and 3 iodothyronine selenodeiodinases. |journal=Endocrinology |volume=144 |issue= 3 |pages= 937-46 |year= 2003 |pmid= 12586771 |doi= }}
*{{cite journal | author=Ambroziak M, Pachucki J, Chojnowski K, ''et al.'' |title=Pax-8 expression correlates with type II 5' deiodinase expression in thyroids from patients with Graves' disease. |journal=Thyroid |volume=13 |issue= 2 |pages= 141-8 |year= 2003 |pmid= 12699588 |doi= 10.1089/105072503321319440 }}
*{{cite journal | author=Dentice M, Morisco C, Vitale M, ''et al.'' |title=The different cardiac expression of the type 2 iodothyronine deiodinase gene between human and rat is related to the differential response of the Dio2 genes to Nkx-2.5 and GATA-4 transcription factors. |journal=Mol. Endocrinol. |volume=17 |issue= 8 |pages= 1508-21 |year= 2004 |pmid= 12775767 |doi= 10.1210/me.2002-0348 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DNM2... {November 18, 2007 11:24:39 AM PST}
- SEARCH REDIRECT: Control Box Found: DNM2 {November 18, 2007 11:25:34 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:25:42 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:25:42 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:25:42 AM PST}
- UPDATED: Updated protein page: DNM2 {November 18, 2007 11:25:53 AM PST}
- INFO: Beginning work on GRB7... {November 18, 2007 11:26:49 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:27:27 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_GRB7_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1mw4.
| PDB = {{PDB2|1mw4}}, {{PDB2|1wgr}}
| Name = Growth factor receptor-bound protein 7
| HGNCid = 4567
| Symbol = GRB7
| AltSymbols =;
| OMIM = 601522
| ECnumber =
| Homologene = 3881
| MGIid = 102683
| GeneAtlas_image1 = PBB_GE_GRB7_210761_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005070 |text = SH3/SH2 adaptor activity}}
| Component =
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007173 |text = epidermal growth factor receptor signaling pathway}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2886
| Hs_Ensembl = ENSG00000141738
| Hs_RefseqProtein = NP_001025173
| Hs_RefseqmRNA = NM_001030002
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 35147713
| Hs_GenLoc_end = 35157061
| Hs_Uniprot = Q14451
| Mm_EntrezGene = 14786
| Mm_Ensembl = ENSMUSG00000019312
| Mm_RefseqmRNA = NM_010346
| Mm_RefseqProtein = NP_034476
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 98262929
| Mm_GenLoc_end = 98271460
| Mm_Uniprot = Q3TH55
}}
}}
'''Growth factor receptor-bound protein 7''', also known as '''GRB7''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GRB7 growth factor receptor-bound protein 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2886| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The product of this gene belongs to a small family of adapter proteins that are known to interact with a number of receptor tyrosine kinases and signaling molecules. This gene encodes a growth factor receptor-binding protein that interacts with epidermal growth factor receptor (EGFR) and ephrin receptors. The protein plays a role in the integrin signaling pathway and cell migration by binding with focal adhesion kinase (FAK). Alternative splicing results in multiple transcript variants encoding different isoforms, although the full-length natures of only two of the variants have been determined to date.<ref name="entrez">{{cite web | title = Entrez Gene: GRB7 growth factor receptor-bound protein 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2886| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Han DC, Shen TL, Guan JL |title=The Grb7 family proteins: structure, interactions with other signaling molecules and potential cellular functions. |journal=Oncogene |volume=20 |issue= 44 |pages= 6315-21 |year= 2001 |pmid= 11607834 |doi= 10.1038/sj.onc.1204775 }}
*{{cite journal | author=Margolis B, Silvennoinen O, Comoglio F, ''et al.'' |title=High-efficiency expression/cloning of epidermal growth factor-receptor-binding proteins with Src homology 2 domains. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 19 |pages= 8894-8 |year= 1992 |pmid= 1409582 |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=Pandey A, Liu X, Dixon JE, ''et al.'' |title=Direct association between the Ret receptor tyrosine kinase and the Src homology 2-containing adapter protein Grb7. |journal=J. Biol. Chem. |volume=271 |issue= 18 |pages= 10607-10 |year= 1996 |pmid= 8631863 |doi= }}
*{{cite journal | author=Yokote K, Margolis B, Heldin CH, Claesson-Welsh L |title=Grb7 is a downstream signaling component of platelet-derived growth factor alpha- and beta-receptors. |journal=J. Biol. Chem. |volume=271 |issue= 48 |pages= 30942-9 |year= 1997 |pmid= 8940081 |doi= }}
*{{cite journal | author=Tanaka S, Mori M, Akiyoshi T, ''et al.'' |title=Coexpression of Grb7 with epidermal growth factor receptor or Her2/erbB2 in human advanced esophageal carcinoma. |journal=Cancer Res. |volume=57 |issue= 1 |pages= 28-31 |year= 1997 |pmid= 8988034 |doi= }}
*{{cite journal | author=Janes PW, Lackmann M, Church WB, ''et al.'' |title=Structural determinants of the interaction between the erbB2 receptor and the Src homology 2 domain of Grb7. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8490-7 |year= 1997 |pmid= 9079677 |doi= }}
*{{cite journal | author=Kishi T, Sasaki H, Akiyama N, ''et al.'' |title=Molecular cloning of human GRB-7 co-amplified with CAB1 and c-ERBB-2 in primary gastric cancer. |journal=Biochem. Biophys. Res. Commun. |volume=232 |issue= 1 |pages= 5-9 |year= 1997 |pmid= 9125150 |doi= 10.1006/bbrc.1997.6218 }}
*{{cite journal | author=Dong LQ, Du H, Porter SG, ''et al.'' |title=Cloning, chromosome localization, expression, and characterization of an Src homology 2 and pleckstrin homology domain-containing insulin receptor binding protein hGrb10gamma. |journal=J. Biol. Chem. |volume=272 |issue= 46 |pages= 29104-12 |year= 1997 |pmid= 9360986 |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=Fiddes RJ, Campbell DH, Janes PW, ''et al.'' |title=Analysis of Grb7 recruitment by heregulin-activated erbB receptors reveals a novel target selectivity for erbB3. |journal=J. Biol. Chem. |volume=273 |issue= 13 |pages= 7717-24 |year= 1998 |pmid= 9516479 |doi= }}
*{{cite journal | author=Tanaka S, Mori M, Akiyoshi T, ''et al.'' |title=A novel variant of human Grb7 is associated with invasive esophageal carcinoma. |journal=J. Clin. Invest. |volume=102 |issue= 4 |pages= 821-7 |year= 1998 |pmid= 9710451 |doi= }}
*{{cite journal | author=Thömmes K, Lennartsson J, Carlberg M, Rönnstrand L |title=Identification of Tyr-703 and Tyr-936 as the primary association sites for Grb2 and Grb7 in the c-Kit/stem cell factor receptor. |journal=Biochem. J. |volume=341 ( Pt 1) |issue= |pages= 211-6 |year= 1999 |pmid= 10377264 |doi= }}
*{{cite journal | author=Han DC, Guan JL |title=Association of focal adhesion kinase with Grb7 and its role in cell migration. |journal=J. Biol. Chem. |volume=274 |issue= 34 |pages= 24425-30 |year= 1999 |pmid= 10446223 |doi= }}
*{{cite journal | author=Jones N, Master Z, Jones J, ''et al.'' |title=Identification of Tek/Tie2 binding partners. Binding to a multifunctional docking site mediates cell survival and migration. |journal=J. Biol. Chem. |volume=274 |issue= 43 |pages= 30896-905 |year= 1999 |pmid= 10521483 |doi= }}
*{{cite journal | author=Vayssière B, Zalcman G, Mahé Y, ''et al.'' |title=Interaction of the Grb7 adapter protein with Rnd1, a new member of the Rho family. |journal=FEBS Lett. |volume=467 |issue= 1 |pages= 91-6 |year= 2000 |pmid= 10664463 |doi= }}
*{{cite journal | author=Kasus-Jacobi A, Béréziat V, Perdereau D, ''et al.'' |title=Evidence for an interaction between the insulin receptor and Grb7. A role for two of its binding domains, PIR and SH2. |journal=Oncogene |volume=19 |issue= 16 |pages= 2052-9 |year= 2000 |pmid= 10803466 |doi= 10.1038/sj.onc.1203469 }}
*{{cite journal | author=Han DC, Shen TL, Guan JL |title=Role of Grb7 targeting to focal contacts and its phosphorylation by focal adhesion kinase in regulation of cell migration. |journal=J. Biol. Chem. |volume=275 |issue= 37 |pages= 28911-7 |year= 2000 |pmid= 10893408 |doi= 10.1074/jbc.M001997200 }}
*{{cite journal | author=Lee H, Volonte D, Galbiati F, ''et al.'' |title=Constitutive and growth factor-regulated phosphorylation of caveolin-1 occurs at the same site (Tyr-14) in vivo: identification of a c-Src/Cav-1/Grb7 signaling cassette. |journal=Mol. Endocrinol. |volume=14 |issue= 11 |pages= 1750-75 |year= 2001 |pmid= 11075810 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HDAC5... {November 18, 2007 11:44:23 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:45:51 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Histone deacetylase 5
| HGNCid = 14068
| Symbol = HDAC5
| AltSymbols =; FLJ90614; HD5; NY-CO-9
| OMIM = 605315
| ECnumber =
| Homologene = 3995
| MGIid = 1333784
| GeneAtlas_image1 = PBB_GE_HDAC5_202455_at_tn.png
| Function = {{GNF_GO|id=GO:0003714 |text = transcription corepressor activity}} {{GNF_GO|id=GO:0004407 |text = histone deacetylase activity}} {{GNF_GO|id=GO:0008134 |text = transcription factor binding}} {{GNF_GO|id=GO:0016566 |text = specific transcriptional repressor activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0000118 |text = histone deacetylase complex}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0016604 |text = nuclear body}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006338 |text = chromatin remodeling}} {{GNF_GO|id=GO:0006342 |text = chromatin silencing}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0030183 |text = B cell differentiation}} {{GNF_GO|id=GO:0045843 |text = negative regulation of striated muscle development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10014
| Hs_Ensembl = ENSG00000108840
| Hs_RefseqProtein = NP_001015053
| Hs_RefseqmRNA = NM_001015053
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 39509647
| Hs_GenLoc_end = 39556540
| Hs_Uniprot = Q9UQL6
| Mm_EntrezGene = 15184
| Mm_Ensembl = ENSMUSG00000008855
| Mm_RefseqmRNA = NM_001077696
| Mm_RefseqProtein = NP_001071164
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 102011839
| Mm_GenLoc_end = 102046214
| Mm_Uniprot = Q3TSM2
}}
}}
'''Histone deacetylase 5''', also known as '''HDAC5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HDAC5 histone deacetylase 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10014| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Histones play a critical role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation alters chromosome structure and affects transcription factor access to DNA. The protein encoded by this gene belongs to the class II histone deacetylase/acuc/apha family. It possesses histone deacetylase activity and represses transcription when tethered to a promoter. It coimmunoprecipitates only with HDAC3 family member and might form multicomplex proteins. It also interacts with myocyte enhancer factor-2 (MEF2) proteins, resulting in repression of MEF2-dependent genes. This gene is thought to be associated with colon cancer. Two transcript variants encoding different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: HDAC5 histone deacetylase 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10014| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nakajima D, Okazaki N, Yamakawa H, ''et al.'' |title=Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. |journal=DNA Res. |volume=9 |issue= 3 |pages= 99-106 |year= 2003 |pmid= 12168954 |doi= }}
