Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 00:06, 17 November 2007 (UTC)
[edit]Proteins without matches (10)
[edit]Proteins with a High Potential Match (9)
[edit]Redirected Proteins (6)
[edit]Manual Inspection (Page not found) (19)
[edit]
Protein Status Grid - Date: 00:06, 17 November 2007 (UTC)
[edit]Vebose Log - Date: 00:06, 17 November 2007 (UTC)
[edit]- INFO: Beginning work on ADAR... {November 16, 2007 3:43:00 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 3:43:51 PM PST}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ADAR_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1qbj.
| PDB = {{PDB2|1qbj}}, {{PDB2|1qgp}}, {{PDB2|1xmk}}, {{PDB2|2acj}}, {{PDB2|2gxb}}
| Name = Adenosine deaminase, RNA-specific
| HGNCid = 225
| Symbol = ADAR
| AltSymbols =; ADAR1; DRADA; DSH; DSRAD; G1P1; IFI-4; IFI4; K88dsRBP; p136
| OMIM = 601059
| ECnumber =
| Homologene = 9281
| MGIid = 1889575
| GeneAtlas_image1 = PBB_GE_ADAR_201786_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003725 |text = double-stranded RNA binding}} {{GNF_GO|id=GO:0003726 |text = double-stranded RNA adenosine deaminase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006397 |text = mRNA processing}} {{GNF_GO|id=GO:0016553 |text = base conversion or substitution editing}} {{GNF_GO|id=GO:0019735 |text = antimicrobial humoral response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 103
| Hs_Ensembl = ENSG00000160710
| Hs_RefseqProtein = NP_001020278
| Hs_RefseqmRNA = NM_001025107
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 152821161
| Hs_GenLoc_end = 152867098
| Hs_Uniprot = P55265
| Mm_EntrezGene = 56417
| Mm_Ensembl = ENSMUSG00000027951
| Mm_RefseqmRNA = NM_001038587
| Mm_RefseqProtein = NP_001033676
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 89800987
| Mm_GenLoc_end = 89839372
| Mm_Uniprot = Q5J3Q8
}}
}}
'''Adenosine deaminase, RNA-specific''', also known as '''ADAR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ADAR adenosine deaminase, RNA-specific| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=103| 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 enzyme responsible for RNA editing by site-specific deamination of adenosines. This enzyme destabilizes double stranded RNA through conversion of adenosine to inosine. Mutations in this gene have been associated with dyschromatosis symmetrica hereditaria. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.<ref name="entrez">{{cite web | title = Entrez Gene: ADAR adenosine deaminase, RNA-specific| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=103| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Valenzuela A, Blanco J, Callebaut C, ''et al.'' |title=HIV-1 envelope gp120 and viral particles block adenosine deaminase binding to human CD26. |journal=Adv. Exp. Med. Biol. |volume=421 |issue= |pages= 185-92 |year= 1997 |pmid= 9330696 |doi= }}
*{{cite journal | author=Wathelet MG, Szpirer J, Nols CB, ''et al.'' |title=Cloning and chromosomal location of human genes inducible by type I interferon. |journal=Somat. Cell Mol. Genet. |volume=14 |issue= 5 |pages= 415-26 |year= 1988 |pmid= 3175763 |doi= }}
*{{cite journal | author=Wang Y, Zeng Y, Murray JM, Nishikura K |title=Genomic organization and chromosomal location of the human dsRNA adenosine deaminase gene: the enzyme for glutamate-activated ion channel RNA editing. |journal=J. Mol. Biol. |volume=254 |issue= 2 |pages= 184-95 |year= 1996 |pmid= 7490742 |doi= 10.1006/jmbi.1995.0610 }}
*{{cite journal | author=Patterson JB, Samuel CE |title=Expression and regulation by interferon of a double-stranded-RNA-specific adenosine deaminase from human cells: evidence for two forms of the deaminase. |journal=Mol. Cell. Biol. |volume=15 |issue= 10 |pages= 5376-88 |year= 1995 |pmid= 7565688 |doi= }}
*{{cite journal | author=Patterson JB, Thomis DC, Hans SL, Samuel CE |title=Mechanism of interferon action: double-stranded RNA-specific adenosine deaminase from human cells is inducible by alpha and gamma interferons. |journal=Virology |volume=210 |issue= 2 |pages= 508-11 |year= 1995 |pmid= 7618288 |doi= 10.1006/viro.1995.1370 }}
*{{cite journal | author=O'Connell MA, Krause S, Higuchi M, ''et al.'' |title=Cloning of cDNAs encoding mammalian double-stranded RNA-specific adenosine deaminase. |journal=Mol. Cell. Biol. |volume=15 |issue= 3 |pages= 1389-97 |year= 1995 |pmid= 7862132 |doi= }}
*{{cite journal | author=Kim U, Wang Y, Sanford T, ''et al.'' |title=Molecular cloning of cDNA for double-stranded RNA adenosine deaminase, a candidate enzyme for nuclear RNA editing. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 24 |pages= 11457-61 |year= 1994 |pmid= 7972084 |doi= }}
*{{cite journal | author=Weier HU, George CX, Greulich KM, Samuel CE |title=The interferon-inducible, double-stranded RNA-specific adenosine deaminase gene (DSRAD) maps to human chromosome 1q21.1-21.2. |journal=Genomics |volume=30 |issue= 2 |pages= 372-5 |year= 1996 |pmid= 8586444 |doi= 10.1006/geno.1995.0034 }}
*{{cite journal | author=Liu Y, George CX, Patterson JB, Samuel CE |title=Functionally distinct double-stranded RNA-binding domains associated with alternative splice site variants of the interferon-inducible double-stranded RNA-specific adenosine deaminase. |journal=J. Biol. Chem. |volume=272 |issue= 7 |pages= 4419-28 |year= 1997 |pmid= 9020165 |doi= }}
*{{cite journal | author=Valenzuela A, Blanco J, Callebaut C, ''et al.'' |title=Adenosine deaminase binding to human CD26 is inhibited by HIV-1 envelope glycoprotein gp120 and viral particles. |journal=J. Immunol. |volume=158 |issue= 8 |pages= 3721-9 |year= 1997 |pmid= 9103436 |doi= }}
*{{cite journal | author=Herbert A, Alfken J, Kim YG, ''et al.'' |title=A Z-DNA binding domain present in the human editing enzyme, double-stranded RNA adenosine deaminase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 16 |pages= 8421-6 |year= 1997 |pmid= 9237992 |doi= }}
*{{cite journal | author=Liu Y, Herbert A, Rich A, Samuel CE |title=Double-stranded RNA-specific adenosine deaminase: nucleic acid binding properties. |journal=Methods |volume=15 |issue= 3 |pages= 199-205 |year= 1998 |pmid= 9735305 |doi= 10.1006/meth.1998.0624 }}
*{{cite journal | author=George CX, Samuel CE |title=Human RNA-specific adenosine deaminase ADAR1 transcripts possess alternative exon 1 structures that initiate from different promoters, one constitutively active and the other interferon inducible. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 8 |pages= 4621-6 |year= 1999 |pmid= 10200312 |doi= }}
*{{cite journal | author=Schwartz T, Rould MA, Lowenhaupt K, ''et al.'' |title=Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA. |journal=Science |volume=284 |issue= 5421 |pages= 1841-5 |year= 1999 |pmid= 10364558 |doi= }}
*{{cite journal | author=Schade M, Turner CJ, Kühne R, ''et al.'' |title=The solution structure of the Zalpha domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 22 |pages= 12465-70 |year= 1999 |pmid= 10535945 |doi= }}
*{{cite journal | author=Blanco J, Valenzuela A, Herrera C, ''et al.'' |title=The HIV-1 gp120 inhibits the binding of adenosine deaminase to CD26 by a mechanism modulated by CD4 and CXCR4 expression. |journal=FEBS Lett. |volume=477 |issue= 1-2 |pages= 123-8 |year= 2000 |pmid= 10899322 |doi= }}
*{{cite journal | author=Herrera C, Morimoto C, Blanco J, ''et al.'' |title=Comodulation of CXCR4 and CD26 in human lymphocytes. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 19532-9 |year= 2001 |pmid= 11278278 |doi= 10.1074/jbc.M004586200 }}
*{{cite journal | author=Wong SK, Sato S, Lazinski DW |title=Substrate recognition by ADAR1 and ADAR2. |journal=RNA |volume=7 |issue= 6 |pages= 846-58 |year= 2001 |pmid= 11421361 |doi= }}
*{{cite journal | author=Eckmann CR, Neunteufl A, Pfaffstetter L, Jantsch MF |title=The human but not the Xenopus RNA-editing enzyme ADAR1 has an atypical nuclear localization signal and displays the characteristics of a shuttling protein. |journal=Mol. Biol. Cell |volume=12 |issue= 7 |pages= 1911-24 |year= 2001 |pmid= 11451992 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ADD1... {November 16, 2007 3:43:51 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 3:44:21 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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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 = Adducin 1 (alpha)
| HGNCid = 243
| Symbol = ADD1
| AltSymbols =; ADDA; MGC3339; MGC44427
| OMIM = 102680
| ECnumber =
| Homologene = 22758
| MGIid = 87918
| GeneAtlas_image1 = PBB_GE_ADD1_208030_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ADD1_214726_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_ADD1_214736_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 118
| Hs_Ensembl = ENSG00000087274
| Hs_RefseqProtein = NP_001110
| Hs_RefseqmRNA = NM_001119
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 2815382
| Hs_GenLoc_end = 2901587
| Hs_Uniprot =
| Mm_EntrezGene = 11518
| Mm_Ensembl = ENSMUSG00000029106
| Mm_RefseqmRNA = NM_001024458
| Mm_RefseqProtein = NP_001019629
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 34890720
| Mm_GenLoc_end = 34949162
| Mm_Uniprot = Q8BJT2
}}
}}
'''Adducin 1 (alpha)''', also known as '''ADD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ADD1 adducin 1 (alpha)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=118| 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 = Adducins are a family of cytoskeleton proteins encoded by three genes (alpha, beta, gamma). Adducin is a heterodimeric protein that consists of related subunits, which are produced from distinct genes but share a similar structure. Alpha- and beta-adducin include a protease-resistant N-terminal region and a protease-sensitive, hydrophilic C-terminal region. Alpha- and gamma-adducins are ubiquitously expressed. In contrast, beta-adducin is expressed at high levels in brain and hematopoietic tissues. Adducin binds with high affinity to Ca(2+)/calmodulin and is a substrate for protein kinases A and C. Alternative splicing results in multiple variants encoding distinct isoforms; however, not all variants have been fully described.<ref name="entrez">{{cite web | title = Entrez Gene: ADD1 adducin 1 (alpha)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=118| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Mangeat PH |title=Interaction of biological membranes with the cytoskeletal framework of living cells. |journal=Biol. Cell |volume=64 |issue= 3 |pages= 261-81 |year= 1989 |pmid= 2976282 |doi= }}
*{{cite journal | author=Matsuoka Y, Li X, Bennett V |title=Adducin: structure, function and regulation. |journal=Cell. Mol. Life Sci. |volume=57 |issue= 6 |pages= 884-95 |year= 2000 |pmid= 10950304 |doi= }}
*{{cite journal | author=Goldberg YP, Lin BY, Andrew SE, ''et al.'' |title=Cloning and mapping of the alpha-adducin gene close to D4S95 and assessment of its relationship to Huntington disease. |journal=Hum. Mol. Genet. |volume=1 |issue= 9 |pages= 669-75 |year= 1993 |pmid= 1284592 |doi= }}
*{{cite journal | author=Taylor SA, Snell RG, Buckler A, ''et al.'' |title=Cloning of the alpha-adducin gene from the Huntington's disease candidate region of chromosome 4 by exon amplification. |journal=Nat. Genet. |volume=2 |issue= 3 |pages= 223-7 |year= 1994 |pmid= 1345173 |doi= 10.1038/ng1192-223 }}
*{{cite journal | author=Joshi R, Gilligan DM, Otto E, ''et al.'' |title=Primary structure and domain organization of human alpha and beta adducin. |journal=J. Cell Biol. |volume=115 |issue= 3 |pages= 665-75 |year= 1991 |pmid= 1840603 |doi= }}
*{{cite journal | author=Gardner K, Bennett V |title=Modulation of spectrin-actin assembly by erythrocyte adducin. |journal=Nature |volume=328 |issue= 6128 |pages= 359-62 |year= 1987 |pmid= 3600811 |doi= 10.1038/328359a0 }}
*{{cite journal | author=Gilligan DM, Lieman J, Bennett V |title=Assignment of the human beta-adducin gene (ADD2) to 2p13-p14 by in situ hybridization. |journal=Genomics |volume=28 |issue= 3 |pages= 610-2 |year= 1996 |pmid= 7490111 |doi= 10.1006/geno.1995.1205 }}
*{{cite journal | author=Lin B, Nasir J, McDonald H, ''et al.'' |title=Genomic organization of the human alpha-adducin gene and its alternately spliced isoforms. |journal=Genomics |volume=25 |issue= 1 |pages= 93-9 |year= 1995 |pmid= 7774961 |doi= }}
*{{cite journal | author=Nasir J, Lin B, Bucan M, ''et al.'' |title=The murine homologues of the Huntington disease gene (Hdh) and the alpha-adducin gene (Add1) map to mouse chromosome 5 within a region of conserved synteny with human chromosome 4p16.3. |journal=Genomics |volume=22 |issue= 1 |pages= 198-201 |year= 1994 |pmid= 7959767 |doi= 10.1006/geno.1994.1361 }}
*{{cite journal | author=Kuhlman PA, Hughes CA, Bennett V, Fowler VM |title=A new function for adducin. Calcium/calmodulin-regulated capping of the barbed ends of actin filaments. |journal=J. Biol. Chem. |volume=271 |issue= 14 |pages= 7986-91 |year= 1996 |pmid= 8626479 |doi= }}
*{{cite journal | author=Li X, Bennett V |title=Identification of the spectrin subunit and domains required for formation of spectrin/adducin/actin complexes. |journal=J. Biol. Chem. |volume=271 |issue= 26 |pages= 15695-702 |year= 1996 |pmid= 8663089 |doi= }}
*{{cite journal | author=Matsuoka Y, Hughes CA, Bennett V |title=Adducin regulation. Definition of the calmodulin-binding domain and sites of phosphorylation by protein kinases A and C. |journal=J. Biol. Chem. |volume=271 |issue= 41 |pages= 25157-66 |year= 1996 |pmid= 8810272 |doi= }}
*{{cite journal | author=Hadano S, Ishida Y, Tomiyasu H, ''et al.'' |title=Transcript map of the human chromosome 4p16.3 consisting of 627 cDNA clones derived from 1 Mb of the Huntington's disease locus. |journal=DNA Res. |volume=3 |issue= 4 |pages= 239-55 |year= 1997 |pmid= 8946164 |doi= }}
*{{cite journal | author=Cusi D, Barlassina C, Azzani T, ''et al.'' |title=Polymorphisms of alpha-adducin and salt sensitivity in patients with essential hypertension. |journal=Lancet |volume=349 |issue= 9062 |pages= 1353-7 |year= 1997 |pmid= 9149697 |doi= }}
*{{cite journal | author=Kamitani A, Wong ZY, Fraser R, ''et al.'' |title=Human alpha-adducin gene, blood pressure, and sodium metabolism. |journal=Hypertension |volume=32 |issue= 1 |pages= 138-43 |year= 1998 |pmid= 9674650 |doi= }}
*{{cite journal | author=Matsuoka Y, Li X, Bennett V |title=Adducin is an in vivo substrate for protein kinase C: phosphorylation in the MARCKS-related domain inhibits activity in promoting spectrin-actin complexes and occurs in many cells, including dendritic spines of neurons. |journal=J. Cell Biol. |volume=142 |issue= 2 |pages= 485-97 |year= 1998 |pmid= 9679146 |doi= }}
*{{cite journal | author=Fukata Y, Oshiro N, Kinoshita N, ''et al.'' |title=Phosphorylation of adducin by Rho-kinase plays a crucial role in cell motility. |journal=J. Cell Biol. |volume=145 |issue= 2 |pages= 347-61 |year= 1999 |pmid= 10209029 |doi= }}
*{{cite journal | author=Halushka MK, Fan JB, Bentley K, ''et al.'' |title=Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. |journal=Nat. Genet. |volume=22 |issue= 3 |pages= 239-47 |year= 1999 |pmid= 10391210 |doi= 10.1038/10297 }}
*{{cite journal | author=Ferrandi M, Salardi S, Tripodi G, ''et al.'' |title=Evidence for an interaction between adducin and Na(+)-K(+)-ATPase: relation to genetic hypertension. |journal=Am. J. Physiol. |volume=277 |issue= 4 Pt 2 |pages= H1338-49 |year= 1999 |pmid= 10516168 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on C5... {November 16, 2007 3:44:21 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 3:44:45 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_C5_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cfa.
