Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 20:09, 19 November 2007 (UTC)
[edit]Proteins without matches (14)
[edit]Proteins with a High Potential Match (2)
[edit]Redirected Proteins (9)
[edit]Manual Inspection (Page not found) (16)
[edit]
Protein Status Grid - Date: 20:09, 19 November 2007 (UTC)
[edit]Vebose Log - Date: 20:09, 19 November 2007 (UTC)
[edit]- INFO: Beginning work on ABCB4... {November 19, 2007 11:49:42 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 11:50:21 AM PST}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = ATP-binding cassette, sub-family B (MDR/TAP), member 4
| HGNCid = 45
| Symbol = ABCB4
| AltSymbols =; ABC21; MDR2/3; MDR3; PFIC-3; PGY3
| OMIM = 171060
| ECnumber =
| Homologene = 56421
| MGIid = 97569
| GeneAtlas_image1 = PBB_GE_ABCB4_207819_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ABCB4_209994_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008559 |text = xenobiotic-transporting ATPase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016887 |text = ATPase activity}} {{GNF_GO|id=GO:0042626 |text = ATPase activity, coupled to transmembrane movement of substances}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0009410 |text = response to xenobiotic stimulus}} {{GNF_GO|id=GO:0042493 |text = response to drug}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5244
| Hs_Ensembl = ENSG00000005471
| Hs_RefseqProtein = NP_000434
| Hs_RefseqmRNA = NM_000443
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 86869302
| Hs_GenLoc_end = 86942991
| Hs_Uniprot = P21439
| Mm_EntrezGene = 18670
| Mm_Ensembl = ENSMUSG00000042476
| Mm_RefseqmRNA = NM_008830
| Mm_RefseqProtein = NP_032856
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 8899723
| Mm_GenLoc_end = 8965232
| Mm_Uniprot = P21440
}}
}}
'''ATP-binding cassette, sub-family B (MDR/TAP), member 4''', also known as '''ABCB4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ABCB4 ATP-binding cassette, sub-family B (MDR/TAP), member 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5244| 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 membrane-associated protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the MDR/TAP subfamily. Members of the MDR/TAP subfamily are involved in multidrug resistance as well as antigen presentation. This gene encodes a full transporter and member of the p-glycoprotein family of membrane proteins with phosphatidylcholine as its substrate. The function of this protein has not yet been determined; however, it may involve transport of phospholipids from liver hepatocytes into bile. Alternative splicing of this gene results in several products of undetermined function.<ref name="entrez">{{cite web | title = Entrez Gene: ABCB4 ATP-binding cassette, sub-family B (MDR/TAP), member 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5244| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Rosmorduc O, Poupon R |title=Low phospholipid associated cholelithiasis: association with mutation in the MDR3/ABCB4 gene. |journal=Orphanet journal of rare diseases |volume=2 |issue= |pages= 29 |year= 2007 |pmid= 17562004 |doi= 10.1186/1750-1172-2-29 }}
*{{cite journal | author=Mbongo-Kama E, Harnois F, Mennecier D, ''et al.'' |title=MDR3 mutations associated with intrahepatic and gallbladder cholesterol cholelithiasis: an update. |journal=Annals of hepatology : official journal of the Mexican Association of Hepatology |volume=6 |issue= 3 |pages= 143-9 |year= 2007 |pmid= 17786139 |doi= }}
*{{cite journal | author=Lincke CR, Smit JJ, van der Velde-Koerts T, Borst P |title=Structure of the human MDR3 gene and physical mapping of the human MDR locus. |journal=J. Biol. Chem. |volume=266 |issue= 8 |pages= 5303-10 |year= 1991 |pmid= 2002063 |doi= }}
*{{cite journal | author=Van der Bliek AM, Baas F, Ten Houte de Lange T, ''et al.'' |title=The human mdr3 gene encodes a novel P-glycoprotein homologue and gives rise to alternatively spliced mRNAs in liver. |journal=EMBO J. |volume=6 |issue= 11 |pages= 3325-31 |year= 1988 |pmid= 2892668 |doi= }}
*{{cite journal | author=van der Bliek AM, Kooiman PM, Schneider C, Borst P |title=Sequence of mdr3 cDNA encoding a human P-glycoprotein. |journal=Gene |volume=71 |issue= 2 |pages= 401-11 |year= 1989 |pmid= 2906314 |doi= }}
*{{cite journal | author=Callen DF, Baker E, Simmers RN, ''et al.'' |title=Localization of the human multiple drug resistance gene, MDR1, to 7q21.1. |journal=Hum. Genet. |volume=77 |issue= 2 |pages= 142-4 |year= 1987 |pmid= 3477522 |doi= }}
*{{cite journal | author=Smit JJ, Schinkel AH, Mol CA, ''et al.'' |title=Tissue distribution of the human MDR3 P-glycoprotein. |journal=Lab. Invest. |volume=71 |issue= 5 |pages= 638-49 |year= 1994 |pmid= 7734012 |doi= }}
*{{cite journal | author=Smit JJ, Mol CA, van Deemter L, ''et al.'' |title=Characterization of the promoter region of the human MDR3 P-glycoprotein gene. |journal=Biochim. Biophys. Acta |volume=1261 |issue= 1 |pages= 44-56 |year= 1995 |pmid= 7893760 |doi= }}
*{{cite journal | author=Whitington PF, Freese DK, Alonso EM, ''et al.'' |title=Clinical and biochemical findings in progressive familial intrahepatic cholestasis. |journal=J. Pediatr. Gastroenterol. Nutr. |volume=18 |issue= 2 |pages= 134-41 |year= 1994 |pmid= 7912266 |doi= }}
*{{cite journal | author=Ruetz S, Gros P |title=Phosphatidylcholine translocase: a physiological role for the mdr2 gene. |journal=Cell |volume=77 |issue= 7 |pages= 1071-81 |year= 1994 |pmid= 7912658 |doi= }}
*{{cite journal | author=Smit JJ, Schinkel AH, Oude Elferink RP, ''et al.'' |title=Homozygous disruption of the murine mdr2 P-glycoprotein gene leads to a complete absence of phospholipid from bile and to liver disease. |journal=Cell |volume=75 |issue= 3 |pages= 451-62 |year= 1993 |pmid= 8106172 |doi= }}
*{{cite journal | author=van Helvoort A, Smith AJ, Sprong H, ''et al.'' |title=MDR1 P-glycoprotein is a lipid translocase of broad specificity, while MDR3 P-glycoprotein specifically translocates phosphatidylcholine. |journal=Cell |volume=87 |issue= 3 |pages= 507-17 |year= 1996 |pmid= 8898203 |doi= }}
*{{cite journal | author=de Vree JM, Jacquemin E, Sturm E, ''et al.'' |title=Mutations in the MDR3 gene cause progressive familial intrahepatic cholestasis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 1 |pages= 282-7 |year= 1998 |pmid= 9419367 |doi= }}
*{{cite journal | author=Malorni W, Lucia MB, Rainaldi G, ''et al.'' |title=Intracellular expression of P-170 glycoprotein in peripheral blood mononuclear cell subsets from healthy donors and HIV-infected patients. |journal=Haematologica |volume=83 |issue= 1 |pages= 13-20 |year= 1998 |pmid= 9542318 |doi= }}
*{{cite journal | author=Jacquemin E, Cresteil D, Manouvrier S, ''et al.'' |title=Heterozygous non-sense mutation of the MDR3 gene in familial intrahepatic cholestasis of pregnancy. |journal=Lancet |volume=353 |issue= 9148 |pages= 210-1 |year= 1999 |pmid= 9923886 |doi= }}
*{{cite journal | author=Dixon PH, Weerasekera N, Linton KJ, ''et al.'' |title=Heterozygous MDR3 missense mutation associated with intrahepatic cholestasis of pregnancy: evidence for a defect in protein trafficking. |journal=Hum. Mol. Genet. |volume=9 |issue= 8 |pages= 1209-17 |year= 2000 |pmid= 10767346 |doi= }}
*{{cite journal | author=Rosmorduc O, Hermelin B, Poupon R |title=MDR3 gene defect in adults with symptomatic intrahepatic and gallbladder cholesterol cholelithiasis. |journal=Gastroenterology |volume=120 |issue= 6 |pages= 1459-67 |year= 2001 |pmid= 11313316 |doi= }}
*{{cite journal | author=Jacquemin E |title=Role of multidrug resistance 3 deficiency in pediatric and adult liver disease: one gene for three diseases. |journal=Semin. Liver Dis. |volume=21 |issue= 4 |pages= 551-62 |year= 2002 |pmid= 11745043 |doi= 10.1055/s-2001-19033 }}
*{{cite journal | author=Eloranta ML, Heiskanen JT, Hiltunen MJ, ''et al.'' |title=Multidrug resistance 3 gene mutation 1712delT and estrogen receptor alpha gene polymorphisms in Finnish women with obstetric cholestasis. |journal=Eur. J. Obstet. Gynecol. Reprod. Biol. |volume=104 |issue= 2 |pages= 109-12 |year= 2003 |pmid= 12206920 |doi= }}
*{{cite journal | author=Eloranta ML, Heiskanen JT, Hiltunen MJ, ''et al.'' |title=Multidrug resistance 3 gene mutation 1712delT and estrogen receptor alpha gene polymorphisms in Finnish women with obstetric cholestasis. |journal=Eur. J. Obstet. Gynecol. Reprod. Biol. |volume=105 |issue= 2 |pages= 132-5 |year= 2003 |pmid= 12381474 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ATP2A1... {November 19, 2007 11:45:45 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 11:46:13 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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| update_protein_box = 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 = PBB_Protein_ATP2A1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1iwo.
| PDB = {{PDB2|1iwo}}, {{PDB2|1kju}}, {{PDB2|1su4}}, {{PDB2|1t5s}}, {{PDB2|1t5t}}, {{PDB2|1vfp}}, {{PDB2|1wpe}}, {{PDB2|1wpg}}, {{PDB2|1xp5}}, {{PDB2|2agv}}, {{PDB2|2by4}}, {{PDB2|2c88}}, {{PDB2|2c8k}}, {{PDB2|2c8l}}, {{PDB2|2c9m}}, {{PDB2|2dqs}}, {{PDB2|2ear}}, {{PDB2|2eas}}, {{PDB2|2eat}}, {{PDB2|2eau}}, {{PDB2|2o9j}}, {{PDB2|2oa0}}
| Name = ATPase, Ca++ transporting, cardiac muscle, fast twitch 1
| HGNCid = 811
| Symbol = ATP2A1
| AltSymbols =; ATP2A; SERCA1
| OMIM = 108730
| ECnumber =
| Homologene = 7635
| MGIid = 105058
| GeneAtlas_image1 = PBB_GE_ATP2A1_205444_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0005388 |text = calcium-transporting ATPase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016820 |text = hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0016529 |text = sarcoplasmic reticulum}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006812 |text = cation transport}} {{GNF_GO|id=GO:0006816 |text = calcium ion transport}} {{GNF_GO|id=GO:0006942 |text = regulation of striated muscle contraction}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0015992 |text = proton transport}} {{GNF_GO|id=GO:0031448 |text = positive regulation of striated fast muscle contraction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 487
| Hs_Ensembl = ENSG00000196296
| Hs_RefseqProtein = XP_001127578
| Hs_RefseqmRNA = XM_001127578
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 28797310
| Hs_GenLoc_end = 28823331
| Hs_Uniprot = O14983
| Mm_EntrezGene = 11937
| Mm_Ensembl = ENSMUSG00000030730
| Mm_RefseqmRNA = NM_007504
| Mm_RefseqProtein = NP_031530
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 126238017
| Mm_GenLoc_end = 126254070
| Mm_Uniprot = Q3TUZ7
}}
}}
'''ATPase, Ca++ transporting, cardiac muscle, fast twitch 1''', also known as '''ATP2A1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATP2A1 ATPase, Ca++ transporting, cardiac muscle, fast twitch 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=487| 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 the SERCA Ca(2+)-ATPases, which are intracellular pumps located in the sarcoplasmic or endoplasmic reticula of muscle cells. This enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen, and is involved in muscular excitation and contraction. Mutations in this gene cause some autosomal recessive forms of Brody disease, characterized by increasing impairment of muscular relaxation during exercise. Alternative splicing results in two transcript variants encoding different isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: ATP2A1 ATPase, Ca++ transporting, cardiac muscle, fast twitch 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=487| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Baba-Aissa F, Raeymaekers L, Wuytack F, ''et al.'' |title=Distribution and isoform diversity of the organellar Ca2+ pumps in the brain. |journal=Mol. Chem. Neuropathol. |volume=33 |issue= 3 |pages= 199-208 |year= 1998 |pmid= 9642673 |doi= }}
*{{cite journal | author=Callen DF, Baker E, Lane S, ''et al.'' |title=Regional mapping of the Batten disease locus (CLN3) to human chromosome 16p12. |journal=Am. J. Hum. Genet. |volume=49 |issue= 6 |pages= 1372-7 |year= 1992 |pmid= 1746562 |doi= }}
*{{cite journal | author=MacLennan DH, Brandl CJ, Champaneria S, ''et al.'' |title=Fast-twitch and slow-twitch/cardiac Ca2+ ATPase genes map to human chromosomes 16 and 12. |journal=Somat. Cell Mol. Genet. |volume=13 |issue= 4 |pages= 341-6 |year= 1988 |pmid= 2842876 |doi= }}
*{{cite journal | author=Brandl CJ, Green NM, Korczak B, MacLennan DH |title=Two Ca2+ ATPase genes: homologies and mechanistic implications of deduced amino acid sequences. |journal=Cell |volume=44 |issue= 4 |pages= 597-607 |year= 1986 |pmid= 2936465 |doi= }}
*{{cite journal | author=Benders AA, Wevers RA, Veerkamp JH |title=Ion transport in human skeletal muscle cells: disturbances in myotonic dystrophy and Brody's disease. |journal=Acta Physiol. Scand. |volume=156 |issue= 3 |pages= 355-67 |year= 1996 |pmid= 8729696 |doi= }}
*{{cite journal | author=Zhang Y, Fujii J, Phillips MS, ''et al.'' |title=Characterization of cDNA and genomic DNA encoding SERCA1, the Ca(2+)-ATPase of human fast-twitch skeletal muscle sarcoplasmic reticulum, and its elimination as a candidate gene for Brody disease. |journal=Genomics |volume=30 |issue= 3 |pages= 415-24 |year= 1997 |pmid= 8825625 |doi= 10.1006/geno.1995.1259 }}
*{{cite journal | author=Odermatt A, Taschner PE, Khanna VK, ''et al.'' |title=Mutations in the gene-encoding SERCA1, the fast-twitch skeletal muscle sarcoplasmic reticulum Ca2+ ATPase, are associated with Brody disease. |journal=Nat. Genet. |volume=14 |issue= 2 |pages= 191-4 |year= 1996 |pmid= 8841193 |doi= 10.1038/ng1096-191 }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Algenstaedt P, Antonetti DA, Yaffe MB, Kahn CR |title=Insulin receptor substrate proteins create a link between the tyrosine phosphorylation cascade and the Ca2+-ATPases in muscle and heart. |journal=J. Biol. Chem. |volume=272 |issue= 38 |pages= 23696-702 |year= 1997 |pmid= 9295312 |doi= }}
*{{cite journal | author=Odermatt A, Taschner PE, Scherer SW, ''et al.'' |title=Characterization of the gene encoding human sarcolipin (SLN), a proteolipid associated with SERCA1: absence of structural mutations in five patients with Brody disease. |journal=Genomics |volume=45 |issue= 3 |pages= 541-53 |year= 1998 |pmid= 9367679 |doi= 10.1006/geno.1997.4967 }}
*{{cite journal | author=MacLennan DH, Rice WJ, Odermatt A |title=Structure/function analysis of the Ca2+ binding and translocation domain of SERCA1 and the role in Brody disease of the ATP2A1 gene encoding SERCA1. |journal=Ann. N. Y. Acad. Sci. |volume=834 |issue= |pages= 175-85 |year= 1998 |pmid= 9405806 |doi= }}
*{{cite journal | author=Odermatt A, Becker S, Khanna VK, ''et al.'' |title=Sarcolipin regulates the activity of SERCA1, the fast-twitch skeletal muscle sarcoplasmic reticulum Ca2+-ATPase. |journal=J. Biol. Chem. |volume=273 |issue= 20 |pages= 12360-9 |year= 1998 |pmid= 9575189 |doi= }}
*{{cite journal | author=Asahi M, Kimura Y, Kurzydlowski K, ''et al.'' |title=Transmembrane helix M6 in sarco(endo)plasmic reticulum Ca(2+)-ATPase forms a functional interaction site with phospholamban. Evidence for physical interactions at other sites. |journal=J. Biol. Chem. |volume=274 |issue= 46 |pages= 32855-62 |year= 2000 |pmid= 10551848 |doi= }}
*{{cite journal | author=Odermatt A, Barton K, Khanna VK, ''et al.'' |title=The mutation of Pro789 to Leu reduces the activity of the fast-twitch skeletal muscle sarco(endo)plasmic reticulum Ca2+ ATPase (SERCA1) and is associated with Brody disease. |journal=Hum. Genet. |volume=106 |issue= 5 |pages= 482-91 |year= 2000 |pmid= 10914677 |doi= }}
*{{cite journal | author=Daiho T, Yamasaki K, Saino T, ''et al.'' |title=Mutations of either or both Cys876 and Cys888 residues of sarcoplasmic reticulum Ca2+-ATPase result in a complete loss of Ca2+ transport activity without a loss of Ca2+-dependent ATPase activity. Role of the CYS876-CYS888 disulfide bond. |journal=J. Biol. Chem. |volume=276 |issue= 35 |pages= 32771-8 |year= 2001 |pmid= 11438520 |doi= 10.1074/jbc.M101229200 }}
*{{cite journal | author=Asahi M, Green NM, Kurzydlowski K, ''et al.'' |title=Phospholamban domain IB forms an interaction site with the loop between transmembrane helices M6 and M7 of sarco(endo)plasmic reticulum Ca2+ ATPases. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 18 |pages= 10061-6 |year= 2001 |pmid= 11526231 |doi= 10.1073/pnas.181348298 }}
*{{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=Pieske B, Maier LS, Schmidt-Schweda S |title=Sarcoplasmic reticulum Ca2+ load in human heart failure. |journal=Basic Res. Cardiol. |volume=97 Suppl 1 |issue= |pages= I63-71 |year= 2002 |pmid= 12479237 |doi= }}
*{{cite journal | author=Toyoshima C, Asahi M, Sugita Y, ''et al.'' |title=Modeling of the inhibitory interaction of phospholamban with the Ca2+ ATPase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 2 |pages= 467-72 |year= 2003 |pmid= 12525698 |doi= 10.1073/pnas.0237326100 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on AZGP1... {November 19, 2007 11:46:13 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 11:46:48 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_AZGP1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1t7v.