*{{cite journal | author=Verdin E, Dequiedt F, Kasler HG |title=Class II histone deacetylases: versatile regulators. |journal=Trends Genet. |volume=19 |issue= 5 |pages= 286-93 |year= 2003 |pmid= 12711221 |doi= }}
*{{cite journal | author=Scanlan MJ, Chen YT, Williamson B, ''et al.'' |title=Characterization of human colon cancer antigens recognized by autologous antibodies. |journal=Int. J. Cancer |volume=76 |issue= 5 |pages= 652-8 |year= 1998 |pmid= 9610721 |doi= }}
*{{cite journal | author=Nagase T, Ishikawa K, Miyajima N, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. |journal=DNA Res. |volume=5 |issue= 1 |pages= 31-9 |year= 1998 |pmid= 9628581 |doi= }}
*{{cite journal | author=Grozinger CM, Hassig CA, Schreiber SL |title=Three proteins define a class of human histone deacetylases related to yeast Hda1p. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 9 |pages= 4868-73 |year= 1999 |pmid= 10220385 |doi= }}
*{{cite journal | author=Huang EY, Zhang J, Miska EA, ''et al.'' |title=Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway. |journal=Genes Dev. |volume=14 |issue= 1 |pages= 45-54 |year= 2000 |pmid= 10640275 |doi= }}
*{{cite journal | author=Lemercier C, Verdel A, Galloo B, ''et al.'' |title=mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity. |journal=J. Biol. Chem. |volume=275 |issue= 20 |pages= 15594-9 |year= 2000 |pmid= 10748098 |doi= 10.1074/jbc.M908437199 }}
*{{cite journal | author=Grozinger CM, Schreiber SL |title=Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 14 |pages= 7835-40 |year= 2000 |pmid= 10869435 |doi= 10.1073/pnas.140199597 }}
*{{cite journal | author=Huynh KD, Fischle W, Verdin E, Bardwell VJ |title=BCoR, a novel corepressor involved in BCL-6 repression. |journal=Genes Dev. |volume=14 |issue= 14 |pages= 1810-23 |year= 2000 |pmid= 10898795 |doi= }}
*{{cite journal | author=Mahlknecht U, Schnittger S, Ottmann OG, ''et al.'' |title=Chromosomal organization and localization of the human histone deacetylase 5 gene (HDAC5). |journal=Biochim. Biophys. Acta |volume=1493 |issue= 3 |pages= 342-8 |year= 2000 |pmid= 11018260 |doi= }}
*{{cite journal | author=Zhang CL, McKinsey TA, Lu JR, Olson EN |title=Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor. |journal=J. Biol. Chem. |volume=276 |issue= 1 |pages= 35-9 |year= 2001 |pmid= 11022042 |doi= 10.1074/jbc.M007364200 }}
*{{cite journal | author=McKinsey TA, Zhang CL, Lu J, Olson EN |title=Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation. |journal=Nature |volume=408 |issue= 6808 |pages= 106-11 |year= 2000 |pmid= 11081517 |doi= 10.1038/35040593 }}
*{{cite journal | author=McKinsey TA, Zhang CL, Olson EN |title=Activation of the myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase-stimulated binding of 14-3-3 to histone deacetylase 5. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 26 |pages= 14400-5 |year= 2001 |pmid= 11114197 |doi= 10.1073/pnas.260501497 }}
*{{cite journal | author=Fischle W, Dequiedt F, Fillion M, ''et al.'' |title=Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo. |journal=J. Biol. Chem. |volume=276 |issue= 38 |pages= 35826-35 |year= 2001 |pmid= 11466315 |doi= 10.1074/jbc.M104935200 }}
*{{cite journal | author=McKinsey TA, Zhang CL, Olson EN |title=Identification of a signal-responsive nuclear export sequence in class II histone deacetylases. |journal=Mol. Cell. Biol. |volume=21 |issue= 18 |pages= 6312-21 |year= 2001 |pmid= 11509672 |doi= }}
*{{cite journal | author=Ozawa Y, Towatari M, Tsuzuki S, ''et al.'' |title=Histone deacetylase 3 associates with and represses the transcription factor GATA-2. |journal=Blood |volume=98 |issue= 7 |pages= 2116-23 |year= 2001 |pmid= 11567998 |doi= }}
*{{cite journal | author=Potter GB, Beaudoin GM, DeRenzo CL, ''et al.'' |title=The hairless gene mutated in congenital hair loss disorders encodes a novel nuclear receptor corepressor. |journal=Genes Dev. |volume=15 |issue= 20 |pages= 2687-701 |year= 2001 |pmid= 11641275 |doi= 10.1101/gad.916701 }}
*{{cite journal | author=Fischle W, Dequiedt F, Hendzel MJ, ''et al.'' |title=Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR. |journal=Mol. Cell |volume=9 |issue= 1 |pages= 45-57 |year= 2002 |pmid= 11804585 |doi= }}
*{{cite journal | author=Lemercier C, Brocard MP, Puvion-Dutilleul F, ''et al.'' |title=Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor. |journal=J. Biol. Chem. |volume=277 |issue= 24 |pages= 22045-52 |year= 2002 |pmid= 11929873 |doi= 10.1074/jbc.M201736200 }}
*{{cite journal | author=Huang Y, Tan M, Gosink M, ''et al.'' |title=Histone deacetylase 5 is not a p53 target gene, but its overexpression inhibits tumor cell growth and induces apoptosis. |journal=Cancer Res. |volume=62 |issue= 10 |pages= 2913-22 |year= 2002 |pmid= 12019172 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HIST1H3B... {November 18, 2007 11:35:59 AM PST}
- SEARCH REDIRECT: Control Box Found: HIST1H3B {November 18, 2007 11:36:34 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:36:36 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:36:36 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:36:36 AM PST}
- UPDATED: Updated protein page: HIST1H3B {November 18, 2007 11:36:48 AM PST}
- INFO: Beginning work on HMGCR... {November 18, 2007 11:27:28 AM PST}
- SEARCH REDIRECT: Control Box Found: HMGCR {November 18, 2007 11:28:07 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:28:09 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:28:09 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:28:09 AM PST}
- UPDATED: Updated protein page: HMGCR {November 18, 2007 11:28:21 AM PST}
- INFO: Beginning work on IKZF1... {November 18, 2007 11:45:51 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:47:25 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = IKAROS family zinc finger 1 (Ikaros)
| HGNCid = 13176
| Symbol = IKZF1
| AltSymbols =; IK1; Hs.54452; IKAROS; LYF1; PRO0758; ZNFN1A1; hIk-1
| OMIM = 603023
| ECnumber =
| Homologene = 55948
| MGIid = 1342540
| GeneAtlas_image1 = PBB_GE_IKZF1_205039_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_IKZF1_216901_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007498 |text = mesoderm development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10320
| Hs_Ensembl = ENSG00000185811
| Hs_RefseqProtein = NP_006051
| Hs_RefseqmRNA = NM_006060
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 50314924
| Hs_GenLoc_end = 50438053
| Hs_Uniprot = Q13422
| Mm_EntrezGene = 22778
| Mm_Ensembl = ENSMUSG00000018654
| Mm_RefseqmRNA = NM_001025597
| Mm_RefseqProtein = NP_001020768
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 11585928
| Mm_GenLoc_end = 11672929
| Mm_Uniprot = Q5GGW4
}}
}}
'''IKAROS family zinc finger 1 (Ikaros)''', also known as '''IKZF1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IKZF1 IKAROS family zinc finger 1 (Ikaros)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10320| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tonnelle C, Calmels B, Maroc C, ''et al.'' |title=Ikaros gene expression and leukemia. |journal=Leuk. Lymphoma |volume=43 |issue= 1 |pages= 29-35 |year= 2003 |pmid= 11908734 |doi= }}
*{{cite journal | author=Westman BJ, Mackay JP, Gell D |title=Ikaros: a key regulator of haematopoiesis. |journal=Int. J. Biochem. Cell Biol. |volume=34 |issue= 10 |pages= 1304-7 |year= 2002 |pmid= 12127581 |doi= }}
*{{cite journal | author=Georgopoulos K, Moore DD, Derfler B |title=Ikaros, an early lymphoid-specific transcription factor and a putative mediator for T cell commitment. |journal=Science |volume=258 |issue= 5083 |pages= 808-12 |year= 1992 |pmid= 1439790 |doi= }}
*{{cite journal | author=Hahm K, Ernst P, Lo K, ''et al.'' |title=The lymphoid transcription factor LyF-1 is encoded by specific, alternatively spliced mRNAs derived from the Ikaros gene. |journal=Mol. Cell. Biol. |volume=14 |issue= 11 |pages= 7111-23 |year= 1994 |pmid= 7935426 |doi= }}
*{{cite journal | author=Molnár A, Wu P, Largespada DA, ''et al.'' |title=The Ikaros gene encodes a family of lymphocyte-restricted zinc finger DNA binding proteins, highly conserved in human and mouse. |journal=J. Immunol. |volume=156 |issue= 2 |pages= 585-92 |year= 1996 |pmid= 8543809 |doi= }}
*{{cite journal | author=Nietfeld W, Meyerhans A |title=Cloning and sequencing of hIk-1, a cDNA encoding a human homologue of mouse Ikaros/LyF-1. |journal=Immunol. Lett. |volume=49 |issue= 1-2 |pages= 139-41 |year= 1996 |pmid= 8964602 |doi= }}
*{{cite journal | author=Morgan B, Sun L, Avitahl N, ''et al.'' |title=Aiolos, a lymphoid restricted transcription factor that interacts with Ikaros to regulate lymphocyte differentiation. |journal=EMBO J. |volume=16 |issue= 8 |pages= 2004-13 |year= 1997 |pmid= 9155026 |doi= 10.1093/emboj/16.8.2004 }}
*{{cite journal | author=Kelley CM, Ikeda T, Koipally J, ''et al.'' |title=Helios, a novel dimerization partner of Ikaros expressed in the earliest hematopoietic progenitors. |journal=Curr. Biol. |volume=8 |issue= 9 |pages= 508-15 |year= 1998 |pmid= 9560339 |doi= }}
*{{cite journal | author=Sun L, Heerema N, Crotty L, ''et al.'' |title=Expression of dominant-negative and mutant isoforms of the antileukemic transcription factor Ikaros in infant acute lymphoblastic leukemia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 2 |pages= 680-5 |year= 1999 |pmid= 9892693 |doi= }}
*{{cite journal | author=Kim J, Sif S, Jones B, ''et al.'' |title=Ikaros DNA-binding proteins direct formation of chromatin remodeling complexes in lymphocytes. |journal=Immunity |volume=10 |issue= 3 |pages= 345-55 |year= 1999 |pmid= 10204490 |doi= }}
*{{cite journal | author=Honma Y, Kiyosawa H, Mori T, ''et al.'' |title=Eos: a novel member of the Ikaros gene family expressed predominantly in the developing nervous system. |journal=FEBS Lett. |volume=447 |issue= 1 |pages= 76-80 |year= 1999 |pmid= 10218586 |doi= }}
*{{cite journal | author=Koipally J, Renold A, Kim J, Georgopoulos K |title=Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes. |journal=EMBO J. |volume=18 |issue= 11 |pages= 3090-100 |year= 1999 |pmid= 10357820 |doi= 10.1093/emboj/18.11.3090 }}
*{{cite journal | author=Sun L, Goodman PA, Wood CM, ''et al.'' |title=Expression of aberrantly spliced oncogenic ikaros isoforms in childhood acute lymphoblastic leukemia. |journal=J. Clin. Oncol. |volume=17 |issue= 12 |pages= 3753-66 |year= 2000 |pmid= 10577847 |doi= }}
*{{cite journal | author=Hosokawa Y, Maeda Y, Ichinohasama R, ''et al.'' |title=The Ikaros gene, a central regulator of lymphoid differentiation, fuses to the BCL6 gene as a result of t(3;7)(q27;p12) translocation in a patient with diffuse large B-cell lymphoma. |journal=Blood |volume=95 |issue= 8 |pages= 2719-21 |year= 2000 |pmid= 10753856 |doi= }}
