Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 19:25, 18 November 2007 (UTC)[edit]
Proteins without matches (12)[edit]
Proteins with a High Potential Match (5)[edit]
Redirected Proteins (8)[edit]
Manual Inspection (Page not found) (17)[edit]
Updated (8)[edit]
Protein Status Grid - Date: 19:25, 18 November 2007 (UTC)[edit]
Vebose Log - Date: 19:25, 18 November 2007 (UTC)[edit]
- INFO: Beginning work on ACADM... {November 18, 2007 10:58:52 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:59:33 AM PST}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ACADM_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1egc.
| PDB = {{PDB2|1egc}}, {{PDB2|1egd}}, {{PDB2|1ege}}, {{PDB2|1t9g}}, {{PDB2|2a1t}}
| Name = Acyl-Coenzyme A dehydrogenase, C-4 to C-12 straight chain
| HGNCid = 89
| Symbol = ACADM
| AltSymbols =; ACAD1; MCAD; MCADH
| OMIM = 607008
| ECnumber =
| Homologene = 3
| MGIid =
| Function = {{GNF_GO|id=GO:0003995 |text = acyl-CoA dehydrogenase activity}} {{GNF_GO|id=GO:0050660 |text = FAD binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005759 |text = mitochondrial matrix}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006631 |text = fatty acid metabolic process}} {{GNF_GO|id=GO:0006635 |text = fatty acid beta-oxidation}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 34
| Hs_Ensembl = ENSG00000117054
| Hs_RefseqProtein = NP_000007
| Hs_RefseqmRNA = NM_000016
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 75962624
| Hs_GenLoc_end = 76001952
| Hs_Uniprot = P11310
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Acyl-Coenzyme A dehydrogenase, C-4 to C-12 straight chain''', also known as '''ACADM''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACADM acyl-Coenzyme A dehydrogenase, C-4 to C-12 straight chain| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=34| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes the medium-chain specific (C4 to C12 straight chain) acyl-Coenzyme A dehydrogenase. The homotetramer enzyme catalyzes the initial step of the mitochondrial fatty acid beta-oxidation pathway. Clinical phenotypes are associated with ACADM hereditary deficiency.<ref name="entrez">{{cite web | title = Entrez Gene: ACADM acyl-Coenzyme A dehydrogenase, C-4 to C-12 straight chain| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=34| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tanaka K, Yokota I, Coates PM, ''et al.'' |title=Mutations in the medium chain acyl-CoA dehydrogenase (MCAD) gene. |journal=Hum. Mutat. |volume=1 |issue= 4 |pages= 271-9 |year= 1993 |pmid= 1363805 |doi= 10.1002/humu.1380010402 }}
*{{cite journal | author=Blakemore AI, Singleton H, Pollitt RJ, ''et al.'' |title=Frequency of the G985 MCAD mutation in the general population. |journal=Lancet |volume=337 |issue= 8736 |pages= 298-9 |year= 1991 |pmid= 1671131 |doi= }}
*{{cite journal | author=Kølvraa S, Gregersen N, Blakemore AI, ''et al.'' |title=The most common mutation causing medium-chain acyl-CoA dehydrogenase deficiency is strongly associated with a particular haplotype in the region of the gene. |journal=Hum. Genet. |volume=87 |issue= 4 |pages= 425-8 |year= 1991 |pmid= 1679031 |doi= }}
*{{cite journal | author=Yokota I, Coates PM, Hale DE, ''et al.'' |title=Molecular survey of a prevalent mutation, 985A-to-G transition, and identification of five infrequent mutations in the medium-chain Acyl-CoA dehydrogenase (MCAD) gene in 55 patients with MCAD deficiency. |journal=Am. J. Hum. Genet. |volume=49 |issue= 6 |pages= 1280-91 |year= 1992 |pmid= 1684086 |doi= }}
*{{cite journal | author=Ding JH, Yang BZ, Bao Y, ''et al.'' |title=Identification of a new mutation in medium-chain acyl-CoA dehydrogenase (MCAD) deficiency. |journal=Am. J. Hum. Genet. |volume=50 |issue= 1 |pages= 229-33 |year= 1992 |pmid= 1729890 |doi= }}
*{{cite journal | author=Zhang ZF, Kelly DP, Kim JJ, ''et al.'' |title=Structural organization and regulatory regions of the human medium-chain acyl-CoA dehydrogenase gene. |journal=Biochemistry |volume=31 |issue= 1 |pages= 81-9 |year= 1992 |pmid= 1731887 |doi= }}
*{{cite journal | author=Gregersen N, Andresen BS, Bross P, ''et al.'' |title=Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: identification of a lys329 to glu mutation in the MCAD gene, and expression of inactive mutant enzyme protein in E. coli. |journal=Hum. Genet. |volume=86 |issue= 6 |pages= 545-51 |year= 1991 |pmid= 1902818 |doi= }}
*{{cite journal | author=Kelly DP, Whelan AJ, Ogden ML, ''et al.'' |title=Molecular characterization of inherited medium-chain acyl-CoA dehydrogenase deficiency. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 23 |pages= 9236-40 |year= 1991 |pmid= 2251268 |doi= }}
*{{cite journal | author=Matsubara Y, Narisawa K, Miyabayashi S, ''et al.'' |title=Identification of a common mutation in patients with medium-chain acyl-CoA dehydrogenase deficiency. |journal=Biochem. Biophys. Res. Commun. |volume=171 |issue= 1 |pages= 498-505 |year= 1990 |pmid= 2393404 |doi= }}
*{{cite journal | author=Yokota I, Indo Y, Coates PM, Tanaka K |title=Molecular basis of medium chain acyl-coenzyme A dehydrogenase deficiency. An A to G transition at position 985 that causes a lysine-304 to glutamate substitution in the mature protein is the single prevalent mutation. |journal=J. Clin. Invest. |volume=86 |issue= 3 |pages= 1000-3 |year= 1990 |pmid= 2394825 |doi= }}
*{{cite journal | author=Kelly DP, Kim JJ, Billadello JJ, ''et al.'' |title=Nucleotide sequence of medium-chain acyl-CoA dehydrogenase mRNA and its expression in enzyme-deficient human tissue. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 12 |pages= 4068-72 |year= 1987 |pmid= 3035565 |doi= }}
*{{cite journal | author=Matsubara Y, Kraus JP, Yang-Feng TL, ''et al.'' |title=Molecular cloning of cDNAs encoding rat and human medium-chain acyl-CoA dehydrogenase and assignment of the gene to human chromosome 1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 17 |pages= 6543-7 |year= 1986 |pmid= 3462713 |doi= }}
*{{cite journal | author=Finocchiaro G, Ito M, Tanaka K |title=Purification and properties of short chain acyl-CoA, medium chain acyl-CoA, and isovaleryl-CoA dehydrogenases from human liver. |journal=J. Biol. Chem. |volume=262 |issue= 17 |pages= 7982-9 |year= 1987 |pmid= 3597357 |doi= }}
*{{cite journal | author=Duran M, Hofkamp M, Rhead WJ, ''et al.'' |title=Sudden child death and 'healthy' affected family members with medium-chain acyl-coenzyme A dehydrogenase deficiency. |journal=Pediatrics |volume=78 |issue= 6 |pages= 1052-7 |year= 1987 |pmid= 3786030 |doi= }}
*{{cite journal | author=Rhead WJ, Amendt BA, Fritchman KS, Felts SJ |title=Dicarboxylic aciduria: deficient [1-14C]octanoate oxidation and medium-chain acyl-CoA dehydrogenase in fibroblasts. |journal=Science |volume=221 |issue= 4605 |pages= 73-5 |year= 1983 |pmid= 6857268 |doi= }}
*{{cite journal | author=Ziadeh R, Hoffman EP, Finegold DN, ''et al.'' |title=Medium chain acyl-CoA dehydrogenase deficiency in Pennsylvania: neonatal screening shows high incidence and unexpected mutation frequencies. |journal=Pediatr. Res. |volume=37 |issue= 5 |pages= 675-8 |year= 1995 |pmid= 7603790 |doi= }}
*{{cite journal | author=Leone TC, Cresci S, Carter ME, ''et al.'' |title=The human medium chain Acyl-CoA dehydrogenase gene promoter consists of a complex arrangement of nuclear receptor response elements and Sp1 binding sites. |journal=J. Biol. Chem. |volume=270 |issue= 27 |pages= 16308-14 |year= 1995 |pmid= 7608198 |doi= }}
*{{cite journal | author=Brackett JC, Sims HF, Steiner RD, ''et al.'' |title=A novel mutation in medium chain acyl-CoA dehydrogenase causes sudden neonatal death. |journal=J. Clin. Invest. |volume=94 |issue= 4 |pages= 1477-83 |year= 1994 |pmid= 7929823 |doi= }}
*{{cite journal | author=Andresen BS, Jensen TG, Bross P, ''et al.'' |title=Disease-causing mutations in exon 11 of the medium-chain acyl-CoA dehydrogenase gene. |journal=Am. J. Hum. Genet. |volume=54 |issue= 6 |pages= 975-88 |year= 1994 |pmid= 8198141 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ACTA2... {November 18, 2007 10:59:33 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:00:15 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ACTA2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1atn.
