Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 07:04, 19 November 2007 (UTC)
[edit]Proteins without matches (6)
[edit]Proteins with a High Potential Match (11)
[edit]Redirected Proteins (8)
[edit]Manual Inspection (Page not found) (17)
[edit]Updated with Warning (1)
[edit]
Protein Status Grid - Date: 07:04, 19 November 2007 (UTC)
[edit]Vebose Log - Date: 07:04, 19 November 2007 (UTC)
[edit]- INFO: Beginning work on AGA... {November 18, 2007 10:39:12 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:39:47 PM PST}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_AGA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1apy.
| PDB = {{PDB2|1apy}}, {{PDB2|1apz}}
| Name = Aspartylglucosaminidase
| HGNCid = 318
| Symbol = AGA
| AltSymbols =; AGU; ASRG; GA
| OMIM = 208400
| ECnumber =
| Homologene = 13
| MGIid = 104873
| GeneAtlas_image1 = PBB_GE_AGA_204333_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_AGA_204332_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_AGA_216064_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003948 |text = N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005764 |text = lysosome}}
| Process = {{GNF_GO|id=GO:0006517 |text = protein deglycosylation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 175
| Hs_Ensembl = ENSG00000038002
| Hs_RefseqProtein = NP_000018
| Hs_RefseqmRNA = NM_000027
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 178588918
| Hs_GenLoc_end = 178600585
| Hs_Uniprot = P20933
| Mm_EntrezGene = 11593
| Mm_Ensembl = ENSMUSG00000031521
| Mm_RefseqmRNA = NM_001005847
| Mm_RefseqProtein = NP_001005847
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 55010424
| Mm_GenLoc_end = 55022120
| Mm_Uniprot = Q64191
}}
}}
'''Aspartylglucosaminidase''', also known as '''AGA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AGA aspartylglucosaminidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=175| 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 = Aspartylglucosaminidase is involved in the catabolism of N-linked oligosaccharides of glycoproteins. It cleaves asparagine from N-acetylglucosamines as one of the final steps in the lysosomal breakdown of glycoproteins. The lysosomal storage disease aspartylglycosaminuria is caused by a deficiency in the AGA enzyme.<ref name="entrez">{{cite web | title = Entrez Gene: AGA aspartylglucosaminidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=175| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ikonen E, Peltonen L |title=Mutations causing aspartylglucosaminuria (AGU): a lysosomal accumulation disease. |journal=Hum. Mutat. |volume=1 |issue= 5 |pages= 361-5 |year= 1993 |pmid= 1301945 |doi= 10.1002/humu.1380010503 }}
*{{cite journal | author=Mononen I, Fisher KJ, Kaartinen V, Aronson NN |title=Aspartylglycosaminuria: protein chemistry and molecular biology of the most common lysosomal storage disorder of glycoprotein degradation. |journal=FASEB J. |volume=7 |issue= 13 |pages= 1247-56 |year= 1993 |pmid= 8405810 |doi= }}
*{{cite journal | author=Enomaa N, Heiskanen T, Halila R, ''et al.'' |title=Human aspartylglucosaminidase. A biochemical and immunocytochemical characterization of the enzyme in normal and aspartylglucosaminuria fibroblasts. |journal=Biochem. J. |volume=286 ( Pt 2) |issue= |pages= 613-8 |year= 1992 |pmid= 1530592 |doi= }}
*{{cite journal | author=Ikonen E, Baumann M, Grön K, ''et al.'' |title=Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease. |journal=EMBO J. |volume=10 |issue= 1 |pages= 51-8 |year= 1991 |pmid= 1703489 |doi= }}
*{{cite journal | author=Morris C, Heisterkamp N, Groffen J, ''et al.'' |title=Chromosomal localization of the human glycoasparaginase gene to 4q32-q33. |journal=Hum. Genet. |volume=88 |issue= 3 |pages= 295-7 |year= 1992 |pmid= 1733831 |doi= }}
*{{cite journal | author=Ikonen E, Enomaa N, Ulmanen I, Peltonen L |title=In vitro mutagenesis helps to unravel the biological consequences of aspartylglucosaminuria mutation. |journal=Genomics |volume=11 |issue= 1 |pages= 206-11 |year= 1992 |pmid= 1765378 |doi= }}
*{{cite journal | author=Park H, Fisher KJ, Aronson NN |title=Genomic structure of human lysosomal glycosylasparaginase. |journal=FEBS Lett. |volume=288 |issue= 1-2 |pages= 168-72 |year= 1991 |pmid= 1840528 |doi= }}
*{{cite journal | author=Mononen T, Mononen I, Matilainen R, Airaksinen E |title=High prevalence of aspartylglycosaminuria among school-age children in eastern Finland. |journal=Hum. Genet. |volume=87 |issue= 3 |pages= 266-8 |year= 1991 |pmid= 1864600 |doi= }}
*{{cite journal | author=Fisher KJ, Aronson NN |title=Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients. Amino acid substitution Cys163----Ser abolishes the activity of lysosomal glycosylasparaginase and its conversion into subunits. |journal=J. Biol. Chem. |volume=266 |issue= 18 |pages= 12105-13 |year= 1991 |pmid= 1904874 |doi= }}
*{{cite journal | author=Mononen I, Heisterkamp N, Kaartinen V, ''et al.'' |title=Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 7 |pages= 2941-5 |year= 1991 |pmid= 2011603 |doi= }}
*{{cite journal | author=Halila R, Baumann M, Ikonen E, ''et al.'' |title=Human leucocyte aspartylglucosaminidase. Evidence for two different subunits in a more complex native structure. |journal=Biochem. J. |volume=276 ( Pt 1) |issue= |pages= 251-6 |year= 1991 |pmid= 2039475 |doi= }}
*{{cite journal | author=Fisher KJ, Tollersrud OK, Aronson NN |title=Cloning and sequence analysis of a cDNA for human glycosylasparaginase. A single gene encodes the subunits of this lysosomal amidase. |journal=FEBS Lett. |volume=276 |issue= 1-2 |pages= 232 |year= 1991 |pmid= 2265705 |doi= }}
*{{cite journal | author=Fisher KJ, Tollersrud OK, Aronson NN |title=Cloning and sequence analysis of a cDNA for human glycosylasparaginase. A single gene encodes the subunits of this lysosomal amidase. |journal=FEBS Lett. |volume=269 |issue= 2 |pages= 440-4 |year= 1990 |pmid= 2401370 |doi= }}
*{{cite journal | author=Tollersrud OK, Aronson NN |title=Purification and characterization of rat liver glycosylasparaginase. |journal=Biochem. J. |volume=260 |issue= 1 |pages= 101-8 |year= 1989 |pmid= 2775174 |doi= }}
*{{cite journal | author=Hreidarsson S, Thomas GH, Valle DL, ''et al.'' |title=Aspartylglucosaminuria in the United States. |journal=Clin. Genet. |volume=23 |issue= 6 |pages= 427-35 |year= 1983 |pmid= 6883788 |doi= }}
*{{cite journal | author=Enomaa NE, Lukinmaa PL, Ikonen EM, ''et al.'' |title=Expression of aspartylglucosaminidase in human tissues from normal individuals and aspartylglucosaminuria patients. |journal=J. Histochem. Cytochem. |volume=41 |issue= 7 |pages= 981-9 |year= 1993 |pmid= 7685790 |doi= }}
*{{cite journal | author=McCormack AL, Mononen I, Kaartinen V, Yates JR |title=Localization of the disulfide bond involved in post-translational processing of glycosylasparaginase and disrupted by a mutation in the Finnish-type aspartylglycosaminuria. |journal=J. Biol. Chem. |volume=270 |issue= 7 |pages= 3212-5 |year= 1995 |pmid= 7852406 |doi= }}
*{{cite journal | author=Tollersrud OK, Heiskanen T, Peltonen L |title=Human leucocyte glycosylasparaginase is an alpha/beta-heterodimer of 19 kDa alpha-subunit and 17 and 18 kDa beta-subunit. |journal=Biochem. J. |volume=300 ( Pt 2) |issue= |pages= 541-4 |year= 1994 |pmid= 8002961 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on AMPH... {November 18, 2007 10:39:48 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:40:08 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Amphiphysin (Stiff-Man syndrome with breast cancer 128kDa autoantigen)
| HGNCid = 471
| Symbol = AMPH
| AltSymbols =; AMPH1
| OMIM = 600418
| ECnumber =
| Homologene = 36072
| MGIid = 103574
| GeneAtlas_image1 = PBB_GE_AMPH_205257_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0008021 |text = synaptic vesicle}} {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}}
| Process = {{GNF_GO|id=GO:0006897 |text = endocytosis}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 273
| Hs_Ensembl = ENSG00000078053
| Hs_RefseqProtein = NP_001626
| Hs_RefseqmRNA = NM_001635
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 38389832
| Hs_GenLoc_end = 38637545
| Hs_Uniprot = P49418
| Mm_EntrezGene = 218038
| Mm_Ensembl = ENSMUSG00000021314
| Mm_RefseqmRNA = NM_175007
| Mm_RefseqProtein = NP_778172
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 18955836
| Mm_GenLoc_end = 19158380
| Mm_Uniprot = Q80YA2
}}
}}
'''Amphiphysin (Stiff-Man syndrome with breast cancer 128kDa autoantigen)''', also known as '''AMPH''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AMPH amphiphysin (Stiff-Man syndrome with breast cancer 128kDa autoantigen)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=273| 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 protein associated with the cytoplasmic surface of synaptic vesicles. A subset of patients with stiff-man syndrome who were also affected by breast cancer are positive for autoantibodies against this protein. Alternate splicing of this gene results in two transcript variants encoding different isoforms. Additional splice variants have been described, but their full length sequences have not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: AMPH amphiphysin (Stiff-Man syndrome with breast cancer 128kDa autoantigen)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=273| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lichte B, Veh RW, Meyer HE, Kilimann MW |title=Amphiphysin, a novel protein associated with synaptic vesicles. |journal=EMBO J. |volume=11 |issue= 7 |pages= 2521-30 |year= 1992 |pmid= 1628617 |doi= }}
*{{cite journal | author=Yamamoto R, Li X, Winter S, ''et al.'' |title=Primary structure of human amphiphysin, the dominant autoantigen of paraneoplastic stiff-man syndrome, and mapping of its gene (AMPH) to chromosome 7p13-p14. |journal=Hum. Mol. Genet. |volume=4 |issue= 2 |pages= 265-8 |year= 1995 |pmid= 7757077 |doi= }}
*{{cite journal | author=David C, Solimena M, De Camilli P |title=Autoimmunity in stiff-Man syndrome with breast cancer is targeted to the C-terminal region of human amphiphysin, a protein similar to the yeast proteins, Rvs167 and Rvs161. |journal=FEBS Lett. |volume=351 |issue= 1 |pages= 73-9 |year= 1994 |pmid= 8076697 |doi= }}
*{{cite journal | author=De Camilli P, Thomas A, Cofiell R, ''et al.'' |title=The synaptic vesicle-associated protein amphiphysin is the 128-kD autoantigen of Stiff-Man syndrome with breast cancer. |journal=J. Exp. Med. |volume=178 |issue= 6 |pages= 2219-23 |year= 1993 |pmid= 8245793 |doi= }}
*{{cite journal | author=David C, McPherson PS, Mundigl O, de Camilli P |title=A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 1 |pages= 331-5 |year= 1996 |pmid= 8552632 |doi= }}
*{{cite journal | author=Grabs D, Slepnev VI, Songyang Z, ''et al.'' |title=The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding consensus sequence. |journal=J. Biol. Chem. |volume=272 |issue= 20 |pages= 13419-25 |year= 1997 |pmid= 9148966 |doi= }}
*{{cite journal | author=Butler MH, David C, Ochoa GC, ''et al.'' |title=Amphiphysin II (SH3P9; BIN1), a member of the amphiphysin/Rvs family, is concentrated in the cortical cytomatrix of axon initial segments and nodes of ranvier in brain and around T tubules in skeletal muscle. |journal=J. Cell Biol. |volume=137 |issue= 6 |pages= 1355-67 |year= 1997 |pmid= 9182667 |doi= }}
*{{cite journal | author=Ramjaun AR, Micheva KD, Bouchelet I, McPherson PS |title=Identification and characterization of a nerve terminal-enriched amphiphysin isoform. |journal=J. Biol. Chem. |volume=272 |issue= 26 |pages= 16700-6 |year= 1997 |pmid= 9195986 |doi= }}
*{{cite journal | author=McMahon HT, Wigge P, Smith C |title=Clathrin interacts specifically with amphiphysin and is displaced by dynamin. |journal=FEBS Lett. |volume=413 |issue= 2 |pages= 319-22 |year= 1997 |pmid= 9280305 |doi= }}
*{{cite journal | author=Micheva KD, Ramjaun AR, Kay BK, McPherson PS |title=SH3 domain-dependent interactions of endophilin with amphiphysin. |journal=FEBS Lett. |volume=414 |issue= 2 |pages= 308-12 |year= 1997 |pmid= 9315708 |doi= }}
*{{cite journal | author=Wigge P, Köhler K, Vallis Y, ''et al.'' |title=Amphiphysin heterodimers: potential role in clathrin-mediated endocytosis. |journal=Mol. Biol. Cell |volume=8 |issue= 10 |pages= 2003-15 |year= 1997 |pmid= 9348539 |doi= }}
*{{cite journal | author=Floyd S, Butler MH, Cremona O, ''et al.'' |title=Expression of amphiphysin I, an autoantigen of paraneoplastic neurological syndromes, in breast cancer. |journal=Mol. Med. |volume=4 |issue= 1 |pages= 29-39 |year= 1998 |pmid= 9513187 |doi= }}
*{{cite journal | author=Ramjaun AR, McPherson PS |title=Multiple amphiphysin II splice variants display differential clathrin binding: identification of two distinct clathrin-binding sites. |journal=J. Neurochem. |volume=70 |issue= 6 |pages= 2369-76 |year= 1998 |pmid= 9603201 |doi= }}
*{{cite journal | author=Slepnev VI, Ochoa GC, Butler MH, ''et al.'' |title=Role of phosphorylation in regulation of the assembly of endocytic coat complexes. |journal=Science |volume=281 |issue= 5378 |pages= 821-4 |year= 1998 |pmid= 9694653 |doi= }}
*{{cite journal | author=Cestra G, Castagnoli L, Dente L, ''et al.'' |title=The SH3 domains of endophilin and amphiphysin bind to the proline-rich region of synaptojanin 1 at distinct sites that display an unconventional binding specificity. |journal=J. Biol. Chem. |volume=274 |issue= 45 |pages= 32001-7 |year= 1999 |pmid= 10542231 |doi= }}
*{{cite journal | author=Slepnev VI, Ochoa GC, Butler MH, De Camilli P |title=Tandem arrangement of the clathrin and AP-2 binding domains in amphiphysin 1 and disruption of clathrin coat function by amphiphysin fragments comprising these sites. |journal=J. Biol. Chem. |volume=275 |issue= 23 |pages= 17583-9 |year= 2000 |pmid= 10748223 |doi= 10.1074/jbc.M910430199 }}
*{{cite journal | author=Lee C, Kim SR, Chung JK, ''et al.'' |title=Inhibition of phospholipase D by amphiphysins. |journal=J. Biol. Chem. |volume=275 |issue= 25 |pages= 18751-8 |year= 2000 |pmid= 10764771 |doi= 10.1074/jbc.M001695200 }}
*{{cite journal | author=Onofri F, Giovedi S, Kao HT, ''et al.'' |title=Specificity of the binding of synapsin I to Src homology 3 domains. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29857-67 |year= 2000 |pmid= 10899172 |doi= 10.1074/jbc.M006018200 }}
*{{cite journal | author=Lai MM, Luo HR, Burnett PE, ''et al.'' |title=The calcineurin-binding protein cain is a negative regulator of synaptic vesicle endocytosis. |journal=J. Biol. Chem. |volume=275 |issue= 44 |pages= 34017-20 |year= 2000 |pmid= 10931822 |doi= 10.1074/jbc.C000429200 }}
*{{cite journal | author=Floyd SR, Porro EB, Slepnev VI, ''et al.'' |title=Amphiphysin 1 binds the cyclin-dependent kinase (cdk) 5 regulatory subunit p35 and is phosphorylated by cdk5 and cdc2. |journal=J. Biol. Chem. |volume=276 |issue= 11 |pages= 8104-10 |year= 2001 |pmid= 11113134 |doi= 10.1074/jbc.M008932200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CBX1... {November 18, 2007 10:52:41 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:53:17 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CBX1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ap0.