| PDB = {{PDB2|1cfa}}, {{PDB2|1kjs}}, {{PDB2|1xwe}}
| Name = Complement component 5
| HGNCid = 1331
| Symbol = C5
| AltSymbols =; CPAMD4; MGC142298
| OMIM = 120900
| ECnumber =
| Homologene = 20412
| MGIid = 96031
| GeneAtlas_image1 = PBB_GE_C5_205500_at_tn.png
| Function = {{GNF_GO|id=GO:0004866 |text = endopeptidase inhibitor activity}} {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0008009 |text = chemokine activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005579 |text = membrane attack complex}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0000187 |text = activation of MAPK activity}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006950 |text = response to stress}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006956 |text = complement activation}} {{GNF_GO|id=GO:0006957 |text = complement activation, alternative pathway}} {{GNF_GO|id=GO:0006958 |text = complement activation, classical pathway}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0019835 |text = cytolysis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 727
| Hs_Ensembl = ENSG00000106804
| Hs_RefseqProtein = NP_001726
| Hs_RefseqmRNA = NM_001735
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 122754437
| Hs_GenLoc_end = 122852375
| Hs_Uniprot = P01031
| Mm_EntrezGene = 15139
| Mm_Ensembl = ENSMUSG00000026874
| Mm_RefseqmRNA = NM_010406
| Mm_RefseqProtein = NP_034536
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 34805340
| Mm_GenLoc_end = 34883447
| Mm_Uniprot = Q8BNV3
}}
}}
'''Complement component 5''', also known as '''C5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: C5 complement component 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=727| 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=Tack BF, Morris SC, Prahl JW |title=Fifth component of human complement: purification from plasma and polypeptide chain structure. |journal=Biochemistry |volume=18 |issue= 8 |pages= 1490-7 |year= 1979 |pmid= 106884 |doi= }}
*{{cite journal | author=Fernandez HN, Hugli TE |title=Primary structural analysis of the polypeptide portion of human C5a anaphylatoxin. Polypeptide sequence determination and assignment of the oligosaccharide attachment site in C5a. |journal=J. Biol. Chem. |volume=253 |issue= 19 |pages= 6955-64 |year= 1978 |pmid= 690134 |doi= }}
*{{cite journal | author=DiScipio RG |title=Formation and structure of the C5b-7 complex of the lytic pathway of complement. |journal=J. Biol. Chem. |volume=267 |issue= 24 |pages= 17087-94 |year= 1992 |pmid= 1387399 |doi= }}
*{{cite journal | author=Haviland DL, Haviland JC, Fleischer DT, ''et al.'' |title=Complete cDNA sequence of human complement pro-C5. Evidence of truncated transcripts derived from a single copy gene. |journal=J. Immunol. |volume=146 |issue= 1 |pages= 362-8 |year= 1991 |pmid= 1984448 |doi= }}
*{{cite journal | author=Bohnsack JF, Mollison KW, Buko AM, ''et al.'' |title=Group B streptococci inactivate complement component C5a by enzymic cleavage at the C-terminus. |journal=Biochem. J. |volume=273 ( Pt 3) |issue= |pages= 635-40 |year= 1991 |pmid= 1996961 |doi= }}
*{{cite journal | author=Lundwall AB, Wetsel RA, Kristensen T, ''et al.'' |title=Isolation and sequence analysis of a cDNA clone encoding the fifth complement component. |journal=J. Biol. Chem. |volume=260 |issue= 4 |pages= 2108-12 |year= 1985 |pmid= 2579066 |doi= }}
*{{cite journal | author=Zuiderweg ER, Fesik SW |title=Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a. |journal=Biochemistry |volume=28 |issue= 6 |pages= 2387-91 |year= 1989 |pmid= 2730871 |doi= }}
*{{cite journal | author=Zuiderweg ER, Nettesheim DG, Mollison KW, Carter GW |title=Tertiary structure of human complement component C5a in solution from nuclear magnetic resonance data. |journal=Biochemistry |volume=28 |issue= 1 |pages= 172-85 |year= 1989 |pmid= 2784981 |doi= }}
*{{cite journal | author=Haefliger JA, Tschopp J, Vial N, Jenne DE |title=Complete primary structure and functional characterization of the sixth component of the human complement system. Identification of the C5b-binding domain in complement C6. |journal=J. Biol. Chem. |volume=264 |issue= 30 |pages= 18041-51 |year= 1989 |pmid= 2808363 |doi= }}
*{{cite journal | author=Wetsel RA, Lemons RS, Le Beau MM, ''et al.'' |title=Molecular analysis of human complement component C5: localization of the structural gene to chromosome 9. |journal=Biochemistry |volume=27 |issue= 5 |pages= 1474-82 |year= 1988 |pmid= 3365401 |doi= }}
*{{cite journal | author=Zuiderweg ER, Mollison KW, Henkin J, Carter GW |title=Sequence-specific assignments in the 1H NMR spectrum of the human inflammatory protein C5a. |journal=Biochemistry |volume=27 |issue= 10 |pages= 3568-80 |year= 1988 |pmid= 3408713 |doi= }}
*{{cite journal | author=Stewart JL, Kolb WP, Sodetz JM |title=Evidence that C5b recognizes and mediates C8 incorporation into the cytolytic complex of complement. |journal=J. Immunol. |volume=139 |issue= 6 |pages= 1960-4 |year= 1987 |pmid= 3624872 |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=Babkina IN, Seregin SV, Daniliuk NK, ''et al.'' |title=[Chemico-enzymatic synthesis, cloning and expression of a gene for an analog of human anaphylatoxin C5a] |journal=Bioorg. Khim. |volume=21 |issue= 5 |pages= 359-64 |year= 1995 |pmid= 7661861 |doi= }}
*{{cite journal | author=Wang X, Fleischer DT, Whitehead WT, ''et al.'' |title=Inherited human complement C5 deficiency. Nonsense mutations in exons 1 (Gln1 to Stop) and 36 (Arg1458 to Stop) and compound heterozygosity in three African-American families. |journal=J. Immunol. |volume=154 |issue= 10 |pages= 5464-71 |year= 1995 |pmid= 7730648 |doi= }}
*{{cite journal | author=Oppermann M, Götze O |title=Plasma clearance of the human C5a anaphylatoxin by binding to leucocyte C5a receptors. |journal=Immunology |volume=82 |issue= 4 |pages= 516-21 |year= 1995 |pmid= 7835913 |doi= }}
*{{cite journal | author=Süsal C, Kirschfink M, Kröpelin M, ''et al.'' |title=Complement activation by recombinant HIV-1 glycoprotein gp120. |journal=J. Immunol. |volume=152 |issue= 12 |pages= 6028-34 |year= 1994 |pmid= 7911492 |doi= }}
*{{cite journal | author=Arribas J, Arizti P, Castaño JG |title=Antibodies against the C2 COOH-terminal region discriminate the active and latent forms of the multicatalytic proteinase complex. |journal=J. Biol. Chem. |volume=269 |issue= 17 |pages= 12858-64 |year= 1994 |pmid= 8175701 |doi= }}
*{{cite journal | author=Süsal C, Kirschfink M, Kröpelin M, ''et al.'' |title=Identification of complement activation sites in human immunodeficiency virus type-1 glycoprotein gp120. |journal=Blood |volume=87 |issue= 6 |pages= 2329-36 |year= 1996 |pmid= 8630395 |doi= }}
*{{cite journal | author=Ames RS, Li Y, Sarau HM, ''et al.'' |title=Molecular cloning and characterization of the human anaphylatoxin C3a receptor. |journal=J. Biol. Chem. |volume=271 |issue= 34 |pages= 20231-4 |year= 1996 |pmid= 8702752 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CAPN10... {November 16, 2007 3:59:05 PM PST}
- SEARCH REDIRECT: Control Box Found: CAPN10 {November 16, 2007 3:59:28 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 3:59:32 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 3:59:32 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 3:59:32 PM PST}
- UPDATED: Updated protein page: CAPN10 {November 16, 2007 3:59:38 PM PST}
- INFO: Beginning work on CD47... {November 16, 2007 3:45:18 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 3:45:53 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = CD47 molecule
| HGNCid = 1682
| Symbol = CD47
| AltSymbols =; IAP; MER6; OA3
| OMIM = 601028
| ECnumber =
| Homologene = 1346
| MGIid = 96617
| GeneAtlas_image1 = PBB_GE_CD47_213857_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CD47_211075_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_CD47_213055_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007160 |text = cell-matrix adhesion}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 961
| Hs_Ensembl = ENSG00000196776
| Hs_RefseqProtein = NP_001020250
| Hs_RefseqmRNA = NM_001025079
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 109244631
| Hs_GenLoc_end = 109292625
| Hs_Uniprot = Q08722
| Mm_EntrezGene = 16423
| Mm_Ensembl = ENSMUSG00000055447
| Mm_RefseqmRNA = NM_010581
| Mm_RefseqProtein = NP_034711
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 49775244
| Mm_GenLoc_end = 49834636
| Mm_Uniprot = Q3U967
}}
}}
'''CD47 molecule''', also known as '''CD47''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CD47 CD47 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=961| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a membrane protein, which is involved in the increase in intracellular calcium concentration that occurs upon cell adhesion to extracellular matrix. The encoded protein is also a receptor for the C-terminal cell binding domain of thrombospondin, and it may play a role in membrane transport and signal transduction. This gene has broad tissue distribution, and is reduced in expression on Rh erythrocytes. Four alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: CD47 CD47 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=961| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Brown EJ, Frazier WA |title=Integrin-associated protein (CD47) and its ligands. |journal=Trends Cell Biol. |volume=11 |issue= 3 |pages= 130-5 |year= 2001 |pmid= 11306274 |doi= }}
*{{cite journal | author=Oldenborg PA |title=Role of CD47 in erythroid cells and in autoimmunity. |journal=Leuk. Lymphoma |volume=45 |issue= 7 |pages= 1319-27 |year= 2004 |pmid= 15359629 |doi= 10.1080/1042819042000201989 }}
*{{cite journal | author=Kaczorowski DJ, Billiar TR |title=Targeting CD47: NO limit on therapeutic potential. |journal=Circ. Res. |volume=100 |issue= 5 |pages= 602-3 |year= 2007 |pmid= 17363705 |doi= 10.1161/01.RES.0000261609.44977.25 }}
*{{cite journal | author=Campbell IG, Freemont PS, Foulkes W, Trowsdale J |title=An ovarian tumor marker with homology to vaccinia virus contains an IgV-like region and multiple transmembrane domains. |journal=Cancer Res. |volume=52 |issue= 19 |pages= 5416-20 |year= 1992 |pmid= 1394148 |doi= }}
*{{cite journal | author=Brown E, Hooper L, Ho T, Gresham H |title=Integrin-associated protein: a 50-kD plasma membrane antigen physically and functionally associated with integrins. |journal=J. Cell Biol. |volume=111 |issue= 6 Pt 1 |pages= 2785-94 |year= 1991 |pmid= 2277087 |doi= }}
*{{cite journal | author=Lindberg FP, Gresham HD, Schwarz E, Brown EJ |title=Molecular cloning of integrin-associated protein: an immunoglobulin family member with multiple membrane-spanning domains implicated in alpha v beta 3-dependent ligand binding. |journal=J. Cell Biol. |volume=123 |issue= 2 |pages= 485-96 |year= 1993 |pmid= 7691831 |doi= }}
*{{cite journal | author=Mawby WJ, Holmes CH, Anstee DJ, ''et al.'' |title=Isolation and characterization of CD47 glycoprotein: a multispanning membrane protein which is the same as integrin-associated protein (IAP) and the ovarian tumour marker OA3. |journal=Biochem. J. |volume=304 ( Pt 2) |issue= |pages= 525-30 |year= 1995 |pmid= 7998989 |doi= }}
*{{cite journal | author=Lindberg FP, Lublin DM, Telen MJ, ''et al.'' |title=Rh-related antigen CD47 is the signal-transducer integrin-associated protein. |journal=J. Biol. Chem. |volume=269 |issue= 3 |pages= 1567-70 |year= 1994 |pmid= 8294396 |doi= }}
*{{cite journal | author=Gao AG, Lindberg FP, Finn MB, ''et al.'' |title=Integrin-associated protein is a receptor for the C-terminal domain of thrombospondin. |journal=J. Biol. Chem. |volume=271 |issue= 1 |pages= 21-4 |year= 1996 |pmid= 8550562 |doi= }}
*{{cite journal | author=Cherif-Zahar B, Raynal V, Gane P, ''et al.'' |title=Candidate gene acting as a suppressor of the RH locus in most cases of Rh-deficiency. |journal=Nat. Genet. |volume=12 |issue= 2 |pages= 168-73 |year= 1996 |pmid= 8563755 |doi= 10.1038/ng0296-168 }}
*{{cite journal | author=Chung J, Gao AG, Frazier WA |title=Thrombspondin acts via integrin-associated protein to activate the platelet integrin alphaIIbbeta3. |journal=J. Biol. Chem. |volume=272 |issue= 23 |pages= 14740-6 |year= 1997 |pmid= 9169439 |doi= }}
*{{cite journal | author=Jiang P, Lagenaur CF, Narayanan V |title=Integrin-associated protein is a ligand for the P84 neural adhesion molecule. |journal=J. Biol. Chem. |volume=274 |issue= 2 |pages= 559-62 |year= 1999 |pmid= 9872987 |doi= }}
*{{cite journal | author=Hermann P, Armant M, Brown E, ''et al.'' |title=The vitronectin receptor and its associated CD47 molecule mediates proinflammatory cytokine synthesis in human monocytes by interaction with soluble CD23. |journal=J. Cell Biol. |volume=144 |issue= 4 |pages= 767-75 |year= 1999 |pmid= 10037797 |doi= }}
*{{cite journal | author=Chung J, Wang XQ, Lindberg FP, Frazier WA |title=Thrombospondin-1 acts via IAP/CD47 to synergize with collagen in alpha2beta1-mediated platelet activation. |journal=Blood |volume=94 |issue= 2 |pages= 642-8 |year= 1999 |pmid= 10397731 |doi= }}
*{{cite journal | author=Longhurst CM, White MM, Wilkinson DA, Jennings LK |title=A CD9, alphaIIbbeta3, integrin-associated protein, and GPIb/V/IX complex on the surface of human platelets is influenced by alphaIIbbeta3 conformational states. |journal=Eur. J. Biochem. |volume=263 |issue= 1 |pages= 104-11 |year= 1999 |pmid= 10429193 |doi= }}
*{{cite journal | author=Mateo V, Lagneaux L, Bron D, ''et al.'' |title=CD47 ligation induces caspase-independent cell death in chronic lymphocytic leukemia. |journal=Nat. Med. |volume=5 |issue= 11 |pages= 1277-84 |year= 1999 |pmid= 10545994 |doi= 10.1038/15233 }}
*{{cite journal | author=Wu AL, Wang J, Zheleznyak A, Brown EJ |title=Ubiquitin-related proteins regulate interaction of vimentin intermediate filaments with the plasma membrane. |journal=Mol. Cell |volume=4 |issue= 4 |pages= 619-25 |year= 1999 |pmid= 10549293 |doi= }}
*{{cite journal | author=Erb L, Liu J, Ockerhausen J, ''et al.'' |title=An RGD sequence in the P2Y(2) receptor interacts with alpha(V)beta(3) integrins and is required for G(o)-mediated signal transduction. |journal=J. Cell Biol. |volume=153 |issue= 3 |pages= 491-501 |year= 2001 |pmid= 11331301 |doi= }}
*{{cite journal | author=Rebres RA, Vaz LE, Green JM, Brown EJ |title=Normal ligand binding and signaling by CD47 (integrin-associated protein) requires a long range disulfide bond between the extracellular and membrane-spanning domains. |journal=J. Biol. Chem. |volume=276 |issue= 37 |pages= 34607-16 |year= 2001 |pmid= 11454874 |doi= 10.1074/jbc.M106107200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CD8A... {November 16, 2007 3:44:45 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 3:45:18 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CD8A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1akj.
| PDB = {{PDB2|1akj}}, {{PDB2|1cd8}}, {{PDB2|2hp4}}
| Name = CD8a molecule
| HGNCid = 1706
| Symbol = CD8A
| AltSymbols =; p32; CD8; Leu2; MAL
| OMIM = 186910
| ECnumber =
| Homologene = 1339
| MGIid = 88346
| GeneAtlas_image1 = PBB_GE_CD8A_205758_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0015026 |text = coreceptor activity}} {{GNF_GO|id=GO:0042288 |text = MHC class I protein binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0009897 |text = external side of plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0042101 |text = T cell receptor complex}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0006968 |text = cellular defense response}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}} {{GNF_GO|id=GO:0019882 |text = antigen processing and presentation}} {{GNF_GO|id=GO:0042110 |text = T cell activation}} {{GNF_GO|id=GO:0045065 |text = cytotoxic T cell differentiation}} {{GNF_GO|id=GO:0050850 |text = positive regulation of calcium-mediated signaling}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 925
| Hs_Ensembl = ENSG00000153563
| Hs_RefseqProtein = NP_001759
| Hs_RefseqmRNA = NM_001768
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 86865245
| Hs_GenLoc_end = 86871578
| Hs_Uniprot = P01732
| Mm_EntrezGene = 12525
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_132621
| Mm_RefseqProtein = XP_132621
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''CD8a molecule''', also known as '''CD8A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CD8A CD8a molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=925| 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 CD8 antigen is a cell surface glycoprotein found on most cytotoxic T lymphocytes that mediates efficient cell-cell interactions within the immune system. The CD8 antigen, acting as a coreceptor, and the T-cell receptor on the T lymphocyte recognize antigen displayed by an antigen presenting cell (APC) in the context of class I MHC molecules. The functional coreceptor is either a homodimer composed of two alpha chains, or a heterodimer composed of one alpha and one beta chain. Both alpha and beta chains share significant homology to immunoglobulin variable light chains. This gene encodes the CD8 alpha chain isoforms. Two alternative transcripts encoding distinct isoforms, one membrane associated and one secreted, have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: CD8A CD8a molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=925| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Parnes JR |title=Molecular biology and function of CD4 and CD8. |journal=Adv. Immunol. |volume=44 |issue= |pages= 265-311 |year= 1989 |pmid= 2493728 |doi= }}
*{{cite journal | author=Li L, Li HS, Pauza CD, ''et al.'' |title=Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions. |journal=Cell Res. |volume=15 |issue= 11-12 |pages= 923-34 |year= 2006 |pmid= 16354571 |doi= 10.1038/sj.cr.7290370 }}
*{{cite journal | author=Stove V, Verhasselt B |title=Modelling thymic HIV-1 Nef effects. |journal=Curr. HIV Res. |volume=4 |issue= 1 |pages= 57-64 |year= 2006 |pmid= 16454711 |doi= }}
*{{cite journal | author=Nakayama K, Kawachi Y, Tokito S, ''et al.'' |title=Recent duplication of the two human CD8 beta-chain genes. |journal=J. Immunol. |volume=148 |issue= 6 |pages= 1919-27 |year= 1992 |pmid= 1541829 |doi= }}
*{{cite journal | author=Leahy DJ, Axel R, Hendrickson WA |title=Crystal structure of a soluble form of the human T cell coreceptor CD8 at 2.6 A resolution. |journal=Cell |volume=68 |issue= 6 |pages= 1145-62 |year= 1992 |pmid= 1547508 |doi= }}
*{{cite journal | author=Erickson JD, Trojanowski JQ, Eiden LE |title=Regional distribution and partial molecular characterization of CD4-related mRNA in human brain and peripheral tissues. |journal=Brain Res. Mol. Brain Res. |volume=10 |issue= 1 |pages= 23-31 |year= 1991 |pmid= 1676132 |doi= }}
*{{cite journal | author=Moebius U, Kober G, Griscelli AL, ''et al.'' |title=Expression of different CD8 isoforms on distinct human lymphocyte subpopulations. |journal=Eur. J. Immunol. |volume=21 |issue= 8 |pages= 1793-800 |year= 1991 |pmid= 1831127 |doi= }}
*{{cite journal | author=Mittler RS, Rankin BM, Kiener PA |title=Physical associations between CD45 and CD4 or CD8 occur as late activation events in antigen receptor-stimulated human T cells. |journal=J. Immunol. |volume=147 |issue= 10 |pages= 3434-40 |year= 1991 |pmid= 1834739 |doi= }}
*{{cite journal | author=Sanders SK, Giblin PA, Kavathas P |title=Cell-cell adhesion mediated by CD8 and human histocompatibility leukocyte antigen G, a nonclassical major histocompatibility complex class 1 molecule on cytotrophoblasts. |journal=J. Exp. Med. |volume=174 |issue= 3 |pages= 737-40 |year= 1991 |pmid= 1908512 |doi= }}