| PDB = {{PDB2|1atn}}, {{PDB2|1c0f}}, {{PDB2|1c0g}}, {{PDB2|1d4x}}, {{PDB2|1dej}}, {{PDB2|1eqy}}, {{PDB2|1esv}}, {{PDB2|1h1v}}, {{PDB2|1hlu}}, {{PDB2|1ijj}}, {{PDB2|1j6z}}, {{PDB2|1kxp}}, {{PDB2|1lcu}}, {{PDB2|1lot}}, {{PDB2|1m8q}}, {{PDB2|1ma9}}, {{PDB2|1mdu}}, {{PDB2|1mvw}}, {{PDB2|1nlv}}, {{PDB2|1nm1}}, {{PDB2|1nmd}}, {{PDB2|1nwk}}, {{PDB2|1o18}}, {{PDB2|1o19}}, {{PDB2|1o1a}}, {{PDB2|1o1b}}, {{PDB2|1o1c}}, {{PDB2|1o1d}}, {{PDB2|1o1e}}, {{PDB2|1o1f}}, {{PDB2|1o1g}}, {{PDB2|1p8z}}, {{PDB2|1qz5}}, {{PDB2|1qz6}}, {{PDB2|1rdw}}, {{PDB2|1rfq}}, {{PDB2|1rgi}}, {{PDB2|1s22}}, {{PDB2|1sqk}}, {{PDB2|1t44}}, {{PDB2|1wua}}, {{PDB2|1y64}}, {{PDB2|1yxq}}, {{PDB2|2a3z}}, {{PDB2|2a40}}, {{PDB2|2a41}}, {{PDB2|2a42}}, {{PDB2|2a5x}}, {{PDB2|2asm}}, {{PDB2|2aso}}, {{PDB2|2asp}}, {{PDB2|2btf}}, {{PDB2|2d1k}}, {{PDB2|2ff3}}, {{PDB2|2ff6}}, {{PDB2|2fxu}}, {{PDB2|2gwj}}, {{PDB2|2gwk}}, {{PDB2|2hf3}}, {{PDB2|2hf4}}, {{PDB2|2hmp}}, {{PDB2|2oan}}, {{PDB2|2q1n}}, {{PDB2|2q31}}, {{PDB2|2q36}}
| Name = Actin, alpha 2, smooth muscle, aorta
| HGNCid = 130
| Symbol = ACTA2
| AltSymbols =; ACTSA
| OMIM = 102620
| ECnumber =
| Homologene = 48026
| MGIid = 87909
| GeneAtlas_image1 = PBB_GE_ACTA2_200974_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}}
| Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}}
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 59
| Hs_Ensembl = ENSG00000107796
| Hs_RefseqProtein = NP_001604
| Hs_RefseqmRNA = NM_001613
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 90684811
| Hs_GenLoc_end = 90741084
| Hs_Uniprot = P62736
| Mm_EntrezGene = 11475
| Mm_Ensembl = ENSMUSG00000035783
| Mm_RefseqmRNA = NM_007392
| Mm_RefseqProtein = NP_031418
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 34307088
| Mm_GenLoc_end = 34321333
| Mm_Uniprot = Q3U122
}}
}}
'''Actin, alpha 2, smooth muscle, aorta''', also known as '''ACTA2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACTA2 actin, alpha 2, smooth muscle, aorta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=59| 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 = Actin alpha 2, the human aortic smooth muscle actin gene, is one of six different actin isoforms which have been identified. Actins are highly conserved proteins that are involved in cell motility, structure and integrity. Alpha actins are a major constituent of the contractile apparatus.<ref name="entrez">{{cite web | title = Entrez Gene: ACTA2 actin, alpha 2, smooth muscle, aorta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=59| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Snásel J, Pichová I |title=The cleavage of host cell proteins by HIV-1 protease. |journal=Folia Biol. (Praha) |volume=42 |issue= 5 |pages= 227-30 |year= 1997 |pmid= 8997639 |doi= }}
*{{cite journal | author=Adams LD, Tomasselli AG, Robbins P, ''et al.'' |title=HIV-1 protease cleaves actin during acute infection of human T-lymphocytes. |journal=AIDS Res. Hum. Retroviruses |volume=8 |issue= 2 |pages= 291-5 |year= 1992 |pmid= 1540415 |doi= }}
*{{cite journal | author=Harris DE, Warshaw DM, Periasamy M |title=Nucleotide sequences of the rabbit alpha-smooth-muscle and beta-non-muscle actin mRNAs. |journal=Gene |volume=112 |issue= 2 |pages= 265-6 |year= 1992 |pmid= 1555776 |doi= }}
*{{cite journal | author=Tomasselli AG, Hui JO, Adams L, ''et al.'' |title=Actin, troponin C, Alzheimer amyloid precursor protein and pro-interleukin 1 beta as substrates of the protease from human immunodeficiency virus. |journal=J. Biol. Chem. |volume=266 |issue= 22 |pages= 14548-53 |year= 1991 |pmid= 1907279 |doi= }}
*{{cite journal | author=Jahoda CA, Reynolds AJ, Chaponnier C, ''et al.'' |title=Smooth muscle alpha-actin is a marker for hair follicle dermis in vivo and in vitro. |journal=J. Cell. Sci. |volume=99 ( Pt 3) |issue= |pages= 627-36 |year= 1991 |pmid= 1939373 |doi= }}
*{{cite journal | author=Ueyama H, Ohsugi R |title=TaqI polymorphism in the 3' flanking region of the human aortic smooth muscle actin gene. |journal=Nucleic Acids Res. |volume=18 |issue= 5 |pages= 1318 |year= 1990 |pmid= 1969628 |doi= }}
*{{cite journal | author=Shoeman RL, Kesselmier C, Mothes E, ''et al.'' |title=Non-viral cellular substrates for human immunodeficiency virus type 1 protease. |journal=FEBS Lett. |volume=278 |issue= 2 |pages= 199-203 |year= 1991 |pmid= 1991513 |doi= }}
*{{cite journal | author=Nakano Y, Nishihara T, Sasayama S, ''et al.'' |title=Transcriptional regulatory elements in the 5' upstream and first intron regions of the human smooth muscle (aortic type) alpha-actin-encoding gene. |journal=Gene |volume=99 |issue= 2 |pages= 285-9 |year= 1991 |pmid= 2022339 |doi= }}
*{{cite journal | author=Reddy S, Ozgur K, Lu M, ''et al.'' |title=Structure of the human smooth muscle alpha-actin gene. Analysis of a cDNA and 5' upstream region. |journal=J. Biol. Chem. |volume=265 |issue= 3 |pages= 1683-7 |year= 1990 |pmid= 2295650 |doi= }}
*{{cite journal | author=Ueyama H, Bruns G, Kanda N |title=Assignment of the vascular smooth muscle actin gene ACTSA to human chromosome 10. |journal=Jinrui Idengaku Zasshi |volume=35 |issue= 2 |pages= 145-50 |year= 1990 |pmid= 2398629 |doi= }}
*{{cite journal | author=Kamada S, Nakano Y, Kakunaga T |title=Structure of 3'-downstream segment of the human smooth muscle (aortic-type) alpha-actin-encoding gene and isolation of the specific DNA probe. |journal=Gene |volume=84 |issue= 2 |pages= 455-62 |year= 1990 |pmid= 2612915 |doi= }}
*{{cite journal | author=Kamada S, Kakunaga T |title=The nucleotide sequence of a human smooth muscle alpha-actin (aortic type) cDNA. |journal=Nucleic Acids Res. |volume=17 |issue= 4 |pages= 1767 |year= 1989 |pmid= 2701935 |doi= }}
*{{cite journal | author=Kedes L, Ng SY, Lin CS, ''et al.'' |title=The human beta-actin multigene family. |journal=Trans. Assoc. Am. Physicians |volume=98 |issue= |pages= 42-6 |year= 1986 |pmid= 3842206 |doi= }}
*{{cite journal | author=Ueyama H, Hamada H, Battula N, Kakunaga T |title=Structure of a human smooth muscle actin gene (aortic type) with a unique intron site. |journal=Mol. Cell. Biol. |volume=4 |issue= 6 |pages= 1073-8 |year= 1984 |pmid= 6330528 |doi= }}
*{{cite journal | author=Strauch AR, Rubenstein PA |title=A vascular smooth muscle alpha-isoactin biosynthetic intermediate in BC3H1 cells. Identification of acetylcysteine at the NH2 terminus. |journal=J. Biol. Chem. |volume=259 |issue= 11 |pages= 7224-9 |year= 1984 |pmid= 6725286 |doi= }}
*{{cite journal | author=Ueyama H, Inazawa J, Ariyama T, ''et al.'' |title=Reexamination of chromosomal loci of human muscle actin genes by fluorescence in situ hybridization. |journal=Jpn. J. Hum. Genet. |volume=40 |issue= 1 |pages= 145-8 |year= 1995 |pmid= 7780165 |doi= }}
*{{cite journal | author=Arora PD, McCulloch CA |title=Dependence of collagen remodelling on alpha-smooth muscle actin expression by fibroblasts. |journal=J. Cell. Physiol. |volume=159 |issue= 1 |pages= 161-75 |year= 1994 |pmid= 8138584 |doi= 10.1002/jcp.1041590120 }}
*{{cite journal | author=Iwata Y, Pan Y, Yoshida T, ''et al.'' |title=Alpha1-syntrophin has distinct binding sites for actin and calmodulin. |journal=FEBS Lett. |volume=423 |issue= 2 |pages= 173-7 |year= 1998 |pmid= 9512352 |doi= }}
*{{cite journal | author=Comer KA, Dennis PA, Armstrong L, ''et al.'' |title=Human smooth muscle alpha-actin gene is a transcriptional target of the p53 tumor suppressor protein. |journal=Oncogene |volume=16 |issue= 10 |pages= 1299-308 |year= 1998 |pmid= 9546431 |doi= 10.1038/sj.onc.1201645 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ERVWE1... {November 18, 2007 11:15:26 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:16:11 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Endogenous retroviral family W, env(C7), member 1 (syncytin)