| PDB = {{PDB2|1ap0}}, {{PDB2|1dz1}}, {{PDB2|1guw}}, {{PDB2|1s4z}}, {{PDB2|2fmm}}
| Name = Chromobox homolog 1 (HP1 beta homolog Drosophila )
| HGNCid = 1551
| Symbol = CBX1
| AltSymbols =; CBX; HP1-BETA; HP1Hs-beta; M31; MOD1
| OMIM = 604511
| ECnumber =
| Homologene = 38228
| MGIid = 105369
| GeneAtlas_image1 = PBB_GE_CBX1_201518_at_tn.png
| Function = {{GNF_GO|id=GO:0003682 |text = chromatin binding}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0000785 |text = chromatin}} {{GNF_GO|id=GO:0001939 |text = female pronucleus}} {{GNF_GO|id=GO:0001940 |text = male pronucleus}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005654 |text = nucleoplasm}} {{GNF_GO|id=GO:0005701 |text = polytene chromosome chromocenter}} {{GNF_GO|id=GO:0005720 |text = nuclear heterochromatin}} {{GNF_GO|id=GO:0005721 |text = centric heterochromatin}}
| Process = {{GNF_GO|id=GO:0006333 |text = chromatin assembly or disassembly}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10951
| Hs_Ensembl = ENSG00000108468
| Hs_RefseqProtein = NP_006798
| Hs_RefseqmRNA = NM_006807
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 43502414
| Hs_GenLoc_end = 43533806
| Hs_Uniprot = P83916
| Mm_EntrezGene = 12412
| Mm_Ensembl = ENSMUSG00000018666
| Mm_RefseqmRNA = XM_990275
| Mm_RefseqProtein = XP_995369
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 96605249
| Mm_GenLoc_end = 96624730
| Mm_Uniprot = Q7TPM0
}}
}}
'''Chromobox homolog 1 (HP1 beta homolog Drosophila )''', also known as '''CBX1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CBX1 chromobox homolog 1 (HP1 beta homolog Drosophila )| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10951| 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 = Heterochromatin protein-1 (HP1) is localized at heterochromatin sites, where it mediates gene silencing.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: CBX1 chromobox homolog 1 (HP1 beta homolog Drosophila )| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10951| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Furuta K, Chan EK, Kiyosawa K, ''et al.'' |title=Heterochromatin protein HP1Hsbeta (p25beta) and its localization with centromeres in mitosis. |journal=Chromosoma |volume=106 |issue= 1 |pages= 11-9 |year= 1997 |pmid= 9169582 |doi= }}
*{{cite journal | author=Lessard J, Baban S, Sauvageau G |title=Stage-specific expression of polycomb group genes in human bone marrow cells. |journal=Blood |volume=91 |issue= 4 |pages= 1216-24 |year= 1998 |pmid= 9454751 |doi= }}
*{{cite journal | author=Aagaard L, Laible G, Selenko P, ''et al.'' |title=Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31. |journal=EMBO J. |volume=18 |issue= 7 |pages= 1923-38 |year= 1999 |pmid= 10202156 |doi= 10.1093/emboj/18.7.1923 }}
*{{cite journal | author=Minc E, Allory Y, Worman HJ, ''et al.'' |title=Localization and phosphorylation of HP1 proteins during the cell cycle in mammalian cells. |journal=Chromosoma |volume=108 |issue= 4 |pages= 220-34 |year= 1999 |pmid= 10460410 |doi= }}
*{{cite journal | author=Murzina N, Verreault A, Laue E, Stillman B |title=Heterochromatin dynamics in mouse cells: interaction between chromatin assembly factor 1 and HP1 proteins. |journal=Mol. Cell |volume=4 |issue= 4 |pages= 529-40 |year= 1999 |pmid= 10549285 |doi= }}
*{{cite journal | author=Nielsen AL, Ortiz JA, You J, ''et al.'' |title=Interaction with members of the heterochromatin protein 1 (HP1) family and histone deacetylation are differentially involved in transcriptional silencing by members of the TIF1 family. |journal=EMBO J. |volume=18 |issue= 22 |pages= 6385-95 |year= 2000 |pmid= 10562550 |doi= 10.1093/emboj/18.22.6385 }}
*{{cite journal | author=Brasher SV, Smith BO, Fogh RH, ''et al.'' |title=The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chromo domain dimer. |journal=EMBO J. |volume=19 |issue= 7 |pages= 1587-97 |year= 2000 |pmid= 10747027 |doi= 10.1093/emboj/19.7.1587 }}
*{{cite journal | author=Zhao T, Heyduk T, Allis CD, Eissenberg JC |title=Heterochromatin protein 1 binds to nucleosomes and DNA in vitro. |journal=J. Biol. Chem. |volume=275 |issue= 36 |pages= 28332-8 |year= 2000 |pmid= 10882726 |doi= 10.1074/jbc.M003493200 }}
*{{cite journal | author=Lachner M, O'Carroll D, Rea S, ''et al.'' |title=Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. |journal=Nature |volume=410 |issue= 6824 |pages= 116-20 |year= 2001 |pmid= 11242053 |doi= 10.1038/35065132 }}
*{{cite journal | author=Bannister AJ, Zegerman P, Partridge JF, ''et al.'' |title=Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain. |journal=Nature |volume=410 |issue= 6824 |pages= 120-4 |year= 2001 |pmid= 11242054 |doi= 10.1038/35065138 }}
*{{cite journal | author=Nielsen AL, Oulad-Abdelghani M, Ortiz JA, ''et al.'' |title=Heterochromatin formation in mammalian cells: interaction between histones and HP1 proteins. |journal=Mol. Cell |volume=7 |issue= 4 |pages= 729-39 |year= 2001 |pmid= 11336697 |doi= }}
*{{cite journal | author=Andersen JS, Lyon CE, Fox AH, ''et al.'' |title=Directed proteomic analysis of the human nucleolus. |journal=Curr. Biol. |volume=12 |issue= 1 |pages= 1-11 |year= 2002 |pmid= 11790298 |doi= }}
*{{cite journal | author=Scholzen T, Endl E, Wohlenberg C, ''et al.'' |title=The Ki-67 protein interacts with members of the heterochromatin protein 1 (HP1) family: a potential role in the regulation of higher-order chromatin structure. |journal=J. Pathol. |volume=196 |issue= 2 |pages= 135-44 |year= 2002 |pmid= 11793364 |doi= 10.1002/path.1016 }}
*{{cite journal | author=Nielsen PR, Nietlispach D, Mott HR, ''et al.'' |title=Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9. |journal=Nature |volume=416 |issue= 6876 |pages= 103-7 |year= 2002 |pmid= 11882902 |doi= 10.1038/nature722 }}
*{{cite journal | author=Vassallo MF, Tanese N |title=Isoform-specific interaction of HP1 with human TAFII130. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 9 |pages= 5919-24 |year= 2002 |pmid= 11959914 |doi= 10.1073/pnas.092025499 }}
*{{cite journal | author=Hwang KK, Worman HJ |title=Gene regulation by human orthologs of Drosophila heterochromatin protein 1. |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue= 4 |pages= 1217-22 |year= 2002 |pmid= 12054505 |doi= 10.1016/S0006-291X(02)00377-7 }}
*{{cite journal | author=Bhattacharya N, Wang Z, Davitt C, ''et al.'' |title=Pim-1 associates with protein complexes necessary for mitosis. |journal=Chromosoma |volume=111 |issue= 2 |pages= 80-95 |year= 2003 |pmid= 12111331 |doi= 10.1007/s00412-002-0192-6 }}
*{{cite journal | author=Lin CY, Li CC, Huang PH, Lee FJ |title=A developmentally regulated ARF-like 5 protein (ARL5), localized to nuclei and nucleoli, interacts with heterochromatin protein 1. |journal=J. Cell. Sci. |volume=115 |issue= Pt 23 |pages= 4433-45 |year= 2003 |pmid= 12414990 |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=Festenstein R, Pagakis SN, Hiragami K, ''et al.'' |title=Modulation of heterochromatin protein 1 dynamics in primary Mammalian cells. |journal=Science |volume=299 |issue= 5607 |pages= 719-21 |year= 2003 |pmid= 12560554 |doi= 10.1126/science.1078694 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CBX3... {November 18, 2007 10:53:58 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:54:22 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- 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 = Chromobox homolog 3 (HP1 gamma homolog, Drosophila)
| HGNCid = 1553
| Symbol = CBX3
| AltSymbols =; HECH; HP1-GAMMA; HP1Hs-gamma
| OMIM = 604477
| ECnumber =
| Homologene = 40583
| MGIid = 108515
| GeneAtlas_image1 = PBB_GE_CBX3_200037_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003682 |text = chromatin binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0000785 |text = chromatin}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006333 |text = chromatin assembly or disassembly}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0016568 |text = chromatin modification}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 11335
| Hs_Ensembl =
| Hs_RefseqProtein = NP_009207
| Hs_RefseqmRNA = NM_007276
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 12417
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_001037798
| Mm_RefseqProtein = NP_001032887
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Chromobox homolog 3 (HP1 gamma homolog, Drosophila)''', also known as '''CBX3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CBX3 chromobox homolog 3 (HP1 gamma homolog, Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11335| 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 = At the nuclear envelope, the nuclear lamina and heterochromatin are adjacent to the inner nuclear membrane. The protein encoded by this gene binds DNA and is a component of heterochromatin. This protein also can bind lamin B receptor, an integral membrane protein found in the inner nuclear membrane. The dual binding functions of the encoded protein may explain the association of heterochromatin with the inner nuclear membrane. Two transcript variants encoding the same protein but differing in the 5' UTR, have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: CBX3 chromobox homolog 3 (HP1 gamma homolog, Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11335| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ye Q, Worman HJ |title=Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1. |journal=J. Biol. Chem. |volume=271 |issue= 25 |pages= 14653-6 |year= 1996 |pmid= 8663349 |doi= }}
*{{cite journal | author=Ye Q, Callebaut I, Pezhman A, ''et al.'' |title=Domain-specific interactions of human HP1-type chromodomain proteins and inner nuclear membrane protein LBR. |journal=J. Biol. Chem. |volume=272 |issue= 23 |pages= 14983-9 |year= 1997 |pmid= 9169472 |doi= }}
*{{cite journal | author=Lessard J, Baban S, Sauvageau G |title=Stage-specific expression of polycomb group genes in human bone marrow cells. |journal=Blood |volume=91 |issue= 4 |pages= 1216-24 |year= 1998 |pmid= 9454751 |doi= }}
*{{cite journal | author=Seeler JS, Marchio A, Sitterlin D, ''et al.'' |title=Interaction of SP100 with HP1 proteins: a link between the promyelocytic leukemia-associated nuclear bodies and the chromatin compartment. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 13 |pages= 7316-21 |year= 1998 |pmid= 9636146 |doi= }}
*{{cite journal | author=Lehming N, Le Saux A, Schüller J, Ptashne M |title=Chromatin components as part of a putative transcriptional repressing complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 13 |pages= 7322-6 |year= 1998 |pmid= 9636147 |doi= }}
*{{cite journal | author=Ainsztein AM, Kandels-Lewis SE, Mackay AM, Earnshaw WC |title=INCENP centromere and spindle targeting: identification of essential conserved motifs and involvement of heterochromatin protein HP1. |journal=J. Cell Biol. |volume=143 |issue= 7 |pages= 1763-74 |year= 1999 |pmid= 9864353 |doi= }}
*{{cite journal | author=Ryan RF, Schultz DC, Ayyanathan K, ''et al.'' |title=KAP-1 corepressor protein interacts and colocalizes with heterochromatic and euchromatic HP1 proteins: a potential role for Krüppel-associated box-zinc finger proteins in heterochromatin-mediated gene silencing. |journal=Mol. Cell. Biol. |volume=19 |issue= 6 |pages= 4366-78 |year= 1999 |pmid= 10330177 |doi= }}
*{{cite journal | author=Minc E, Allory Y, Worman HJ, ''et al.'' |title=Localization and phosphorylation of HP1 proteins during the cell cycle in mammalian cells. |journal=Chromosoma |volume=108 |issue= 4 |pages= 220-34 |year= 1999 |pmid= 10460410 |doi= }}
*{{cite journal | author=Nielsen AL, Ortiz JA, You J, ''et al.'' |title=Interaction with members of the heterochromatin protein 1 (HP1) family and histone deacetylation are differentially involved in transcriptional silencing by members of the TIF1 family. |journal=EMBO J. |volume=18 |issue= 22 |pages= 6385-95 |year= 2000 |pmid= 10562550 |doi= 10.1093/emboj/18.22.6385 }}
*{{cite journal | author=Koike N, Maita H, Taira T, ''et al.'' |title=Identification of heterochromatin protein 1 (HP1) as a phosphorylation target by Pim-1 kinase and the effect of phosphorylation on the transcriptional repression function of HP1(1). |journal=FEBS Lett. |volume=467 |issue= 1 |pages= 17-21 |year= 2000 |pmid= 10664448 |doi= }}
*{{cite journal | author=Minc E, Courvalin JC, Buendia B |title=HP1gamma associates with euchromatin and heterochromatin in mammalian nuclei and chromosomes. |journal=Cytogenet. Cell Genet. |volume=90 |issue= 3-4 |pages= 279-84 |year= 2001 |pmid= 11124534 |doi= }}
*{{cite journal | author=Lachner M, O'Carroll D, Rea S, ''et al.'' |title=Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. |journal=Nature |volume=410 |issue= 6824 |pages= 116-20 |year= 2001 |pmid= 11242053 |doi= 10.1038/35065132 }}
*{{cite journal | author=Nielsen AL, Oulad-Abdelghani M, Ortiz JA, ''et al.'' |title=Heterochromatin formation in mammalian cells: interaction between histones and HP1 proteins. |journal=Mol. Cell |volume=7 |issue= 4 |pages= 729-39 |year= 2001 |pmid= 11336697 |doi= }}
*{{cite journal | author=Scholzen T, Endl E, Wohlenberg C, ''et al.'' |title=The Ki-67 protein interacts with members of the heterochromatin protein 1 (HP1) family: a potential role in the regulation of higher-order chromatin structure. |journal=J. Pathol. |volume=196 |issue= 2 |pages= 135-44 |year= 2002 |pmid= 11793364 |doi= 10.1002/path.1016 }}
*{{cite journal | author=Vassallo MF, Tanese N |title=Isoform-specific interaction of HP1 with human TAFII130. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 9 |pages= 5919-24 |year= 2002 |pmid= 11959914 |doi= 10.1073/pnas.092025499 }}
*{{cite journal | author=Ogawa H, Ishiguro K, Gaubatz S, ''et al.'' |title=A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells. |journal=Science |volume=296 |issue= 5570 |pages= 1132-6 |year= 2002 |pmid= 12004135 |doi= 10.1126/science.1069861 }}
*{{cite journal | author=Hwang KK, Worman HJ |title=Gene regulation by human orthologs of Drosophila heterochromatin protein 1. |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue= 4 |pages= 1217-22 |year= 2002 |pmid= 12054505 |doi= 10.1016/S0006-291X(02)00377-7 }}
*{{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=Kametaka A, Takagi M, Hayakawa T, ''et al.'' |title=Interaction of the chromatin compaction-inducing domain (LR domain) of Ki-67 antigen with HP1 proteins. |journal=Genes Cells |volume=7 |issue= 12 |pages= 1231-42 |year= 2003 |pmid= 12485163 |doi= }}
*{{cite journal | author=Cheutin T, McNairn AJ, Jenuwein T, ''et al.'' |title=Maintenance of stable heterochromatin domains by dynamic HP1 binding. |journal=Science |volume=299 |issue= 5607 |pages= 721-5 |year= 2003 |pmid= 12560555 |doi= 10.1126/science.1078572 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CNTF... {November 18, 2007 10:40:08 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:40:28 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_CNTF_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cnt.
| PDB = {{PDB2|1cnt}}
| Name = Ciliary neurotrophic factor
| HGNCid = 2169
| Symbol = CNTF
| AltSymbols =; HCNTF
| OMIM = 118945
| ECnumber =
| Homologene = 8288
| MGIid = 88439
| GeneAtlas_image1 = PBB_GE_CNTF_208597_at_tn.png
| Function = {{GNF_GO|id=GO:0005127 |text = ciliary neurotrophic factor receptor binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0040007 |text = growth}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1270
| Hs_Ensembl = ENSG00000205003
| Hs_RefseqProtein = NP_000605
| Hs_RefseqmRNA = NM_000614
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 58146721
| Hs_GenLoc_end = 58149778
| Hs_Uniprot = P26441
| Mm_EntrezGene = 12803
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_053007
| Mm_RefseqProtein = NP_443733
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Ciliary neurotrophic factor''', also known as '''CNTF''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CNTF ciliary neurotrophic factor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1270| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.<ref name="entrez">{{cite web | title = Entrez Gene: CNTF ciliary neurotrophic factor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1270| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Sendtner M, Carroll P, Holtmann B, ''et al.'' |title=Ciliary neurotrophic factor. |journal=J. Neurobiol. |volume=25 |issue= 11 |pages= 1436-53 |year= 1995 |pmid= 7852996 |doi= 10.1002/neu.480251110 }}
*{{cite journal | author=Sleeman MW, Anderson KD, Lambert PD, ''et al.'' |title=The ciliary neurotrophic factor and its receptor, CNTFR alpha. |journal=Pharmaceutica acta Helvetiae |volume=74 |issue= 2-3 |pages= 265-72 |year= 2000 |pmid= 10812968 |doi= }}
*{{cite journal | author=Schooltink H, Stoyan T, Roeb E, ''et al.'' |title=Ciliary neurotrophic factor induces acute-phase protein expression in hepatocytes. |journal=FEBS Lett. |volume=314 |issue= 3 |pages= 280-4 |year= 1993 |pmid= 1281789 |doi= }}
*{{cite journal | author=Bazan JF |title=Neuropoietic cytokines in the hematopoietic fold. |journal=Neuron |volume=7 |issue= 2 |pages= 197-208 |year= 1991 |pmid= 1714745 |doi= }}
*{{cite journal | author=Lam A, Fuller F, Miller J, ''et al.'' |title=Sequence and structural organization of the human gene encoding ciliary neurotrophic factor. |journal=Gene |volume=102 |issue= 2 |pages= 271-6 |year= 1991 |pmid= 1840538 |doi= }}
*{{cite journal | author=Masiakowski P, Liu HX, Radziejewski C, ''et al.'' |title=Recombinant human and rat ciliary neurotrophic factors. |journal=J. Neurochem. |volume=57 |issue= 3 |pages= 1003-12 |year= 1991 |pmid= 1861138 |doi= }}
*{{cite journal | author=McDonald JR, Ko C, Mismer D, ''et al.'' |title=Expression and characterization of recombinant human ciliary neurotrophic factor from Escherichia coli. |journal=Biochim. Biophys. Acta |volume=1090 |issue= 1 |pages= 70-80 |year= 1991 |pmid= 1883844 |doi= }}
*{{cite journal | author=Negro A, Tolosano E, Skaper SD, ''et al.'' |title=Cloning and expression of human ciliary neurotrophic factor. |journal=Eur. J. Biochem. |volume=201 |issue= 1 |pages= 289-94 |year= 1991 |pmid= 1915374 |doi= }}
*{{cite journal | author=Lichter P, Tang CJ, Call K, ''et al.'' |title=High-resolution mapping of human chromosome 11 by in situ hybridization with cosmid clones. |journal=Science |volume=247 |issue= 4938 |pages= 64-9 |year= 1990 |pmid= 2294592 |doi= }}
*{{cite journal | author=Winter CG, Saotome Y, Levison SW, Hirsh D |title=A role for ciliary neurotrophic factor as an inducer of reactive gliosis, the glial response to central nervous system injury. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 13 |pages= 5865-9 |year= 1995 |pmid= 7597043 |doi= }}
*{{cite journal | author=Yokoji H, Ariyama T, Takahashi R, ''et al.'' |title=cDNA cloning and chromosomal localization of the human ciliary neurotrophic factor gene. |journal=Neurosci. Lett. |volume=185 |issue= 3 |pages= 175-8 |year= 1995 |pmid= 7753485 |doi= }}
*{{cite journal | author=McDonald NQ, Panayotatos N, Hendrickson WA |title=Crystal structure of dimeric human ciliary neurotrophic factor determined by MAD phasing. |journal=EMBO J. |volume=14 |issue= 12 |pages= 2689-99 |year= 1995 |pmid= 7796798 |doi= }}
*{{cite journal | author=Saggio I, Paonessa G, Gloaguen I, ''et al.'' |title=Nonradioactive receptor binding assay for ciliary neurotrophic factor. |journal=Anal. Biochem. |volume=221 |issue= 2 |pages= 387-91 |year= 1995 |pmid= 7810882 |doi= }}
*{{cite journal | author=Takahashi R, Yokoji H, Misawa H, ''et al.'' |title=A null mutation in the human CNTF gene is not causally related to neurological diseases. |journal=Nat. Genet. |volume=7 |issue= 1 |pages= 79-84 |year= 1994 |pmid= 8075647 |doi= 10.1038/ng0594-79 }}
*{{cite journal | author=Giovannini M, Romo AJ, Evans GA |title=Chromosomal localization of the human ciliary neurotrophic factor gene (CNTF) to 11q12 by fluorescence in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=63 |issue= 1 |pages= 62-3 |year= 1993 |pmid= 8449041 |doi= }}
*{{cite journal | author=Robledo O, Auguste P, Coupey L, ''et al.'' |title=Binding interactions of leukemia inhibitory factor and ciliary neurotrophic factor with the different subunits of their high affinity receptors. |journal=J. Neurochem. |volume=66 |issue= 4 |pages= 1391-9 |year= 1996 |pmid= 8627290 |doi= }}
*{{cite journal | author=Gutman CR, Strittmatter WJ, Weisgraber KH, Matthew WD |title=Apolipoprotein E binds to and potentiates the biological activity of ciliary neurotrophic factor. |journal=J. Neurosci. |volume=17 |issue= 16 |pages= 6114-21 |year= 1997 |pmid= 9236223 |doi= }}
*{{cite journal | author=Cargill M, Altshuler D, Ireland J, ''et al.'' |title=Characterization of single-nucleotide polymorphisms in coding regions of human genes. |journal=Nat. Genet. |volume=22 |issue= 3 |pages= 231-8 |year= 1999 |pmid= 10391209 |doi= 10.1038/10290 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on COPS6... {November 18, 2007 10:53:17 PM PST}
- SEARCH REDIRECT: Control Box Found: COPS6 {November 18, 2007 10:53:48 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:53:52 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:53:52 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:53:52 PM PST}
- UPDATED: Updated protein page: COPS6 {November 18, 2007 10:53:58 PM PST}
- INFO: Beginning work on CYB5A... {November 18, 2007 10:40:28 PM PST}
- SEARCH REDIRECT: Control Box Found: Cytochrome b5, type A {November 18, 2007 10:40:56 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:40:57 PM PST}
- SKIP SUMMARY: SKIPPING Summary, No Errors. {November 18, 2007 10:40:57 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:40:57 PM PST}
- UPDATED: Warning while updating page: Could not find summary box. {November 18, 2007 10:41:04 PM PST}
- UPDATED: Updated protein page (with warnings): Cytochrome b5, type A {November 18, 2007 10:41:04 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CYB5A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cyo.