*{{cite journal | author=Barber EK, Dasgupta JD, Schlossman SF, ''et al.'' |title=The CD4 and CD8 antigens are coupled to a protein-tyrosine kinase (p56lck) that phosphorylates the CD3 complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 9 |pages= 3277-81 |year= 1989 |pmid= 2470098 |doi= }}
*{{cite journal | author=Norment AM, Lonberg N, Lacy E, Littman DR |title=Alternatively spliced mRNA encodes a secreted form of human CD8 alpha. Characterization of the human CD8 alpha gene. |journal=J. Immunol. |volume=142 |issue= 9 |pages= 3312-9 |year= 1989 |pmid= 2496167 |doi= }}
*{{cite journal | author=Nakayama K, Tokito S, Okumura K, Nakauchi H |title=Structure and expression of the gene encoding CD8 alpha chain (Leu-2/T8). |journal=Immunogenetics |volume=30 |issue= 5 |pages= 393-7 |year= 1989 |pmid= 2509342 |doi= }}
*{{cite journal | author=Giblin P, Ledbetter JA, Kavathas P |title=A secreted form of the human lymphocyte cell surface molecule CD8 arises from alternative splicing. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 3 |pages= 998-1002 |year= 1989 |pmid= 2536941 |doi= }}
*{{cite journal | author=Aruffo A, Seed B |title=Expression of cDNA clones encoding the thymocyte antigens CD1a, b, c demonstrates a hierarchy of exclusion in fibroblasts. |journal=J. Immunol. |volume=143 |issue= 5 |pages= 1723-30 |year= 1989 |pmid= 2701945 |doi= }}
*{{cite journal | author=Bowcock AM, Kavathas P, Margolskee RF, ''et al.'' |title=An RFLP associated with pcDLeu2-14, a human T-cell differentiation antigen CD8 (Leu2) cDNA mapped to 2p12. |journal=Nucleic Acids Res. |volume=14 |issue= 19 |pages= 7817 |year= 1986 |pmid= 2877435 |doi= }}
*{{cite journal | author=Norment AM, Littman DR |title=A second subunit of CD8 is expressed in human T cells. |journal=EMBO J. |volume=7 |issue= 11 |pages= 3433-9 |year= 1989 |pmid= 3145195 |doi= }}
*{{cite journal | author=Littman DR, Thomas Y, Maddon PJ, ''et al.'' |title=The isolation and sequence of the gene encoding T8: a molecule defining functional classes of T lymphocytes. |journal=Cell |volume=40 |issue= 2 |pages= 237-46 |year= 1985 |pmid= 3871356 |doi= }}
*{{cite journal | author=Sukhatme VP, Sizer KC, Vollmer AC, ''et al.'' |title=The T cell differentiation antigen Leu-2/T8 is homologous to immunoglobulin and T cell receptor variable regions. |journal=Cell |volume=40 |issue= 3 |pages= 591-7 |year= 1985 |pmid= 3918796 |doi= }}
*{{cite journal | author=Parnes JR, Sizer KC, Sukhatme VP, Hunkapiller T |title=Structure of Leu-2/T8 as deduced from the sequence of a cDNA clone. |journal=Behring Inst. Mitt. |volume= |issue= 77 |pages= 48-55 |year= 1986 |pmid= 3936473 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CHRM2... {November 16, 2007 3:45:53 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 3:46:20 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Cholinergic receptor, muscarinic 2
| HGNCid = 1951
| Symbol = CHRM2
| AltSymbols =; FLJ43243; HM2; MGC120006; MGC120007
| OMIM = 118493
| ECnumber =
| Homologene = 20190
| MGIid = 88397
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004981 |text = muscarinic acetylcholine receptor activity}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0045211 |text = postsynaptic membrane}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007188 |text = G-protein signaling, coupled to cAMP nucleotide second messenger}} {{GNF_GO|id=GO:0007197 |text = muscarinic acetylcholine receptor, adenylate cyclase inhibiting pathway}} {{GNF_GO|id=GO:0007207 |text = muscarinic acetylcholine receptor, phospholipase C activating pathway}} {{GNF_GO|id=GO:0007213 |text = acetylcholine receptor signaling, muscarinic pathway}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0008016 |text = regulation of heart contraction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1129
| Hs_Ensembl = ENSG00000181072
| Hs_RefseqProtein = NP_000730
| Hs_RefseqmRNA = NM_000739
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 136203956
| Hs_GenLoc_end = 136355539
| Hs_Uniprot = P08172
| Mm_EntrezGene = 243764
| Mm_Ensembl = ENSMUSG00000045613
| Mm_RefseqmRNA = NM_203491
| Mm_RefseqProtein = NP_987076
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 36453362
| Mm_GenLoc_end = 36454762
| Mm_Uniprot = Q05CZ8
}}
}}
'''Cholinergic receptor, muscarinic 2''', also known as '''CHRM2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CHRM2 cholinergic receptor, muscarinic 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1129| 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 muscarinic cholinergic receptors belong to a larger family of G protein-coupled receptors. The functional diversity of these receptors is defined by the binding of acetylcholine to these receptors and includes cellular responses such as adenylate cyclase inhibition, phosphoinositide degeneration, and potassium channel mediation. Muscarinic receptors influence many effects of acetylcholine in the central and peripheral nervous system. The muscarinic cholinergic receptor 2 is involved in mediation of bradycardia and a decrease in cardiac contractility. Multiple alternatively spliced transcript variants have been described for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: CHRM2 cholinergic receptor, muscarinic 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1129| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Goyal RK |title=Muscarinic receptor subtypes. Physiology and clinical implications. |journal=N. Engl. J. Med. |volume=321 |issue= 15 |pages= 1022-9 |year= 1989 |pmid= 2674717 |doi= }}
*{{cite journal | author=Brann MR, Ellis J, Jørgensen H, ''et al.'' |title=Muscarinic acetylcholine receptor subtypes: localization and structure/function. |journal=Prog. Brain Res. |volume=98 |issue= |pages= 121-7 |year= 1994 |pmid= 8248499 |doi= }}
*{{cite journal | author=van Koppen CJ, Nathanson NM |title=Site-directed mutagenesis of the m2 muscarinic acetylcholine receptor. Analysis of the role of N-glycosylation in receptor expression and function. |journal=J. Biol. Chem. |volume=265 |issue= 34 |pages= 20887-92 |year= 1991 |pmid= 2249995 |doi= }}
*{{cite journal | author=Ashkenazi A, Ramachandran J, Capon DJ |title=Acetylcholine analogue stimulates DNA synthesis in brain-derived cells via specific muscarinic receptor subtypes. |journal=Nature |volume=340 |issue= 6229 |pages= 146-50 |year= 1989 |pmid= 2739737 |doi= 10.1038/340146a0 }}
*{{cite journal | author=Bonner TI, Buckley NJ, Young AC, Brann MR |title=Identification of a family of muscarinic acetylcholine receptor genes. |journal=Science |volume=237 |issue= 4814 |pages= 527-32 |year= 1987 |pmid= 3037705 |doi= }}
*{{cite journal | author=Peralta EG, Ashkenazi A, Winslow JW, ''et al.'' |title=Distinct primary structures, ligand-binding properties and tissue-specific expression of four human muscarinic acetylcholine receptors. |journal=EMBO J. |volume=6 |issue= 13 |pages= 3923-9 |year= 1988 |pmid= 3443095 |doi= }}
*{{cite journal | author=Badner JA, Yoon SW, Turner G, ''et al.'' |title=Multipoint genetic linkage analysis of the m2 human muscarinic receptor gene. |journal=Mamm. Genome |volume=6 |issue= 7 |pages= 489-90 |year= 1995 |pmid= 7579899 |doi= }}
*{{cite journal | author=Offermanns S, Simon MI |title=G alpha 15 and G alpha 16 couple a wide variety of receptors to phospholipase C. |journal=J. Biol. Chem. |volume=270 |issue= 25 |pages= 15175-80 |year= 1995 |pmid= 7797501 |doi= }}
*{{cite journal | author=Russell M, Winitz S, Johnson GL |title=Acetylcholine muscarinic m1 receptor regulation of cyclic AMP synthesis controls growth factor stimulation of Raf activity. |journal=Mol. Cell. Biol. |volume=14 |issue= 4 |pages= 2343-51 |year= 1994 |pmid= 8139539 |doi= }}
*{{cite journal | author=Kunapuli P, Onorato JJ, Hosey MM, Benovic JL |title=Expression, purification, and characterization of the G protein-coupled receptor kinase GRK5. |journal=J. Biol. Chem. |volume=269 |issue= 2 |pages= 1099-105 |year= 1994 |pmid= 8288567 |doi= }}
*{{cite journal | author=Haga K, Kameyama K, Haga T, ''et al.'' |title=Phosphorylation of human m1 muscarinic acetylcholine receptors by G protein-coupled receptor kinase 2 and protein kinase C. |journal=J. Biol. Chem. |volume=271 |issue= 5 |pages= 2776-82 |year= 1996 |pmid= 8576254 |doi= }}
*{{cite journal | author=Kostenis E, Conklin BR, Wess J |title=Molecular basis of receptor/G protein coupling selectivity studied by coexpression of wild type and mutant m2 muscarinic receptors with mutant G alpha(q) subunits. |journal=Biochemistry |volume=36 |issue= 6 |pages= 1487-95 |year= 1997 |pmid= 9063897 |doi= 10.1021/bi962554d }}
*{{cite journal | author=Smiley JF, Levey AI, Mesulam MM |title=Infracortical interstitial cells concurrently expressing m2-muscarinic receptors, acetylcholinesterase and nicotinamide adenine dinucleotide phosphate-diaphorase in the human and monkey cerebral cortex. |journal=Neuroscience |volume=84 |issue= 3 |pages= 755-69 |year= 1998 |pmid= 9579781 |doi= }}
*{{cite journal | author=von der Kammer H, Mayhaus M, Albrecht C, ''et al.'' |title=Muscarinic acetylcholine receptors activate expression of the EGR gene family of transcription factors. |journal=J. Biol. Chem. |volume=273 |issue= 23 |pages= 14538-44 |year= 1998 |pmid= 9603968 |doi= }}
*{{cite journal | author=Sato KZ, Fujii T, Watanabe Y, ''et al.'' |title=Diversity of mRNA expression for muscarinic acetylcholine receptor subtypes and neuronal nicotinic acetylcholine receptor subunits in human mononuclear leukocytes and leukemic cell lines. |journal=Neurosci. Lett. |volume=266 |issue= 1 |pages= 17-20 |year= 1999 |pmid= 10336173 |doi= }}
*{{cite journal | author=Retondaro FC, Dos Santos Costa PC, Pedrosa RC, Kurtenbach E |title=Presence of antibodies against the third intracellular loop of the m2 muscarinic receptor in the sera of chronic chagasic patients. |journal=FASEB J. |volume=13 |issue= 14 |pages= 2015-20 |year= 1999 |pmid= 10544184 |doi= }}
*{{cite journal | author=Waid DK, Chell M, El-Fakahany EE |title=M(2) and M(4) muscarinic receptor subtypes couple to activation of endothelial nitric oxide synthase. |journal=Pharmacology |volume=61 |issue= 1 |pages= 37-42 |year= 2000 |pmid= 10895079 |doi= }}
*{{cite journal | author=Obara K, Arai K, Miyajima N, ''et al.'' |title=Expression of m2 muscarinic acetylcholine receptor mRNA in primary culture of human prostate stromal cells. |journal=Urol. Res. |volume=28 |issue= 3 |pages= 196-200 |year= 2000 |pmid= 10929429 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CTCF... {November 16, 2007 3:56:55 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 3:59:05 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
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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_CTCF_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1x6h.
| PDB = {{PDB2|1x6h}}, {{PDB2|2ct1}}
| Name = CCCTC-binding factor (zinc finger protein)
| HGNCid = 13723
| Symbol = CTCF
| AltSymbols =;
| OMIM = 604167
| ECnumber =
| Homologene = 4786
| MGIid = 109447
| GeneAtlas_image1 = PBB_GE_CTCF_202521_at_tn.png
| Function = {{GNF_GO|id=GO:0003676 |text = nucleic acid binding}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003702 |text = RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0003714 |text = transcription corepressor activity}} {{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:0005622 |text = intracellular}} {{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:0006349 |text = imprinting}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0010216 |text = maintenance of DNA methylation}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}} {{GNF_GO|id=GO:0045893 |text = positive regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10664
| Hs_Ensembl = ENSG00000102974
| Hs_RefseqProtein = NP_006556
| Hs_RefseqmRNA = NM_006565
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 66153965
| Hs_GenLoc_end = 66230584
| Hs_Uniprot = P49711
| Mm_EntrezGene = 13018
| Mm_Ensembl = ENSMUSG00000005698
| Mm_RefseqmRNA = NM_007794
| Mm_RefseqProtein = NP_031820
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 108525670
| Mm_GenLoc_end = 108572051
| Mm_Uniprot = Q05CK6
}}
}}
'''CCCTC-binding factor (zinc finger protein)''', also known as '''CTCF''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CTCF CCCTC-binding factor (zinc finger protein)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10664| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is a member of the BORIS + CTCF gene family and encodes a transcriptional regulator protein with 11 highly conserved zinc finger (ZF) domains. This nuclear protein is able to use different combinations of the ZF domains to bind different DNA target sequences and proteins. Depending upon the context of the site, the protein can bind a histone acetyltransferase (HAT)-containing complex and function as a transcriptional activator or bind a histone deacetylase (HDAC)-containing complex and function as a transcriptional repressor. If the protein is bound to a transcriptional insulator element, it can block communication between enhancers and upstream promoters, thereby regulating imprinted expression. Mutations in this gene have been associated with invasive breast cancers, prostate cancers, and Wilms' tumors.<ref name="entrez">{{cite web | title = Entrez Gene: CTCF CCCTC-binding factor (zinc finger protein)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10664| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ohlsson R, Renkawitz R, Lobanenkov V |title=CTCF is a uniquely versatile transcription regulator linked to epigenetics and disease. |journal=Trends Genet. |volume=17 |issue= 9 |pages= 520-7 |year= 2001 |pmid= 11525835 |doi= }}
*{{cite journal | author=Klenova EM, Morse HC, Ohlsson R, Lobanenkov VV |title=The novel BORIS + CTCF gene family is uniquely involved in the epigenetics of normal biology and cancer. |journal=Semin. Cancer Biol. |volume=12 |issue= 5 |pages= 399-414 |year= 2003 |pmid= 12191639 |doi= }}
*{{cite journal | author=Kuhn EJ, Geyer PK |title=Genomic insulators: connecting properties to mechanism. |journal=Curr. Opin. Cell Biol. |volume=15 |issue= 3 |pages= 259-65 |year= 2004 |pmid= 12787766 |doi= }}
*{{cite journal | author=Recillas-Targa F, De La Rosa-Velázquez IA, Soto-Reyes E, Benítez-Bribiesca L |title=Epigenetic boundaries of tumour suppressor gene promoters: the CTCF connection and its role in carcinogenesis. |journal=J. Cell. Mol. Med. |volume=10 |issue= 3 |pages= 554-68 |year= 2007 |pmid= 16989720 |doi= }}
*{{cite journal | author=Filippova GN, Fagerlie S, Klenova EM, ''et al.'' |title=An exceptionally conserved transcriptional repressor, CTCF, employs different combinations of zinc fingers to bind diverged promoter sequences of avian and mammalian c-myc oncogenes. |journal=Mol. Cell. Biol. |volume=16 |issue= 6 |pages= 2802-13 |year= 1996 |pmid= 8649389 |doi= }}
*{{cite journal | author=Vostrov AA, Quitschke WW |title=The zinc finger protein CTCF binds to the APBbeta domain of the amyloid beta-protein precursor promoter. Evidence for a role in transcriptional activation. |journal=J. Biol. Chem. |volume=272 |issue= 52 |pages= 33353-9 |year= 1998 |pmid= 9407128 |doi= }}
*{{cite journal | author=Filippova GN, Lindblom A, Meincke LJ, ''et al.'' |title=A widely expressed transcription factor with multiple DNA sequence specificity, CTCF, is localized at chromosome segment 16q22.1 within one of the smallest regions of overlap for common deletions in breast and prostate cancers. |journal=Genes Chromosomes Cancer |volume=22 |issue= 1 |pages= 26-36 |year= 1998 |pmid= 9591631 |doi= }}
*{{cite journal | author=Bell AC, West AG, Felsenfeld G |title=The protein CTCF is required for the enhancer blocking activity of vertebrate insulators. |journal=Cell |volume=98 |issue= 3 |pages= 387-96 |year= 1999 |pmid= 10458613 |doi= }}
*{{cite journal | author=Pérez-Juste G, García-Silva S, Aranda A |title=An element in the region responsible for premature termination of transcription mediates repression of c-myc gene expression by thyroid hormone in neuroblastoma cells. |journal=J. Biol. Chem. |volume=275 |issue= 2 |pages= 1307-14 |year= 2000 |pmid= 10625678 |doi= }}
*{{cite journal | author=Lutz M, Burke LJ, Barreto G, ''et al.'' |title=Transcriptional repression by the insulator protein CTCF involves histone deacetylases. |journal=Nucleic Acids Res. |volume=28 |issue= 8 |pages= 1707-13 |year= 2000 |pmid= 10734189 |doi= }}
*{{cite journal | author=Bell AC, Felsenfeld G |title=Methylation of a CTCF-dependent boundary controls imprinted expression of the Igf2 gene. |journal=Nature |volume=405 |issue= 6785 |pages= 482-5 |year= 2000 |pmid= 10839546 |doi= 10.1038/35013100 }}
*{{cite journal | author=Hark AT, Schoenherr CJ, Katz DJ, ''et al.'' |title=CTCF mediates methylation-sensitive enhancer-blocking activity at the H19/Igf2 locus. |journal=Nature |volume=405 |issue= 6785 |pages= 486-9 |year= 2000 |pmid= 10839547 |doi= 10.1038/35013106 }}
*{{cite journal | author=Chernukhin IV, Shamsuddin S, Robinson AF, ''et al.'' |title=Physical and functional interaction between two pluripotent proteins, the Y-box DNA/RNA-binding factor, YB-1, and the multivalent zinc finger factor, CTCF. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29915-21 |year= 2000 |pmid= 10906122 |doi= 10.1074/jbc.M001538200 }}
*{{cite journal | author=Chao W, Huynh KD, Spencer RJ, ''et al.'' |title=CTCF, a candidate trans-acting factor for X-inactivation choice. |journal=Science |volume=295 |issue= 5553 |pages= 345-7 |year= 2002 |pmid= 11743158 |doi= 10.1126/science.1065982 }}
*{{cite journal | author=Dintilhac A, Bernués J |title=HMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid sequences. |journal=J. Biol. Chem. |volume=277 |issue= 9 |pages= 7021-8 |year= 2002 |pmid= 11748221 |doi= 10.1074/jbc.M108417200 }}
*{{cite journal | author=Filippova GN, Qi CF, Ulmer JE, ''et al.'' |title=Tumor-associated zinc finger mutations in the CTCF transcription factor selectively alter tts DNA-binding specificity. |journal=Cancer Res. |volume=62 |issue= 1 |pages= 48-52 |year= 2002 |pmid= 11782357 |doi= }}
*{{cite journal | author=Jia L, Young MF, Powell J, ''et al.'' |title=Gene expression profile of human bone marrow stromal cells: high-throughput expressed sequence tag sequencing analysis. |journal=Genomics |volume=79 |issue= 1 |pages= 7-17 |year= 2002 |pmid= 11827452 |doi= 10.1006/geno.2001.6683 }}
*{{cite journal | author=Kanduri M, Kanduri C, Mariano P, ''et al.'' |title=Multiple nucleosome positioning sites regulate the CTCF-mediated insulator function of the H19 imprinting control region. |journal=Mol. Cell. Biol. |volume=22 |issue= 10 |pages= 3339-44 |year= 2002 |pmid= 11971967 |doi= }}
*{{cite journal | author=Farrell CM, West AG, Felsenfeld G |title=Conserved CTCF insulator elements flank the mouse and human beta-globin loci. |journal=Mol. Cell. Biol. |volume=22 |issue= 11 |pages= 3820-31 |year= 2002 |pmid= 11997516 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CYP27B1... {November 16, 2007 3:46:20 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 3:47:05 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Cytochrome P450, family 27, subfamily B, polypeptide 1
| HGNCid = 2606
| Symbol = CYP27B1
| AltSymbols =; CYP1; CP2B; CYP1alpha; CYP27B; P450c1; PDDR; VDD1; VDDR; VDDRI; VDR
| OMIM = 609506
| ECnumber =
| Homologene = 37139
| MGIid = 1098274
| GeneAtlas_image1 = PBB_GE_CYP27B1_205676_at_tn.png
| Function = {{GNF_GO|id=GO:0004497 |text = monooxygenase activity}} {{GNF_GO|id=GO:0004498 |text = calcidiol 1-monooxygenase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0019825 |text = oxygen binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006816 |text = calcium ion transport}} {{GNF_GO|id=GO:0006874 |text = cellular calcium ion homeostasis}} {{GNF_GO|id=GO:0009110 |text = vitamin biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1594