| PDB = {{PDB2|1t7v}}, {{PDB2|1t7w}}, {{PDB2|1t7x}}, {{PDB2|1t7y}}, {{PDB2|1t7z}}, {{PDB2|1t80}}, {{PDB2|1zag}}, {{PDB2|2icn}}
| Name = Alpha-2-glycoprotein 1, zinc-binding
| HGNCid = 910
| Symbol = AZGP1
| AltSymbols =; ZA2G; ZAG
| OMIM = 194460
| ECnumber =
| Homologene = 915
| MGIid = 103163
| GeneAtlas_image1 = PBB_GE_AZGP1_209309_at_tn.png
| GeneAtlas_image2 = PBB_GE_AZGP1_217014_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004540 |text = ribonuclease activity}} {{GNF_GO|id=GO:0005504 |text = fatty acid binding}} {{GNF_GO|id=GO:0008320 |text = protein carrier activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0042612 |text = MHC class I protein complex}}
| Process = {{GNF_GO|id=GO:0002474 |text = antigen processing and presentation of peptide antigen via MHC class I}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0016042 |text = lipid catabolic process}} {{GNF_GO|id=GO:0019882 |text = antigen processing and presentation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 563
| Hs_Ensembl = ENSG00000160862
| Hs_RefseqProtein = NP_001176
| Hs_RefseqmRNA = NM_001185
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 99402290
| Hs_GenLoc_end = 99411623
| Hs_Uniprot = P25311
| Mm_EntrezGene = 12007
| Mm_Ensembl = ENSMUSG00000037053
| Mm_RefseqmRNA = NM_013478
| Mm_RefseqProtein = NP_038506
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 138211324
| Mm_GenLoc_end = 138220018
| Mm_Uniprot = Q9DBB7
}}
}}
'''Alpha-2-glycoprotein 1, zinc-binding''', also known as '''AZGP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AZGP1 alpha-2-glycoprotein 1, zinc-binding| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=563| 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=Freije JP, Fueyo A, Uría J, López-Otín C |title=Human Zn-alpha 2-glycoprotein cDNA cloning and expression analysis in benign and malignant breast tissues. |journal=FEBS Lett. |volume=290 |issue= 1-2 |pages= 247-9 |year= 1991 |pmid= 1915885 |doi= }}
*{{cite journal | author=Tada T, Ohkubo I, Niwa M, ''et al.'' |title=Immunohistochemical localization of Zn-alpha 2-glycoprotein in normal human tissues. |journal=J. Histochem. Cytochem. |volume=39 |issue= 9 |pages= 1221-6 |year= 1991 |pmid= 1918940 |doi= }}
*{{cite journal | author=Ueyama H, Niwa M, Tada T, ''et al.'' |title=Cloning and nucleotide sequence of a human Zn-alpha 2-glycoprotein cDNA and chromosomal assignment of its gene. |journal=Biochem. Biophys. Res. Commun. |volume=177 |issue= 2 |pages= 696-703 |year= 1991 |pmid= 2049092 |doi= }}
*{{cite journal | author=Araki T, Gejyo F, Takagaki K, ''et al.'' |title=Complete amino acid sequence of human plasma Zn-alpha 2-glycoprotein and its homology to histocompatibility antigens. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 3 |pages= 679-83 |year= 1988 |pmid= 3422450 |doi= }}
*{{cite journal | author=Shibata S, Miura K |title=Nephritogenic glycoprotein. IX. Plasma Zn-alpha2-glycoprotein as a second source of nephritogenic glycoprotein in urine. |journal=Nephron |volume=31 |issue= 2 |pages= 170-6 |year= 1982 |pmid= 6896906 |doi= }}
*{{cite journal | author=Ueyama H, Deng HX, Ohkubo I |title=Molecular cloning and chromosomal assignment of the gene for human Zn-alpha 2-glycoprotein. |journal=Biochemistry |volume=32 |issue= 48 |pages= 12968-76 |year= 1994 |pmid= 8241150 |doi= }}
*{{cite journal | author=Freije JP, Fueyo A, Uría JA, ''et al.'' |title=Human Zn-alpha 2-glycoprotein: complete genomic sequence, identification of a related pseudogene and relationship to class I major histocompatibility complex genes. |journal=Genomics |volume=18 |issue= 3 |pages= 575-87 |year= 1994 |pmid= 8307568 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Sánchez LM, López-Otín C, Bjorkman PJ |title=Biochemical characterization and crystalization of human Zn-alpha2-glycoprotein, a soluble class I major histocompatibility complex homolog. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 9 |pages= 4626-30 |year= 1997 |pmid= 9114041 |doi= }}
*{{cite journal | author=Brysk MM, Lei G, Rajaraman S, ''et al.'' |title=Gene expression of zinc-alpha 2-glycoprotein in normal human epidermal and buccal epithelia. |journal=In Vivo |volume=11 |issue= 3 |pages= 271-4 |year= 1997 |pmid= 9239523 |doi= }}
*{{cite journal | author=Lei G, Arany I, Selvanayagam P, ''et al.'' |title=Detection and cloning of epidermal zinc-alpha 2-glycoprotein cDNA and expression in normal human skin and in tumors. |journal=J. Cell. Biochem. |volume=67 |issue= 2 |pages= 216-22 |year= 1997 |pmid= 9328826 |doi= }}
*{{cite journal | author=Ogikubo O, Maeda T, Yamane T, ''et al.'' |title=Regulation of Zn-alpha2-glycoprotein-mediated cell adhesion by kininogens and their derivatives. |journal=Biochem. Biophys. Res. Commun. |volume=252 |issue= 1 |pages= 257-62 |year= 1998 |pmid= 9813179 |doi= }}
*{{cite journal | author=Sánchez LM, Chirino AJ, Bjorkman P |title=Crystal structure of human ZAG, a fat-depleting factor related to MHC molecules. |journal=Science |volume=283 |issue= 5409 |pages= 1914-9 |year= 1999 |pmid= 10206894 |doi= }}
*{{cite journal | author=Lei G, Brysk H, Arany I, ''et al.'' |title=Characterization of zinc-alpha(2)-glycoprotein as a cell adhesion molecule that inhibits the proliferation of an oral tumor cell line. |journal=J. Cell. Biochem. |volume=75 |issue= 1 |pages= 160-9 |year= 1999 |pmid= 10462714 |doi= }}
*{{cite journal | author=Davidsson P, Nilsson CL |title=Peptide mapping of proteins in cerebrospinal fluid utilizing a rapid preparative two-dimensional electrophoretic procedure and matrix-assisted laser desorption/ionization mass spectrometry. |journal=Biochim. Biophys. Acta |volume=1473 |issue= 2-3 |pages= 391-9 |year= 2000 |pmid= 10594376 |doi= }}
*{{cite journal | author=Kennedy MW, Heikema AP, Cooper A, ''et al.'' |title=Hydrophobic ligand binding by Zn-alpha 2-glycoprotein, a soluble fat-depleting factor related to major histocompatibility complex proteins. |journal=J. Biol. Chem. |volume=276 |issue= 37 |pages= 35008-13 |year= 2001 |pmid= 11425849 |doi= 10.1074/jbc.C100301200 }}
*{{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=Scherer SW, Cheung J, MacDonald JR, ''et al.'' |title=Human chromosome 7: DNA sequence and biology. |journal=Science |volume=300 |issue= 5620 |pages= 767-72 |year= 2003 |pmid= 12690205 |doi= 10.1126/science.1083423 }}
*{{cite journal | author=Hillier LW, Fulton RS, Fulton LA, ''et al.'' |title=The DNA sequence of human chromosome 7. |journal=Nature |volume=424 |issue= 6945 |pages= 157-64 |year= 2003 |pmid= 12853948 |doi= 10.1038/nature01782 }}
*{{cite journal | author=BURGI W, SCHMID K |title=Preparation and properties of Zn-alpha 2-glycoprotein of normal human plasma. |journal=J. Biol. Chem. |volume=236 |issue= |pages= 1066-74 |year= 1998 |pmid= 13689030 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KLF5... {November 19, 2007 11:46:48 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 11:47:19 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
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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 = Kruppel-like factor 5 (intestinal)
| HGNCid = 6349
| Symbol = KLF5
| AltSymbols =; BTEB2; CKLF; IKLF
| OMIM = 602903
| ECnumber =
| Homologene = 37520
| MGIid = 1338056
| GeneAtlas_image1 = PBB_GE_KLF5_209211_at_tn.png
| GeneAtlas_image2 = PBB_GE_KLF5_209212_s_at_tn.png
| Function = {{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: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:0001525 |text = angiogenesis}} {{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:0030033 |text = microvillus biogenesis}} {{GNF_GO|id=GO:0045941 |text = positive regulation of transcription}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 688
| Hs_Ensembl = ENSG00000102554
| Hs_RefseqProtein = NP_001721
| Hs_RefseqmRNA = NM_001730
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 13
| Hs_GenLoc_start = 72530931
| Hs_GenLoc_end = 72549677
| Hs_Uniprot = Q13887
| Mm_EntrezGene = 12224
| Mm_Ensembl = ENSMUSG00000005148
| Mm_RefseqmRNA = NM_009769
| Mm_RefseqProtein = NP_033899
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 98181825
| Mm_GenLoc_end = 98196556
| Mm_Uniprot = Q923C0
}}
}}
'''Kruppel-like factor 5 (intestinal)''', also known as '''KLF5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KLF5 Kruppel-like factor 5 (intestinal)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=688| 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 Kruppel-like factor subfamily of zinc finger proteins. Since the protein localizes to the nucleus and binds the epidermal growth factor response element, it is thought to be a transcription factor.<ref name="entrez">{{cite web | title = Entrez Gene: KLF5 Kruppel-like factor 5 (intestinal)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=688| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nagai R, Suzuki T, Aizawa K, ''et al.'' |title=Significance of the transcription factor KLF5 in cardiovascular remodeling. |journal=J. Thromb. Haemost. |volume=3 |issue= 8 |pages= 1569-76 |year= 2005 |pmid= 16102021 |doi= 10.1111/j.1538-7836.2005.01366.x }}
*{{cite journal | author=Sogawa K, Imataka H, Yamasaki Y, ''et al.'' |title=cDNA cloning and transcriptional properties of a novel GC box-binding protein, BTEB2. |journal=Nucleic Acids Res. |volume=21 |issue= 7 |pages= 1527-32 |year= 1993 |pmid= 8479902 |doi= }}
*{{cite journal | author=Kojima S, Kobayashi A, Gotoh O, ''et al.'' |title=Transcriptional activation domain of human BTEB2, a GC box-binding factor. |journal=J. Biochem. |volume=121 |issue= 2 |pages= 389-96 |year= 1997 |pmid= 9089417 |doi= }}
*{{cite journal | author=Conkright MD, Wani MA, Anderson KP, Lingrel JB |title=A gene encoding an intestinal-enriched member of the Krüppel-like factor family expressed in intestinal epithelial cells. |journal=Nucleic Acids Res. |volume=27 |issue= 5 |pages= 1263-70 |year= 1999 |pmid= 9973612 |doi= }}
*{{cite journal | author=Shi H, Zhang Z, Wang X, ''et al.'' |title=Isolation and characterization of a gene encoding human Kruppel-like factor 5 (IKLF): binding to the CAAT/GT box of the mouse lactoferrin gene promoter. |journal=Nucleic Acids Res. |volume=27 |issue= 24 |pages= 4807-15 |year= 2000 |pmid= 10572182 |doi= }}
*{{cite journal | author=Hoshino Y, Kurabayashi M, Kanda T, ''et al.'' |title=Regulated expression of the BTEB2 transcription factor in vascular smooth muscle cells: analysis of developmental and pathological expression profiles shows implications as a predictive factor for restenosis. |journal=Circulation |volume=102 |issue= 20 |pages= 2528-34 |year= 2000 |pmid= 11076828 |doi= }}
*{{cite journal | author=Sun R, Chen X, Yang VW |title=Intestinal-enriched Krüppel-like factor (Krüppel-like factor 5) is a positive regulator of cellular proliferation. |journal=J. Biol. Chem. |volume=276 |issue= 10 |pages= 6897-900 |year= 2001 |pmid= 11152667 |doi= 10.1074/jbc.C000870200 }}
*{{cite journal | author=Shindo T, Manabe I, Fukushima Y, ''et al.'' |title=Krüppel-like zinc-finger transcription factor KLF5/BTEB2 is a target for angiotensin II signaling and an essential regulator of cardiovascular remodeling. |journal=Nat. Med. |volume=8 |issue= 8 |pages= 856-63 |year= 2002 |pmid= 12101409 |doi= 10.1038/nm738 }}
*{{cite journal | author=Sur I, Undén AB, Toftgård R |title=Human Krüppel-like factor5/KLF5: synergy with NF-kappaB/Rel factors and expression in human skin and hair follicles. |journal=Eur. J. Cell Biol. |volume=81 |issue= 6 |pages= 323-34 |year= 2003 |pmid= 12113473 |doi= }}
*{{cite journal | author=Chen C, Bhalala HV, Qiao H, Dong JT |title=A possible tumor suppressor role of the KLF5 transcription factor in human breast cancer. |journal=Oncogene |volume=21 |issue= 43 |pages= 6567-72 |year= 2002 |pmid= 12242654 |doi= 10.1038/sj.onc.1205817 }}
*{{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=Yang XO, Doty RT, Hicks JS, Willerford DM |title=Regulation of T-cell receptor D beta 1 promoter by KLF5 through reiterated GC-rich motifs. |journal=Blood |volume=101 |issue= 11 |pages= 4492-9 |year= 2003 |pmid= 12576331 |doi= 10.1182/blood-2002-08-2579 }}
*{{cite journal | author=Chen C, Bhalala HV, Vessella RL, Dong JT |title=KLF5 is frequently deleted and down-regulated but rarely mutated in prostate cancer. |journal=Prostate |volume=55 |issue= 2 |pages= 81-8 |year= 2003 |pmid= 12661032 |doi= 10.1002/pros.10205 }}
*{{cite journal | author=Zhang Z, Teng CT |title=Phosphorylation of Kruppel-like factor 5 (KLF5/IKLF) at the CBP interaction region enhances its transactivation function. |journal=Nucleic Acids Res. |volume=31 |issue= 8 |pages= 2196-208 |year= 2003 |pmid= 12682370 |doi= }}
*{{cite journal | author=Ohnishi S, Ohnami S, Laub F, ''et al.'' |title=Downregulation and growth inhibitory effect of epithelial-type Krüppel-like transcription factor KLF4, but not KLF5, in bladder cancer. |journal=Biochem. Biophys. Res. Commun. |volume=308 |issue= 2 |pages= 251-6 |year= 2003 |pmid= 12901861 |doi= }}
*{{cite journal | author=Aizawa K, Suzuki T, Kada N, ''et al.'' |title=Regulation of platelet-derived growth factor-A chain by Krüppel-like factor 5: new pathway of cooperative activation with nuclear factor-kappaB. |journal=J. Biol. Chem. |volume=279 |issue= 1 |pages= 70-6 |year= 2004 |pmid= 14573617 |doi= 10.1074/jbc.M306621200 }}
*{{cite journal | author=Sato T, Kanda T, Iida T, ''et al.'' |title=Immunohistochemical study of surgically excised choroidal neovascular membranes. |journal=J. Int. Med. Res. |volume=31 |issue= 5 |pages= 402-6 |year= 2004 |pmid= 14587307 |doi= }}
*{{cite journal | author=Miyamoto S, Suzuki T, Muto S, ''et al.'' |title=Positive and negative regulation of the cardiovascular transcription factor KLF5 by p300 and the oncogenic regulator SET through interaction and acetylation on the DNA-binding domain. |journal=Mol. Cell. Biol. |volume=23 |issue= 23 |pages= 8528-41 |year= 2003 |pmid= 14612398 |doi= }}
*{{cite journal | author=Bateman NW, Tan D, Pestell RG, ''et al.'' |title=Intestinal tumor progression is associated with altered function of KLF5. |journal=J. Biol. Chem. |volume=279 |issue= 13 |pages= 12093-101 |year= 2004 |pmid= 14726538 |doi= 10.1074/jbc.M311532200 }}
*{{cite journal | author=Nandan MO, Yoon HS, Zhao W, ''et al.'' |title=Krüppel-like factor 5 mediates the transforming activity of oncogenic H-Ras. |journal=Oncogene |volume=23 |issue= 19 |pages= 3404-13 |year= 2004 |pmid= 15077182 |doi= 10.1038/sj.onc.1207397 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KLK6... {November 19, 2007 11:51:56 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 11:52:40 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_KLK6_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1gvl.
