Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 19:50, 17 November 2007 (UTC)
[edit]Proteins without matches (9)
[edit]Proteins with a High Potential Match (6)
[edit]Redirected Proteins (10)
[edit]Manual Inspection (Page not found) (15)
[edit]
Protein Status Grid - Date: 19:50, 17 November 2007 (UTC)
[edit]Vebose Log - Date: 19:50, 17 November 2007 (UTC)
[edit]- INFO: Beginning work on ACTN2... {November 17, 2007 11:26:17 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:26:43 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
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| 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_ACTN2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1h8b.
| PDB = {{PDB2|1h8b}}, {{PDB2|1hci}}, {{PDB2|1quu}}, {{PDB2|1tjt}}, {{PDB2|1wku}}
| Name = Actinin, alpha 2
| HGNCid = 164
| Symbol = ACTN2
| AltSymbols =;
| OMIM = 102573
| ECnumber =
| Homologene = 31016
| MGIid = 109192
| GeneAtlas_image1 = PBB_GE_ACTN2_203862_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ACTN2_203861_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_ACTN2_203863_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005178 |text = integrin binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0008307 |text = structural constituent of muscle}} {{GNF_GO|id=GO:0030375 |text = thyroid hormone receptor coactivator activity}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0051370 |text = ZASP binding}} {{GNF_GO|id=GO:0051374 |text = FATZ 1 binding}}
| Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005884 |text = actin filament}} {{GNF_GO|id=GO:0005925 |text = focal adhesion}} {{GNF_GO|id=GO:0030018 |text = Z disc}} {{GNF_GO|id=GO:0030175 |text = filopodium}} {{GNF_GO|id=GO:0031143 |text = pseudopodium}} {{GNF_GO|id=GO:0043197 |text = dendritic spine}}
| Process = {{GNF_GO|id=GO:0006936 |text = muscle contraction}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0030035 |text = microspike biogenesis}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}} {{GNF_GO|id=GO:0048041 |text = focal adhesion formation}} {{GNF_GO|id=GO:0051289 |text = protein homotetramerization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 88
| Hs_Ensembl = ENSG00000077522
| Hs_RefseqProtein = NP_001094
| Hs_RefseqmRNA = NM_001103
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 234916431
| Hs_GenLoc_end = 234994554
| Hs_Uniprot = P35609
| Mm_EntrezGene = 11472
| Mm_Ensembl = ENSMUSG00000052374
| Mm_RefseqmRNA = NM_033268
| Mm_RefseqProtein = NP_150371
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 12323759
| Mm_GenLoc_end = 12395065
| Mm_Uniprot = Q5FW75
}}
}}
'''Actinin, alpha 2''', also known as '''ACTN2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACTN2 actinin, alpha 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=88| 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 = Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments. This gene encodes a muscle-specific, alpha actinin isoform that is expressed in both skeletal and cardiac muscles. Transcript variants resulting from the use of multiple poly_A sites have been observed.<ref name="entrez">{{cite web | title = Entrez Gene: ACTN2 actinin, alpha 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=88| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Faulkner G, Lanfranchi G, Valle G |title=Telethonin and other new proteins of the Z-disc of skeletal muscle. |journal=IUBMB Life |volume=51 |issue= 5 |pages= 275-82 |year= 2002 |pmid= 11699871 |doi= }}
*{{cite journal | author=Beggs AH, Byers TJ, Knoll JH, ''et al.'' |title=Cloning and characterization of two human skeletal muscle alpha-actinin genes located on chromosomes 1 and 11. |journal=J. Biol. Chem. |volume=267 |issue= 13 |pages= 9281-8 |year= 1992 |pmid= 1339456 |doi= }}
*{{cite journal | author=Beggs AH, Phillips HA, Kozman H, ''et al.'' |title=A (CA)n repeat polymorphism for the human skeletal muscle alpha-actinin gene ACTN2 and its localization on the linkage map of chromosome 1. |journal=Genomics |volume=13 |issue= 4 |pages= 1314-5 |year= 1992 |pmid= 1505962 |doi= }}
*{{cite journal | author=Yürüker B, Niggli V |title=Alpha-actinin and vinculin in human neutrophils: reorganization during adhesion and relation to the actin network. |journal=J. Cell. Sci. |volume=101 ( Pt 2) |issue= |pages= 403-14 |year= 1992 |pmid= 1629252 |doi= }}
*{{cite journal | author=Pavalko FM, LaRoche SM |title=Activation of human neutrophils induces an interaction between the integrin beta 2-subunit (CD18) and the actin binding protein alpha-actinin. |journal=J. Immunol. |volume=151 |issue= 7 |pages= 3795-807 |year= 1993 |pmid= 8104223 |doi= }}
*{{cite journal | author=Yoshida M, Westlin WF, Wang N, ''et al.'' |title=Leukocyte adhesion to vascular endothelium induces E-selectin linkage to the actin cytoskeleton. |journal=J. Cell Biol. |volume=133 |issue= 2 |pages= 445-55 |year= 1996 |pmid= 8609175 |doi= }}
*{{cite journal | author=Wyszynski M, Lin J, Rao A, ''et al.'' |title=Competitive binding of alpha-actinin and calmodulin to the NMDA receptor. |journal=Nature |volume=385 |issue= 6615 |pages= 439-42 |year= 1997 |pmid= 9009191 |doi= 10.1038/385439a0 }}
*{{cite journal | author=Mukai H, Toshimori M, Shibata H, ''et al.'' |title=Interaction of PKN with alpha-actinin. |journal=J. Biol. Chem. |volume=272 |issue= 8 |pages= 4740-6 |year= 1997 |pmid= 9030526 |doi= }}
*{{cite journal | author=Young P, Ferguson C, Bañuelos S, Gautel M |title=Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of alpha-actinin. |journal=EMBO J. |volume=17 |issue= 6 |pages= 1614-24 |year= 1998 |pmid= 9501083 |doi= 10.1093/emboj/17.6.1614 }}
*{{cite journal | author=Zhang S, Ehlers MD, Bernhardt JP, ''et al.'' |title=Calmodulin mediates calcium-dependent inactivation of N-methyl-D-aspartate receptors. |journal=Neuron |volume=21 |issue= 2 |pages= 443-53 |year= 1998 |pmid= 9728925 |doi= }}
*{{cite journal | author=Krupp JJ, Vissel B, Thomas CG, ''et al.'' |title=Interactions of calmodulin and alpha-actinin with the NR1 subunit modulate Ca2+-dependent inactivation of NMDA receptors. |journal=J. Neurosci. |volume=19 |issue= 4 |pages= 1165-78 |year= 1999 |pmid= 9952395 |doi= }}
*{{cite journal | author=Zhou Q, Ruiz-Lozano P, Martone ME, Chen J |title=Cypher, a striated muscle-restricted PDZ and LIM domain-containing protein, binds to alpha-actinin-2 and protein kinase C. |journal=J. Biol. Chem. |volume=274 |issue= 28 |pages= 19807-13 |year= 1999 |pmid= 10391924 |doi= }}
*{{cite journal | author=Faulkner G, Pallavicini A, Formentin E, ''et al.'' |title=ZASP: a new Z-band alternatively spliced PDZ-motif protein. |journal=J. Cell Biol. |volume=146 |issue= 2 |pages= 465-75 |year= 1999 |pmid= 10427098 |doi= }}
*{{cite journal | author=Tiso N, Majetti M, Stanchi F, ''et al.'' |title=Fine mapping and genomic structure of ACTN2, the human gene coding for the sarcomeric isoform of alpha-actinin-2, expressed in skeletal and cardiac muscle. |journal=Biochem. Biophys. Res. Commun. |volume=265 |issue= 1 |pages= 256-9 |year= 1999 |pmid= 10548523 |doi= 10.1006/bbrc.1999.1661 }}
*{{cite journal | author=Nikolopoulos SN, Spengler BA, Kisselbach K, ''et al.'' |title=The human non-muscle alpha-actinin protein encoded by the ACTN4 gene suppresses tumorigenicity of human neuroblastoma cells. |journal=Oncogene |volume=19 |issue= 3 |pages= 380-6 |year= 2000 |pmid= 10656685 |doi= 10.1038/sj.onc.1203310 }}
*{{cite journal | author=Galliano MF, Huet C, Frygelius J, ''et al.'' |title=Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha -actinin-2, is required for myoblast fusion. |journal=J. Biol. Chem. |volume=275 |issue= 18 |pages= 13933-9 |year= 2000 |pmid= 10788519 |doi= }}
*{{cite journal | author=Maruoka ND, Steele DF, Au BP, ''et al.'' |title=alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells. |journal=FEBS Lett. |volume=473 |issue= 2 |pages= 188-94 |year= 2000 |pmid= 10812072 |doi= }}
*{{cite journal | author=Kotaka M, Kostin S, Ngai S, ''et al.'' |title=Interaction of hCLIM1, an enigma family protein, with alpha-actinin 2. |journal=J. Cell. Biochem. |volume=78 |issue= 4 |pages= 558-65 |year= 2000 |pmid= 10861853 |doi= }}
*{{cite journal | author=Parast MM, Otey CA |title=Characterization of palladin, a novel protein localized to stress fibers and cell adhesions. |journal=J. Cell Biol. |volume=150 |issue= 3 |pages= 643-56 |year= 2000 |pmid= 10931874 |doi= }}
*{{cite journal | author=Faulkner G, Pallavicini A, Comelli A, ''et al.'' |title=FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle. |journal=J. Biol. Chem. |volume=275 |issue= 52 |pages= 41234-42 |year= 2001 |pmid= 10984498 |doi= 10.1074/jbc.M007493200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ACTR3... {November 17, 2007 11:39:11 AM PST}
- SEARCH REDIRECT: Control Box Found: ACTR3 {November 17, 2007 11:39:46 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:39:47 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:39:47 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:39:47 AM PST}
- UPDATED: Updated protein page: ACTR3 {November 17, 2007 11:39:54 AM PST}
- INFO: Beginning work on APCS... {November 17, 2007 11:26:43 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:27:19 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_APCS_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1gyk.
| PDB = {{PDB2|1gyk}}, {{PDB2|1lgn}}, {{PDB2|1sac}}, {{PDB2|2a3w}}, {{PDB2|2a3x}}, {{PDB2|2a3y}}
| Name = Amyloid P component, serum
| HGNCid = 584
| Symbol = APCS
| AltSymbols =; MGC88159; PTX2; SAP
| OMIM = 104770
| ECnumber =
| Homologene = 1239
| MGIid = 98229
| GeneAtlas_image1 = PBB_GE_APCS_206350_at_tn.png
| Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005529 |text = sugar binding}} {{GNF_GO|id=GO:0051082 |text = unfolded protein binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0006953 |text = acute-phase response}} {{GNF_GO|id=GO:0051131 |text = chaperone-mediated protein complex assembly}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 325
| Hs_Ensembl = ENSG00000132703
| Hs_RefseqProtein = NP_001630
| Hs_RefseqmRNA = NM_001639
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 157824240
| Hs_GenLoc_end = 157825284
| Hs_Uniprot = P02743
| Mm_EntrezGene = 20219
| Mm_Ensembl = ENSMUSG00000026542
| Mm_RefseqmRNA = NM_011318
| Mm_RefseqProtein = NP_035448
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 174730637
| Mm_GenLoc_end = 174731718
| Mm_Uniprot = Q4JFI8
}}
}}
'''Amyloid P component, serum''', also known as '''APCS''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: APCS amyloid P component, serum| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=325| 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 glycoprotein, belonging to the pentraxin family of proteins, which has a characteristic pentameric organization. These family members have considerable sequence homology which is thought to be the result of gene duplication. The binding of the encoded protein to proteins in the pathological amyloid cross-beta fold suggests its possible role as a chaperone. This protein is also thought to control the degradation of chromatin. It has been demonstrated that this protein binds to apoptotic cells at an early stage, which raises the possibility that it is involved in dealing with apoptotic cells in vivo. This gene has multiple polyadenylation sites.<ref name="entrez">{{cite web | title = Entrez Gene: APCS amyloid P component, serum| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=325| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Thompson AR, Enfield DL |title=Human plasma P component: isolation and characterization. |journal=Biochemistry |volume=17 |issue= 20 |pages= 4304-11 |year= 1979 |pmid= 81686 |doi= }}
*{{cite journal | author=Swanson SJ, Christner RB, Mortensen RF |title=Human serum amyloid P-component (SAP) selectively binds to immobilized or bound forms of C-reactive protein (CRP). |journal=Biochim. Biophys. Acta |volume=1160 |issue= 3 |pages= 309-16 |year= 1993 |pmid= 1477104 |doi= }}
*{{cite journal | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi= }}
*{{cite journal | author=Mantzouranis EC, Dowton SB, Whitehead AS, ''et al.'' |title=Human serum amyloid P component. cDNA isolation, complete sequence of pre-serum amyloid P component, and localization of the gene to chromosome 1. |journal=J. Biol. Chem. |volume=260 |issue= 12 |pages= 7752-6 |year= 1985 |pmid= 2987268 |doi= }}
*{{cite journal | author=Ohnishi S, Maeda S, Shimada K, Arao T |title=Isolation and characterization of the complete complementary and genomic DNA sequences of human serum amyloid P component. |journal=J. Biochem. |volume=100 |issue= 4 |pages= 849-58 |year= 1987 |pmid= 3029048 |doi= }}
*{{cite journal | author=Wood SP, Oliva G, O'Hara BP, ''et al.'' |title=A pentameric form of human serum amyloid P component. Crystallization, X-ray diffraction and neutron scattering studies. |journal=J. Mol. Biol. |volume=202 |issue= 1 |pages= 169-73 |year= 1988 |pmid= 3172210 |doi= }}
*{{cite journal | author=Kubak BM, Potempa LA, Anderson B, ''et al.'' |title=Evidence that serum amyloid P component binds to mannose-terminated sequences of polysaccharides and glycoproteins. |journal=Mol. Immunol. |volume=25 |issue= 9 |pages= 851-8 |year= 1989 |pmid= 3211159 |doi= }}