| HGNCid = 13525
| Symbol = ERVWE1
| AltSymbols =; Env-W; HERV-7q; HERV-W; HERV-W-ENV; HERVW; env
| OMIM = 604659
| ECnumber =
| Homologene =
| MGIid =
| Function = {{GNF_GO|id=GO:0005198 |text = structural molecule activity}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0019028 |text = viral capsid}} {{GNF_GO|id=GO:0019031 |text = viral envelope}}
| Process = {{GNF_GO|id=GO:0006313 |text = transposition, DNA-mediated}} {{GNF_GO|id=GO:0006949 |text = syncytium formation}} {{GNF_GO|id=GO:0009653 |text = anatomical structure morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 30816
| Hs_Ensembl = ENSG00000197604
| Hs_RefseqProtein = NP_055405
| Hs_RefseqmRNA = NM_014590
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 91936015
| Hs_GenLoc_end = 91937631
| Hs_Uniprot = Q9UQF0
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Endogenous retroviral family W, env(C7), member 1 (syncytin)''', also known as '''ERVWE1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ERVWE1 endogenous retroviral family W, env(C7), member 1 (syncytin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=30816| 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 = Many different human endogenous retrovirus (HERV) families are expressed in normal placental tissue at high levels, suggesting that HERVs are functionally important in reproduction. This gene is part of an HERV provirus on chromosome 7 that has inactivating mutations in the gag and pol genes. This gene is the envelope glycoprotein gene which appears to have been selectively preserved. The product of this gene, syncytin, is expressed in the placental syncytiotrophoblast and is involved in fusion of the cytotrophoblast cells to form the syncytial layer of the placenta. The protein has the characteristics of a typical retroviral envelope protein, including a furin cleavage site that separates the surface (SU) and transmembrane (TM) proteins which form a heterodimer.<ref name="entrez">{{cite web | title = Entrez Gene: ERVWE1 endogenous retroviral family W, env(C7), member 1 (syncytin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=30816| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Muir A, Lever A, Moffett A |title=Expression and functions of human endogenous retroviruses in the placenta: an update. |journal=Placenta |volume=25 Suppl A |issue= |pages= S16-25 |year= 2004 |pmid= 15033302 |doi= 10.1016/j.placenta.2004.01.012 }}
*{{cite journal | author=Alliel PM, Périn JP, Pierig R, ''et al.'' |title=Endogenous retroviruses and multiple sclerosis. II. HERV-7q. |journal=C. R. Acad. Sci. III, Sci. Vie |volume=321 |issue= 10 |pages= 857-63 |year= 1998 |pmid= 9835022 |doi= }}
*{{cite journal | author=Blond JL, Besème F, Duret L, ''et al.'' |title=Molecular characterization and placental expression of HERV-W, a new human endogenous retrovirus family. |journal=J. Virol. |volume=73 |issue= 2 |pages= 1175-85 |year= 1999 |pmid= 9882319 |doi= }}
*{{cite journal | author=Voisset C, Blancher A, Perron H, ''et al.'' |title=Phylogeny of a novel family of human endogenous retrovirus sequences, HERV-W, in humans and other primates. |journal=AIDS Res. Hum. Retroviruses |volume=15 |issue= 17 |pages= 1529-33 |year= 1999 |pmid= 10580403 |doi= 10.1089/088922299309810 }}
*{{cite journal | author=Mi S, Lee X, Li X, ''et al.'' |title=Syncytin is a captive retroviral envelope protein involved in human placental morphogenesis. |journal=Nature |volume=403 |issue= 6771 |pages= 785-9 |year= 2000 |pmid= 10693809 |doi= 10.1038/35001608 }}
*{{cite journal | author=Blond JL, Lavillette D, Cheynet V, ''et al.'' |title=An envelope glycoprotein of the human endogenous retrovirus HERV-W is expressed in the human placenta and fuses cells expressing the type D mammalian retrovirus receptor. |journal=J. Virol. |volume=74 |issue= 7 |pages= 3321-9 |year= 2000 |pmid= 10708449 |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=Voisset C, Bouton O, Bedin F, ''et al.'' |title=Chromosomal distribution and coding capacity of the human endogenous retrovirus HERV-W family. |journal=AIDS Res. Hum. Retroviruses |volume=16 |issue= 8 |pages= 731-40 |year= 2000 |pmid= 10826480 |doi= 10.1089/088922200308738 }}
*{{cite journal | author=An DS, Xie Ym , Chen IS |title=Envelope gene of the human endogenous retrovirus HERV-W encodes a functional retrovirus envelope. |journal=J. Virol. |volume=75 |issue= 7 |pages= 3488-9 |year= 2001 |pmid= 11238877 |doi= 10.1128/JVI.75.7.3488-3489.2001 }}
*{{cite journal | author=Kim HS, Lee WH |title=Human endogenous retrovirus HERV-W family: chromosomal localization, identification, and phylogeny. |journal=AIDS Res. Hum. Retroviruses |volume=17 |issue= 7 |pages= 643-8 |year= 2001 |pmid= 11375061 |doi= 10.1089/088922201300119752 }}
*{{cite journal | author=Perron H, Jouvin-Marche E, Michel M, ''et al.'' |title=Multiple sclerosis retrovirus particles and recombinant envelope trigger an abnormal immune response in vitro, by inducing polyclonal Vbeta16 T-lymphocyte activation. |journal=Virology |volume=287 |issue= 2 |pages= 321-32 |year= 2001 |pmid= 11531410 |doi= 10.1006/viro.2001.1045 }}
*{{cite journal | author=Knerr I, Beinder E, Rascher W |title=Syncytin, a novel human endogenous retroviral gene in human placenta: evidence for its dysregulation in preeclampsia and HELLP syndrome. |journal=Am. J. Obstet. Gynecol. |volume=186 |issue= 2 |pages= 210-3 |year= 2002 |pmid= 11854637 |doi= }}
*{{cite journal | author=Alliel PM, Périn JP, Goudou D, ''et al.'' |title=The HERV-W/7q family in the human genome. Potential for protein expression and gene regulation. |journal=Cell. Mol. Biol. (Noisy-le-grand) |volume=48 |issue= 2 |pages= 213-7 |year= 2002 |pmid= 11990458 |doi= }}
*{{cite journal | author=Lavillette D, Marin M, Ruggieri A, ''et al.'' |title=The envelope glycoprotein of human endogenous retrovirus type W uses a divergent family of amino acid transporters/cell surface receptors. |journal=J. Virol. |volume=76 |issue= 13 |pages= 6442-52 |year= 2002 |pmid= 12050356 |doi= }}
*{{cite journal | author=Kudo Y, Boyd CA |title=Changes in expression and function of syncytin and its receptor, amino acid transport system B(0) (ASCT2), in human placental choriocarcinoma BeWo cells during syncytialization. |journal=Placenta |volume=23 |issue= 7 |pages= 536-41 |year= 2003 |pmid= 12175968 |doi= }}
*{{cite journal | author=Yu C, Shen K, Lin M, ''et al.'' |title=GCMa regulates the syncytin-mediated trophoblastic fusion. |journal=J. Biol. Chem. |volume=277 |issue= 51 |pages= 50062-8 |year= 2003 |pmid= 12397062 |doi= 10.1074/jbc.M209316200 }}
*{{cite journal | author=Smallwood A, Papageorghiou A, Nicolaides K, ''et al.'' |title=Temporal regulation of the expression of syncytin (HERV-W), maternally imprinted PEG10, and SGCE in human placenta. |journal=Biol. Reprod. |volume=69 |issue= 1 |pages= 286-93 |year= 2004 |pmid= 12620933 |doi= 10.1095/biolreprod.102.013078 }}
*{{cite journal | author=Ponferrada VG, Mauck BS, Wooley DP |title=The envelope glycoprotein of human endogenous retrovirus HERV-W induces cellular resistance to spleen necrosis virus. |journal=Arch. Virol. |volume=148 |issue= 4 |pages= 659-75 |year= 2003 |pmid= 12664292 |doi= 10.1007/s00705-002-0960-x }}