| PDB = {{PDB2|1gvl}}, {{PDB2|1l2e}}, {{PDB2|1lo6}}
| Name = Kallikrein-related peptidase 6
| HGNCid = 6367
| Symbol = KLK6
| AltSymbols =; ZYME; Bssp; Klk7; MGC9355; NEUROSIN; PRSS18; PRSS9; SP59; hK6
| OMIM = 602652
| ECnumber =
| Homologene = 68279
| MGIid = 1343166
| GeneAtlas_image1 = PBB_GE_KLK6_204733_at_tn.png
| Function = {{GNF_GO|id=GO:0004252 |text = serine-type endopeptidase activity}} {{GNF_GO|id=GO:0004293 |text = tissue kallikrein activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007417 |text = central nervous system development}} {{GNF_GO|id=GO:0009611 |text = response to wounding}} {{GNF_GO|id=GO:0016540 |text = protein autoprocessing}} {{GNF_GO|id=GO:0030574 |text = collagen catabolic process}} {{GNF_GO|id=GO:0042246 |text = tissue regeneration}} {{GNF_GO|id=GO:0042445 |text = hormone metabolic process}} {{GNF_GO|id=GO:0042552 |text = myelination}} {{GNF_GO|id=GO:0042982 |text = amyloid precursor protein metabolic process}} {{GNF_GO|id=GO:0045595 |text = regulation of cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5653
| Hs_Ensembl = ENSG00000167755
| Hs_RefseqProtein = NP_001012982
| Hs_RefseqmRNA = NM_001012964
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 56153700
| Hs_GenLoc_end = 56164741
| Hs_Uniprot = Q92876
| Mm_EntrezGene = 19144
| Mm_Ensembl = ENSMUSG00000050063
| Mm_RefseqmRNA = NM_011177
| Mm_RefseqProtein = NP_035307
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 43692600
| Mm_GenLoc_end = 43699828
| Mm_Uniprot =
}}
}}
'''Kallikrein-related peptidase 6''', also known as '''KLK6''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KLK6 kallikrein-related peptidase 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5653| 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 = Kallikreins are a subgroup of serine proteases having diverse physiological functions. Growing evidence suggests that many kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers. This gene is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. The encoded enzyme is regulated by steroid hormones. In tissue culture, the enzyme has been found to generate amyloidogenic fragments from the amyloid precursor protein, suggesting a potential for involvement in Alzheimer's disease. Multiple alternatively spliced transcript variants that encode different isoforms have been identified for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: KLK6 kallikrein-related peptidase 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5653| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Yousef GM, Kishi T, Diamandis EP |title=Role of kallikrein enzymes in the central nervous system. |journal=Clin. Chim. Acta |volume=329 |issue= 1-2 |pages= 1-8 |year= 2003 |pmid= 12589961 |doi= }}
*{{cite journal | author=Anisowicz A, Sotiropoulou G, Stenman G, ''et al.'' |title=A novel protease homolog differentially expressed in breast and ovarian cancer. |journal=Mol. Med. |volume=2 |issue= 5 |pages= 624-36 |year= 1997 |pmid= 8898378 |doi= }}
*{{cite journal | author=Yamashiro K, Tsuruoka N, Kodama S, ''et al.'' |title=Molecular cloning of a novel trypsin-like serine protease (neurosin) preferentially expressed in brain. |journal=Biochim. Biophys. Acta |volume=1350 |issue= 1 |pages= 11-4 |year= 1997 |pmid= 9003450 |doi= }}
*{{cite journal | author=Little SP, Dixon EP, Norris F, ''et al.'' |title=Zyme, a novel and potentially amyloidogenic enzyme cDNA isolated from Alzheimer's disease brain. |journal=J. Biol. Chem. |volume=272 |issue= 40 |pages= 25135-42 |year= 1997 |pmid= 9312124 |doi= }}
*{{cite journal | author=Yousef GM, Luo LY, Scherer SW, ''et al.'' |title=Molecular characterization of zyme/protease M/neurosin (PRSS9), a hormonally regulated kallikrein-like serine protease. |journal=Genomics |volume=62 |issue= 2 |pages= 251-9 |year= 2000 |pmid= 10610719 |doi= 10.1006/geno.1999.6012 }}
*{{cite journal | author=Gan L, Lee I, Smith R, ''et al.'' |title=Sequencing and expression analysis of the serine protease gene cluster located in chromosome 19q13 region. |journal=Gene |volume=257 |issue= 1 |pages= 119-30 |year= 2001 |pmid= 11054574 |doi= }}
*{{cite journal | author=Petraki CD, Karavana VN, Skoufogiannis PT, ''et al.'' |title=The spectrum of human kallikrein 6 (zyme/protease M/neurosin) expression in human tissues as assessed by immunohistochemistry. |journal=J. Histochem. Cytochem. |volume=49 |issue= 11 |pages= 1431-41 |year= 2001 |pmid= 11668196 |doi= }}
*{{cite journal | author=Bernett MJ, Blaber SI, Scarisbrick IA, ''et al.'' |title=Crystal structure and biochemical characterization of human kallikrein 6 reveals that a trypsin-like kallikrein is expressed in the central nervous system. |journal=J. Biol. Chem. |volume=277 |issue= 27 |pages= 24562-70 |year= 2002 |pmid= 11983703 |doi= 10.1074/jbc.M202392200 }}
*{{cite journal | author=Gomis-Rüth FX, Bayés A, Sotiropoulou G, ''et al.'' |title=The structure of human prokallikrein 6 reveals a novel activation mechanism for the kallikrein family. |journal=J. Biol. Chem. |volume=277 |issue= 30 |pages= 27273-81 |year= 2002 |pmid= 12016211 |doi= 10.1074/jbc.M201534200 }}
*{{cite journal | author=Scarisbrick IA, Blaber SI, Lucchinetti CF, ''et al.'' |title=Activity of a newly identified serine protease in CNS demyelination. |journal=Brain |volume=125 |issue= Pt 6 |pages= 1283-96 |year= 2002 |pmid= 12023317 |doi= }}
*{{cite journal | author=Zarghooni M, Soosaipillai A, Grass L, ''et al.'' |title=Decreased concentration of human kallikrein 6 in brain extracts of Alzheimer's disease patients. |journal=Clin. Biochem. |volume=35 |issue= 3 |pages= 225-31 |year= 2002 |pmid= 12074831 |doi= }}
*{{cite journal | author=Hoffman BR, Katsaros D, Scorilas A, ''et al.'' |title=Immunofluorometric quantitation and histochemical localisation of kallikrein 6 protein in ovarian cancer tissue: a new independent unfavourable prognostic biomarker. |journal=Br. J. Cancer |volume=87 |issue= 7 |pages= 763-71 |year= 2002 |pmid= 12232761 |doi= 10.1038/sj.bjc.6600533 }}
*{{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=Mitsui S, Okui A, Uemura H, ''et al.'' |title=Decreased cerebrospinal fluid levels of neurosin (KLK6), an aging-related protease, as a possible new risk factor for Alzheimer's disease. |journal=Ann. N. Y. Acad. Sci. |volume=977 |issue= |pages= 216-23 |year= 2003 |pmid= 12480753 |doi= }}
*{{cite journal | author=Hutchinson S, Luo LY, Yousef GM, ''et al.'' |title=Purification of human kallikrein 6 from biological fluids and identification of its complex with alpha(1)-antichymotrypsin. |journal=Clin. Chem. |volume=49 |issue= 5 |pages= 746-51 |year= 2003 |pmid= 12709365 |doi= }}
*{{cite journal | author=Magklara A, Mellati AA, Wasney GA, ''et al.'' |title=Characterization of the enzymatic activity of human kallikrein 6: Autoactivation, substrate specificity, and regulation by inhibitors. |journal=Biochem. Biophys. Res. Commun. |volume=307 |issue= 4 |pages= 948-55 |year= 2003 |pmid= 12878203 |doi= }}
*{{cite journal | author=Iwata A, Maruyama M, Akagi T, ''et al.'' |title=Alpha-synuclein degradation by serine protease neurosin: implication for pathogenesis of synucleinopathies. |journal=Hum. Mol. Genet. |volume=12 |issue= 20 |pages= 2625-35 |year= 2004 |pmid= 12928483 |doi= 10.1093/hmg/ddg283 }}
*{{cite journal | author=Sauter ER, Lininger J, Magklara A, ''et al.'' |title=Association of kallikrein expression in nipple aspirate fluid with breast cancer risk. |journal=Int. J. Cancer |volume=108 |issue= 4 |pages= 588-91 |year= 2004 |pmid= 14696124 |doi= 10.1002/ijc.11607 }}
*{{cite journal | author=Pampalakis G, Kurlender L, Diamandis EP, Sotiropoulou G |title=Cloning and characterization of novel isoforms of the human kallikrein 6 gene. |journal=Biochem. Biophys. Res. Commun. |volume=320 |issue= 1 |pages= 54-61 |year= 2004 |pmid= 15207701 |doi= 10.1016/j.bbrc.2004.04.205 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on OCA2... {November 19, 2007 11:47:52 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 11:48:25 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Oculocutaneous albinism II (pink-eye dilution homolog, mouse)
| HGNCid = 8101
| Symbol = OCA2
| AltSymbols =; BOCA; D15S12; P; PED
| OMIM = 203200
| ECnumber =
| Homologene = 37281
| MGIid = 97454
| GeneAtlas_image1 = PBB_GE_OCA2_206498_at_tn.png
| Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005302 |text = L-tyrosine transmembrane transporter activity}} {{GNF_GO|id=GO:0005395 |text = eye pigment precursor transporter activity}} {{GNF_GO|id=GO:0015105 |text = arsenite transmembrane transporter activity}} {{GNF_GO|id=GO:0015137 |text = citrate transmembrane transporter activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006726 |text = eye pigment biosynthetic process}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0007286 |text = spermatid development}} {{GNF_GO|id=GO:0015746 |text = citrate transport}} {{GNF_GO|id=GO:0048066 |text = pigmentation during development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4948
| Hs_Ensembl = ENSG00000104044
| Hs_RefseqProtein = NP_000266
| Hs_RefseqmRNA = NM_000275
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 25673628
| Hs_GenLoc_end = 26018061
| Hs_Uniprot = Q04671
| Mm_EntrezGene = 18431
| Mm_Ensembl = ENSMUSG00000030450
| Mm_RefseqmRNA = NM_021879
| Mm_RefseqProtein = NP_068679
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 56107790
| Mm_GenLoc_end = 56404536
| Mm_Uniprot = Q0VBP9
}}
}}
'''Oculocutaneous albinism II (pink-eye dilution homolog, mouse)''', also known as '''OCA2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: OCA2 oculocutaneous albinism II (pink-eye dilution homolog, mouse)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4948| 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 = OCA2 encodes the human homologue of the mouse p (pink-eyed dilution) gene. The P protein is believed to be an integral membrane protein involved in small molecule transport, specifically tyrosine - a precursor of melanin. Mutations in OCA2 result in type 2 oculocutaneous albinism.<ref name="entrez">{{cite web | title = Entrez Gene: OCA2 oculocutaneous albinism II (pink-eye dilution homolog, mouse)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4948| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Oetting WS, King RA |title=Molecular basis of albinism: mutations and polymorphisms of pigmentation genes associated with albinism. |journal=Hum. Mutat. |volume=13 |issue= 2 |pages= 99-115 |year= 1999 |pmid= 10094567 |doi= 10.1002/(SICI)1098-1004(1999)13:2<99::AID-HUMU2>3.0.CO;2-C }}
*{{cite journal | author=Brilliant MH |title=The mouse p (pink-eyed dilution) and human P genes, oculocutaneous albinism type 2 (OCA2), and melanosomal pH. |journal=Pigment Cell Res. |volume=14 |issue= 2 |pages= 86-93 |year= 2001 |pmid= 11310796 |doi= }}
*{{cite journal | author=Ramsay M, Colman MA, Stevens G, ''et al.'' |title=The tyrosinase-positive oculocutaneous albinism locus maps to chromosome 15q11.2-q12. |journal=Am. J. Hum. Genet. |volume=51 |issue= 4 |pages= 879-84 |year= 1992 |pmid= 1415228 |doi= }}
*{{cite journal | author=Gardner JM, Nakatsu Y, Gondo Y, ''et al.'' |title=The mouse pink-eyed dilution gene: association with human Prader-Willi and Angelman syndromes. |journal=Science |volume=257 |issue= 5073 |pages= 1121-4 |year= 1992 |pmid= 1509264 |doi= }}
*{{cite journal | author=Ludowese CJ, Thompson KJ, Sekhon GS, Pauli RM |title=Absence of predictable phenotypic expression in proximal 15q duplications. |journal=Clin. Genet. |volume=40 |issue= 3 |pages= 194-201 |year= 1992 |pmid= 1773534 |doi= }}
*{{cite journal | author=Lee ST, Nicholls RD, Jong MT, ''et al.'' |title=Organization and sequence of the human P gene and identification of a new family of transport proteins. |journal=Genomics |volume=26 |issue= 2 |pages= 354-63 |year= 1995 |pmid= 7601462 |doi= }}
*{{cite journal | author=Spritz RA, Fukai K, Holmes SA, Luande J |title=Frequent intragenic deletion of the P gene in Tanzanian patients with type II oculocutaneous albinism (OCA2). |journal=Am. J. Hum. Genet. |volume=56 |issue= 6 |pages= 1320-3 |year= 1995 |pmid= 7762554 |doi= }}
*{{cite journal | author=Lee ST, Nicholls RD, Schnur RE, ''et al.'' |title=Diverse mutations of the P gene among African-Americans with type II (tyrosinase-positive) oculocutaneous albinism (OCA2). |journal=Hum. Mol. Genet. |volume=3 |issue= 11 |pages= 2047-51 |year= 1995 |pmid= 7874125 |doi= }}
*{{cite journal | author=Durham-Pierre D, Gardner JM, Nakatsu Y, ''et al.'' |title=African origin of an intragenic deletion of the human P gene in tyrosinase positive oculocutaneous albinism. |journal=Nat. Genet. |volume=7 |issue= 2 |pages= 176-9 |year= 1994 |pmid= 7920637 |doi= 10.1038/ng0694-176 }}
*{{cite journal | author=Lee ST, Nicholls RD, Bundey S, ''et al.'' |title=Mutations of the P gene in oculocutaneous albinism, ocular albinism, and Prader-Willi syndrome plus albinism. |journal=N. Engl. J. Med. |volume=330 |issue= 8 |pages= 529-34 |year= 1994 |pmid= 8302318 |doi= }}
*{{cite journal | author=Rinchik EM, Bultman SJ, Horsthemke B, ''et al.'' |title=A gene for the mouse pink-eyed dilution locus and for human type II oculocutaneous albinism. |journal=Nature |volume=361 |issue= 6407 |pages= 72-6 |year= 1993 |pmid= 8421497 |doi= 10.1038/361072a0 }}
*{{cite journal | author=Spritz RA, Lee ST, Fukai K, ''et al.'' |title=Novel mutations of the P gene in type II oculocutaneous albinism (OCA2). |journal=Hum. Mutat. |volume=10 |issue= 2 |pages= 175-7 |year= 1997 |pmid= 9259203 |doi= 10.1002/(SICI)1098-1004(1997)10:2<175::AID-HUMU12>3.0.CO;2-X }}
*{{cite journal | author=Kerr R, Stevens G, Manga P, ''et al.'' |title=Identification of P gene mutations in individuals with oculocutaneous albinism in sub-Saharan Africa. |journal=Hum. Mutat. |volume=15 |issue= 2 |pages= 166-72 |year= 2000 |pmid= 10649493 |doi= 10.1002/(SICI)1098-1004(200002)15:2<166::AID-HUMU5>3.0.CO;2-Z }}
*{{cite journal | author=Oetting WS, Gardner JM, Fryer JP, ''et al.'' |title=Mutations of the human P gene associated with Type II oculocutaneous albinism (OCA2). Mutations in brief no. 205. Online. |journal=Hum. Mutat. |volume=12 |issue= 6 |pages= 434 |year= 2000 |pmid= 10671067 |doi= 10.1002/(SICI)1098-1004(1998)12:6<434::AID-HUMU16>3.0.CO;2-7 }}
*{{cite journal | author=Passmore LA, Kaesmann-Kellner B, Weber BH |title=Novel and recurrent mutations in the tyrosinase gene and the P gene in the German albino population. |journal=Hum. Genet. |volume=105 |issue= 3 |pages= 200-10 |year= 2000 |pmid= 10987646 |doi= }}
*{{cite journal | author=Manga P, Kromberg J, Turner A, ''et al.'' |title=In Southern Africa, brown oculocutaneous albinism (BOCA) maps to the OCA2 locus on chromosome 15q: P-gene mutations identified. |journal=Am. J. Hum. Genet. |volume=68 |issue= 3 |pages= 782-7 |year= 2001 |pmid= 11179026 |doi= }}
*{{cite journal | author=Manga P, Orlow SJ |title=Inverse correlation between pink-eyed dilution protein expression and induction of melanogenesis by bafilomycin A1. |journal=Pigment Cell Res. |volume=14 |issue= 5 |pages= 362-7 |year= 2002 |pmid= 11601658 |doi= }}
*{{cite journal | author=Toyofuku K, Valencia JC, Kushimoto T, ''et al.'' |title=The etiology of oculocutaneous albinism (OCA) type II: the pink protein modulates the processing and transport of tyrosinase. |journal=Pigment Cell Res. |volume=15 |issue= 3 |pages= 217-24 |year= 2002 |pmid= 12028586 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PA2G4... {November 19, 2007 11:48:26 AM PST}
- SEARCH REDIRECT: Control Box Found: PA2G4 {November 19, 2007 11:49:07 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 11:49:10 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 11:49:10 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 11:49:10 AM PST}