*{{cite journal | author=Floyd-Smith G, Whitehead AS, Colten HR, Francke U |title=The human C-reactive protein gene (CRP) and serum amyloid P component gene (APCS) are located on the proximal long arm of chromosome 1. |journal=Immunogenetics |volume=24 |issue= 3 |pages= 171-6 |year= 1986 |pmid= 3759147 |doi= }}
*{{cite journal | author=Borojevic R, Druguet M, Scharfstein J, Stocker S |title=Amyloid P component is present in cultured human smooth muscle cells but not in cultured skin fibroblasts. |journal=Braz. J. Med. Biol. Res. |volume=18 |issue= 4 |pages= 493-8 |year= 1986 |pmid= 3915434 |doi= }}
*{{cite journal | author=Prelli F, Pras M, Frangione B |title=The primary structure of human tissue amyloid P component from a patient with primary idiopathic amyloidosis. |journal=J. Biol. Chem. |volume=260 |issue= 24 |pages= 12895-8 |year= 1985 |pmid= 4055725 |doi= }}
*{{cite journal | author=García de Frutos P, Härdig Y, Dahlbäck B |title=Serum amyloid P component binding to C4b-binding protein. |journal=J. Biol. Chem. |volume=270 |issue= 45 |pages= 26950-5 |year= 1995 |pmid= 7592941 |doi= }}
*{{cite journal | author=Emsley J, White HE, O'Hara BP, ''et al.'' |title=Structure of pentameric human serum amyloid P component. |journal=Nature |volume=367 |issue= 6461 |pages= 338-45 |year= 1994 |pmid= 8114934 |doi= 10.1038/367338a0 }}
*{{cite journal | author=Christner RB, Mortensen RF |title=Specificity of the binding interaction between human serum amyloid P-component and immobilized human C-reactive protein. |journal=J. Biol. Chem. |volume=269 |issue= 13 |pages= 9760-6 |year= 1994 |pmid= 8144569 |doi= }}
*{{cite journal | author=Pepys MB, Rademacher TW, Amatayakul-Chantler S, ''et al.'' |title=Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 12 |pages= 5602-6 |year= 1994 |pmid= 8202534 |doi= }}
*{{cite journal | author=Ying SC, Gewurz AT, Jiang H, Gewurz H |title=Human serum amyloid P component oligomers bind and activate the classical complement pathway via residues 14-26 and 76-92 of the A chain collagen-like region of C1q. |journal=J. Immunol. |volume=150 |issue= 1 |pages= 169-76 |year= 1993 |pmid= 8417122 |doi= }}
*{{cite journal | author=Zahedi K |title=Characterization of the binding of serum amyloid P to type IV collagen. |journal=J. Biol. Chem. |volume=271 |issue= 25 |pages= 14897-902 |year= 1996 |pmid= 8662978 |doi= }}
*{{cite journal | author=Zahedi K |title=Characterization of the binding of serum amyloid P to laminin. |journal=J. Biol. Chem. |volume=272 |issue= 4 |pages= 2143-8 |year= 1997 |pmid= 8999915 |doi= }}
*{{cite journal | author=Hohenester E, Hutchinson WL, Pepys MB, Wood SP |title=Crystal structure of a decameric complex of human serum amyloid P component with bound dAMP. |journal=J. Mol. Biol. |volume=269 |issue= 4 |pages= 570-8 |year= 1997 |pmid= 9217261 |doi= 10.1006/jmbi.1997.1075 }}
*{{cite journal | author=Vorum H, Jacobsen C, Honoré B |title=Calumenin interacts with serum amyloid P component. |journal=FEBS Lett. |volume=465 |issue= 2-3 |pages= 129-34 |year= 2000 |pmid= 10631319 |doi= }}
*{{cite journal | author=Coker AR, Purvis A, Baker D, ''et al.'' |title=Molecular chaperone properties of serum amyloid P component. |journal=FEBS Lett. |volume=473 |issue= 2 |pages= 199-202 |year= 2000 |pmid= 10812074 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CAPN2... {November 17, 2007 11:27:19 AM PST}
- SEARCH REDIRECT: Control Box Found: CAPN2 {November 17, 2007 11:27:50 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:27:51 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:27:51 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:27:51 AM PST}
- UPDATED: Updated protein page: CAPN2 {November 17, 2007 11:27:57 AM PST}
- INFO: Beginning work on CD74... {November 17, 2007 11:27:57 AM PST}
- SEARCH REDIRECT: Control Box Found: CD74 {November 17, 2007 11:28:30 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:28:31 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:28:31 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:28:31 AM PST}
- UPDATED: Updated protein page: CD74 {November 17, 2007 11:28:40 AM PST}
- INFO: Beginning work on CDC25B... {November 17, 2007 11:28:40 AM PST}
- SEARCH REDIRECT: Control Box Found: CDC25B {November 17, 2007 11:29:07 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:29:08 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:29:08 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:29:08 AM PST}
- UPDATED: Updated protein page: CDC25B {November 17, 2007 11:29:13 AM PST}
- INFO: Beginning work on CHRNA4... {November 17, 2007 11:29:14 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:29:53 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 =
| image_source =
| PDB =
| Name = Cholinergic receptor, nicotinic, alpha 4
| HGNCid = 1958
| Symbol = CHRNA4
| AltSymbols =; BFNC; EBN; EBN1; NACRA4
| OMIM = 118504
| ECnumber =
| Homologene = 592
| MGIid = 87888
| GeneAtlas_image1 = PBB_GE_CHRNA4_206735_at_tn.png
| GeneAtlas_image2 = PBB_GE_CHRNA4_206736_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_CHRNA4_216900_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004889 |text = nicotinic acetylcholine-activated cation-selective channel activity}} {{GNF_GO|id=GO:0005216 |text = ion channel activity}} {{GNF_GO|id=GO:0005230 |text = extracellular ligand-gated ion channel activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0015464 |text = acetylcholine receptor activity}} {{GNF_GO|id=GO:0030594 |text = neurotransmitter receptor activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005892 |text = nicotinic acetylcholine-gated receptor-channel complex}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0045211 |text = postsynaptic membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007271 |text = synaptic transmission, cholinergic}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0007610 |text = behavior}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1137
| Hs_Ensembl = ENSG00000101204
| Hs_RefseqProtein = NP_000735
| Hs_RefseqmRNA = NM_000744
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 61445864
| Hs_GenLoc_end = 61475777
| Hs_Uniprot = P43681
| Mm_EntrezGene = 11438
| Mm_Ensembl = ENSMUSG00000027577
| Mm_RefseqmRNA = NM_015730
| Mm_RefseqProtein = NP_056545
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 180951719
| Mm_GenLoc_end = 180968585
| Mm_Uniprot = Q53YK0
}}
}}
'''Cholinergic receptor, nicotinic, alpha 4''', also known as '''CHRNA4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CHRNA4 cholinergic receptor, nicotinic, alpha 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1137| 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 nicotinic acetylcholine receptors (nAChRs) are members of a superfamily of ligand-gated ion channels that mediate fast signal transmission at synapses. After binding acetylcholine, these pentameric receptors respond by undergoing an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The protein encoded by this gene is an integral membrane receptor subunit that can interact with either nAChR beta-2 or nAChR beta-4 to form a functional receptor. Mutations in this gene appear to account for a small proportion of the cases of nocturnal frontal lobe epilepsy.<ref name="entrez">{{cite web | title = Entrez Gene: CHRNA4 cholinergic receptor, nicotinic, alpha 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1137| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Skorupska E, Rózycka A, Trzeciak WH |title=[Molecular and genetic basis of idiopathic nocturnal frontal lobe epilepsy] |journal=Neurol. Neurochir. Pol. |volume=36 |issue= 3 |pages= 513-25 |year= 2002 |pmid= 12185808 |doi= }}
*{{cite journal | author=Pilz AJ, Willer E, Povey S, Abbott CM |title=The genes coding for phosphoenolpyruvate carboxykinase-1 (PCK1) and neuronal nicotinic acetylcholine receptor alpha 4 subunit (CHRNA4) map to human chromosome 20, extending the known region of homology with mouse chromosome 2. |journal=Ann. Hum. Genet. |volume=56 |issue= Pt 4 |pages= 289-93 |year= 1993 |pmid= 1492743 |doi= }}
*{{cite journal | author=Anand R, Lindstrom J |title=Chromosomal localization of seven neuronal nicotinic acetylcholine receptor subunit genes in humans. |journal=Genomics |volume=13 |issue= 4 |pages= 962-7 |year= 1992 |pmid= 1505988 |doi= }}
*{{cite journal | author=McLane KE, Wu XD, Conti-Tronconi BM |title=Identification of a brain acetylcholine receptor alpha subunit able to bind alpha-bungarotoxin. |journal=J. Biol. Chem. |volume=265 |issue= 17 |pages= 9816-24 |year= 1990 |pmid= 2351675 |doi= }}
*{{cite journal | author=Steinlein OK, Mulley JC, Propping P, ''et al.'' |title=A missense mutation in the neuronal nicotinic acetylcholine receptor alpha 4 subunit is associated with autosomal dominant nocturnal frontal lobe epilepsy. |journal=Nat. Genet. |volume=11 |issue= 2 |pages= 201-3 |year= 1995 |pmid= 7550350 |doi= 10.1038/ng1095-201 }}
*{{cite journal | author=Phillips HA, Scheffer IE, Berkovic SF, ''et al.'' |title=Localization of a gene for autosomal dominant nocturnal frontal lobe epilepsy to chromosome 20q 13.2. |journal=Nat. Genet. |volume=10 |issue= 1 |pages= 117-8 |year= 1995 |pmid= 7647781 |doi= 10.1038/ng0595-117 }}
*{{cite journal | author=Monteggia LM, Gopalakrishnan M, Touma E, ''et al.'' |title=Cloning and transient expression of genes encoding the human alpha 4 and beta 2 neuronal nicotinic acetylcholine receptor (nAChR) subunits. |journal=Gene |volume=155 |issue= 2 |pages= 189-93 |year= 1995 |pmid= 7721089 |doi= }}
*{{cite journal | author=Steinlein O, Smigrodzki R, Lindstrom J, ''et al.'' |title=Refinement of the localization of the gene for neuronal nicotinic acetylcholine receptor alpha 4 subunit (CHRNA4) to human chromosome 20q13.2-q13.3. |journal=Genomics |volume=22 |issue= 2 |pages= 493-5 |year= 1995 |pmid= 7806245 |doi= 10.1006/geno.1994.1420 }}
*{{cite journal | author=Steinlein O, Weiland S, Stoodt J, Propping P |title=Exon-intron structure of the human neuronal nicotinic acetylcholine receptor alpha 4 subunit (CHRNA4). |journal=Genomics |volume=32 |issue= 2 |pages= 289-94 |year= 1997 |pmid= 8833159 |doi= 10.1006/geno.1996.0119 }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Elliott KJ, Ellis SB, Berckhan KJ, ''et al.'' |title=Comparative structure of human neuronal alpha 2-alpha 7 and beta 2-beta 4 nicotinic acetylcholine receptor subunits and functional expression of the alpha 2, alpha 3, alpha 4, alpha 7, beta 2, and beta 4 subunits. |journal=J. Mol. Neurosci. |volume=7 |issue= 3 |pages= 217-28 |year= 1997 |pmid= 8906617 |doi= }}
*{{cite journal | author=Groot Kormelink PJ, Luyten WH |title=Cloning and sequence of full-length cDNAs encoding the human neuronal nicotinic acetylcholine receptor (nAChR) subunits beta3 and beta4 and expression of seven nAChR subunits in the human neuroblastoma cell line SH-SY5Y and/or IMR-32. |journal=FEBS Lett. |volume=400 |issue= 3 |pages= 309-14 |year= 1997 |pmid= 9009220 |doi= }}
*{{cite journal | author=Hirose S, Iwata H, Akiyoshi H, ''et al.'' |title=A novel mutation of CHRNA4 responsible for autosomal dominant nocturnal frontal lobe epilepsy. |journal=Neurology |volume=53 |issue= 8 |pages= 1749-53 |year= 1999 |pmid= 10563623 |doi= }}
*{{cite journal | author=Samochocki M, Zerlin M, Jostock R, ''et al.'' |title=Galantamine is an allosterically potentiating ligand of the human alpha4/beta2 nAChR. |journal=Acta Neurol. Scand., Suppl. |volume=176 |issue= |pages= 68-73 |year= 2001 |pmid= 11261808 |doi= }}
*{{cite journal | author=Jeanclos EM, Lin L, Treuil MW, ''et al.'' |title=The chaperone protein 14-3-3eta interacts with the nicotinic acetylcholine receptor alpha 4 subunit. Evidence for a dynamic role in subunit stabilization. |journal=J. Biol. Chem. |volume=276 |issue= 30 |pages= 28281-90 |year= 2001 |pmid= 11352901 |doi= 10.1074/jbc.M011549200 }}
*{{cite journal | author=Engidawork E, Gulesserian T, Balic N, ''et al.'' |title=Changes in nicotinic acetylcholine receptor subunits expression in brain of patients with Down syndrome and Alzheimer's disease. |journal=J. Neural Transm. Suppl. |volume= |issue= 61 |pages= 211-22 |year= 2002 |pmid= 11771745 |doi= }}
*{{cite journal | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
*{{cite journal | author=Bertrand D, Picard F, Le Hellard S, ''et al.'' |title=How mutations in the nAChRs can cause ADNFLE epilepsy. |journal=Epilepsia |volume=43 Suppl 5 |issue= |pages= 112-22 |year= 2002 |pmid= 12121305 |doi= }}
*{{cite journal | author=Heeschen C, Weis M, Aicher A, ''et al.'' |title=A novel angiogenic pathway mediated by non-neuronal nicotinic acetylcholine receptors. |journal=J. Clin. Invest. |volume=110 |issue= 4 |pages= 527-36 |year= 2002 |pmid= 12189247 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CRHR1... {November 17, 2007 11:29:53 AM PST}
- SEARCH REDIRECT: Control Box Found: CRHR1 {November 17, 2007 11:30:39 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:30:42 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:30:42 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:30:42 AM PST}
- UPDATED: Updated protein page: CRHR1 {November 17, 2007 11:30:48 AM PST}
- INFO: Beginning work on DEFB1... {November 17, 2007 11:31:37 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:32:16 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_DEFB1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1e4s.