| Hs_Ensembl = ENSG00000111012
| Hs_RefseqProtein = NP_000776
| Hs_RefseqmRNA = NM_000785
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 56442385
| Hs_GenLoc_end = 56447243
| Hs_Uniprot = O15528
| Mm_EntrezGene = 13115
| Mm_Ensembl = ENSMUSG00000006724
| Mm_RefseqmRNA = NM_010009
| Mm_RefseqProtein = NP_034139
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 126451199
| Mm_GenLoc_end = 126455954
| Mm_Uniprot = Q66JY8
}}
}}
'''Cytochrome P450, family 27, subfamily B, polypeptide 1''', also known as '''CYP27B1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CYP27B1 cytochrome P450, family 27, subfamily B, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1594| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. The protein encoded by this gene localizes to the inner mitochondrial membrane where it hydroxylates 25-hydroxyvitamin D3 at the 1alpha position. This reaction synthesizes 1alpha,25-dihydroxyvitamin D3, the active form of vitamin D3, which binds to the vitamin D receptor and regulates calcium metabolism. Thus this enzyme regulates the level of biologically active vitamin D and plays an important role in calcium homeostasis. Mutations in this gene can result in vitamin D-dependent rickets type I.<ref name="entrez">{{cite web | title = Entrez Gene: CYP27B1 cytochrome P450, family 27, subfamily B, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1594| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Szpirer J, Szpirer C, Riviere M, ''et al.'' |title=The Sp1 transcription factor gene (SP1) and the 1,25-dihydroxyvitamin D3 receptor gene (VDR) are colocalized on human chromosome arm 12q and rat chromosome 7. |journal=Genomics |volume=11 |issue= 1 |pages= 168-73 |year= 1992 |pmid= 1662663 |doi= }}
*{{cite journal | author=Pryke AM, Duggan C, White CP, ''et al.'' |title=Tumor necrosis factor-alpha induces vitamin D-1-hydroxylase activity in normal human alveolar macrophages. |journal=J. Cell. Physiol. |volume=142 |issue= 3 |pages= 652-6 |year= 1990 |pmid= 1690216 |doi= 10.1002/jcp.1041420327 }}
*{{cite journal | author=Labuda M, Morgan K, Glorieux FH |title=Mapping autosomal recessive vitamin D dependency type I to chromosome 12q14 by linkage analysis. |journal=Am. J. Hum. Genet. |volume=47 |issue= 1 |pages= 28-36 |year= 1990 |pmid= 1971995 |doi= }}
*{{cite journal | author=Besançon F, Just J, Bourgeade MF, ''et al.'' |title=HIV-1 p17 and IFN-gamma both induce fructose 1,6-bisphosphatase. |journal=J. Interferon Cytokine Res. |volume=17 |issue= 8 |pages= 461-7 |year= 1997 |pmid= 9282826 |doi= }}
*{{cite journal | author=Takeyama K, Kitanaka S, Sato T, ''et al.'' |title=25-Hydroxyvitamin D3 1alpha-hydroxylase and vitamin D synthesis. |journal=Science |volume=277 |issue= 5333 |pages= 1827-30 |year= 1997 |pmid= 9295274 |doi= }}
*{{cite journal | author=St-Arnaud R, Messerlian S, Moir JM, ''et al.'' |title=The 25-hydroxyvitamin D 1-alpha-hydroxylase gene maps to the pseudovitamin D-deficiency rickets (PDDR) disease locus. |journal=J. Bone Miner. Res. |volume=12 |issue= 10 |pages= 1552-9 |year= 1998 |pmid= 9333115 |doi= }}
*{{cite journal | author=Monkawa T, Yoshida T, Wakino S, ''et al.'' |title=Molecular cloning of cDNA and genomic DNA for human 25-hydroxyvitamin D3 1 alpha-hydroxylase. |journal=Biochem. Biophys. Res. Commun. |volume=239 |issue= 2 |pages= 527-33 |year= 1997 |pmid= 9344864 |doi= 10.1006/bbrc.1997.7508 }}
*{{cite journal | author=Fu GK, Lin D, Zhang MY, ''et al.'' |title=Cloning of human 25-hydroxyvitamin D-1 alpha-hydroxylase and mutations causing vitamin D-dependent rickets type 1. |journal=Mol. Endocrinol. |volume=11 |issue= 13 |pages= 1961-70 |year= 1998 |pmid= 9415400 |doi= }}
*{{cite journal | author=Fu GK, Portale AA, Miller WL |title=Complete structure of the human gene for the vitamin D 1alpha-hydroxylase, P450c1alpha. |journal=DNA Cell Biol. |volume=16 |issue= 12 |pages= 1499-507 |year= 1998 |pmid= 9428799 |doi= }}
*{{cite journal | author=Kitanaka S, Takeyama K, Murayama A, ''et al.'' |title=Inactivating mutations in the 25-hydroxyvitamin D3 1alpha-hydroxylase gene in patients with pseudovitamin D-deficiency rickets. |journal=N. Engl. J. Med. |volume=338 |issue= 10 |pages= 653-61 |year= 1998 |pmid= 9486994 |doi= }}
*{{cite journal | author=Wang JT, Lin CJ, Burridge SM, ''et al.'' |title=Genetics of vitamin D 1alpha-hydroxylase deficiency in 17 families. |journal=Am. J. Hum. Genet. |volume=63 |issue= 6 |pages= 1694-702 |year= 1999 |pmid= 9837822 |doi= }}
*{{cite journal | author=Smith SJ, Rucka AK, Berry JL, ''et al.'' |title=Novel mutations in the 1alpha-hydroxylase (P450c1) gene in three families with pseudovitamin D-deficiency rickets resulting in loss of functional enzyme activity in blood-derived macrophages. |journal=J. Bone Miner. Res. |volume=14 |issue= 5 |pages= 730-9 |year= 1999 |pmid= 10320521 |doi= }}
*{{cite journal | author=Kong XF, Zhu XH, Pei YL, ''et al.'' |title=Molecular cloning, characterization, and promoter analysis of the human 25-hydroxyvitamin D3-1alpha-hydroxylase gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 12 |pages= 6988-93 |year= 1999 |pmid= 10359826 |doi= }}
*{{cite journal | author=Kitanaka S, Murayama A, Sakaki T, ''et al.'' |title=No enzyme activity of 25-hydroxyvitamin D3 1alpha-hydroxylase gene product in pseudovitamin D deficiency rickets, including that with mild clinical manifestation. |journal=J. Clin. Endocrinol. Metab. |volume=84 |issue= 11 |pages= 4111-7 |year= 1999 |pmid= 10566658 |doi= }}
*{{cite journal | author=Weinmann AS, Yan PS, Oberley MJ, ''et al.'' |title=Isolating human transcription factor targets by coupling chromatin immunoprecipitation and CpG island microarray analysis. |journal=Genes Dev. |volume=16 |issue= 2 |pages= 235-44 |year= 2002 |pmid= 11799066 |doi= 10.1101/gad.943102 }}
*{{cite journal | author=Pani MA, Regulla K, Segni M, ''et al.'' |title=Vitamin D 1alpha-hydroxylase (CYP1alpha) polymorphism in Graves' disease, Hashimoto's thyroiditis and type 1 diabetes mellitus. |journal=Eur. J. Endocrinol. |volume=146 |issue= 6 |pages= 777-81 |year= 2002 |pmid= 12039697 |doi= }}
*{{cite journal | author=Wang X, Zhang MY, Miller WL, Portale AA |title=Novel gene mutations in patients with 1alpha-hydroxylase deficiency that confer partial enzyme activity in vitro. |journal=J. Clin. Endocrinol. Metab. |volume=87 |issue= 6 |pages= 2424-30 |year= 2002 |pmid= 12050193 |doi= }}
*{{cite journal | author=Segersten U, Correa P, Hewison M, ''et al.'' |title=25-hydroxyvitamin D(3)-1alpha-hydroxylase expression in normal and pathological parathyroid glands. |journal=J. Clin. Endocrinol. Metab. |volume=87 |issue= 6 |pages= 2967-72 |year= 2002 |pmid= 12050281 |doi= }}
*{{cite journal | author=Zehnder D, Evans KN, Kilby MD, ''et al.'' |title=The ontogeny of 25-hydroxyvitamin D(3) 1alpha-hydroxylase expression in human placenta and decidua. |journal=Am. J. Pathol. |volume=161 |issue= 1 |pages= 105-14 |year= 2002 |pmid= 12107095 |doi= }}
*{{cite journal | author=Whitlatch LW, Young MV, Schwartz GG, ''et al.'' |title=25-Hydroxyvitamin D-1alpha-hydroxylase activity is diminished in human prostate cancer cells and is enhanced by gene transfer. |journal=J. Steroid Biochem. Mol. Biol. |volume=81 |issue= 2 |pages= 135-40 |year= 2002 |pmid= 12137802 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DNMT3B... {November 16, 2007 3:47:05 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 3:47:30 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_protein_box = yes
| update_summary = yes
| 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_DNMT3B_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1khc.
| PDB = {{PDB2|1khc}}
| Name = DNA (cytosine-5-)-methyltransferase 3 beta
| HGNCid = 2979
| Symbol = DNMT3B
| AltSymbols =; ICF; M.HsaIIIB
| OMIM = 602900
| ECnumber =
| Homologene = 56000
| MGIid = 1261819
| GeneAtlas_image1 = PBB_GE_DNMT3B_220668_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003886 |text = DNA (cytosine-5-)-methyltransferase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008168 |text = methyltransferase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0008326 |text = site-specific DNA-methyltransferase (cytosine-specific) activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005720 |text = nuclear heterochromatin}}
| Process = {{GNF_GO|id=GO:0006306 |text = DNA methylation}} {{GNF_GO|id=GO:0006349 |text = imprinting}} {{GNF_GO|id=GO:0031503 |text = protein complex localization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1789
| Hs_Ensembl = ENSG00000088305
| Hs_RefseqProtein = NP_008823
| Hs_RefseqmRNA = NM_006892
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 30813852
| Hs_GenLoc_end = 30860823
| Hs_Uniprot = Q9UBC3
| Mm_EntrezGene = 13436
| Mm_Ensembl = ENSMUSG00000027478
| Mm_RefseqmRNA = XM_001003158
| Mm_RefseqProtein = XP_001003158
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 153340894
| Mm_GenLoc_end = 153379171
| Mm_Uniprot = O88509
}}
}}
'''DNA (cytosine-5-)-methyltransferase 3 beta''', also known as '''DNMT3B''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DNMT3B DNA (cytosine-5-)-methyltransferase 3 beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1789| 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 = CpG methylation is an epigenetic modification that is important for embryonic development, imprinting, and X-chromosome inactivation. Studies in mice have demonstrated that DNA methylation is required for mammalian development. This gene encodes a DNA methyltransferase which is thought to function in de novo methylation, rather than maintenance methylation. The protein localizes primarily to the nucleus and its expression is developmentally regulated. Mutations in this gene cause the immunodeficiency-centromeric instability-facial anomalies (ICF) syndrome. Six alternatively spliced transcript variants have been described. The full length sequences of variants 4 and 5 have not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: DNMT3B DNA (cytosine-5-)-methyltransferase 3 beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1789| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wijmenga C, Hansen RS, Gimelli G, ''et al.'' |title=Genetic variation in ICF syndrome: evidence for genetic heterogeneity. |journal=Hum. Mutat. |volume=16 |issue= 6 |pages= 509-17 |year= 2001 |pmid= 11102980 |doi= 10.1002/1098-1004(200012)16:6<509::AID-HUMU8>3.0.CO;2-V }}
*{{cite journal | author=Okano M, Xie S, Li E |title=Cloning and characterization of a family of novel mammalian DNA (cytosine-5) methyltransferases. |journal=Nat. Genet. |volume=19 |issue= 3 |pages= 219-20 |year= 1998 |pmid= 9662389 |doi= 10.1038/890 }}
*{{cite journal | author=Robertson KD, Uzvolgyi E, Liang G, ''et al.'' |title=The human DNA methyltransferases (DNMTs) 1, 3a and 3b: coordinate mRNA expression in normal tissues and overexpression in tumors. |journal=Nucleic Acids Res. |volume=27 |issue= 11 |pages= 2291-8 |year= 1999 |pmid= 10325416 |doi= }}
*{{cite journal | author=Xie S, Wang Z, Okano M, ''et al.'' |title=Cloning, expression and chromosome locations of the human DNMT3 gene family. |journal=Gene |volume=236 |issue= 1 |pages= 87-95 |year= 1999 |pmid= 10433969 |doi= }}
*{{cite journal | author=Okano M, Bell DW, Haber DA, Li E |title=DNA methyltransferases Dnmt3a and Dnmt3b are essential for de novo methylation and mammalian development. |journal=Cell |volume=99 |issue= 3 |pages= 247-57 |year= 1999 |pmid= 10555141 |doi= }}
*{{cite journal | author=Hansen RS, Wijmenga C, Luo P, ''et al.'' |title=The DNMT3B DNA methyltransferase gene is mutated in the ICF immunodeficiency syndrome. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 25 |pages= 14412-7 |year= 2000 |pmid= 10588719 |doi= }}
*{{cite journal | author=Xu GL, Bestor TH, Bourc'his D, ''et al.'' |title=Chromosome instability and immunodeficiency syndrome caused by mutations in a DNA methyltransferase gene. |journal=Nature |volume=402 |issue= 6758 |pages= 187-91 |year= 2000 |pmid= 10647011 |doi= 10.1038/46052 }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
*{{cite journal | author=Fuks F, Burgers WA, Godin N, ''et al.'' |title=Dnmt3a binds deacetylases and is recruited by a sequence-specific repressor to silence transcription. |journal=EMBO J. |volume=20 |issue= 10 |pages= 2536-44 |year= 2001 |pmid= 11350943 |doi= 10.1093/emboj/20.10.2536 }}
*{{cite journal | author=Kang ES, Park CW, Chung JH |title=Dnmt3b, de novo DNA methyltransferase, interacts with SUMO-1 and Ubc9 through its N-terminal region and is subject to modification by SUMO-1. |journal=Biochem. Biophys. Res. Commun. |volume=289 |issue= 4 |pages= 862-8 |year= 2002 |pmid= 11735126 |doi= 10.1006/bbrc.2001.6057 }}
*{{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=Rhee I, Bachman KE, Park BH, ''et al.'' |title=DNMT1 and DNMT3b cooperate to silence genes in human cancer cells. |journal=Nature |volume=416 |issue= 6880 |pages= 552-6 |year= 2002 |pmid= 11932749 |doi= 10.1038/416552a }}
*{{cite journal | author=Hata K, Okano M, Lei H, Li E |title=Dnmt3L cooperates with the Dnmt3 family of de novo DNA methyltransferases to establish maternal imprints in mice. |journal=Development |volume=129 |issue= 8 |pages= 1983-93 |year= 2002 |pmid= 11934864 |doi= }}
*{{cite journal | author=Beaulieu N, Morin S, Chute IC, ''et al.'' |title=An essential role for DNA methyltransferase DNMT3B in cancer cell survival. |journal=J. Biol. Chem. |volume=277 |issue= 31 |pages= 28176-81 |year= 2002 |pmid= 12015329 |doi= 10.1074/jbc.M204734200 }}
*{{cite journal | author=Saito Y, Kanai Y, Sakamoto M, ''et al.'' |title=Overexpression of a splice variant of DNA methyltransferase 3b, DNMT3b4, associated with DNA hypomethylation on pericentromeric satellite regions during human hepatocarcinogenesis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 15 |pages= 10060-5 |year= 2002 |pmid= 12110732 |doi= 10.1073/pnas.152121799 }}
*{{cite journal | author=Kim GD, Ni J, Kelesoglu N, ''et al.'' |title=Co-operation and communication between the human maintenance and de novo DNA (cytosine-5) methyltransferases. |journal=EMBO J. |volume=21 |issue= 15 |pages= 4183-95 |year= 2002 |pmid= 12145218 |doi= }}
*{{cite journal | author=Deplus R, Brenner C, Burgers WA, ''et al.'' |title=Dnmt3L is a transcriptional repressor that recruits histone deacetylase. |journal=Nucleic Acids Res. |volume=30 |issue= 17 |pages= 3831-8 |year= 2002 |pmid= 12202768 |doi= }}
*{{cite journal | author=Shen H, Wang L, Spitz MR, ''et al.'' |title=A novel polymorphism in human cytosine DNA-methyltransferase-3B promoter is associated with an increased risk of lung cancer. |journal=Cancer Res. |volume=62 |issue= 17 |pages= 4992-5 |year= 2002 |pmid= 12208751 |doi= }}
*{{cite journal | author=Shirohzu H, Kubota T, Kumazawa A, ''et al.'' |title=Three novel DNMT3B mutations in Japanese patients with ICF syndrome. |journal=Am. J. Med. Genet. |volume=112 |issue= 1 |pages= 31-7 |year= 2003 |pmid= 12239717 |doi= 10.1002/ajmg.10658 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ENO1... {November 16, 2007 3:47:31 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 3:48:04 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Enolase 1, (alpha)
| HGNCid = 3350
| Symbol = ENO1
| AltSymbols =; ENO1L1; MBP-1; MPB1; NNE; PPH
| OMIM = 172430
| ECnumber =
| Homologene = 68183
| MGIid = 95393
| GeneAtlas_image1 = PBB_GE_ENO1_201231_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ENO1_217294_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003714 |text = transcription corepressor activity}} {{GNF_GO|id=GO:0004634 |text = phosphopyruvate hydratase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008243 |text = plasminogen activator activity}} {{GNF_GO|id=GO:0016829 |text = lyase activity}}
| Component = {{GNF_GO|id=GO:0000015 |text = phosphopyruvate hydratase complex}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006096 |text = glycolysis}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0030308 |text = negative regulation of cell growth}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2023
| Hs_Ensembl = ENSG00000074800
| Hs_RefseqProtein = NP_001419
| Hs_RefseqmRNA = NM_001428
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 8843648
| Hs_GenLoc_end = 8978713
| Hs_Uniprot = P06733
| Mm_EntrezGene = 13806
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_001006583
| Mm_RefseqProtein = XP_001006583
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Enolase 1, (alpha)''', also known as '''ENO1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ENO1 enolase 1, (alpha)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2023| 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 one of three enolase isoenzymes found in mammals; it encodes alpha-enolase, a homodimeric soluble enzyme, and also encodes a shorter monomeric structural lens protein, tau-crystallin. The two proteins are made from the same message. The full length protein, the isoenzyme, is found in the cytoplasm. The shorter protein is produced from an alternative translation start, is localized to the nucleus, and has been found to bind to an element in the c-myc promoter. A pseudogene has been identified that is located on the other arm of the same chromosome.<ref name="entrez">{{cite web | title = Entrez Gene: ENO1 enolase 1, (alpha)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2023| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Pancholi V |title=Multifunctional alpha-enolase: its role in diseases. |journal=Cell. Mol. Life Sci. |volume=58 |issue= 7 |pages= 902-20 |year= 2001 |pmid= 11497239 |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=Ray R, Miller DM |title=Cloning and characterization of a human c-myc promoter-binding protein. |journal=Mol. Cell. Biol. |volume=11 |issue= 4 |pages= 2154-61 |year= 1991 |pmid= 2005901 |doi= }}
*{{cite journal | author=Oliva D, Calì L, Feo S, Giallongo A |title=Complete structure of the human gene encoding neuron-specific enolase. |journal=Genomics |volume=10 |issue= 1 |pages= 157-65 |year= 1991 |pmid= 2045099 |doi= }}
*{{cite journal | author=Giallongo A, Oliva D, Calì L, ''et al.'' |title=Structure of the human gene for alpha-enolase. |journal=Eur. J. Biochem. |volume=190 |issue= 3 |pages= 567-73 |year= 1990 |pmid= 2373081 |doi= }}
*{{cite journal | author=Giallongo A, Feo S, Moore R, ''et al.'' |title=Molecular cloning and nucleotide sequence of a full-length cDNA for human alpha enolase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 18 |pages= 6741-5 |year= 1986 |pmid= 3529090 |doi= }}
*{{cite journal | author=Mohammad RM, Hamdan MY, al-Katib A |title=Induced expression of alpha-enolase in differentiated diffuse large cell lymphoma. |journal=Enzyme Protein |volume=48 |issue= 1 |pages= 37-44 |year= 1995 |pmid= 7787969 |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=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=Walter M, Berg H, Leidenberger FA, ''et al.'' |title=Autoreactive epitopes within the human alpha-enolase and their recognition by sera from patients with endometriosis. |journal=J. Autoimmun. |volume=8 |issue= 6 |pages= 931-45 |year= 1996 |pmid= 8824716 |doi= }}
*{{cite journal | author=Ray RB, Srinivas RV |title=Inhibition of human immunodeficiency virus type 1 replication by a cellular transcriptional factor MBP-1. |journal=J. Cell. Biochem. |volume=64 |issue= 4 |pages= 565-72 |year= 1997 |pmid= 9093905 |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=White RA, Adkison LR, Dowler LL, Ray RB |title=Chromosomal localization of the human gene encoding c-myc promoter-binding protein (MPB1) to chromosome 1p35-pter. |journal=Genomics |volume=39 |issue= 3 |pages= 406-8 |year= 1997 |pmid= 9119380 |doi= 10.1006/geno.1996.4499 }}