*{{cite journal | author=Koipally J, Georgopoulos K |title=Ikaros interactions with CtBP reveal a repression mechanism that is independent of histone deacetylase activity. |journal=J. Biol. Chem. |volume=275 |issue= 26 |pages= 19594-602 |year= 2000 |pmid= 10766745 |doi= 10.1074/jbc.M000254200 }}
*{{cite journal | author=Perdomo J, Holmes M, Chong B, Crossley M |title=Eos and pegasus, two members of the Ikaros family of proteins with distinct DNA binding activities. |journal=J. Biol. Chem. |volume=275 |issue= 49 |pages= 38347-54 |year= 2001 |pmid= 10978333 |doi= 10.1074/jbc.M005457200 }}
*{{cite journal | author=Payne KJ, Nicolas JH, Zhu JY, ''et al.'' |title=Cutting edge: predominant expression of a novel Ikaros isoform in normal human hemopoiesis. |journal=J. Immunol. |volume=167 |issue= 4 |pages= 1867-70 |year= 2001 |pmid= 11489963 |doi= }}
*{{cite journal | author=Koipally J, Heller EJ, Seavitt JR, Georgopoulos K |title=Unconventional potentiation of gene expression by Ikaros. |journal=J. Biol. Chem. |volume=277 |issue= 15 |pages= 13007-15 |year= 2002 |pmid= 11799125 |doi= 10.1074/jbc.M111371200 }}
*{{cite journal | author=Dorsam G, Goetzl EJ |title=Vasoactive intestinal peptide receptor-1 (VPAC-1) is a novel gene target of the hemolymphopoietic transcription factor Ikaros. |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 13488-93 |year= 2002 |pmid= 11812772 |doi= 10.1074/jbc.M107922200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IL1R2... {November 18, 2007 11:34:50 AM PST}
- SEARCH REDIRECT: Control Box Found: IL1R2 {November 18, 2007 11:35:38 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:35:47 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:35:47 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:35:47 AM PST}
- UPDATED: Updated protein page: IL1R2 {November 18, 2007 11:35:58 AM PST}
- INFO: Beginning work on MBD2... {November 18, 2007 11:37:37 AM PST}
- SEARCH REDIRECT: Control Box Found: MBD2 {November 18, 2007 11:38:30 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:38:38 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:38:38 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:38:38 AM PST}
- UPDATED: Updated protein page: MBD2 {November 18, 2007 11:38:50 AM PST}
- INFO: Beginning work on MTA1... {November 18, 2007 11:38:50 AM PST}
- SEARCH REDIRECT: Control Box Found: MTA1 {November 18, 2007 11:39:43 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:39:45 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:39:45 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:39:45 AM PST}
- UPDATED: Updated protein page: MTA1 {November 18, 2007 11:40:01 AM PST}
- INFO: Beginning work on NKX2-5... {November 18, 2007 11:23:02 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:23:58 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = NK2 transcription factor related, locus 5 (Drosophila)
| HGNCid = 2488
| Symbol = NKX2-5
| AltSymbols =; CSX; CSX1; NKX2.5; NKX2E
| OMIM = 600584
| ECnumber =
| Homologene = 3230
| MGIid = 97350
| GeneAtlas_image1 = PBB_GE_NKX2-5_206578_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016564 |text = transcription repressor activity}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046982 |text = protein heterodimerization activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005667 |text = transcription factor complex}}
| Process = {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0001947 |text = heart looping}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007512 |text = adult heart development}} {{GNF_GO|id=GO:0035050 |text = embryonic heart tube development}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0048738 |text = cardiac muscle development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1482
| Hs_Ensembl = ENSG00000183072
| Hs_RefseqProtein = NP_004378
| Hs_RefseqmRNA = NM_004387
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 172591744
| Hs_GenLoc_end = 172594868
| Hs_Uniprot = P52952
| Mm_EntrezGene = 18091
| Mm_Ensembl = ENSMUSG00000015579
| Mm_RefseqmRNA = NM_008700
| Mm_RefseqProtein = NP_032726
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 26566254
| Mm_GenLoc_end = 26569154
| Mm_Uniprot = Q3UQU2
}}
}}
'''NK2 transcription factor related, locus 5 (Drosophila)''', also known as '''NKX2-5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NKX2-5 NK2 transcription factor related, locus 5 (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1482| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Homeobox-containing genes play critical roles in regulating tissue-specific gene expression essential for tissue differentiation, as well as determining the temporal and spatial patterns of development (Shiojima et al., 1995). It has been demonstrated that a Drosophila homeobox-containing gene called 'tinman' is expressed in the developing dorsal vessel and in the equivalent of the vertebrate heart. Mutations in tinman result in loss of heart formation in the embryo, suggesting that tinman is essential for Drosophila heart formation. Furthermore, abundant expression of Csx, the presumptive mouse homolog of tinman, is observed only in the heart from the time of cardiac differentiation. CSX, the human homolog of murine Csx, has a homeodomain sequence identical to that of Csx and is expressed only in the heart, again suggesting that CSX plays an important role in human heart formation.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: NKX2-5 NK2 transcription factor related, locus 5 (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1482| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Harvey RP, Lai D, Elliott D, ''et al.'' |title=Homeodomain factor Nkx2-5 in heart development and disease. |journal=Cold Spring Harb. Symp. Quant. Biol. |volume=67 |issue= |pages= 107-14 |year= 2003 |pmid= 12858530 |doi= }}
*{{cite journal | author=Shiojima I, Komuro I, Inazawa J, ''et al.'' |title=Assignment of cardiac homeobox gene CSX to human chromosome 5q34. |journal=Genomics |volume=27 |issue= 1 |pages= 204-6 |year= 1995 |pmid= 7665173 |doi= 10.1006/geno.1995.1027 }}
*{{cite journal | author=Chen CY, Schwartz RJ |title=Recruitment of the tinman homolog Nkx-2.5 by serum response factor activates cardiac alpha-actin gene transcription. |journal=Mol. Cell. Biol. |volume=16 |issue= 11 |pages= 6372-84 |year= 1996 |pmid= 8887666 |doi= }}
*{{cite journal | author=Turbay D, Wechsler SB, Blanchard KM, Izumo S |title=Molecular cloning, chromosomal mapping, and characterization of the human cardiac-specific homeobox gene hCsx. |journal=Mol. Med. |volume=2 |issue= 1 |pages= 86-96 |year= 1997 |pmid= 8900537 |doi= }}
*{{cite journal | author=Durocher D, Charron F, Warren R, ''et al.'' |title=The cardiac transcription factors Nkx2-5 and GATA-4 are mutual cofactors. |journal=EMBO J. |volume=16 |issue= 18 |pages= 5687-96 |year= 1997 |pmid= 9312027 |doi= 10.1093/emboj/16.18.5687 }}
*{{cite journal | author=Schott JJ, Benson DW, Basson CT, ''et al.'' |title=Congenital heart disease caused by mutations in the transcription factor NKX2-5. |journal=Science |volume=281 |issue= 5373 |pages= 108-11 |year= 1998 |pmid= 9651244 |doi= }}
*{{cite journal | author=Kim YH, Choi CY, Lee SJ, ''et al.'' |title=Homeodomain-interacting protein kinases, a novel family of co-repressors for homeodomain transcription factors. |journal=J. Biol. Chem. |volume=273 |issue= 40 |pages= 25875-9 |year= 1998 |pmid= 9748262 |doi= }}
*{{cite journal | author=Kasahara H, Izumo S |title=Identification of the in vivo casein kinase II phosphorylation site within the homeodomain of the cardiac tisue-specifying homeobox gene product Csx/Nkx2.5. |journal=Mol. Cell. Biol. |volume=19 |issue= 1 |pages= 526-36 |year= 1999 |pmid= 9858576 |doi= }}
*{{cite journal | author=Benson DW, Silberbach GM, Kavanaugh-McHugh A, ''et al.'' |title=Mutations in the cardiac transcription factor NKX2.5 affect diverse cardiac developmental pathways. |journal=J. Clin. Invest. |volume=104 |issue= 11 |pages= 1567-73 |year= 2000 |pmid= 10587520 |doi= }}
*{{cite journal | author=Kasahara H, Lee B, Schott JJ, ''et al.'' |title=Loss of function and inhibitory effects of human CSX/NKX2.5 homeoprotein mutations associated with congenital heart disease. |journal=J. Clin. Invest. |volume=106 |issue= 2 |pages= 299-308 |year= 2000 |pmid= 10903346 |doi= }}
*{{cite journal | author=Zhu W, Shiojima I, Hiroi Y, ''et al.'' |title=Functional analyses of three Csx/Nkx-2.5 mutations that cause human congenital heart disease. |journal=J. Biol. Chem. |volume=275 |issue= 45 |pages= 35291-6 |year= 2001 |pmid= 10948187 |doi= 10.1074/jbc.M000525200 }}
*{{cite journal | author=Hiroi Y, Kudoh S, Monzen K, ''et al.'' |title=Tbx5 associates with Nkx2-5 and synergistically promotes cardiomyocyte differentiation. |journal=Nat. Genet. |volume=28 |issue= 3 |pages= 276-80 |year= 2001 |pmid= 11431700 |doi= 10.1038/90123 }}
*{{cite journal | author=Goldmuntz E, Geiger E, Benson DW |title=NKX2.5 mutations in patients with tetralogy of fallot. |journal=Circulation |volume=104 |issue= 21 |pages= 2565-8 |year= 2001 |pmid= 11714651 |doi= }}
*{{cite journal | author=Toko H, Zhu W, Takimoto E, ''et al.'' |title=Csx/Nkx2-5 is required for homeostasis and survival of cardiac myocytes in the adult heart. |journal=J. Biol. Chem. |volume=277 |issue= 27 |pages= 24735-43 |year= 2002 |pmid= 11889119 |doi= 10.1074/jbc.M107669200 }}
*{{cite journal | author=Habets PE, Moorman AF, Clout DE, ''et al.'' |title=Cooperative action of Tbx2 and Nkx2.5 inhibits ANF expression in the atrioventricular canal: implications for cardiac chamber formation. |journal=Genes Dev. |volume=16 |issue= 10 |pages= 1234-46 |year= 2002 |pmid= 12023302 |doi= 10.1101/gad.222902 }}
*{{cite journal | author=Ikeda Y, Hiroi Y, Hosoda T, ''et al.'' |title=Novel point mutation in the cardiac transcription factor CSX/NKX2.5 associated with congenital heart disease. |journal=Circ. J. |volume=66 |issue= 6 |pages= 561-3 |year= 2002 |pmid= 12074273 |doi= }}
*{{cite journal | author=Shirai M, Osugi T, Koga H, ''et al.'' |title=The Polycomb-group gene Rae28 sustains Nkx2.5/Csx expression and is essential for cardiac morphogenesis. |journal=J. Clin. Invest. |volume=110 |issue= 2 |pages= 177-84 |year= 2002 |pmid= 12122109 |doi= }}
*{{cite journal | author=Watanabe Y, Benson DW, Yano S, ''et al.'' |title=Two novel frameshift mutations in NKX2.5 result in novel features including visceral inversus and sinus venosus type ASD. |journal=J. Med. Genet. |volume=39 |issue= 11 |pages= 807-11 |year= 2002 |pmid= 12414819 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Fan C, Liu M, Wang Q |title=Functional analysis of TBX5 missense mutations associated with Holt-Oram syndrome. |journal=J. Biol. Chem. |volume=278 |issue= 10 |pages= 8780-5 |year= 2003 |pmid= 12499378 |doi= 10.1074/jbc.M208120200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NR5A2... {November 18, 2007 11:25:53 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:26:49 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_NR5A2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1yok.