| PDB = {{PDB2|1cyo}}, {{PDB2|1do9}}, {{PDB2|1ehb}}, {{PDB2|1es1}}, {{PDB2|1f03}}, {{PDB2|1f04}}, {{PDB2|1i5u}}, {{PDB2|1j0q}}, {{PDB2|1lqx}}, {{PDB2|1lr6}}, {{PDB2|1m20}}, {{PDB2|1m2i}}, {{PDB2|1m2m}}, {{PDB2|1m59}}, {{PDB2|1nx7}}, {{PDB2|1sh4}}, {{PDB2|1u9m}}, {{PDB2|1u9u}}
| Name = Cytochrome b5 type A (microsomal)
| HGNCid = 2570
| Symbol = CYB5A
| AltSymbols =; CYB5; MCB5
| OMIM = 250790
| ECnumber =
| Homologene = 41475
| MGIid = 1926952
| GeneAtlas_image1 = PBB_GE_CYB5A_215726_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CYB5A_207843_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_CYB5A_209366_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004129 |text = cytochrome-c oxidase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006810 |text = transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1528
| Hs_Ensembl = ENSG00000166347
| Hs_RefseqProtein = NP_001905
| Hs_RefseqmRNA = NM_001914
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 18
| Hs_GenLoc_start = 70071508
| Hs_GenLoc_end = 70110201
| Hs_Uniprot = P00167
| Mm_EntrezGene = 109672
| Mm_Ensembl = ENSMUSG00000024646
| Mm_RefseqmRNA = NM_025797
| Mm_RefseqProtein = NP_080073
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 18
| Mm_GenLoc_start = 84985602
| Mm_GenLoc_end = 85014051
| Mm_Uniprot = Q544Z9
}}
}}
'''Cytochrome b5 type A (microsomal)''', also known as '''CYB5A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CYB5A cytochrome b5 type A (microsomal)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1528| 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=Ng S, Smith MB, Smith HT, Millett F |title=Effect of modification of individual cytochrome c lysines on the reaction with cytochrome b5. |journal=Biochemistry |volume=16 |issue= 23 |pages= 4975-8 |year= 1977 |pmid= 199233 |doi= }}
*{{cite journal | author=Dailey HA, Strittmatter P |title=Modification and identification of cytochrome b5 carboxyl groups involved in protein-protein interaction with cytochrome b5 reductase. |journal=J. Biol. Chem. |volume=254 |issue= 12 |pages= 5388-96 |year= 1979 |pmid= 221468 |doi= }}
*{{cite journal | author=Mitoma J, Ito A |title=The carboxy-terminal 10 amino acid residues of cytochrome b5 are necessary for its targeting to the endoplasmic reticulum. |journal=EMBO J. |volume=11 |issue= 11 |pages= 4197-203 |year= 1992 |pmid= 1396600 |doi= }}
*{{cite journal | author=Giordano SJ, Steggles AW |title=The human liver and reticulocyte cytochrome b5 mRNAs are products from a single gene. |journal=Biochem. Biophys. Res. Commun. |volume=178 |issue= 1 |pages= 38-44 |year= 1991 |pmid= 1712589 |doi= }}
*{{cite journal | author=Shephard EA, Povey S, Spurr NK, Phillips IR |title=Chromosomal localization of a cytochrome b5 gene to human chromosome 18 and a cytochrome b5 pseudogene to the X chromosome. |journal=Genomics |volume=11 |issue= 2 |pages= 302-8 |year= 1992 |pmid= 1840560 |doi= }}
*{{cite journal | author=Strittmatter P, Hackett CS, Korza G, Ozols J |title=Characterization of the covalent cross-links of the active sites of amidinated cytochrome b5 and NADH:cytochrome b5 reductase. |journal=J. Biol. Chem. |volume=265 |issue= 35 |pages= 21709-13 |year= 1991 |pmid= 2123873 |doi= }}
*{{cite journal | author=Ozols J |title=Structure of cytochrome b5 and its topology in the microsomal membrane. |journal=Biochim. Biophys. Acta |volume=997 |issue= 1-2 |pages= 121-30 |year= 1989 |pmid= 2752049 |doi= }}
*{{cite journal | author=Yoo M, Steggles AW |title=The complete nucleotide sequence of human liver cytochrome b5 mRNA. |journal=Biochem. Biophys. Res. Commun. |volume=156 |issue= 1 |pages= 576-80 |year= 1988 |pmid= 3178851 |doi= }}
*{{cite journal | author=Hegesh E, Hegesh J, Kaftory A |title=Congenital methemoglobinemia with a deficiency of cytochrome b5. |journal=N. Engl. J. Med. |volume=314 |issue= 12 |pages= 757-61 |year= 1986 |pmid= 3951505 |doi= }}
*{{cite journal | author=Abe K, Kimura S, Kizawa R, ''et al.'' |title=Amino acid sequences of cytochrome b5 from human, porcine, and bovine erythrocytes and comparison with liver microsomal cytochrome b5. |journal=J. Biochem. |volume=97 |issue= 6 |pages= 1659-68 |year= 1985 |pmid= 4030743 |doi= }}
*{{cite journal | author=Strittmatter P, Spatz L, Corcoran D, ''et al.'' |title=Purification and properties of rat liver microsomal stearyl coenzyme A desaturase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=71 |issue= 11 |pages= 4565-9 |year= 1975 |pmid= 4373719 |doi= }}
*{{cite journal | author=Rashid MA, Hagihara B, Kobayashi M, ''et al.'' |title=Structural studies of cytochrome b5. 3. Sequential studies on human liver cytochrome b5. |journal=J. Biochem. |volume=74 |issue= 5 |pages= 985-1002 |year= 1974 |pmid= 4770377 |doi= }}
*{{cite journal | author=Nóbrega FG, Ozols J |title=Amino acid sequences of tryptic peptides of cytochromes b5 from microsomes of human, monkey, porcine, and chicken liver. |journal=J. Biol. Chem. |volume=246 |issue= 6 |pages= 1706-17 |year= 1971 |pmid= 4993957 |doi= }}
*{{cite journal | author=Ozols J |title=Cytochrome b 5 from a normal human liver. Isolation and the partial amino acid sequence. |journal=J. Biol. Chem. |volume=247 |issue= 7 |pages= 2242-5 |year= 1972 |pmid= 5062820 |doi= }}
*{{cite journal | author=Dailey HA, Strittmatter P |title=Characterization of the interaction of amphipathic cytochrome b5 with stearyl coenzyme A desaturase and NADPH:cytochrome P-450 reductase. |journal=J. Biol. Chem. |volume=255 |issue= 11 |pages= 5184-9 |year= 1980 |pmid= 6102994 |doi= }}
*{{cite journal | author=De Silvestris M, D'Arrigo A, Borgese N |title=The targeting information of the mitochondrial outer membrane isoform of cytochrome b5 is contained within the carboxyl-terminal region. |journal=FEBS Lett. |volume=370 |issue= 1-2 |pages= 69-74 |year= 1995 |pmid= 7649306 |doi= }}
*{{cite journal | author=Li XR, Giordano SJ, Yoo M, Steggles AW |title=The isolation and characterization of the human cytochrome b5 gene. |journal=Biochem. Biophys. Res. Commun. |volume=209 |issue= 3 |pages= 894-900 |year= 1995 |pmid= 7733981 |doi= 10.1006/bbrc.1995.1582 }}
*{{cite journal | author=Giordano SJ, Yoo M, Ward DC, ''et al.'' |title=The human cytochrome b5 gene and two of its pseudogenes are located on chromosomes 18q23, 14q31-32.1 and 20p11.2, respectively. |journal=Hum. Genet. |volume=92 |issue= 6 |pages= 615-8 |year= 1994 |pmid= 8262522 |doi= }}
*{{cite journal | author=Guengerich FP, Johnson WW |title=Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: rapid reduction in the absence of substrate and variations among cytochrome P450 systems. |journal=Biochemistry |volume=36 |issue= 48 |pages= 14741-50 |year= 1998 |pmid= 9398194 |doi= 10.1021/bi9719399 }}
*{{cite journal | author=Lee-Robichaud P, Akhtar ME, Akhtar M |title=Control of androgen biosynthesis in the human through the interaction of Arg347 and Arg358 of CYP17 with cytochrome b5. |journal=Biochem. J. |volume=332 ( Pt 2) |issue= |pages= 293-6 |year= 1998 |pmid= 9601054 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CYLD... {November 18, 2007 10:41:04 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:41:44 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CYLD_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ixd.
| PDB = {{PDB2|1ixd}}, {{PDB2|1whl}}, {{PDB2|1whm}}
| Name = Cylindromatosis (turban tumor syndrome)
| HGNCid = 2584
| Symbol = CYLD
| AltSymbols =; CDMT; CYLD1; CYLDI; EAC; FLJ20180; FLJ31664; HSPC057; KIAA0849; USPL2
| OMIM = 605018
| ECnumber =
| Homologene = 9069
| MGIid = 1921506
| GeneAtlas_image1 = PBB_GE_CYLD_214272_at_tn.png
| GeneAtlas_image2 = PBB_GE_CYLD_221903_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_CYLD_221905_at_tn.png
| Function = {{GNF_GO|id=GO:0003735 |text = structural constituent of ribosome}} {{GNF_GO|id=GO:0004221 |text = ubiquitin thiolesterase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008234 |text = cysteine-type peptidase activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005840 |text = ribosome}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}}
| Process = {{GNF_GO|id=GO:0006412 |text = translation}} {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}} {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1540
| Hs_Ensembl = ENSG00000083799
| Hs_RefseqProtein = NP_001035814
| Hs_RefseqmRNA = NM_001042355
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 49333486
| Hs_GenLoc_end = 49390029
| Hs_Uniprot = Q9NQC7
| Mm_EntrezGene = 74256
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_173369
| Mm_RefseqProtein = NP_775545
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Cylindromatosis (turban tumor syndrome)''', also known as '''CYLD''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CYLD cylindromatosis (turban tumor syndrome)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1540| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is encodes a cytoplasmic protein with three cytoskeletal-associated protein-glycine-conserved (CAP-GLY) domains that functions as a deubiquitinating enzyme. Mutations in this gene have been associated with cylindromatosis, multiple familial trichoepithelioma, and Brooke-Spiegler syndrome. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.<ref name="entrez">{{cite web | title = Entrez Gene: CYLD cylindromatosis (turban tumor syndrome)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1540| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nakajima D, Okazaki N, Yamakawa H, ''et al.'' |title=Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. |journal=DNA Res. |volume=9 |issue= 3 |pages= 99-106 |year= 2003 |pmid= 12168954 |doi= }}
*{{cite journal | author=Lian F, Cockerell CJ |title=Cutaneous appendage tumors: familial cylindromatosis and associated tumors update. |journal=Advances in dermatology |volume=21 |issue= |pages= 217-34 |year= 2006 |pmid= 16350444 |doi= }}
*{{cite journal | author=Biggs PJ, Wooster R, Ford D, ''et al.'' |title=Familial cylindromatosis (turban tumour syndrome) gene localised to chromosome 16q12-q13: evidence for its role as a tumour suppressor gene. |journal=Nat. Genet. |volume=11 |issue= 4 |pages= 441-3 |year= 1996 |pmid= 7493027 |doi= 10.1038/ng1295-441 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Biggs PJ, Chapman P, Lakhani SR, ''et al.'' |title=The cylindromatosis gene (cyld1) on chromosome 16q may be the only tumour suppressor gene involved in the development of cylindromas. |journal=Oncogene |volume=12 |issue= 6 |pages= 1375-7 |year= 1996 |pmid= 8649842 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Nagase T, Ishikawa K, Suyama M, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=5 |issue= 6 |pages= 355-64 |year= 1999 |pmid= 10048485 |doi= }}
*{{cite journal | author=Thomson SA, Rasmussen SA, Zhang J, Wallace MR |title=A new hereditary cylindromatosis family associated with CYLD1 on chromosome 16. |journal=Hum. Genet. |volume=105 |issue= 1-2 |pages= 171-3 |year= 1999 |pmid= 10480375 |doi= }}
*{{cite journal | author=Bignell GR, Warren W, Seal S, ''et al.'' |title=Identification of the familial cylindromatosis tumour-suppressor gene. |journal=Nat. Genet. |volume=25 |issue= 2 |pages= 160-5 |year= 2000 |pmid= 10835629 |doi= 10.1038/76006 }}
*{{cite journal | author=Zhang QH, Ye M, Wu XY, ''et al.'' |title=Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. |journal=Genome Res. |volume=10 |issue= 10 |pages= 1546-60 |year= 2001 |pmid= 11042152 |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=Trompouki E, Hatzivassiliou E, Tsichritzis T, ''et al.'' |title=CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members. |journal=Nature |volume=424 |issue= 6950 |pages= 793-6 |year= 2003 |pmid= 12917689 |doi= 10.1038/nature01803 }}
*{{cite journal | author=Brummelkamp TR, Nijman SM, Dirac AM, Bernards R |title=Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB. |journal=Nature |volume=424 |issue= 6950 |pages= 797-801 |year= 2003 |pmid= 12917690 |doi= 10.1038/nature01811 }}
*{{cite journal | author=Kovalenko A, Chable-Bessia C, Cantarella G, ''et al.'' |title=The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination. |journal=Nature |volume=424 |issue= 6950 |pages= 801-5 |year= 2003 |pmid= 12917691 |doi= 10.1038/nature01802 }}
*{{cite journal | author=Hu G, Onder M, Gill M, ''et al.'' |title=A novel missense mutation in CYLD in a family with Brooke-Spiegler syndrome. |journal=J. Invest. Dermatol. |volume=121 |issue= 4 |pages= 732-4 |year= 2003 |pmid= 14632188 |doi= 10.1046/j.1523-1747.2003.12514.x }}
*{{cite journal | author=Regamey A, Hohl D, Liu JW, ''et al.'' |title=The tumor suppressor CYLD interacts with TRIP and regulates negatively nuclear factor kappaB activation by tumor necrosis factor. |journal=J. Exp. Med. |volume=198 |issue= 12 |pages= 1959-64 |year= 2004 |pmid= 14676304 |doi= 10.1084/jem.20031187 }}
*{{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=Zhang XJ, Liang YH, He PP, ''et al.'' |title=Identification of the cylindromatosis tumor-suppressor gene responsible for multiple familial trichoepithelioma. |journal=J. Invest. Dermatol. |volume=122 |issue= 3 |pages= 658-64 |year= 2004 |pmid= 15086550 |doi= 10.1111/j.0022-202X.2004.22321.x }}
*{{cite journal | author=Jono H, Lim JH, Chen LF, ''et al.'' |title=NF-kappaB is essential for induction of CYLD, the negative regulator of NF-kappaB: evidence for a novel inducible autoregulatory feedback pathway. |journal=J. Biol. Chem. |volume=279 |issue= 35 |pages= 36171-4 |year= 2004 |pmid= 15226292 |doi= 10.1074/jbc.M406638200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DBI... {November 18, 2007 10:41:44 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:42:18 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_DBI_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aca.