- UPDATED: Updated protein page: PA2G4 {November 19, 2007 11:49:16 AM PST}
- INFO: Beginning work on PDZK1... {November 19, 2007 11:49:16 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 11:49:42 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- 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 = PDZ domain containing 1
| HGNCid = 8821
| Symbol = PDZK1
| AltSymbols =; CAP70; CLAMP; PDZD1
| OMIM = 603831
| ECnumber =
| Homologene = 1964
| MGIid = 1928901
| Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008022 |text = protein C-terminus binding}} {{GNF_GO|id=GO:0030165 |text = PDZ domain binding}}
| Component =
| Process = {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0015893 |text = drug transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5174
| Hs_Ensembl =
| Hs_RefseqProtein = XP_001126677
| Hs_RefseqmRNA = XM_001126677
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 59020
| Mm_Ensembl = ENSMUSG00000038298
| Mm_RefseqmRNA = NM_021517
| Mm_RefseqProtein = NP_067492
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 96935635
| Mm_GenLoc_end = 96955568
| Mm_Uniprot = Q9JIL4
}}
}}
'''PDZ domain containing 1''', also known as '''PDZK1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PDZK1 PDZ domain containing 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5174| 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=Kocher O, Comella N, Tognazzi K, Brown LF |title=Identification and partial characterization of PDZK1: a novel protein containing PDZ interaction domains. |journal=Lab. Invest. |volume=78 |issue= 1 |pages= 117-25 |year= 1998 |pmid= 9461128 |doi= }}
*{{cite journal | author=White KE, Biber J, Murer H, Econs MJ |title=A PDZ domain-containing protein with homology to Diphor-1 maps to human chromosome 1q21. |journal=Ann. Hum. Genet. |volume=62 |issue= Pt 4 |pages= 287-90 |year= 1999 |pmid= 9924606 |doi= 10.1046/j.1469-1809.1998.6240287.x }}
*{{cite journal | author=Kocher O, Comella N, Gilchrist A, ''et al.'' |title=PDZK1, a novel PDZ domain-containing protein up-regulated in carcinomas and mapped to chromosome 1q21, interacts with cMOAT (MRP2), the multidrug resistance-associated protein. |journal=Lab. Invest. |volume=79 |issue= 9 |pages= 1161-70 |year= 1999 |pmid= 10496535 |doi= }}
*{{cite journal | author=Ikemoto M, Arai H, Feng D, ''et al.'' |title=Identification of a PDZ-domain-containing protein that interacts with the scavenger receptor class B type I. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 12 |pages= 6538-43 |year= 2000 |pmid= 10829064 |doi= 10.1073/pnas.100114397 }}
*{{cite journal | author=Wang S, Yue H, Derin RB, ''et al.'' |title=Accessory protein facilitated CFTR-CFTR interaction, a molecular mechanism to potentiate the chloride channel activity. |journal=Cell |volume=103 |issue= 1 |pages= 169-79 |year= 2000 |pmid= 11051556 |doi= }}
*{{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=Gisler SM, Stagljar I, Traebert M, ''et al.'' |title=Interaction of the type IIa Na/Pi cotransporter with PDZ proteins. |journal=J. Biol. Chem. |volume=276 |issue= 12 |pages= 9206-13 |year= 2001 |pmid= 11099500 |doi= 10.1074/jbc.M008745200 }}
*{{cite journal | author=Silver DL |title=A carboxyl-terminal PDZ-interacting domain of scavenger receptor B, type I is essential for cell surface expression in liver. |journal=J. Biol. Chem. |volume=277 |issue= 37 |pages= 34042-7 |year= 2002 |pmid= 12119305 |doi= 10.1074/jbc.M206584200 }}
*{{cite journal | author=Sellin L, Huber TB, Gerke P, ''et al.'' |title=NEPH1 defines a novel family of podocin interacting proteins. |journal=FASEB J. |volume=17 |issue= 1 |pages= 115-7 |year= 2003 |pmid= 12424224 |doi= 10.1096/fj.02-0242fje }}
*{{cite journal | author=Gentzsch M, Cui L, Mengos A, ''et al.'' |title=The PDZ-binding chloride channel ClC-3B localizes to the Golgi and associates with cystic fibrosis transmembrane conductance regulator-interacting PDZ proteins. |journal=J. Biol. Chem. |volume=278 |issue= 8 |pages= 6440-9 |year= 2003 |pmid= 12471024 |doi= 10.1074/jbc.M211050200 }}
*{{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=Hegedüs T, Sessler T, Scott R, ''et al.'' |title=C-terminal phosphorylation of MRP2 modulates its interaction with PDZ proteins. |journal=Biochem. Biophys. Res. Commun. |volume=302 |issue= 3 |pages= 454-61 |year= 2003 |pmid= 12615054 |doi= }}
*{{cite journal | author=Silver DL, Wang N, Vogel S |title=Identification of small PDZK1-associated protein, DD96/MAP17, as a regulator of PDZK1 and plasma high density lipoprotein levels. |journal=J. Biol. Chem. |volume=278 |issue= 31 |pages= 28528-32 |year= 2003 |pmid= 12754212 |doi= 10.1074/jbc.M304109200 }}
*{{cite journal | author=Pribanic S, Gisler SM, Bacic D, ''et al.'' |title=Interactions of MAP17 with the NaPi-IIa/PDZK1 protein complex in renal proximal tubular cells. |journal=Am. J. Physiol. Renal Physiol. |volume=285 |issue= 4 |pages= F784-91 |year= 2003 |pmid= 12837682 |doi= 10.1152/ajprenal.00109.2003 }}
*{{cite journal | author=Gisler SM, Pribanic S, Bacic D, ''et al.'' |title=PDZK1: I. a major scaffolder in brush borders of proximal tubular cells. |journal=Kidney Int. |volume=64 |issue= 5 |pages= 1733-45 |year= 2004 |pmid= 14531806 |doi= 10.1046/j.1523-1755.2003.00266.x }}
*{{cite journal | author=Kocher O, Yesilaltay A, Cirovic C, ''et al.'' |title=Targeted disruption of the PDZK1 gene in mice causes tissue-specific depletion of the high density lipoprotein receptor scavenger receptor class B type I and altered lipoprotein metabolism. |journal=J. Biol. Chem. |volume=278 |issue= 52 |pages= 52820-5 |year= 2004 |pmid= 14551195 |doi= 10.1074/jbc.M310482200 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Inoue J, Otsuki T, Hirasawa A, ''et al.'' |title=Overexpression of PDZK1 within the 1q12-q22 amplicon is likely to be associated with drug-resistance phenotype in multiple myeloma. |journal=Am. J. Pathol. |volume=165 |issue= 1 |pages= 71-81 |year= 2004 |pmid= 15215163 |doi= }}
*{{cite journal | author=Anzai N, Miyazaki H, Noshiro R, ''et al.'' |title=The multivalent PDZ domain-containing protein PDZK1 regulates transport activity of renal urate-anion exchanger URAT1 via its C terminus. |journal=J. Biol. Chem. |volume=279 |issue= 44 |pages= 45942-50 |year= 2004 |pmid= 15304510 |doi= 10.1074/jbc.M406724200 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on POLK... {November 19, 2007 12:01:38 PM PST}
- SEARCH REDIRECT: Control Box Found: POLK {November 19, 2007 12:02:39 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:02:41 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:02:41 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:02:41 PM PST}
- UPDATED: Updated protein page: POLK {November 19, 2007 12:02:47 PM PST}
- INFO: Beginning work on PPP1CB... {November 19, 2007 11:50:21 AM PST}
- SEARCH REDIRECT: Control Box Found: PPP1CB {November 19, 2007 11:50:46 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 11:50:47 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 11:50:47 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 11:50:47 AM PST}
- UPDATED: Updated protein page: PPP1CB {November 19, 2007 11:50:53 AM PST}
- INFO: Beginning work on PPP1R12A... {November 19, 2007 11:47:19 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 11:47:51 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PPP1R12A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1s70.
| PDB = {{PDB2|1s70}}
| Name = Protein phosphatase 1, regulatory (inhibitor) subunit 12A
| HGNCid = 7618
| Symbol = PPP1R12A
| AltSymbols =; MBS; MGC133042; MYPT1
| OMIM = 602021
| ECnumber =
| Homologene = 1855
| MGIid = 1309528
| GeneAtlas_image1 = PBB_GE_PPP1R12A_201603_at_tn.png
| GeneAtlas_image2 = PBB_GE_PPP1R12A_201602_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_PPP1R12A_201604_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004871 |text = signal transducer activity}}
| Component = {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}}
| Process = {{GNF_GO|id=GO:0006937 |text = regulation of muscle contraction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4659
| Hs_Ensembl = ENSG00000058272
| Hs_RefseqProtein = NP_002471
| Hs_RefseqmRNA = NM_002480
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 78692317
| Hs_GenLoc_end = 78853366
| Hs_Uniprot = O14974
| Mm_EntrezGene = 17931
| Mm_Ensembl = ENSMUSG00000019907
| Mm_RefseqmRNA = XM_001004092
| Mm_RefseqProtein = XP_001004092
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 107566510
| Mm_GenLoc_end = 107681685
| Mm_Uniprot = Q05A74
}}
}}
'''Protein phosphatase 1, regulatory (inhibitor) subunit 12A''', also known as '''PPP1R12A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PPP1R12A protein phosphatase 1, regulatory (inhibitor) subunit 12A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4659| 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 = Myosin phosphatase target subunit 1, which is also called the myosin-binding subunit of myosin phosphatase, is one of the subunits of myosin phosphatase. Myosin phosphatase regulates the interaction of actin and myosin downstream of the guanosine triphosphatase Rho. The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate (GTP)-bound, active form of RhoA (GTP.RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP. RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase. Overexpression of RhoA or activated RhoA in NIH 3T3 cells increased phosphorylation of MBS and MLC. Thus, Rho appears to inhibit myosin phosphatase through the action of Rho-kinase.<ref name="entrez">{{cite web | title = Entrez Gene: PPP1R12A protein phosphatase 1, regulatory (inhibitor) subunit 12A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4659| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Somlyo AP, Wu X, Walker LA, Somlyo AV |title=Pharmacomechanical coupling: the role of calcium, G-proteins, kinases and phosphatases. |journal=Rev. Physiol. Biochem. Pharmacol. |volume=134 |issue= |pages= 201-34 |year= 1999 |pmid= 10087910 |doi= }}
*{{cite journal | author=Ziter FA, Wiser WC, Robinson A |title=Three-generation pedigree of a Möbius syndrome variant with chromosome translocation. |journal=Arch. Neurol. |volume=34 |issue= 7 |pages= 437-42 |year= 1977 |pmid= 880069 |doi= }}
*{{cite journal | author=Slee JJ, Smart RD, Viljoen DL |title=Deletion of chromosome 13 in Moebius syndrome. |journal=J. Med. Genet. |volume=28 |issue= 6 |pages= 413-4 |year= 1991 |pmid= 1870098 |doi= }}
*{{cite journal | author=Kimura K, Ito M, Amano M, ''et al.'' |title=Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase) |journal=Science |volume=273 |issue= 5272 |pages= 245-8 |year= 1996 |pmid= 8662509 |doi= }}
*{{cite journal | author=Ito M, Feng J, Tsujino S, ''et al.'' |title=Interaction of smooth muscle myosin phosphatase with phospholipids. |journal=Biochemistry |volume=36 |issue= 24 |pages= 7607-14 |year= 1997 |pmid= 9200713 |doi= 10.1021/bi9702647 }}
*{{cite journal | author=Takahashi N, Ito M, Tanaka J, ''et al.'' |title=Localization of the gene coding for myosin phosphatase, target subunit 1 (MYPT1) to human chromosome 12q15-q21. |journal=Genomics |volume=44 |issue= 1 |pages= 150-2 |year= 1997 |pmid= 9286714 |doi= 10.1006/geno.1997.4859 }}
*{{cite journal | author=Nakai K, Suzuki Y, Kihira H, ''et al.'' |title=Regulation of myosin phosphatase through phosphorylation of the myosin-binding subunit in platelet activation. |journal=Blood |volume=90 |issue= 10 |pages= 3936-42 |year= 1997 |pmid= 9354661 |doi= }}
*{{cite journal | author=Somlyo AP |title=Kinases, myosin phosphatase and Rho proteins: curiouser and curiouser. |journal=J. Physiol. (Lond.) |volume=516 ( Pt 3) |issue= |pages= 630 |year= 1999 |pmid= 10200412 |doi= }}
*{{cite journal | author=Surks HK, Mochizuki N, Kasai Y, ''et al.'' |title=Regulation of myosin phosphatase by a specific interaction with cGMP- dependent protein kinase Ialpha. |journal=Science |volume=286 |issue= 5444 |pages= 1583-7 |year= 1999 |pmid= 10567269 |doi= }}
*{{cite journal | author=Feng J, Ito M, Ichikawa K, ''et al.'' |title=Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase. |journal=J. Biol. Chem. |volume=274 |issue= 52 |pages= 37385-90 |year= 2000 |pmid= 10601309 |doi= }}
*{{cite journal | author=Arimura T, Suematsu N, Zhou YB, ''et al.'' |title=Identification, characterization, and functional analysis of heart-specific myosin light chain phosphatase small subunit. |journal=J. Biol. Chem. |volume=276 |issue= 9 |pages= 6073-82 |year= 2001 |pmid= 11067852 |doi= 10.1074/jbc.M008566200 }}
*{{cite journal | author=Sebbagh M, Renvoizé C, Hamelin J, ''et al.'' |title=Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing. |journal=Nat. Cell Biol. |volume=3 |issue= 4 |pages= 346-52 |year= 2001 |pmid= 11283607 |doi= 10.1038/35070019 }}
*{{cite journal | author=Murányi A, Zhang R, Liu F, ''et al.'' |title=Myotonic dystrophy protein kinase phosphorylates the myosin phosphatase targeting subunit and inhibits myosin phosphatase activity. |journal=FEBS Lett. |volume=493 |issue= 2-3 |pages= 80-4 |year= 2001 |pmid= 11287000 |doi= }}
*{{cite journal | author=Machida H, Ito M, Okamoto R, ''et al.'' |title=Molecular cloning and analysis of the 5'-flanking region of the human MYPT1 gene. |journal=Biochim. Biophys. Acta |volume=1517 |issue= 3 |pages= 424-9 |year= 2001 |pmid= 11342221 |doi= }}
*{{cite journal | author=Kiss E, Murányi A, Csortos C, ''et al.'' |title=Integrin-linked kinase phosphorylates the myosin phosphatase target subunit at the inhibitory site in platelet cytoskeleton. |journal=Biochem. J. |volume=365 |issue= Pt 1 |pages= 79-87 |year= 2002 |pmid= 11931630 |doi= 10.1042/BJ20011295 }}
*{{cite journal | author=Velasco G, Armstrong C, Morrice N, ''et al.'' |title=Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1M at Thr850 induces its dissociation from myosin. |journal=FEBS Lett. |volume=527 |issue= 1-3 |pages= 101-4 |year= 2002 |pmid= 12220642 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Kitazawa T, Eto M, Woodsome TP, Khalequzzaman M |title=Phosphorylation of the myosin phosphatase targeting subunit and CPI-17 during Ca2+ sensitization in rabbit smooth muscle. |journal=J. Physiol. (Lond.) |volume=546 |issue= Pt 3 |pages= 879-89 |year= 2003 |pmid= 12563012 |doi= }}
*{{cite journal | author=Seko T, Ito M, Kureishi Y, ''et al.'' |title=Activation of RhoA and inhibition of myosin phosphatase as important components in hypertension in vascular smooth muscle. |journal=Circ. Res. |volume=92 |issue= 4 |pages= 411-8 |year= 2003 |pmid= 12600888 |doi= 10.1161/01.RES.0000059987.90200.44 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PPP2R2A... {November 19, 2007 11:50:53 AM PST}
- SEARCH REDIRECT: Control Box Found: PPP2R2A {November 19, 2007 11:51:47 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 11:51:50 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 11:51:50 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 11:51:50 AM PST}
- UPDATED: Updated protein page: PPP2R2A {November 19, 2007 11:51:56 AM PST}
- INFO: Beginning work on PTGER2... {November 19, 2007 11:52:40 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 11:53:15 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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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 = Prostaglandin E receptor 2 (subtype EP2), 53kDa
| HGNCid = 9594
| Symbol = PTGER2
| AltSymbols =; EP2
| OMIM = 176804
| ECnumber =
| Homologene = 739
| MGIid = 97794
| GeneAtlas_image1 = PBB_GE_PTGER2_206631_at_tn.png