| PDB = {{PDB2|1e4s}}, {{PDB2|1iju}}, {{PDB2|1ijv}}, {{PDB2|1kj5}}, {{PDB2|2nlb}}, {{PDB2|2nlc}}, {{PDB2|2nld}}, {{PDB2|2nle}}, {{PDB2|2nlf}}, {{PDB2|2nlg}}, {{PDB2|2nlh}}, {{PDB2|2nlp}}, {{PDB2|2nlq}}, {{PDB2|2nls}}
| Name = Defensin, beta 1
| HGNCid = 2766
| Symbol = DEFB1
| AltSymbols =; BD1; DEFB-1; DEFB101; HBD1; MGC51822
| OMIM = 602056
| ECnumber =
| Homologene = 88476
| MGIid =
| GeneAtlas_image1 = PBB_GE_DEFB1_210397_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0019735 |text = antimicrobial humoral response}} {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}} {{GNF_GO|id=GO:0045087 |text = innate immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1672
| Hs_Ensembl = ENSG00000164825
| Hs_RefseqProtein = NP_005209
| Hs_RefseqmRNA = NM_005218
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 6715511
| Hs_GenLoc_end = 6722939
| Hs_Uniprot = P60022
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Defensin, beta 1''', also known as '''DEFB1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DEFB1 defensin, beta 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1672| 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 = Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 1, an antimicrobial peptide implicated in the resistance of epithelial surfaces to microbial colonization. This gene maps in close proximity to defensin family member, defensin, alpha 1 and has been implicated in the pathogenesis of cystic fibrosis.<ref name="entrez">{{cite web | title = Entrez Gene: DEFB1 defensin, beta 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1672| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ganz T, Lehrer RI |title=Defensins. |journal=Pharmacol. Ther. |volume=66 |issue= 2 |pages= 191-205 |year= 1995 |pmid= 7667395 |doi= }}
*{{cite journal | author=Bensch KW, Raida M, Mägert HJ, ''et al.'' |title=hBD-1: a novel beta-defensin from human plasma. |journal=FEBS Lett. |volume=368 |issue= 2 |pages= 331-5 |year= 1995 |pmid= 7628632 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Goldman MJ, Anderson GM, Stolzenberg ED, ''et al.'' |title=Human beta-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis. |journal=Cell |volume=88 |issue= 4 |pages= 553-60 |year= 1997 |pmid= 9038346 |doi= }}
*{{cite journal | author=McCray PB, Bentley L |title=Human airway epithelia express a beta-defensin. |journal=Am. J. Respir. Cell Mol. Biol. |volume=16 |issue= 3 |pages= 343-9 |year= 1997 |pmid= 9070620 |doi= }}
*{{cite journal | author=Liu L, Zhao C, Heng HH, Ganz T |title=The human beta-defensin-1 and alpha-defensins are encoded by adjacent genes: two peptide families with differing disulfide topology share a common ancestry. |journal=Genomics |volume=43 |issue= 3 |pages= 316-20 |year= 1997 |pmid= 9268634 |doi= 10.1006/geno.1997.4801 }}
*{{cite journal | author=Valore EV, Park CH, Quayle AJ, ''et al.'' |title=Human beta-defensin-1: an antimicrobial peptide of urogenital tissues. |journal=J. Clin. Invest. |volume=101 |issue= 8 |pages= 1633-42 |year= 1998 |pmid= 9541493 |doi= }}
*{{cite journal | author=Schnapp D, Reid CJ, Harris A |title=Localization of expression of human beta defensin-1 in the pancreas and kidney. |journal=J. Pathol. |volume=186 |issue= 1 |pages= 99-103 |year= 1999 |pmid= 9875146 |doi= 10.1002/(SICI)1096-9896(199809)186:1<99::AID-PATH133>3.0.CO;2-# }}
*{{cite journal | author=Hiratsuka T, Nakazato M, Ashitani J, Matsukura S |title=[A study of human beta-defensin-1 and human beta-defensin-2 in airway mucosal defense] |journal=Kansenshogaku Zasshi |volume=73 |issue= 2 |pages= 156-62 |year= 1999 |pmid= 10213993 |doi= }}
*{{cite journal | author=Gropp R, Frye M, Wagner TO, Bargon J |title=Epithelial defensins impair adenoviral infection: implication for adenovirus-mediated gene therapy. |journal=Hum. Gene Ther. |volume=10 |issue= 6 |pages= 957-64 |year= 1999 |pmid= 10223729 |doi= 10.1089/10430349950018355 }}
*{{cite journal | author=Mathews M, Jia HP, Guthmiller JM, ''et al.'' |title=Production of beta-defensin antimicrobial peptides by the oral mucosa and salivary glands. |journal=Infect. Immun. |volume=67 |issue= 6 |pages= 2740-5 |year= 1999 |pmid= 10338476 |doi= }}
*{{cite journal | author=Bøe R, Silvola J, Yang J, ''et al.'' |title=Human beta-defensin-1 mRNA is transcribed in tympanic membrane and adjacent auditory canal epithelium. |journal=Infect. Immun. |volume=67 |issue= 9 |pages= 4843-6 |year= 1999 |pmid= 10456939 |doi= }}
*{{cite journal | author=Yang D, Chertov O, Bykovskaia SN, ''et al.'' |title=Beta-defensins: linking innate and adaptive immunity through dendritic and T cell CCR6. |journal=Science |volume=286 |issue= 5439 |pages= 525-8 |year= 1999 |pmid= 10521347 |doi= }}
*{{cite journal | author=Tunzi CR, Harper PA, Bar-Oz B, ''et al.'' |title=Beta-defensin expression in human mammary gland epithelia. |journal=Pediatr. Res. |volume=48 |issue= 1 |pages= 30-5 |year= 2000 |pmid= 10879797 |doi= }}
*{{cite journal | author=Sahasrabudhe KS, Kimball JR, Morton TH, ''et al.'' |title=Expression of the antimicrobial peptide, human beta-defensin 1, in duct cells of minor salivary glands and detection in saliva. |journal=J. Dent. Res. |volume=79 |issue= 9 |pages= 1669-74 |year= 2000 |pmid= 11023262 |doi= }}
*{{cite journal | author=Jia HP, Starner T, Ackermann M, ''et al.'' |title=Abundant human beta-defensin-1 expression in milk and mammary gland epithelium. |journal=J. Pediatr. |volume=138 |issue= 1 |pages= 109-12 |year= 2001 |pmid= 11148522 |doi= 10.1067/mpd.2001.109375 }}
*{{cite journal | author=Ali RS, Falconer A, Ikram M, ''et al.'' |title=Expression of the peptide antibiotics human beta defensin-1 and human beta defensin-2 in normal human skin. |journal=J. Invest. Dermatol. |volume=117 |issue= 1 |pages= 106-11 |year= 2001 |pmid= 11442756 |doi= 10.1046/j.0022-202x.2001.01401.x }}
*{{cite journal | author=Carothers DG, Graham SM, Jia HP, ''et al.'' |title=Production of beta-defensin antimicrobial peptides by maxillary sinus mucosa. |journal=American journal of rhinology |volume=15 |issue= 3 |pages= 175-9 |year= 2001 |pmid= 11453504 |doi= }}
*{{cite journal | author=Hoover DM, Chertov O, Lubkowski J |title=The structure of human beta-defensin-1: new insights into structural properties of beta-defensins. |journal=J. Biol. Chem. |volume=276 |issue= 42 |pages= 39021-6 |year= 2001 |pmid= 11486002 |doi= 10.1074/jbc.M103830200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DHX9... {November 17, 2007 11:30:48 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:31:36 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_DHX9_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1uil.
| PDB = {{PDB2|1uil}}
| Name = DEAH (Asp-Glu-Ala-His) box polypeptide 9
| HGNCid = 2750
| Symbol = DHX9
| AltSymbols =; DDX9; LKP; NDH II; NDHII; RHA
| OMIM = 603115
| ECnumber =
| Homologene = 1039
| MGIid = 108177
| GeneAtlas_image1 = PBB_GE_DHX9_202420_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_DHX9_212105_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_DHX9_212107_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003725 |text = double-stranded RNA binding}} {{GNF_GO|id=GO:0004003 |text = ATP-dependent DNA helicase activity}} {{GNF_GO|id=GO:0004004 |text = ATP-dependent RNA helicase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1660
| Hs_Ensembl = ENSG00000135829
| Hs_RefseqProtein = NP_001348
| Hs_RefseqmRNA = NM_001357
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 181075127
| Hs_GenLoc_end = 181123510
| Hs_Uniprot = Q08211
| Mm_EntrezGene = 13211
| Mm_Ensembl = ENSMUSG00000042699
| Mm_RefseqmRNA = NM_007842
| Mm_RefseqProtein = NP_031868
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 155218031
| Mm_GenLoc_end = 155249826
| Mm_Uniprot = Q05BR6
}}
}}
'''DEAH (Asp-Glu-Ala-His) box polypeptide 9''', also known as '''DHX9''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DHX9 DEAH (Asp-Glu-Ala-His) box polypeptide 9| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1660| 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 = DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein with RNA helicase activity. It may participate in melting of DNA:RNA hybrids, such as those that occur during transcription, and may play a role in X-linked gene expression. It contains 2 copies of a double-stranded RNA-binding domain, a DEXH core domain and an RGG box. The RNA-binding domains and RGG box influence and regulate RNA helicase activity.<ref name="entrez">{{cite web | title = Entrez Gene: DHX9 DEAH (Asp-Glu-Ala-His) box polypeptide 9| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1660| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lee CG, Hurwitz J |title=A new RNA helicase isolated from HeLa cells that catalytically translocates in the 3' to 5' direction. |journal=J. Biol. Chem. |volume=267 |issue= 7 |pages= 4398-407 |year= 1992 |pmid= 1537828 |doi= }}
*{{cite journal | author=Lee CG, Zamore PD, Green MR, Hurwitz J |title=RNA annealing activity is intrinsically associated with U2AF. |journal=J. Biol. Chem. |volume=268 |issue= 18 |pages= 13472-8 |year= 1993 |pmid= 7685763 |doi= }}
*{{cite journal | author=Lee CG, Hurwitz J |title=Human RNA helicase A is homologous to the maleless protein of Drosophila. |journal=J. Biol. Chem. |volume=268 |issue= 22 |pages= 16822-30 |year= 1993 |pmid= 8344961 |doi= }}
*{{cite journal | author=Abdelhaleem MM, Hameed S, Klassen D, Greenberg AH |title=Leukophysin: an RNA helicase A-related molecule identified in cytotoxic T cell granules and vesicles. |journal=J. Immunol. |volume=156 |issue= 6 |pages= 2026-35 |year= 1996 |pmid= 8690889 |doi= }}
*{{cite journal | author=Zhang S, Grosse F |title=Domain structure of human nuclear DNA helicase II (RNA helicase A). |journal=J. Biol. Chem. |volume=272 |issue= 17 |pages= 11487-94 |year= 1997 |pmid= 9111062 |doi= }}
*{{cite journal | author=Nakajima T, Uchida C, Anderson SF, ''et al.'' |title=RNA helicase A mediates association of CBP with RNA polymerase II. |journal=Cell |volume=90 |issue= 6 |pages= 1107-12 |year= 1997 |pmid= 9323138 |doi= }}
*{{cite journal | author=Loor G, Zhang SJ, Zhang P, ''et al.'' |title=Identification of DNA replication and cell cycle proteins that interact with PCNA. |journal=Nucleic Acids Res. |volume=25 |issue= 24 |pages= 5041-6 |year= 1998 |pmid= 9396813 |doi= }}
*{{cite journal | author=Lee CG, Eki T, Okumura K, ''et al.'' |title=Molecular analysis of the cDNA and genomic DNA encoding mouse RNA helicase A. |journal=Genomics |volume=47 |issue= 3 |pages= 365-71 |year= 1998 |pmid= 9480750 |doi= }}
*{{cite journal | author=Anderson SF, Schlegel BP, Nakajima T, ''et al.'' |title=BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A. |journal=Nat. Genet. |volume=19 |issue= 3 |pages= 254-6 |year= 1998 |pmid= 9662397 |doi= 10.1038/930 }}
*{{cite journal | author=Lee CG, da Costa Soares V, Newberger C, ''et al.'' |title=RNA helicase A is essential for normal gastrulation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 23 |pages= 13709-13 |year= 1998 |pmid= 9811865 |doi= }}
*{{cite journal | author=Li J, Tang H, Mullen TM, ''et al.'' |title=A role for RNA helicase A in post-transcriptional regulation of HIV type 1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 2 |pages= 709-14 |year= 1999 |pmid= 9892698 |doi= }}
*{{cite journal | author=Tang H, McDonald D, Middlesworth T, ''et al.'' |title=The carboxyl terminus of RNA helicase A contains a bidirectional nuclear transport domain. |journal=Mol. Cell. Biol. |volume=19 |issue= 5 |pages= 3540-50 |year= 1999 |pmid= 10207077 |doi= }}
*{{cite journal | author=Westberg C, Yang JP, Tang H, ''et al.'' |title=A novel shuttle protein binds to RNA helicase A and activates the retroviral constitutive transport element. |journal=J. Biol. Chem. |volume=275 |issue= 28 |pages= 21396-401 |year= 2000 |pmid= 10748171 |doi= 10.1074/jbc.M909887199 }}
*{{cite journal | author=Tang H, Wong-Staal F |title=Specific interaction between RNA helicase A and Tap, two cellular proteins that bind to the constitutive transport element of type D retrovirus. |journal=J. Biol. Chem. |volume=275 |issue= 42 |pages= 32694-700 |year= 2000 |pmid= 10924507 |doi= 10.1074/jbc.M003933200 }}
*{{cite journal | author=Lee CG, Eki T, Okumura K, ''et al.'' |title=The human RNA helicase A (DDX9) gene maps to the prostate cancer susceptibility locus at chromosome band 1q25 and its pseudogene (DDX9P) to 13q22, respectively. |journal=Somat. Cell Mol. Genet. |volume=25 |issue= 1 |pages= 33-9 |year= 2000 |pmid= 10925702 |doi= }}
*{{cite journal | author=Reddy TR, Tang H, Xu W, Wong-Staal F |title=Sam68, RNA helicase A and Tap cooperate in the post-transcriptional regulation of human immunodeficiency virus and type D retroviral mRNA. |journal=Oncogene |volume=19 |issue= 32 |pages= 3570-5 |year= 2000 |pmid= 10951562 |doi= 10.1038/sj.onc.1203676 }}
*{{cite journal | author=Pellizzoni L, Charroux B, Rappsilber J, ''et al.'' |title=A functional interaction between the survival motor neuron complex and RNA polymerase II. |journal=J. Cell Biol. |volume=152 |issue= 1 |pages= 75-85 |year= 2001 |pmid= 11149922 |doi= }}
*{{cite journal | author=Takasaki Y, Kogure T, Takeuchi K, ''et al.'' |title=Reactivity of anti-proliferating cell nuclear antigen (PCNA) murine monoclonal antibodies and human autoantibodies to the PCNA multiprotein complexes involved in cell proliferation. |journal=J. Immunol. |volume=166 |issue= 7 |pages= 4780-7 |year= 2001 |pmid= 11254741 |doi= }}
*{{cite journal | author=Yang JP, Tang H, Reddy TR, Wong-Staal F |title=Mapping the functional domains of HAP95, a protein that binds RNA helicase A and activates the constitutive transport element of type D retroviruses. |journal=J. Biol. Chem. |volume=276 |issue= 33 |pages= 30694-700 |year= 2001 |pmid= 11402034 |doi= 10.1074/jbc.M102809200 }}
*{{cite journal | author=Aratani S, Fujii R, Oishi T, ''et al.'' |title=Dual roles of RNA helicase A in CREB-dependent transcription. |journal=Mol. Cell. Biol. |volume=21 |issue= 14 |pages= 4460-9 |year= 2001 |pmid= 11416126 |doi= 10.1128/MCB.21.14.4460-4469.2001 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GABBR1... {November 17, 2007 11:32:16 AM PST}
- SEARCH REDIRECT: Control Box Found: GABBR1 {November 17, 2007 11:33:11 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:33:12 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:33:12 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:33:12 AM PST}
- UPDATED: Updated protein page: GABBR1 {November 17, 2007 11:33:18 AM PST}
- INFO: Beginning work on GNA13... {November 17, 2007 11:39:55 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:40:36 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_GNA13_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1zcb.