| PDB = {{PDB2|1aca}}, {{PDB2|1hb6}}, {{PDB2|1hb8}}, {{PDB2|1nti}}, {{PDB2|1nvl}}, {{PDB2|2abd}}, {{PDB2|2cb8}}, {{PDB2|2fj9}}
| Name = Diazepam binding inhibitor (GABA receptor modulator, acyl-Coenzyme A binding protein)
| HGNCid = 2690
| Symbol = DBI
| AltSymbols =; ACBP; ACBD1; CCK-RP; EP; MGC70414
| OMIM = 125950
| ECnumber =
| Homologene = 39086
| MGIid = 94865
| GeneAtlas_image1 = PBB_GE_DBI_202428_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_DBI_209389_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_DBI_211070_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000062 |text = acyl-CoA binding}} {{GNF_GO|id=GO:0005488 |text = binding}} {{GNF_GO|id=GO:0008289 |text = lipid binding}} {{GNF_GO|id=GO:0030156 |text = benzodiazepine receptor binding}}
| Component =
| Process = {{GNF_GO|id=GO:0006810 |text = transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1622
| Hs_Ensembl = ENSG00000155368
| Hs_RefseqProtein = NP_001073331
| Hs_RefseqmRNA = NM_001079862
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 119841055
| Hs_GenLoc_end = 119846586
| Hs_Uniprot = P07108
| Mm_EntrezGene = 13167
| Mm_Ensembl = ENSMUSG00000026385
| Mm_RefseqmRNA = NM_001037999
| Mm_RefseqProtein = NP_001033088
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 121940826
| Mm_GenLoc_end = 121948625
| Mm_Uniprot = Q3ULV8
}}
}}
'''Diazepam binding inhibitor (GABA receptor modulator, acyl-Coenzyme A binding protein)''', also known as '''DBI''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DBI diazepam binding inhibitor (GABA receptor modulator, acyl-Coenzyme A binding protein)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1622| 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 diazepam binding inhibitor, a protein that is regulated by hormones and is involved in lipid metabolism and the displacement of beta-carbolines and benzodiazepines, which modulate signal transduction at type A gamma-aminobutyric acid receptors located in brain synapses. The protein is conserved from yeast to mammals, with the most highly conserved domain consisting of seven contiguous residues that constitute the hydrophobic binding site for medium- and long-chain acyl-Coenzyme A esters. Diazepam binding inhibitor is also known to mediate the feedback regulation of pancreatic secretion and the postprandial release of cholecystokinin, in addition to its role as a mediator in corticotropin-dependent adrenal steroidogenesis. Three pseudogenes located on chromosomes 6, 8 and 16 have been identified. Multiple transcript variants encoding different isoforms have been described for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: DBI diazepam binding inhibitor (GABA receptor modulator, acyl-Coenzyme A binding protein)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1622| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Papadopoulos V, Brown AS |title=Role of the peripheral-type benzodiazepine receptor and the polypeptide diazepam binding inhibitor in steroidogenesis. |journal=J. Steroid Biochem. Mol. Biol. |volume=53 |issue= 1-6 |pages= 103-10 |year= 1995 |pmid= 7626442 |doi= }}
*{{cite journal | author=Costa E, Auta J, Guidotti A, ''et al.'' |title=The pharmacology of neurosteroidogenesis. |journal=J. Steroid Biochem. Mol. Biol. |volume=49 |issue= 4-6 |pages= 385-9 |year= 1994 |pmid= 8043504 |doi= }}
*{{cite journal | author=Todd S, Naylor SL |title=New chromosomal mapping assignments for argininosuccinate synthetase pseudogene 1, interferon-beta 3 gene, and the diazepam binding inhibitor gene. |journal=Somat. Cell Mol. Genet. |volume=18 |issue= 4 |pages= 381-5 |year= 1992 |pmid= 1440058 |doi= }}
*{{cite journal | author=Mandrup S, Hummel R, Ravn S, ''et al.'' |title=Acyl-CoA-binding protein/diazepam-binding inhibitor gene and pseudogenes. A typical housekeeping gene family. |journal=J. Mol. Biol. |volume=228 |issue= 3 |pages= 1011-22 |year= 1993 |pmid= 1469708 |doi= }}
*{{cite journal | author=Webb NR, Rose TM, Malik N, ''et al.'' |title=Bovine and human cDNA sequences encoding a putative benzodiazepine receptor ligand. |journal=DNA |volume=6 |issue= 1 |pages= 71-9 |year= 1987 |pmid= 2881742 |doi= }}
*{{cite journal | author=Gray PW, Glaister D, Seeburg PH, ''et al.'' |title=Cloning and expression of cDNA for human diazepam binding inhibitor, a natural ligand of an allosteric regulatory site of the gamma-aminobutyric acid type A receptor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 19 |pages= 7547-51 |year= 1986 |pmid= 3020548 |doi= }}
*{{cite journal | author=DeBernardi MA, Crowe RR, Mocchetti I, ''et al.'' |title=Chromosomal localization of the human diazepam binding inhibitor gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 17 |pages= 6561-5 |year= 1988 |pmid= 3413112 |doi= }}
*{{cite journal | author=Marquardt H, Todaro GJ, Shoyab M |title=Complete amino acid sequences of bovine and human endozepines. Homology with rat diazepam binding inhibitor. |journal=J. Biol. Chem. |volume=261 |issue= 21 |pages= 9727-31 |year= 1986 |pmid= 3525533 |doi= }}
*{{cite journal | author=Swinnen JV, Esquenet M, Heyns W, ''et al.'' |title=Androgen regulation of the messenger RNA encoding diazepam-binding inhibitor/acyl-CoA-binding protein in the human prostatic adenocarcinoma cell line LNCaP. |journal=Mol. Cell. Endocrinol. |volume=104 |issue= 2 |pages= 153-62 |year= 1995 |pmid= 7527352 |doi= }}
*{{cite journal | author=Kolmer M, Rovio A, Alho H |title=The characterization of two diazepam binding inhibitor (DBI) transcripts in humans. |journal=Biochem. J. |volume=306 ( Pt 2) |issue= |pages= 327-30 |year= 1995 |pmid= 7534063 |doi= }}
*{{cite journal | author=Gersuk VH, Rose TM, Todaro GJ |title=Molecular cloning and chromosomal localization of a pseudogene related to the human acyl-CoA binding protein/diazepam binding inhibitor. |journal=Genomics |volume=25 |issue= 2 |pages= 469-76 |year= 1995 |pmid= 7789980 |doi= }}
*{{cite journal | author=Alho H, Kolmer M, Harjuntausta T, Helén P |title=Increased expression of diazepam binding inhibitor in human brain tumors. |journal=Cell Growth Differ. |volume=6 |issue= 3 |pages= 309-14 |year= 1995 |pmid= 7794798 |doi= }}
*{{cite journal | author=Alho H, Vaalasti A, Podkletnova I, Rechardt L |title=Expression of diazepam-binding inhibitor peptide in human skin: an immunohistochemical and ultrastructural study. |journal=J. Invest. Dermatol. |volume=101 |issue= 6 |pages= 800-3 |year= 1994 |pmid= 8245508 |doi= }}
*{{cite journal | author=Cavallaro S, Pani L, Guidotti A, Costa E |title=ACTH-induced mitochondrial DBI receptor (MDR) and diazepam binding inhibitor (DBI) expression in adrenals of hypophysectomized rats is not cause-effect related to its immediate steroidogenic action. |journal=Life Sci. |volume=53 |issue= 14 |pages= 1137-47 |year= 1993 |pmid= 8396705 |doi= }}
*{{cite journal | author=Swinnen JV, Esquenet M, Rosseels J, ''et al.'' |title=A human gene encoding diazepam-binding inhibitor/acy1-CoA-binding protein: transcription and hormonal regulation in the androgen-sensitive human prostatic adenocarcinoma cell line LNCaP. |journal=DNA Cell Biol. |volume=15 |issue= 3 |pages= 197-208 |year= 1996 |pmid= 8634149 |doi= }}
*{{cite journal | author=Krøll JB, Nøhr J, Gregersen N, ''et al.'' |title=Structure of the rat gene encoding the multifunctional acyl-CoA-binding protein: conservation of intron 1 sequences in rodents and man. Addendum. |journal=Gene |volume=173 |issue= 2 |pages= 239-40 |year= 1996 |pmid= 8964506 |doi= }}
*{{cite journal | author=Kolmer M, Pelto-Huikko M, Parvinen M, ''et al.'' |title=The transcriptional and translational control of diazepam binding inhibitor expression in rat male germ-line cells. |journal=DNA Cell Biol. |volume=16 |issue= 1 |pages= 59-72 |year= 1997 |pmid= 9022045 |doi= }}
*{{cite journal | author=Ferrarese C, Cogliati T, Tortorella R, ''et al.'' |title=Diazepam binding inhibitor (DBI) in the plasma of pediatric and adult epileptic patients. |journal=Epilepsy Res. |volume=29 |issue= 2 |pages= 129-34 |year= 1998 |pmid= 9477145 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DLL1... {November 18, 2007 10:55:40 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:56:03 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Delta-like 1 (Drosophila)
| HGNCid = 2908
| Symbol = DLL1
| AltSymbols =; DELTA1; Delta
| OMIM = 606582
| ECnumber =
| Homologene = 4104
| MGIid = 104659
| GeneAtlas_image1 = PBB_GE_DLL1_gnf1h00074_at_tn.png
| Function = {{GNF_GO|id=GO:0005112 |text = Notch binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0031410 |text = cytoplasmic vesicle}}
| Process = {{GNF_GO|id=GO:0001701 |text = in utero embryonic development}} {{GNF_GO|id=GO:0001709 |text = cell fate determination}} {{GNF_GO|id=GO:0001757 |text = somite specification}} {{GNF_GO|id=GO:0007154 |text = cell communication}} {{GNF_GO|id=GO:0007219 |text = Notch signaling pathway}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007368 |text = determination of left/right symmetry}} {{GNF_GO|id=GO:0007386 |text = compartment specification}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0009912 |text = auditory receptor cell fate commitment}} {{GNF_GO|id=GO:0030097 |text = hemopoiesis}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0030155 |text = regulation of cell adhesion}} {{GNF_GO|id=GO:0042472 |text = inner ear morphogenesis}} {{GNF_GO|id=GO:0042475 |text = odontogenesis (sensu Vertebrata)}} {{GNF_GO|id=GO:0045596 |text = negative regulation of cell differentiation}} {{GNF_GO|id=GO:0045608 |text = negative regulation of auditory receptor cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 28514
| Hs_Ensembl = ENSG00000198719
| Hs_RefseqProtein = NP_005609
| Hs_RefseqmRNA = NM_005618
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 170433219
| Hs_GenLoc_end = 170441486
| Hs_Uniprot = O00548
| Mm_EntrezGene = 13388
| Mm_Ensembl = ENSMUSG00000014773
| Mm_RefseqmRNA = NM_007865
| Mm_RefseqProtein = NP_031891
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 15073094
| Mm_GenLoc_end = 15080203
| Mm_Uniprot = Q6PFV7
}}
}}
'''Delta-like 1 (Drosophila)''', also known as '''DLL1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DLL1 delta-like 1 (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=28514| 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 = DLL1 is a human homolog of the Notch Delta ligand and is a member of the delta/serrate/jagged family. It plays a role in mediating cell fate decisions during hematopoiesis. It may play a role in cell-to-cell communication.<ref name="entrez">{{cite web | title = Entrez Gene: DLL1 delta-like 1 (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=28514| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Watt FM |title=The stem cell compartment in human interfollicular epidermis. |journal=J. Dermatol. Sci. |volume=28 |issue= 3 |pages= 173-80 |year= 2002 |pmid= 11912004 |doi= }}
*{{cite journal | author=Lewis AK, Frantz GD, Carpenter DA, ''et al.'' |title=Distinct expression patterns of notch family receptors and ligands during development of the mammalian inner ear. |journal=Mech. Dev. |volume=78 |issue= 1-2 |pages= 159-63 |year= 1999 |pmid= 9858718 |doi= }}
*{{cite journal | author=Mitsiadis TA, Hirsinger E, Lendahl U, Goridis C |title=Delta-notch signaling in odontogenesis: correlation with cytodifferentiation and evidence for feedback regulation. |journal=Dev. Biol. |volume=204 |issue= 2 |pages= 420-31 |year= 1999 |pmid= 9882480 |doi= 10.1006/dbio.1998.9092 }}
*{{cite journal | author=Gray GE, Mann RS, Mitsiadis E, ''et al.'' |title=Human ligands of the Notch receptor. |journal=Am. J. Pathol. |volume=154 |issue= 3 |pages= 785-94 |year= 1999 |pmid= 10079256 |doi= }}
*{{cite journal | author=Beckers J, Clark A, Wünsch K, ''et al.'' |title=Expression of the mouse Delta1 gene during organogenesis and fetal development. |journal=Mech. Dev. |volume=84 |issue= 1-2 |pages= 165-8 |year= 1999 |pmid= 10473134 |doi= }}
*{{cite journal | author=Morrison A, Hodgetts C, Gossler A, ''et al.'' |title=Expression of Delta1 and Serrate1 (Jagged1) in the mouse inner ear. |journal=Mech. Dev. |volume=84 |issue= 1-2 |pages= 169-72 |year= 1999 |pmid= 10473135 |doi= }}
*{{cite journal | author=Han W, Ye Q, Moore MA |title=A soluble form of human Delta-like-1 inhibits differentiation of hematopoietic progenitor cells. |journal=Blood |volume=95 |issue= 5 |pages= 1616-25 |year= 2000 |pmid= 10688816 |doi= }}
*{{cite journal | author=Shimizu K, Chiba S, Hosoya N, ''et al.'' |title=Binding of Delta1, Jagged1, and Jagged2 to Notch2 rapidly induces cleavage, nuclear translocation, and hyperphosphorylation of Notch2. |journal=Mol. Cell. Biol. |volume=20 |issue= 18 |pages= 6913-22 |year= 2000 |pmid= 10958687 |doi= }}
*{{cite journal | author=Shimizu K, Chiba S, Saito T, ''et al.'' |title=Physical interaction of Delta1, Jagged1, and Jagged2 with Notch1 and Notch3 receptors. |journal=Biochem. Biophys. Res. Commun. |volume=276 |issue= 1 |pages= 385-9 |year= 2000 |pmid= 11006133 |doi= 10.1006/bbrc.2000.3469 }}
*{{cite journal | author=Jaleco AC, Neves H, Hooijberg E, ''et al.'' |title=Differential effects of Notch ligands Delta-1 and Jagged-1 in human lymphoid differentiation. |journal=J. Exp. Med. |volume=194 |issue= 7 |pages= 991-1002 |year= 2001 |pmid= 11581320 |doi= }}
*{{cite journal | author=Shimizu K, Chiba S, Saito T, ''et al.'' |title=Integrity of intracellular domain of Notch ligand is indispensable for cleavage required for release of the Notch2 intracellular domain. |journal=EMBO J. |volume=21 |issue= 3 |pages= 294-302 |year= 2002 |pmid= 11823422 |doi= 10.1093/emboj/21.3.294 }}
*{{cite journal | author=Panin VM, Shao L, Lei L, ''et al.'' |title=Notch ligands are substrates for protein O-fucosyltransferase-1 and Fringe. |journal=J. Biol. Chem. |volume=277 |issue= 33 |pages= 29945-52 |year= 2002 |pmid= 12036964 |doi= 10.1074/jbc.M204445200 }}
*{{cite journal | author=Sakamoto K, Yamaguchi S, Ando R, ''et al.'' |title=The nephroblastoma overexpressed gene (NOV/ccn3) protein associates with Notch1 extracellular domain and inhibits myoblast differentiation via Notch signaling pathway. |journal=J. Biol. Chem. |volume=277 |issue= 33 |pages= 29399-405 |year= 2002 |pmid= 12050162 |doi= 10.1074/jbc.M203727200 }}
*{{cite journal | author=Ohishi K, Varnum-Finney B, Bernstein ID |title=Delta-1 enhances marrow and thymus repopulating ability of human CD34(+)CD38(-) cord blood cells. |journal=J. Clin. Invest. |volume=110 |issue= 8 |pages= 1165-74 |year= 2002 |pmid= 12393852 |doi= }}
*{{cite journal | author=Karlström H, Beatus P, Dannaeus K, ''et al.'' |title=A CADASIL-mutated Notch 3 receptor exhibits impaired intracellular trafficking and maturation but normal ligand-induced signaling. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 17119-24 |year= 2003 |pmid= 12482954 |doi= 10.1073/pnas.252624099 }}
*{{cite journal | author=Tohda S, Murata-Ohsawa M, Sakano S, Nara N |title=Notch ligands, Delta-1 and Delta-4 suppress the self-renewal capacity and long-term growth of two myeloblastic leukemia cell lines. |journal=Int. J. Oncol. |volume=22 |issue= 5 |pages= 1073-9 |year= 2003 |pmid= 12684674 |doi= }}
*{{cite journal | author=Six E, Ndiaye D, Laabi Y, ''et al.'' |title=The Notch ligand Delta1 is sequentially cleaved by an ADAM protease and gamma-secretase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 13 |pages= 7638-43 |year= 2003 |pmid= 12794186 |doi= 10.1073/pnas.1230693100 }}
*{{cite journal | author=LaVoie MJ, Selkoe DJ |title=The Notch ligands, Jagged and Delta, are sequentially processed by alpha-secretase and presenilin/gamma-secretase and release signaling fragments. |journal=J. Biol. Chem. |volume=278 |issue= 36 |pages= 34427-37 |year= 2003 |pmid= 12826675 |doi= 10.1074/jbc.M302659200 }}
*{{cite journal | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on E2F3... {November 18, 2007 10:42:19 PM PST}
- SEARCH REDIRECT: Control Box Found: E2F3 {November 18, 2007 10:42:42 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:42:45 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:42:45 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:42:45 PM PST}
- UPDATED: Updated protein page: E2F3 {November 18, 2007 10:42:52 PM PST}
- INFO: Beginning work on EIF4G2... {November 18, 2007 10:42:52 PM PST}
- SEARCH REDIRECT: Control Box Found: EIF4G2 {November 18, 2007 10:43:18 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:43:21 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:43:21 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:43:21 PM PST}
- UPDATED: Updated protein page: EIF4G2 {November 18, 2007 10:43:27 PM PST}
- INFO: Beginning work on FCGR3B... {November 18, 2007 10:44:07 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:44:55 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_FCGR3B_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1e4j.