| PDB = {{PDB2|1yok}}, {{PDB2|1yuc}}, {{PDB2|1zdu}}, {{PDB2|2a66}}, {{PDB2|2ff0}}
| Name = Nuclear receptor subfamily 5, group A, member 2
| HGNCid = 7984
| Symbol = NR5A2
| AltSymbols =; B1F; B1F2; CPF; FTF; FTZ-F1; FTZ-F1beta; LRH-1; hB1F; hB1F-2
| OMIM = 604453
| ECnumber =
| Homologene = 20827
| MGIid = 1346834
| Function = {{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:0003707 |text = steroid hormone receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0008289 |text = lipid binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0008206 |text = bile acid metabolic process}} {{GNF_GO|id=GO:0009653 |text = anatomical structure morphogenesis}} {{GNF_GO|id=GO:0009790 |text = embryonic development}} {{GNF_GO|id=GO:0042592 |text = homeostatic process}} {{GNF_GO|id=GO:0042632 |text = cholesterol homeostasis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2494
| Hs_Ensembl = ENSG00000116833
| Hs_RefseqProtein = NP_003813
| Hs_RefseqmRNA = NM_003822
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 198263353
| Hs_GenLoc_end = 198413175
| Hs_Uniprot = O00482
| Mm_EntrezGene = 26424
| Mm_Ensembl = ENSMUSG00000026398
| Mm_RefseqmRNA = XM_990082
| Mm_RefseqProtein = XP_995176
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 138660687
| Mm_GenLoc_end = 138776859
| Mm_Uniprot = Q1WLP7
}}
}}
'''Nuclear receptor subfamily 5, group A, member 2''', also known as '''NR5A2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NR5A2 nuclear receptor subfamily 5, group A, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2494| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bernier D, Thomassin H, Allard D, ''et al.'' |title=Functional analysis of developmentally regulated chromatin-hypersensitive domains carrying the alpha 1-fetoprotein gene promoter and the albumin/alpha 1-fetoprotein intergenic enhancer. |journal=Mol. Cell. Biol. |volume=13 |issue= 3 |pages= 1619-33 |year= 1993 |pmid= 7680097 |doi= }}
*{{cite journal | author=Wong M, Ramayya MS, Chrousos GP, ''et al.'' |title=Cloning and sequence analysis of the human gene encoding steroidogenic factor 1. |journal=J. Mol. Endocrinol. |volume=17 |issue= 2 |pages= 139-47 |year= 1997 |pmid= 8938589 |doi= }}
*{{cite journal | author=Li M, Xie YH, Kong YY, ''et al.'' |title=Cloning and characterization of a novel human hepatocyte transcription factor, hB1F, which binds and activates enhancer II of hepatitis B virus. |journal=J. Biol. Chem. |volume=273 |issue= 44 |pages= 29022-31 |year= 1998 |pmid= 9786908 |doi= }}
*{{cite journal | author=Galarneau L, Drouin R, Bélanger L |title=Assignment of the fetoprotein transcription factor gene (FTF) to human chromosome band 1q32.11 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=82 |issue= 3-4 |pages= 269-70 |year= 1999 |pmid= 9858833 |doi= }}
*{{cite journal | author=Nitta M, Ku S, Brown C, ''et al.'' |title=CPF: an orphan nuclear receptor that regulates liver-specific expression of the human cholesterol 7alpha-hydroxylase gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 12 |pages= 6660-5 |year= 1999 |pmid= 10359768 |doi= }}
*{{cite journal | author=Goodwin B, Jones SA, Price RR, ''et al.'' |title=A regulatory cascade of the nuclear receptors FXR, SHP-1, and LRH-1 represses bile acid biosynthesis. |journal=Mol. Cell |volume=6 |issue= 3 |pages= 517-26 |year= 2000 |pmid= 11030332 |doi= }}
*{{cite journal | author=Wang ZN, Bassett M, Rainey WE |title=Liver receptor homologue-1 is expressed in the adrenal and can regulate transcription of 11 beta-hydroxylase. |journal=J. Mol. Endocrinol. |volume=27 |issue= 2 |pages= 255-8 |year= 2001 |pmid= 11564608 |doi= }}
*{{cite journal | author=Zhang CK, Lin W, Cai YN, ''et al.'' |title=Characterization of the genomic structure and tissue-specific promoter of the human nuclear receptor NR5A2 (hB1F) gene. |journal=Gene |volume=273 |issue= 2 |pages= 239-49 |year= 2001 |pmid= 11595170 |doi= }}
*{{cite journal | author=Lee YK, Moore DD |title=Dual mechanisms for repression of the monomeric orphan receptor liver receptor homologous protein-1 by the orphan small heterodimer partner. |journal=J. Biol. Chem. |volume=277 |issue= 4 |pages= 2463-7 |year= 2002 |pmid= 11668176 |doi= 10.1074/jbc.M105161200 }}
*{{cite journal | author=Clyne CD, Speed CJ, Zhou J, Simpson ER |title=Liver receptor homologue-1 (LRH-1) regulates expression of aromatase in preadipocytes. |journal=J. Biol. Chem. |volume=277 |issue= 23 |pages= 20591-7 |year= 2002 |pmid= 11927588 |doi= 10.1074/jbc.M201117200 }}
*{{cite journal | author=Brendel C, Gelman L, Auwerx J |title=Multiprotein bridging factor-1 (MBF-1) is a cofactor for nuclear receptors that regulate lipid metabolism. |journal=Mol. Endocrinol. |volume=16 |issue= 6 |pages= 1367-77 |year= 2003 |pmid= 12040021 |doi= }}
*{{cite journal | author=Sirianni R, Seely JB, Attia G, ''et al.'' |title=Liver receptor homologue-1 is expressed in human steroidogenic tissues and activates transcription of genes encoding steroidogenic enzymes. |journal=J. Endocrinol. |volume=174 |issue= 3 |pages= R13-7 |year= 2002 |pmid= 12208674 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Sablin EP, Krylova IN, Fletterick RJ, Ingraham HA |title=Structural basis for ligand-independent activation of the orphan nuclear receptor LRH-1. |journal=Mol. Cell |volume=11 |issue= 6 |pages= 1575-85 |year= 2003 |pmid= 12820970 |doi= }}
*{{cite journal | author=Privalsky ML |title=Activation incarnate. |journal=Dev. Cell |volume=5 |issue= 1 |pages= 1-2 |year= 2003 |pmid= 12852843 |doi= }}
*{{cite journal | author=Fayard E, Schoonjans K, Annicotte JS, Auwerx J |title=Liver receptor homolog 1 controls the expression of carboxyl ester lipase. |journal=J. Biol. Chem. |volume=278 |issue= 37 |pages= 35725-31 |year= 2003 |pmid= 12853459 |doi= 10.1074/jbc.M302370200 }}
*{{cite journal | author=Annicotte JS, Fayard E, Swift GH, ''et al.'' |title=Pancreatic-duodenal homeobox 1 regulates expression of liver receptor homolog 1 during pancreas development. |journal=Mol. Cell. Biol. |volume=23 |issue= 19 |pages= 6713-24 |year= 2003 |pmid= 12972592 |doi= }}
*{{cite journal | author=Peng N, Kim JW, Rainey WE, ''et al.'' |title=The role of the orphan nuclear receptor, liver receptor homologue-1, in the regulation of human corpus luteum 3beta-hydroxysteroid dehydrogenase type II. |journal=J. Clin. Endocrinol. Metab. |volume=88 |issue= 12 |pages= 6020-8 |year= 2004 |pmid= 14671206 |doi= }}
*{{cite journal | author=Cai YN, Zhou Q, Kong YY, ''et al.'' |title=LRH-1/hB1F and HNF1 synergistically up-regulate hepatitis B virus gene transcription and DNA replication. |journal=Cell Res. |volume=13 |issue= 6 |pages= 451-8 |year= 2004 |pmid= 14728801 |doi= 10.1038/sj.cr.7290187 }}
*{{cite journal | author=Saxena D, Safi R, Little-Ihrig L, Zeleznik AJ |title=Liver receptor homolog-1 stimulates the progesterone biosynthetic pathway during follicle-stimulating hormone-induced granulosa cell differentiation. |journal=Endocrinology |volume=145 |issue= 8 |pages= 3821-9 |year= 2004 |pmid= 15117876 |doi= 10.1210/en.2004-0423 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PSIP1... {November 18, 2007 11:47:25 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:48:14 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PSIP1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1z9e.