*{{cite journal | author=Frendo JL, Olivier D, Cheynet V, ''et al.'' |title=Direct involvement of HERV-W Env glycoprotein in human trophoblast cell fusion and differentiation. |journal=Mol. Cell. Biol. |volume=23 |issue= 10 |pages= 3566-74 |year= 2003 |pmid= 12724415 |doi= }}
*{{cite journal | author=Kudo Y, Boyd CA, Sargent IL, Redman CW |title=Hypoxia alters expression and function of syncytin and its receptor during trophoblast cell fusion of human placental BeWo cells: implications for impaired trophoblast syncytialisation in pre-eclampsia. |journal=Biochim. Biophys. Acta |volume=1638 |issue= 1 |pages= 63-71 |year= 2003 |pmid= 12757936 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FBXW7... {November 18, 2007 11:16:57 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:18:03 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_FBXW7_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2ovp.
| PDB = {{PDB2|2ovp}}, {{PDB2|2ovq}}, {{PDB2|2ovr}}
| Name = F-box and WD repeat domain containing 7
| HGNCid = 16712
| Symbol = FBXW7
| AltSymbols =; AGO; CDC4; DKFZp686F23254; FBW7; FBX30; FBXW6; SEL-10; SEL10
| OMIM = 606278
| ECnumber =
| Homologene = 69520
| MGIid = 1354695
| GeneAtlas_image1 = PBB_GE_FBXW7_218751_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}}
| Process = {{GNF_GO|id=GO:0007219 |text = Notch signaling pathway}} {{GNF_GO|id=GO:0016567 |text = protein ubiquitination}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 55294
| Hs_Ensembl = ENSG00000109670
| Hs_RefseqProtein = NP_001013433
| Hs_RefseqmRNA = NM_001013415
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 153461860
| Hs_GenLoc_end = 153675622
| Hs_Uniprot = Q969H0
| Mm_EntrezGene = 50754
| Mm_Ensembl = ENSMUSG00000028086
| Mm_RefseqmRNA = NM_080428
| Mm_RefseqProtein = NP_536353
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 85038138
| Mm_GenLoc_end = 85063572
| Mm_Uniprot = Q8VBV4
}}
}}
'''F-box and WD repeat domain containing 7''', also known as '''FBXW7''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FBXW7 F-box and WD repeat domain containing 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55294| 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 F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene was previously referred to as FBX30, and belongs to the Fbws class; in addition to an F-box, this protein contains 7 tandem WD40 repeats. This protein binds directly to cyclin E and probably targets cyclin E for ubiquitin-mediated degradation. Mutations in this gene are detected in ovarian and breast cancer cell lines, implicating the gene's potential role in the pathogenesis of human cancers. Three transcript variants encoding three different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: FBXW7 F-box and WD repeat domain containing 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=55294| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Robertson NG, Khetarpal U, Gutiérrez-Espeleta GA, ''et al.'' |title=Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening. |journal=Genomics |volume=23 |issue= 1 |pages= 42-50 |year= 1995 |pmid= 7829101 |doi= 10.1006/geno.1994.1457 }}
*{{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=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=Winston JT, Koepp DM, Zhu C, ''et al.'' |title=A family of mammalian F-box proteins. |journal=Curr. Biol. |volume=9 |issue= 20 |pages= 1180-2 |year= 1999 |pmid= 10531037 |doi= 10.1016/S0960-9822(00)80021-4 }}
*{{cite journal | author=Gupta-Rossi N, Le Bail O, Gonen H, ''et al.'' |title=Functional interaction between SEL-10, an F-box protein, and the nuclear form of activated Notch1 receptor. |journal=J. Biol. Chem. |volume=276 |issue= 37 |pages= 34371-8 |year= 2001 |pmid= 11425854 |doi= 10.1074/jbc.M101343200 }}
*{{cite journal | author=Oberg C, Li J, Pauley A, ''et al.'' |title=The Notch intracellular domain is ubiquitinated and negatively regulated by the mammalian Sel-10 homolog. |journal=J. Biol. Chem. |volume=276 |issue= 38 |pages= 35847-53 |year= 2001 |pmid= 11461910 |doi= 10.1074/jbc.M103992200 }}
*{{cite journal | author=Koepp DM, Schaefer LK, Ye X, ''et al.'' |title=Phosphorylation-dependent ubiquitination of cyclin E by the SCFFbw7 ubiquitin ligase. |journal=Science |volume=294 |issue= 5540 |pages= 173-7 |year= 2001 |pmid= 11533444 |doi= 10.1126/science.1065203 }}
*{{cite journal | author=Moberg KH, Bell DW, Wahrer DC, ''et al.'' |title=Archipelago regulates Cyclin E levels in Drosophila and is mutated in human cancer cell lines. |journal=Nature |volume=413 |issue= 6853 |pages= 311-6 |year= 2001 |pmid= 11565033 |doi= 10.1038/35095068 }}
*{{cite journal | author=Strohmaier H, Spruck CH, Kaiser P, ''et al.'' |title=Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line. |journal=Nature |volume=413 |issue= 6853 |pages= 316-22 |year= 2001 |pmid= 11565034 |doi= 10.1038/35095076 }}
*{{cite journal | author=Wu G, Lyapina S, Das I, ''et al.'' |title=SEL-10 is an inhibitor of notch signaling that targets notch for ubiquitin-mediated protein degradation. |journal=Mol. Cell. Biol. |volume=21 |issue= 21 |pages= 7403-15 |year= 2001 |pmid= 11585921 |doi= 10.1128/MCB.21.21.7403-7415.2001 }}
*{{cite journal | author=Spruck CH, Strohmaier H, Sangfelt O, ''et al.'' |title=hCDC4 gene mutations in endometrial cancer. |journal=Cancer Res. |volume=62 |issue= 16 |pages= 4535-9 |year= 2002 |pmid= 12183400 |doi= }}
*{{cite journal | author=Li J, Pauley AM, Myers RL, ''et al.'' |title=SEL-10 interacts with presenilin 1, facilitates its ubiquitination, and alters A-beta peptide production. |journal=J. Neurochem. |volume=82 |issue= 6 |pages= 1540-8 |year= 2002 |pmid= 12354302 |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=Staropoli JF, McDermott C, Martinat C, ''et al.'' |title=Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity. |journal=Neuron |volume=37 |issue= 5 |pages= 735-49 |year= 2003 |pmid= 12628165 |doi= }}
*{{cite journal | author=Calhoun ES, Jones JB, Ashfaq R, ''et al.'' |title=BRAF and FBXW7 (CDC4, FBW7, AGO, SEL10) mutations in distinct subsets of pancreatic cancer: potential therapeutic targets. |journal=Am. J. Pathol. |volume=163 |issue= 4 |pages= 1255-60 |year= 2003 |pmid= 14507635 |doi= }}
*{{cite journal | author=Welcker M, Singer J, Loeb KR, ''et al.'' |title=Multisite phosphorylation by Cdk2 and GSK3 controls cyclin E degradation. |journal=Mol. Cell |volume=12 |issue= 2 |pages= 381-92 |year= 2003 |pmid= 14536078 |doi= }}
*{{cite journal | author=Busino L, Donzelli M, Chiesa M, ''et al.'' |title=Degradation of Cdc25A by beta-TrCP during S phase and in response to DNA damage. |journal=Nature |volume=426 |issue= 6962 |pages= 87-91 |year= 2003 |pmid= 14603323 |doi= 10.1038/nature02082 }}
*{{cite journal | author=Cassia R, Moreno-Bueno G, Rodríguez-Perales S, ''et al.'' |title=Cyclin E gene (CCNE) amplification and hCDC4 mutations in endometrial carcinoma. |journal=J. Pathol. |volume=201 |issue= 4 |pages= 589-95 |year= 2004 |pmid= 14648662 |doi= 10.1002/path.1474 }}
*{{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=Nateri AS, Riera-Sans L, Da Costa C, Behrens A |title=The ubiquitin ligase SCFFbw7 antagonizes apoptotic JNK signaling. |journal=Science |volume=303 |issue= 5662 |pages= 1374-8 |year= 2004 |pmid= 14739463 |doi= 10.1126/science.1092880 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GTF2H2... {November 18, 2007 11:01:21 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:02:07 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_GTF2H2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1z60.