| PDB = {{PDB2|1e4j}}, {{PDB2|1e4k}}, {{PDB2|1fnl}}, {{PDB2|1iis}}, {{PDB2|1iix}}, {{PDB2|1t83}}, {{PDB2|1t89}}
| Name = Fc fragment of IgG, low affinity IIIb, receptor (CD16b)
| HGNCid = 3620
| Symbol = FCGR3B
| AltSymbols =; CD16; FCG3; FCGR3; CD16b
| OMIM = 610665
| ECnumber =
| Homologene = 88333
| MGIid =
| GeneAtlas_image1 = PBB_GE_FCGR3B_204007_at_tn.png
| GeneAtlas_image2 = PBB_GE_FCGR3B_204006_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0019864 |text = IgG binding}} {{GNF_GO|id=GO:0048503 |text = GPI anchor binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2215
| Hs_Ensembl = ENSG00000162747
| Hs_RefseqProtein = NP_000561
| Hs_RefseqmRNA = NM_000570
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 159859610
| Hs_GenLoc_end = 159867620
| Hs_Uniprot = O75015
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Fc fragment of IgG, low affinity IIIb, receptor (CD16b)''', also known as '''FCGR3B''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FCGR3B Fc fragment of IgG, low affinity IIIb, receptor (CD16b)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2215| 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=Qiu WQ, de Bruin D, Brownstein BH, ''et al.'' |title=Organization of the human and mouse low-affinity Fc gamma R genes: duplication and recombination. |journal=Science |volume=248 |issue= 4956 |pages= 732-5 |year= 1990 |pmid= 2139735 |doi= }}
*{{cite journal | author=Peltz GA, Grundy HO, Lebo RV, ''et al.'' |title=Human Fc gamma RIII: cloning, expression, and identification of the chromosomal locus of two Fc receptors for IgG. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 3 |pages= 1013-7 |year= 1989 |pmid= 2521732 |doi= }}
*{{cite journal | author=Scallon BJ, Scigliano E, Freedman VH, ''et al.'' |title=A human immunoglobulin G receptor exists in both polypeptide-anchored and phosphatidylinositol-glycan-anchored forms. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 13 |pages= 5079-83 |year= 1989 |pmid= 2525780 |doi= }}
*{{cite journal | author=Ravetch JV, Perussia B |title=Alternative membrane forms of Fc gamma RIII(CD16) on human natural killer cells and neutrophils. Cell type-specific expression of two genes that differ in single nucleotide substitutions. |journal=J. Exp. Med. |volume=170 |issue= 2 |pages= 481-97 |year= 1989 |pmid= 2526846 |doi= }}
*{{cite journal | author=Simmons D, Seed B |title=The Fc gamma receptor of natural killer cells is a phospholipid-linked membrane protein. |journal=Nature |volume=333 |issue= 6173 |pages= 568-70 |year= 1988 |pmid= 2967436 |doi= 10.1038/333568a0 }}
*{{cite journal | author=Gessner JE, Grussenmeyer T, Kolanus W, Schmidt RE |title=The human low affinity immunoglobulin G Fc receptor III-A and III-B genes. Molecular characterization of the promoter regions. |journal=J. Biol. Chem. |volume=270 |issue= 3 |pages= 1350-61 |year= 1995 |pmid= 7836402 |doi= }}
*{{cite journal | author=Gessner JE, Grussenmeyer T, Dumbsky M, Schmidt RE |title=Separate promoters from proximal and medial control regions contribute to the natural killer cell-specific transcription of the human FcgammaRIII-A (CD16-A) receptor gene. |journal=J. Biol. Chem. |volume=271 |issue= 48 |pages= 30755-64 |year= 1997 |pmid= 8940055 |doi= }}
*{{cite journal | author=Bux J, Stein EL, Bierling P, ''et al.'' |title=Characterization of a new alloantigen (SH) on the human neutrophil Fc gamma receptor IIIb. |journal=Blood |volume=89 |issue= 3 |pages= 1027-34 |year= 1997 |pmid= 9028335 |doi= }}
*{{cite journal | author=Zocchi MR, Rubartelli A, Morgavi P, Poggi A |title=HIV-1 Tat inhibits human natural killer cell function by blocking L-type calcium channels. |journal=J. Immunol. |volume=161 |issue= 6 |pages= 2938-43 |year= 1998 |pmid= 9743356 |doi= }}
*{{cite journal | author=Sondermann P, Huber R, Oosthuizen V, Jacob U |title=The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex. |journal=Nature |volume=406 |issue= 6793 |pages= 267-73 |year= 2000 |pmid= 10917521 |doi= 10.1038/35018508 }}
*{{cite journal | author=Zhang Y, Boesen CC, Radaev S, ''et al.'' |title=Crystal structure of the extracellular domain of a human Fc gamma RIII. |journal=Immunity |volume=13 |issue= 3 |pages= 387-95 |year= 2000 |pmid= 11021536 |doi= }}
*{{cite journal | author=Watanabe Y, Shimada E, Fujiwara K, ''et al.'' |title=Nucleotide sequence of a new Fc gamma receptor IIIB allele that codes for a neutrophil antigen. |journal=Tissue Antigens |volume=56 |issue= 3 |pages= 272-5 |year= 2001 |pmid= 11034564 |doi= }}
*{{cite journal | author=Bharadwaj D, Mold C, Markham E, Du Clos TW |title=Serum amyloid P component binds to Fc gamma receptors and opsonizes particles for phagocytosis. |journal=J. Immunol. |volume=166 |issue= 11 |pages= 6735-41 |year= 2001 |pmid= 11359830 |doi= }}
*{{cite journal | author=Davoine F, Lavigne S, Chakir J, ''et al.'' |title=Expression of FcgammaRIII (CD16) on human peripheral blood eosinophils increases in allergic conditions. |journal=J. Allergy Clin. Immunol. |volume=109 |issue= 3 |pages= 463-9 |year= 2002 |pmid= 11897993 |doi= }}
*{{cite journal | author=Fossati G, Moots RJ, Bucknall RC, Edwards SW |title=Differential role of neutrophil Fcgamma receptor IIIB (CD16) in phagocytosis, bacterial killing, and responses to immune complexes. |journal=Arthritis Rheum. |volume=46 |issue= 5 |pages= 1351-61 |year= 2002 |pmid= 12115243 |doi= 10.1002/art.10230 }}
*{{cite journal | author=Cauza K, Grassauer A, Hinterhuber G, ''et al.'' |title=FcgammaRIII expression on cultured human keratinocytes and upregulation by interferon-gamma. |journal=J. Invest. Dermatol. |volume=119 |issue= 5 |pages= 1074-9 |year= 2003 |pmid= 12445195 |doi= 10.1046/j.1523-1747.2002.19527.x }}
*{{cite journal | author=Siriboonrit U, Tsuchiya N, Sirikong M, ''et al.'' |title=Association of Fcgamma receptor IIb and IIIb polymorphisms with susceptibility to systemic lupus erythematosus in Thais. |journal=Tissue Antigens |volume=61 |issue= 5 |pages= 374-83 |year= 2004 |pmid= 12753656 |doi= }}
*{{cite journal | author=Breij EC, van der Pol WL, van Winsen L, ''et al.'' |title=No association of Fc gamma RIIa, Fc gamma RIIIa and Fc gamma RIIIb polymorphisms with MS. |journal=J. Neuroimmunol. |volume=140 |issue= 1-2 |pages= 210-5 |year= 2003 |pmid= 12864991 |doi= }}
*{{cite journal | author=Tong Y, Jin J, Yan L, ''et al.'' |title=FCGR3B gene frequencies and FCGR3 variants in a Chinese population from Zhejiang Province. |journal=Ann. Hematol. |volume=82 |issue= 9 |pages= 574-8 |year= 2003 |pmid= 12898191 |doi= 10.1007/s00277-003-0725-y }}
*{{cite journal | author=Tanaka S, Edberg JC, Chatham W, ''et al.'' |title=Fc gamma RIIIb allele-sensitive release of alpha-defensins: anti-neutrophil cytoplasmic antibody-induced release of chemotaxins. |journal=J. Immunol. |volume=171 |issue= 11 |pages= 6090-6 |year= 2004 |pmid= 14634123 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FSHB... {November 18, 2007 10:44:55 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:45:15 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_FSHB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1fl7.
| PDB = {{PDB2|1fl7}}, {{PDB2|1xwd}}
| Name = Follicle stimulating hormone, beta polypeptide
| HGNCid = 3964
| Symbol = FSHB
| AltSymbols =;
| OMIM = 136530
| ECnumber =
| Homologene = 430
| MGIid = 95582
| GeneAtlas_image1 = PBB_GE_FSHB_214489_at_tn.png
| Function = {{GNF_GO|id=GO:0016913 |text = follicle-stimulating hormone activity}} {{GNF_GO|id=GO:0046982 |text = protein heterodimerization activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}}
| Process = {{GNF_GO|id=GO:0001541 |text = ovarian follicle development}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007283 |text = spermatogenesis}} {{GNF_GO|id=GO:0007292 |text = female gamete generation}} {{GNF_GO|id=GO:0007565 |text = female pregnancy}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2488
| Hs_Ensembl = ENSG00000131808
| Hs_RefseqProtein = NP_000501
| Hs_RefseqmRNA = NM_000510
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 30209139
| Hs_GenLoc_end = 30213384
| Hs_Uniprot = P01225
| Mm_EntrezGene = 14308
| Mm_Ensembl = ENSMUSG00000027120
| Mm_RefseqmRNA = NM_008045
| Mm_RefseqProtein = NP_032071
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 106856973
| Mm_GenLoc_end = 106860490
| Mm_Uniprot = Q60687
}}
}}
'''Follicle stimulating hormone, beta polypeptide''', also known as '''FSHB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FSHB follicle stimulating hormone, beta polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2488| 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 pituitary glycoprotein hormone family includes follicle-stimulating hormone, luteinizing hormone, chorionic gonadotropin, and thyroid-stimulating hormone. All of these glycoproteins consist of an identical alpha subunit and a hormone-specific beta subunit. This gene encodes the beta subunit of follicle-stimulating hormone. In conjunction with luteinizing hormone, follicle-stimulating hormone induces egg and sperm production. Alternative splicing results in two transcript variants encoding the same protein.<ref name="entrez">{{cite web | title = Entrez Gene: FSHB follicle stimulating hormone, beta polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2488| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Barrios-De-Tomasi J, Timossi C, Merchant H, ''et al.'' |title=Assessment of the in vitro and in vivo biological activities of the human follicle-stimulating isohormones. |journal=Mol. Cell. Endocrinol. |volume=186 |issue= 2 |pages= 189-98 |year= 2002 |pmid= 11900895 |doi= }}
*{{cite journal | author=Saxena BB, Rathnam P |title=Amino acid sequence of the beta subunit of follicle-stimulating hormone from human pituitary glands. |journal=J. Biol. Chem. |volume=251 |issue= 4 |pages= 993-1005 |year= 1976 |pmid= 1249074 |doi= }}
*{{cite journal | author=Keene JL, Matzuk MM, Otani T, ''et al.'' |title=Expression of biologically active human follitropin in Chinese hamster ovary cells. |journal=J. Biol. Chem. |volume=264 |issue= 9 |pages= 4769-75 |year= 1989 |pmid= 2494176 |doi= }}
*{{cite journal | author=Watkins PC, Eddy R, Beck AK, ''et al.'' |title=DNA sequence and regional assignment of the human follicle-stimulating hormone beta-subunit gene to the short arm of human chromosome 11. |journal=DNA |volume=6 |issue= 3 |pages= 205-12 |year= 1987 |pmid= 2885163 |doi= }}
*{{cite journal | author=Jameson JL, Becker CB, Lindell CM, Habener JF |title=Human follicle-stimulating hormone beta-subunit gene encodes multiple messenger ribonucleic acids. |journal=Mol. Endocrinol. |volume=2 |issue= 9 |pages= 806-15 |year= 1988 |pmid= 3139991 |doi= }}
*{{cite journal | author=Shome B, Parlow AF, Liu WK, ''et al.'' |title=A reevaluation of the amino acid sequence of human follitropin beta-subunit. |journal=J. Protein Chem. |volume=7 |issue= 4 |pages= 325-39 |year= 1989 |pmid= 3151250 |doi= }}
*{{cite journal | author=Shome B, Parlow AF |title=Human follicle stimulating hormone: first proposal for the amino acid sequence of the hormone-specific, beta subunit (hFSHb). |journal=J. Clin. Endocrinol. Metab. |volume=39 |issue= 1 |pages= 203-5 |year= 1974 |pmid= 4835136 |doi= }}
*{{cite journal | author=Fujiki Y, Rathnam P, Saxena BB |title=Studies on the disulfide bonds in human pituitary follicle-stimulating hormone. |journal=Biochim. Biophys. Acta |volume=624 |issue= 2 |pages= 428-35 |year= 1980 |pmid= 6774759 |doi= }}
*{{cite journal | author=Böckers TM, Nieschlag E, Kreutz MR, Bergmann M |title=Localization of follicle-stimulating hormone (FSH) immunoreactivity and hormone receptor mRNA in testicular tissue of infertile men. |journal=Cell Tissue Res. |volume=278 |issue= 3 |pages= 595-600 |year= 1995 |pmid= 7850869 |doi= }}
*{{cite journal | author=Matthews CH, Borgato S, Beck-Peccoz P, ''et al.'' |title=Primary amenorrhoea and infertility due to a mutation in the beta-subunit of follicle-stimulating hormone. |journal=Nat. Genet. |volume=5 |issue= 1 |pages= 83-6 |year= 1993 |pmid= 8220432 |doi= 10.1038/ng0993-83 }}
*{{cite journal | author=Layman LC, Lee EJ, Peak DB, ''et al.'' |title=Delayed puberty and hypogonadism caused by mutations in the follicle-stimulating hormone beta-subunit gene. |journal=N. Engl. J. Med. |volume=337 |issue= 9 |pages= 607-11 |year= 1997 |pmid= 9271483 |doi= }}
*{{cite journal | author=Cargill M, Altshuler D, Ireland J, ''et al.'' |title=Characterization of single-nucleotide polymorphisms in coding regions of human genes. |journal=Nat. Genet. |volume=22 |issue= 3 |pages= 231-8 |year= 1999 |pmid= 10391209 |doi= 10.1038/10290 }}
*{{cite journal | author=Grasso P, Rozhavskaya-Arena M, Reichert LE |title=Cysteine residues in a synthetic peptide corresponding to human follicle-stimulating hormone beta-subunit receptor-binding domain 81-95 [hFSH-beta-(81-95)] modulate the in vivo effects of hFSH-beta-(81-95) on the mouse estrous cycle. |journal=Regul. Pept. |volume=81 |issue= 1-3 |pages= 67-71 |year= 1999 |pmid= 10395410 |doi= }}
*{{cite journal | author=Ben-Menahem D, Hyde R, Pixley M, ''et al.'' |title=Synthesis of multi-subunit domain gonadotropin complexes: a model for alpha/beta heterodimer formation. |journal=Biochemistry |volume=38 |issue= 46 |pages= 15070-7 |year= 1999 |pmid= 10563789 |doi= }}
*{{cite journal | author=Dias Neto E, Correa RG, Verjovski-Almeida S, ''et al.'' |title=Shotgun sequencing of the human transcriptome with ORF expressed sequence tags. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3491-6 |year= 2000 |pmid= 10737800 |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=Fox KM, Dias JA, Van Roey P |title=Three-dimensional structure of human follicle-stimulating hormone. |journal=Mol. Endocrinol. |volume=15 |issue= 3 |pages= 378-89 |year= 2001 |pmid= 11222739 |doi= }}
*{{cite journal | author=Amoresano A, Orrù S, Siciliano RA, ''et al.'' |title=Assignment of the complete disulphide bridge pattern in the human recombinant follitropin beta-chain. |journal=Biol. Chem. |volume=382 |issue= 6 |pages= 961-8 |year= 2002 |pmid= 11501762 |doi= }}
*{{cite journal | author=Walton WJ, Nguyen VT, Butnev VY, ''et al.'' |title=Characterization of human FSH isoforms reveals a nonglycosylated beta-subunit in addition to the conventional glycosylated beta-subunit. |journal=J. Clin. Endocrinol. Metab. |volume=86 |issue= 8 |pages= 3675-85 |year= 2001 |pmid= 11502795 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FUCA1... {November 18, 2007 10:45:15 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:45:32 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Fucosidase, alpha-L- 1, tissue
| HGNCid = 4006
| Symbol = FUCA1
| AltSymbols =;
| OMIM = 230000
| ECnumber =
| Homologene = 20078
| MGIid = 95593
| GeneAtlas_image1 = PBB_GE_FUCA1_202838_at_tn.png
| Function = {{GNF_GO|id=GO:0003824 |text = catalytic activity}} {{GNF_GO|id=GO:0004560 |text = alpha-L-fucosidase activity}} {{GNF_GO|id=GO:0016798 |text = hydrolase activity, acting on glycosyl bonds}} {{GNF_GO|id=GO:0043169 |text = cation binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005764 |text = lysosome}}
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006027 |text = glycosaminoglycan catabolic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2517
| Hs_Ensembl = ENSG00000179163
| Hs_RefseqProtein = NP_000138
| Hs_RefseqmRNA = NM_000147
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 24044154
| Hs_GenLoc_end = 24067371
| Hs_Uniprot = P04066
| Mm_EntrezGene = 71665
| Mm_Ensembl = ENSMUSG00000028673
| Mm_RefseqmRNA = NM_024243
| Mm_RefseqProtein = NP_077205
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 135192833
| Mm_GenLoc_end = 135212389
| Mm_Uniprot = Q3TCW3
}}
}}
'''Fucosidase, alpha-L- 1, tissue''', also known as '''FUCA1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FUCA1 fucosidase, alpha-L- 1, tissue| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2517| 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 = Fucosidosis is an autosomal recessive lysosomal storage disease caused by defective alpha-L-fucosidase with accumulation of fucose in the tissues. Different phenotypes include clinical features such as neurologic deterioration, growth retardation, visceromegaly, and seizures in a severe early form; coarse facial features, angiokeratoma corporis diffusum, spasticity and delayed psychomotor development in a longer surviving form; and an unusual spondylometaphyseoepiphyseal dysplasia in yet another form.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: FUCA1 fucosidase, alpha-L- 1, tissue| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2517| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Willems PJ, Gatti R, Darby JK, ''et al.'' |title=Fucosidosis revisited: a review of 77 patients. |journal=Am. J. Med. Genet. |volume=38 |issue= 1 |pages= 111-31 |year= 1991 |pmid= 2012122 |doi= 10.1002/ajmg.1320380125 }}
*{{cite journal | author=Willems PJ, Seo HC, Coucke P, ''et al.'' |title=Spectrum of mutations in fucosidosis. |journal=Eur. J. Hum. Genet. |volume=7 |issue= 1 |pages= 60-7 |year= 1999 |pmid= 10094192 |doi= 10.1038/sj.ejhg.5200272 }}
*{{cite journal | author=Yang M, Allen H, DiCioccio RA |title=A mutation generating a stop codon in the alpha-L-fucosidase gene of a fucosidosis patient. |journal=Biochem. Biophys. Res. Commun. |volume=189 |issue= 2 |pages= 1063-8 |year= 1993 |pmid= 1281988 |doi= }}