| PDB = {{PDB2|1z9e}}, {{PDB2|2b4j}}
| Name = PC4 and SFRS1 interacting protein 1
| HGNCid = 9527
| Symbol = PSIP1
| AltSymbols =; p75; p52; DFS70; LEDGF; MGC74712; PAIP; PSIP2
| OMIM = 603620
| ECnumber =
| Homologene = 13242
| MGIid = 2142116
| GeneAtlas_image1 = PBB_GE_PSIP1_210758_at_tn.png
| GeneAtlas_image2 = PBB_GE_PSIP1_205961_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_PSIP1_209337_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 11168
| Hs_Ensembl = ENSG00000164985
| Hs_RefseqProtein = NP_066967
| Hs_RefseqmRNA = NM_021144
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 15454064
| Hs_GenLoc_end = 15501017
| Hs_Uniprot = O75475
| Mm_EntrezGene = 101739
| Mm_Ensembl = ENSMUSG00000028484
| Mm_RefseqmRNA = NM_133948
| Mm_RefseqProtein = NP_598709
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 82926911
| Mm_GenLoc_end = 82957621
| Mm_Uniprot = Q05CD2
}}
}}
'''PC4 and SFRS1 interacting protein 1''', also known as '''PSIP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSIP1 PC4 and SFRS1 interacting protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11168| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Van Maele B, Debyser Z |title=HIV-1 integration: an interplay between HIV-1 integrase, cellular and viral proteins. |journal=AIDS reviews |volume=7 |issue= 1 |pages= 26-43 |year= 2005 |pmid= 15875659 |doi= }}
*{{cite journal | author=Van Maele B, Busschots K, Vandekerckhove L, ''et al.'' |title=Cellular co-factors of HIV-1 integration. |journal=Trends Biochem. Sci. |volume=31 |issue= 2 |pages= 98-105 |year= 2006 |pmid= 16403635 |doi= 10.1016/j.tibs.2005.12.002 }}
*{{cite journal | author=Freed EO, Mouland AJ |title=The cell biology of HIV-1 and other retroviruses. |journal=Retrovirology |volume=3 |issue= |pages= 77 |year= 2006 |pmid= 17083721 |doi= 10.1186/1742-4690-3-77 }}
*{{cite journal | author=Ge H, Si Y, Roeder RG |title=Isolation of cDNAs encoding novel transcription coactivators p52 and p75 reveals an alternate regulatory mechanism of transcriptional activation. |journal=EMBO J. |volume=17 |issue= 22 |pages= 6723-9 |year= 1999 |pmid= 9822615 |doi= 10.1093/emboj/17.22.6723 }}
*{{cite journal | author=Ge H, Si Y, Wolffe AP |title=A novel transcriptional coactivator, p52, functionally interacts with the essential splicing factor ASF/SF2. |journal=Mol. Cell |volume=2 |issue= 6 |pages= 751-9 |year= 1999 |pmid= 9885563 |doi= }}
*{{cite journal | author=Singh DP, Ohguro N, Kikuchi T, ''et al.'' |title=Lens epithelium-derived growth factor: effects on growth and survival of lens epithelial cells, keratinocytes, and fibroblasts. |journal=Biochem. Biophys. Res. Commun. |volume=267 |issue= 1 |pages= 373-81 |year= 2000 |pmid= 10623627 |doi= 10.1006/bbrc.1999.1979 }}
*{{cite journal | author=Singh DP, Kimura A, Chylack LT, Shinohara T |title=Lens epithelium-derived growth factor (LEDGF/p75) and p52 are derived from a single gene by alternative splicing. |journal=Gene |volume=242 |issue= 1-2 |pages= 265-73 |year= 2000 |pmid= 10721720 |doi= }}
*{{cite journal | author=Ochs RL, Muro Y, Si Y, ''et al.'' |title=Autoantibodies to DFS 70 kd/transcription coactivator p75 in atopic dermatitis and other conditions. |journal=J. Allergy Clin. Immunol. |volume=105 |issue= 6 Pt 1 |pages= 1211-20 |year= 2000 |pmid= 10856157 |doi= }}
*{{cite journal | author=Kubo E, Fatma N, Sharma P, ''et al.'' |title=Transactivation of involucrin, a marker of differentiation in keratinocytes, by lens epithelium-derived growth factor (LEDGF). |journal=J. Mol. Biol. |volume=320 |issue= 5 |pages= 1053-63 |year= 2002 |pmid= 12126624 |doi= }}
*{{cite journal | author=Wu X, Daniels T, Molinaro C, ''et al.'' |title=Caspase cleavage of the nuclear autoantigen LEDGF/p75 abrogates its pro-survival function: implications for autoimmunity in atopic disorders. |journal=Cell Death Differ. |volume=9 |issue= 9 |pages= 915-25 |year= 2003 |pmid= 12181742 |doi= 10.1038/sj.cdd.4401063 }}
*{{cite journal | author=Cherepanov P, Maertens G, Proost P, ''et al.'' |title=HIV-1 integrase forms stable tetramers and associates with LEDGF/p75 protein in human cells. |journal=J. Biol. Chem. |volume=278 |issue= 1 |pages= 372-81 |year= 2003 |pmid= 12407101 |doi= 10.1074/jbc.M209278200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Maertens G, Cherepanov P, Pluymers W, ''et al.'' |title=LEDGF/p75 is essential for nuclear and chromosomal targeting of HIV-1 integrase in human cells. |journal=J. Biol. Chem. |volume=278 |issue= 35 |pages= 33528-39 |year= 2003 |pmid= 12796494 |doi= 10.1074/jbc.M303594200 }}
*{{cite journal | author=Maertens G, Cherepanov P, Debyser Z, ''et al.'' |title=Identification and characterization of a functional nuclear localization signal in the HIV-1 integrase interactor LEDGF/p75. |journal=J. Biol. Chem. |volume=279 |issue= 32 |pages= 33421-9 |year= 2004 |pmid= 15163664 |doi= 10.1074/jbc.M404700200 }}
*{{cite journal | author=Beausoleil SA, Jedrychowski M, Schwartz D, ''et al.'' |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130-5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 }}
*{{cite journal | author=Llano M, Vanegas M, Fregoso O, ''et al.'' |title=LEDGF/p75 determines cellular trafficking of diverse lentiviral but not murine oncoretroviral integrase proteins and is a component of functional lentiviral preintegration complexes. |journal=J. Virol. |volume=78 |issue= 17 |pages= 9524-37 |year= 2004 |pmid= 15308744 |doi= 10.1128/JVI.78.17.9524-9537.2004 }}
*{{cite journal | author=Cherepanov P, Devroe E, Silver PA, Engelman A |title=Identification of an evolutionarily conserved domain in human lens epithelium-derived growth factor/transcriptional co-activator p75 (LEDGF/p75) that binds HIV-1 integrase. |journal=J. Biol. Chem. |volume=279 |issue= 47 |pages= 48883-92 |year= 2005 |pmid= 15371438 |doi= 10.1074/jbc.M406307200 }}
*{{cite journal | author=Llano M, Delgado S, Vanegas M, Poeschla EM |title=Lens epithelium-derived growth factor/p75 prevents proteasomal degradation of HIV-1 integrase. |journal=J. Biol. Chem. |volume=279 |issue= 53 |pages= 55570-7 |year= 2005 |pmid= 15475359 |doi= 10.1074/jbc.M408508200 }}
*{{cite journal | author=Ogawa Y, Sugiura K, Watanabe A, ''et al.'' |title=Autoantigenicity of DFS70 is restricted to the conformational epitope of C-terminal alpha-helical domain. |journal=J. Autoimmun. |volume=23 |issue= 3 |pages= 221-31 |year= 2005 |pmid= 15501393 |doi= 10.1016/j.jaut.2004.07.003 }}
*{{cite journal | author=Okamoto M, Ogawa Y, Watanabe A, ''et al.'' |title=Autoantibodies to DFS70/LEDGF are increased in alopecia areata patients. |journal=J. Autoimmun. |volume=23 |issue= 3 |pages= 257-66 |year= 2005 |pmid= 15501396 |doi= 10.1016/j.jaut.2004.07.004 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RBX1... {November 18, 2007 11:42:15 AM PST}
- SEARCH REDIRECT: Control Box Found: RBX1 {November 18, 2007 11:44:08 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:44:09 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:44:09 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:44:09 AM PST}
- UPDATED: Updated protein page: RBX1 {November 18, 2007 11:44:23 AM PST}
- INFO: Beginning work on REST... {November 18, 2007 11:28:22 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:29:30 AM PST}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = RE1-silencing transcription factor
| HGNCid = 9966
| Symbol = REST
| AltSymbols =; NRSF; XBR
| OMIM = 600571
| ECnumber =
| Homologene = 4099
| MGIid = 104897
| GeneAtlas_image1 = PBB_GE_REST_212920_at_tn.png
| GeneAtlas_image2 = PBB_GE_REST_204535_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003676 |text = nucleic acid binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016564 |text = transcription repressor activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5978
| Hs_Ensembl = ENSG00000084093
| Hs_RefseqProtein = NP_005603
| Hs_RefseqmRNA = NM_005612
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 57468832
| Hs_GenLoc_end = 57496767
| Hs_Uniprot = Q13127
| Mm_EntrezGene = 19712
| Mm_Ensembl = ENSMUSG00000029249
| Mm_RefseqmRNA = NM_011263
| Mm_RefseqProtein = NP_035393
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 78342716
| Mm_GenLoc_end = 78357759
| Mm_Uniprot = A0JNY8
}}
}}
'''RE1-silencing transcription factor''', also known as '''REST''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: REST RE1-silencing transcription factor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5978| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a transcriptional repressor which represses neuronal genes in non-neuronal tissues. It is a member of the Kruppel-type zinc finger transcription factor family. It represses transcription by binding a DNA sequence element called the neuron-restrictive silencer element. The protein is also found in undifferentiated neuronal progenitor cells, and it is thought that this repressor may act as a master negative regular of neurogenesis. Alternatively spliced transcript variants have been described; however, their full length nature has not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: REST RE1-silencing transcription factor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5978| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Chong JA, Tapia-Ramírez J, Kim S, ''et al.'' |title=REST: a mammalian silencer protein that restricts sodium channel gene expression to neurons. |journal=Cell |volume=80 |issue= 6 |pages= 949-57 |year= 1995 |pmid= 7697725 |doi= }}
*{{cite journal | author=Schoenherr CJ, Anderson DJ |title=The neuron-restrictive silencer factor (NRSF): a coordinate repressor of multiple neuron-specific genes. |journal=Science |volume=267 |issue= 5202 |pages= 1360-3 |year= 1995 |pmid= 7871435 |doi= }}
*{{cite journal | author=Scholl T, Stevens MB, Mahanta S, Strominger JL |title=A zinc finger protein that represses transcription of the human MHC class II gene, DPA. |journal=J. Immunol. |volume=156 |issue= 4 |pages= 1448-57 |year= 1996 |pmid= 8568247 |doi= }}