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004957 |text = prostaglandin E receptor activity}} {{GNF_GO|id=GO:0004960 |text = thromboxane receptor activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5732
| Hs_Ensembl = ENSG00000125384
| Hs_RefseqProtein = NP_000947
| Hs_RefseqmRNA = NM_000956
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 51850863
| Hs_GenLoc_end = 51865062
| Hs_Uniprot = P43116
| Mm_EntrezGene = 19217
| Mm_Ensembl = ENSMUSG00000037759
| Mm_RefseqmRNA = NM_008964
| Mm_RefseqProtein = NP_032990
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 43910072
| Mm_GenLoc_end = 43925090
| Mm_Uniprot = Q3UW60
}}
}}
'''Prostaglandin E receptor 2 (subtype EP2), 53kDa''', also known as '''PTGER2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTGER2 prostaglandin E receptor 2 (subtype EP2), 53kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5732| 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=Duncan AM, Anderson LL, Funk CD, ''et al.'' |title=Chromosomal localization of the human prostanoid receptor gene family. |journal=Genomics |volume=25 |issue= 3 |pages= 740-2 |year= 1995 |pmid= 7759114 |doi= }}
*{{cite journal | author=Regan JW, Bailey TJ, Pepperl DJ, ''et al.'' |title=Cloning of a novel human prostaglandin receptor with characteristics of the pharmacologically defined EP2 subtype. |journal=Mol. Pharmacol. |volume=46 |issue= 2 |pages= 213-20 |year= 1994 |pmid= 8078484 |doi= }}
*{{cite journal | author=Bastien L, Sawyer N, Grygorczyk R, ''et al.'' |title=Cloning, functional expression, and characterization of the human prostaglandin E2 receptor EP2 subtype. |journal=J. Biol. Chem. |volume=269 |issue= 16 |pages= 11873-7 |year= 1994 |pmid= 8163486 |doi= }}
*{{cite journal | author=An S, Yang J, Xia M, Goetzl EJ |title=Cloning and expression of the EP2 subtype of human receptors for prostaglandin E2. |journal=Biochem. Biophys. Res. Commun. |volume=197 |issue= 1 |pages= 263-70 |year= 1994 |pmid= 8250933 |doi= }}
*{{cite journal | author=Stillman BA, Breyer MD, Breyer RM |title=Importance of the extracellular domain for prostaglandin EP(2) receptor function. |journal=Mol. Pharmacol. |volume=56 |issue= 3 |pages= 545-51 |year= 1999 |pmid= 10462542 |doi= }}
*{{cite journal | author=Smock SL, Pan LC, Castleberry TA, ''et al.'' |title=Cloning, structural characterization, and chromosomal localization of the gene encoding the human prostaglandin E(2) receptor EP2 subtype. |journal=Gene |volume=237 |issue= 2 |pages= 393-402 |year= 1999 |pmid= 10521663 |doi= }}
*{{cite journal | author=Desai S, April H, Nwaneshiudu C, Ashby B |title=Comparison of agonist-induced internalization of the human EP2 and EP4 prostaglandin receptors: role of the carboxyl terminus in EP4 receptor sequestration. |journal=Mol. Pharmacol. |volume=58 |issue= 6 |pages= 1279-86 |year= 2001 |pmid= 11093764 |doi= }}
*{{cite journal | author=Duckworth N, Marshall K, Clayton JK |title=An investigation of the effect of the prostaglandin EP2 receptor agonist, butaprost, on the human isolated myometrium from pregnant and non-pregnant women. |journal=J. Endocrinol. |volume=172 |issue= 2 |pages= 263-9 |year= 2002 |pmid= 11834444 |doi= }}
*{{cite journal | author=Kyveris A, Maruscak E, Senchyna M |title=Optimization of RNA isolation from human ocular tissues and analysis of prostanoid receptor mRNA expression using RT-PCR. |journal=Mol. Vis. |volume=8 |issue= |pages= 51-8 |year= 2002 |pmid= 11951086 |doi= }}
*{{cite journal | author=Takafuji VA, Evans A, Lynch KR, Roche JK |title=PGE(2) receptors and synthesis in human gastric mucosa: perturbation in cancer. |journal=Prostaglandins Leukot. Essent. Fatty Acids |volume=66 |issue= 1 |pages= 71-81 |year= 2003 |pmid= 12051958 |doi= 10.1054/plef.2001.0299 }}
*{{cite journal | author=Scandella E, Men Y, Gillessen S, ''et al.'' |title=Prostaglandin E2 is a key factor for CCR7 surface expression and migration of monocyte-derived dendritic cells. |journal=Blood |volume=100 |issue= 4 |pages= 1354-61 |year= 2002 |pmid= 12149218 |doi= 10.1182/blood-2001-11-0017 }}
*{{cite journal | author=Okuyama T, Ishihara S, Sato H, ''et al.'' |title=Activation of prostaglandin E2-receptor EP2 and EP4 pathways induces growth inhibition in human gastric carcinoma cell lines. |journal=J. Lab. Clin. Med. |volume=140 |issue= 2 |pages= 92-102 |year= 2002 |pmid= 12228765 |doi= }}
*{{cite journal | author=Konger RL, Scott GA, Landt Y, ''et al.'' |title=Loss of the EP2 prostaglandin E2 receptor in immortalized human keratinocytes results in increased invasiveness and decreased paxillin expression. |journal=Am. J. Pathol. |volume=161 |issue= 6 |pages= 2065-78 |year= 2003 |pmid= 12466123 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Abulencia JP, Gaspard R, Healy ZR, ''et al.'' |title=Shear-induced cyclooxygenase-2 via a JNK2/c-Jun-dependent pathway regulates prostaglandin receptor expression in chondrocytic cells. |journal=J. Biol. Chem. |volume=278 |issue= 31 |pages= 28388-94 |year= 2003 |pmid= 12743126 |doi= 10.1074/jbc.M301378200 }}
*{{cite journal | author=Richards JA, Brueggemeier RW |title=Prostaglandin E2 regulates aromatase activity and expression in human adipose stromal cells via two distinct receptor subtypes. |journal=J. Clin. Endocrinol. Metab. |volume=88 |issue= 6 |pages= 2810-6 |year= 2003 |pmid= 12788892 |doi= }}
*{{cite journal | author=Sun HS, Hsiao KY, Hsu CC, ''et al.'' |title=Transactivation of steroidogenic acute regulatory protein in human endometriotic stromalcells is mediated by the prostaglandin EP2 receptor. |journal=Endocrinology |volume=144 |issue= 9 |pages= 3934-42 |year= 2003 |pmid= 12933667 |doi= }}
*{{cite journal | author=Bradbury DA, Newton R, Zhu YM, ''et al.'' |title=Cyclooxygenase-2 induction by bradykinin in human pulmonary artery smooth muscle cells is mediated by the cyclic AMP response element through a novel autocrine loop involving endogenous prostaglandin E2, E-prostanoid 2 (EP2), and EP4 receptors. |journal=J. Biol. Chem. |volume=278 |issue= 50 |pages= 49954-64 |year= 2004 |pmid= 14517215 |doi= 10.1074/jbc.M307964200 }}
*{{cite journal | author=Moreland RB, Kim N, Nehra A, ''et al.'' |title=Functional prostaglandin E (EP) receptors in human penile corpus cavernosum. |journal=Int. J. Impot. Res. |volume=15 |issue= 5 |pages= 362-8 |year= 2004 |pmid= 14562138 |doi= 10.1038/sj.ijir.3901042 }}
*{{cite journal | author=Sugimoto Y, Nakato T, Kita A, ''et al.'' |title=A cluster of aromatic amino acids in the i2 loop plays a key role for Gs coupling in prostaglandin EP2 and EP3 receptors. |journal=J. Biol. Chem. |volume=279 |issue= 12 |pages= 11016-26 |year= 2004 |pmid= 14699136 |doi= 10.1074/jbc.M307404200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PVRL1... {November 19, 2007 11:53:15 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 11:54:19 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Poliovirus receptor-related 1 (herpesvirus entry mediator C; nectin)
| HGNCid = 9706
| Symbol = PVRL1
| AltSymbols =; PRR1; CD111; CLPED1; ED4; HIgR; HVEC; MGC142031; MGC16207; OFC7; PRR; PVRR; PVRR1; SK-12; nectin-1
| OMIM = 600644
| ECnumber =
| Homologene = 2138
| MGIid = 1926483
| GeneAtlas_image1 = PBB_GE_PVRL1_208455_at_tn.png
| GeneAtlas_image2 = PBB_GE_PVRL1_211846_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_PVRL1_211845_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0015026 |text = coreceptor activity}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}}
| Component = {{GNF_GO|id=GO:0005913 |text = cell-cell adherens junction}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007156 |text = homophilic cell adhesion}} {{GNF_GO|id=GO:0007157 |text = heterophilic cell adhesion}} {{GNF_GO|id=GO:0046718 |text = entry of virus into host cell}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5818
| Hs_Ensembl = ENSG00000110400
| Hs_RefseqProtein = NP_002846
| Hs_RefseqmRNA = NM_002855
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 119014018
| Hs_GenLoc_end = 119104645
| Hs_Uniprot = Q15223
| Mm_EntrezGene = 58235
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_021424
| Mm_RefseqProtein = NP_067399
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Poliovirus receptor-related 1 (herpesvirus entry mediator C; nectin)''', also known as '''PVRL1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PVRL1 poliovirus receptor-related 1 (herpesvirus entry mediator C; nectin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5818| 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=Bustos T, Simosa V, Pinto-Cisternas J, ''et al.'' |title=Autosomal recessive ectodermal dysplasia: I. An undescribed dysplasia/malformation syndrome. |journal=Am. J. Med. Genet. |volume=41 |issue= 4 |pages= 398-404 |year= 1992 |pmid= 1776626 |doi= 10.1002/ajmg.1320410403 }}
*{{cite journal | author=Lopez M, Eberlé F, Mattei MG, ''et al.'' |title=Complementary DNA characterization and chromosomal localization of a human gene related to the poliovirus receptor-encoding gene. |journal=Gene |volume=155 |issue= 2 |pages= 261-5 |year= 1995 |pmid= 7721102 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Geraghty RJ, Krummenacher C, Cohen GH, ''et al.'' |title=Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor. |journal=Science |volume=280 |issue= 5369 |pages= 1618-20 |year= 1998 |pmid= 9616127 |doi= }}
*{{cite journal | author=Suzuki K, Bustos T, Spritz RA |title=Linkage disequilibrium mapping of the gene for Margarita Island ectodermal dysplasia (ED4) to 11q23. |journal=Am. J. Hum. Genet. |volume=63 |issue= 4 |pages= 1102-7 |year= 1998 |pmid= 9758630 |doi= }}
*{{cite journal | author=Cocchi F, Menotti L, Mirandola P, ''et al.'' |title=The ectodomain of a novel member of the immunoglobulin subfamily related to the poliovirus receptor has the attributes of a bona fide receptor for herpes simplex virus types 1 and 2 in human cells. |journal=J. Virol. |volume=72 |issue= 12 |pages= 9992-10002 |year= 1998 |pmid= 9811737 |doi= }}
*{{cite journal | author=Cocchi F, Lopez M, Menotti L, ''et al.'' |title=The V domain of herpesvirus Ig-like receptor (HIgR) contains a major functional region in herpes simplex virus-1 entry into cells and interacts physically with the viral glycoprotein D. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 26 |pages= 15700-5 |year= 1999 |pmid= 9861033 |doi= }}
*{{cite journal | author=Takahashi K, Nakanishi H, Miyahara M, ''et al.'' |title=Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein. |journal=J. Cell Biol. |volume=145 |issue= 3 |pages= 539-49 |year= 1999 |pmid= 10225955 |doi= }}
*{{cite journal | author=Miyahara M, Nakanishi H, Takahashi K, ''et al.'' |title=Interaction of nectin with afadin is necessary for its clustering at cell-cell contact sites but not for its cis dimerization or trans interaction. |journal=J. Biol. Chem. |volume=275 |issue= 1 |pages= 613-8 |year= 2000 |pmid= 10617658 |doi= }}
*{{cite journal | author=Suzuki K, Hu D, Bustos T, ''et al.'' |title=Mutations of PVRL1, encoding a cell-cell adhesion molecule/herpesvirus receptor, in cleft lip/palate-ectodermal dysplasia. |journal=Nat. Genet. |volume=25 |issue= 4 |pages= 427-30 |year= 2000 |pmid= 10932188 |doi= 10.1038/78119 }}
*{{cite journal | author=Lopez M, Cocchi F, Avitabile E, ''et al.'' |title=Novel, soluble isoform of the herpes simplex virus (HSV) receptor nectin1 (or PRR1-HIgR-HveC) modulates positively and negatively susceptibility to HSV infection. |journal=J. Virol. |volume=75 |issue= 12 |pages= 5684-91 |year= 2001 |pmid= 11356977 |doi= 10.1128/JVI.75.12.5684-5691.2001 }}
*{{cite journal | author=Sözen MA, Suzuki K, Tolarova MM, ''et al.'' |title=Mutation of PVRL1 is associated with sporadic, non-syndromic cleft lip/palate in northern Venezuela. |journal=Nat. Genet. |volume=29 |issue= 2 |pages= 141-2 |year= 2001 |pmid= 11559849 |doi= 10.1038/ng740 }}
*{{cite journal | author=Struyf F, Posavad CM, Keyaerts E, ''et al.'' |title=Search for polymorphisms in the genes for herpesvirus entry mediator, nectin-1, and nectin-2 in immune seronegative individuals. |journal=J. Infect. Dis. |volume=185 |issue= 1 |pages= 36-44 |year= 2002 |pmid= 11756979 |doi= }}
*{{cite journal | author=Fabre S, Reymond N, Cocchi F, ''et al.'' |title=Prominent role of the Ig-like V domain in trans-interactions of nectins. Nectin3 and nectin 4 bind to the predicted C-C'-C"-D beta-strands of the nectin1 V domain. |journal=J. Biol. Chem. |volume=277 |issue= 30 |pages= 27006-13 |year= 2002 |pmid= 12011057 |doi= 10.1074/jbc.M203228200 }}
*{{cite journal | author=Yoon M, Spear PG |title=Disruption of adherens junctions liberates nectin-1 to serve as receptor for herpes simplex virus and pseudorabies virus entry. |journal=J. Virol. |volume=76 |issue= 14 |pages= 7203-8 |year= 2002 |pmid= 12072519 |doi= }}
*{{cite journal | author=Struyf F, Martinez WM, Spear PG |title=Mutations in the N-terminal domains of nectin-1 and nectin-2 reveal differences in requirements for entry of various alphaherpesviruses and for nectin-nectin interactions. |journal=J. Virol. |volume=76 |issue= 24 |pages= 12940-50 |year= 2002 |pmid= 12438620 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Takekuni K, Ikeda W, Fujito T, ''et al.'' |title=Direct binding of cell polarity protein PAR-3 to cell-cell adhesion molecule nectin at neuroepithelial cells of developing mouse. |journal=J. Biol. Chem. |volume=278 |issue= 8 |pages= 5497-500 |year= 2003 |pmid= 12515806 |doi= 10.1074/jbc.C200707200 }}
*{{cite journal | author=Krummenacher C, Baribaud I, Eisenberg RJ, Cohen GH |title=Cellular localization of nectin-1 and glycoprotein D during herpes simplex virus infection. |journal=J. Virol. |volume=77 |issue= 16 |pages= 8985-99 |year= 2003 |pmid= 12885915 |doi= }}
*{{cite journal | author=Bender FC, Whitbeck JC, Ponce de Leon M, ''et al.'' |title=Specific association of glycoprotein B with lipid rafts during herpes simplex virus entry. |journal=J. Virol. |volume=77 |issue= 17 |pages= 9542-52 |year= 2003 |pmid= 12915568 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SAFB... {November 19, 2007 11:54:19 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 11:54:49 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Scaffold attachment factor B
| HGNCid = 10520
| Symbol = SAFB
| AltSymbols =; HET; HAP; DKFZp779C1727; SAFB1
| OMIM = 602895
| ECnumber =
| Homologene = 2229
| MGIid = 2146974
| GeneAtlas_image1 = PBB_GE_SAFB_201748_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SAFB_201747_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003676 |text = nucleic acid binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003690 |text = double-stranded DNA binding}} {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006325 |text = establishment and/or maintenance of chromatin architecture}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6294
| Hs_Ensembl = ENSG00000160633
| Hs_RefseqProtein = NP_002958
| Hs_RefseqmRNA = NM_002967
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 5574164
| Hs_GenLoc_end = 5619488
| Hs_Uniprot = Q15424
| Mm_EntrezGene = 224903
| Mm_Ensembl = ENSMUSG00000071054
| Mm_RefseqmRNA = XM_001002609
| Mm_RefseqProtein = XP_001002609
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 56270255
| Mm_GenLoc_end = 56291399
| Mm_Uniprot =
}}
}}