*{{cite journal | author=Fukushima H, Nishimoto J, Okada S |title=Sequencing and expression of a full-length cDNA for human alpha-L-fucosidase. |journal=J. Inherit. Metab. Dis. |volume=13 |issue= 5 |pages= 761-5 |year= 1991 |pmid= 2174090 |doi= }}
*{{cite journal | author=Kretz KA, Darby JK, Willems PJ, O'Brien JS |title=Characterization of EcoRI mutation in fucosidosis patients: a stop codon in the open reading frame. |journal=J. Mol. Neurosci. |volume=1 |issue= 3 |pages= 177-80 |year= 1990 |pmid= 2642067 |doi= }}
*{{cite journal | author=Occhiodoro T, Beckmann KR, Morris CP, Hopwood JJ |title=Human alpha-L-fucosidase: complete coding sequence from cDNA clones. |journal=Biochem. Biophys. Res. Commun. |volume=164 |issue= 1 |pages= 439-45 |year= 1989 |pmid= 2803312 |doi= }}
*{{cite journal | author=O'Brien JS, Willems PJ, Fukushima H, ''et al.'' |title=Molecular biology of the alpha-L-fucosidase gene and fucosidosis. |journal=Enzyme |volume=38 |issue= 1-4 |pages= 45-53 |year= 1988 |pmid= 2894306 |doi= }}
*{{cite journal | author=Fukushima H, de Wet JR, O'Brien JS |title=Molecular cloning of a cDNA for human alpha-L-fucosidase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 4 |pages= 1262-5 |year= 1985 |pmid= 2983333 |doi= }}
*{{cite journal | author=Fowler ML, Nakai H, Byers MG, ''et al.'' |title=Chromosome 1 localization of the human alpha-L-fucosidase structural gene with a homologous site on chromosome 2. |journal=Cytogenet. Cell Genet. |volume=43 |issue= 1-2 |pages= 103-8 |year= 1987 |pmid= 3780313 |doi= }}
*{{cite journal | author=Kido A, Komatsu N, Ose Y, Oya M |title=alpha-L-fucosidase phenotyping in human tissues, dental pulps and hair roots. |journal=Forensic Sci. Int. |volume=33 |issue= 1 |pages= 53-9 |year= 1987 |pmid= 3817676 |doi= }}
*{{cite journal | author=Hopfer RL, Alhadeff JA |title=Solubilization and characterization of pellet-associated human brain alpha-L-fucosidase activity. |journal=Biochem. J. |volume=229 |issue= 3 |pages= 679-85 |year= 1985 |pmid= 4052017 |doi= }}
*{{cite journal | author=Johnson K, Dawson G |title=Molecular defect in processing alpha-fucosidase in fucosidosis. |journal=Biochem. Biophys. Res. Commun. |volume=133 |issue= 1 |pages= 90-7 |year= 1986 |pmid= 4074382 |doi= }}
*{{cite journal | author=de Wet JR, Fukushima H, Dewji NN, ''et al.'' |title=Chromogenic immunodetection of human serum albumin and alpha-L-fucosidase clones in a human hepatoma cDNA expression library. |journal=DNA |volume=3 |issue= 6 |pages= 437-47 |year= 1985 |pmid= 6096099 |doi= }}
*{{cite journal | author=Cragg H, Winchester B, Seo HC, ''et al.'' |title=Molecular basis of the common electrophoretic polymorphism (Fu1/Fu2) in human alpha-L-fucosidase. |journal=J. Med. Genet. |volume=31 |issue= 8 |pages= 659-60 |year= 1995 |pmid= 7815431 |doi= }}
*{{cite journal | author=Beyer E, Ivleva T, Artykova G, Wiederschain G |title=Change of isoforms' spectra of alpha-L-fucosidase from human skin fibroblasts in intracellular storage of nonhydrolyzable substances. |journal=Biochim. Biophys. Acta |volume=1270 |issue= 1 |pages= 7-11 |year= 1995 |pmid= 7827138 |doi= }}
*{{cite journal | author=Seo HC, Yang M, Tonlorenzi R, ''et al.'' |title=A missense mutation (S63L) in alpha-L-fucosidase is responsible for fucosidosis in an Italian patient. |journal=Hum. Mol. Genet. |volume=3 |issue= 11 |pages= 2065-6 |year= 1995 |pmid= 7874128 |doi= }}
*{{cite journal | author=Williamson M, Cragg H, Grant J, ''et al.'' |title=A 5' splice site mutation in fucosidosis. |journal=J. Med. Genet. |volume=30 |issue= 3 |pages= 218-23 |year= 1993 |pmid= 8097260 |doi= }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Yang M, Allen H, DiCioccio RA |title=Pedigree analysis of alpha-L-fucosidase gene mutations in a fucosidosis family. |journal=Biochim. Biophys. Acta |volume=1182 |issue= 3 |pages= 245-9 |year= 1993 |pmid= 8399358 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FUT3... {November 18, 2007 10:45:32 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:46:05 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Fucosyltransferase 3 (galactoside 3(4)-L-fucosyltransferase, Lewis blood group)
| HGNCid = 4014
| Symbol = FUT3
| AltSymbols =; CD174; LE; Les; MGC131739
| OMIM = 111100
| ECnumber =
| Homologene = 55438
| MGIid =
| GeneAtlas_image1 = PBB_GE_FUT3_214088_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_FUT3_210398_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_FUT3_211882_x_at_tn.png
| Function = {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}} {{GNF_GO|id=GO:0017060 |text = 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006486 |text = protein amino acid glycosylation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2525
| Hs_Ensembl = ENSG00000171124
| Hs_RefseqProtein = NP_000140
| Hs_RefseqmRNA = NM_000149
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 5793902
| Hs_GenLoc_end = 5802482
| Hs_Uniprot = P21217
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Fucosyltransferase 3 (galactoside 3(4)-L-fucosyltransferase, Lewis blood group)''', also known as '''FUT3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FUT3 fucosyltransferase 3 (galactoside 3(4)-L-fucosyltransferase, Lewis blood group)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2525| 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 Lewis histo-blood group system comprises a set of fucosylated glycosphingolipids that are synthesized by exocrine epithelial cells and circulate in body fluids. The glycosphingolipids function in embryogenesis, tissue differentiation, tumor metastasis, inflammation, and bacterial adhesion. They are secondarily absorbed to red blood cells giving rise to their Lewis phenotype. This gene is a member of the fucosyltransferase family, which catalyzes the addition of fucose to precursor polysaccharides in the last step of Lewis antigen biosynthesis. It encodes an enzyme with alpha(1,3)-fucosyltransferase and alpha(1,4)-fucosyltransferase activities. Mutations in this gene are responsible for the majority of Lewis antigen-negative phenotypes. Multiple alternatively spliced variants, encoding the same protein, have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: FUT3 fucosyltransferase 3 (galactoside 3(4)-L-fucosyltransferase, Lewis blood group)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2525| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Weston BW, Nair RP, Larsen RD, Lowe JB |title=Isolation of a novel human alpha (1,3)fucosyltransferase gene and molecular comparison to the human Lewis blood group alpha (1,3/1,4)fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities. |journal=J. Biol. Chem. |volume=267 |issue= 6 |pages= 4152-60 |year= 1992 |pmid= 1740457 |doi= }}
*{{cite journal | author=Kukowska-Latallo JF, Larsen RD, Nair RP, Lowe JB |title=A cloned human cDNA determines expression of a mouse stage-specific embryonic antigen and the Lewis blood group alpha(1,3/1,4)fucosyltransferase. |journal=Genes Dev. |volume=4 |issue= 8 |pages= 1288-303 |year= 1990 |pmid= 1977660 |doi= }}
*{{cite journal | author=Cameron HS, Szczepaniak D, Weston BW |title=Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms. |journal=J. Biol. Chem. |volume=270 |issue= 34 |pages= 20112-22 |year= 1995 |pmid= 7650030 |doi= }}
*{{cite journal | author=Reguigne-Arnould I, Couillin P, Mollicone R, ''et al.'' |title=Relative positions of two clusters of human alpha-L-fucosyltransferases in 19q (FUT1-FUT2) and 19p (FUT6-FUT3-FUT5) within the microsatellite genetic map of chromosome 19. |journal=Cytogenet. Cell Genet. |volume=71 |issue= 2 |pages= 158-62 |year= 1995 |pmid= 7656588 |doi= }}
*{{cite journal | author=Nishihara S, Nakazato M, Kudo T, ''et al.'' |title=Human alpha-1,3 fucosyltransferase (FucT-VI) gene is located at only 13 kb 3' to the Lewis type fucosyltransferase (FucT-III) gene on chromosome 19. |journal=Biochem. Biophys. Res. Commun. |volume=190 |issue= 1 |pages= 42-6 |year= 1993 |pmid= 7916594 |doi= 10.1006/bbrc.1993.1008 }}
*{{cite journal | author=Nishihara S, Narimatsu H, Iwasaki H, ''et al.'' |title=Molecular genetic analysis of the human Lewis histo-blood group system. |journal=J. Biol. Chem. |volume=269 |issue= 46 |pages= 29271-8 |year= 1994 |pmid= 7961897 |doi= }}
*{{cite journal | author=Mollicone R, Reguigne I, Kelly RJ, ''et al.'' |title=Molecular basis for Lewis alpha(1,3/1,4)-fucosyltransferase gene deficiency (FUT3) found in Lewis-negative Indonesian pedigrees. |journal=J. Biol. Chem. |volume=269 |issue= 33 |pages= 20987-94 |year= 1994 |pmid= 8063716 |doi= }}
*{{cite journal | author=Koda Y, Kimura H, Mekada E |title=Analysis of Lewis fucosyltransferase genes from the human gastric mucosa of Lewis-positive and -negative individuals. |journal=Blood |volume=82 |issue= 9 |pages= 2915-9 |year= 1993 |pmid= 8219240 |doi= }}
*{{cite journal | author=Elmgren A, Rydberg L, Larson G |title=Genotypic heterogeneity among Lewis negative individuals. |journal=Biochem. Biophys. Res. Commun. |volume=196 |issue= 2 |pages= 515-20 |year= 1993 |pmid= 8240322 |doi= 10.1006/bbrc.1993.2280 }}
*{{cite journal | author=Nishihara S, Yazawa S, Iwasaki H, ''et al.'' |title=Alpha (1,3/1,4)fucosyltransferase (FucT-III) gene is inactivated by a single amino acid substitution in Lewis histo-blood type negative individuals. |journal=Biochem. Biophys. Res. Commun. |volume=196 |issue= 2 |pages= 624-31 |year= 1993 |pmid= 8240337 |doi= 10.1006/bbrc.1993.2295 }}
*{{cite journal | author=Elmgren A, Börjeson C, Svensson L, ''et al.'' |title=DNA sequencing and screening for point mutations in the human Lewis (FUT3) gene enables molecular genotyping of the human Lewis blood group system. |journal=Vox Sang. |volume=70 |issue= 2 |pages= 97-103 |year= 1996 |pmid= 8801770 |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=Orntoft TF, Vestergaard EM, Holmes E, ''et al.'' |title=Influence of Lewis alpha1-3/4-L-fucosyltransferase (FUT3) gene mutations on enzyme activity, erythrocyte phenotyping, and circulating tumor marker sialyl-Lewis a levels. |journal=J. Biol. Chem. |volume=271 |issue= 50 |pages= 32260-8 |year= 1997 |pmid= 8943285 |doi= }}
*{{cite journal | author=Elmgren A, Mollicone R, Costache M, ''et al.'' |title=Significance of individual point mutations, T202C and C314T, in the human Lewis (FUT3) gene for expression of Lewis antigens by the human alpha(1,3/1,4)-fucosyltransferase, Fuc-TIII. |journal=J. Biol. Chem. |volume=272 |issue= 35 |pages= 21994-8 |year= 1997 |pmid= 9268337 |doi= }}
*{{cite journal | author=Pang H, Liu Y, Koda Y, ''et al.'' |title=Five novel missense mutations of the Lewis gene (FUT3) in African (Xhosa) and Caucasian populations in South Africa. |journal=Hum. Genet. |volume=102 |issue= 6 |pages= 675-80 |year= 1998 |pmid= 9703429 |doi= }}
*{{cite journal | author=Nishihara S, Hiraga T, Ikehara Y, ''et al.'' |title=Molecular behavior of mutant Lewis enzymes in vivo. |journal=Glycobiology |volume=9 |issue= 4 |pages= 373-82 |year= 1999 |pmid= 10089211 |doi= }}
*{{cite journal | author=Yazawa S, Tanaka S, Nishimura T, ''et al.'' |title=Plasma alpha1,3-fucosyltransferase deficiency in schizophrenia. |journal=Exp. Clin. Immunogenet. |volume=16 |issue= 3 |pages= 125-30 |year= 1999 |pmid= 10394050 |doi= }}
*{{cite journal | author=Holmes EH, Yen TY, Thomas S, ''et al.'' |title=Human alpha 1,3/4 fucosyltransferases. Characterization of highly conserved cysteine residues and N-linked glycosylation sites. |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24237-45 |year= 2000 |pmid= 10816554 |doi= 10.1074/jbc.M000888200 }}
*{{cite journal | author=Grahn A, Elmgren A, Aberg L, ''et al.'' |title=Determination of Lewis FUT3 gene mutations by PCR using sequence-specific primers enables efficient genotyping of clinical samples. |journal=Hum. Mutat. |volume=18 |issue= 4 |pages= 358-9 |year= 2002 |pmid= 11668626 |doi= 10.1002/humu.1204 }}
*{{cite journal | author=Roos C, Kolmer M, Mattila P, Renkonen R |title=Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism. |journal=J. Biol. Chem. |volume=277 |issue= 5 |pages= 3168-75 |year= 2002 |pmid= 11698403 |doi= 10.1074/jbc.M107927200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GHSR... {November 18, 2007 10:46:05 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:49:16 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Growth hormone secretagogue receptor
| HGNCid = 4267
| Symbol = GHSR
| AltSymbols =;
| OMIM = 601898
| ECnumber =
| Homologene = 57161
| MGIid = 2441906
| GeneAtlas_image1 = PBB_GE_GHSR_221360_s_at_tn.png
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0001616 |text = growth hormone secretagogue receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0016520 |text = growth hormone-releasing hormone receptor activity}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0009986 |text = cell surface}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0008343 |text = adult feeding behavior}} {{GNF_GO|id=GO:0009755 |text = hormone-mediated signaling}} {{GNF_GO|id=GO:0030252 |text = growth hormone secretion}} {{GNF_GO|id=GO:0032100 |text = positive regulation of appetite}} {{GNF_GO|id=GO:0040018 |text = positive regulation of body size}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2693
| Hs_Ensembl = ENSG00000121853
| Hs_RefseqProtein = NP_004113
| Hs_RefseqmRNA = NM_004122
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 173645645
| Hs_GenLoc_end = 173648897
| Hs_Uniprot = Q92847
| Mm_EntrezGene = 208188
| Mm_Ensembl = ENSMUSG00000051136
| Mm_RefseqmRNA = NM_177330
| Mm_RefseqProtein = NP_796304
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 27562424
| Mm_GenLoc_end = 27569083
| Mm_Uniprot = Q0VBE5
}}
}}
'''Growth hormone secretagogue receptor''', also known as '''GHSR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GHSR growth hormone secretagogue receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2693| 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 G-protein coupled receptor family. The encoded protein may play a role in energy homeostasis and regulation of body weight. Two identified transcript variants are expressed in several tissues and are evolutionary conserved in fish and swine. One transcript, 1a, excises an intron and encodes the functional protein; this protein is the receptor for the Ghrelin ligand and defines a neuroendocrine pathway for growth hormone release. The second transcript (1b) retains the intron and does not function as a receptor for Ghrelin; however, it may function to attenuate activity of isoform 1a.<ref name="entrez">{{cite web | title = Entrez Gene: GHSR growth hormone secretagogue receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2693| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Smith RG, Leonard R, Bailey AR, ''et al.'' |title=Growth hormone secretagogue receptor family members and ligands. |journal=Endocrine |volume=14 |issue= 1 |pages= 9-14 |year= 2001 |pmid= 11322507 |doi= }}
*{{cite journal | author=Petersenn S |title=Structure and regulation of the growth hormone secretagogue receptor. |journal=Minerva Endocrinol. |volume=27 |issue= 4 |pages= 243-56 |year= 2003 |pmid= 12511847 |doi= }}
*{{cite journal | author=Holst B, Schwartz TW |title=Ghrelin receptor mutations--too little height and too much hunger. |journal=J. Clin. Invest. |volume=116 |issue= 3 |pages= 637-41 |year= 2006 |pmid= 16511600 |doi= 10.1172/JCI27999 }}
*{{cite journal | author=Nogueiras R, Perez-Tilve D, Wortley KE, Tschöp M |title=Growth hormone secretagogue (ghrelin-) receptors--a complex drug target for the regulation of body weight. |journal=CNS & neurological disorders drug targets |volume=5 |issue= 3 |pages= 335-43 |year= 2006 |pmid= 16787234 |doi= }}
*{{cite journal | author=Engbaek K |title=[Giardia lamblia and other intestinal parasites in children in day-institutions. Incidence and significance] |journal=Ugeskr. Laeg. |volume=140 |issue= 1 |pages= 14-7 |year= 1978 |pmid= 601898 |doi= }}
*{{cite journal | author=Howard AD, Feighner SD, Cully DF, ''et al.'' |title=A receptor in pituitary and hypothalamus that functions in growth hormone release. |journal=Science |volume=273 |issue= 5277 |pages= 974-7 |year= 1996 |pmid= 8688086 |doi= }}
*{{cite journal | author=McKee KK, Palyha OC, Feighner SD, ''et al.'' |title=Molecular analysis of rat pituitary and hypothalamic growth hormone secretagogue receptors. |journal=Mol. Endocrinol. |volume=11 |issue= 4 |pages= 415-23 |year= 1997 |pmid= 9092793 |doi= }}
*{{cite journal | author=Kaji H, Tai S, Okimura Y, ''et al.'' |title=Cloning and characterization of the 5'-flanking region of the human growth hormone secretagogue receptor gene. |journal=J. Biol. Chem. |volume=273 |issue= 51 |pages= 33885-8 |year= 1999 |pmid= 9852035 |doi= }}
*{{cite journal | author=Kojima M, Hosoda H, Date Y, ''et al.'' |title=Ghrelin is a growth-hormone-releasing acylated peptide from stomach. |journal=Nature |volume=402 |issue= 6762 |pages= 656-60 |year= 2000 |pmid= 10604470 |doi= 10.1038/45230 }}
*{{cite journal | author=Deghenghi R, Papotti M, Ghigo E, Muccioli G |title=Cortistatin, but not somatostatin, binds to growth hormone secretagogue (GHS) receptors of human pituitary gland. |journal=J. Endocrinol. Invest. |volume=24 |issue= 1 |pages= RC1-3 |year= 2001 |pmid= 11227737 |doi= }}
*{{cite journal | author=Tannenbaum GS, Bowers CY |title=Interactions of growth hormone secretagogues and growth hormone-releasing hormone/somatostatin. |journal=Endocrine |volume=14 |issue= 1 |pages= 21-7 |year= 2001 |pmid= 11322498 |doi= }}