*{{cite journal | author=Thiel G, Lietz M, Cramer M |title=Biological activity and modular structure of RE-1-silencing transcription factor (REST), a repressor of neuronal genes. |journal=J. Biol. Chem. |volume=273 |issue= 41 |pages= 26891-9 |year= 1998 |pmid= 9756936 |doi= }}
*{{cite journal | author=Andrés ME, Burger C, Peral-Rubio MJ, ''et al.'' |title=CoREST: a functional corepressor required for regulation of neural-specific gene expression. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 17 |pages= 9873-8 |year= 1999 |pmid= 10449787 |doi= }}
*{{cite journal | author=Palm K, Metsis M, Timmusk T |title=Neuron-specific splicing of zinc finger transcription factor REST/NRSF/XBR is frequent in neuroblastomas and conserved in human, mouse and rat. |journal=Brain Res. Mol. Brain Res. |volume=72 |issue= 1 |pages= 30-9 |year= 1999 |pmid= 10521596 |doi= }}
*{{cite journal | author=Naruse Y, Aoki T, Kojima T, Mori N |title=Neural restrictive silencer factor recruits mSin3 and histone deacetylase complex to repress neuron-specific target genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 24 |pages= 13691-6 |year= 2000 |pmid= 10570134 |doi= }}
*{{cite journal | author=Grimes JA, Nielsen SJ, Battaglioli E, ''et al.'' |title=The co-repressor mSin3A is a functional component of the REST-CoREST repressor complex. |journal=J. Biol. Chem. |volume=275 |issue= 13 |pages= 9461-7 |year= 2000 |pmid= 10734093 |doi= }}
*{{cite journal | author=Coulson JM, Edgson JL, Woll PJ, Quinn JP |title=A splice variant of the neuron-restrictive silencer factor repressor is expressed in small cell lung cancer: a potential role in derepression of neuroendocrine genes and a useful clinical marker. |journal=Cancer Res. |volume=60 |issue= 7 |pages= 1840-4 |year= 2000 |pmid= 10766169 |doi= }}
*{{cite journal | author=Kojima T, Murai K, Naruse Y, ''et al.'' |title=Cell-type non-selective transcription of mouse and human genes encoding neural-restrictive silencer factor. |journal=Brain Res. Mol. Brain Res. |volume=90 |issue= 2 |pages= 174-86 |year= 2001 |pmid= 11406295 |doi= }}
*{{cite journal | author=Battaglioli E, Andrés ME, Rose DW, ''et al.'' |title=REST repression of neuronal genes requires components of the hSWI.SNF complex. |journal=J. Biol. Chem. |volume=277 |issue= 43 |pages= 41038-45 |year= 2002 |pmid= 12192000 |doi= 10.1074/jbc.M205691200 }}
*{{cite journal | author=Lunyak VV, Burgess R, Prefontaine GG, ''et al.'' |title=Corepressor-dependent silencing of chromosomal regions encoding neuronal genes. |journal=Science |volume=298 |issue= 5599 |pages= 1747-52 |year= 2002 |pmid= 12399542 |doi= 10.1126/science.1076469 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Lietz M, Hohl M, Thiel G |title=RE-1 silencing transcription factor (REST) regulates human synaptophysin gene transcription through an intronic sequence-specific DNA-binding site. |journal=Eur. J. Biochem. |volume=270 |issue= 1 |pages= 2-9 |year= 2003 |pmid= 12492469 |doi= }}
*{{cite journal | author=Hersh LB, Shimojo M |title=Regulation of cholinergic gene expression by the neuron restrictive silencer factor/repressor element-1 silencing transcription factor. |journal=Life Sci. |volume=72 |issue= 18-19 |pages= 2021-8 |year= 2003 |pmid= 12628452 |doi= }}
*{{cite journal | author=Kemp DM, Lin JC, Habener JF |title=Regulation of Pax4 paired homeodomain gene by neuron-restrictive silencer factor. |journal=J. Biol. Chem. |volume=278 |issue= 37 |pages= 35057-62 |year= 2003 |pmid= 12829700 |doi= 10.1074/jbc.M305891200 }}
*{{cite journal | author=Zuccato C, Tartari M, Crotti A, ''et al.'' |title=Huntingtin interacts with REST/NRSF to modulate the transcription of NRSE-controlled neuronal genes. |journal=Nat. Genet. |volume=35 |issue= 1 |pages= 76-83 |year= 2003 |pmid= 12881722 |doi= 10.1038/ng1219 }}
*{{cite journal | author=Martin D, Tawadros T, Meylan L, ''et al.'' |title=Critical role of the transcriptional repressor neuron-restrictive silencer factor in the specific control of connexin36 in insulin-producing cell lines. |journal=J. Biol. Chem. |volume=278 |issue= 52 |pages= 53082-9 |year= 2004 |pmid= 14565956 |doi= 10.1074/jbc.M306861200 }}
*{{cite journal | author=Kuwahara K, Saito Y, Takano M, ''et al.'' |title=NRSF regulates the fetal cardiac gene program and maintains normal cardiac structure and function. |journal=EMBO J. |volume=22 |issue= 23 |pages= 6310-21 |year= 2004 |pmid= 14633990 |doi= 10.1093/emboj/cdg601 }}
*{{cite journal | author=Kuwabara T, Hsieh J, Nakashima K, ''et al.'' |title=A small modulatory dsRNA specifies the fate of adult neural stem cells. |journal=Cell |volume=116 |issue= 6 |pages= 779-93 |year= 2004 |pmid= 15035981 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RPL5... {November 18, 2007 11:29:30 AM PST}
- SEARCH REDIRECT: Control Box Found: RPL5 {November 18, 2007 11:30:27 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:30:35 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:30:35 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:30:35 AM PST}
- UPDATED: Updated protein page: RPL5 {November 18, 2007 11:30:47 AM PST}
- INFO: Beginning work on TMSB4X... {November 18, 2007 11:31:51 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:33:03 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Thymosin, beta 4, X-linked
| HGNCid = 11881
| Symbol = TMSB4X
| AltSymbols =; FX; PTMB4; TB4X; TMSB4
| OMIM = 300159
| ECnumber =
| Homologene =
| MGIid =
| GeneAtlas_image1 = PBB_GE_TMSB4X_216438_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}}
| Process = {{GNF_GO|id=GO:0007010 |text = cytoskeleton organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7114
| Hs_Ensembl = ENSG00000205542
| Hs_RefseqProtein = NP_066932
| Hs_RefseqmRNA = NM_021109
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 12903148
| Hs_GenLoc_end = 12905267
| Hs_Uniprot = P62328
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Thymosin, beta 4, X-linked''', also known as '''TMSB4X''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TMSB4X thymosin, beta 4, X-linked| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7114| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes an actin sequestering protein which plays a role in regulation of actin polymerization. The protein is also involved in cell proliferation, migration, and differentiation. This gene escapes X inactivation and has a homolog on chromosome Y.<ref name="entrez">{{cite web | title = Entrez Gene: TMSB4X thymosin, beta 4, X-linked| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7114| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Huff T, Müller CS, Otto AM, ''et al.'' |title=beta-Thymosins, small acidic peptides with multiple functions. |journal=Int. J. Biochem. Cell Biol. |volume=33 |issue= 3 |pages= 205-20 |year= 2001 |pmid= 11311852 |doi= }}
*{{cite journal | author=Bubb MR |title=Thymosin beta 4 interactions. |journal=Vitam. Horm. |volume=66 |issue= |pages= 297-316 |year= 2003 |pmid= 12852258 |doi= }}
*{{cite journal | author=Goldschmidt-Clermont PJ, Furman MI, Wachsstock D, ''et al.'' |title=The control of actin nucleotide exchange by thymosin beta 4 and profilin. A potential regulatory mechanism for actin polymerization in cells. |journal=Mol. Biol. Cell |volume=3 |issue= 9 |pages= 1015-24 |year= 1992 |pmid= 1330091 |doi= }}
*{{cite journal | author=Sanders MC, Goldstein AL, Wang YL |title=Thymosin beta 4 (Fx peptide) is a potent regulator of actin polymerization in living cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 10 |pages= 4678-82 |year= 1992 |pmid= 1584803 |doi= }}
*{{cite journal | author=Safer D, Elzinga M, Nachmias VT |title=Thymosin beta 4 and Fx, an actin-sequestering peptide, are indistinguishable. |journal=J. Biol. Chem. |volume=266 |issue= 7 |pages= 4029-32 |year= 1991 |pmid= 1999398 |doi= }}
*{{cite journal | author=Clauss IM, Wathelet MG, Szpirer J, ''et al.'' |title=Human thymosin-beta 4/6-26 gene is part of a multigene family composed of seven members located on seven different chromosomes. |journal=Genomics |volume=9 |issue= 1 |pages= 174-80 |year= 1991 |pmid= 2004759 |doi= }}
*{{cite journal | author=Gómez-Márquez J, Dosil M, Segade F, ''et al.'' |title=Thymosin-beta 4 gene. Preliminary characterization and expression in tissues, thymic cells, and lymphocytes. |journal=J. Immunol. |volume=143 |issue= 8 |pages= 2740-4 |year= 1989 |pmid= 2677145 |doi= }}
*{{cite journal | author=Soma G, Murata M, Kitahara N, ''et al.'' |title=Detection of a countertranscript in promyelocytic leukemia cells HL60 during early differentiation by TPA. |journal=Biochem. Biophys. Res. Commun. |volume=132 |issue= 1 |pages= 100-9 |year= 1985 |pmid= 2998351 |doi= }}
*{{cite journal | author=Gondo H, Kudo J, White JW, ''et al.'' |title=Differential expression of the human thymosin-beta 4 gene in lymphocytes, macrophages, and granulocytes. |journal=J. Immunol. |volume=139 |issue= 11 |pages= 3840-8 |year= 1988 |pmid= 3500230 |doi= }}
*{{cite journal | author=Friedman RL, Manly SP, McMahon M, ''et al.'' |title=Transcriptional and posttranscriptional regulation of interferon-induced gene expression in human cells. |journal=Cell |volume=38 |issue= 3 |pages= 745-55 |year= 1984 |pmid= 6548414 |doi= }}
*{{cite journal | author=Erickson-Viitanen S, Ruggieri S, Natalini P, Horecker BL |title=Distribution of thymosin beta 4 in vertebrate classes. |journal=Arch. Biochem. Biophys. |volume=221 |issue= 2 |pages= 570-6 |year= 1983 |pmid= 6838210 |doi= }}
*{{cite journal | author=Pantaloni D, Carlier MF |title=How profilin promotes actin filament assembly in the presence of thymosin beta 4. |journal=Cell |volume=75 |issue= 5 |pages= 1007-14 |year= 1994 |pmid= 8252614 |doi= }}
*{{cite journal | author=Van Troys M, Dewitte D, Goethals M, ''et al.'' |title=The actin binding site of thymosin beta 4 mapped by mutational analysis. |journal=EMBO J. |volume=15 |issue= 2 |pages= 201-10 |year= 1996 |pmid= 8617195 |doi= }}