*{{cite journal | author=Ji H, Reid GE, Moritz RL, ''et al.'' |title=A two-dimensional gel database of human colon carcinoma proteins. |journal=Electrophoresis |volume=18 |issue= 3-4 |pages= 605-13 |year= 1997 |pmid= 9150948 |doi= 10.1002/elps.1150180344 }}
*{{cite journal | author=Arza B, Félez J, Lopez-Alemany R, ''et al.'' |title=Identification of an epitope of alpha-enolase (a candidate plasminogen receptor) by phage display. |journal=Thromb. Haemost. |volume=78 |issue= 3 |pages= 1097-103 |year= 1998 |pmid= 9308760 |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=Onyango P, Lubyova B, Gardellin P, ''et al.'' |title=Molecular cloning and expression analysis of five novel genes in chromosome 1p36. |journal=Genomics |volume=50 |issue= 2 |pages= 187-98 |year= 1998 |pmid= 9653645 |doi= 10.1006/geno.1997.5186 }}
*{{cite journal | author=White PS, Jensen SJ, Rajalingam V, ''et al.'' |title=Physical mapping of the CA6, ENO1, and SLC2A5 (GLUT5) genes and reassignment of SLC2A5 to 1p36.2. |journal=Cytogenet. Cell Genet. |volume=81 |issue= 1 |pages= 60-4 |year= 1998 |pmid= 9691177 |doi= }}
*{{cite journal | author=Adamus G, Amundson D, Seigel GM, Machnicki M |title=Anti-enolase-alpha autoantibodies in cancer-associated retinopathy: epitope mapping and cytotoxicity on retinal cells. |journal=J. Autoimmun. |volume=11 |issue= 6 |pages= 671-7 |year= 1999 |pmid= 9878089 |doi= 10.1006/jaut.1998.0239 }}
*{{cite journal | author=Ghosh AK, Steele R, Ray RB |title=Functional domains of c-myc promoter binding protein 1 involved in transcriptional repression and cell growth regulation. |journal=Mol. Cell. Biol. |volume=19 |issue= 4 |pages= 2880-6 |year= 1999 |pmid= 10082554 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GAB1... {November 16, 2007 3:48:04 PM PST}
- SEARCH REDIRECT: Control Box Found: GAB1 {November 16, 2007 3:48:33 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 3:48:36 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 3:48:36 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 3:48:36 PM PST}
- UPDATED: Updated protein page: GAB1 {November 16, 2007 3:48:42 PM PST}
- INFO: Beginning work on GATA3... {November 16, 2007 3:48:42 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 3:49:16 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = GATA binding protein 3
| HGNCid = 4172
| Symbol = GATA3
| AltSymbols =; HDR; MGC2346; MGC5199; MGC5445
| OMIM = 131320
| ECnumber =
| Homologene = 1550
| MGIid = 95663
| GeneAtlas_image1 = PBB_GE_GATA3_209604_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_GATA3_209602_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_GATA3_209603_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006952 |text = defense response}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0009653 |text = anatomical structure morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2625
| Hs_Ensembl = ENSG00000107485
| Hs_RefseqProtein = NP_001002295
| Hs_RefseqmRNA = NM_001002295
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 8136662
| Hs_GenLoc_end = 8157170
| Hs_Uniprot = P23771
| Mm_EntrezGene = 14462
| Mm_Ensembl = ENSMUSG00000015619
| Mm_RefseqmRNA = NM_008091
| Mm_RefseqProtein = NP_032117
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 9774921
| Mm_GenLoc_end = 9796453
| Mm_Uniprot = Q3TZD6
}}
}}
'''GATA binding protein 3''', also known as '''GATA3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GATA3 GATA binding protein 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2625| 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=Naylor MJ, Ormandy CJ |title=Gata-3 and mammary cell fate. |journal=Breast Cancer Res. |volume=9 |issue= 2 |pages= 302 |year= 2007 |pmid= 17381824 |doi= 10.1186/bcr1661 }}
*{{cite journal | author=Ho IC, Vorhees P, Marin N, ''et al.'' |title=Human GATA-3: a lineage-restricted transcription factor that regulates the expression of the T cell receptor alpha gene. |journal=EMBO J. |volume=10 |issue= 5 |pages= 1187-92 |year= 1991 |pmid= 1827068 |doi= }}
*{{cite journal | author=Marine J, Winoto A |title=The human enhancer-binding protein Gata3 binds to several T-cell receptor regulatory elements. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 16 |pages= 7284-8 |year= 1991 |pmid= 1871134 |doi= }}
*{{cite journal | author=Ko LJ, Yamamoto M, Leonard MW, ''et al.'' |title=Murine and human T-lymphocyte GATA-3 factors mediate transcription through a cis-regulatory element within the human T-cell receptor delta gene enhancer. |journal=Mol. Cell. Biol. |volume=11 |issue= 5 |pages= 2778-84 |year= 1991 |pmid= 2017177 |doi= }}
*{{cite journal | author=Joulin V, Bories D, Eléouet JF, ''et al.'' |title=A T-cell specific TCR delta DNA binding protein is a member of the human GATA family. |journal=EMBO J. |volume=10 |issue= 7 |pages= 1809-16 |year= 1991 |pmid= 2050118 |doi= }}
*{{cite journal | author=Siegel MD, Zhang DH, Ray P, Ray A |title=Activation of the interleukin-5 promoter by cAMP in murine EL-4 cells requires the GATA-3 and CLE0 elements. |journal=J. Biol. Chem. |volume=270 |issue= 41 |pages= 24548-55 |year= 1995 |pmid= 7592673 |doi= }}
*{{cite journal | author=Labastie MC, Bories D, Chabret C, ''et al.'' |title=Structure and expression of the human GATA3 gene. |journal=Genomics |volume=21 |issue= 1 |pages= 1-6 |year= 1994 |pmid= 8088776 |doi= 10.1006/geno.1994.1217 }}
*{{cite journal | author=Ono Y, Fukuhara N, Yoshie O |title=Transcriptional activity of TAL1 in T cell acute lymphoblastic leukemia (T-ALL) requires RBTN1 or -2 and induces TALLA1, a highly specific tumor marker of T-ALL. |journal=J. Biol. Chem. |volume=272 |issue= 7 |pages= 4576-81 |year= 1997 |pmid= 9020185 |doi= }}
*{{cite journal | author=Ono Y, Fukuhara N, Yoshie O |title=TAL1 and LIM-only proteins synergistically induce retinaldehyde dehydrogenase 2 expression in T-cell acute lymphoblastic leukemia by acting as cofactors for GATA3. |journal=Mol. Cell. Biol. |volume=18 |issue= 12 |pages= 6939-50 |year= 1998 |pmid= 9819382 |doi= }}
*{{cite journal | author=Yang GP, Ross DT, Kuang WW, ''et al.'' |title=Combining SSH and cDNA microarrays for rapid identification of differentially expressed genes. |journal=Nucleic Acids Res. |volume=27 |issue= 6 |pages= 1517-23 |year= 1999 |pmid= 10037815 |doi= }}
*{{cite journal | author=Blumenthal SG, Aichele G, Wirth T, ''et al.'' |title=Regulation of the human interleukin-5 promoter by Ets transcription factors. Ets1 and Ets2, but not Elf-1, cooperate with GATA3 and HTLV-I Tax1. |journal=J. Biol. Chem. |volume=274 |issue= 18 |pages= 12910-6 |year= 1999 |pmid= 10212281 |doi= }}
*{{cite journal | author=Van Esch H, Groenen P, Nesbit MA, ''et al.'' |title=GATA3 haplo-insufficiency causes human HDR syndrome. |journal=Nature |volume=406 |issue= 6794 |pages= 419-22 |year= 2000 |pmid= 10935639 |doi= 10.1038/35019088 }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
*{{cite journal | author=Muroya K, Hasegawa T, Ito Y, ''et al.'' |title=GATA3 abnormalities and the phenotypic spectrum of HDR syndrome. |journal=J. Med. Genet. |volume=38 |issue= 6 |pages= 374-80 |year= 2001 |pmid= 11389161 |doi= }}
*{{cite journal | author=Crawford SE, Qi C, Misra P, ''et al.'' |title=Defects of the heart, eye, and megakaryocytes in peroxisome proliferator activator receptor-binding protein (PBP) null embryos implicate GATA family of transcription factors. |journal=J. Biol. Chem. |volume=277 |issue= 5 |pages= 3585-92 |year= 2002 |pmid= 11724781 |doi= 10.1074/jbc.M107995200 }}
*{{cite journal | author=Kieffer LJ, Greally JM, Landres I, ''et al.'' |title=Identification of a candidate regulatory region in the human CD8 gene complex by colocalization of DNase I hypersensitive sites and matrix attachment regions which bind SATB1 and GATA-3. |journal=J. Immunol. |volume=168 |issue= 8 |pages= 3915-22 |year= 2002 |pmid= 11937547 |doi= }}
*{{cite journal | author=Asnagli H, Afkarian M, Murphy KM |title=Cutting edge: Identification of an alternative GATA-3 promoter directing tissue-specific gene expression in mouse and human. |journal=J. Immunol. |volume=168 |issue= 9 |pages= 4268-71 |year= 2002 |pmid= 11970965 |doi= }}
*{{cite journal | author=Steenbergen RD, OudeEngberink VE, Kramer D, ''et al.'' |title=Down-regulation of GATA-3 expression during human papillomavirus-mediated immortalization and cervical carcinogenesis. |journal=Am. J. Pathol. |volume=160 |issue= 6 |pages= 1945-51 |year= 2002 |pmid= 12057898 |doi= }}
*{{cite journal | author=Höfer T, Nathansen H, Löhning M, ''et al.'' |title=GATA-3 transcriptional imprinting in Th2 lymphocytes: a mathematical model. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 14 |pages= 9364-8 |year= 2002 |pmid= 12087127 |doi= 10.1073/pnas.142284699 }}
*{{cite journal | author=Karunaratne A, Hargrave M, Poh A, Yamada T |title=GATA proteins identify a novel ventral interneuron subclass in the developing chick spinal cord. |journal=Dev. Biol. |volume=249 |issue= 1 |pages= 30-43 |year= 2002 |pmid= 12217316 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GATA4... {November 16, 2007 3:49:16 PM PST}
- SEARCH REDIRECT: Control Box Found: GATA4 {November 16, 2007 3:49:43 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 3:49:47 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 3:49:47 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 3:49:47 PM PST}
- UPDATED: Updated protein page: GATA4 {November 16, 2007 3:49:53 PM PST}
- INFO: Beginning work on GPX1... {November 16, 2007 3:49:53 PM PST}
- SEARCH REDIRECT: Control Box Found: GPX1 {November 16, 2007 3:50:16 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 3:50:17 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 3:50:17 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 3:50:17 PM PST}
- UPDATED: Updated protein page: GPX1 {November 16, 2007 3:50:23 PM PST}
- INFO: Beginning work on ID2... {November 16, 2007 3:50:23 PM PST}
- SEARCH REDIRECT: Control Box Found: ID2 {November 16, 2007 3:51:03 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 3:51:05 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 3:51:05 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 3:51:05 PM PST}
- UPDATED: Updated protein page: ID2 {November 16, 2007 3:51:12 PM PST}
- INFO: Beginning work on IQGAP1... {November 16, 2007 3:56:13 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 3:56:55 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_IQGAP1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1x0h.
| PDB = {{PDB2|1x0h}}
| Name = IQ motif containing GTPase activating protein 1
| HGNCid = 6110
| Symbol = IQGAP1
| AltSymbols =; HUMORFA01; KIAA0051; SAR1; p195
| OMIM = 603379
| ECnumber =
| Homologene = 74514
| MGIid = 1352757
| GeneAtlas_image1 = PBB_GE_IQGAP1_210840_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_IQGAP1_200791_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_IQGAP1_213446_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005095 |text = GTPase inhibitor activity}} {{GNF_GO|id=GO:0005099 |text = Ras GTPase activator activity}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005884 |text = actin filament}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0046580 |text = negative regulation of Ras protein signal transduction}} {{GNF_GO|id=GO:0051056 |text = regulation of small GTPase mediated signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8826
| Hs_Ensembl = ENSG00000140575
| Hs_RefseqProtein = NP_003861
| Hs_RefseqmRNA = NM_003870
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 88732477
| Hs_GenLoc_end = 88846479
| Hs_Uniprot = P46940
| Mm_EntrezGene = 29875
| Mm_Ensembl = ENSMUSG00000030536
| Mm_RefseqmRNA = NM_016721
| Mm_RefseqProtein = NP_057930
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 80586294
| Mm_GenLoc_end = 80676807
| Mm_Uniprot = Q05CQ4
}}
}}
'''IQ motif containing GTPase activating protein 1''', also known as '''IQGAP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IQGAP1 IQ motif containing GTPase activating protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8826| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the IQGAP family. The protein contains four IQ domains, one calponin homology domain, one Ras-GAP domain and one WW domain. It interacts with components of the cytoskeleton, with cell adhesion molecules, and with several signaling molecules to regulate cell morphology and motility. Expression of the protein is upregulated by gene amplification in two gastric cancer cell lines.<ref name="entrez">{{cite web | title = Entrez Gene: IQGAP1 IQ motif containing GTPase activating protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8826| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tirnauer JS |title=A new cytoskeletal connection for APC: linked to actin through IQGAP. |journal=Dev. Cell |volume=7 |issue= 6 |pages= 778-80 |year= 2005 |pmid= 15572120 |doi= 10.1016/j.devcel.2004.11.012 }}
*{{cite journal | author=Nomura N, Nagase T, Miyajima N, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1. |journal=DNA Res. |volume=1 |issue= 5 |pages= 223-9 |year= 1995 |pmid= 7584044 |doi= }}
*{{cite journal | author=Weissbach L, Settleman J, Kalady MF, ''et al.'' |title=Identification of a human rasGAP-related protein containing calmodulin-binding motifs. |journal=J. Biol. Chem. |volume=269 |issue= 32 |pages= 20517-21 |year= 1994 |pmid= 8051149 |doi= }}
*{{cite journal | author=Hart MJ, Callow MG, Souza B, Polakis P |title=IQGAP1, a calmodulin-binding protein with a rasGAP-related domain, is a potential effector for cdc42Hs. |journal=EMBO J. |volume=15 |issue= 12 |pages= 2997-3005 |year= 1996 |pmid= 8670801 |doi= }}
*{{cite journal | author=McCallum SJ, Wu WJ, Cerione RA |title=Identification of a putative effector for Cdc42Hs with high sequence similarity to the RasGAP-related protein IQGAP1 and a Cdc42Hs binding partner with similarity to IQGAP2. |journal=J. Biol. Chem. |volume=271 |issue= 36 |pages= 21732-7 |year= 1996 |pmid= 8702968 |doi= }}
*{{cite journal | author=Brill S, Li S, Lyman CW, ''et al.'' |title=The Ras GTPase-activating-protein-related human protein IQGAP2 harbors a potential actin binding domain and interacts with calmodulin and Rho family GTPases. |journal=Mol. Cell. Biol. |volume=16 |issue= 9 |pages= 4869-78 |year= 1996 |pmid= 8756646 |doi= }}
*{{cite journal | author=Kuroda S, Fukata M, Kobayashi K, ''et al.'' |title=Identification of IQGAP as a putative target for the small GTPases, Cdc42 and Rac1. |journal=J. Biol. Chem. |volume=271 |issue= 38 |pages= 23363-7 |year= 1996 |pmid= 8798539 |doi= }}
*{{cite journal | author=Joyal JL, Annan RS, Ho YD, ''et al.'' |title=Calmodulin modulates the interaction between IQGAP1 and Cdc42. Identification of IQGAP1 by nanoelectrospray tandem mass spectrometry. |journal=J. Biol. Chem. |volume=272 |issue= 24 |pages= 15419-25 |year= 1997 |pmid= 9182573 |doi= }}
*{{cite journal | author=Bashour AM, Fullerton AT, Hart MJ, Bloom GS |title=IQGAP1, a Rac- and Cdc42-binding protein, directly binds and cross-links microfilaments. |journal=J. Cell Biol. |volume=137 |issue= 7 |pages= 1555-66 |year= 1997 |pmid= 9199170 |doi= }}
*{{cite journal | author=McCallum SJ, Erickson JW, Cerione RA |title=Characterization of the association of the actin-binding protein, IQGAP, and activated Cdc42 with Golgi membranes. |journal=J. Biol. Chem. |volume=273 |issue= 35 |pages= 22537-44 |year= 1998 |pmid= 9712880 |doi= }}
*{{cite journal | author=Li Z, Kim SH, Higgins JM, ''et al.'' |title=IQGAP1 and calmodulin modulate E-cadherin function. |journal=J. Biol. Chem. |volume=274 |issue= 53 |pages= 37885-92 |year= 2000 |pmid= 10608854 |doi= }}
*{{cite journal | author=Berryman M, Bretscher A |title=Identification of a novel member of the chloride intracellular channel gene family (CLIC5) that associates with the actin cytoskeleton of placental microvilli. |journal=Mol. Biol. Cell |volume=11 |issue= 5 |pages= 1509-21 |year= 2000 |pmid= 10793131 |doi= }}
*{{cite journal | author=Sugimoto N, Imoto I, Fukuda Y, ''et al.'' |title=IQGAP1, a negative regulator of cell-cell adhesion, is upregulated by gene amplification at 15q26 in gastric cancer cell lines HSC39 and 40A. |journal=J. Hum. Genet. |volume=46 |issue= 1 |pages= 21-5 |year= 2001 |pmid= 11289714 |doi= }}
*{{cite journal | author=Briggs MW, Li Z, Sacks DB |title=IQGAP1-mediated stimulation of transcriptional co-activation by beta-catenin is modulated by calmodulin. |journal=J. Biol. Chem. |volume=277 |issue= 9 |pages= 7453-65 |year= 2002 |pmid= 11734550 |doi= 10.1074/jbc.M104315200 }}
*{{cite journal | author=Nabeshima K, Shimao Y, Inoue T, Koono M |title=Immunohistochemical analysis of IQGAP1 expression in human colorectal carcinomas: its overexpression in carcinomas and association with invasion fronts. |journal=Cancer Lett. |volume=176 |issue= 1 |pages= 101-9 |year= 2002 |pmid= 11790459 |doi= }}
*{{cite journal | author=Mateer SC, McDaniel AE, Nicolas V, ''et al.'' |title=The mechanism for regulation of the F-actin binding activity of IQGAP1 by calcium/calmodulin. |journal=J. Biol. Chem. |volume=277 |issue= 14 |pages= 12324-33 |year= 2002 |pmid= 11809768 |doi= 10.1074/jbc.M109535200 }}
*{{cite journal | author=Swart-Mataraza JM, Li Z, Sacks DB |title=IQGAP1 is a component of Cdc42 signaling to the cytoskeleton. |journal=J. Biol. Chem. |volume=277 |issue= 27 |pages= 24753-63 |year= 2002 |pmid= 11948177 |doi= 10.1074/jbc.M111165200 }}
*{{cite journal | author=Fukata M, Watanabe T, Noritake J, ''et al.'' |title=Rac1 and Cdc42 capture microtubules through IQGAP1 and CLIP-170. |journal=Cell |volume=109 |issue= 7 |pages= 873-85 |year= 2002 |pmid= 12110184 |doi= }}
*{{cite journal | author=Mbele GO, Deloulme JC, Gentil BJ, ''et al.'' |title=The zinc- and calcium-binding S100B interacts and co-localizes with IQGAP1 during dynamic rearrangement of cell membranes. |journal=J. Biol. Chem. |volume=277 |issue= 51 |pages= 49998-50007 |year= 2003 |pmid= 12377780 |doi= 10.1074/jbc.M205363200 }}
*{{cite journal | author=Li Z, Sacks DB |title=Elucidation of the interaction of calmodulin with the IQ motifs of IQGAP1. |journal=J. Biol. Chem. |volume=278 |issue= 6 |pages= 4347-52 |year= 2003 |pmid= 12446675 |doi= 10.1074/jbc.M208579200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KRT1... {November 16, 2007 3:51:12 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 3:51:38 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Keratin 1 (epidermolytic hyperkeratosis)
| HGNCid = 6412
| Symbol = KRT1
| AltSymbols =; CK1; EHK1; K1; KRT1A
| OMIM = 139350
| ECnumber =
| Homologene = 38146
| MGIid = 96698
| GeneAtlas_image1 = PBB_GE_KRT1_205900_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005529 |text = sugar binding}}
| Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005882 |text = intermediate filament}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0001867 |text = complement activation, lectin pathway}} {{GNF_GO|id=GO:0006979 |text = response to oxidative stress}} {{GNF_GO|id=GO:0008544 |text = epidermis development}} {{GNF_GO|id=GO:0042730 |text = fibrinolysis}} {{GNF_GO|id=GO:0045765 |text = regulation of angiogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3848
| Hs_Ensembl = ENSG00000167768
| Hs_RefseqProtein = NP_006112
| Hs_RefseqmRNA = NM_006121
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 51354719
| Hs_GenLoc_end = 51360446
| Hs_Uniprot = P04264
| Mm_EntrezGene = 16678
| Mm_Ensembl = ENSMUSG00000046834
| Mm_RefseqmRNA = NM_008473
| Mm_RefseqProtein = NP_032499
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 101673462
| Mm_GenLoc_end = 101678828
| Mm_Uniprot = P04104
}}
}}