*{{cite journal | author=Petersenn S, Rasch AC, Penshorn M, ''et al.'' |title=Genomic structure and transcriptional regulation of the human growth hormone secretagogue receptor. |journal=Endocrinology |volume=142 |issue= 6 |pages= 2649-59 |year= 2001 |pmid= 11356716 |doi= }}
*{{cite journal | author=Shuto Y, Shibasaki T, Otagiri A, ''et al.'' |title=Hypothalamic growth hormone secretagogue receptor regulates growth hormone secretion, feeding, and adiposity. |journal=J. Clin. Invest. |volume=109 |issue= 11 |pages= 1429-36 |year= 2002 |pmid= 12045256 |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=Gaytan F, Barreiro ML, Chopin LK, ''et al.'' |title=Immunolocalization of ghrelin and its functional receptor, the type 1a growth hormone secretagogue receptor, in the cyclic human ovary. |journal=J. Clin. Endocrinol. Metab. |volume=88 |issue= 2 |pages= 879-87 |year= 2003 |pmid= 12574228 |doi= }}
*{{cite journal | author=Lall S, Balthasar N, Carmignac D, ''et al.'' |title=Physiological studies of transgenic mice overexpressing growth hormone (GH) secretagogue receptor 1A in GH-releasing hormone neurons. |journal=Endocrinology |volume=145 |issue= 4 |pages= 1602-11 |year= 2004 |pmid= 14701677 |doi= 10.1210/en.2003-1509 }}
*{{cite journal | author=Wang HJ, Geller F, Dempfle A, ''et al.'' |title=Ghrelin receptor gene: identification of several sequence variants in extremely obese children and adolescents, healthy normal-weight and underweight students, and children with short normal stature. |journal=J. Clin. Endocrinol. Metab. |volume=89 |issue= 1 |pages= 157-62 |year= 2004 |pmid= 14715843 |doi= }}
*{{cite journal | author=Gaytan F, Barreiro ML, Caminos JE, ''et al.'' |title=Expression of ghrelin and its functional receptor, the type 1a growth hormone secretagogue receptor, in normal human testis and testicular tumors. |journal=J. Clin. Endocrinol. Metab. |volume=89 |issue= 1 |pages= 400-9 |year= 2004 |pmid= 14715878 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GIPC1... {November 18, 2007 10:50:35 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:51:25 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = GIPC PDZ domain containing family, member 1
| HGNCid = 1226
| Symbol = GIPC1
| AltSymbols =; C19orf3; GIPC; GLUT1CBP; Hs.6454; IIP-1; MGC15889; MGC3774; NIP; RGS19IP1; SEMCAP; SYNECTIIN; TIP-2
| OMIM = 605072
| ECnumber =
| Homologene = 21167
| MGIid = 1926252
| GeneAtlas_image1 = PBB_GE_GIPC1_207525_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005938 |text = cell cortex}} {{GNF_GO|id=GO:0008021 |text = synaptic vesicle}} {{GNF_GO|id=GO:0012506 |text = vesicle membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016023 |text = cytoplasmic membrane-bound vesicle}} {{GNF_GO|id=GO:0043197 |text = dendritic spine}} {{GNF_GO|id=GO:0043198 |text = dendritic shaft}}
| Process = {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0014047 |text = glutamate secretion}} {{GNF_GO|id=GO:0048167 |text = regulation of synaptic plasticity}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10755
| Hs_Ensembl = ENSG00000123159
| Hs_RefseqProtein = NP_005707
| Hs_RefseqmRNA = NM_005716
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 14449572
| Hs_GenLoc_end = 14467944
| Hs_Uniprot = O14908
| Mm_EntrezGene = 67903
| Mm_Ensembl = ENSMUSG00000019433
| Mm_RefseqmRNA = NM_018771
| Mm_RefseqProtein = NP_061241
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 86542783
| Mm_GenLoc_end = 86554894
| Mm_Uniprot = Q9Z0G0
}}
}}
'''GIPC PDZ domain containing family, member 1''', also known as '''GIPC1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GIPC1 GIPC PDZ domain containing family, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10755| 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=Katoh M |title=GIPC gene family (Review). |journal=Int. J. Mol. Med. |volume=9 |issue= 6 |pages= 585-9 |year= 2002 |pmid= 12011974 |doi= }}
*{{cite journal | author=Hasson T |title=Myosin VI: two distinct roles in endocytosis. |journal=J. Cell. Sci. |volume=116 |issue= Pt 17 |pages= 3453-61 |year= 2004 |pmid= 12893809 |doi= 10.1242/jcs.00669 }}
*{{cite journal | author=Gress TM, Müller-Pillasch F, Geng M, ''et al.'' |title=A pancreatic cancer-specific expression profile. |journal=Oncogene |volume=13 |issue= 8 |pages= 1819-30 |year= 1996 |pmid= 8895530 |doi= }}
*{{cite journal | author=De Vries L, Elenko E, Hubler L, ''et al.'' |title=GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 26 |pages= 15203-8 |year= 1997 |pmid= 8986788 |doi= }}
*{{cite journal | author=Rousset R, Fabre S, Desbois C, ''et al.'' |title=The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the PDZ domain of cellular proteins. |journal=Oncogene |volume=16 |issue= 5 |pages= 643-54 |year= 1998 |pmid= 9482110 |doi= 10.1038/sj.onc.1201567 }}
*{{cite journal | author=De Vries L, Lou X, Zhao G, ''et al.'' |title=GIPC, a PDZ domain containing protein, interacts specifically with the C terminus of RGS-GAIP. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 21 |pages= 12340-5 |year= 1998 |pmid= 9770488 |doi= }}
*{{cite journal | author=Bunn RC, Jensen MA, Reed BC |title=Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton. |journal=Mol. Biol. Cell |volume=10 |issue= 4 |pages= 819-32 |year= 1999 |pmid= 10198040 |doi= }}
*{{cite journal | author=Wang LH, Kalb RG, Strittmatter SM |title=A PDZ protein regulates the distribution of the transmembrane semaphorin, M-SemF. |journal=J. Biol. Chem. |volume=274 |issue= 20 |pages= 14137-46 |year= 1999 |pmid= 10318831 |doi= }}
*{{cite journal | author=Cai H, Reed RR |title=Cloning and characterization of neuropilin-1-interacting protein: a PSD-95/Dlg/ZO-1 domain-containing protein that interacts with the cytoplasmic domain of neuropilin-1. |journal=J. Neurosci. |volume=19 |issue= 15 |pages= 6519-27 |year= 1999 |pmid= 10414980 |doi= }}
*{{cite journal | author=Gotthardt M, Trommsdorff M, Nevitt MF, ''et al.'' |title=Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction. |journal=J. Biol. Chem. |volume=275 |issue= 33 |pages= 25616-24 |year= 2000 |pmid= 10827173 |doi= 10.1074/jbc.M000955200 }}
*{{cite journal | author=Gao Y, Li M, Chen W, Simons M |title=Synectin, syndecan-4 cytoplasmic domain binding PDZ protein, inhibits cell migration. |journal=J. Cell. Physiol. |volume=184 |issue= 3 |pages= 373-9 |year= 2000 |pmid= 10911369 |doi= 10.1002/1097-4652(200009)184:3<373::AID-JCP12>3.0.CO;2-I }}
*{{cite journal | author=Von Kap-Herr C, Kandala G, Mann SS, ''et al.'' |title=Assignment of PDZ domain-containing protein GIPC gene (C19orf3) to human chromosome band 19p13.1 by in situ hybridization and radiation hybrid mapping. |journal=Cytogenet. Cell Genet. |volume=89 |issue= 3-4 |pages= 234-5 |year= 2000 |pmid= 10965131 |doi= }}
*{{cite journal | author=Lou X, Yano H, Lee F, ''et al.'' |title=GIPC and GAIP form a complex with TrkA: a putative link between G protein and receptor tyrosine kinase pathways. |journal=Mol. Biol. Cell |volume=12 |issue= 3 |pages= 615-27 |year= 2001 |pmid= 11251075 |doi= }}
*{{cite journal | author=Liu TF, Kandala G, Setaluri V |title=PDZ domain protein GIPC interacts with the cytoplasmic tail of melanosomal membrane protein gp75 (tyrosinase-related protein-1). |journal=J. Biol. Chem. |volume=276 |issue= 38 |pages= 35768-77 |year= 2001 |pmid= 11441007 |doi= 10.1074/jbc.M103585200 }}
*{{cite journal | author=Ligensa T, Krauss S, Demuth D, ''et al.'' |title=A PDZ domain protein interacts with the C-terminal tail of the insulin-like growth factor-1 receptor but not with the insulin receptor. |journal=J. Biol. Chem. |volume=276 |issue= 36 |pages= 33419-27 |year= 2001 |pmid= 11445579 |doi= 10.1074/jbc.M104509200 }}
*{{cite journal | author=Tani TT, Mercurio AM |title=PDZ interaction sites in integrin alpha subunits. T14853, TIP/GIPC binds to a type I recognition sequence in alpha 6A/alpha 5 and a novel sequence in alpha 6B. |journal=J. Biol. Chem. |volume=276 |issue= 39 |pages= 36535-42 |year= 2001 |pmid= 11479315 |doi= 10.1074/jbc.M105785200 }}
*{{cite journal | author=Blobe GC, Liu X, Fang SJ, ''et al.'' |title=A novel mechanism for regulating transforming growth factor beta (TGF-beta) signaling. Functional modulation of type III TGF-beta receptor expression through interaction with the PDZ domain protein, GIPC. |journal=J. Biol. Chem. |volume=276 |issue= 43 |pages= 39608-17 |year= 2001 |pmid= 11546783 |doi= 10.1074/jbc.M106831200 }}
*{{cite journal | author=Awan A, Lucic MR, Shaw DM, ''et al.'' |title=5T4 interacts with TIP-2/GIPC, a PDZ protein, with implications for metastasis. |journal=Biochem. Biophys. Res. Commun. |volume=290 |issue= 3 |pages= 1030-6 |year= 2002 |pmid= 11798178 |doi= 10.1006/bbrc.2001.6288 }}
*{{cite journal | author=El Mourabit H, Poinat P, Koster J, ''et al.'' |title=The PDZ domain of TIP-2/GIPC interacts with the C-terminus of the integrin alpha5 and alpha6 subunits. |journal=Matrix Biol. |volume=21 |issue= 2 |pages= 207-14 |year= 2002 |pmid= 11852236 |doi= }}
*{{cite journal | author=Lou X, McQuistan T, Orlando RA, Farquhar MG |title=GAIP, GIPC and Galphai3 are concentrated in endocytic compartments of proximal tubule cells: putative role in regulating megalin's function. |journal=J. Am. Soc. Nephrol. |volume=13 |issue= 4 |pages= 918-27 |year= 2002 |pmid= 11912251 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GJA5... {November 18, 2007 10:49:16 PM PST}
- SEARCH REDIRECT: Control Box Found: GJA5 {November 18, 2007 10:49:50 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:49:53 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:49:53 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:49:53 PM PST}
- UPDATED: Updated protein page: GJA5 {November 18, 2007 10:49:59 PM PST}
- INFO: Beginning work on GJB6... {November 18, 2007 10:51:25 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:51:59 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Gap junction protein, beta 6
| HGNCid = 4288
| Symbol = GJB6
| AltSymbols =; HED; DFNA3; CX30; ED2; EDH
| OMIM = 604418
| ECnumber =
| Homologene = 4936
| MGIid = 107588
| Function = {{GNF_GO|id=GO:0003823 |text = antigen binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0015285 |text = gap-junction channel activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005922 |text = connexon complex}} {{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:0007154 |text = cell communication}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0042471 |text = ear morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10804
| Hs_Ensembl = ENSG00000121742
| Hs_RefseqProtein = NP_006774
| Hs_RefseqmRNA = NM_006783
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 13
| Hs_GenLoc_start = 19694103
| Hs_GenLoc_end = 19704366
| Hs_Uniprot = O95452
| Mm_EntrezGene = 14623
| Mm_Ensembl = ENSMUSG00000040055
| Mm_RefseqmRNA = NM_001010937
| Mm_RefseqProtein = NP_001010937
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 56077413
| Mm_GenLoc_end = 56087687
| Mm_Uniprot = Q3URC5
}}
}}
'''Gap junction protein, beta 6''', also known as '''GJB6''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GJB6 gap junction protein, beta 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10804| 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 connexin gene family codes for the protein subunits of gap junction channels that mediate direct diffusion of ions and metabolites between the cytoplasm of adjacent cells. Connexins span the plasma membrane 4 times, with amino- and carboxy-terminal regions facing the cytoplasm. Connexin genes are expressed in a cell type-specific manner with overlapping specificity. The gap junction channels have unique properties depending on the type of connexins constituting the channel.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: GJB6 gap junction protein, beta 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10804| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Stoppini M, Bellotti V, Negri A, ''et al.'' |title=Characterization of the two unique human anti-flavin monoclonal immunoglobulins. |journal=Eur. J. Biochem. |volume=228 |issue= 3 |pages= 886-93 |year= 1995 |pmid= 7737190 |doi= }}
*{{cite journal | author=Eggena M, Targan SR, Iwanczyk L, ''et al.'' |title=Phage display cloning and characterization of an immunogenetic marker (perinuclear anti-neutrophil cytoplasmic antibody) in ulcerative colitis. |journal=J. Immunol. |volume=156 |issue= 10 |pages= 4005-11 |year= 1996 |pmid= 8621942 |doi= }}
*{{cite journal | author=Kibar Z, Der Kaloustian VM, Brais B, ''et al.'' |title=The gene responsible for Clouston hidrotic ectodermal dysplasia maps to the pericentromeric region of chromosome 13q. |journal=Hum. Mol. Genet. |volume=5 |issue= 4 |pages= 543-7 |year= 1996 |pmid= 8845850 |doi= }}
*{{cite journal | author=Radhakrishna U, Blouin JL, Mehenni H, ''et al.'' |title=The gene for autosomal dominant hidrotic ectodermal dysplasia (Clouston syndrome) in a large Indian family maps to the 13q11-q12.1 pericentromeric region. |journal=Am. J. Med. Genet. |volume=71 |issue= 1 |pages= 80-6 |year= 1997 |pmid= 9215774 |doi= }}
*{{cite journal | author=Clausen BE, Bridges SL, Lavelle JC, ''et al.'' |title=Clonally-related immunoglobulin VH domains and nonrandom use of DH gene segments in rheumatoid arthritis synovium. |journal=Mol. Med. |volume=4 |issue= 4 |pages= 240-57 |year= 1998 |pmid= 9606177 |doi= }}
*{{cite journal | author=Grifa A, Wagner CA, D'Ambrosio L, ''et al.'' |title=Mutations in GJB6 cause nonsyndromic autosomal dominant deafness at DFNA3 locus. |journal=Nat. Genet. |volume=23 |issue= 1 |pages= 16-8 |year= 1999 |pmid= 10471490 |doi= 10.1038/12612 }}
*{{cite journal | author=Kelley PM, Abe S, Askew JW, ''et al.'' |title=Human connexin 30 (GJB6), a candidate gene for nonsyndromic hearing loss: molecular cloning, tissue-specific expression, and assignment to chromosome 13q12. |journal=Genomics |volume=62 |issue= 2 |pages= 172-6 |year= 2000 |pmid= 10610709 |doi= 10.1006/geno.1999.6002 }}
*{{cite journal | author=Dias Neto E, Correa RG, Verjovski-Almeida S, ''et al.'' |title=Shotgun sequencing of the human transcriptome with ORF expressed sequence tags. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3491-6 |year= 2000 |pmid= 10737800 |doi= }}
*{{cite journal | author=Lamartine J, Munhoz Essenfelder G, Kibar Z, ''et al.'' |title=Mutations in GJB6 cause hidrotic ectodermal dysplasia. |journal=Nat. Genet. |volume=26 |issue= 2 |pages= 142-4 |year= 2000 |pmid= 11017065 |doi= 10.1038/79851 }}
*{{cite journal | author=Rash JE, Yasumura T, Dudek FE, Nagy JI |title=Cell-specific expression of connexins and evidence of restricted gap junctional coupling between glial cells and between neurons. |journal=J. Neurosci. |volume=21 |issue= 6 |pages= 1983-2000 |year= 2001 |pmid= 11245683 |doi= }}
*{{cite journal | author=Lerer I, Sagi M, Ben-Neriah Z, ''et al.'' |title=A deletion mutation in GJB6 cooperating with a GJB2 mutation in trans in non-syndromic deafness: A novel founder mutation in Ashkenazi Jews. |journal=Hum. Mutat. |volume=18 |issue= 5 |pages= 460 |year= 2002 |pmid= 11668644 |doi= 10.1002/humu.1222 }}
*{{cite journal | author=del Castillo I, Villamar M, Moreno-Pelayo MA, ''et al.'' |title=A deletion involving the connexin 30 gene in nonsyndromic hearing impairment. |journal=N. Engl. J. Med. |volume=346 |issue= 4 |pages= 243-9 |year= 2002 |pmid= 11807148 |doi= 10.1056/NEJMoa012052 }}
*{{cite journal | author=Smith FJ, Morley SM, McLean WH |title=A novel connexin 30 mutation in Clouston syndrome. |journal=J. Invest. Dermatol. |volume=118 |issue= 3 |pages= 530-2 |year= 2002 |pmid= 11874494 |doi= 10.1046/j.0022-202x.2001.01689.x }}
*{{cite journal | author=Pallares-Ruiz N, Blanchet P, Mondain M, ''et al.'' |title=A large deletion including most of GJB6 in recessive non syndromic deafness: a digenic effect? |journal=Eur. J. Hum. Genet. |volume=10 |issue= 1 |pages= 72-6 |year= 2002 |pmid= 11896458 |doi= 10.1038/sj.ejhg.5200762 }}
*{{cite journal | author=Common JE, Becker D, Di WL, ''et al.'' |title=Functional studies of human skin disease- and deafness-associated connexin 30 mutations. |journal=Biochem. Biophys. Res. Commun. |volume=298 |issue= 5 |pages= 651-6 |year= 2003 |pmid= 12419304 |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=Beltramello M, Bicego M, Piazza V, ''et al.'' |title=Permeability and gating properties of human connexins 26 and 30 expressed in HeLa cells. |journal=Biochem. Biophys. Res. Commun. |volume=305 |issue= 4 |pages= 1024-33 |year= 2003 |pmid= 12767933 |doi= }}
*{{cite journal | author=Zhang XJ, Chen JJ, Yang S, ''et al.'' |title=A mutation in the connexin 30 gene in Chinese Han patients with hidrotic ectodermal dysplasia. |journal=J. Dermatol. Sci. |volume=32 |issue= 1 |pages= 11-7 |year= 2004 |pmid= 12788524 |doi= }}
*{{cite journal | author=Pandya A, Arnos KS, Xia XJ, ''et al.'' |title=Frequency and distribution of GJB2 (connexin 26) and GJB6 (connexin 30) mutations in a large North American repository of deaf probands. |journal=Genet. Med. |volume=5 |issue= 4 |pages= 295-303 |year= 2004 |pmid= 12865758 |doi= 10.1097/01.GIM.0000078026.01140.68 }}
*{{cite journal | author=Günther B, Steiner A, Nekahm-Heis D, ''et al.'' |title=The 342-kb deletion in GJB6 is not present in patients with non-syndromic hearing loss from Austria. |journal=Hum. Mutat. |volume=22 |issue= 2 |pages= 180 |year= 2004 |pmid= 12872268 |doi= 10.1002/humu.9167 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NLRP3... {November 18, 2007 10:56:03 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:56:53 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- 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 = NLR family, pyrin domain containing 3