| PDB = {{PDB2|1z60}}
| Name = General transcription factor IIH, polypeptide 2, 44kDa
| HGNCid = 4656
| Symbol = GTF2H2
| AltSymbols =; BTF2; TFIIH; BTF2P44; MGC102806; T-BTF2P44
| OMIM = 601748
| ECnumber =
| Homologene = 1159
| MGIid = 1345669
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003702 |text = RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0008135 |text = translation factor activity, nucleic acid binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005675 |text = holo TFIIH complex}}
| Process = {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006352 |text = transcription initiation}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0009411 |text = response to UV}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2966
| Hs_Ensembl =
| Hs_RefseqProtein = NP_001506
| Hs_RefseqmRNA = NM_001515
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 23894
| Mm_Ensembl = ENSMUSG00000021639
| Mm_RefseqmRNA = NM_022011
| Mm_RefseqProtein = NP_071294
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 101568837
| Mm_GenLoc_end = 101592836
| Mm_Uniprot = Q7TPV0
}}
}}
'''General transcription factor IIH, polypeptide 2, 44kDa''', also known as '''GTF2H2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GTF2H2 general transcription factor IIH, polypeptide 2, 44kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2966| 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 part of a 500 kb inverted duplication on chromosome 5q13. This duplicated region contains at least four genes and repetitive elements which make it prone to rearrangements and deletions. The repetitiveness and complexity of the sequence have also caused difficulty in determining the organization of this genomic region. This gene is within the telomeric copy of the duplication. Deletion of this gene sometimes accompanies deletion of the neighboring SMN1 gene in spinal muscular atrophy (SMA) patients but it is unclear if deletion of this gene contributes to the SMA phenotype. This gene encodes the 44 kDa subunit of RNA polymerase II transcription initiation factor IIH which is involved in basal transcription and nucleotide excision repair. Transcript variants for this gene have been described, but their full length nature has not been determined. A second copy of this gene within the centromeric copy of the duplication has been described in the literature. It is reported to be different by either two or four base pairs; however, no sequence data is currently available for the centromeric copy of the gene.<ref name="entrez">{{cite web | title = Entrez Gene: GTF2H2 general transcription factor IIH, polypeptide 2, 44kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2966| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Svejstrup JQ, Vichi P, Egly JM |title=The multiple roles of transcription/repair factor TFIIH. |journal=Trends Biochem. Sci. |volume=21 |issue= 9 |pages= 346-50 |year= 1996 |pmid= 8870499 |doi= }}
*{{cite journal | author=Jeang KT |title=Tat, Tat-associated kinase, and transcription. |journal=J. Biomed. Sci. |volume=5 |issue= 1 |pages= 24-7 |year= 1998 |pmid= 9570510 |doi= }}
*{{cite journal | author=Yankulov K, Bentley D |title=Transcriptional control: Tat cofactors and transcriptional elongation. |journal=Curr. Biol. |volume=8 |issue= 13 |pages= R447-9 |year= 1998 |pmid= 9651670 |doi= }}
*{{cite journal | author=van der Steege G, Draaijers TG, Grootscholten PM, ''et al.'' |title=A provisional transcript map of the spinal muscular atrophy (SMA) critical region. |journal=Eur. J. Hum. Genet. |volume=3 |issue= 2 |pages= 87-95 |year= 1995 |pmid= 7552146 |doi= }}
*{{cite journal | author=Henning KA, Li L, Iyer N, ''et al.'' |title=The Cockayne syndrome group A gene encodes a WD repeat protein that interacts with CSB protein and a subunit of RNA polymerase II TFIIH. |journal=Cell |volume=82 |issue= 4 |pages= 555-64 |year= 1995 |pmid= 7664335 |doi= }}
*{{cite journal | author=Humbert S, van Vuuren H, Lutz Y, ''et al.'' |title=p44 and p34 subunits of the BTF2/TFIIH transcription factor have homologies with SSL1, a yeast protein involved in DNA repair. |journal=EMBO J. |volume=13 |issue= 10 |pages= 2393-8 |year= 1994 |pmid= 8194529 |doi= }}
*{{cite journal | author=Blau J, Xiao H, McCracken S, ''et al.'' |title=Three functional classes of transcriptional activation domain. |journal=Mol. Cell. Biol. |volume=16 |issue= 5 |pages= 2044-55 |year= 1996 |pmid= 8628270 |doi= }}
*{{cite journal | author=Iyer N, Reagan MS, Wu KJ, ''et al.'' |title=Interactions involving the human RNA polymerase II transcription/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein. |journal=Biochemistry |volume=35 |issue= 7 |pages= 2157-67 |year= 1996 |pmid= 8652557 |doi= 10.1021/bi9524124 }}
*{{cite journal | author=Reardon JT, Ge H, Gibbs E, ''et al.'' |title=Isolation and characterization of two human transcription factor IIH (TFIIH)-related complexes: ERCC2/CAK and TFIIH. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 13 |pages= 6482-7 |year= 1996 |pmid= 8692841 |doi= }}
*{{cite journal | author=Drapkin R, Le Roy G, Cho H, ''et al.'' |title=Human cyclin-dependent kinase-activating kinase exists in three distinct complexes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 13 |pages= 6488-93 |year= 1996 |pmid= 8692842 |doi= }}
*{{cite journal | author=Zhou Q, Sharp PA |title=Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. |journal=Science |volume=274 |issue= 5287 |pages= 605-10 |year= 1996 |pmid= 8849451 |doi= }}
*{{cite journal | author=Parada CA, Roeder RG |title=Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain. |journal=Nature |volume=384 |issue= 6607 |pages= 375-8 |year= 1996 |pmid= 8934526 |doi= 10.1038/384375a0 }}
*{{cite journal | author=Bürglen L, Seroz T, Miniou P, ''et al.'' |title=The gene encoding p44, a subunit of the transcription factor TFIIH, is involved in large-scale deletions associated with Werdnig-Hoffmann disease. |journal=Am. J. Hum. Genet. |volume=60 |issue= 1 |pages= 72-9 |year= 1997 |pmid= 8981949 |doi= }}
*{{cite journal | author=García-Martínez LF, Ivanov D, Gaynor RB |title=Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes. |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 6951-8 |year= 1997 |pmid= 9054383 |doi= }}
*{{cite journal | author=Carter TA, Bönnemann CG, Wang CH, ''et al.'' |title=A multicopy transcription-repair gene, BTF2p44, maps to the SMA region and demonstrates SMA associated deletions. |journal=Hum. Mol. Genet. |volume=6 |issue= 2 |pages= 229-36 |year= 1997 |pmid= 9063743 |doi= }}
*{{cite journal | author=Marinoni JC, Roy R, Vermeulen W, ''et al.'' |title=Cloning and characterization of p52, the fifth subunit of the core of the transcription/DNA repair factor TFIIH. |journal=EMBO J. |volume=16 |issue= 5 |pages= 1093-102 |year= 1997 |pmid= 9118947 |doi= 10.1093/emboj/16.5.1093 }}
*{{cite journal | author=Cujec TP, Cho H, Maldonado E, ''et al.'' |title=The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme. |journal=Mol. Cell. Biol. |volume=17 |issue= 4 |pages= 1817-23 |year= 1997 |pmid= 9121429 |doi= }}
*{{cite journal | author=Rossignol M, Kolb-Cheynel I, Egly JM |title=Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH. |journal=EMBO J. |volume=16 |issue= 7 |pages= 1628-37 |year= 1997 |pmid= 9130708 |doi= 10.1093/emboj/16.7.1628 }}
*{{cite journal | author=García-Martínez LF, Mavankal G, Neveu JM, ''et al.'' |title=Purification of a Tat-associated kinase reveals a TFIIH complex that modulates HIV-1 transcription. |journal=EMBO J. |volume=16 |issue= 10 |pages= 2836-50 |year= 1997 |pmid= 9184228 |doi= 10.1093/emboj/16.10.2836 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HLA-DMA... {November 18, 2007 11:03:03 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:04:10 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_HLA-DMA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hdm.