'''Keratin 1 (epidermolytic hyperkeratosis)''', also known as '''KRT1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KRT1 keratin 1 (epidermolytic hyperkeratosis)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3848| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the keratin gene family. The type II cytokeratins consist of basic or neutral proteins which are arranged in pairs of heterotypic keratin chains coexpressed during differentiation of simple and stratified epithelial tissues. This type II cytokeratin is specifically expressed in the spinous and granular layers of the epidermis with family member KRT10 and mutations in these genes have been associated with bullous congenital ichthyosiform erythroderma. The type II cytokeratins are clustered in a region of chromosome 12q12-q13.<ref name="entrez">{{cite web | title = Entrez Gene: KRT1 keratin 1 (epidermolytic hyperkeratosis)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3848| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Whittock NV, Ashton GH, Griffiths WA, ''et al.'' |title=New mutations in keratin 1 that cause bullous congenital ichthyosiform erythroderma and keratin 2e that cause ichthyosis bullosa of Siemens. |journal=Br. J. Dermatol. |volume=145 |issue= 2 |pages= 330-5 |year= 2001 |pmid= 11531804 |doi= }}
*{{cite journal | author=Langbein L, Schweizer J |title=Keratins of the human hair follicle. |journal=Int. Rev. Cytol. |volume=243 |issue= |pages= 1-78 |year= 2005 |pmid= 15797458 |doi= 10.1016/S0074-7696(05)43001-6 }}
*{{cite journal | author=Korge BP, Compton JG, Steinert PM, Mischke D |title=The two size alleles of human keratin 1 are due to a deletion in the glycine-rich carboxyl-terminal V2 subdomain. |journal=J. Invest. Dermatol. |volume=99 |issue= 6 |pages= 697-702 |year= 1993 |pmid= 1281859 |doi= }}
*{{cite journal | author=Compton JG, DiGiovanna JJ, Santucci SK, ''et al.'' |title=Linkage of epidermolytic hyperkeratosis to the type II keratin gene cluster on chromosome 12q. |journal=Nat. Genet. |volume=1 |issue= 4 |pages= 301-5 |year= 1993 |pmid= 1284546 |doi= 10.1038/ng0792-301 }}
*{{cite journal | author=Rothnagel JA, Dominey AM, Dempsey LD, ''et al.'' |title=Mutations in the rod domains of keratins 1 and 10 in epidermolytic hyperkeratosis. |journal=Science |volume=257 |issue= 5073 |pages= 1128-30 |year= 1992 |pmid= 1380725 |doi= }}
*{{cite journal | author=Chipev CC, Korge BP, Markova N, ''et al.'' |title=A leucine----proline mutation in the H1 subdomain of keratin 1 causes epidermolytic hyperkeratosis. |journal=Cell |volume=70 |issue= 5 |pages= 821-8 |year= 1992 |pmid= 1381288 |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=Mansbridge JN, Hanawalt PC |title=Role of transforming growth factor beta in the maturation of human epidermal keratinocytes. |journal=J. Invest. Dermatol. |volume=90 |issue= 3 |pages= 336-41 |year= 1988 |pmid= 2450142 |doi= }}
*{{cite journal | author=Lessin SR, Huebner K, Isobe M, ''et al.'' |title=Chromosomal mapping of human keratin genes: evidence of non-linkage. |journal=J. Invest. Dermatol. |volume=91 |issue= 6 |pages= 572-8 |year= 1989 |pmid= 2461420 |doi= }}
*{{cite journal | author=Popescu NC, Bowden PE, DiPaolo JA |title=Two type II keratin genes are localized on human chromosome 12. |journal=Hum. Genet. |volume=82 |issue= 2 |pages= 109-12 |year= 1989 |pmid= 2470667 |doi= }}
*{{cite journal | author=Johnson LD, Idler WW, Zhou XM, ''et al.'' |title=Structure of a gene for the human epidermal 67-kDa keratin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 7 |pages= 1896-900 |year= 1985 |pmid= 2580302 |doi= }}
*{{cite journal | author=Steinert PM, Parry DA, Idler WW, ''et al.'' |title=Amino acid sequences of mouse and human epidermal type II keratins of Mr 67,000 provide a systematic basis for the structural and functional diversity of the end domains of keratin intermediate filament subunits. |journal=J. Biol. Chem. |volume=260 |issue= 11 |pages= 7142-9 |year= 1985 |pmid= 2581964 |doi= }}
*{{cite journal | author=Yang JM, Chipev CC, DiGiovanna JJ, ''et al.'' |title=Mutations in the H1 and 1A domains in the keratin 1 gene in epidermolytic hyperkeratosis. |journal=J. Invest. Dermatol. |volume=102 |issue= 1 |pages= 17-23 |year= 1994 |pmid= 7507151 |doi= }}
*{{cite journal | author=McLean WH, Eady RA, Dopping-Hepenstal PJ, ''et al.'' |title=Mutations in the rod 1A domain of keratins 1 and 10 in bullous congenital ichthyosiform erythroderma (BCIE). |journal=J. Invest. Dermatol. |volume=102 |issue= 1 |pages= 24-30 |year= 1994 |pmid= 7507152 |doi= }}
*{{cite journal | author=Syder AJ, Yu QC, Paller AS, ''et al.'' |title=Genetic mutations in the K1 and K10 genes of patients with epidermolytic hyperkeratosis. Correlation between location and disease severity. |journal=J. Clin. Invest. |volume=93 |issue= 4 |pages= 1533-42 |year= 1994 |pmid= 7512983 |doi= }}
*{{cite journal | author=Kimonis V, DiGiovanna JJ, Yang JM, ''et al.'' |title=A mutation in the V1 end domain of keratin 1 in non-epidermolytic palmar-plantar keratoderma. |journal=J. Invest. Dermatol. |volume=103 |issue= 6 |pages= 764-9 |year= 1995 |pmid= 7528239 |doi= }}
*{{cite journal | author=Yoon SJ, LeBlanc-Straceski J, Ward D, ''et al.'' |title=Organization of the human keratin type II gene cluster at 12q13. |journal=Genomics |volume=24 |issue= 3 |pages= 502-8 |year= 1995 |pmid= 7536183 |doi= 10.1006/geno.1994.1659 }}
*{{cite journal | author=Peehl DM, Wong ST, Stamey TA |title=Vitamin A regulates proliferation and differentiation of human prostatic epithelial cells. |journal=Prostate |volume=23 |issue= 1 |pages= 69-78 |year= 1993 |pmid= 7687781 |doi= }}
*{{cite journal | author=Senshu T, Kan S, Ogawa H, ''et al.'' |title=Preferential deimination of keratin K1 and filaggrin during the terminal differentiation of human epidermis. |journal=Biochem. Biophys. Res. Commun. |volume=225 |issue= 3 |pages= 712-9 |year= 1996 |pmid= 8780679 |doi= 10.1006/bbrc.1996.1240 }}
*{{cite journal | author=Steinert PM, Marekov LN |title=Direct evidence that involucrin is a major early isopeptide cross-linked component of the keratinocyte cornified cell envelope. |journal=J. Biol. Chem. |volume=272 |issue= 3 |pages= 2021-30 |year= 1997 |pmid= 8999895 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PIAS1... {November 16, 2007 3:55:35 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 3:56:13 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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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_PIAS1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1v66.
| PDB = {{PDB2|1v66}}
| Name = Protein inhibitor of activated STAT, 1
| HGNCid = 2752
| Symbol = PIAS1
| AltSymbols =; GBP; DDXBP1; GU/RH-II; MGC141878; MGC141879; ZMIZ3
| OMIM = 603566
| ECnumber =
| Homologene = 22953
| MGIid = 1913125
| GeneAtlas_image1 = PBB_GE_PIAS1_217864_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0003714 |text = transcription corepressor activity}} {{GNF_GO|id=GO:0004004 |text = ATP-dependent RNA helicase activity}} {{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}} {{GNF_GO|id=GO:0050681 |text = androgen receptor binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007259 |text = JAK-STAT cascade}} {{GNF_GO|id=GO:0030521 |text = androgen receptor signaling pathway}} {{GNF_GO|id=GO:0045893 |text = positive regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8554
| Hs_Ensembl = ENSG00000033800
| Hs_RefseqProtein = NP_057250
| Hs_RefseqmRNA = NM_016166
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 66165695
| Hs_GenLoc_end = 66267392
| Hs_Uniprot = O75925
| Mm_EntrezGene = 56469
| Mm_Ensembl = ENSMUSG00000032405
| Mm_RefseqmRNA = NM_019663
| Mm_RefseqProtein = NP_062637
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 62679132
| Mm_GenLoc_end = 62778885
| Mm_Uniprot = Q2M4G9
}}
}}
'''Protein inhibitor of activated STAT, 1''', also known as '''PIAS1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PIAS1 protein inhibitor of activated STAT, 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8554| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the mammalian PIAS [protein inhibitor of activated STAT-1 (signal transducer and activator of transcription-1)] family. This member contains a putative zinc-binding motif and a highly acidic region. It inhibits STAT1-mediated gene activation and the DNA binding activity, binds to Gu protein/RNA helicase II/DEAD box polypeptide 21, and interacts with androgen receptor (AR). It functions in testis as a nuclear receptor transcriptional coregulator and may have a role in AR initiation and maintenance of spermatogenesis.<ref name="entrez">{{cite web | title = Entrez Gene: PIAS1 protein inhibitor of activated STAT, 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8554| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Valdez BC, Henning D, Perlaky L, ''et al.'' |title=Cloning and characterization of Gu/RH-II binding protein. |journal=Biochem. Biophys. Res. Commun. |volume=234 |issue= 2 |pages= 335-40 |year= 1997 |pmid= 9177271 |doi= 10.1006/bbrc.1997.6642 }}
*{{cite journal | author=Liu B, Liao J, Rao X, ''et al.'' |title=Inhibition of Stat1-mediated gene activation by PIAS1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 18 |pages= 10626-31 |year= 1998 |pmid= 9724754 |doi= }}
*{{cite journal | author=Tan J, Hall SH, Hamil KG, ''et al.'' |title=Protein inhibitor of activated STAT-1 (signal transducer and activator of transcription-1) is a nuclear receptor coregulator expressed in human testis. |journal=Mol. Endocrinol. |volume=14 |issue= 1 |pages= 14-26 |year= 2000 |pmid= 10628744 |doi= }}
*{{cite journal | author=Liao J, Fu Y, Shuai K |title=Distinct roles of the NH2- and COOH-terminal domains of the protein inhibitor of activated signal transducer and activator of transcription (STAT) 1 (PIAS1) in cytokine-induced PIAS1-Stat1 interaction. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 10 |pages= 5267-72 |year= 2000 |pmid= 10805787 |doi= }}
*{{cite journal | author=Kotaja N, Aittomäki S, Silvennoinen O, ''et al.'' |title=ARIP3 (androgen receptor-interacting protein 3) and other PIAS (protein inhibitor of activated STAT) proteins differ in their ability to modulate steroid receptor-dependent transcriptional activation. |journal=Mol. Endocrinol. |volume=14 |issue= 12 |pages= 1986-2000 |year= 2001 |pmid= 11117529 |doi= }}
*{{cite journal | author=Gross M, Liu B, Tan J, ''et al.'' |title=Distinct effects of PIAS proteins on androgen-mediated gene activation in prostate cancer cells. |journal=Oncogene |volume=20 |issue= 29 |pages= 3880-7 |year= 2001 |pmid= 11439351 |doi= 10.1038/sj.onc.1204489 }}
*{{cite journal | author=Liu B, Shuai K |title=Induction of apoptosis by protein inhibitor of activated Stat1 through c-Jun NH2-terminal kinase activation. |journal=J. Biol. Chem. |volume=276 |issue= 39 |pages= 36624-31 |year= 2001 |pmid= 11451946 |doi= 10.1074/jbc.M101085200 }}
*{{cite journal | author=Kahyo T, Nishida T, Yasuda H |title=Involvement of PIAS1 in the sumoylation of tumor suppressor p53. |journal=Mol. Cell |volume=8 |issue= 3 |pages= 713-8 |year= 2001 |pmid= 11583632 |doi= }}
*{{cite journal | author=Weiskirchen R, Moser M, Weiskirchen S, ''et al.'' |title=LIM-domain protein cysteine- and glycine-rich protein 2 (CRP2) is a novel marker of hepatic stellate cells and binding partner of the protein inhibitor of activated STAT1. |journal=Biochem. J. |volume=359 |issue= Pt 3 |pages= 485-96 |year= 2001 |pmid= 11672422 |doi= }}
*{{cite journal | author=Megidish T, Xu JH, Xu CW |title=Activation of p53 by protein inhibitor of activated Stat1 (PIAS1). |journal=J. Biol. Chem. |volume=277 |issue= 10 |pages= 8255-9 |year= 2002 |pmid= 11788578 |doi= 10.1074/jbc.C200001200 }}
*{{cite journal | author=Schmidt D, Müller S |title=Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 5 |pages= 2872-7 |year= 2002 |pmid= 11867732 |doi= 10.1073/pnas.052559499 }}
*{{cite journal | author=Tan JA, Hall SH, Hamil KG, ''et al.'' |title=Protein inhibitors of activated STAT resemble scaffold attachment factors and function as interacting nuclear receptor coregulators. |journal=J. Biol. Chem. |volume=277 |issue= 19 |pages= 16993-7001 |year= 2002 |pmid= 11877418 |doi= 10.1074/jbc.M109217200 }}
*{{cite journal | author=Nishida T, Yasuda H |title=PIAS1 and PIASxalpha function as SUMO-E3 ligases toward androgen receptor and repress androgen receptor-dependent transcription. |journal=J. Biol. Chem. |volume=277 |issue= 44 |pages= 41311-7 |year= 2003 |pmid= 12177000 |doi= 10.1074/jbc.M206741200 }}
*{{cite journal | author=Rui HL, Fan E, Zhou HM, ''et al.'' |title=SUMO-1 modification of the C-terminal KVEKVD of Axin is required for JNK activation but has no effect on Wnt signaling. |journal=J. Biol. Chem. |volume=277 |issue= 45 |pages= 42981-6 |year= 2003 |pmid= 12223491 |doi= 10.1074/jbc.M208099200 }}
*{{cite journal | author=Sapetschnig A, Rischitor G, Braun H, ''et al.'' |title=Transcription factor Sp3 is silenced through SUMO modification by PIAS1. |journal=EMBO J. |volume=21 |issue= 19 |pages= 5206-15 |year= 2002 |pmid= 12356736 |doi= }}
*{{cite journal | author=Miyauchi Y, Yogosawa S, Honda R, ''et al.'' |title=Sumoylation of Mdm2 by protein inhibitor of activated STAT (PIAS) and RanBP2 enzymes. |journal=J. Biol. Chem. |volume=277 |issue= 51 |pages= 50131-6 |year= 2003 |pmid= 12393906 |doi= 10.1074/jbc.M208319200 }}
*{{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=Ungureanu D, Vanhatupa S, Kotaja N, ''et al.'' |title=PIAS proteins promote SUMO-1 conjugation to STAT1. |journal=Blood |volume=102 |issue= 9 |pages= 3311-3 |year= 2004 |pmid= 12855578 |doi= 10.1182/blood-2002-12-3816 }}
*{{cite journal | author=Kadaré G, Toutant M, Formstecher E, ''et al.'' |title=PIAS1-mediated sumoylation of focal adhesion kinase activates its autophosphorylation. |journal=J. Biol. Chem. |volume=278 |issue= 48 |pages= 47434-40 |year= 2004 |pmid= 14500712 |doi= 10.1074/jbc.M308562200 }}
*{{cite journal | author=Tallec LP, Kirsh O, Lecomte MC, ''et al.'' |title=Protein inhibitor of activated signal transducer and activator of transcription 1 interacts with the N-terminal domain of mineralocorticoid receptor and represses its transcriptional activity: implication of small ubiquitin-related modifier 1 modification. |journal=Mol. Endocrinol. |volume=17 |issue= 12 |pages= 2529-42 |year= 2004 |pmid= 14500761 |doi= 10.1210/me.2003-0299 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PPARBP... {November 16, 2007 3:51:38 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 3:52:32 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = PPAR binding protein
| HGNCid = 9234
| Symbol = PPARBP
| AltSymbols =; PBP; CRSP1; CRSP200; DRIP205; DRIP230; MED1; MGC71488; PPARGBP; RB18A; TRAP220; TRIP2
| OMIM = 604311
| ECnumber =
| Homologene = 21002
| MGIid = 1100846
| GeneAtlas_image1 = PBB_GE_PPARBP_203497_at_tn.png
| GeneAtlas_image2 = PBB_GE_PPARBP_203496_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003682 |text = chromatin binding}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016455 |text = RNA polymerase II transcription mediator activity}} {{GNF_GO|id=GO:0030374 |text = ligand-dependent nuclear receptor transcription coactivator activity}} {{GNF_GO|id=GO:0031177 |text = phosphopantetheine binding}} {{GNF_GO|id=GO:0042809 |text = vitamin D receptor binding}} {{GNF_GO|id=GO:0046966 |text = thyroid hormone receptor binding}}
| Component = {{GNF_GO|id=GO:0000119 |text = mediator complex}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0001701 |text = in utero embryonic development}} {{GNF_GO|id=GO:0001889 |text = liver development}} {{GNF_GO|id=GO:0001892 |text = embryonic placenta development}} {{GNF_GO|id=GO:0006260 |text = DNA replication}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006367 |text = transcription initiation from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006590 |text = thyroid hormone generation}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007420 |text = brain development}} {{GNF_GO|id=GO:0030521 |text = androgen receptor signaling pathway}} {{GNF_GO|id=GO:0035050 |text = embryonic heart tube development}} {{GNF_GO|id=GO:0035116 |text = embryonic hindlimb morphogenesis}} {{GNF_GO|id=GO:0035162 |text = embryonic hemopoiesis}} {{GNF_GO|id=GO:0045444 |text = fat cell differentiation}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5469
| Hs_Ensembl = ENSG00000125686
| Hs_RefseqProtein = NP_004765
| Hs_RefseqmRNA = NM_004774
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 34816380
| Hs_GenLoc_end = 34861030
| Hs_Uniprot = Q15648
| Mm_EntrezGene = 19014
| Mm_Ensembl = ENSMUSG00000018160
| Mm_RefseqmRNA = NM_001080118
| Mm_RefseqProtein = NP_001073587
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 97968244
| Mm_GenLoc_end = 98009350
| Mm_Uniprot = Q925J9
}}
}}
'''PPAR binding protein''', also known as '''PPARBP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PPARBP PPAR binding protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5469| 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 activation of gene transcription is a multistep process that is triggered by factors that recognize transcriptional enhancer sites in DNA. These factors work with co-activators to direct transcriptional initiation by the RNA polymerase II apparatus. The protein encoded by this gene is a subunit of the CRSP (cofactor required for SP1 activation) complex, which, along with TFIID, is required for efficient activation by SP1. This protein is also a component of other multisubunit complexes e.g. thyroid hormone receptor-(TR-) associated proteins which interact with TR and facilitate TR function on DNA templates in conjunction with initiation factors and cofactors. It also regulates p53-dependent apoptosis and it is essential for adipogenesis. This protein is known to have the ability to self-oligomerize.<ref name="entrez">{{cite web | title = Entrez Gene: PPARBP PPAR binding protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5469| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lee JW, Choi HS, Gyuris J, ''et al.'' |title=Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor. |journal=Mol. Endocrinol. |volume=9 |issue= 2 |pages= 243-54 |year= 1995 |pmid= 7776974 |doi= }}
*{{cite journal | author=Fondell JD, Ge H, Roeder RG |title=Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 16 |pages= 8329-33 |year= 1996 |pmid= 8710870 |doi= }}
*{{cite journal | author=Zhu Y, Qi C, Jain S, ''et al.'' |title=Isolation and characterization of PBP, a protein that interacts with peroxisome proliferator-activated receptor. |journal=J. Biol. Chem. |volume=272 |issue= 41 |pages= 25500-6 |year= 1997 |pmid= 9325263 |doi= }}
*{{cite journal | author=Drané P, Barel M, Balbo M, Frade R |title=Identification of RB18A, a 205 kDa new p53 regulatory protein which shares antigenic and functional properties with p53. |journal=Oncogene |volume=15 |issue= 25 |pages= 3013-24 |year= 1998 |pmid= 9444950 |doi= 10.1038/sj.onc.1201492 }}
*{{cite journal | author=Yuan CX, Ito M, Fondell JD, ''et al.'' |title=The TRAP220 component of a thyroid hormone receptor- associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 14 |pages= 7939-44 |year= 1998 |pmid= 9653119 |doi= }}
*{{cite journal | author=Ryu S, Zhou S, Ladurner AG, Tjian R |title=The transcriptional cofactor complex CRSP is required for activity of the enhancer-binding protein Sp1. |journal=Nature |volume=397 |issue= 6718 |pages= 446-50 |year= 1999 |pmid= 9989412 |doi= 10.1038/17141 }}
*{{cite journal | author=Gu W, Malik S, Ito M, ''et al.'' |title=A novel human SRB/MED-containing cofactor complex, SMCC, involved in transcription regulation. |journal=Mol. Cell |volume=3 |issue= 1 |pages= 97-108 |year= 1999 |pmid= 10024883 |doi= }}