| PDB = {{PDB2|1zcb}}
| Name = Guanine nucleotide binding protein (G protein), alpha 13
| HGNCid = 4381
| Symbol = GNA13
| AltSymbols =; G13; MGC46138
| OMIM = 604406
| ECnumber =
| Homologene = 55976
| MGIid = 95768
| GeneAtlas_image1 = PBB_GE_GNA13_206917_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005057 |text = receptor signaling protein activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0001569 |text = patterning of blood vessels}} {{GNF_GO|id=GO:0001701 |text = in utero embryonic development}} {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007243 |text = protein kinase cascade}} {{GNF_GO|id=GO:0007266 |text = Rho protein signal transduction}} {{GNF_GO|id=GO:0008360 |text = regulation of cell shape}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0030168 |text = platelet activation}} {{GNF_GO|id=GO:0030334 |text = regulation of cell migration}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10672
| Hs_Ensembl = ENSG00000120063
| Hs_RefseqProtein = NP_006563
| Hs_RefseqmRNA = NM_006572
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 60437296
| Hs_GenLoc_end = 60483216
| Hs_Uniprot = Q14344
| Mm_EntrezGene = 14674
| Mm_Ensembl = ENSMUSG00000020611
| Mm_RefseqmRNA = NM_010303
| Mm_RefseqProtein = NP_034433
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 109178921
| Mm_GenLoc_end = 109212576
| Mm_Uniprot = Q3UE40
}}
}}
'''Guanine nucleotide binding protein (G protein), alpha 13''', also known as '''GNA13''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GNA13 guanine nucleotide binding protein (G protein), alpha 13| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10672| 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=Downes GB, Gautam N |title=The G protein subunit gene families. |journal=Genomics |volume=62 |issue= 3 |pages= 544-52 |year= 2000 |pmid= 10644457 |doi= 10.1006/geno.1999.5992 }}
*{{cite journal | author=Kabouridis PS, Waters ST, Escobar S, ''et al.'' |title=Expression of GTP-binding protein alpha subunits in human thymocytes. |journal=Mol. Cell. Biochem. |volume=144 |issue= 1 |pages= 45-51 |year= 1995 |pmid= 7791744 |doi= }}
*{{cite journal | author=Offermanns S, Laugwitz KL, Spicher K, Schultz G |title=G proteins of the G12 family are activated via thromboxane A2 and thrombin receptors in human platelets. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 2 |pages= 504-8 |year= 1994 |pmid= 8290554 |doi= }}
*{{cite journal | author=Laugwitz KL, Allgeier A, Offermanns S, ''et al.'' |title=The human thyrotropin receptor: a heptahelical receptor capable of stimulating members of all four G protein families. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 1 |pages= 116-20 |year= 1996 |pmid= 8552586 |doi= }}
*{{cite journal | author=Offermanns S, Hu YH, Simon MI |title=Galpha12 and galpha13 are phosphorylated during platelet activation. |journal=J. Biol. Chem. |volume=271 |issue= 42 |pages= 26044-8 |year= 1996 |pmid= 8824244 |doi= }}
*{{cite journal | author=Offermanns S, Mancino V, Revel JP, Simon MI |title=Vascular system defects and impaired cell chemokinesis as a result of Galpha13 deficiency. |journal=Science |volume=275 |issue= 5299 |pages= 533-6 |year= 1997 |pmid= 8999798 |doi= }}
*{{cite journal | author=Macrez-Leprêtre N, Kalkbrenner F, Morel JL, ''et al.'' |title=G protein heterotrimer Galpha13beta1gamma3 couples the angiotensin AT1A receptor to increases in cytoplasmic Ca2+ in rat portal vein myocytes. |journal=J. Biol. Chem. |volume=272 |issue= 15 |pages= 10095-102 |year= 1997 |pmid= 9092554 |doi= }}
*{{cite journal | author=Hart MJ, Jiang X, Kozasa T, ''et al.'' |title=Direct stimulation of the guanine nucleotide exchange activity of p115 RhoGEF by Galpha13. |journal=Science |volume=280 |issue= 5372 |pages= 2112-4 |year= 1998 |pmid= 9641916 |doi= }}
*{{cite journal | author=Fukuhara S, Murga C, Zohar M, ''et al.'' |title=A novel PDZ domain containing guanine nucleotide exchange factor links heterotrimeric G proteins to Rho. |journal=J. Biol. Chem. |volume=274 |issue= 9 |pages= 5868-79 |year= 1999 |pmid= 10026210 |doi= }}
*{{cite journal | author=Becker KP, Garnovskaya M, Gettys T, Halushka PV |title=Coupling of thromboxane A2 receptor isoforms to Galpha13: effects on ligand binding and signalling. |journal=Biochim. Biophys. Acta |volume=1450 |issue= 3 |pages= 288-96 |year= 1999 |pmid= 10395940 |doi= }}
*{{cite journal | author=Windh RT, Lee MJ, Hla T, ''et al.'' |title=Differential coupling of the sphingosine 1-phosphate receptors Edg-1, Edg-3, and H218/Edg-5 to the G(i), G(q), and G(12) families of heterotrimeric G proteins. |journal=J. Biol. Chem. |volume=274 |issue= 39 |pages= 27351-8 |year= 1999 |pmid= 10488065 |doi= }}
*{{cite journal | author=Brydon L, Roka F, Petit L, ''et al.'' |title=Dual signaling of human Mel1a melatonin receptors via G(i2), G(i3), and G(q/11) proteins. |journal=Mol. Endocrinol. |volume=13 |issue= 12 |pages= 2025-38 |year= 2000 |pmid= 10598579 |doi= }}
*{{cite journal | author=Bhattacharyya R, Wedegaertner PB |title=Galpha 13 requires palmitoylation for plasma membrane localization, Rho-dependent signaling, and promotion of p115-RhoGEF membrane binding. |journal=J. Biol. Chem. |volume=275 |issue= 20 |pages= 14992-9 |year= 2000 |pmid= 10747909 |doi= 10.1074/jbc.M000415200 }}
*{{cite journal | author=Vaiskunaite R, Adarichev V, Furthmayr H, ''et al.'' |title=Conformational activation of radixin by G13 protein alpha subunit. |journal=J. Biol. Chem. |volume=275 |issue= 34 |pages= 26206-12 |year= 2000 |pmid= 10816569 |doi= 10.1074/jbc.M001863200 }}
*{{cite journal | author=Shi CS, Sinnarajah S, Cho H, ''et al.'' |title=G13alpha-mediated PYK2 activation. PYK2 is a mediator of G13alpha -induced serum response element-dependent transcription. |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24470-6 |year= 2000 |pmid= 10821841 |doi= 10.1074/jbc.M908449199 }}
*{{cite journal | author=Ponimaskin E, Behn H, Adarichev V, ''et al.'' |title=Acylation of Galpha(13) is important for its interaction with thrombin receptor, transforming activity and actin stress fiber formation. |journal=FEBS Lett. |volume=478 |issue= 1-2 |pages= 173-7 |year= 2000 |pmid= 10922491 |doi= }}
*{{cite journal | author=Jin S, Exton JH |title=Activation of RhoA by association of Galpha(13) with Dbl. |journal=Biochem. Biophys. Res. Commun. |volume=277 |issue= 3 |pages= 718-21 |year= 2000 |pmid= 11062019 |doi= 10.1006/bbrc.2000.3744 }}
*{{cite journal | author=Fukuhara S, Chikumi H, Gutkind JS |title=Leukemia-associated Rho guanine nucleotide exchange factor (LARG) links heterotrimeric G proteins of the G(12) family to Rho. |journal=FEBS Lett. |volume=485 |issue= 2-3 |pages= 183-8 |year= 2000 |pmid= 11094164 |doi= }}
*{{cite journal | author=Meigs TE, Fields TA, McKee DD, Casey PJ |title=Interaction of Galpha 12 and Galpha 13 with the cytoplasmic domain of cadherin provides a mechanism for beta -catenin release. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 2 |pages= 519-24 |year= 2001 |pmid= 11136230 |doi= 10.1073/pnas.021350998 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GNB1... {November 17, 2007 11:33:18 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:33:42 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_GNB1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a0r.
| PDB = {{PDB2|1a0r}}, {{PDB2|1b9x}}, {{PDB2|1b9y}}, {{PDB2|1gg2}}, {{PDB2|1got}}, {{PDB2|1gp2}}, {{PDB2|1omw}}, {{PDB2|1tbg}}, {{PDB2|1xhm}}, {{PDB2|2bcj}}, {{PDB2|2trc}}
| Name = Guanine nucleotide binding protein (G protein), beta polypeptide 1
| HGNCid = 4396
| Symbol = GNB1
| AltSymbols =;
| OMIM = 139380
| ECnumber =
| Homologene = 55532
| MGIid = 95781
| GeneAtlas_image1 = PBB_GE_GNB1_200745_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_GNB1_200744_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_GNB1_200746_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}}
| Component = {{GNF_GO|id=GO:0005834 |text = heterotrimeric G-protein complex}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007200 |text = G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)}} {{GNF_GO|id=GO:0007213 |text = acetylcholine receptor signaling, muscarinic pathway}} {{GNF_GO|id=GO:0007265 |text = Ras protein signal transduction}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0050909 |text = sensory perception of taste}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2782
| Hs_Ensembl = ENSG00000078369
| Hs_RefseqProtein = NP_002065
| Hs_RefseqmRNA = NM_002074
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 1706589
| Hs_GenLoc_end = 1812355
| Hs_Uniprot = P62873
| Mm_EntrezGene = 14688
| Mm_Ensembl = ENSMUSG00000029064
| Mm_RefseqmRNA = NM_008142
| Mm_RefseqProtein = NP_032168
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 154335170
| Mm_GenLoc_end = 154401618
| Mm_Uniprot = Q3TQ70
}}
}}
'''Guanine nucleotide binding protein (G protein), beta polypeptide 1''', also known as '''GNB1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GNB1 guanine nucleotide binding protein (G protein), beta polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2782| 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 = Heterotrimeric guanine nucleotide-binding proteins (G proteins), which integrate signals between receptors and effector proteins, are composed of an alpha, a beta, and a gamma subunit. These subunits are encoded by families of related genes. This gene encodes a beta subunit. Beta subunits are important regulators of alpha subunits, as well as of certain signal transduction receptors and effectors. This gene uses alternative polyadenylation signals.<ref name="entrez">{{cite web | title = Entrez Gene: GNB1 guanine nucleotide binding protein (G protein), beta polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2782| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Downes GB, Gautam N |title=The G protein subunit gene families. |journal=Genomics |volume=62 |issue= 3 |pages= 544-52 |year= 2000 |pmid= 10644457 |doi= 10.1006/geno.1999.5992 }}
*{{cite journal | author=Levine MA, Modi WS, O'Brien SJ |title=Chromosomal localization of the genes encoding two forms of the G protein beta polypeptide, beta 1 and beta 3, in man. |journal=Genomics |volume=8 |issue= 2 |pages= 380-6 |year= 1991 |pmid= 1979057 |doi= }}
*{{cite journal | author=Codina J, Stengel D, Woo SL, Birnbaumer L |title=Beta-subunits of the human liver Gs/Gi signal-transducing proteins and those of bovine retinal rod cell transducin are identical. |journal=FEBS Lett. |volume=207 |issue= 2 |pages= 187-92 |year= 1986 |pmid= 3095147 |doi= }}
*{{cite journal | author=Buhl AM, Osawa S, Johnson GL |title=Mitogen-activated protein kinase activation requires two signal inputs from the human anaphylatoxin C5a receptor. |journal=J. Biol. Chem. |volume=270 |issue= 34 |pages= 19828-32 |year= 1995 |pmid= 7649993 |doi= }}
*{{cite journal | author=Ray K, Kunsch C, Bonner LM, Robishaw JD |title=Isolation of cDNA clones encoding eight different human G protein gamma subunits, including three novel forms designated the gamma 4, gamma 10, and gamma 11 subunits. |journal=J. Biol. Chem. |volume=270 |issue= 37 |pages= 21765-71 |year= 1995 |pmid= 7665596 |doi= }}
*{{cite journal | author=Kozasa T, Gilman AG |title=Purification of recombinant G proteins from Sf9 cells by hexahistidine tagging of associated subunits. Characterization of alpha 12 and inhibition of adenylyl cyclase by alpha z. |journal=J. Biol. Chem. |volume=270 |issue= 4 |pages= 1734-41 |year= 1995 |pmid= 7829508 |doi= }}
*{{cite journal | author=Tsukada S, Simon MI, Witte ON, Katz A |title=Binding of beta gamma subunits of heterotrimeric G proteins to the PH domain of Bruton tyrosine kinase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 23 |pages= 11256-60 |year= 1994 |pmid= 7972043 |doi= }}
*{{cite journal | author=Ueda N, Iñiguez-Lluhi JA, Lee E, ''et al.'' |title=G protein beta gamma subunits. Simplified purification and properties of novel isoforms. |journal=J. Biol. Chem. |volume=269 |issue= 6 |pages= 4388-95 |year= 1994 |pmid= 8308009 |doi= }}
*{{cite journal | author=Wall MA, Coleman DE, Lee E, ''et al.'' |title=The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2. |journal=Cell |volume=83 |issue= 6 |pages= 1047-58 |year= 1996 |pmid= 8521505 |doi= }}
*{{cite journal | author=Sondek J, Bohm A, Lambright DG, ''et al.'' |title=Crystal structure of a G-protein beta gamma dimer at 2.1A resolution. |journal=Nature |volume=379 |issue= 6563 |pages= 369-74 |year= 1996 |pmid= 8552196 |doi= 10.1038/379369a0 }}
*{{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=Mattingly RR, Macara IG |title=Phosphorylation-dependent activation of the Ras-GRF/CDC25Mm exchange factor by muscarinic receptors and G-protein beta gamma subunits. |journal=Nature |volume=382 |issue= 6588 |pages= 268-72 |year= 1996 |pmid= 8717044 |doi= 10.1038/382268a0 }}
*{{cite journal | author=De Waard M, Liu H, Walker D, ''et al.'' |title=Direct binding of G-protein betagamma complex to voltage-dependent calcium channels. |journal=Nature |volume=385 |issue= 6615 |pages= 446-50 |year= 1997 |pmid= 9009193 |doi= 10.1038/385446a0 }}
*{{cite journal | author=Huang CL, Jan YN, Jan LY |title=Binding of the G protein betagamma subunit to multiple regions of G protein-gated inward-rectifying K+ channels. |journal=FEBS Lett. |volume=405 |issue= 3 |pages= 291-8 |year= 1997 |pmid= 9108307 |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=Qin N, Platano D, Olcese R, ''et al.'' |title=Direct interaction of gbetagamma with a C-terminal gbetagamma-binding domain of the Ca2+ channel alpha1 subunit is responsible for channel inhibition by G protein-coupled receptors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 16 |pages= 8866-71 |year= 1997 |pmid= 9238069 |doi= }}
*{{cite journal | author=Nishida K, Kaziro Y, Satoh T |title=Association of the proto-oncogene product dbl with G protein betagamma subunits. |journal=FEBS Lett. |volume=459 |issue= 2 |pages= 186-90 |year= 1999 |pmid= 10518015 |doi= }}
*{{cite journal | author=Huang L, Shanker YG, Dubauskaite J, ''et al.'' |title=Ggamma13 colocalizes with gustducin in taste receptor cells and mediates IP3 responses to bitter denatonium. |journal=Nat. Neurosci. |volume=2 |issue= 12 |pages= 1055-62 |year= 2000 |pmid= 10570481 |doi= 10.1038/15981 }}