'''Scaffold attachment factor B''', also known as '''SAFB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SAFB scaffold attachment factor B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6294| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a DNA-binding protein that has high specificity for scaffold or matrix attachment region DNA elements (S/MAR DNA). This protein is thought to be involved in attaching the base of chromatin loops to the nuclear matrix but there is conflicting evidence as to whether this protein is a component of chromatin or a nuclear matrix protein. Scaffold attachment factors are a specific subset of nuclear matrix proteins (NMP) that specifically bind to S/MAR. This encoded protein is thought to serve as a molecular base to assemble a 'transcriptosome complex' in the vicinity of actively transcribed genes. It is involved in the regulation of the heat shock protein 27 transcription and also can act as an estrogen receptor corepressor. This gene is a candidate gene for breast tumorigenesis.<ref name="entrez">{{cite web | title = Entrez Gene: SAFB scaffold attachment factor B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6294| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Oesterreich S |title=Scaffold attachment factors SAFB1 and SAFB2: Innocent bystanders or critical players in breast tumorigenesis? |journal=J. Cell. Biochem. |volume=90 |issue= 4 |pages= 653-61 |year= 2004 |pmid= 14587024 |doi= 10.1002/jcb.10685 }}
*{{cite journal | author=Romig H, Fackelmayer FO, Renz A, ''et al.'' |title=Characterization of SAF-A, a novel nuclear DNA binding protein from HeLa cells with high affinity for nuclear matrix/scaffold attachment DNA elements. |journal=EMBO J. |volume=11 |issue= 9 |pages= 3431-40 |year= 1992 |pmid= 1324173 |doi= }}
*{{cite journal | author=Renz A, Fackelmayer FO |title=Purification and molecular cloning of the scaffold attachment factor B (SAF-B), a novel human nuclear protein that specifically binds to S/MAR-DNA. |journal=Nucleic Acids Res. |volume=24 |issue= 5 |pages= 843-9 |year= 1996 |pmid= 8600450 |doi= }}
*{{cite journal | author=Oesterreich S, Lee AV, Sullivan TM, ''et al.'' |title=Novel nuclear matrix protein HET binds to and influences activity of the HSP27 promoter in human breast cancer cells. |journal=J. Cell. Biochem. |volume=67 |issue= 2 |pages= 275-86 |year= 1997 |pmid= 9328833 |doi= }}
*{{cite journal | author=DuPont BR, Garcia DK, Sullivan TM, ''et al.'' |title=Assignment of SAFB encoding Hsp27 ERE-TATA binding protein (HET)/scaffold attachment factor B (SAF-B) to human chromosome 19 band p13. |journal=Cytogenet. Cell Genet. |volume=79 |issue= 3-4 |pages= 284-5 |year= 1998 |pmid= 9605873 |doi= }}
*{{cite journal | author=Nayler O, Strätling W, Bourquin JP, ''et al.'' |title=SAF-B protein couples transcription and pre-mRNA splicing to SAR/MAR elements. |journal=Nucleic Acids Res. |volume=26 |issue= 15 |pages= 3542-9 |year= 1998 |pmid= 9671816 |doi= }}
*{{cite journal | author=Weighardt F, Cobianchi F, Cartegni L, ''et al.'' |title=A novel hnRNP protein (HAP/SAF-B) enters a subset of hnRNP complexes and relocates in nuclear granules in response to heat shock. |journal=J. Cell. Sci. |volume=112 ( Pt 10) |issue= |pages= 1465-76 |year= 1999 |pmid= 10212141 |doi= }}
*{{cite journal | author=Oesterreich S, Zhang Q, Hopp T, ''et al.'' |title=Tamoxifen-bound estrogen receptor (ER) strongly interacts with the nuclear matrix protein HET/SAF-B, a novel inhibitor of ER-mediated transactivation. |journal=Mol. Endocrinol. |volume=14 |issue= 3 |pages= 369-81 |year= 2000 |pmid= 10707955 |doi= }}
*{{cite journal | author=Shnyreva M, Schullery DS, Suzuki H, ''et al.'' |title=Interaction of two multifunctional proteins. Heterogeneous nuclear ribonucleoprotein K and Y-box-binding protein. |journal=J. Biol. Chem. |volume=275 |issue= 20 |pages= 15498-503 |year= 2000 |pmid= 10809782 |doi= }}
*{{cite journal | author=Arao Y, Kuriyama R, Kayama F, Kato S |title=A nuclear matrix-associated factor, SAF-B, interacts with specific isoforms of AUF1/hnRNP D. |journal=Arch. Biochem. Biophys. |volume=380 |issue= 2 |pages= 228-36 |year= 2000 |pmid= 10933876 |doi= 10.1006/abbi.2000.1938 }}
*{{cite journal | author=Stoss O, Olbrich M, Hartmann AM, ''et al.'' |title=The STAR/GSG family protein rSLM-2 regulates the selection of alternative splice sites. |journal=J. Biol. Chem. |volume=276 |issue= 12 |pages= 8665-73 |year= 2001 |pmid= 11118435 |doi= 10.1074/jbc.M006851200 }}
*{{cite journal | author=Oesterreich S, Allredl DC, Mohsin SK, ''et al.'' |title=High rates of loss of heterozygosity on chromosome 19p13 in human breast cancer. |journal=Br. J. Cancer |volume=84 |issue= 4 |pages= 493-8 |year= 2001 |pmid= 11207044 |doi= 10.1054/bjoc.2000.1606 }}
*{{cite journal | author=Nikolakaki E, Kohen R, Hartmann AM, ''et al.'' |title=Cloning and characterization of an alternatively spliced form of SR protein kinase 1 that interacts specifically with scaffold attachment factor-B. |journal=J. Biol. Chem. |volume=276 |issue= 43 |pages= 40175-82 |year= 2001 |pmid= 11509566 |doi= 10.1074/jbc.M104755200 }}
*{{cite journal | author=Paul C, Manero F, Gonin S, ''et al.'' |title=Hsp27 as a negative regulator of cytochrome C release. |journal=Mol. Cell. Biol. |volume=22 |issue= 3 |pages= 816-34 |year= 2002 |pmid= 11784858 |doi= }}
*{{cite journal | author=Traweger A, Fuchs R, Krizbai IA, ''et al.'' |title=The tight junction protein ZO-2 localizes to the nucleus and interacts with the heterogeneous nuclear ribonucleoprotein scaffold attachment factor-B. |journal=J. Biol. Chem. |volume=278 |issue= 4 |pages= 2692-700 |year= 2003 |pmid= 12403786 |doi= 10.1074/jbc.M206821200 }}
*{{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=Townson SM, Dobrzycka KM, Lee AV, ''et al.'' |title=SAFB2, a new scaffold attachment factor homolog and estrogen receptor corepressor. |journal=J. Biol. Chem. |volume=278 |issue= 22 |pages= 20059-68 |year= 2003 |pmid= 12660241 |doi= 10.1074/jbc.M212988200 }}
*{{cite journal | author=van den IJssel P, Wheelock R, Prescott A, ''et al.'' |title=Nuclear speckle localisation of the small heat shock protein alpha B-crystallin and its inhibition by the R120G cardiomyopathy-linked mutation. |journal=Exp. Cell Res. |volume=287 |issue= 2 |pages= 249-61 |year= 2003 |pmid= 12837281 |doi= }}
*{{cite journal | author=Tai HH, Geisterfer M, Bell JC, ''et al.'' |title=CHD1 associates with NCoR and histone deacetylase as well as with RNA splicing proteins. |journal=Biochem. Biophys. Res. Commun. |volume=308 |issue= 1 |pages= 170-6 |year= 2003 |pmid= 12890497 |doi= }}
*{{cite journal | author=Li J, Hawkins IC, Harvey CD, ''et al.'' |title=Regulation of alternative splicing by SRrp86 and its interacting proteins. |journal=Mol. Cell. Biol. |volume=23 |issue= 21 |pages= 7437-47 |year= 2003 |pmid= 14559993 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SDCBP... {November 19, 2007 11:54:49 AM PST}
- SEARCH REDIRECT: Control Box Found: SDCBP {November 19, 2007 11:55:18 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 11:55:19 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 11:55:19 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 11:55:19 AM PST}
- UPDATED: Updated protein page: SDCBP {November 19, 2007 11:55:25 AM PST}
- INFO: Beginning work on SOX10... {November 19, 2007 11:56:09 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 11:56:46 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = SRY (sex determining region Y)-box 10
| HGNCid = 11190
| Symbol = SOX10
| AltSymbols =; DOM; MGC15649; WS4
| OMIM = 602229
| ECnumber =
| Homologene = 5055
| MGIid = 98358
| GeneAtlas_image1 = PBB_GE_SOX10_209842_at_tn.png
| GeneAtlas_image2 = PBB_GE_SOX10_209843_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:0003705 |text = RNA polymerase II transcription factor activity, enhancer binding}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0009653 |text = anatomical structure morphogenesis}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0048469 |text = cell maturation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6663
| Hs_Ensembl = ENSG00000100146
| Hs_RefseqProtein = NP_008872
| Hs_RefseqmRNA = NM_006941
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 36698254
| Hs_GenLoc_end = 36713375
| Hs_Uniprot = P56693
| Mm_EntrezGene = 20665
| Mm_Ensembl = ENSMUSG00000033006
| Mm_RefseqmRNA = XM_001001494
| Mm_RefseqProtein = XP_001001494
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 78982186
| Mm_GenLoc_end = 78992495
| Mm_Uniprot = Q80V12
}}
}}
'''SRY (sex determining region Y)-box 10''', also known as '''SOX10''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SOX10 SRY (sex determining region Y)-box 10| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6663| 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 SOX (SRY-related HMG-box) family of transcription factors involved in the regulation of embryonic development and in the determination of the cell fate. The encoded protein may act as a transcriptional activator after forming a protein complex with other proteins. This protein acts as a nucleocytoplasmic shuttle protein and is important for neural crest and peripheral nervous system development. Mutations in this gene are associated with Waardenburg-Shah and Waardenburg-Hirschsprung disease.<ref name="entrez">{{cite web | title = Entrez Gene: SOX10 SRY (sex determining region Y)-box 10| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6663| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Jacobs JM, Wilson J |title=An unusual demyelinating neuropathy in a patient with Waardenburg's syndrome. |journal=Acta Neuropathol. |volume=83 |issue= 6 |pages= 670-4 |year= 1992 |pmid= 1636383 |doi= }}
*{{cite journal | author=Southard-Smith EM, Kos L, Pavan WJ |title=Sox10 mutation disrupts neural crest development in Dom Hirschsprung mouse model. |journal=Nat. Genet. |volume=18 |issue= 1 |pages= 60-4 |year= 1998 |pmid= 9425902 |doi= 10.1038/ng0198-60 }}
*{{cite journal | author=Pingault V, Bondurand N, Kuhlbrodt K, ''et al.'' |title=SOX10 mutations in patients with Waardenburg-Hirschsprung disease. |journal=Nat. Genet. |volume=18 |issue= 2 |pages= 171-3 |year= 1998 |pmid= 9462749 |doi= 10.1038/ng0298-171 }}
*{{cite journal | author=Kuhlbrodt K, Schmidt C, Sock E, ''et al.'' |title=Functional analysis of Sox10 mutations found in human Waardenburg-Hirschsprung patients. |journal=J. Biol. Chem. |volume=273 |issue= 36 |pages= 23033-8 |year= 1998 |pmid= 9722528 |doi= }}
*{{cite journal | author=Pusch C, Hustert E, Pfeifer D, ''et al.'' |title=The SOX10/Sox10 gene from human and mouse: sequence, expression, and transactivation by the encoded HMG domain transcription factor. |journal=Hum. Genet. |volume=103 |issue= 2 |pages= 115-23 |year= 1998 |pmid= 9760192 |doi= }}
*{{cite journal | author=Bondurand N, Kuhlbrodt K, Pingault V, ''et al.'' |title=A molecular analysis of the yemenite deaf-blind hypopigmentation syndrome: SOX10 dysfunction causes different neurocristopathies. |journal=Hum. Mol. Genet. |volume=8 |issue= 9 |pages= 1785-9 |year= 2000 |pmid= 10441344 |doi= }}
*{{cite journal | author=Inoue K, Tanabe Y, Lupski JR |title=Myelin deficiencies in both the central and the peripheral nervous systems associated with a SOX10 mutation. |journal=Ann. Neurol. |volume=46 |issue= 3 |pages= 313-8 |year= 1999 |pmid= 10482261 |doi= }}
*{{cite journal | author=Dunham I, Shimizu N, Roe BA, ''et al.'' |title=The DNA sequence of human chromosome 22. |journal=Nature |volume=402 |issue= 6761 |pages= 489-95 |year= 1999 |pmid= 10591208 |doi= 10.1038/990031 }}
*{{cite journal | author=Touraine RL, Attié-Bitach T, Manceau E, ''et al.'' |title=Neurological phenotype in Waardenburg syndrome type 4 correlates with novel SOX10 truncating mutations and expression in developing brain. |journal=Am. J. Hum. Genet. |volume=66 |issue= 5 |pages= 1496-503 |year= 2000 |pmid= 10762540 |doi= }}
*{{cite journal | author=Bondurand N, Pingault V, Goerich DE, ''et al.'' |title=Interaction among SOX10, PAX3 and MITF, three genes altered in Waardenburg syndrome. |journal=Hum. Mol. Genet. |volume=9 |issue= 13 |pages= 1907-17 |year= 2000 |pmid= 10942418 |doi= }}
*{{cite journal | author=Smit DJ, Smith AG, Parsons PG, ''et al.'' |title=Domains of Brn-2 that mediate homodimerization and interaction with general and melanocytic transcription factors. |journal=Eur. J. Biochem. |volume=267 |issue= 21 |pages= 6413-22 |year= 2000 |pmid= 11029584 |doi= }}
*{{cite journal | author=Sham MH, Lui VC, Chen BL, ''et al.'' |title=Novel mutations of SOX10 suggest a dominant negative role in Waardenburg-Shah syndrome. |journal=J. Med. Genet. |volume=38 |issue= 9 |pages= E30 |year= 2002 |pmid= 11546831 |doi= }}
*{{cite journal | author=Rehberg S, Lischka P, Glaser G, ''et al.'' |title=Sox10 is an active nucleocytoplasmic shuttle protein, and shuttling is crucial for Sox10-mediated transactivation. |journal=Mol. Cell. Biol. |volume=22 |issue= 16 |pages= 5826-34 |year= 2002 |pmid= 12138193 |doi= }}
*{{cite journal | author=Pingault V, Girard M, Bondurand N, ''et al.'' |title=SOX10 mutations in chronic intestinal pseudo-obstruction suggest a complex physiopathological mechanism. |journal=Hum. Genet. |volume=111 |issue= 2 |pages= 198-206 |year= 2002 |pmid= 12189494 |doi= 10.1007/s00439-002-0765-8 }}
*{{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=Lang D, Epstein JA |title=Sox10 and Pax3 physically interact to mediate activation of a conserved c-RET enhancer. |journal=Hum. Mol. Genet. |volume=12 |issue= 8 |pages= 937-45 |year= 2004 |pmid= 12668617 |doi= }}
*{{cite journal | author=Shimotake T, Tomiyama H, Aoi S, Iwai N |title=Discrepancy between macroscopic and microscopic transitional zones in Hirschsprung's disease with reference to the type of RET/GDNF/SOX10 gene mutation. |journal=J. Pediatr. Surg. |volume=38 |issue= 5 |pages= 698-701 |year= 2003 |pmid= 12720173 |doi= 10.1016/jpsu.2003.50186 }}
*{{cite journal | author=Huber WE, Price ER, Widlund HR, ''et al.'' |title=A tissue-restricted cAMP transcriptional response: SOX10 modulates alpha-melanocyte-stimulating hormone-triggered expression of microphthalmia-associated transcription factor in melanocytes. |journal=J. Biol. Chem. |volume=278 |issue= 46 |pages= 45224-30 |year= 2003 |pmid= 12944398 |doi= 10.1074/jbc.M309036200 }}
*{{cite journal | author=Chan KK, Wong CK, Lui VC, ''et al.'' |title=Analysis of SOX10 mutations identified in Waardenburg-Hirschsprung patients: Differential effects on target gene regulation. |journal=J. Cell. Biochem. |volume=90 |issue= 3 |pages= 573-85 |year= 2004 |pmid= 14523991 |doi= 10.1002/jcb.10656 }}
*{{cite journal | author=Inoue K, Khajavi M, Ohyama T, ''et al.'' |title=Molecular mechanism for distinct neurological phenotypes conveyed by allelic truncating mutations. |journal=Nat. Genet. |volume=36 |issue= 4 |pages= 361-9 |year= 2004 |pmid= 15004559 |doi= 10.1038/ng1322 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ST6GAL1... {November 19, 2007 11:55:25 AM PST}
- SEARCH REDIRECT: Control Box Found: ST6GAL1 {November 19, 2007 11:55:57 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 11:56:01 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 11:56:01 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 11:56:01 AM PST}
- UPDATED: Updated protein page: ST6GAL1 {November 19, 2007 11:56:09 AM PST}
- INFO: Beginning work on STK4... {November 19, 2007 11:56:46 AM PST}
- SEARCH REDIRECT: Control Box Found: STK4 {November 19, 2007 11:57:31 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 11:57:32 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 11:57:32 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 11:57:32 AM PST}
- UPDATED: Updated protein page: STK4 {November 19, 2007 11:57:39 AM PST}
- INFO: Beginning work on SULT1A3... {November 19, 2007 11:57:39 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 11:58:16 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_SULT1A3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cjm.