*{{cite journal | author=Feinberg J, Heitz F, Benyamin Y, Roustan C |title=The N-terminal sequences (5-20) of thymosin beta 4 binds to monomeric actin in an alpha-helical conformation. |journal=Biochem. Biophys. Res. Commun. |volume=222 |issue= 1 |pages= 127-32 |year= 1996 |pmid= 8630056 |doi= }}
*{{cite journal | author=Safer D, Sosnick TR, Elzinga M |title=Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends. |journal=Biochemistry |volume=36 |issue= 19 |pages= 5806-16 |year= 1997 |pmid= 9153421 |doi= 10.1021/bi970185v }}
*{{cite journal | author=Malinda KM, Goldstein AL, Kleinman HK |title=Thymosin beta 4 stimulates directional migration of human umbilical vein endothelial cells. |journal=FASEB J. |volume=11 |issue= 6 |pages= 474-81 |year= 1997 |pmid= 9194528 |doi= }}
*{{cite journal | author=Lahn BT, Page DC |title=Functional coherence of the human Y chromosome. |journal=Science |volume=278 |issue= 5338 |pages= 675-80 |year= 1997 |pmid= 9381176 |doi= }}
*{{cite journal | author=Chen J, Peterson RT, Schreiber SL |title=Alpha 4 associates with protein phosphatases 2A, 4, and 6. |journal=Biochem. Biophys. Res. Commun. |volume=247 |issue= 3 |pages= 827-32 |year= 1998 |pmid= 9647778 |doi= 10.1006/bbrc.1998.8792 }}
*{{cite journal | author=Huff T, Ballweber E, Humeny A, ''et al.'' |title=Thymosin beta(4) serves as a glutaminyl substrate of transglutaminase. Labeling with fluorescent dansylcadaverine does not abolish interaction with G-actin. |journal=FEBS Lett. |volume=464 |issue= 1-2 |pages= 14-20 |year= 2000 |pmid= 10611475 |doi= }}
*{{cite journal | author=De La Cruz EM, Ostap EM, Brundage RA, ''et al.'' |title=Thymosin-beta(4) changes the conformation and dynamics of actin monomers. |journal=Biophys. J. |volume=78 |issue= 5 |pages= 2516-27 |year= 2000 |pmid= 10777749 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TNFSF14... {November 18, 2007 11:36:48 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:37:37 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Tumor necrosis factor (ligand) superfamily, member 14
| HGNCid = 11930
| Symbol = TNFSF14
| AltSymbols =; TR2; CD258; HVEML; LIGHT; LTg
| OMIM = 604520
| ECnumber =
| Homologene = 2822
| MGIid = 1355317
| GeneAtlas_image1 = PBB_GE_TNFSF14_207907_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005164 |text = tumor necrosis factor receptor binding}} {{GNF_GO|id=GO:0043027 |text = caspase inhibitor activity}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0008588 |text = release of cytoplasmic sequestered NF-kappaB}} {{GNF_GO|id=GO:0043029 |text = T cell homeostasis}} {{GNF_GO|id=GO:0050798 |text = activated T cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8740
| Hs_Ensembl = ENSG00000125735
| Hs_RefseqProtein = NP_003798
| Hs_RefseqmRNA = NM_003807
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 6615568
| Hs_GenLoc_end = 6621599
| Hs_Uniprot = O43557
| Mm_EntrezGene = 50930
| Mm_Ensembl = ENSMUSG00000005824
| Mm_RefseqmRNA = NM_019418
| Mm_RefseqProtein = NP_062291
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 56874827
| Mm_GenLoc_end = 56879512
| Mm_Uniprot = Q059Y9
}}
}}
'''Tumor necrosis factor (ligand) superfamily, member 14''', also known as '''TNFSF14''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TNFSF14 tumor necrosis factor (ligand) superfamily, member 14| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8740| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the tumor necrosis factor (TNF) ligand family. This protein is a ligand for TNFRSF14, which is a member of the tumor necrosis factor receptor superfamily, and which is also known as a herpesvirus entry mediator (HVEM). This protein may function as a costimulatory factor for the activation of lymphoid cells and as a deterrent to infection by herpesvirus. This protein has been shown to stimulate the proliferation of T cells, and trigger apoptosis of various tumor cells. This protein is also reported to prevent tumor necrosis factor alpha mediated apoptosis in primary hepatocyte. Two alternatively spliced transcript variant encoding distinct isoforms have been reported.<ref name="entrez">{{cite web | title = Entrez Gene: TNFSF14 tumor necrosis factor (ligand) superfamily, member 14| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8740| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Yang D, Zhai Y, Zhang M |title=LIGHT, a new member of the TNF superfamily. |journal=J. Biol. Regul. Homeost. Agents |volume=16 |issue= 3 |pages= 206-10 |year= 2003 |pmid= 12456019 |doi= }}
*{{cite journal | author=Bénichou S, Benmerah A |title=[The HIV nef and the Kaposi-sarcoma-associated virus K3/K5 proteins: "parasites"of the endocytosis pathway] |journal=Med Sci (Paris) |volume=19 |issue= 1 |pages= 100-6 |year= 2003 |pmid= 12836198 |doi= }}
*{{cite journal | author=Anderson JL, Hope TJ |title=HIV accessory proteins and surviving the host cell. |journal=Current HIV/AIDS reports |volume=1 |issue= 1 |pages= 47-53 |year= 2005 |pmid= 16091223 |doi= }}
*{{cite journal | author=Mauri DN, Ebner R, Montgomery RI, ''et al.'' |title=LIGHT, a new member of the TNF superfamily, and lymphotoxin alpha are ligands for herpesvirus entry mediator. |journal=Immunity |volume=8 |issue= 1 |pages= 21-30 |year= 1998 |pmid= 9462508 |doi= }}
*{{cite journal | author=Marsters SA, Sheridan JP, Pitti RM, ''et al.'' |title=Identification of a ligand for the death-domain-containing receptor Apo3. |journal=Curr. Biol. |volume=8 |issue= 9 |pages= 525-8 |year= 1998 |pmid= 9560343 |doi= }}
*{{cite journal | author=Zhai Y, Guo R, Hsu TL, ''et al.'' |title=LIGHT, a novel ligand for lymphotoxin beta receptor and TR2/HVEM induces apoptosis and suppresses in vivo tumor formation via gene transfer. |journal=J. Clin. Invest. |volume=102 |issue= 6 |pages= 1142-51 |year= 1998 |pmid= 9739048 |doi= }}
*{{cite journal | author=Harrop JA, McDonnell PC, Brigham-Burke M, ''et al.'' |title=Herpesvirus entry mediator ligand (HVEM-L), a novel ligand for HVEM/TR2, stimulates proliferation of T cells and inhibits HT29 cell growth. |journal=J. Biol. Chem. |volume=273 |issue= 42 |pages= 27548-56 |year= 1998 |pmid= 9765287 |doi= }}
*{{cite journal | author=Yu KY, Kwon B, Ni J, ''et al.'' |title=A newly identified member of tumor necrosis factor receptor superfamily (TR6) suppresses LIGHT-mediated apoptosis. |journal=J. Biol. Chem. |volume=274 |issue= 20 |pages= 13733-6 |year= 1999 |pmid= 10318773 |doi= }}
*{{cite journal | author=Rooney IA, Butrovich KD, Glass AA, ''et al.'' |title=The lymphotoxin-beta receptor is necessary and sufficient for LIGHT-mediated apoptosis of tumor cells. |journal=J. Biol. Chem. |volume=275 |issue= 19 |pages= 14307-15 |year= 2000 |pmid= 10799510 |doi= }}
*{{cite journal | author=Lama J, Ware CF |title=Human immunodeficiency virus type 1 Nef mediates sustained membrane expression of tumor necrosis factor and the related cytokine LIGHT on activated T cells. |journal=J. Virol. |volume=74 |issue= 20 |pages= 9396-402 |year= 2000 |pmid= 11000208 |doi= }}
*{{cite journal | author=Morel Y, Schiano de Colella JM, Harrop J, ''et al.'' |title=Reciprocal expression of the TNF family receptor herpes virus entry mediator and its ligand LIGHT on activated T cells: LIGHT down-regulates its own receptor. |journal=J. Immunol. |volume=165 |issue= 8 |pages= 4397-404 |year= 2000 |pmid= 11035077 |doi= }}
*{{cite journal | author=Zhang J, Salcedo TW, Wan X, ''et al.'' |title=Modulation of T-cell responses to alloantigens by TR6/DcR3. |journal=J. Clin. Invest. |volume=107 |issue= 11 |pages= 1459-68 |year= 2001 |pmid= 11390428 |doi= }}
*{{cite journal | author=Granger SW, Butrovich KD, Houshmand P, ''et al.'' |title=Genomic characterization of LIGHT reveals linkage to an immune response locus on chromosome 19p13.3 and distinct isoforms generated by alternate splicing or proteolysis. |journal=J. Immunol. |volume=167 |issue= 9 |pages= 5122-8 |year= 2001 |pmid= 11673523 |doi= }}
*{{cite journal | author=Shaikh RB, Santee S, Granger SW, ''et al.'' |title=Constitutive expression of LIGHT on T cells leads to lymphocyte activation, inflammation, and tissue destruction. |journal=J. Immunol. |volume=167 |issue= 11 |pages= 6330-7 |year= 2002 |pmid= 11714797 |doi= }}
*{{cite journal | author=Bobik A, Kalinina N |title=Tumor necrosis factor receptor and ligand superfamily family members TNFRSF14 and LIGHT: new players in human atherogenesis. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=21 |issue= 12 |pages= 1873-5 |year= 2002 |pmid= 11742858 |doi= }}
*{{cite journal | author=Wang J, Lo JC, Foster A, ''et al.'' |title=The regulation of T cell homeostasis and autoimmunity by T cell-derived LIGHT. |journal=J. Clin. Invest. |volume=108 |issue= 12 |pages= 1771-80 |year= 2002 |pmid= 11748260 |doi= }}
*{{cite journal | author=Hsu TL, Chang YC, Chen SJ, ''et al.'' |title=Modulation of dendritic cell differentiation and maturation by decoy receptor 3. |journal=J. Immunol. |volume=168 |issue= 10 |pages= 4846-53 |year= 2002 |pmid= 11994433 |doi= }}
*{{cite journal | author=Castellano R, Van Lint C, Peri V, ''et al.'' |title=Mechanisms regulating expression of the tumor necrosis factor-related light gene. Role of calcium-signaling pathway in the transcriptional control. |journal=J. Biol. Chem. |volume=277 |issue= 45 |pages= 42841-51 |year= 2003 |pmid= 12215452 |doi= 10.1074/jbc.M207689200 }}
*{{cite journal | author=Matsui H, Hikichi Y, Tsuji I, ''et al.'' |title=LIGHT, a member of the tumor necrosis factor ligand superfamily, prevents tumor necrosis factor-alpha-mediated human primary hepatocyte apoptosis, but not Fas-mediated apoptosis. |journal=J. Biol. Chem. |volume=277 |issue= 51 |pages= 50054-61 |year= 2003 |pmid= 12393901 |doi= 10.1074/jbc.M206562200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on U2AF1... {November 18, 2007 11:33:03 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:33:53 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_U2AF1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1jmt.