| PDB = {{PDB2|1hdm}}, {{PDB2|2bc4}}
| Name = Major histocompatibility complex, class II, DM alpha
| HGNCid = 4934
| Symbol = HLA-DMA
| AltSymbols =; D6S222E; DMA; HLADM; RING6
| OMIM = 142855
| ECnumber =
| Homologene = 4464
| MGIid = 95921
| GeneAtlas_image1 = PBB_GE_HLA-DMA_217478_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0032395 |text = MHC class II receptor activity}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005765 |text = lysosomal membrane}} {{GNF_GO|id=GO:0005771 |text = multivesicular body}} {{GNF_GO|id=GO:0010008 |text = endosome membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0042613 |text = MHC class II protein complex}}
| Process = {{GNF_GO|id=GO:0002504 |text = antigen processing and presentation of peptide or polysaccharide antigen via MHC class II}} {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0008150 |text = biological_process}} {{GNF_GO|id=GO:0015031 |text = protein transport}} {{GNF_GO|id=GO:0016064 |text = immunoglobulin mediated immune response}} {{GNF_GO|id=GO:0019886 |text = antigen processing and presentation of exogenous peptide antigen via MHC class II}} {{GNF_GO|id=GO:0045059 |text = positive thymic T cell selection}} {{GNF_GO|id=GO:0045582 |text = positive regulation of T cell differentiation}} {{GNF_GO|id=GO:0050778 |text = positive regulation of immune response}} {{GNF_GO|id=GO:0051085 |text = chaperone cofactor-dependent protein folding}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3108
| Hs_Ensembl = ENSG00000204257
| Hs_RefseqProtein = NP_006111
| Hs_RefseqmRNA = NM_006120
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 33024367
| Hs_GenLoc_end = 33028877
| Hs_Uniprot = P28067
| Mm_EntrezGene = 14998
| Mm_Ensembl = ENSMUSG00000037649
| Mm_RefseqmRNA = NM_010386
| Mm_RefseqProtein = NP_034516
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 33746125
| Mm_GenLoc_end = 33748991
| Mm_Uniprot = Q31096
}}
}}
'''Major histocompatibility complex, class II, DM alpha''', also known as '''HLA-DMA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HLA-DMA major histocompatibility complex, class II, DM alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3108| 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 = HLA-DMA belongs to the HLA class II alpha chain paralogues. This class II molecule is a heterodimer consisting of an alpha (DMA) and a beta chain (DMB), both anchored in the membrane. It is located in intracellular vesicles. DM plays a central role in the peptide loading of MHC class II molecules by helping to release the CLIP molecule from the peptide binding site. Class II molecules are expressed in antigen presenting cells (APC: B lymphocytes, dendritic cells, macrophages). The alpha chain is approximately 33-35 kDa and its gene contains 5 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, exon 4 encodes the transmembrane domain and the cytoplasmic tail.<ref name="entrez">{{cite web | title = Entrez Gene: HLA-DMA major histocompatibility complex, class II, DM alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3108| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Vogt AB, Kropshofer H |title=HLA-DM - an endosomal and lysosomal chaperone for the immune system. |journal=Trends Biochem. Sci. |volume=24 |issue= 4 |pages= 150-4 |year= 1999 |pmid= 10322421 |doi= }}
*{{cite journal | author=Kropshofer H, Hämmerling GJ, Vogt AB |title=The impact of the non-classical MHC proteins HLA-DM and HLA-DO on loading of MHC class II molecules. |journal=Immunol. Rev. |volume=172 |issue= |pages= 267-78 |year= 2000 |pmid= 10631952 |doi= }}
*{{cite journal | author=Piatier-Tonneau D, Gastinel LN, Amblard F, ''et al.'' |title=Interaction of CD4 with HLA class II antigens and HIV gp120. |journal=Immunogenetics |volume=34 |issue= 2 |pages= 121-8 |year= 1991 |pmid= 1869305 |doi= }}
*{{cite journal | author=Kelly AP, Monaco JJ, Cho SG, Trowsdale J |title=A new human HLA class II-related locus, DM. |journal=Nature |volume=353 |issue= 6344 |pages= 571-3 |year= 1991 |pmid= 1922365 |doi= 10.1038/353571a0 }}
*{{cite journal | author=Kelly A, Powis SH, Glynne R, ''et al.'' |title=Second proteasome-related gene in the human MHC class II region. |journal=Nature |volume=353 |issue= 6345 |pages= 667-8 |year= 1991 |pmid= 1922385 |doi= 10.1038/353667a0 }}
*{{cite journal | author=Rosenstein Y, Burakoff SJ, Herrmann SH |title=HIV-gp120 can block CD4-class II MHC-mediated adhesion. |journal=J. Immunol. |volume=144 |issue= 2 |pages= 526-31 |year= 1990 |pmid= 1967269 |doi= }}
*{{cite journal | author=Bowman MR, MacFerrin KD, Schreiber SL, Burakoff SJ |title=Identification and structural analysis of residues in the V1 region of CD4 involved in interaction with human immunodeficiency virus envelope glycoprotein gp120 and class II major histocompatibility complex molecules. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 22 |pages= 9052-6 |year= 1991 |pmid= 1978941 |doi= }}
*{{cite journal | author=Clayton LK, Sieh M, Pious DA, Reinherz EL |title=Identification of human CD4 residues affecting class II MHC versus HIV-1 gp120 binding. |journal=Nature |volume=339 |issue= 6225 |pages= 548-51 |year= 1989 |pmid= 2543930 |doi= 10.1038/339548a0 }}
*{{cite journal | author=Diamond DC, Sleckman BP, Gregory T, ''et al.'' |title=Inhibition of CD4+ T cell function by the HIV envelope protein, gp120. |journal=J. Immunol. |volume=141 |issue= 11 |pages= 3715-7 |year= 1988 |pmid= 2846691 |doi= }}
*{{cite journal | author=Andrieu JM, Even P, Venet A |title=AIDS and related syndromes as a viral-induced autoimmune disease of the immune system: an anti-MHC II disorder. Therapeutic implications. |journal=AIDS research |volume=2 |issue= 3 |pages= 163-74 |year= 1986 |pmid= 3489470 |doi= }}
*{{cite journal | author=Houlgatte R, Scarmato P, el Marhomy S, ''et al.'' |title=HLA class II antigens and the HIV envelope glycoprotein gp120 bind to the same face of CD4. |journal=J. Immunol. |volume=152 |issue= 9 |pages= 4475-88 |year= 1994 |pmid= 7512597 |doi= }}
*{{cite journal | author=Chirmule N, McCloskey TW, Hu R, ''et al.'' |title=HIV gp120 inhibits T cell activation by interfering with expression of costimulatory molecules CD40 ligand and CD80 (B71). |journal=J. Immunol. |volume=155 |issue= 2 |pages= 917-24 |year= 1995 |pmid= 7541827 |doi= }}
*{{cite journal | author=Rowell JF, Stanhope PE, Siliciano RF |title=Endocytosis of endogenously synthesized HIV-1 envelope protein. Mechanism and role in processing for association with class II MHC. |journal=J. Immunol. |volume=155 |issue= 1 |pages= 473-88 |year= 1995 |pmid= 7602119 |doi= }}
*{{cite journal | author=Carrington M, Harding A |title=Sequence analysis of two novel HLA-DMA alleles. |journal=Immunogenetics |volume=40 |issue= 2 |pages= 165 |year= 1994 |pmid= 8026867 |doi= }}
*{{cite journal | author=Radley E, Alderton RP, Kelly A, ''et al.'' |title=Genomic organization of HLA-DMA and HLA-DMB. Comparison of the gene organization of all six class II families in the human major histocompatibility complex. |journal=J. Biol. Chem. |volume=269 |issue= 29 |pages= 18834-8 |year= 1994 |pmid= 8034636 |doi= }}