| PDB = {{PDB2|1cjm}}, {{PDB2|1ls6}}, {{PDB2|1z28}}, {{PDB2|1z29}}, {{PDB2|2a3r}}, {{PDB2|2d06}}
| Name = Sulfotransferase family, cytosolic, 1A, phenol-preferring, member 3
| HGNCid = 11455
| Symbol = SULT1A3
| AltSymbols =; HAST; HAST3; M-PST; MGC117469; ST1A5; STM; SULT1A4; TL-PST
| OMIM = 600641
| ECnumber =
| Homologene = 81075
| MGIid =
| Function = {{GNF_GO|id=GO:0004062 |text = aryl sulfotransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006584 |text = catecholamine metabolic process}} {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0008202 |text = steroid metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6818
| Hs_Ensembl =
| Hs_RefseqProtein = XP_001126153
| Hs_RefseqmRNA = XM_001126153
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Sulfotransferase family, cytosolic, 1A, phenol-preferring, member 3''', also known as '''SULT1A3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SULT1A3 sulfotransferase family, cytosolic, 1A, phenol-preferring, member 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6818| 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 = Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. The gene structure (number and length of exons) is similar among family members. This gene encodes a phenol sulfotransferase with thermolabile enzyme activity. Four sulfotransferase genes are located on the p arm of chromosome 16; this gene and SULT1A4 arose from a segmental duplication. This gene is the most centromeric of the four sulfotransferase genes. Exons of this gene overlap with exons of a gene that encodes a protein containing GIY-YIG domains (GIYD1). Three alternatively spliced variants that encode the same protein have been described.<ref name="entrez">{{cite web | title = Entrez Gene: SULT1A3 sulfotransferase family, cytosolic, 1A, phenol-preferring, member 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6818| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Weinshilboum RM, Otterness DM, Aksoy IA, ''et al.'' |title=Sulfation and sulfotransferases 1: Sulfotransferase molecular biology: cDNAs and genes. |journal=FASEB J. |volume=11 |issue= 1 |pages= 3-14 |year= 1997 |pmid= 9034160 |doi= }}
*{{cite journal | author=Glatt H, Engelke CE, Pabel U, ''et al.'' |title=Sulfotransferases: genetics and role in toxicology. |journal=Toxicol. Lett. |volume=112-113 |issue= |pages= 341-8 |year= 2000 |pmid= 10720750 |doi= }}
*{{cite journal | author=Glatt H |title=Sulfotransferases in the bioactivation of xenobiotics. |journal=Chem. Biol. Interact. |volume=129 |issue= 1-2 |pages= 141-70 |year= 2001 |pmid= 11154739 |doi= }}
*{{cite journal | author=Glatt H, Boeing H, Engelke CE, ''et al.'' |title=Human cytosolic sulphotransferases: genetics, characteristics, toxicological aspects. |journal=Mutat. Res. |volume=482 |issue= 1-2 |pages= 27-40 |year= 2001 |pmid= 11535246 |doi= }}
*{{cite journal | author=Aksoy IA, Weinshilboum RM |title=Human thermolabile phenol sulfotransferase gene (STM): molecular cloning and structural characterization. |journal=Biochem. Biophys. Res. Commun. |volume=208 |issue= 2 |pages= 786-95 |year= 1995 |pmid= 7695637 |doi= 10.1006/bbrc.1995.1406 }}
*{{cite journal | author=Jones AL, Hagen M, Coughtrie MW, ''et al.'' |title=Human platelet phenolsulfotransferases: cDNA cloning, stable expression in V79 cells and identification of a novel allelic variant of the phenol-sulfating form. |journal=Biochem. Biophys. Res. Commun. |volume=208 |issue= 2 |pages= 855-62 |year= 1995 |pmid= 7695643 |doi= 10.1006/bbrc.1995.1414 }}
*{{cite journal | author=Dooley TP, Probst P, Munroe PB, ''et al.'' |title=Genomic organization and DNA sequence of the human catecholamine-sulfating phenol sulfotransferase gene (STM). |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 2 |pages= 1325-32 |year= 1995 |pmid= 7802665 |doi= 10.1006/bbrc.1994.2810 }}
*{{cite journal | author=Aksoy IA, Callen DF, Apostolou S, ''et al.'' |title=Thermolabile phenol sulfotransferase gene (STM): localization to human chromosome 16p11.2. |journal=Genomics |volume=23 |issue= 1 |pages= 275-7 |year= 1995 |pmid= 7829089 |doi= 10.1006/geno.1994.1494 }}
*{{cite journal | author=Bernier F, Leblanc G, Labrie F, Luu-The V |title=Structure of human estrogen and aryl sulfotransferase gene. Two mRNA species issued from a single gene. |journal=J. Biol. Chem. |volume=269 |issue= 45 |pages= 28200-5 |year= 1994 |pmid= 7961757 |doi= }}
*{{cite journal | author=Veronese ME, Burgess W, Zhu X, McManus ME |title=Functional characterization of two human sulphotransferase cDNAs that encode monoamine- and phenol-sulphating forms of phenol sulphotransferase: substrate kinetics, thermal-stability and inhibitor-sensitivity studies. |journal=Biochem. J. |volume=302 ( Pt 2) |issue= |pages= 497-502 |year= 1994 |pmid= 8093002 |doi= }}
*{{cite journal | author=Wood TC, Aksoy IA, Aksoy S, Weinshilboum RM |title=Human liver thermolabile phenol sulfotransferase: cDNA cloning, expression and characterization. |journal=Biochem. Biophys. Res. Commun. |volume=198 |issue= 3 |pages= 1119-27 |year= 1994 |pmid= 8117269 |doi= 10.1006/bbrc.1994.1159 }}
*{{cite journal | author=Bernier F, Lopez Solache I, Labrie F, Luu-The V |title=Cloning and expression of cDNA encoding human placental estrogen sulfotransferase. |journal=Mol. Cell. Endocrinol. |volume=99 |issue= 1 |pages= R11-5 |year= 1994 |pmid= 8187949 |doi= }}
*{{cite journal | author=Zhu X, Veronese ME, Bernard CC, ''et al.'' |title=Identification of two human brain aryl sulfotransferase cDNAs. |journal=Biochem. Biophys. Res. Commun. |volume=195 |issue= 1 |pages= 120-7 |year= 1993 |pmid= 8363592 |doi= }}
*{{cite journal | author=Her C, Raftogianis R, Weinshilboum RM |title=Human phenol sulfotransferase STP2 gene: molecular cloning, structural characterization, and chromosomal localization. |journal=Genomics |volume=33 |issue= 3 |pages= 409-20 |year= 1996 |pmid= 8661000 |doi= 10.1006/geno.1996.0216 }}
*{{cite journal | author=Dooley TP, Huang Z |title=Genomic organization and DNA sequences of two human phenol sulfotransferase genes (STP1 and STP2) on the short arm of chromosome 16. |journal=Biochem. Biophys. Res. Commun. |volume=228 |issue= 1 |pages= 134-40 |year= 1996 |pmid= 8912648 |doi= 10.1006/bbrc.1996.1628 }}
*{{cite journal | author=Dajani R, Sharp S, Graham S, ''et al.'' |title=Kinetic properties of human dopamine sulfotransferase (SULT1A3) expressed in prokaryotic and eukaryotic systems: comparison with the recombinant enzyme purified from Escherichia coli. |journal=Protein Expr. Purif. |volume=16 |issue= 1 |pages= 11-8 |year= 1999 |pmid= 10336855 |doi= 10.1006/prep.1999.1030 }}
*{{cite journal | author=Bidwell LM, McManus ME, Gaedigk A, ''et al.'' |title=Crystal structure of human catecholamine sulfotransferase. |journal=J. Mol. Biol. |volume=293 |issue= 3 |pages= 521-30 |year= 1999 |pmid= 10543947 |doi= 10.1006/jmbi.1999.3153 }}
*{{cite journal | author=Dajani R, Cleasby A, Neu M, ''et al.'' |title=X-ray crystal structure of human dopamine sulfotransferase, SULT1A3. Molecular modeling and quantitative structure-activity relationship analysis demonstrate a molecular basis for sulfotransferase substrate specificity. |journal=J. Biol. Chem. |volume=274 |issue= 53 |pages= 37862-8 |year= 2000 |pmid= 10608851 |doi= }}
*{{cite journal | author=Harris RM, Waring RH, Kirk CJ, Hughes PJ |title=Sulfation of "estrogenic" alkylphenols and 17beta-estradiol by human platelet phenol sulfotransferases. |journal=J. Biol. Chem. |volume=275 |issue= 1 |pages= 159-66 |year= 2000 |pmid= 10617600 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TAF6... {November 19, 2007 11:58:16 AM PST}
- SEARCH REDIRECT: Control Box Found: TAF6 {November 19, 2007 11:58:47 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 11:58:50 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 11:58:50 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 11:58:50 AM PST}
- UPDATED: Updated protein page: TAF6 {November 19, 2007 11:58:57 AM PST}
- INFO: Beginning work on TAF7... {November 19, 2007 11:58:57 AM PST}
- SEARCH REDIRECT: Control Box Found: TAF7 {November 19, 2007 11:59:39 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 11:59:42 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 11:59:42 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 11:59:42 AM PST}
- UPDATED: Updated protein page: TAF7 {November 19, 2007 11:59:48 AM PST}
- INFO: Beginning work on TCF4... {November 19, 2007 11:59:48 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:00:38 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
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| 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 = Transcription factor 4
| HGNCid = 11634
| Symbol = TCF4
| AltSymbols =; E2-2; ITF2; MGC149723; MGC149724; SEF2; SEF2-1; SEF2-1A; SEF2-1B
| OMIM = 602272
| ECnumber =
| Homologene = 2407
| MGIid = 98506
| GeneAtlas_image1 = PBB_GE_TCF4_203753_at_tn.png
| GeneAtlas_image2 = PBB_GE_TCF4_212382_at_tn.png
| GeneAtlas_image3 = PBB_GE_TCF4_222146_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003702 |text = RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006357 |text = regulation of transcription from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6925
| Hs_Ensembl = ENSG00000196628
| Hs_RefseqProtein = NP_003190
| Hs_RefseqmRNA = NM_003199
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 18
| Hs_GenLoc_start = 51046093
| Hs_GenLoc_end = 51406858
| Hs_Uniprot = P15884
| Mm_EntrezGene = 21413
| Mm_Ensembl = ENSMUSG00000053477
| Mm_RefseqmRNA = NM_013685
| Mm_RefseqProtein = NP_038713
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 18
| Mm_GenLoc_start = 69469890
| Mm_GenLoc_end = 69809713
| Mm_Uniprot = Q91XK1
}}
}}
'''Transcription factor 4''', also known as '''TCF4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TCF4 transcription factor 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6925| 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 transcription factor 4, a basic helix-turn-helix transcription factor. The encoded protein recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a motif first identified in immunoglobulin enhancers. This gene is expressed predominantly in pre-B-cells, although it is found in other tissues as well. Multiple alternatively spliced transcript variants that encode different proteins have been described.<ref name="entrez">{{cite web | title = Entrez Gene: TCF4 transcription factor 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6925| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bain G, Murre C |title=The role of E-proteins in B- and T-lymphocyte development. |journal=Semin. Immunol. |volume=10 |issue= 2 |pages= 143-53 |year= 1998 |pmid= 9618760 |doi= 10.1006/smim.1998.0116 }}
*{{cite journal | author=Corneliussen B, Thornell A, Hallberg B, Grundström T |title=Helix-loop-helix transcriptional activators bind to a sequence in glucocorticoid response elements of retrovirus enhancers. |journal=J. Virol. |volume=65 |issue= 11 |pages= 6084-93 |year= 1991 |pmid= 1681116 |doi= }}
*{{cite journal | author=Henthorn P, Kiledjian M, Kadesch T |title=Two distinct transcription factors that bind the immunoglobulin enhancer microE5/kappa 2 motif. |journal=Science |volume=247 |issue= 4941 |pages= 467-70 |year= 1990 |pmid= 2105528 |doi= }}
*{{cite journal | author=Henthorn P, McCarrick-Walmsley R, Kadesch T |title=Sequence of the cDNA encoding ITF-2, a positive-acting transcription factor. |journal=Nucleic Acids Res. |volume=18 |issue= 3 |pages= 678 |year= 1990 |pmid= 2308860 |doi= }}
*{{cite journal | author=Goldfarb AN, Lewandowska K, Shoham M |title=Determinants of helix-loop-helix dimerization affinity. Random mutational analysis of SCL/tal. |journal=J. Biol. Chem. |volume=271 |issue= 5 |pages= 2683-8 |year= 1996 |pmid= 8576241 |doi= }}
*{{cite journal | author=Pscherer A, Dörflinger U, Kirfel J, ''et al.'' |title=The helix-loop-helix transcription factor SEF-2 regulates the activity of a novel initiator element in the promoter of the human somatostatin receptor II gene. |journal=EMBO J. |volume=15 |issue= 23 |pages= 6680-90 |year= 1997 |pmid= 8978694 |doi= }}
*{{cite journal | author=Chen B, Lim RW |title=Physical and functional interactions between the transcriptional inhibitors Id3 and ITF-2b. Evidence toward a novel mechanism regulating muscle-specific gene expression. |journal=J. Biol. Chem. |volume=272 |issue= 4 |pages= 2459-63 |year= 1997 |pmid= 8999959 |doi= }}
*{{cite journal | author=Langlands K, Yin X, Anand G, Prochownik EV |title=Differential interactions of Id proteins with basic-helix-loop-helix transcription factors. |journal=J. Biol. Chem. |volume=272 |issue= 32 |pages= 19785-93 |year= 1997 |pmid= 9242638 |doi= }}
*{{cite journal | author=Breschel TS, McInnis MG, Margolis RL, ''et al.'' |title=A novel, heritable, expanding CTG repeat in an intron of the SEF2-1 gene on chromosome 18q21.1. |journal=Hum. Mol. Genet. |volume=6 |issue= 11 |pages= 1855-63 |year= 1998 |pmid= 9302263 |doi= }}
*{{cite journal | author=Massari ME, Rivera RR, Voland JR, ''et al.'' |title=Characterization of ABF-1, a novel basic helix-loop-helix transcription factor expressed in activated B lymphocytes. |journal=Mol. Cell. Biol. |volume=18 |issue= 6 |pages= 3130-9 |year= 1998 |pmid= 9584154 |doi= }}
*{{cite journal | author=Liu Y, Ray SK, Yang XQ, ''et al.'' |title=A splice variant of E2-2 basic helix-loop-helix protein represses the brain-specific fibroblast growth factor 1 promoter through the binding to an imperfect E-box. |journal=J. Biol. Chem. |volume=273 |issue= 30 |pages= 19269-76 |year= 1998 |pmid= 9668116 |doi= }}
*{{cite journal | author=Onions J, Hermann S, Grundström T |title=A novel type of calmodulin interaction in the inhibition of basic helix-loop-helix transcription factors. |journal=Biochemistry |volume=39 |issue= 15 |pages= 4366-74 |year= 2000 |pmid= 10757985 |doi= }}
*{{cite journal | author=Persson P, Jögi A, Grynfeld A, ''et al.'' |title=HASH-1 and E2-2 are expressed in human neuroblastoma cells and form a functional complex. |journal=Biochem. Biophys. Res. Commun. |volume=274 |issue= 1 |pages= 22-31 |year= 2000 |pmid= 10903890 |doi= 10.1006/bbrc.2000.3090 }}
*{{cite journal | author=Larsson G, Schleucher J, Onions J, ''et al.'' |title=A novel target recognition revealed by calmodulin in complex with the basic helix--loop--helix transcription factor SEF2-1/E2-2. |journal=Protein Sci. |volume=10 |issue= 1 |pages= 169-86 |year= 2001 |pmid= 11266605 |doi= }}
*{{cite journal | author=Sampson EM, Haque ZK, Ku MC, ''et al.'' |title=Negative regulation of the Wnt-beta-catenin pathway by the transcriptional repressor HBP1. |journal=EMBO J. |volume=20 |issue= 16 |pages= 4500-11 |year= 2001 |pmid= 11500377 |doi= 10.1093/emboj/20.16.4500 }}
*{{cite journal | author=Suzuki H, Fukunishi Y, Kagawa I, ''et al.'' |title=Protein-protein interaction panel using mouse full-length cDNAs. |journal=Genome Res. |volume=11 |issue= 10 |pages= 1758-65 |year= 2001 |pmid= 11591653 |doi= 10.1101/gr.180101 }}
*{{cite journal | author=Graham TA, Ferkey DM, Mao F, ''et al.'' |title=Tcf4 can specifically recognize beta-catenin using alternative conformations. |journal=Nat. Struct. Biol. |volume=8 |issue= 12 |pages= 1048-52 |year= 2002 |pmid= 11713475 |doi= 10.1038/nsb718 }}
*{{cite journal | author=Poy F, Lepourcelet M, Shivdasani RA, Eck MJ |title=Structure of a human Tcf4-beta-catenin complex. |journal=Nat. Struct. Biol. |volume=8 |issue= 12 |pages= 1053-7 |year= 2002 |pmid= 11713476 |doi= 10.1038/nsb720 }}
*{{cite journal | author=Jögi A, Persson P, Grynfeld A, ''et al.'' |title=Modulation of basic helix-loop-helix transcription complex formation by Id proteins during neuronal differentiation. |journal=J. Biol. Chem. |volume=277 |issue= 11 |pages= 9118-26 |year= 2002 |pmid= 11756408 |doi= 10.1074/jbc.M107713200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TDG... {November 19, 2007 12:00:38 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:01:00 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_TDG_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1wyw.