*{{cite journal | author=Carman CV, Barak LS, Chen C, ''et al.'' |title=Mutational analysis of Gbetagamma and phospholipid interaction with G protein-coupled receptor kinase 2. |journal=J. Biol. Chem. |volume=275 |issue= 14 |pages= 10443-52 |year= 2000 |pmid= 10744734 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GNRH1... {November 17, 2007 11:33:42 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:34:30 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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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 = Gonadotropin-releasing hormone 1 (luteinizing-releasing hormone)
| HGNCid = 4419
| Symbol = GNRH1
| AltSymbols =; GNRH; GRH; LHRH; LNRH
| OMIM = 152760
| ECnumber =
| Homologene = 641
| MGIid = 95789
| GeneAtlas_image1 = PBB_GE_GNRH1_207987_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005183 |text = luteinizing hormone-releasing factor activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2796
| Hs_Ensembl = ENSG00000147437
| Hs_RefseqProtein = NP_000816
| Hs_RefseqmRNA = NM_000825
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 25332697
| Hs_GenLoc_end = 25338087
| Hs_Uniprot = P01148
| Mm_EntrezGene = 14714
| Mm_Ensembl = ENSMUSG00000015812
| Mm_RefseqmRNA = NM_008145
| Mm_RefseqProtein = NP_032171
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 66699676
| Mm_GenLoc_end = 66702621
| Mm_Uniprot = Q14AC4
}}
}}
'''Gonadotropin-releasing hormone 1 (luteinizing-releasing hormone)''', also known as '''GNRH1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GNRH1 gonadotropin-releasing hormone 1 (luteinizing-releasing hormone)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2796| 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=Flanagan CA, Millar RP, Illing N |title=Advances in understanding gonadotrophin-releasing hormone receptor structure and ligand interactions. |journal=Rev. Reprod. |volume=2 |issue= 2 |pages= 113-20 |year= 1998 |pmid= 9414473 |doi= }}
*{{cite journal | author=Leung PC, Cheng CK, Zhu XM |title=Multi-factorial role of GnRH-I and GnRH-II in the human ovary. |journal=Mol. Cell. Endocrinol. |volume=202 |issue= 1-2 |pages= 145-53 |year= 2004 |pmid= 12770744 |doi= }}
*{{cite journal | author=Gründker C, Emons G |title=Role of gonadotropin-releasing hormone (GnRH) in ovarian cancer. |journal=Reprod. Biol. Endocrinol. |volume=1 |issue= |pages= 65 |year= 2004 |pmid= 14594454 |doi= 10.1186/1477-7827-1-65 }}
*{{cite journal | author=Limonta P, Moretti RM, Marelli MM, Motta M |title=The biology of gonadotropin hormone-releasing hormone: role in the control of tumor growth and progression in humans. |journal=Frontiers in neuroendocrinology |volume=24 |issue= 4 |pages= 279-95 |year= 2004 |pmid= 14726258 |doi= }}
*{{cite journal | author=Janáky T, Juhász A, Bajusz S, ''et al.'' |title=Analogues of luteinizing hormone-releasing hormone containing cytotoxic groups. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 3 |pages= 972-6 |year= 1992 |pmid= 1310542 |doi= }}
*{{cite journal | author=Healey SC, Martin NG, Chenevix-Trench G |title=NcoI RFLP of the human LHRH gene on chromosome 8p. |journal=Nucleic Acids Res. |volume=19 |issue= 21 |pages= 6059 |year= 1991 |pmid= 1682898 |doi= }}
*{{cite journal | author=Williamson P, Lang J, Boyd Y |title=The gonadotropin-releasing hormone (Gnrh) gene maps to mouse chromosome 14 and identifies a homologous region on human chromosome 8. |journal=Somat. Cell Mol. Genet. |volume=17 |issue= 6 |pages= 609-15 |year= 1992 |pmid= 1767338 |doi= }}
*{{cite journal | author=Hayflick JS, Adelman JP, Seeburg PH |title=The complete nucleotide sequence of the human gonadotropin-releasing hormone gene. |journal=Nucleic Acids Res. |volume=17 |issue= 15 |pages= 6403-4 |year= 1989 |pmid= 2671939 |doi= }}
*{{cite journal | author=Nikolics K, Mason AJ, Szönyi E, ''et al.'' |title=A prolactin-inhibiting factor within the precursor for human gonadotropin-releasing hormone. |journal=Nature |volume=316 |issue= 6028 |pages= 511-7 |year= 1985 |pmid= 2863757 |doi= }}
*{{cite journal | author=Adelman JP, Mason AJ, Hayflick JS, Seeburg PH |title=Isolation of the gene and hypothalamic cDNA for the common precursor of gonadotropin-releasing hormone and prolactin release-inhibiting factor in human and rat. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 1 |pages= 179-83 |year= 1986 |pmid= 2867548 |doi= }}
*{{cite journal | author=Yang-Feng TL, Seeburg PH, Francke U |title=Human luteinizing hormone-releasing hormone gene (LHRH) is located on short arm of chromosome 8 (region 8p11.2----p21). |journal=Somat. Cell Mol. Genet. |volume=12 |issue= 1 |pages= 95-100 |year= 1986 |pmid= 3511544 |doi= }}
*{{cite journal | author=Seeburg PH, Adelman JP |title=Characterization of cDNA for precursor of human luteinizing hormone releasing hormone. |journal=Nature |volume=311 |issue= 5987 |pages= 666-8 |year= 1984 |pmid= 6090951 |doi= }}
*{{cite journal | author=Tan L, Rousseau P |title=The chemical identity of the immunoreactive LHRH-like peptide biosynthesized in the human placenta. |journal=Biochem. Biophys. Res. Commun. |volume=109 |issue= 3 |pages= 1061-71 |year= 1983 |pmid= 6760865 |doi= }}
*{{cite journal | author=Dong KW, Yu KL, Roberts JL |title=Identification of a major up-stream transcription start site for the human progonadotropin-releasing hormone gene used in reproductive tissues and cell lines. |journal=Mol. Endocrinol. |volume=7 |issue= 12 |pages= 1654-66 |year= 1994 |pmid= 8145771 |doi= }}
*{{cite journal | author=Kakar SS, Jennes L |title=Expression of gonadotropin-releasing hormone and gonadotropin-releasing hormone receptor mRNAs in various non-reproductive human tissues. |journal=Cancer Lett. |volume=98 |issue= 1 |pages= 57-62 |year= 1996 |pmid= 8529206 |doi= }}
*{{cite journal | author=Nagy A, Schally AV, Armatis P, ''et al.'' |title=Cytotoxic analogs of luteinizing hormone-releasing hormone containing doxorubicin or 2-pyrrolinodoxorubicin, a derivative 500-1000 times more potent. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 14 |pages= 7269-73 |year= 1996 |pmid= 8692981 |doi= }}
*{{cite journal | author=Chegini N, Rong H, Dou Q, ''et al.'' |title=Gonadotropin-releasing hormone (GnRH) and GnRH receptor gene expression in human myometrium and leiomyomata and the direct action of GnRH analogs on myometrial smooth muscle cells and interaction with ovarian steroids in vitro. |journal=J. Clin. Endocrinol. Metab. |volume=81 |issue= 9 |pages= 3215-21 |year= 1996 |pmid= 8784072 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Dong KW, Yu KL, Chen ZG, ''et al.'' |title=Characterization of multiple promoters directing tissue-specific expression of the human gonadotropin-releasing hormone gene. |journal=Endocrinology |volume=138 |issue= 7 |pages= 2754-62 |year= 1997 |pmid= 9202214 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HIST4H4... {November 17, 2007 11:43:06 AM PST}
- SEARCH REDIRECT: Control Box Found: HIST4H4 {November 17, 2007 11:43:25 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:43:26 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:43:26 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:43:26 AM PST}
- UPDATED: Updated protein page: HIST4H4 {November 17, 2007 11:43:35 AM PST}
- INFO: Beginning work on HNRPA2B1... {November 17, 2007 11:34:30 AM PST}
- SEARCH REDIRECT: Control Box Found: HNRPA2B1 {November 17, 2007 11:35:15 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:35:17 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:35:17 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:35:17 AM PST}
- UPDATED: Updated protein page: HNRPA2B1 {November 17, 2007 11:35:26 AM PST}
- INFO: Beginning work on ICOS... {November 17, 2007 11:40:36 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:42:26 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 = Inducible T-cell co-stimulator
| HGNCid = 5351
| Symbol = ICOS
| AltSymbols =; AILIM; CD278; MGC39850
| OMIM = 604558
| ECnumber =
| Homologene = 8097
| MGIid = 1858745
| GeneAtlas_image1 = PBB_GE_ICOS_210439_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 29851
| Hs_Ensembl = ENSG00000163600
| Hs_RefseqProtein = NP_036224
| Hs_RefseqmRNA = NM_012092
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 204509716
| Hs_GenLoc_end = 204534541
| Hs_Uniprot = Q9Y6W8
| Mm_EntrezGene = 54167
| Mm_Ensembl = ENSMUSG00000026009
| Mm_RefseqmRNA = NM_017480
| Mm_RefseqProtein = NP_059508
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 60922460
| Mm_GenLoc_end = 60944866
| Mm_Uniprot = Q3V3X2
}}
}}
'''Inducible T-cell co-stimulator''', also known as '''ICOS''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ICOS inducible T-cell co-stimulator| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29851| 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 CD28 and CTLA-4 cell-surface receptor family. It forms homodimers and plays an important role in cell-cell signaling, immune responses, and regulation of cell proliferation.<ref name="entrez">{{cite web | title = Entrez Gene: ICOS inducible T-cell co-stimulator| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29851| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Flesch IE |title=Inducible costimulator (ICOS). |journal=J. Biol. Regul. Homeost. Agents |volume=16 |issue= 3 |pages= 214-6 |year= 2003 |pmid= 12456021 |doi= }}
*{{cite journal | author=Shilling RA, Bandukwala HS, Sperling AI |title=Regulation of T:B cell interactions by the inducible costimulator molecule: does ICOS "induce" disease? |journal=Clin. Immunol. |volume=121 |issue= 1 |pages= 13-8 |year= 2006 |pmid= 16790364 |doi= 10.1016/j.clim.2006.04.574 }}
*{{cite journal | author=Hutloff A, Dittrich AM, Beier KC, ''et al.'' |title=ICOS is an inducible T-cell co-stimulator structurally and functionally related to CD28. |journal=Nature |volume=397 |issue= 6716 |pages= 263-6 |year= 1999 |pmid= 9930702 |doi= 10.1038/16717 }}
*{{cite journal | author=Yoshinaga SK, Whoriskey JS, Khare SD, ''et al.'' |title=T-cell co-stimulation through B7RP-1 and ICOS. |journal=Nature |volume=402 |issue= 6763 |pages= 827-32 |year= 2000 |pmid= 10617205 |doi= 10.1038/45582 }}
*{{cite journal | author=Ling V, Wu PW, Finnerty HF, ''et al.'' |title=Cutting edge: identification of GL50, a novel B7-like protein that functionally binds to ICOS receptor. |journal=J. Immunol. |volume=164 |issue= 4 |pages= 1653-7 |year= 2000 |pmid= 10657606 |doi= }}
*{{cite journal | author=Aicher A, Hayden-Ledbetter M, Brady WA, ''et al.'' |title=Characterization of human inducible costimulator ligand expression and function. |journal=J. Immunol. |volume=164 |issue= 9 |pages= 4689-96 |year= 2000 |pmid= 10779774 |doi= }}
*{{cite journal | author=Machado RD, Pauciulo MW, Fretwell N, ''et al.'' |title=A physical and transcript map based upon refinement of the critical interval for PPH1, a gene for familial primary pulmonary hypertension. The International PPH Consortium. |journal=Genomics |volume=68 |issue= 2 |pages= 220-8 |year= 2001 |pmid= 10964520 |doi= 10.1006/geno.2000.6291 }}
*{{cite journal | author=Tezuka K, Tsuji T, Hirano D, ''et al.'' |title=Identification and characterization of rat AILIM/ICOS, a novel T-cell costimulatory molecule, related to the CD28/CTLA4 family. |journal=Biochem. Biophys. Res. Commun. |volume=276 |issue= 1 |pages= 335-45 |year= 2000 |pmid= 11006126 |doi= 10.1006/bbrc.2000.3466 }}
*{{cite journal | author=Wang S, Zhu G, Chapoval AI, ''et al.'' |title=Costimulation of T cells by B7-H2, a B7-like molecule that binds ICOS. |journal=Blood |volume=96 |issue= 8 |pages= 2808-13 |year= 2000 |pmid= 11023515 |doi= }}
*{{cite journal | author=Breitfeld D, Ohl L, Kremmer E, ''et al.'' |title=Follicular B helper T cells express CXC chemokine receptor 5, localize to B cell follicles, and support immunoglobulin production. |journal=J. Exp. Med. |volume=192 |issue= 11 |pages= 1545-52 |year= 2001 |pmid= 11104797 |doi= }}
*{{cite journal | author=Beier KC, Hutloff A, Dittrich AM, ''et al.'' |title=Induction, binding specificity and function of human ICOS. |journal=Eur. J. Immunol. |volume=30 |issue= 12 |pages= 3707-17 |year= 2001 |pmid= 11169414 |doi= }}
*{{cite journal | author=Ling V, Wu PW, Finnerty HF, ''et al.'' |title=Assembly and annotation of human chromosome 2q33 sequence containing the CD28, CTLA4, and ICOS gene cluster: analysis by computational, comparative, and microarray approaches. |journal=Genomics |volume=78 |issue= 3 |pages= 155-68 |year= 2002 |pmid= 11735222 |doi= 10.1006/geno.2001.6655 }}
*{{cite journal | author=Lee YH, Ji JD, Sohn J, Song GG |title=Polymorphsims of CTLA-4 exon 1 +49, CTLA-4 promoter -318 and Fas promoter -670 in spondyloarthropathies. |journal=Clin. Rheumatol. |volume=20 |issue= 6 |pages= 420-2 |year= 2002 |pmid= 11771526 |doi= }}
*{{cite journal | author=Haimila KE, Partanen JA, Holopainen PM |title=Genetic polymorphism of the human ICOS gene. |journal=Immunogenetics |volume=53 |issue= 12 |pages= 1028-32 |year= 2002 |pmid= 11904679 |doi= 10.1007/s00251-002-0431-2 }}
*{{cite journal | author=Wang S, Zhu G, Tamada K, ''et al.'' |title=Ligand binding sites of inducible costimulator and high avidity mutants with improved function. |journal=J. Exp. Med. |volume=195 |issue= 8 |pages= 1033-41 |year= 2002 |pmid= 11956294 |doi= }}
*{{cite journal | author=Riley JL, Mao M, Kobayashi S, ''et al.'' |title=Modulation of TCR-induced transcriptional profiles by ligation of CD28, ICOS, and CTLA-4 receptors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 18 |pages= 11790-5 |year= 2002 |pmid= 12195015 |doi= 10.1073/pnas.162359999 }}
*{{cite journal | author=Witsch EJ, Peiser M, Hutloff A, ''et al.'' |title=ICOS and CD28 reversely regulate IL-10 on re-activation of human effector T cells with mature dendritic cells. |journal=Eur. J. Immunol. |volume=32 |issue= 9 |pages= 2680-6 |year= 2002 |pmid= 12207353 |doi= 10.1002/1521-4141(200209)32:9<2680::AID-IMMU2680>3.0.CO;2-6 }}
*{{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=Grimbacher B, Hutloff A, Schlesier M, ''et al.'' |title=Homozygous loss of ICOS is associated with adult-onset common variable immunodeficiency. |journal=Nat. Immunol. |volume=4 |issue= 3 |pages= 261-8 |year= 2003 |pmid= 12577056 |doi= 10.1038/ni902 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IDE... {November 17, 2007 11:35:26 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:35:59 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_IDE_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2g47.