*{{cite journal | author=Chen YH, Böck G, Vornhagen R, ''et al.'' |title=HIV-1 gp41 binding proteins and antibodies to gp41 could inhibit enhancement of human Raji cell MHC class I and II expression by gp41. |journal=Mol. Immunol. |volume=31 |issue= 13 |pages= 977-82 |year= 1994 |pmid= 8084338 |doi= }}
*{{cite journal | author=Fling SP, Arp B, Pious D |title=HLA-DMA and -DMB genes are both required for MHC class II/peptide complex formation in antigen-presenting cells. |journal=Nature |volume=368 |issue= 6471 |pages= 554-8 |year= 1994 |pmid= 8139690 |doi= 10.1038/368554a0 }}
*{{cite journal | author=Chirmule N, Wang XP, Hu R, ''et al.'' |title=Envelope glycoproteins of HIV-1 interfere with T-cell-dependent B cell differentiation: role of CD4-MHC class II interaction in the effector phase of T cell help. |journal=Cell. Immunol. |volume=155 |issue= 1 |pages= 169-82 |year= 1994 |pmid= 8168144 |doi= 10.1006/cimm.1994.1110 }}
*{{cite journal | author=Sanderson F, Powis SH, Kelly AP, Trowsdale J |title=Limited polymorphism in HLA-DM does not involve the peptide binding groove. |journal=Immunogenetics |volume=39 |issue= 1 |pages= 56-8 |year= 1993 |pmid= 8225438 |doi= }}
*{{cite journal | author=Callahan KM, Rowell JF, Soloski MJ, ''et al.'' |title=HIV-1 envelope protein is expressed on the surface of infected cells before its processing and presentation to class II-restricted T lymphocytes. |journal=J. Immunol. |volume=151 |issue= 6 |pages= 2928-42 |year= 1993 |pmid= 8376762 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HSP90AB1... {November 18, 2007 11:04:10 AM PST}
- SEARCH REDIRECT: Control Box Found: HSP90AB1 {November 18, 2007 11:04:45 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:04:47 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:04:47 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:04:47 AM PST}
- UPDATED: Updated protein page: HSP90AB1 {November 18, 2007 11:04:53 AM PST}
- INFO: Beginning work on ICAM2... {November 18, 2007 11:04:53 AM PST}
- SEARCH REDIRECT: Control Box Found: ICAM2 {November 18, 2007 11:05:22 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:05:23 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:05:23 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:05:23 AM PST}
- UPDATED: Updated protein page: ICAM2 {November 18, 2007 11:05:30 AM PST}
- INFO: Beginning work on IDUA... {November 18, 2007 11:05:30 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:05:58 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Iduronidase, alpha-L-
| HGNCid = 5391
| Symbol = IDUA
| AltSymbols =; IDA; MPS1
| OMIM = 252800
| ECnumber =
| Homologene = 170
| MGIid = 96418
| GeneAtlas_image1 = PBB_GE_IDUA_205059_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_IDUA_205057_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003940 |text = L-iduronidase activity}} {{GNF_GO|id=GO:0004553 |text = hydrolase activity, hydrolyzing O-glycosyl compounds}} {{GNF_GO|id=GO:0043169 |text = cation binding}}
| Component = {{GNF_GO|id=GO:0005764 |text = lysosome}}
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0005984 |text = disaccharide metabolic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0030203 |text = glycosaminoglycan metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3425
| Hs_Ensembl = ENSG00000127415
| Hs_RefseqProtein = NP_000194
| Hs_RefseqmRNA = NM_000203
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 970785
| Hs_GenLoc_end = 988316
| Hs_Uniprot = P35475
| Mm_EntrezGene = 15932
| Mm_Ensembl = ENSMUSG00000033540
| Mm_RefseqmRNA = NM_008325
| Mm_RefseqProtein = NP_032351
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 108909613
| Mm_GenLoc_end = 108924856
| Mm_Uniprot = Q3TDU4
}}
}}
'''Iduronidase, alpha-L-''', also known as '''IDUA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IDUA iduronidase, alpha-L-| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3425| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes an enzyme that hydrolyzes the teminal alpha-L-iduronic acid residues of two glycosaminoglycans, dermatan sulfate and heparan sulfate. This hydrolysis is required for the lysosomal degradation of these glycosaminoglycans. Mutations in this gene that result in enzymatic deficiency lead to the autosomal recessive disease Mucopolysaccharidosis Type I (MPS I).<ref name="entrez">{{cite web | title = Entrez Gene: IDUA iduronidase, alpha-L-| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3425| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Neufeld EF |title=Lysosomal storage diseases. |journal=Annu. Rev. Biochem. |volume=60 |issue= |pages= 257-80 |year= 1991 |pmid= 1883197 |doi= 10.1146/annurev.bi.60.070191.001353 }}
*{{cite journal | author=Scott HS, Bunge S, Gal A, ''et al.'' |title=Molecular genetics of mucopolysaccharidosis type I: diagnostic, clinical, and biological implications. |journal=Hum. Mutat. |volume=6 |issue= 4 |pages= 288-302 |year= 1996 |pmid= 8680403 |doi= 10.1002/humu.1380060403 }}
*{{cite journal | author=Scott HS, Litjens T, Nelson PV, ''et al.'' |title=alpha-L-iduronidase mutations (Q70X and P533R) associate with a severe Hurler phenotype. |journal=Hum. Mutat. |volume=1 |issue= 4 |pages= 333-9 |year= 1993 |pmid= 1301941 |doi= 10.1002/humu.1380010412 }}
*{{cite journal | author=Scott HS, Litjens T, Hopwood JJ, Morris CP |title=PCR detection of two RFLPs in exon I of the alpha-L-iduronidase (IDUA) gene. |journal=Hum. Genet. |volume=90 |issue= 3 |pages= 327 |year= 1993 |pmid= 1362562 |doi= }}
*{{cite journal | author=Scott HS, Guo XH, Hopwood JJ, Morris CP |title=Structure and sequence of the human alpha-L-iduronidase gene. |journal=Genomics |volume=13 |issue= 4 |pages= 1311-3 |year= 1992 |pmid= 1505961 |doi= }}
*{{cite journal | author=Ashton LJ, Brooks DA, McCourt PA, ''et al.'' |title=Immunoquantification and enzyme kinetics of alpha-L-iduronidase in cultured fibroblasts from normal controls and mucopolysaccharidosis type I patients. |journal=Am. J. Hum. Genet. |volume=50 |issue= 4 |pages= 787-94 |year= 1992 |pmid= 1550122 |doi= }}
*{{cite journal | author=Stoltzfus LJ, Sosa-Pineda B, Moskowitz SM, ''et al.'' |title=Cloning and characterization of cDNA encoding canine alpha-L-iduronidase. mRNA deficiency in mucopolysaccharidosis I dog. |journal=J. Biol. Chem. |volume=267 |issue= 10 |pages= 6570-5 |year= 1992 |pmid= 1551868 |doi= }}
*{{cite journal | author=MacDonald ME, Scott HS, Whaley WL, ''et al.'' |title=Huntington disease-linked locus D4S111 exposed as the alpha-L-iduronidase gene. |journal=Somat. Cell Mol. Genet. |volume=17 |issue= 4 |pages= 421-5 |year= 1991 |pmid= 1832239 |doi= }}
*{{cite journal | author=Scott HS, Anson DS, Orsborn AM, ''et al.'' |title=Human alpha-L-iduronidase: cDNA isolation and expression. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 21 |pages= 9695-9 |year= 1991 |pmid= 1946389 |doi= }}