| PDB = {{PDB2|1jmt}}
| Name = U2 small nuclear RNA auxiliary factor 1
| HGNCid = 12453
| Symbol = U2AF1
| AltSymbols =; DKFZp313J1712; FP793; RN; RNU2AF1; U2AF35; U2AFBP
| OMIM = 191317
| ECnumber =
| Homologene = 14345
| MGIid = 98884
| GeneAtlas_image1 = PBB_GE_U2AF1_202858_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005681 |text = spliceosome}} {{GNF_GO|id=GO:0015030 |text = Cajal body}}
| Process = {{GNF_GO|id=GO:0000398 |text = nuclear mRNA splicing, via spliceosome}} {{GNF_GO|id=GO:0008380 |text = RNA splicing}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7307
| Hs_Ensembl = ENSG00000160201
| Hs_RefseqProtein = NP_001020374
| Hs_RefseqmRNA = NM_001025203
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 21
| Hs_GenLoc_start = 43386136
| Hs_GenLoc_end = 43400757
| Hs_Uniprot = Q01081
| Mm_EntrezGene = 108121
| Mm_Ensembl = ENSMUSG00000061613
| Mm_RefseqmRNA = NM_024187
| Mm_RefseqProtein = NP_077149
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 31375793
| Mm_GenLoc_end = 31387432
| Mm_Uniprot = Q14C24
}}
}}
'''U2 small nuclear RNA auxiliary factor 1''', also known as '''U2AF1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: U2AF1 U2 small nuclear RNA auxiliary factor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7307| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene belongs to the splicing factor SR family of genes. U2 auxiliary factor, comprising a large and a small subunit, is a non-snRNP protein required for the binding of U2 snRNP to the pre-mRNA branch site. This gene encodes the small subunit which plays a critical role in both constitutive and enhancer-dependent RNA splicing by directly mediating interactions between the large subunit and proteins bound to the enhancers. Alternatively spliced transcript variants encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: U2AF1 U2 small nuclear RNA auxiliary factor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7307| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Zhang M, Zamore PD, Carmo-Fonseca M, ''et al.'' |title=Cloning and intracellular localization of the U2 small nuclear ribonucleoprotein auxiliary factor small subunit. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 18 |pages= 8769-73 |year= 1992 |pmid= 1388271 |doi= }}
*{{cite journal | author=Zamore PD, Green MR |title=Biochemical characterization of U2 snRNP auxiliary factor: an essential pre-mRNA splicing factor with a novel intranuclear distribution. |journal=EMBO J. |volume=10 |issue= 1 |pages= 207-14 |year= 1991 |pmid= 1824937 |doi= }}
*{{cite journal | author=Kalcheva I, Plass C, Sait S, ''et al.'' |title=Comparative mapping of the imprinted U2afbpL gene on mouse chromosome 11 and human chromosome 5. |journal=Cytogenet. Cell Genet. |volume=68 |issue= 1-2 |pages= 19-24 |year= 1994 |pmid= 7956352 |doi= }}
*{{cite journal | author=Wu JY, Maniatis T |title=Specific interactions between proteins implicated in splice site selection and regulated alternative splicing. |journal=Cell |volume=75 |issue= 6 |pages= 1061-70 |year= 1994 |pmid= 8261509 |doi= }}
*{{cite journal | author=Zuo P, Maniatis T |title=The splicing factor U2AF35 mediates critical protein-protein interactions in constitutive and enhancer-dependent splicing. |journal=Genes Dev. |volume=10 |issue= 11 |pages= 1356-68 |year= 1996 |pmid= 8647433 |doi= }}
*{{cite journal | author=Lalioti MD, Gos A, Green MR, ''et al.'' |title=The gene for human U2 snRNP auxiliary factor small 35-kDa subunit (U2AF1) maps to the progressive myoclonus epilepsy (EPM1) critical region on chromosome 21q22.3. |journal=Genomics |volume=33 |issue= 2 |pages= 298-300 |year= 1997 |pmid= 8660980 |doi= 10.1006/geno.1996.0196 }}
*{{cite journal | author=Hong W, Bennett M, Xiao Y, ''et al.'' |title=Association of U2 snRNP with the spliceosomal complex E. |journal=Nucleic Acids Res. |volume=25 |issue= 2 |pages= 354-61 |year= 1997 |pmid= 9016565 |doi= }}
*{{cite journal | author=Tronchère H, Wang J, Fu XD |title=A protein related to splicing factor U2AF35 that interacts with U2AF65 and SR proteins in splicing of pre-mRNA. |journal=Nature |volume=388 |issue= 6640 |pages= 397-400 |year= 1997 |pmid= 9237760 |doi= 10.1038/41137 }}
*{{cite journal | author=Wang HY, Lin W, Dyck JA, ''et al.'' |title=SRPK2: a differentially expressed SR protein-specific kinase involved in mediating the interaction and localization of pre-mRNA splicing factors in mammalian cells. |journal=J. Cell Biol. |volume=140 |issue= 4 |pages= 737-50 |year= 1998 |pmid= 9472028 |doi= }}
*{{cite journal | author=Rudner DZ, Kanaar R, Breger KS, Rio DC |title=Interaction between subunits of heterodimeric splicing factor U2AF is essential in vivo. |journal=Mol. Cell. Biol. |volume=18 |issue= 4 |pages= 1765-73 |year= 1998 |pmid= 9528748 |doi= }}
*{{cite journal | author=Lallena MJ, Martínez C, Valcárcel J, Correas I |title=Functional association of nuclear protein 4.1 with pre-mRNA splicing factors. |journal=J. Cell. Sci. |volume=111 ( Pt 14) |issue= |pages= 1963-71 |year= 1998 |pmid= 9645944 |doi= }}
*{{cite journal | author=Gozani O, Potashkin J, Reed R |title=A potential role for U2AF-SAP 155 interactions in recruiting U2 snRNP to the branch site. |journal=Mol. Cell. Biol. |volume=18 |issue= 8 |pages= 4752-60 |year= 1998 |pmid= 9671485 |doi= }}
*{{cite journal | author=Neubauer G, King A, Rappsilber J, ''et al.'' |title=Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex. |journal=Nat. Genet. |volume=20 |issue= 1 |pages= 46-50 |year= 1998 |pmid= 9731529 |doi= 10.1038/1700 }}
*{{cite journal | author=Xiao SH, Manley JL |title=Phosphorylation-dephosphorylation differentially affects activities of splicing factor ASF/SF2. |journal=EMBO J. |volume=17 |issue= 21 |pages= 6359-67 |year= 1999 |pmid= 9799243 |doi= 10.1093/emboj/17.21.6359 }}
*{{cite journal | author=Hattori M, Fujiyama A, Taylor TD, ''et al.'' |title=The DNA sequence of human chromosome 21. |journal=Nature |volume=405 |issue= 6784 |pages= 311-9 |year= 2000 |pmid= 10830953 |doi= 10.1038/35012518 }}
*{{cite journal | author=de Vries H, Rüegsegger U, Hübner W, ''et al.'' |title=Human pre-mRNA cleavage factor II(m) contains homologs of yeast proteins and bridges two other cleavage factors. |journal=EMBO J. |volume=19 |issue= 21 |pages= 5895-904 |year= 2000 |pmid= 11060040 |doi= 10.1093/emboj/19.21.5895 }}
*{{cite journal | author=Gama-Carvalho M, Carvalho MP, Kehlenbach A, ''et al.'' |title=Nucleocytoplasmic shuttling of heterodimeric splicing factor U2AF. |journal=J. Biol. Chem. |volume=276 |issue= 16 |pages= 13104-12 |year= 2001 |pmid= 11118443 |doi= 10.1074/jbc.M008759200 }}
*{{cite journal | author=Adams DJ, van der Weyden L, Mayeda A, ''et al.'' |title=ZNF265--a novel spliceosomal protein able to induce alternative splicing. |journal=J. Cell Biol. |volume=154 |issue= 1 |pages= 25-32 |year= 2001 |pmid= 11448987 |doi= }}
*{{cite journal | author=Will CL, Schneider C, MacMillan AM, ''et al.'' |title=A novel U2 and U11/U12 snRNP protein that associates with the pre-mRNA branch site. |journal=EMBO J. |volume=20 |issue= 16 |pages= 4536-46 |year= 2001 |pmid= 11500380 |doi= 10.1093/emboj/20.16.4536 }}
*{{cite journal | author=Nesic D, Krämer A |title=Domains in human splicing factors SF3a60 and SF3a66 required for binding to SF3a120, assembly of the 17S U2 snRNP, and prespliceosome formation. |journal=Mol. Cell. Biol. |volume=21 |issue= 19 |pages= 6406-17 |year= 2001 |pmid= 11533230 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on XRCC3... {November 18, 2007 11:33:54 AM PST}
- SEARCH REDIRECT: Control Box Found: XRCC3 {November 18, 2007 11:34:29 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:34:36 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:34:36 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:34:36 AM PST}
- UPDATED: Updated protein page: XRCC3 {November 18, 2007 11:34:50 AM PST}
end log.