| PDB = {{PDB2|2g47}}, {{PDB2|2g48}}, {{PDB2|2g49}}, {{PDB2|2g54}}, {{PDB2|2g56}}
| Name = Insulin-degrading enzyme
| HGNCid = 5381
| Symbol = IDE
| AltSymbols =; FLJ35968; INSULYSIN
| OMIM = 146680
| ECnumber =
| Homologene = 3645
| MGIid = 96412
| GeneAtlas_image1 = PBB_GE_IDE_203327_at_tn.png
| GeneAtlas_image2 = PBB_GE_IDE_203328_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_IDE_217496_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004231 |text = insulysin activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005777 |text = peroxisome}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007548 |text = sex differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3416
| Hs_Ensembl = ENSG00000119912
| Hs_RefseqProtein = NP_004960
| Hs_RefseqmRNA = NM_004969
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 94201421
| Hs_GenLoc_end = 94323813
| Hs_Uniprot = P14735
| Mm_EntrezGene = 15925
| Mm_Ensembl = ENSMUSG00000056999
| Mm_RefseqmRNA = XM_974712
| Mm_RefseqProtein = XP_979806
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 37335574
| Mm_GenLoc_end = 37395757
| Mm_Uniprot = Q8CGB9
}}
}}
'''Insulin-degrading enzyme''', also known as '''IDE''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IDE insulin-degrading enzyme| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3416| 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 may belong to a protease family responsible for intercellular peptide signalling. Though its role in the cellular processing of insulin has not yet been defined, insulin-degrading enzyme is thought to be involved in the termination of the insulin response.<ref name="entrez">{{cite web | title = Entrez Gene: IDE insulin-degrading enzyme| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3416| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Whitsett JA, Lessard JL |title=Characteristics of the microvillus brush border of human placenta: insulin receptor localization in brush border membranes. |journal=Endocrinology |volume=103 |issue= 4 |pages= 1458-68 |year= 1979 |pmid= 758022 |doi= }}
*{{cite journal | author=Wroblewski VJ, Masnyk M, Khambatta SS, Becker GW |title=Mechanisms involved in degradation of human insulin by cytosolic fractions of human, monkey, and rat liver. |journal=Diabetes |volume=41 |issue= 4 |pages= 539-47 |year= 1992 |pmid= 1607078 |doi= }}
*{{cite journal | author=Ding L, Becker AB, Suzuki A, Roth RA |title=Comparison of the enzymatic and biochemical properties of human insulin-degrading enzyme and Escherichia coli protease III. |journal=J. Biol. Chem. |volume=267 |issue= 4 |pages= 2414-20 |year= 1992 |pmid= 1733942 |doi= }}
*{{cite journal | author=Espinosa R, Lemons RS, Perlman RK, ''et al.'' |title=Localization of the gene encoding insulin-degrading enzyme to human chromosome 10, bands q23----q25. |journal=Cytogenet. Cell Genet. |volume=57 |issue= 4 |pages= 184-6 |year= 1992 |pmid= 1743072 |doi= }}
*{{cite journal | author=Affholter JA, Hsieh CL, Francke U, Roth RA |title=Insulin-degrading enzyme: stable expression of the human complementary DNA, characterization of its protein product, and chromosomal mapping of the human and mouse genes. |journal=Mol. Endocrinol. |volume=4 |issue= 8 |pages= 1125-35 |year= 1991 |pmid= 2293021 |doi= }}
*{{cite journal | author=Affholter JA, Fried VA, Roth RA |title=Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III. |journal=Science |volume=242 |issue= 4884 |pages= 1415-8 |year= 1989 |pmid= 3059494 |doi= }}
*{{cite journal | author=Kirschner RJ, Goldberg AL |title=A high molecular weight metalloendoprotease from the cytosol of mammalian cells. |journal=J. Biol. Chem. |volume=258 |issue= 2 |pages= 967-76 |year= 1983 |pmid= 6401723 |doi= }}
*{{cite journal | author=Authier F, Bergeron JJ, Ou WJ, ''et al.'' |title=Degradation of the cleaved leader peptide of thiolase by a peroxisomal proteinase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 9 |pages= 3859-63 |year= 1995 |pmid= 7731996 |doi= }}
*{{cite journal | author=Kupfer SR, Wilson EM, French FS |title=Androgen and glucocorticoid receptors interact with insulin degrading enzyme. |journal=J. Biol. Chem. |volume=269 |issue= 32 |pages= 20622-8 |year= 1994 |pmid= 8051160 |doi= }}
*{{cite journal | author=Kuo WL, Gehm BD, Rosner MR, ''et al.'' |title=Inducible expression and cellular localization of insulin-degrading enzyme in a stably transfected cell line. |journal=J. Biol. Chem. |volume=269 |issue= 36 |pages= 22599-606 |year= 1994 |pmid= 8077210 |doi= }}
*{{cite journal | author=Baumeister H, Müller D, Rehbein M, Richter D |title=The rat insulin-degrading enzyme. Molecular cloning and characterization of tissue-specific transcripts. |journal=FEBS Lett. |volume=317 |issue= 3 |pages= 250-4 |year= 1993 |pmid= 8425612 |doi= }}
*{{cite journal | author=Seta KA, Roth RA |title=Overexpression of insulin degrading enzyme: cellular localization and effects on insulin signaling. |journal=Biochem. Biophys. Res. Commun. |volume=231 |issue= 1 |pages= 167-71 |year= 1997 |pmid= 9070242 |doi= 10.1006/bbrc.1997.6066 }}
*{{cite journal | author=Qiu WQ, Walsh DM, Ye Z, ''et al.'' |title=Insulin-degrading enzyme regulates extracellular levels of amyloid beta-protein by degradation. |journal=J. Biol. Chem. |volume=273 |issue= 49 |pages= 32730-8 |year= 1999 |pmid= 9830016 |doi= }}
*{{cite journal | author=Vekrellis K, Ye Z, Qiu WQ, ''et al.'' |title=Neurons regulate extracellular levels of amyloid beta-protein via proteolysis by insulin-degrading enzyme. |journal=J. Neurosci. |volume=20 |issue= 5 |pages= 1657-65 |year= 2000 |pmid= 10684867 |doi= }}
*{{cite journal | author=Authier F, Danielsen GM, Kouach M, ''et al.'' |title=Identification of insulin domains important for binding to and degradation by endosomal acidic insulinase. |journal=Endocrinology |volume=142 |issue= 1 |pages= 276-89 |year= 2001 |pmid= 11145591 |doi= }}
*{{cite journal | author=Edbauer D, Willem M, Lammich S, ''et al.'' |title=Insulin-degrading enzyme rapidly removes the beta-amyloid precursor protein intracellular domain (AICD). |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 13389-93 |year= 2002 |pmid= 11809755 |doi= 10.1074/jbc.M111571200 }}
*{{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=Cook DG, Leverenz JB, McMillan PJ, ''et al.'' |title=Reduced hippocampal insulin-degrading enzyme in late-onset Alzheimer's disease is associated with the apolipoprotein E-epsilon4 allele. |journal=Am. J. Pathol. |volume=162 |issue= 1 |pages= 313-9 |year= 2003 |pmid= 12507914 |doi= }}
*{{cite journal | author=Farris W, Mansourian S, Chang Y, ''et al.'' |title=Insulin-degrading enzyme regulates the levels of insulin, amyloid beta-protein, and the beta-amyloid precursor protein intracellular domain in vivo. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 7 |pages= 4162-7 |year= 2003 |pmid= 12634421 |doi= 10.1073/pnas.0230450100 }}
*{{cite journal | author=Groves CJ, Wiltshire S, Smedley D, ''et al.'' |title=Association and haplotype analysis of the insulin-degrading enzyme (IDE) gene, a strong positional and biological candidate for type 2 diabetes susceptibility. |journal=Diabetes |volume=52 |issue= 5 |pages= 1300-5 |year= 2003 |pmid= 12716770 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IL16... {November 17, 2007 11:35:59 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:36:38 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_IL16_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1i16.
| PDB = {{PDB2|1i16}}, {{PDB2|1x6d}}
| Name = Interleukin 16 (lymphocyte chemoattractant factor)
| HGNCid = 5980
| Symbol = IL16
| AltSymbols =; FLJ16806; FLJ42735; FLJ44234; HsT19289; IL-16; LCF; prIL-16
| OMIM = 603035
| ECnumber =
| Homologene = 18157
| MGIid = 1270855
| GeneAtlas_image1 = PBB_GE_IL16_209827_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_IL16_209828_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005622 |text = intracellular}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0030595 |text = leukocyte chemotaxis}} {{GNF_GO|id=GO:0050930 |text = induction of positive chemotaxis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3603
| Hs_Ensembl = ENSG00000172349
| Hs_RefseqProtein = NP_004504
| Hs_RefseqmRNA = NM_004513
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 79262148
| Hs_GenLoc_end = 79388491
| Hs_Uniprot = Q14005
| Mm_EntrezGene = 16170
| Mm_Ensembl = ENSMUSG00000001741
| Mm_RefseqmRNA = NM_010551
| Mm_RefseqProtein = NP_034681
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 83519249
| Mm_GenLoc_end = 83611708
| Mm_Uniprot = Q3UZ81
}}
}}
'''Interleukin 16 (lymphocyte chemoattractant factor)''', also known as '''IL16''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IL16 interleukin 16 (lymphocyte chemoattractant factor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3603| 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 pleiotropic cytokine that functions as a chemoattractant, a modulator of T cell activation, and an inhibitor of HIV replication. The signaling process of this cytokine is mediated by CD4. The product of this gene undergoes proteolytic processing, which is found to yield two functional proteins. The cytokine function is exclusively attributed to the secreted C-terminal peptide, while the N-terminal product may play a role in cell cycle control. Caspase 3 is reported to be involved in the proteolytic processing of this protein. Two alternatively spliced transcript variants encoding distinct isoforms have been reported.<ref name="entrez">{{cite web | title = Entrez Gene: IL16 interleukin 16 (lymphocyte chemoattractant factor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3603| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wilson KC, Center DM, Cruikshank WW |title=The effect of interleukin-16 and its precursor on T lymphocyte activation and growth. |journal=Growth Factors |volume=22 |issue= 2 |pages= 97-104 |year= 2005 |pmid= 15253385 |doi= }}
*{{cite journal | author=Copeland KF |title=Modulation of HIV-1 transcription by cytokines and chemokines. |journal=Mini reviews in medicinal chemistry |volume=5 |issue= 12 |pages= 1093-101 |year= 2006 |pmid= 16375755 |doi= }}
*{{cite journal | author=Rand TH, Cruikshank WW, Center DM, Weller PF |title=CD4-mediated stimulation of human eosinophils: lymphocyte chemoattractant factor and other CD4-binding ligands elicit eosinophil migration. |journal=J. Exp. Med. |volume=173 |issue= 6 |pages= 1521-8 |year= 1991 |pmid= 1851800 |doi= }}
*{{cite journal | author=Ryan TC, Cruikshank WW, Kornfeld H, ''et al.'' |title=The CD4-associated tyrosine kinase p56lck is required for lymphocyte chemoattractant factor-induced T lymphocyte migration. |journal=J. Biol. Chem. |volume=270 |issue= 29 |pages= 17081-6 |year= 1995 |pmid= 7615501 |doi= }}
*{{cite journal | author=Cruikshank WW, Center DM, Nisar N, ''et al.'' |title=Molecular and functional analysis of a lymphocyte chemoattractant factor: association of biologic function with CD4 expression. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 11 |pages= 5109-13 |year= 1994 |pmid= 7910967 |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=Parada NA, Cruikshank WW, Danis HL, ''et al.'' |title=IL-16- and other CD4 ligand-induced migration is dependent upon protein kinase C. |journal=Cell. Immunol. |volume=168 |issue= 1 |pages= 100-6 |year= 1996 |pmid= 8599832 |doi= 10.1006/cimm.1996.0054 }}
*{{cite journal | author=Bannert N, Baier M, Werner A, Kurth R |title=Interleukin-16 or not? |journal=Nature |volume=381 |issue= 6577 |pages= 30 |year= 1996 |pmid= 8609984 |doi= 10.1038/381030a0 }}
*{{cite journal | author=Maciaszek JW, Parada NA, Cruikshank WW, ''et al.'' |title=IL-16 represses HIV-1 promoter activity. |journal=J. Immunol. |volume=158 |issue= 1 |pages= 5-8 |year= 1997 |pmid= 8977168 |doi= }}
*{{cite journal | author=Baier M, Bannert N, Werner A, ''et al.'' |title=Molecular cloning, sequence, expression, and processing of the interleukin 16 precursor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 10 |pages= 5273-7 |year= 1997 |pmid= 9144227 |doi= }}
*{{cite journal | author=Laberge S, Ernst P, Ghaffar O, ''et al.'' |title=Increased expression of interleukin-16 in bronchial mucosa of subjects with atopic asthma. |journal=Am. J. Respir. Cell Mol. Biol. |volume=17 |issue= 2 |pages= 193-202 |year= 1997 |pmid= 9271307 |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=Zhang Y, Center DM, Wu DM, ''et al.'' |title=Processing and activation of pro-interleukin-16 by caspase-3. |journal=J. Biol. Chem. |volume=273 |issue= 2 |pages= 1144-9 |year= 1998 |pmid= 9422780 |doi= }}
*{{cite journal | author=Mühlhahn P, Zweckstetter M, Georgescu J, ''et al.'' |title=Structure of interleukin 16 resembles a PDZ domain with an occluded peptide binding site. |journal=Nat. Struct. Biol. |volume=5 |issue= 8 |pages= 682-6 |year= 1998 |pmid= 9699630 |doi= 10.1038/1376 }}
*{{cite journal | author=Chupp GL, Wright EA, Wu D, ''et al.'' |title=Tissue and T cell distribution of precursor and mature IL-16. |journal=J. Immunol. |volume=161 |issue= 6 |pages= 3114-9 |year= 1998 |pmid= 9743378 |doi= }}
*{{cite journal | author=Bannert N, Avots A, Baier M, ''et al.'' |title=GA-binding protein factors, in concert with the coactivator CREB binding protein/p300, control the induction of the interleukin 16 promoter in T lymphocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 4 |pages= 1541-6 |year= 1999 |pmid= 9990060 |doi= }}
*{{cite journal | author=Kim HS |title=Assignment of human interleukin 16 (IL16) to chromosome 15q26.3 by radiation hybrid mapping. |journal=Cytogenet. Cell Genet. |volume=84 |issue= 1-2 |pages= 93 |year= 1999 |pmid= 10343113 |doi= }}
*{{cite journal | author=Liu Y, Cruikshank WW, O'Loughlin T, ''et al.'' |title=Identification of a CD4 domain required for interleukin-16 binding and lymphocyte activation. |journal=J. Biol. Chem. |volume=274 |issue= 33 |pages= 23387-95 |year= 1999 |pmid= 10438516 |doi= }}
*{{cite journal | author=Kaser A, Dunzendorfer S, Offner FA, ''et al.'' |title=A role for IL-16 in the cross-talk between dendritic cells and T cells. |journal=J. Immunol. |volume=163 |issue= 6 |pages= 3232-8 |year= 1999 |pmid= 10477592 |doi= }}
*{{cite journal | author=Kurschner C, Yuzaki M |title=Neuronal interleukin-16 (NIL-16): a dual function PDZ domain protein. |journal=J. Neurosci. |volume=19 |issue= 18 |pages= 7770-80 |year= 1999 |pmid= 10479680 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on INHBB... {November 17, 2007 11:36:38 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:37:04 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 = Inhibin, beta B (activin AB beta polypeptide)
| HGNCid = 6067
| Symbol = INHBB
| AltSymbols =;
| OMIM = 147390
| ECnumber =
| Homologene = 1654
| MGIid = 96571