| HGNCid = 16400
| Symbol = NLRP3
| AltSymbols =; AVP; AGTAVPRL; AII; AII/AVP; C1orf7; CIAS1; CLR1.1; FCAS; FCU; MWS; NALP3; PYPAF1
| OMIM = 606416
| ECnumber =
| Homologene = 3600
| MGIid = 2653833
| GeneAtlas_image1 = PBB_GE_NLRP3_216015_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_NLRP3_207075_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0042834 |text = peptidoglycan binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0009595 |text = detection of biotic stimulus}} {{GNF_GO|id=GO:0032088 |text = inhibition of NF-kappaB transcription factor}} {{GNF_GO|id=GO:0042347 |text = negative regulation of NF-kappaB import into nucleus}} {{GNF_GO|id=GO:0043280 |text = positive regulation of caspase activity}} {{GNF_GO|id=GO:0050718 |text = positive regulation of interleukin-1 beta secretion}} {{GNF_GO|id=GO:0051259 |text = protein oligomerization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 114548
| Hs_Ensembl = ENSG00000162711
| Hs_RefseqProtein = NP_001073289
| Hs_RefseqmRNA = NM_001079821
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 245647974
| Hs_GenLoc_end = 245679033
| Hs_Uniprot = Q96P20
| Mm_EntrezGene = 216799
| Mm_Ensembl = ENSMUSG00000032691
| Mm_RefseqmRNA = XM_001003938
| Mm_RefseqProtein = XP_001003938
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 59357780
| Mm_GenLoc_end = 59383151
| Mm_Uniprot = Q1JQ87
}}
}}
'''NLR family, pyrin domain containing 3''', also known as '''NLRP3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NLRP3 NLR family, pyrin domain containing 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=114548| 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 pyrin-like protein which contains a pyrin domain, a nucleotide-binding site (NBS) domain, and a leucine-rich repeat (LRR) motif. This protein interacts with apoptosis-associated speck-like protein containing a CARD. Proteins which contain the caspase recruitment domain, CARD, have been shown to be involved in inflammation and immune response. This protein may function as an activator of NF-kappaB signaling. The encoded protein may play a role in the regulation of inflammation and apoptosis. Mutations in this gene have been associated with familial cold autoinflammatory syndrome (FCAS), Muckle-Wells syndrome (MWS), chronic infantile neurological cutaneous and articular (CINCA) syndrome, and neonatal-onset multisystem inflammatory disease (NOMID). Multiple alternatively spliced transcript variants encoding distinct isoforms have been identified for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: NLRP3 NLR family, pyrin domain containing 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=114548| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tschopp J, Martinon F, Burns K |title=NALPs: a novel protein family involved in inflammation. |journal=Nat. Rev. Mol. Cell Biol. |volume=4 |issue= 2 |pages= 95-104 |year= 2003 |pmid= 12563287 |doi= 10.1038/nrm1019 }}
*{{cite journal | author=Martinon F, Tschopp J |title=NLRs join TLRs as innate sensors of pathogens. |journal=Trends Immunol. |volume=26 |issue= 8 |pages= 447-54 |year= 2006 |pmid= 15967716 |doi= 10.1016/j.it.2005.06.004 }}
*{{cite journal | author=Mao M, Fu G, Wu JS, ''et al.'' |title=Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 14 |pages= 8175-80 |year= 1998 |pmid= 9653160 |doi= }}
*{{cite journal | author=Hoffman HM, Wright FA, Broide DH, ''et al.'' |title=Identification of a locus on chromosome 1q44 for familial cold urticaria. |journal=Am. J. Hum. Genet. |volume=66 |issue= 5 |pages= 1693-8 |year= 2000 |pmid= 10741953 |doi= }}
*{{cite journal | author=Zhang QH, Ye M, Wu XY, ''et al.'' |title=Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. |journal=Genome Res. |volume=10 |issue= 10 |pages= 1546-60 |year= 2001 |pmid= 11042152 |doi= }}
*{{cite journal | author=Hoffman HM, Mueller JL, Broide DH, ''et al.'' |title=Mutation of a new gene encoding a putative pyrin-like protein causes familial cold autoinflammatory syndrome and Muckle-Wells syndrome. |journal=Nat. Genet. |volume=29 |issue= 3 |pages= 301-5 |year= 2001 |pmid= 11687797 |doi= 10.1038/ng756 }}
*{{cite journal | author=Manji GA, Wang L, Geddes BJ, ''et al.'' |title=PYPAF1, a PYRIN-containing Apaf1-like protein that assembles with ASC and regulates activation of NF-kappa B. |journal=J. Biol. Chem. |volume=277 |issue= 13 |pages= 11570-5 |year= 2002 |pmid= 11786556 |doi= 10.1074/jbc.M112208200 }}
*{{cite journal | author=Srinivasula SM, Poyet JL, Razmara M, ''et al.'' |title=The PYRIN-CARD protein ASC is an activating adaptor for caspase-1. |journal=J. Biol. Chem. |volume=277 |issue= 24 |pages= 21119-22 |year= 2002 |pmid= 11967258 |doi= 10.1074/jbc.C200179200 }}
*{{cite journal | author=Dodé C, Le Dû N, Cuisset L, ''et al.'' |title=New mutations of CIAS1 that are responsible for Muckle-Wells syndrome and familial cold urticaria: a novel mutation underlies both syndromes. |journal=Am. J. Hum. Genet. |volume=70 |issue= 6 |pages= 1498-506 |year= 2002 |pmid= 11992256 |doi= }}
*{{cite journal | author=Feldmann J, Prieur AM, Quartier P, ''et al.'' |title=Chronic infantile neurological cutaneous and articular syndrome is caused by mutations in CIAS1, a gene highly expressed in polymorphonuclear cells and chondrocytes. |journal=Am. J. Hum. Genet. |volume=71 |issue= 1 |pages= 198-203 |year= 2002 |pmid= 12032915 |doi= }}
*{{cite journal | author=Fiorentino L, Stehlik C, Oliveira V, ''et al.'' |title=A novel PAAD-containing protein that modulates NF-kappa B induction by cytokines tumor necrosis factor-alpha and interleukin-1beta. |journal=J. Biol. Chem. |volume=277 |issue= 38 |pages= 35333-40 |year= 2002 |pmid= 12093792 |doi= 10.1074/jbc.M200446200 }}
*{{cite journal | author=Aganna E, Martinon F, Hawkins PN, ''et al.'' |title=Association of mutations in the NALP3/CIAS1/PYPAF1 gene with a broad phenotype including recurrent fever, cold sensitivity, sensorineural deafness, and AA amyloidosis. |journal=Arthritis Rheum. |volume=46 |issue= 9 |pages= 2445-52 |year= 2002 |pmid= 12355493 |doi= 10.1002/art.10509 }}
*{{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=Aksentijevich I, Nowak M, Mallah M, ''et al.'' |title=De novo CIAS1 mutations, cytokine activation, and evidence for genetic heterogeneity in patients with neonatal-onset multisystem inflammatory disease (NOMID): a new member of the expanding family of pyrin-associated autoinflammatory diseases. |journal=Arthritis Rheum. |volume=46 |issue= 12 |pages= 3340-8 |year= 2003 |pmid= 12483741 |doi= 10.1002/art.10688 }}
*{{cite journal | author=Hoffman HM, Gregory SG, Mueller JL, ''et al.'' |title=Fine structure mapping of CIAS1: identification of an ancestral haplotype and a common FCAS mutation, L353P. |journal=Hum. Genet. |volume=112 |issue= 2 |pages= 209-16 |year= 2003 |pmid= 12522564 |doi= 10.1007/s00439-002-0860-x }}
*{{cite journal | author=Dowds TA, Masumoto J, Chen FF, ''et al.'' |title=Regulation of cryopyrin/Pypaf1 signaling by pyrin, the familial Mediterranean fever gene product. |journal=Biochem. Biophys. Res. Commun. |volume=302 |issue= 3 |pages= 575-80 |year= 2003 |pmid= 12615073 |doi= }}
*{{cite journal | author=Granel B, Philip N, Serratrice J, ''et al.'' |title=CIAS1 mutation in a patient with overlap between Muckle-Wells and chronic infantile neurological cutaneous and articular syndromes. |journal=Dermatology (Basel) |volume=206 |issue= 3 |pages= 257-9 |year= 2003 |pmid= 12673085 |doi= 10.1159/000068883 }}
*{{cite journal | author=Neven B, Callebaut I, Prieur AM, ''et al.'' |title=Molecular basis of the spectral expression of CIAS1 mutations associated with phagocytic cell-mediated autoinflammatory disorders CINCA/NOMID, MWS, and FCU. |journal=Blood |volume=103 |issue= 7 |pages= 2809-15 |year= 2004 |pmid= 14630794 |doi= 10.1182/blood-2003-07-2531 }}
*{{cite journal | author=O'Connor W, Harton JA, Zhu X, ''et al.'' |title=Cutting edge: CIAS1/cryopyrin/PYPAF1/NALP3/CATERPILLER 1.1 is an inducible inflammatory mediator with NF-kappa B suppressive properties. |journal=J. Immunol. |volume=171 |issue= 12 |pages= 6329-33 |year= 2004 |pmid= 14662828 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PLCB1... {November 18, 2007 10:54:22 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:55:40 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Phospholipase C, beta 1 (phosphoinositide-specific)
| HGNCid = 15917
| Symbol = PLCB1
| AltSymbols =; PI-PLC; FLJ45792; PLC-154; PLC-I
| OMIM = 607120
| ECnumber =
| Homologene = 22876
| MGIid = 97613
| GeneAtlas_image1 = PBB_GE_PLCB1_211925_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PLCB1_213222_at_tn.png
| GeneAtlas_image3 = PBB_GE_PLCB1_215687_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004435 |text = phosphoinositide phospholipase C activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0016042 |text = lipid catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 23236
| Hs_Ensembl = ENSG00000182621
| Hs_RefseqProtein = NP_056007
| Hs_RefseqmRNA = NM_015192
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 8060908
| Hs_GenLoc_end = 8813547
| Hs_Uniprot = Q9NQ66
| Mm_EntrezGene = 18795
| Mm_Ensembl = ENSMUSG00000051177
| Mm_RefseqmRNA = NM_019677
| Mm_RefseqProtein = NP_062651
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 134477974
| Mm_GenLoc_end = 135163721
| Mm_Uniprot = Q2M4J2
}}
}}
'''Phospholipase C, beta 1 (phosphoinositide-specific)''', also known as '''PLCB1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PLCB1 phospholipase C, beta 1 (phosphoinositide-specific)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23236| 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 catalyzes the formation of inositol 1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium as a cofactor and plays an important role in the intracellular transduction of many extracellular signals. This gene is activated by two G-protein alpha subunits, alpha-q and alpha-11. Two transcript variants encoding different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: PLCB1 phospholipase C, beta 1 (phosphoinositide-specific)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23236| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nakajima D, Okazaki N, Yamakawa H, ''et al.'' |title=Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. |journal=DNA Res. |volume=9 |issue= 3 |pages= 99-106 |year= 2003 |pmid= 12168954 |doi= }}
*{{cite journal | author=Martelli AM, Fiume R, Faenza I, ''et al.'' |title=Nuclear phosphoinositide specific phospholipase C (PI-PLC)-beta 1: a central intermediary in nuclear lipid-dependent signal transduction. |journal=Histol. Histopathol. |volume=20 |issue= 4 |pages= 1251-60 |year= 2006 |pmid= 16136505 |doi= }}
*{{cite journal | author=Cefai D, Debre P, Kaczorek M, ''et al.'' |title=Human immunodeficiency virus-1 glycoproteins gp120 and gp160 specifically inhibit the CD3/T cell-antigen receptor phosphoinositide transduction pathway. |journal=J. Clin. Invest. |volume=86 |issue= 6 |pages= 2117-24 |year= 1991 |pmid= 1979339 |doi= }}
*{{cite journal | author=Zauli G, Previati M, Caramelli E, ''et al.'' |title=Exogenous human immunodeficiency virus type-1 Tat protein selectively stimulates a phosphatidylinositol-specific phospholipase C nuclear pathway in the Jurkat T cell line. |journal=Eur. J. Immunol. |volume=25 |issue= 9 |pages= 2695-700 |year= 1995 |pmid= 7589147 |doi= }}
*{{cite journal | author=Hwang SC, Park KH, Ha MJ, ''et al.'' |title=Distribution of phospholipase C isozymes in normal human lung tissue and their immunohistochemical localization. |journal=J. Korean Med. Sci. |volume=11 |issue= 4 |pages= 305-13 |year= 1997 |pmid= 8878798 |doi= }}
*{{cite journal | author=Chen P, Mayne M, Power C, Nath A |title=The Tat protein of HIV-1 induces tumor necrosis factor-alpha production. Implications for HIV-1-associated neurological diseases. |journal=J. Biol. Chem. |volume=272 |issue= 36 |pages= 22385-8 |year= 1997 |pmid= 9278385 |doi= }}
*{{cite journal | author=Nagase T, Ishikawa K, Miyajima N, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. |journal=DNA Res. |volume=5 |issue= 1 |pages= 31-9 |year= 1998 |pmid= 9628581 |doi= }}
*{{cite journal | author=Snow BE, Hall RA, Krumins AM, ''et al.'' |title=GTPase activating specificity of RGS12 and binding specificity of an alternatively spliced PDZ (PSD-95/Dlg/ZO-1) domain. |journal=J. Biol. Chem. |volume=273 |issue= 28 |pages= 17749-55 |year= 1998 |pmid= 9651375 |doi= }}
*{{cite journal | author=Mayne M, Bratanich AC, Chen P, ''et al.'' |title=HIV-1 tat molecular diversity and induction of TNF-alpha: implications for HIV-induced neurological disease. |journal=Neuroimmunomodulation |volume=5 |issue= 3-4 |pages= 184-92 |year= 1998 |pmid= 9730685 |doi= }}
*{{cite journal | author=Haughey NJ, Holden CP, Nath A, Geiger JD |title=Involvement of inositol 1,4,5-trisphosphate-regulated stores of intracellular calcium in calcium dysregulation and neuron cell death caused by HIV-1 protein tat. |journal=J. Neurochem. |volume=73 |issue= 4 |pages= 1363-74 |year= 1999 |pmid= 10501179 |doi= }}
*{{cite journal | author=Peruzzi D, Calabrese G, Faenza I, ''et al.'' |title=Identification and chromosomal localisation by fluorescence in situ hybridisation of human gene of phosphoinositide-specific phospholipase C beta(1). |journal=Biochim. Biophys. Acta |volume=1484 |issue= 2-3 |pages= 175-82 |year= 2000 |pmid= 10760467 |doi= }}
*{{cite journal | author=Mayne M, Holden CP, Nath A, Geiger JD |title=Release of calcium from inositol 1,4,5-trisphosphate receptor-regulated stores by HIV-1 Tat regulates TNF-alpha production in human macrophages. |journal=J. Immunol. |volume=164 |issue= 12 |pages= 6538-42 |year= 2000 |pmid= 10843712 |doi= }}
*{{cite journal | author=Tang Y, Tang J, Chen Z, ''et al.'' |title=Association of mammalian trp4 and phospholipase C isozymes with a PDZ domain-containing protein, NHERF. |journal=J. Biol. Chem. |volume=275 |issue= 48 |pages= 37559-64 |year= 2001 |pmid= 10980202 |doi= 10.1074/jbc.M006635200 }}
*{{cite journal | author=Caricasole A, Sala C, Roncarati R, ''et al.'' |title=Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLC beta 1). |journal=Biochim. Biophys. Acta |volume=1517 |issue= 1 |pages= 63-72 |year= 2001 |pmid= 11118617 |doi= }}
*{{cite journal | author=Dowal L, Elliott J, Popov S, ''et al.'' |title=Determination of the contact energies between a regulator of G protein signaling and G protein subunits and phospholipase C beta 1. |journal=Biochemistry |volume=40 |issue= 2 |pages= 414-21 |year= 2001 |pmid= 11148035 |doi= }}
*{{cite journal | author=Xu A, Wang Y, Xu LY, Gilmour RS |title=Protein kinase C alpha -mediated negative feedback regulation is responsible for the termination of insulin-like growth factor I-induced activation of nuclear phospholipase C beta1 in Swiss 3T3 cells. |journal=J. Biol. Chem. |volume=276 |issue= 18 |pages= 14980-6 |year= 2001 |pmid= 11278470 |doi= 10.1074/jbc.M009144200 }}
*{{cite journal | author=Xu A, Suh PG, Marmy-Conus N, ''et al.'' |title=Phosphorylation of nuclear phospholipase C beta1 by extracellular signal-regulated kinase mediates the mitogenic action of insulin-like growth factor I. |journal=Mol. Cell. Biol. |volume=21 |issue= 9 |pages= 2981-90 |year= 2001 |pmid= 11287604 |doi= 10.1128/MCB.21.9.2981-2990.2001 }}
*{{cite journal | author=Vitale M, Matteucci A, Manzoli L, ''et al.'' |title=Interleukin 2 activates nuclear phospholipase Cbeta by mitogen-activated protein kinase-dependent phosphorylation in human natural killer cells. |journal=FASEB J. |volume=15 |issue= 10 |pages= 1789-91 |year= 2001 |pmid= 11481231 |doi= }}
*{{cite journal | author=Singer AU, Waldo GL, Harden TK, Sondek J |title=A unique fold of phospholipase C-beta mediates dimerization and interaction with G alpha q. |journal=Nat. Struct. Biol. |volume=9 |issue= 1 |pages= 32-6 |year= 2002 |pmid= 11753430 |doi= 10.1038/nsb731 }}
*{{cite journal | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PRPF8... {November 18, 2007 10:49:59 PM PST}
- SEARCH REDIRECT: Control Box Found: PRPF8 {November 18, 2007 10:50:27 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:50:30 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:50:30 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:50:30 PM PST}
- UPDATED: Updated protein page: PRPF8 {November 18, 2007 10:50:35 PM PST}
- INFO: Beginning work on RUVBL2... {November 18, 2007 10:51:59 PM PST}
- SEARCH REDIRECT: Control Box Found: RUVBL2 {November 18, 2007 10:52:32 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:52:34 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:52:34 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:52:34 PM PST}
- UPDATED: Updated protein page: RUVBL2 {November 18, 2007 10:52:41 PM PST}
- INFO: Beginning work on SLC29A1... {November 18, 2007 10:43:27 PM PST}
- SEARCH REDIRECT: Control Box Found: SLC29A1 {November 18, 2007 10:43:58 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:44:01 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:44:01 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:44:01 PM PST}
- UPDATED: Updated protein page: SLC29A1 {November 18, 2007 10:44:07 PM PST}
end log.