| PDB = {{PDB2|1wyw}}, {{PDB2|2d07}}
| Name = Thymine-DNA glycosylase
| HGNCid = 11700
| Symbol = TDG
| AltSymbols =;
| OMIM = 601423
| ECnumber =
| Homologene = 2415
| MGIid =
| GeneAtlas_image1 = PBB_GE_TDG_203743_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003684 |text = damaged DNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008263 |text = pyrimidine-specific mismatch base pair DNA N-glycosylase activity}} {{GNF_GO|id=GO:0016798 |text = hydrolase activity, acting on glycosyl bonds}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005654 |text = nucleoplasm}}
| Process = {{GNF_GO|id=GO:0006284 |text = base-excision repair}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6996
| Hs_Ensembl = ENSG00000139372
| Hs_RefseqProtein = NP_003202
| Hs_RefseqmRNA = NM_003211
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 102883747
| Hs_GenLoc_end = 102906785
| Hs_Uniprot = Q13569
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Thymine-DNA glycosylase''', also known as '''TDG''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TDG thymine-DNA glycosylase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6996| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene belongs to the TDG/mug DNA glycosylase family. Thymine-DNA glycosylase (TDG) removes thymine moieties from G/T mismatches by hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of DNA and the mispaired thymine. With lower activity, this enzyme also removes thymine from C/T and T/T mispairings. TDG can also remove uracil and 5-bromouracil from mispairings with guanine. This enzyme plays a central role in cellular defense against genetic mutation caused by the spontaneous deamination of 5-methylcytosine and cytosine. This gene may have a pseudogene in the p arm of chromosome 12.<ref name="entrez">{{cite web | title = Entrez Gene: TDG thymine-DNA glycosylase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6996| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lindahl T |title=DNA repair enzymes. |journal=Annu. Rev. Biochem. |volume=51 |issue= |pages= 61-87 |year= 1982 |pmid= 6287922 |doi= 10.1146/annurev.bi.51.070182.000425 }}
*{{cite journal | author=Hardeland U, Bentele M, Lettieri T, ''et al.'' |title=Thymine DNA glycosylase. |journal=Prog. Nucleic Acid Res. Mol. Biol. |volume=68 |issue= |pages= 235-53 |year= 2001 |pmid= 11554300 |doi= }}
*{{cite journal | author=Chevray PM, Nathans D |title=Protein interaction cloning in yeast: identification of mammalian proteins that react with the leucine zipper of Jun. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 13 |pages= 5789-93 |year= 1992 |pmid= 1631061 |doi= }}
*{{cite journal | author=Neddermann P, Jiricny J |title=Efficient removal of uracil from G.U mispairs by the mismatch-specific thymine DNA glycosylase from HeLa cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 5 |pages= 1642-6 |year= 1994 |pmid= 8127859 |doi= }}
*{{cite journal | author=Neddermann P, Jiricny J |title=The purification of a mismatch-specific thymine-DNA glycosylase from HeLa cells. |journal=J. Biol. Chem. |volume=268 |issue= 28 |pages= 21218-24 |year= 1993 |pmid= 8407958 |doi= }}
*{{cite journal | author=Neddermann P, Gallinari P, Lettieri T, ''et al.'' |title=Cloning and expression of human G/T mismatch-specific thymine-DNA glycosylase. |journal=J. Biol. Chem. |volume=271 |issue= 22 |pages= 12767-74 |year= 1996 |pmid= 8662714 |doi= }}
*{{cite journal | author=Sard L, Tornielli S, Gallinari P, ''et al.'' |title=Chromosomal localizations and molecular analysis of TDG gene-related sequences. |journal=Genomics |volume=44 |issue= 2 |pages= 222-6 |year= 1997 |pmid= 9299239 |doi= 10.1006/geno.1997.4843 }}
*{{cite journal | author=Barrett TE, Savva R, Panayotou G, ''et al.'' |title=Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions. |journal=Cell |volume=92 |issue= 1 |pages= 117-29 |year= 1998 |pmid= 9489705 |doi= }}
*{{cite journal | author=Missero C, Pirro MT, Simeone S, ''et al.'' |title=The DNA glycosylase T:G mismatch-specific thymine DNA glycosylase represses thyroid transcription factor-1-activated transcription. |journal=J. Biol. Chem. |volume=276 |issue= 36 |pages= 33569-75 |year= 2001 |pmid= 11438542 |doi= 10.1074/jbc.M104963200 }}
*{{cite journal | author=Tini M, Benecke A, Um SJ, ''et al.'' |title=Association of CBP/p300 acetylase and thymine DNA glycosylase links DNA repair and transcription. |journal=Mol. Cell |volume=9 |issue= 2 |pages= 265-77 |year= 2002 |pmid= 11864601 |doi= }}
*{{cite journal | author=Hardeland U, Steinacher R, Jiricny J, Schär P |title=Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover. |journal=EMBO J. |volume=21 |issue= 6 |pages= 1456-64 |year= 2002 |pmid= 11889051 |doi= 10.1093/emboj/21.6.1456 }}
*{{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=Abu M, Waters TR |title=The main role of human thymine-DNA glycosylase is removal of thymine produced by deamination of 5-methylcytosine and not removal of ethenocytosine. |journal=J. Biol. Chem. |volume=278 |issue= 10 |pages= 8739-44 |year= 2003 |pmid= 12493755 |doi= 10.1074/jbc.M211084200 }}
*{{cite journal | author=Shimizu Y, Iwai S, Hanaoka F, Sugasawa K |title=Xeroderma pigmentosum group C protein interacts physically and functionally with thymine DNA glycosylase. |journal=EMBO J. |volume=22 |issue= 1 |pages= 164-73 |year= 2003 |pmid= 12505994 |doi= 10.1093/emboj/cdg016 }}
*{{cite journal | author=Chen D, Lucey MJ, Phoenix F, ''et al.'' |title=T:G mismatch-specific thymine-DNA glycosylase potentiates transcription of estrogen-regulated genes through direct interaction with estrogen receptor alpha. |journal=J. Biol. Chem. |volume=278 |issue= 40 |pages= 38586-92 |year= 2003 |pmid= 12874288 |doi= 10.1074/jbc.M304286200 }}
*{{cite journal | author=Lehner B, Semple JI, Brown SE, ''et al.'' |title=Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region. |journal=Genomics |volume=83 |issue= 1 |pages= 153-67 |year= 2004 |pmid= 14667819 |doi= }}
*{{cite journal | author=Brandenberger R, Wei H, Zhang S, ''et al.'' |title=Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation. |journal=Nat. Biotechnol. |volume=22 |issue= 6 |pages= 707-16 |year= 2005 |pmid= 15146197 |doi= 10.1038/nbt971 }}
*{{cite journal | author=Krześniak M, Butkiewicz D, Samojedny A, ''et al.'' |title=Polymorphisms in TDG and MGMT genes - epidemiological and functional study in lung cancer patients from Poland. |journal=Ann. Hum. Genet. |volume=68 |issue= Pt 4 |pages= 300-12 |year= 2005 |pmid= 15225156 |doi= 10.1046/j.1529-8817.2004.00079.x }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TLE1... {November 19, 2007 12:01:00 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:01:38 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 = PBB_Protein_TLE1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1gxr.
| PDB = {{PDB2|1gxr}}, {{PDB2|2ce8}}, {{PDB2|2ce9}}
| Name = Transducin-like enhancer of split 1 (E(sp1) homolog, Drosophila)
| HGNCid = 11837
| Symbol = TLE1
| AltSymbols =; ESG; ESG1; GRG1
| OMIM = 600189
| ECnumber =
| Homologene = 21058
| MGIid = 104636
| GeneAtlas_image1 = PBB_GE_TLE1_203221_at_tn.png
| GeneAtlas_image2 = PBB_GE_TLE1_203220_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_TLE1_203222_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008134 |text = transcription factor binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007222 |text = Wnt receptor signaling pathway}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0016481 |text = negative regulation of transcription}} {{GNF_GO|id=GO:0030178 |text = negative regulation of Wnt receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7088
| Hs_Ensembl = ENSG00000196781
| Hs_RefseqProtein = NP_005068
| Hs_RefseqmRNA = NM_005077
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 83388418
| Hs_GenLoc_end = 83494270
| Hs_Uniprot = Q04724
| Mm_EntrezGene = 21885
| Mm_Ensembl = ENSMUSG00000008305
| Mm_RefseqmRNA = XM_984048
| Mm_RefseqProtein = XP_989142
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 71603503
| Mm_GenLoc_end = 71687218
| Mm_Uniprot = Q5SQA2
}}
}}
'''Transducin-like enhancer of split 1 (E(sp1) homolog, Drosophila)''', also known as '''TLE1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TLE1 transducin-like enhancer of split 1 (E(sp1) homolog, Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7088| accessdate = }}</ref>
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{{PBB_Summary
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}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Eastman Q, Grosschedl R |title=Regulation of LEF-1/TCF transcription factors by Wnt and other signals. |journal=Curr. Opin. Cell Biol. |volume=11 |issue= 2 |pages= 233-40 |year= 1999 |pmid= 10209158 |doi= }}
*{{cite journal | author=Stifani S, Blaumueller CM, Redhead NJ, ''et al.'' |title=Human homologs of a Drosophila Enhancer of split gene product define a novel family of nuclear proteins. |journal=Nat. Genet. |volume=2 |issue= 2 |pages= 119-27 |year= 1993 |pmid= 1303260 |doi= 10.1038/ng1092-119 }}
*{{cite journal | author=Miyasaka H, Choudhury BK, Hou EW, Li SS |title=Molecular cloning and expression of mouse and human cDNA encoding AES and ESG proteins with strong similarity to Drosophila enhancer of split groucho protein. |journal=Eur. J. Biochem. |volume=216 |issue= 1 |pages= 343-52 |year= 1993 |pmid= 8365415 |doi= }}
*{{cite journal | author=Grbavec D, Stifani S |title=Molecular interaction between TLE1 and the carboxyl-terminal domain of HES-1 containing the WRPW motif. |journal=Biochem. Biophys. Res. Commun. |volume=223 |issue= 3 |pages= 701-5 |year= 1996 |pmid= 8687460 |doi= 10.1006/bbrc.1996.0959 }}
*{{cite journal | author=Husain J, Lo R, Grbavec D, Stifani S |title=Affinity for the nuclear compartment and expression during cell differentiation implicate phosphorylated Groucho/TLE1 forms of higher molecular mass in nuclear functions. |journal=Biochem. J. |volume=317 ( Pt 2) |issue= |pages= 523-31 |year= 1996 |pmid= 8713081 |doi= }}
*{{cite journal | author=Liu Y, Dehni G, Purcell KJ, ''et al.'' |title=Epithelial expression and chromosomal location of human TLE genes: implications for notch signaling and neoplasia. |journal=Genomics |volume=31 |issue= 1 |pages= 58-64 |year= 1996 |pmid= 8808280 |doi= 10.1006/geno.1996.0009 }}
*{{cite journal | author=Palaparti A, Baratz A, Stifani S |title=The Groucho/transducin-like enhancer of split transcriptional repressors interact with the genetically defined amino-terminal silencing domain of histone H3. |journal=J. Biol. Chem. |volume=272 |issue= 42 |pages= 26604-10 |year= 1997 |pmid= 9334241 |doi= }}
*{{cite journal | author=Levanon D, Goldstein RE, Bernstein Y, ''et al.'' |title=Transcriptional repression by AML1 and LEF-1 is mediated by the TLE/Groucho corepressors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 20 |pages= 11590-5 |year= 1998 |pmid= 9751710 |doi= }}
*{{cite journal | author=Grbavec D, Lo R, Liu Y, ''et al.'' |title=Groucho/transducin-like enhancer of split (TLE) family members interact with the yeast transcriptional co-repressor SSN6 and mammalian SSN6-related proteins: implications for evolutionary conservation of transcription repression mechanisms. |journal=Biochem. J. |volume=337 ( Pt 1) |issue= |pages= 13-7 |year= 1999 |pmid= 9854018 |doi= }}
*{{cite journal | author=Grbavec D, Lo R, Liu Y, Stifani S |title=Transducin-like Enhancer of split 2, a mammalian homologue of Drosophila Groucho, acts as a transcriptional repressor, interacts with Hairy/Enhancer of split proteins, and is expressed during neuronal development. |journal=Eur. J. Biochem. |volume=258 |issue= 2 |pages= 339-49 |year= 1999 |pmid= 9874198 |doi= }}
*{{cite journal | author=Ren B, Chee KJ, Kim TH, Maniatis T |title=PRDI-BF1/Blimp-1 repression is mediated by corepressors of the Groucho family of proteins. |journal=Genes Dev. |volume=13 |issue= 1 |pages= 125-37 |year= 1999 |pmid= 9887105 |doi= }}
*{{cite journal | author=Tetsuka T, Uranishi H, Imai H, ''et al.'' |title=Inhibition of nuclear factor-kappaB-mediated transcription by association with the amino-terminal enhancer of split, a Groucho-related protein lacking WD40 repeats. |journal=J. Biol. Chem. |volume=275 |issue= 6 |pages= 4383-90 |year= 2000 |pmid= 10660609 |doi= }}
*{{cite journal | author=Wang JC, Waltner-Law M, Yamada K, ''et al.'' |title=Transducin-like enhancer of split proteins, the human homologs of Drosophila groucho, interact with hepatic nuclear factor 3beta. |journal=J. Biol. Chem. |volume=275 |issue= 24 |pages= 18418-23 |year= 2000 |pmid= 10748198 |doi= 10.1074/jbc.M910211199 }}
*{{cite journal | author=Yao J, Lai E, Stifani S |title=The winged-helix protein brain factor 1 interacts with groucho and hes proteins to repress transcription. |journal=Mol. Cell. Biol. |volume=21 |issue= 6 |pages= 1962-72 |year= 2001 |pmid= 11238932 |doi= 10.1128/MCB.21.6.1962-1972.2001 }}
*{{cite journal | author=Gao X, Chandra T, Gratton MO, ''et al.'' |title=HES6 acts as a transcriptional repressor in myoblasts and can induce the myogenic differentiation program. |journal=J. Cell Biol. |volume=154 |issue= 6 |pages= 1161-71 |year= 2001 |pmid= 11551980 |doi= 10.1083/jcb.200104058 }}
*{{cite journal | author=Dasen JS, Barbera JP, Herman TS, ''et al.'' |title=Temporal regulation of a paired-like homeodomain repressor/TLE corepressor complex and a related activator is required for pituitary organogenesis. |journal=Genes Dev. |volume=15 |issue= 23 |pages= 3193-207 |year= 2001 |pmid= 11731482 |doi= 10.1101/gad.932601 }}
*{{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=Liu F, Liu Y, Li D, ''et al.'' |title=The transcription co-repressor TLE1 interacted with the intracellular region of gpl30 through its Q domain. |journal=Mol. Cell. Biochem. |volume=232 |issue= 1-2 |pages= 163-7 |year= 2003 |pmid= 12030375 |doi= }}
*{{cite journal | author=Pickles LM, Roe SM, Hemingway EJ, ''et al.'' |title=Crystal structure of the C-terminal WD40 repeat domain of the human Groucho/TLE1 transcriptional corepressor. |journal=Structure |volume=10 |issue= 6 |pages= 751-61 |year= 2003 |pmid= 12057191 |doi= }}
}}
{{refend}}
{{protein-stub}}
end log.