| GeneAtlas_image1 = PBB_GE_INHBB_205258_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005179 |text = hormone activity}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0046789 |text = host cell surface receptor binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0001541 |text = ovarian follicle development}} {{GNF_GO|id=GO:0006952 |text = defense response}} {{GNF_GO|id=GO:0009605 |text = response to external stimulus}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0040007 |text = growth}} {{GNF_GO|id=GO:0046881 |text = positive regulation of follicle-stimulating hormone secretion}} {{GNF_GO|id=GO:0046882 |text = negative regulation of follicle-stimulating hormone secretion}} {{GNF_GO|id=GO:0048178 |text = negative regulation of hepatocyte growth factor biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3625
| Hs_Ensembl = ENSG00000163083
| Hs_RefseqProtein = NP_002184
| Hs_RefseqmRNA = NM_002193
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 120819469
| Hs_GenLoc_end = 120825444
| Hs_Uniprot = P09529
| Mm_EntrezGene = 16324
| Mm_Ensembl = ENSMUSG00000037035
| Mm_RefseqmRNA = XM_984243
| Mm_RefseqProtein = XP_989337
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 121243011
| Mm_GenLoc_end = 121249794
| Mm_Uniprot = Q04999
}}
}}
'''Inhibin, beta B (activin AB beta polypeptide)''', also known as '''INHBB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: INHBB inhibin, beta B (activin AB beta polypeptide)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3625| 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 inhibin beta B subunit joins the alpha subunit to form a pituitary FSH secretion inhibitor. Inhibin has been shown to regulate gonadal stromal cell proliferation negatively and to have tumour-suppressor activity. In addition, serum levels of inhibin have been shown to reflect the size of granulosa-cell tumors and can therefore be used as a marker for primary as well as recurrent disease. Because expression in gonadal and various extragonadal tissues may vary severalfold in a tissue-specific fashion, it is proposed that inhibin may be both a growth/differentiation factor and a hormone. Furthermore, the beta B subunit forms a homodimer, activin B, and also joins with the beta A subunit to form a heterodimer, activin AB, both of which stimulate FSH secretion.<ref name="entrez">{{cite web | title = Entrez Gene: INHBB inhibin, beta B (activin AB beta polypeptide)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3625| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ying SY |title=Inhibins and activins: chemical properties and biological activity. |journal=Proc. Soc. Exp. Biol. Med. |volume=186 |issue= 3 |pages= 253-64 |year= 1988 |pmid= 3122219 |doi= }}
*{{cite journal | author=Munz B, Hübner G, Tretter Y, ''et al.'' |title=A novel role of activin in inflammation and repair. |journal=J. Endocrinol. |volume=161 |issue= 2 |pages= 187-93 |year= 1999 |pmid= 10320815 |doi= }}
*{{cite journal | author=Welt CK |title=The physiology and pathophysiology of inhibin, activin and follistatin in female reproduction. |journal=Curr. Opin. Obstet. Gynecol. |volume=14 |issue= 3 |pages= 317-23 |year= 2002 |pmid= 12032389 |doi= }}
*{{cite journal | author=Shav-Tal Y, Zipori D |title=The role of activin a in regulation of hemopoiesis. |journal=Stem Cells |volume=20 |issue= 6 |pages= 493-500 |year= 2003 |pmid= 12456957 |doi= }}
*{{cite journal | author=Lahlou N, Roger M |title=Inhibin B in pubertal development and pubertal disorders. |journal=Semin. Reprod. Med. |volume=22 |issue= 3 |pages= 165-75 |year= 2005 |pmid= 15319819 |doi= 10.1055/s-2004-831892 }}
*{{cite journal | author=Mathews LS, Vale WW |title=Expression cloning of an activin receptor, a predicted transmembrane serine kinase. |journal=Cell |volume=65 |issue= 6 |pages= 973-82 |year= 1991 |pmid= 1646080 |doi= }}
*{{cite journal | author=Schmelzer CH, Burton LE, Tamony CM, ''et al.'' |title=Purification and characterization of recombinant human activin B. |journal=Biochim. Biophys. Acta |volume=1039 |issue= 2 |pages= 135-41 |year= 1990 |pmid= 2364091 |doi= }}
*{{cite journal | author=Mason AJ, Berkemeier LM, Schmelzer CH, Schwall RH |title=Activin B: precursor sequences, genomic structure and in vitro activities. |journal=Mol. Endocrinol. |volume=3 |issue= 9 |pages= 1352-8 |year= 1990 |pmid= 2575216 |doi= }}
*{{cite journal | author=Feng ZM, Bardin CW, Chen CL |title=Characterization and regulation of testicular inhibin beta-subunit mRNA. |journal=Mol. Endocrinol. |volume=3 |issue= 6 |pages= 939-48 |year= 1989 |pmid= 2739657 |doi= }}
*{{cite journal | author=Barton DE, Yang-Feng TL, Mason AJ, ''et al.'' |title=Mapping of genes for inhibin subunits alpha, beta A, and beta B on human and mouse chromosomes and studies of jsd mice. |journal=Genomics |volume=5 |issue= 1 |pages= 91-9 |year= 1989 |pmid= 2767687 |doi= }}
*{{cite journal | author=Burger HG, Igarashi M |title=Inhibin: definition and nomenclature, including related substances. |journal=Endocrinology |volume=122 |issue= 4 |pages= 1701-2 |year= 1988 |pmid= 3345731 |doi= }}
*{{cite journal | author=Mason AJ, Niall HD, Seeburg PH |title=Structure of two human ovarian inhibins. |journal=Biochem. Biophys. Res. Commun. |volume=135 |issue= 3 |pages= 957-64 |year= 1986 |pmid= 3754442 |doi= }}
*{{cite journal | author=Martens JW, de Winter JP, Timmerman MA, ''et al.'' |title=Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells. |journal=Endocrinology |volume=138 |issue= 7 |pages= 2928-36 |year= 1997 |pmid= 9202237 |doi= }}
*{{cite journal | author=Mellor SL, Cranfield M, Ries R, ''et al.'' |title=Localization of activin beta(A)-, beta(B)-, and beta(C)-subunits in humanprostate and evidence for formation of new activin heterodimers of beta(C)-subunit. |journal=J. Clin. Endocrinol. Metab. |volume=85 |issue= 12 |pages= 4851-8 |year= 2001 |pmid= 11134153 |doi= }}
*{{cite journal | author=Chapman SC, Woodruff TK |title=Modulation of activin signal transduction by inhibin B and inhibin-binding protein (INhBP). |journal=Mol. Endocrinol. |volume=15 |issue= 4 |pages= 668-79 |year= 2001 |pmid= 11266516 |doi= }}
*{{cite journal | author=Salmenkivi K, Arola J, Voutilainen R, ''et al.'' |title=Inhibin/activin betaB-subunit expression in pheochromocytomas favors benign diagnosis. |journal=J. Clin. Endocrinol. Metab. |volume=86 |issue= 5 |pages= 2231-5 |year= 2001 |pmid= 11344232 |doi= }}
*{{cite journal | author=Bahathiq AO, Stewart RL, Wells M, ''et al.'' |title=Production of activins by the human endosalpinx. |journal=J. Clin. Endocrinol. Metab. |volume=87 |issue= 11 |pages= 5283-9 |year= 2002 |pmid= 12414903 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MVP... {November 17, 2007 11:38:37 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:39:11 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| 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_MVP_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1y7x.
| PDB = {{PDB2|1y7x}}
| Name = Major vault protein
| HGNCid = 7531
| Symbol = MVP
| AltSymbols =; LRP; VAULT1
| OMIM = 605088
| ECnumber =
| Homologene = 3752
| MGIid = 1925638
| GeneAtlas_image1 = PBB_GE_MVP_202180_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_MVP_gnf1h10986_at_tn.png
| GeneAtlas_image3 = PBB_GE_MVP_gnf1h10989_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0030529 |text = ribonucleoprotein complex}}
| Process = {{GNF_GO|id=GO:0042493 |text = response to drug}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 9961
| Hs_Ensembl = ENSG00000013364
| Hs_RefseqProtein = NP_005106
| Hs_RefseqmRNA = NM_005115
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 29739281
| Hs_GenLoc_end = 29766842
| Hs_Uniprot = Q14764
| Mm_EntrezGene = 78388
| Mm_Ensembl = ENSMUSG00000030681
| Mm_RefseqmRNA = NM_080638
| Mm_RefseqProtein = NP_542369
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 126778012
| Mm_GenLoc_end = 126805742
| Mm_Uniprot = Q3THX5
}}
}}
'''Major vault protein''', also known as '''MVP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MVP major vault protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9961| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes the major vault protein which is a lung resistance-related protein. Vaults are multi-subunit structures that may be involved in nucleo-cytoplasmic transport. This protein mediates drug resistance, perhaps via a transport process. It is widely distributed in normal tissues, and overexpressed in multidrug-resistant cancer cells. The protein overexpression is a potentially useful marker of clinical drug resistance. This gene produces two transcripts by using two alternative exon 2 sequences; however, the open reading frames are the same in both transcripts.<ref name="entrez">{{cite web | title = Entrez Gene: MVP major vault protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9961| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Izquierdo MA, Scheffer GL, Flens MJ, ''et al.'' |title=Major vault protein LRP-related multidrug resistance. |journal=Eur. J. Cancer |volume=32A |issue= 6 |pages= 979-84 |year= 1996 |pmid= 8763338 |doi= }}
*{{cite journal | author=Scheffer GL, Wijngaard PL, Flens MJ, ''et al.'' |title=The drug resistance-related protein LRP is the human major vault protein. |journal=Nat. Med. |volume=1 |issue= 6 |pages= 578-82 |year= 1995 |pmid= 7585126 |doi= }}
*{{cite journal | author=Slovak ML, Ho JP, Cole SP, ''et al.'' |title=The LRP gene encoding a major vault protein associated with drug resistance maps proximal to MRP on chromosome 16: evidence that chromosome breakage plays a key role in MRP or LRP gene amplification. |journal=Cancer Res. |volume=55 |issue= 19 |pages= 4214-9 |year= 1995 |pmid= 7671223 |doi= }}
*{{cite journal | author=Izquierdo MA, Scheffer GL, Flens MJ, ''et al.'' |title=Broad distribution of the multidrug resistance-related vault lung resistance protein in normal human tissues and tumors. |journal=Am. J. Pathol. |volume=148 |issue= 3 |pages= 877-87 |year= 1997 |pmid= 8774142 |doi= }}
*{{cite journal | author=Dingemans AM, van Ark-Otte J, van der Valk P, ''et al.'' |title=Expression of the human major vault protein LRP in human lung cancer samples and normal lung tissues. |journal=Ann. Oncol. |volume=7 |issue= 6 |pages= 625-30 |year= 1997 |pmid= 8879378 |doi= }}
*{{cite journal | author=Sugawara I, Akiyama S, Scheper RJ, Itoyama S |title=Lung resistance protein (LRP) expression in human normal tissues in comparison with that of MDR1 and MRP. |journal=Cancer Lett. |volume=112 |issue= 1 |pages= 23-31 |year= 1997 |pmid= 9029166 |doi= 10.1016/S0304-3835(96)04542-9 }}
*{{cite journal | author=Abbondanza C, Rossi V, Roscigno A, ''et al.'' |title=Interaction of vault particles with estrogen receptor in the MCF-7 breast cancer cell. |journal=J. Cell Biol. |volume=141 |issue= 6 |pages= 1301-10 |year= 1998 |pmid= 9628887 |doi= }}
*{{cite journal | author=Ikeda K, Oka M, Yamada Y, ''et al.'' |title=Adult T-cell leukemia cells over-express the multidrug-resistance-protein (MRP) and lung-resistance-protein (LRP) genes. |journal=Int. J. Cancer |volume=82 |issue= 4 |pages= 599-604 |year= 1999 |pmid= 10404077 |doi= }}
*{{cite journal | author=Rimsza LM, Campbell K, Dalton WS, ''et al.'' |title=The major vault protein (MVP), a new multidrug resistance associated protein, is frequently expressed in multiple myeloma. |journal=Leuk. Lymphoma |volume=34 |issue= 3-4 |pages= 315-24 |year= 1999 |pmid= 10439368 |doi= }}
*{{cite journal | author=Kickhoefer VA, Siva AC, Kedersha NL, ''et al.'' |title=The 193-kD vault protein, VPARP, is a novel poly(ADP-ribose) polymerase. |journal=J. Cell Biol. |volume=146 |issue= 5 |pages= 917-28 |year= 1999 |pmid= 10477748 |doi= }}
*{{cite journal | author=Kickhoefer VA, Stephen AG, Harrington L, ''et al.'' |title=Vaults and telomerase share a common subunit, TEP1. |journal=J. Biol. Chem. |volume=274 |issue= 46 |pages= 32712-7 |year= 2000 |pmid= 10551828 |doi= }}
*{{cite journal | author=Lange C, Walther W, Schwabe H, Stein U |title=Cloning and initial analysis of the human multidrug resistance-related MVP/LRP gene promoter. |journal=Biochem. Biophys. Res. Commun. |volume=278 |issue= 1 |pages= 125-33 |year= 2001 |pmid= 11071864 |doi= 10.1006/bbrc.2000.3782 }}
*{{cite journal | author=Holzmann K, Ambrosch I, Elbling L, ''et al.'' |title=A small upstream open reading frame causes inhibition of human major vault protein expression from a ubiquitous mRNA splice variant. |journal=FEBS Lett. |volume=494 |issue= 1-2 |pages= 99-104 |year= 2001 |pmid= 11297743 |doi= }}
*{{cite journal | author=van Zon A, Mossink MH, Schoester M, ''et al.'' |title=Structural domains of vault proteins: a role for the coiled coil domain in vault assembly. |journal=Biochem. Biophys. Res. Commun. |volume=291 |issue= 3 |pages= 535-41 |year= 2002 |pmid= 11855821 |doi= 10.1006/bbrc.2002.6472 }}
*{{cite journal | author=Sakaki Y, Terashi K, Yamaguchi A, ''et al.'' |title=Human T-cell lymphotropic virus type I Tax activates lung resistance-related protein expression in leukemic clones established from an adult T-cell leukemia patient. |journal=Exp. Hematol. |volume=30 |issue= 4 |pages= 340-5 |year= 2002 |pmid= 11937269 |doi= }}
*{{cite journal | author=Zhao Y, Yu L, Wang Q, ''et al.'' |title=[The relationship between expression of lung resistance-related protein gene or multidrug resistance-associated protein gene and prognosis in newly diagnosed acute leukemia] |journal=Zhonghua Nei Ke Za Zhi |volume=41 |issue= 3 |pages= 183-5 |year= 2002 |pmid= 11940320 |doi= }}
*{{cite journal | author=Scheffer GL, Pijnenborg AC, Smit EF, ''et al.'' |title=Multidrug resistance related molecules in human and murine lung. |journal=J. Clin. Pathol. |volume=55 |issue= 5 |pages= 332-9 |year= 2002 |pmid= 11986335 |doi= }}
*{{cite journal | author=van den Heuvel-Eibrink MM, Wiemer EA, Prins A, ''et al.'' |title=Increased expression of the breast cancer resistance protein (BCRP) in relapsed or refractory acute myeloid leukemia (AML). |journal=Leukemia |volume=16 |issue= 5 |pages= 833-9 |year= 2002 |pmid= 11986944 |doi= 10.1038/sj.leu.2402496 }}
*{{cite journal | author=Yu Z, Fotouhi-Ardakani N, Wu L, ''et al.'' |title=PTEN associates with the vault particles in HeLa cells. |journal=J. Biol. Chem. |volume=277 |issue= 43 |pages= 40247-52 |year= 2002 |pmid= 12177006 |doi= 10.1074/jbc.M207608200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NR0B2... {November 17, 2007 11:38:09 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:38:37 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
}}
<!-- 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 = Nuclear receptor subfamily 0, group B, member 2
| HGNCid = 7961
| Symbol = NR0B2
| AltSymbols =; SHP1; SHP
| OMIM = 604630
| ECnumber =
| Homologene = 8030
| MGIid = 1346344
| GeneAtlas_image1 = PBB_GE_NR0B2_206410_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003707 |text = steroid hormone receptor activity}} {{GNF_GO|id=GO:0003714 |text = transcription corepressor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0008203 |text = cholesterol metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8431
| Hs_Ensembl = ENSG00000131910
| Hs_RefseqProtein = NP_068804
| Hs_RefseqmRNA = NM_021969
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 27110566
| Hs_GenLoc_end = 27113047
| Hs_Uniprot = Q15466
| Mm_EntrezGene = 23957
| Mm_Ensembl = ENSMUSG00000037583