*{{cite journal | author=Ito M, Yuan CX, Malik S, ''et al.'' |title=Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators. |journal=Mol. Cell |volume=3 |issue= 3 |pages= 361-70 |year= 1999 |pmid= 10198638 |doi= }}
*{{cite journal | author=Rachez C, Lemon BD, Suldan Z, ''et al.'' |title=Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex. |journal=Nature |volume=398 |issue= 6730 |pages= 824-8 |year= 1999 |pmid= 10235266 |doi= 10.1038/19783 }}
*{{cite journal | author=Näär AM, Beaurang PA, Zhou S, ''et al.'' |title=Composite co-activator ARC mediates chromatin-directed transcriptional activation. |journal=Nature |volume=398 |issue= 6730 |pages= 828-32 |year= 1999 |pmid= 10235267 |doi= 10.1038/19789 }}
*{{cite journal | author=Atkins GB, Hu X, Guenther MG, ''et al.'' |title=Coactivators for the orphan nuclear receptor RORalpha. |journal=Mol. Endocrinol. |volume=13 |issue= 9 |pages= 1550-7 |year= 1999 |pmid= 10478845 |doi= }}
*{{cite journal | author=Zhu Y, Qi C, Jain S, ''et al.'' |title=Amplification and overexpression of peroxisome proliferator-activated receptor binding protein (PBP/PPARBP) gene in breast cancer. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 19 |pages= 10848-53 |year= 1999 |pmid= 10485914 |doi= }}
*{{cite journal | author=Rachez C, Gamble M, Chang CP, ''et al.'' |title=The DRIP complex and SRC-1/p160 coactivators share similar nuclear receptor binding determinants but constitute functionally distinct complexes. |journal=Mol. Cell. Biol. |volume=20 |issue= 8 |pages= 2718-26 |year= 2000 |pmid= 10733574 |doi= }}
*{{cite journal | author=Frade R, Balbo M, Barel M |title=RB18A, whose gene is localized on chromosome 17q12-q21.1, regulates in vivo p53 transactivating activity. |journal=Cancer Res. |volume=60 |issue= 23 |pages= 6585-9 |year= 2001 |pmid= 11118038 |doi= }}
*{{cite journal | author=Zilliacus J, Holter E, Wakui H, ''et al.'' |title=Regulation of glucocorticoid receptor activity by 14--3-3-dependent intracellular relocalization of the corepressor RIP140. |journal=Mol. Endocrinol. |volume=15 |issue= 4 |pages= 501-11 |year= 2001 |pmid= 11266503 |doi= }}
*{{cite journal | author=Crawford SE, Qi C, Misra P, ''et al.'' |title=Defects of the heart, eye, and megakaryocytes in peroxisome proliferator activator receptor-binding protein (PBP) null embryos implicate GATA family of transcription factors. |journal=J. Biol. Chem. |volume=277 |issue= 5 |pages= 3585-92 |year= 2002 |pmid= 11724781 |doi= 10.1074/jbc.M107995200 }}
*{{cite journal | author=Frade R, Balbo M, Barel M |title=RB18A regulates p53-dependent apoptosis. |journal=Oncogene |volume=21 |issue= 6 |pages= 861-6 |year= 2002 |pmid= 11840331 |doi= 10.1038/sj.onc.1205177 }}
*{{cite journal | author=Kang YK, Guermah M, Yuan CX, Roeder RG |title=The TRAP/Mediator coactivator complex interacts directly with estrogen receptors alpha and beta through the TRAP220 subunit and directly enhances estrogen receptor function in vitro. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 5 |pages= 2642-7 |year= 2002 |pmid= 11867769 |doi= 10.1073/pnas.261715899 }}
*{{cite journal | author=Misra P, Qi C, Yu S, ''et al.'' |title=Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation. |journal=J. Biol. Chem. |volume=277 |issue= 22 |pages= 20011-9 |year= 2002 |pmid= 11912212 |doi= 10.1074/jbc.M201739200 }}
*{{cite journal | author=Ge K, Guermah M, Yuan CX, ''et al.'' |title=Transcription coactivator TRAP220 is required for PPAR gamma 2-stimulated adipogenesis. |journal=Nature |volume=417 |issue= 6888 |pages= 563-7 |year= 2002 |pmid= 12037571 |doi= 10.1038/417563a }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SLPI... {November 16, 2007 3:52:33 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 3:53:22 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Secretory leukocyte peptidase inhibitor
| HGNCid = 11092
| Symbol = SLPI
| AltSymbols =; ALK1; ALP; MPI; BLPI; HUSI; HUSI-I; WAP4; WFDC4
| OMIM = 107285
| ECnumber =
| Homologene = 2305
| MGIid = 109297
| GeneAtlas_image1 = PBB_GE_SLPI_203021_at_tn.png
| Function = {{GNF_GO|id=GO:0004867 |text = serine-type endopeptidase inhibitor activity}}
| Component =
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6590
| Hs_Ensembl = ENSG00000124107
| Hs_RefseqProtein = NP_003055
| Hs_RefseqmRNA = NM_003064
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 43314293
| Hs_GenLoc_end = 43316620
| Hs_Uniprot = P03973
| Mm_EntrezGene = 20568
| Mm_Ensembl = ENSMUSG00000017002
| Mm_RefseqmRNA = NM_011414
| Mm_RefseqProtein = NP_035544
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 164045509
| Mm_GenLoc_end = 164064151
| Mm_Uniprot = Q548X8
}}
}}
'''Secretory leukocyte peptidase inhibitor''', also known as '''SLPI''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SLPI secretory leukocyte peptidase inhibitor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6590| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a secreted inhibitor which protects epithelial tissues from serine proteases. It is found in various secretions including seminal plasma, cervical mucus, and bronchial secretions, and has affinity for trypsin, leukocyte elastase, and cathepsin G. Its inhibitory effect contributes to the immune response by protecting epithelial surfaces from attack by endogenous proteolytic enzymes; the protein is also thought to have broad-spectrum anti-biotic activity.<ref name="entrez">{{cite web | title = Entrez Gene: SLPI secretory leukocyte peptidase inhibitor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6590| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Fritz H |title=Human mucus proteinase inhibitor (human MPI). Human seminal inhibitor I (HUSI-I), antileukoprotease (ALP), secretory leukocyte protease inhibitor (SLPI). |journal=Biol. Chem. Hoppe-Seyler |volume=369 Suppl |issue= |pages= 79-82 |year= 1989 |pmid= 3060147 |doi= }}
*{{cite journal | author=Sallenave JM |title=The role of secretory leukocyte proteinase inhibitor and elafin (elastase-specific inhibitor/skin-derived antileukoprotease) as alarm antiproteinases in inflammatory lung disease. |journal=Respir. Res. |volume=1 |issue= 2 |pages= 87-92 |year= 2003 |pmid= 11667971 |doi= }}
*{{cite journal | author=Rogaev EI, Keryanov SA, Malyako YK |title=Dinucleotide repeat polymorphisms at the P1, HBE1 and MYH7 loci. |journal=Hum. Mol. Genet. |volume=1 |issue= 4 |pages= 285 |year= 1993 |pmid= 1363870 |doi= }}
*{{cite journal | author=Abe T, Kobayashi N, Yoshimura K, ''et al.'' |title=Expression of the secretory leukoprotease inhibitor gene in epithelial cells. |journal=J. Clin. Invest. |volume=87 |issue= 6 |pages= 2207-15 |year= 1991 |pmid= 1674946 |doi= }}
*{{cite journal | author=Sallenave JM, Ryle AP |title=Purification and characterization of elastase-specific inhibitor. Sequence homology with mucus proteinase inhibitor. |journal=Biol. Chem. Hoppe-Seyler |volume=372 |issue= 1 |pages= 13-21 |year= 1991 |pmid= 2039600 |doi= }}
*{{cite journal | author=Eisenberg SP, Hale KK, Heimdal P, Thompson RC |title=Location of the protease-inhibitory region of secretory leukocyte protease inhibitor. |journal=J. Biol. Chem. |volume=265 |issue= 14 |pages= 7976-81 |year= 1990 |pmid= 2110563 |doi= }}
*{{cite journal | author=Grütter MG, Fendrich G, Huber R, Bode W |title=The 2.5 A X-ray crystal structure of the acid-stable proteinase inhibitor from human mucous secretions analysed in its complex with bovine alpha-chymotrypsin. |journal=EMBO J. |volume=7 |issue= 2 |pages= 345-51 |year= 1988 |pmid= 3366116 |doi= }}
*{{cite journal | author=Thompson RC, Ohlsson K |title=Isolation, properties, and complete amino acid sequence of human secretory leukocyte protease inhibitor, a potent inhibitor of leukocyte elastase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 18 |pages= 6692-6 |year= 1986 |pmid= 3462719 |doi= }}
*{{cite journal | author=Seemüller U, Arnhold M, Fritz H, ''et al.'' |title=The acid-stable proteinase inhibitor of human mucous secretions (HUSI-I, antileukoprotease). Complete amino acid sequence as revealed by protein and cDNA sequencing and structural homology to whey proteins and Red Sea turtle proteinase inhibitor. |journal=FEBS Lett. |volume=199 |issue= 1 |pages= 43-8 |year= 1986 |pmid= 3485543 |doi= }}
*{{cite journal | author=Heinzel R, Appelhans H, Gassen G, ''et al.'' |title=Molecular cloning and expression of cDNA for human antileukoprotease from cervix uterus. |journal=Eur. J. Biochem. |volume=160 |issue= 1 |pages= 61-7 |year= 1986 |pmid= 3533531 |doi= }}
*{{cite journal | author=Stetler G, Brewer MT, Thompson RC |title=Isolation and sequence of a human gene encoding a potent inhibitor of leukocyte proteases. |journal=Nucleic Acids Res. |volume=14 |issue= 20 |pages= 7883-96 |year= 1986 |pmid= 3640338 |doi= }}
*{{cite journal | author=Westin U, Fryksmark U, Polling A, Ohlsson K |title=Localisation of secretory leucocyte proteinase inhibitor mRNA in nasal mucosa. |journal=Acta Otolaryngol. |volume=114 |issue= 2 |pages= 199-202 |year= 1994 |pmid= 7515550 |doi= }}
*{{cite journal | author=Ohlsson K, Bjartell A, Lilja H |title=Secretory leucocyte protease inhibitor in the male genital tract: PSA-induced proteolytic processing in human semen and tissue localization. |journal=J. Androl. |volume=16 |issue= 1 |pages= 64-74 |year= 1995 |pmid= 7539415 |doi= }}
*{{cite journal | author=Belorgey D, Dirrig S, Amouric M, ''et al.'' |title=Inhibition of human pancreatic proteinases by mucus proteinase inhibitor, eglin c and aprotinin. |journal=Biochem. J. |volume=313 ( Pt 2) |issue= |pages= 555-60 |year= 1996 |pmid= 8573092 |doi= }}
*{{cite journal | author=Kikuchi T, Abe T, Hoshi S, ''et al.'' |title=Structure of the murine secretory leukoprotease inhibitor (Slpi) gene and chromosomal localization of the human and murine SLPI genes. |journal=Am. J. Respir. Cell Mol. Biol. |volume=19 |issue= 6 |pages= 875-80 |year= 1999 |pmid= 9843921 |doi= }}
*{{cite journal | author=Westin U, Polling A, Ljungkrantz I, Ohlsson K |title=Identification of SLPI (secretory leukocyte protease inhibitor) in human mast cells using immunohistochemistry and in situ hybridisation. |journal=Biol. Chem. |volume=380 |issue= 4 |pages= 489-93 |year= 1999 |pmid= 10355635 |doi= }}
*{{cite journal | author=Mulligan MS, Lentsch AB, Huber-Lang M, ''et al.'' |title=Anti-inflammatory effects of mutant forms of secretory leukocyte protease inhibitor. |journal=Am. J. Pathol. |volume=156 |issue= 3 |pages= 1033-9 |year= 2000 |pmid= 10702419 |doi= }}
*{{cite journal | author=Nyström M, Bergenfeldt M, Ljungcrantz I, ''et al.'' |title=Production of secretory leucocyte protease inhibitor (SLPI) in human pancreatic beta-cells. |journal=Mediators Inflamm. |volume=8 |issue= 3 |pages= 147-51 |year= 2000 |pmid= 10704052 |doi= }}
*{{cite journal | author=Si-Tahar M, Merlin D, Sitaraman S, Madara JL |title=Constitutive and regulated secretion of secretory leukocyte proteinase inhibitor by human intestinal epithelial cells. |journal=Gastroenterology |volume=118 |issue= 6 |pages= 1061-71 |year= 2000 |pmid= 10833481 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SREBF2... {November 16, 2007 3:53:22 PM PST}
- SEARCH REDIRECT: Control Box Found: SREBF2 {November 16, 2007 3:53:41 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 3:53:42 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 3:53:42 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 3:53:42 PM PST}
- UPDATED: Updated protein page: SREBF2 {November 16, 2007 3:53:52 PM PST}
- INFO: Beginning work on STAT2... {November 16, 2007 3:53:52 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 3:54:32 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| 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 = Signal transducer and activator of transcription 2, 113kDa
| HGNCid = 11363
| Symbol = STAT2
| AltSymbols =; ISGF-3; MGC59816; P113; STAT113
| OMIM = 600556
| ECnumber =
| Homologene = 3952
| MGIid = 103039
| GeneAtlas_image1 = PBB_GE_STAT2_205170_at_tn.png
| GeneAtlas_image2 = PBB_GE_STAT2_217199_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005062 |text = hematopoietin/interferon-class (D200-domain) cytokine receptor signal transducer activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006357 |text = regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0007259 |text = JAK-STAT cascade}} {{GNF_GO|id=GO:0009615 |text = response to virus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6773
| Hs_Ensembl = ENSG00000170581
| Hs_RefseqProtein = NP_005410
| Hs_RefseqmRNA = NM_005419
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 55021651
| Hs_GenLoc_end = 55040176
| Hs_Uniprot = P52630
| Mm_EntrezGene = 20847
| Mm_Ensembl = ENSMUSG00000040033
| Mm_RefseqmRNA = XM_990913
| Mm_RefseqProtein = XP_996007
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 127673525
| Mm_GenLoc_end = 127695798
| Mm_Uniprot =
}}
}}
'''Signal transducer and activator of transcription 2, 113kDa''', also known as '''STAT2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: STAT2 signal transducer and activator of transcription 2, 113kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6773| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the STAT protein family. In response to cytokines and growth factors, STAT family members are phosphorylated by the receptor associated kinases, and then form homo- or heterodimers that translocate to the cell nucleus where they act as transcription activators. In response to interferon (IFN), this protein forms a complex with STAT1 and IFN regulatory factor family protein p48 (ISGF3G), in which this protein acts as a transactivator, but lacks the ability to bind DNA directly. Transcription adaptor P300/CBP (EP300/CREBBP) has been shown to interact specifically with this protein, which is thought to be involved in the process of blocking IFN-alpha response by adenovirus.<ref name="entrez">{{cite web | title = Entrez Gene: STAT2 signal transducer and activator of transcription 2, 113kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6773| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Cebulla CM, Miller DM, Sedmak DD |title=Viral inhibition of interferon signal transduction. |journal=Intervirology |volume=42 |issue= 5-6 |pages= 325-30 |year= 2000 |pmid= 10702714 |doi= }}
*{{cite journal | author=Kisseleva T, Bhattacharya S, Braunstein J, Schindler CW |title=Signaling through the JAK/STAT pathway, recent advances and future challenges. |journal=Gene |volume=285 |issue= 1-2 |pages= 1-24 |year= 2002 |pmid= 12039028 |doi= }}
*{{cite journal | author=Fu XY, Schindler C, Improta T, ''et al.'' |title=The proteins of ISGF-3, the interferon alpha-induced transcriptional activator, define a gene family involved in signal transduction. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 16 |pages= 7840-3 |year= 1992 |pmid= 1502204 |doi= }}
*{{cite journal | author=Uddin S, Chamdin A, Platanias LC |title=Interaction of the transcriptional activator Stat-2 with the type I interferon receptor. |journal=J. Biol. Chem. |volume=270 |issue= 42 |pages= 24627-30 |year= 1995 |pmid= 7559568 |doi= }}
*{{cite journal | author=Marrero MB, Schieffer B, Paxton WG, ''et al.'' |title=Direct stimulation of Jak/STAT pathway by the angiotensin II AT1 receptor. |journal=Nature |volume=375 |issue= 6528 |pages= 247-50 |year= 1995 |pmid= 7746328 |doi= 10.1038/375247a0 }}
*{{cite journal | author=Yan R, Qureshi S, Zhong Z, ''et al.'' |title=The genomic structure of the STAT genes: multiple exons in coincident sites in Stat1 and Stat2. |journal=Nucleic Acids Res. |volume=23 |issue= 3 |pages= 459-63 |year= 1995 |pmid= 7885841 |doi= }}
*{{cite journal | author=Sugiyama T, Nishio Y, Kishimoto T, Akira S |title=Identification of alternative splicing form of Stat2. |journal=FEBS Lett. |volume=381 |issue= 3 |pages= 191-4 |year= 1996 |pmid= 8601453 |doi= }}
*{{cite journal | author=Yan H, Krishnan K, Greenlund AC, ''et al.'' |title=Phosphorylated interferon-alpha receptor 1 subunit (IFNaR1) acts as a docking site for the latent form of the 113 kDa STAT2 protein. |journal=EMBO J. |volume=15 |issue= 5 |pages= 1064-74 |year= 1996 |pmid= 8605876 |doi= }}
*{{cite journal | author=Gupta S, Yan H, Wong LH, ''et al.'' |title=The SH2 domains of Stat1 and Stat2 mediate multiple interactions in the transduction of IFN-alpha signals. |journal=EMBO J. |volume=15 |issue= 5 |pages= 1075-84 |year= 1996 |pmid= 8605877 |doi= }}
*{{cite journal | author=Li X, Leung S, Qureshi S, ''et al.'' |title=Formation of STAT1-STAT2 heterodimers and their role in the activation of IRF-1 gene transcription by interferon-alpha. |journal=J. Biol. Chem. |volume=271 |issue= 10 |pages= 5790-4 |year= 1996 |pmid= 8621447 |doi= }}
*{{cite journal | author=Bhattacharya S, Eckner R, Grossman S, ''et al.'' |title=Cooperation of Stat2 and p300/CBP in signalling induced by interferon-alpha. |journal=Nature |volume=383 |issue= 6598 |pages= 344-7 |year= 1996 |pmid= 8848048 |doi= 10.1038/383344a0 }}
*{{cite journal | author=Horvath CM, Stark GR, Kerr IM, Darnell JE |title=Interactions between STAT and non-STAT proteins in the interferon-stimulated gene factor 3 transcription complex. |journal=Mol. Cell. Biol. |volume=16 |issue= 12 |pages= 6957-64 |year= 1997 |pmid= 8943351 |doi= }}
*{{cite journal | author=Bluyssen HA, Levy DE |title=Stat2 is a transcriptional activator that requires sequence-specific contacts provided by stat1 and p48 for stable interaction with DNA. |journal=J. Biol. Chem. |volume=272 |issue= 7 |pages= 4600-5 |year= 1997 |pmid= 9020188 |doi= }}
*{{cite journal | author=Li X, Leung S, Kerr IM, Stark GR |title=Functional subdomains of STAT2 required for preassociation with the alpha interferon receptor and for signaling. |journal=Mol. Cell. Biol. |volume=17 |issue= 4 |pages= 2048-56 |year= 1997 |pmid= 9121453 |doi= }}
*{{cite journal | author=Martinez-Moczygemba M, Gutch MJ, French DL, Reich NC |title=Distinct STAT structure promotes interaction of STAT2 with the p48 subunit of the interferon-alpha-stimulated transcription factor ISGF3. |journal=J. Biol. Chem. |volume=272 |issue= 32 |pages= 20070-6 |year= 1997 |pmid= 9242679 |doi= }}
*{{cite journal | author=Mowen K, David M |title=Role of the STAT1-SH2 domain and STAT2 in the activation and nuclear translocation of STAT1. |journal=J. Biol. Chem. |volume=273 |issue= 46 |pages= 30073-6 |year= 1998 |pmid= 9804758 |doi= }}
*{{cite journal | author=Dumler I, Kopmann A, Wagner K, ''et al.'' |title=Urokinase induces activation and formation of Stat4 and Stat1-Stat2 complexes in human vascular smooth muscle cells. |journal=J. Biol. Chem. |volume=274 |issue= 34 |pages= 24059-65 |year= 1999 |pmid= 10446176 |doi= }}
*{{cite journal | author=Paulson M, Pisharody S, Pan L, ''et al.'' |title=Stat protein transactivation domains recruit p300/CBP through widely divergent sequences. |journal=J. Biol. Chem. |volume=274 |issue= 36 |pages= 25343-9 |year= 1999 |pmid= 10464260 |doi= }}
*{{cite journal | author=Gupta S, Jiang M, Pernis AB |title=IFN-alpha activates Stat6 and leads to the formation of Stat2:Stat6 complexes in B cells. |journal=J. Immunol. |volume=163 |issue= 7 |pages= 3834-41 |year= 1999 |pmid= 10490982 |doi= }}
*{{cite journal | author=Vila-Coro AJ, Rodríguez-Frade JM, Martín De Ana A, ''et al.'' |title=The chemokine SDF-1alpha triggers CXCR4 receptor dimerization and activates the JAK/STAT pathway. |journal=FASEB J. |volume=13 |issue= 13 |pages= 1699-710 |year= 1999 |pmid= 10506573 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on UNG... {November 16, 2007 3:54:32 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 3:55:12 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_UNG_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1akz.
| PDB = {{PDB2|1akz}}, {{PDB2|1emh}}, {{PDB2|1emj}}, {{PDB2|1q3f}}, {{PDB2|1ssp}}, {{PDB2|1ugh}}, {{PDB2|1yuo}}, {{PDB2|2hxm}}, {{PDB2|2ssp}}, {{PDB2|4skn}}
| Name = Uracil-DNA glycosylase
| HGNCid = 12572
| Symbol = UNG
| AltSymbols =; DGU; DKFZp781L1143; HIGM4; UDG; UNG1; UNG15
| OMIM = 191525
| ECnumber =
| Homologene = 6585
| MGIid = 109352
| GeneAtlas_image1 = PBB_GE_UNG_202330_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004844 |text = uracil DNA N-glycosylase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016798 |text = hydrolase activity, acting on glycosyl bonds}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}}
| Process = {{GNF_GO|id=GO:0006284 |text = base-excision repair}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0016446 |text = somatic hypermutation of immunoglobulin genes}} {{GNF_GO|id=GO:0016447 |text = somatic recombination of immunoglobulin gene segments}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7374
| Hs_Ensembl = ENSG00000076248
| Hs_RefseqProtein = NP_003353
| Hs_RefseqmRNA = NM_003362
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 108019798
| Hs_GenLoc_end = 108033181
| Hs_Uniprot = P13051
| Mm_EntrezGene = 22256
| Mm_Ensembl = ENSMUSG00000029591
| Mm_RefseqmRNA = NM_001040691
| Mm_RefseqProtein = NP_001035781
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 114391376
| Mm_GenLoc_end = 114400320
| Mm_Uniprot = Q99KR9
}}
}}
'''Uracil-DNA glycosylase''', also known as '''UNG''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: UNG uracil-DNA glycosylase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7374| 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 one of several uracil-DNA glycosylases. One important function of uracil-DNA glycosylases is to prevent mutagenesis by eliminating uracil from DNA molecules by cleaving the N-glycosylic bond and initiating the base-excision repair (BER) pathway. Uracil bases occur from cytosine deamination or misincorporation of dUMP residues. Alternative promoter usage and splicing of this gene leads to two different isoforms: the mitochondrial UNG1 and the nuclear UNG2.<ref name="entrez">{{cite web | title = Entrez Gene: UNG uracil-DNA glycosylase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7374| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Caradonna S, Muller-Weeks S |title=The nature of enzymes involved in uracil-DNA repair: isoform characteristics of proteins responsible for nuclear and mitochondrial genomic integrity. |journal=Curr. Protein Pept. Sci. |volume=2 |issue= 4 |pages= 335-47 |year= 2002 |pmid= 12369930 |doi= }}
*{{cite journal | author=Kino T, Pavlakis GN |title=Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1. |journal=DNA Cell Biol. |volume=23 |issue= 4 |pages= 193-205 |year= 2004 |pmid= 15142377 |doi= 10.1089/104454904773819789 }}
*{{cite journal | author=Van Maele B, Debyser Z |title=HIV-1 integration: an interplay between HIV-1 integrase, cellular and viral proteins. |journal=AIDS reviews |volume=7 |issue= 1 |pages= 26-43 |year= 2005 |pmid= 15875659 |doi= }}
*{{cite journal | author=Slupphaug G, Olsen LC, Helland D, ''et al.'' |title=Cell cycle regulation and in vitro hybrid arrest analysis of the major human uracil-DNA glycosylase. |journal=Nucleic Acids Res. |volume=19 |issue= 19 |pages= 5131-7 |year= 1991 |pmid= 1923798 |doi= }}
*{{cite journal | author=Muller SJ, Caradonna S |title=Isolation and characterization of a human cDNA encoding uracil-DNA glycosylase. |journal=Biochim. Biophys. Acta |volume=1088 |issue= 2 |pages= 197-207 |year= 1991 |pmid= 2001396 |doi= }}
*{{cite journal | author=Olsen LC, Aasland R, Wittwer CU, ''et al.'' |title=Molecular cloning of human uracil-DNA glycosylase, a highly conserved DNA repair enzyme. |journal=EMBO J. |volume=8 |issue= 10 |pages= 3121-5 |year= 1990 |pmid= 2555154 |doi= }}
*{{cite journal | author=Nagelhus TA, Slupphaug G, Lindmo T, Krokan HE |title=Cell cycle regulation and subcellular localization of the major human uracil-DNA glycosylase. |journal=Exp. Cell Res. |volume=220 |issue= 2 |pages= 292-7 |year= 1995 |pmid= 7556436 |doi= 10.1006/excr.1995.1318 }}
*{{cite journal | author=Mol CD, Arvai AS, Sanderson RJ, ''et al.'' |title=Crystal structure of human uracil-DNA glycosylase in complex with a protein inhibitor: protein mimicry of DNA. |journal=Cell |volume=82 |issue= 5 |pages= 701-8 |year= 1995 |pmid= 7671300 |doi= }}
*{{cite journal | author=Mol CD, Arvai AS, Slupphaug G, ''et al.'' |title=Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis. |journal=Cell |volume=80 |issue= 6 |pages= 869-78 |year= 1995 |pmid= 7697717 |doi= }}
*{{cite journal | author=Haug T, Skorpen F, Lund H, Krokan HE |title=Structure of the gene for human uracil-DNA glycosylase and analysis of the promoter function. |journal=FEBS Lett. |volume=353 |issue= 2 |pages= 180-4 |year= 1994 |pmid= 7926048 |doi= }}
*{{cite journal | author=Slupphaug G, Markussen FH, Olsen LC, ''et al.'' |title=Nuclear and mitochondrial forms of human uracil-DNA glycosylase are encoded by the same gene. |journal=Nucleic Acids Res. |volume=21 |issue= 11 |pages= 2579-84 |year= 1993 |pmid= 8332455 |doi= }}
*{{cite journal | author=Bouhamdan M, Benichou S, Rey F, ''et al.'' |title=Human immunodeficiency virus type 1 Vpr protein binds to the uracil DNA glycosylase DNA repair enzyme. |journal=J. Virol. |volume=70 |issue= 2 |pages= 697-704 |year= 1996 |pmid= 8551605 |doi= }}
*{{cite journal | author=Kavli B, Slupphaug G, Mol CD, ''et al.'' |title=Excision of cytosine and thymine from DNA by mutants of human uracil-DNA glycosylase. |journal=EMBO J. |volume=15 |issue= 13 |pages= 3442-7 |year= 1996 |pmid= 8670846 |doi= }}
*{{cite journal | author=Haug T, Skorpen F, Kvaløy K, ''et al.'' |title=Human uracil-DNA glycosylase gene: sequence organization, methylation pattern, and mapping to chromosome 12q23-q24.1. |journal=Genomics |volume=36 |issue= 3 |pages= 408-16 |year= 1997 |pmid= 8884263 |doi= 10.1006/geno.1996.0485 }}
*{{cite journal | author=Slupphaug G, Mol CD, Kavli B, ''et al.'' |title=A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA. |journal=Nature |volume=384 |issue= 6604 |pages= 87-92 |year= 1996 |pmid= 8900285 |doi= 10.1038/384087a0 }}
*{{cite journal | author=Nilsen H, Otterlei M, Haug T, ''et al.'' |title=Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene. |journal=Nucleic Acids Res. |volume=25 |issue= 4 |pages= 750-5 |year= 1997 |pmid= 9016624 |doi= }}
*{{cite journal | author=Nagelhus TA, Haug T, Singh KK, ''et al.'' |title=A sequence in the N-terminal region of human uracil-DNA glycosylase with homology to XPA interacts with the C-terminal part of the 34-kDa subunit of replication protein A. |journal=J. Biol. Chem. |volume=272 |issue= 10 |pages= 6561-6 |year= 1997 |pmid= 9045683 |doi= }}
*{{cite journal | author=Selig L, Benichou S, Rogel ME, ''et al.'' |title=Uracil DNA glycosylase specifically interacts with Vpr of both human immunodeficiency virus type 1 and simian immunodeficiency virus of sooty mangabeys, but binding does not correlate with cell cycle arrest. |journal=J. Virol. |volume=71 |issue= 6 |pages= 4842-6 |year= 1997 |pmid= 9151883 |doi= }}
*{{cite journal | author=Withers-Ward ES, Jowett JB, Stewart SA, ''et al.'' |title=Human immunodeficiency virus type 1 Vpr interacts with HHR23A, a cellular protein implicated in nucleotide excision DNA repair. |journal=J. Virol. |volume=71 |issue= 12 |pages= 9732-42 |year= 1997 |pmid= 9371639 |doi= }}
*{{cite journal | author=Haug T, Skorpen F, Aas PA, ''et al.'' |title=Regulation of expression of nuclear and mitochondrial forms of human uracil-DNA glycosylase. |journal=Nucleic Acids Res. |volume=26 |issue= 6 |pages= 1449-57 |year= 1998 |pmid= 9490791 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on VASP... {November 16, 2007 3:55:12 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 3:55:35 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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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_VASP_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1egx.
| PDB = {{PDB2|1egx}}, {{PDB2|1usd}}, {{PDB2|1use}}
| Name = Vasodilator-stimulated phosphoprotein
| HGNCid = 12652
| Symbol = VASP
| AltSymbols =;
| OMIM = 601703
| ECnumber =
| Homologene = 7592
| MGIid = 109268
| GeneAtlas_image1 = PBB_GE_VASP_202205_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}}
| Component = {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}}
| Process = {{GNF_GO|id=GO:0006928 |text = cell motility}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7408
| Hs_Ensembl = ENSG00000125753
| Hs_RefseqProtein = NP_001008736
| Hs_RefseqmRNA = NM_001008736
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 50702528
| Hs_GenLoc_end = 50722076
| Hs_Uniprot = P50552
| Mm_EntrezGene = 22323
| Mm_Ensembl = ENSMUSG00000030403
| Mm_RefseqmRNA = NM_009499
| Mm_RefseqProtein = NP_033525
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 18416239
| Mm_GenLoc_end = 18423349
| Mm_Uniprot = P70460
}}
}}
'''Vasodilator-stimulated phosphoprotein''', also known as '''VASP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: VASP vasodilator-stimulated phosphoprotein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7408| 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 = Vasodilator-stimulated phosphoprotein (VASP) is a member of the Ena-VASP protein family. Ena-VASP family members contain an EHV1 N-terminal domain that binds proteins containing E/DFPPPPXD/E motifs and targets Ena-VASP proteins to focal adhesions. In the mid-region of the protein, family members have a proline-rich domain that binds SH3 and WW domain-containing proteins. Their C-terminal EVH2 domain mediates tetramerization and binds both G and F actin. VASP is associated with filamentous actin formation and likely plays a widespread role in cell adhesion and motility. VASP may also be involved in the intracellular signaling pathways that regulate integrin-extracellular matrix interactions. VASP is regulated by the cyclic nucleotide-dependent kinases PKA and PKG.<ref name="entrez">{{cite web | title = Entrez Gene: VASP vasodilator-stimulated phosphoprotein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7408| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Reinhard M, Halbrügge M, Scheer U, ''et al.'' |title=The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts. |journal=EMBO J. |volume=11 |issue= 6 |pages= 2063-70 |year= 1992 |pmid= 1318192 |doi= }}
*{{cite journal | author=Halbrügge M, Eigenthaler M, Polke C, Walter U |title=Protein phosphorylation regulated by cyclic nucleotide-dependent protein kinases in cell extracts and in intact human lymphocytes. |journal=Cell. Signal. |volume=4 |issue= 2 |pages= 189-99 |year= 1992 |pmid= 1319722 |doi= }}
*{{cite journal | author=Reinhard M, Jouvenal K, Tripier D, Walter U |title=Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 17 |pages= 7956-60 |year= 1995 |pmid= 7644520 |doi= }}
*{{cite journal | author=Reinhard M, Giehl K, Abel K, ''et al.'' |title=The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins. |journal=EMBO J. |volume=14 |issue= 8 |pages= 1583-9 |year= 1995 |pmid= 7737110 |doi= }}
*{{cite journal | author=Haffner C, Jarchau T, Reinhard M, ''et al.'' |title=Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP. |journal=EMBO J. |volume=14 |issue= 1 |pages= 19-27 |year= 1995 |pmid= 7828592 |doi= }}
*{{cite journal | author=Horstrup K, Jablonka B, Hönig-Liedl P, ''et al.'' |title=Phosphorylation of focal adhesion vasodilator-stimulated phosphoprotein at Ser157 in intact human platelets correlates with fibrinogen receptor inhibition. |journal=Eur. J. Biochem. |volume=225 |issue= 1 |pages= 21-7 |year= 1994 |pmid= 7925440 |doi= }}
*{{cite journal | author=Butt E, Abel K, Krieger M, ''et al.'' |title=cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets. |journal=J. Biol. Chem. |volume=269 |issue= 20 |pages= 14509-17 |year= 1994 |pmid= 8182057 |doi= }}
*{{cite journal | author=Zimmer M, Fink T, Fischer L, ''et al.'' |title=Cloning of the VASP (vasodilator-stimulated phosphoprotein) genes in human and mouse: structure, sequence, and chromosomal localization. |journal=Genomics |volume=36 |issue= 2 |pages= 227-33 |year= 1997 |pmid= 8812448 |doi= 10.1006/geno.1996.0457 }}
*{{cite journal | author=Laurent V, Loisel TP, Harbeck B, ''et al.'' |title=Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes. |journal=J. Cell Biol. |volume=144 |issue= 6 |pages= 1245-58 |year= 1999 |pmid= 10087267 |doi= }}
*{{cite journal | author=Bachmann C, Fischer L, Walter U, Reinhard M |title=The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation. |journal=J. Biol. Chem. |volume=274 |issue= 33 |pages= 23549-57 |year= 1999 |pmid= 10438535 |doi= }}
*{{cite journal | author=Petit MM, Fradelizi J, Golsteyn RM, ''et al.'' |title=LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacity. |journal=Mol. Biol. Cell |volume=11 |issue= 1 |pages= 117-29 |year= 2000 |pmid= 10637295 |doi= }}
*{{cite journal | author=Krause M, Sechi AS, Konradt M, ''et al.'' |title=Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3 complex link T cell receptor (TCR) signaling to the actin cytoskeleton. |journal=J. Cell Biol. |volume=149 |issue= 1 |pages= 181-94 |year= 2000 |pmid= 10747096 |doi= }}
*{{cite journal | author=Drees B, Friederich E, Fradelizi J, ''et al.'' |title=Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins. |journal=J. Biol. Chem. |volume=275 |issue= 29 |pages= 22503-11 |year= 2000 |pmid= 10801818 |doi= 10.1074/jbc.M001698200 }}
*{{cite journal | author=Smolenski A, Poller W, Walter U, Lohmann SM |title=Regulation of human endothelial cell focal adhesion sites and migration by cGMP-dependent protein kinase I. |journal=J. Biol. Chem. |volume=275 |issue= 33 |pages= 25723-32 |year= 2000 |pmid= 10851246 |doi= 10.1074/jbc.M909632199 }}
*{{cite journal | author=Harbeck B, Hüttelmaier S, Schluter K, ''et al.'' |title=Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin. |journal=J. Biol. Chem. |volume=275 |issue= 40 |pages= 30817-25 |year= 2000 |pmid= 10882740 |doi= 10.1074/jbc.M005066200 }}
*{{cite journal | author=Burkhardt M, Glazova M, Gambaryan S, ''et al.'' |title=KT5823 inhibits cGMP-dependent protein kinase activity in vitro but not in intact human platelets and rat mesangial cells. |journal=J. Biol. Chem. |volume=275 |issue= 43 |pages= 33536-41 |year= 2000 |pmid= 10922374 |doi= 10.1074/jbc.M005670200 }}
*{{cite journal | author=Ball LJ, Kühne R, Hoffmann B, ''et al.'' |title=Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity. |journal=EMBO J. |volume=19 |issue= 18 |pages= 4903-14 |year= 2000 |pmid= 10990454 |doi= 10.1093/emboj/19.18.4903 }}
*{{cite journal | author=Bearer EL, Prakash JM, Manchester RD, Allen PG |title=VASP protects actin filaments from gelsolin: an in vitro study with implications for platelet actin reorganizations. |journal=Cell Motil. Cytoskeleton |volume=47 |issue= 4 |pages= 351-64 |year= 2001 |pmid= 11093254 |doi= 10.1002/1097-0169(200012)47:4<351::AID-CM8>3.0.CO;2-8 }}
*{{cite journal | author=Lawrence DW, Pryzwansky KB |title=The vasodilator-stimulated phosphoprotein is regulated by cyclic GMP-dependent protein kinase during neutrophil spreading. |journal=J. Immunol. |volume=166 |issue= 9 |pages= 5550-6 |year= 2001 |pmid= 11313394 |doi= }}
*{{cite journal | author=Castellano F, Le Clainche C, Patin D, ''et al.'' |title=A WASp-VASP complex regulates actin polymerization at the plasma membrane. |journal=EMBO J. |volume=20 |issue= 20 |pages= 5603-14 |year= 2001 |pmid= 11598004 |doi= 10.1093/emboj/20.20.5603 }}
}}
{{refend}}
{{protein-stub}}
end log.