| Mm_RefseqmRNA = NM_011850
| Mm_RefseqProtein = NP_035980
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 132825456
| Mm_GenLoc_end = 132828611
| Mm_Uniprot = Q62227
}}
}}
'''Nuclear receptor subfamily 0, group B, member 2''', also known as '''NR0B2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NR0B2 nuclear receptor subfamily 0, group B, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8431| 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 an unusual orphan receptor that contains a putative ligand-binding domain but lacks a conventional DNA-binding domain. The gene product is a member of the nuclear hormone receptor family, a group of transcription factors regulated by small hydrophobic hormones, a subset of which do not have known ligands and are referred to as orphan nuclear receptors. The protein has been shown to interact with retinoid and thyroid hormone receptors, inhibiting their ligand-dependent transcriptional activation. In addition, interaction with estrogen receptors has been demonstrated, leading to inhibition of function. Studies suggest that the protein represses nuclear hormone receptor-mediated transactivation via two separate steps: competition with coactivators and the direct effects of its transcriptional repressor function.<ref name="entrez">{{cite web | title = Entrez Gene: NR0B2 nuclear receptor subfamily 0, group B, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8431| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Seol W, Choi HS, Moore DD |title=An orphan nuclear hormone receptor that lacks a DNA binding domain and heterodimerizes with other receptors. |journal=Science |volume=272 |issue= 5266 |pages= 1336-9 |year= 1996 |pmid= 8650544 |doi= }}
*{{cite journal | author=Lee HK, Lee YK, Park SH, ''et al.'' |title=Structure and expression of the orphan nuclear receptor SHP gene. |journal=J. Biol. Chem. |volume=273 |issue= 23 |pages= 14398-402 |year= 1998 |pmid= 9603951 |doi= }}
*{{cite journal | author=Seol W, Hanstein B, Brown M, Moore DD |title=Inhibition of estrogen receptor action by the orphan receptor SHP (short heterodimer partner). |journal=Mol. Endocrinol. |volume=12 |issue= 10 |pages= 1551-7 |year= 1998 |pmid= 9773978 |doi= }}
*{{cite journal | author=Lee YK, Dell H, Dowhan DH, ''et al.'' |title=The orphan nuclear receptor SHP inhibits hepatocyte nuclear factor 4 and retinoid X receptor transactivation: two mechanisms for repression. |journal=Mol. Cell. Biol. |volume=20 |issue= 1 |pages= 187-95 |year= 2000 |pmid= 10594021 |doi= }}
*{{cite journal | author=Johansson L, Båvner A, Thomsen JS, ''et al.'' |title=The orphan nuclear receptor SHP utilizes conserved LXXLL-related motifs for interactions with ligand-activated estrogen receptors. |journal=Mol. Cell. Biol. |volume=20 |issue= 4 |pages= 1124-33 |year= 2000 |pmid= 10648597 |doi= }}
*{{cite journal | author=Lu TT, Makishima M, Repa JJ, ''et al.'' |title=Molecular basis for feedback regulation of bile acid synthesis by nuclear receptors. |journal=Mol. Cell |volume=6 |issue= 3 |pages= 507-15 |year= 2000 |pmid= 11030331 |doi= }}
*{{cite journal | author=Nishigori H, Tomura H, Tonooka N, ''et al.'' |title=Mutations in the small heterodimer partner gene are associated with mild obesity in Japanese subjects. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 2 |pages= 575-80 |year= 2001 |pmid= 11136233 |doi= 10.1073/pnas.021544398 }}
*{{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=Nishizawa H, Yamagata K, Shimomura I, ''et al.'' |title=Small heterodimer partner, an orphan nuclear receptor, augments peroxisome proliferator-activated receptor gamma transactivation. |journal=J. Biol. Chem. |volume=277 |issue= 2 |pages= 1586-92 |year= 2002 |pmid= 11696534 |doi= 10.1074/jbc.M104301200 }}
*{{cite journal | author=Sanyal S, Kim JY, Kim HJ, ''et al.'' |title=Differential regulation of the orphan nuclear receptor small heterodimer partner (SHP) gene promoter by orphan nuclear receptor ERR isoforms. |journal=J. Biol. Chem. |volume=277 |issue= 3 |pages= 1739-48 |year= 2002 |pmid= 11705994 |doi= 10.1074/jbc.M106140200 }}
*{{cite journal | author=Gobinet J, Auzou G, Nicolas JC, ''et al.'' |title=Characterization of the interaction between androgen receptor and a new transcriptional inhibitor, SHP. |journal=Biochemistry |volume=40 |issue= 50 |pages= 15369-77 |year= 2002 |pmid= 11735420 |doi= }}
*{{cite journal | author=Klinge CM, Jernigan SC, Risinger KE |title=The agonist activity of tamoxifen is inhibited by the short heterodimer partner orphan nuclear receptor in human endometrial cancer cells. |journal=Endocrinology |volume=143 |issue= 3 |pages= 853-67 |year= 2002 |pmid= 11861507 |doi= }}
*{{cite journal | author=Ogata M, Awaji T, Iwasaki N, ''et al.'' |title=Nuclear translocation of SHP and visualization of interaction with HNF-4alpha in living cells. |journal=Biochem. Biophys. Res. Commun. |volume=292 |issue= 1 |pages= 8-12 |year= 2002 |pmid= 11890664 |doi= }}
*{{cite journal | author=Cao H, Hegele RA |title=Identification of polymorphisms in the human SHP1 gene. |journal=J. Hum. Genet. |volume=47 |issue= 8 |pages= 445-7 |year= 2002 |pmid= 12181644 |doi= 10.1007/s100380200062 }}
*{{cite journal | author=Brendel C, Schoonjans K, Botrugno OA, ''et al.'' |title=The small heterodimer partner interacts with the liver X receptor alpha and represses its transcriptional activity. |journal=Mol. Endocrinol. |volume=16 |issue= 9 |pages= 2065-76 |year= 2003 |pmid= 12198243 |doi= }}
*{{cite journal | author=Borgius LJ, Steffensen KR, Gustafsson JA, Treuter E |title=Glucocorticoid signaling is perturbed by the atypical orphan receptor and corepressor SHP. |journal=J. Biol. Chem. |volume=277 |issue= 51 |pages= 49761-6 |year= 2003 |pmid= 12324453 |doi= 10.1074/jbc.M205641200 }}
*{{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=Hung CC, Farooqi IS, Ong K, ''et al.'' |title=Contribution of variants in the small heterodimer partner gene to birthweight, adiposity, and insulin levels: mutational analysis and association studies in multiple populations. |journal=Diabetes |volume=52 |issue= 5 |pages= 1288-91 |year= 2003 |pmid= 12716767 |doi= }}
*{{cite journal | author=Lai K, Harnish DC, Evans MJ |title=Estrogen receptor alpha regulates expression of the orphan receptor small heterodimer partner. |journal=J. Biol. Chem. |volume=278 |issue= 38 |pages= 36418-29 |year= 2003 |pmid= 12842887 |doi= 10.1074/jbc.M303913200 }}
*{{cite journal | author=Kovacic A, Speed CJ, Simpson ER, Clyne CD |title=Inhibition of aromatase transcription via promoter II by short heterodimer partner in human preadipocytes. |journal=Mol. Endocrinol. |volume=18 |issue= 1 |pages= 252-9 |year= 2004 |pmid= 14593077 |doi= 10.1210/me.2003-0211 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SH3KBP1... {November 17, 2007 11:42:26 AM PST}
- SEARCH REDIRECT: Control Box Found: SH3KBP1 {November 17, 2007 11:42:58 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:43:00 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:43:00 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:43:00 AM PST}
- UPDATED: Updated protein page: SH3KBP1 {November 17, 2007 11:43:06 AM PST}
- INFO: Beginning work on WEE1... {November 17, 2007 11:37:04 AM PST}
- SEARCH REDIRECT: Control Box Found: WEE1 {November 17, 2007 11:37:30 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:37:31 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:37:31 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:37:31 AM PST}
- UPDATED: Updated protein page: WEE1 {November 17, 2007 11:37:39 AM PST}
- INFO: Beginning work on XPA... {November 17, 2007 11:37:39 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:38:09 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_XPA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1d4u.
| PDB = {{PDB2|1d4u}}, {{PDB2|1xpa}}
| Name = Xeroderma pigmentosum, complementation group A
| HGNCid = 12814
| Symbol = XPA
| AltSymbols =; XP1; XPAC
| OMIM = 278700
| ECnumber =
| Homologene = 37298
| MGIid = 99135
| GeneAtlas_image1 = PBB_GE_XPA_205672_at_tn.png
| Function = {{GNF_GO|id=GO:0003684 |text = damaged DNA 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}}
| Process = {{GNF_GO|id=GO:0006289 |text = nucleotide-excision repair}} {{GNF_GO|id=GO:0006979 |text = response to oxidative stress}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7507
| Hs_Ensembl = ENSG00000136936
| Hs_RefseqProtein = NP_000371
| Hs_RefseqmRNA = NM_000380
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 99477012
| Hs_GenLoc_end = 99499460
| Hs_Uniprot = P23025
| Mm_EntrezGene = 22590
| Mm_Ensembl = ENSMUSG00000028329
| Mm_RefseqmRNA = NM_011728
| Mm_RefseqProtein = NP_035858
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 46176448
| Mm_GenLoc_end = 46217411
| Mm_Uniprot = Q8R4W5
}}
}}
'''Xeroderma pigmentosum, complementation group A''', also known as '''XPA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: XPA xeroderma pigmentosum, complementation group A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7507| 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=Cleaver JE, Thompson LH, Richardson AS, States JC |title=A summary of mutations in the UV-sensitive disorders: xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy. |journal=Hum. Mutat. |volume=14 |issue= 1 |pages= 9-22 |year= 1999 |pmid= 10447254 |doi= 10.1002/(SICI)1098-1004(1999)14:1<9::AID-HUMU2>3.0.CO;2-6 }}
*{{cite journal | author=Morikawa K, Shirakawa M |title=Three-dimensional structural views of damaged-DNA recognition: T4 endonuclease V, E. coli Vsr protein, and human nucleotide excision repair factor XPA. |journal=Mutat. Res. |volume=460 |issue= 3-4 |pages= 257-75 |year= 2000 |pmid= 10946233 |doi= }}
*{{cite journal | author=Satokata I, Tanaka K, Okada Y |title=Molecular basis of group A xeroderma pigmentosum: a missense mutation and two deletions located in a zinc finger consensus sequence of the XPAC gene. |journal=Hum. Genet. |volume=88 |issue= 6 |pages= 603-7 |year= 1992 |pmid= 1339397 |doi= }}
*{{cite journal | author=Satokata I, Tanaka K, Yuba S, Okada Y |title=Identification of splicing mutations of the last nucleotides of exons, a nonsense mutation, and a missense mutation of the XPAC gene as causes of group A xeroderma pigmentosum. |journal=Mutat. Res. |volume=273 |issue= 2 |pages= 203-12 |year= 1992 |pmid= 1372103 |doi= }}
*{{cite journal | author=Miyamoto I, Miura N, Niwa H, ''et al.'' |title=Mutational analysis of the structure and function of the xeroderma pigmentosum group A complementing protein. Identification of essential domains for nuclear localization and DNA excision repair. |journal=J. Biol. Chem. |volume=267 |issue= 17 |pages= 12182-7 |year= 1992 |pmid= 1601884 |doi= }}
*{{cite journal | author=Satokata I, Tanaka K, Miura N, ''et al.'' |title=Characterization of a splicing mutation in group A xeroderma pigmentosum. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 24 |pages= 9908-12 |year= 1991 |pmid= 1702221 |doi= }}
*{{cite journal | author=Miura N, Miyamoto I, Asahina H, ''et al.'' |title=Identification and characterization of xpac protein, the gene product of the human XPAC (xeroderma pigmentosum group A complementing) gene. |journal=J. Biol. Chem. |volume=266 |issue= 29 |pages= 19786-9 |year= 1991 |pmid= 1918083 |doi= }}
*{{cite journal | author=Tanaka K, Miura N, Satokata I, ''et al.'' |title=Analysis of a human DNA excision repair gene involved in group A xeroderma pigmentosum and containing a zinc-finger domain. |journal=Nature |volume=348 |issue= 6296 |pages= 73-6 |year= 1990 |pmid= 2234061 |doi= 10.1038/348073a0 }}
*{{cite journal | author=Li L, Lu X, Peterson CA, Legerski RJ |title=An interaction between the DNA repair factor XPA and replication protein A appears essential for nucleotide excision repair. |journal=Mol. Cell. Biol. |volume=15 |issue= 10 |pages= 5396-402 |year= 1995 |pmid= 7565690 |doi= }}
*{{cite journal | author=Nagai A, Saijo M, Kuraoka I, ''et al.'' |title=Enhancement of damage-specific DNA binding of XPA by interaction with the ERCC1 DNA repair protein. |journal=Biochem. Biophys. Res. Commun. |volume=211 |issue= 3 |pages= 960-6 |year= 1995 |pmid= 7598728 |doi= }}
*{{cite journal | author=Farndon PA, Morris DJ, Hardy C, ''et al.'' |title=Analysis of 133 meioses places the genes for nevoid basal cell carcinoma (Gorlin) syndrome and Fanconi anemia group C in a 2.6-cM interval and contributes to the fine map of 9q22.3. |journal=Genomics |volume=23 |issue= 2 |pages= 486-9 |year= 1995 |pmid= 7835901 |doi= 10.1006/geno.1994.1528 }}
*{{cite journal | author=Park CH, Mu D, Reardon JT, Sancar A |title=The general transcription-repair factor TFIIH is recruited to the excision repair complex by the XPA protein independent of the TFIIE transcription factor. |journal=J. Biol. Chem. |volume=270 |issue= 9 |pages= 4896-902 |year= 1995 |pmid= 7876263 |doi= }}
*{{cite journal | author=Li L, Elledge SJ, Peterson CA, ''et al.'' |title=Specific association between the human DNA repair proteins XPA and ERCC1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 11 |pages= 5012-6 |year= 1994 |pmid= 8197174 |doi= }}
*{{cite journal | author=Satokata I, Iwai K, Matsuda T, ''et al.'' |title=Genomic characterization of the human DNA excision repair-controlling gene XPAC. |journal=Gene |volume=136 |issue= 1-2 |pages= 345-8 |year= 1994 |pmid= 8294029 |doi= }}
*{{cite journal | author=Tanaka K |title=The Japan Society of Human Genetics Award Lecture. Molecular analysis of xeroderma pigmentosum group A gene. |journal=Jpn. J. Hum. Genet. |volume=38 |issue= 1 |pages= 1-14 |year= 1993 |pmid= 8504220 |doi= }}
*{{cite journal | author=Topping RS, Myrand SP, Williams BL, ''et al.'' |title=Characterization of the human XPA promoter. |journal=Gene |volume=166 |issue= 2 |pages= 341-2 |year= 1996 |pmid= 8543191 |doi= }}
*{{cite journal | author=Lench NJ, Telford EA, Andersen SE, ''et al.'' |title=An EST and STS-based YAC contig map of human chromosome 9q22.3. |journal=Genomics |volume=38 |issue= 2 |pages= 199-205 |year= 1997 |pmid= 8954802 |doi= 10.1006/geno.1996.0616 }}
*{{cite journal | author=Selby CP, Sancar A |title=Human transcription-repair coupling factor CSB/ERCC6 is a DNA-stimulated ATPase but is not a helicase and does not disrupt the ternary transcription complex of stalled RNA polymerase II. |journal=J. Biol. Chem. |volume=272 |issue= 3 |pages= 1885-90 |year= 1997 |pmid= 8999876 |doi= }}
*{{cite journal | author=Hayashi T, Takao M, Tanaka K, Yasui A |title=ERCC1 mutations in UV-sensitive Chinese hamster ovary (CHO) cell lines. |journal=Mutat. Res. |volume=407 |issue= 3 |pages= 269-76 |year= 1998 |pmid= 9653453 |doi= }}
*{{cite journal | author=States JC, McDuffie ER, Myrand SP, ''et al.'' |title=Distribution of mutations in the human xeroderma pigmentosum group A gene and their relationships to the functional regions of the DNA damage recognition protein. |journal=Hum. Mutat. |volume=12 |issue= 2 |pages= 103-13 |year= 1998 |pmid= 9671271 |doi= 10.1002/(SICI)1098-1004(1998)12:2<103::AID-HUMU5>3.0.CO;2-6 }}
}}
{{refend}}
{{protein-stub}}
end log.