*{{cite journal | author=Dlott B, d'Azzo A, Quon DV, Neufeld EF |title=Two mutations produce intron insertion in mRNA and elongated beta-subunit of human beta-hexosaminidase. |journal=J. Biol. Chem. |volume=265 |issue= 29 |pages= 17921-7 |year= 1990 |pmid= 2170400 |doi= }}
*{{cite journal | author=Scott HS, Ashton LJ, Eyre HJ, ''et al.'' |title=Chromosomal localization of the human alpha-L-iduronidase gene (IDUA) to 4p16.3. |journal=Am. J. Hum. Genet. |volume=47 |issue= 5 |pages= 802-7 |year= 1990 |pmid= 2220820 |doi= }}
*{{cite journal | author=Clements PR, Brooks DA, McCourt PA, Hopwood JJ |title=Immunopurification and characterization of human alpha-L-iduronidase with the use of monoclonal antibodies. |journal=Biochem. J. |volume=259 |issue= 1 |pages= 199-208 |year= 1989 |pmid= 2470345 |doi= }}
*{{cite journal | author=McKusick VA, Kaplan D, Wise D, ''et al.'' |title=The genetic mucopolysaccharidoses. |journal=Medicine (Baltimore) |volume=44 |issue= 6 |pages= 445-83 |year= 1966 |pmid= 4221470 |doi= }}
*{{cite journal | author=Schaap T, Bach G |title=Incidence of mucopolysaccharidoses in Israel: is Hunter disease a "Jewish disease"? |journal=Hum. Genet. |volume=56 |issue= 2 |pages= 221-3 |year= 1981 |pmid= 6821579 |doi= }}
*{{cite journal | author=Tieu PT, Bach G, Matynia A, ''et al.'' |title=Four novel mutations underlying mild or intermediate forms of alpha-L-iduronidase deficiency (MPS IS and MPS IH/S). |journal=Hum. Mutat. |volume=6 |issue= 1 |pages= 55-9 |year= 1995 |pmid= 7550232 |doi= 10.1002/humu.1380060111 }}
*{{cite journal | author=Bunge S, Kleijer WJ, Steglich C, ''et al.'' |title=Mucopolysaccharidosis type I: identification of 13 novel mutations of the alpha-L-iduronidase gene. |journal=Hum. Mutat. |volume=6 |issue= 1 |pages= 91-4 |year= 1995 |pmid= 7550242 |doi= 10.1002/humu.1380060119 }}
*{{cite journal | author=Bunge S, Kleijer WJ, Steglich C, ''et al.'' |title=Mucopolysaccharidosis type I: identification of 8 novel mutations and determination of the frequency of the two common alpha-L-iduronidase mutations (W402X and Q70X) among European patients. |journal=Hum. Mol. Genet. |volume=3 |issue= 6 |pages= 861-6 |year= 1994 |pmid= 7951228 |doi= }}
*{{cite journal | author=Clarke LA, Nelson PV, Warrington CL, ''et al.'' |title=Mutation analysis of 19 North American mucopolysaccharidosis type I patients: identification of two additional frequent mutations. |journal=Hum. Mutat. |volume=3 |issue= 3 |pages= 275-82 |year= 1994 |pmid= 8019563 |doi= 10.1002/humu.1380030316 }}
*{{cite journal | author=Scott HS, Litjens T, Nelson PV, ''et al.'' |title=Identification of mutations in the alpha-L-iduronidase gene (IDUA) that cause Hurler and Scheie syndromes. |journal=Am. J. Hum. Genet. |volume=53 |issue= 5 |pages= 973-86 |year= 1993 |pmid= 8213840 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LIFR... {November 18, 2007 11:05:58 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:07:08 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Leukemia inhibitory factor receptor alpha
| HGNCid = 6597
| Symbol = LIFR
| AltSymbols =; CD118; SJS2; STWS; SWS
| OMIM = 151443
| ECnumber =
| Homologene = 1735
| MGIid = 96788
| GeneAtlas_image1 = PBB_GE_LIFR_205876_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004923 |text = leukemia inhibitory factor receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3977
| Hs_Ensembl = ENSG00000113594
| Hs_RefseqProtein = NP_002301
| Hs_RefseqmRNA = NM_002310
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 38510823
| Hs_GenLoc_end = 38631253
| Hs_Uniprot = P42702
| Mm_EntrezGene = 16880
| Mm_Ensembl = ENSMUSG00000054263
| Mm_RefseqmRNA = NM_013584
| Mm_RefseqProtein = NP_038612
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 7101575
| Mm_GenLoc_end = 7138433
| Mm_Uniprot = O35672
}}
}}
'''Leukemia inhibitory factor receptor alpha''', also known as '''LIFR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LIFR leukemia inhibitory factor receptor alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3977| 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 leukemia inhibitory factor is a polyfunctional cytokine that affects the differentiation, survival, and proliferation of a wide variety of cells in the adult and the embryo. LIF action appears to be mediated through a high-affinity receptor complex composed of a low-affinity LIF binding chain (LIF receptor) and a high-affinity converter subunit, gp130. Both LIFR and gp130 are members of a family of cytokine receptors that includes components of the receptors for the majority of hematopoietic cytokines and for cytokines that affect other systems, including the ciliary neurotrophic factor, growth hormone and prolactin.<ref name="entrez">{{cite web | title = Entrez Gene: LIFR leukemia inhibitory factor receptor alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3977| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tomida M |title=Structural and functional studies on the leukemia inhibitory factor receptor (LIF-R): gene and soluble form of LIF-R, and cytoplasmic domain of LIF-R required for differentiation and growth arrest of myeloid leukemic cells. |journal=Leuk. Lymphoma |volume=37 |issue= 5-6 |pages= 517-25 |year= 2003 |pmid= 11042511 |doi= }}
*{{cite journal | author=Lass A, Weiser W, Munafo A, Loumaye E |title=Leukemia inhibitory factor in human reproduction. |journal=Fertil. Steril. |volume=76 |issue= 6 |pages= 1091-6 |year= 2002 |pmid= 11730732 |doi= }}
*{{cite journal | author=Gearing DP, Bruce AG |title=Oncostatin M binds the high-affinity leukemia inhibitory factor receptor. |journal=New Biol. |volume=4 |issue= 1 |pages= 61-5 |year= 1992 |pmid= 1536831 |doi= }}
*{{cite journal | author=Gearing DP, Comeau MR, Friend DJ, ''et al.'' |title=The IL-6 signal transducer, gp130: an oncostatin M receptor and affinity converter for the LIF receptor. |journal=Science |volume=255 |issue= 5050 |pages= 1434-7 |year= 1992 |pmid= 1542794 |doi= }}
*{{cite journal | author=Gearing DP, Thut CJ, VandeBos T, ''et al.'' |title=Leukemia inhibitory factor receptor is structurally related to the IL-6 signal transducer, gp130. |journal=EMBO J. |volume=10 |issue= 10 |pages= 2839-48 |year= 1991 |pmid= 1915266 |doi= }}
*{{cite journal | author=Boulton TG, Stahl N, Yancopoulos GD |title=Ciliary neurotrophic factor/leukemia inhibitory factor/interleukin 6/oncostatin M family of cytokines induces tyrosine phosphorylation of a common set of proteins overlapping those induced by other cytokines and growth factors. |journal=J. Biol. Chem. |volume=269 |issue= 15 |pages= 11648-55 |year= 1994 |pmid= 7512571 |doi= }}
*{{cite journal | author=Schiemann WP, Graves LM, Baumann H, ''et al.'' |title=Phosphorylation of the human leukemia inhibitory factor (LIF) receptor by mitogen-activated protein kinase and the regulation of LIF receptor function by heterologous receptor activation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 12 |pages= 5361-5 |year= 1995 |pmid= 7777512 |doi= }}
*{{cite journal | author=Gearing DP, Druck T, Huebner K, ''et al.'' |title=The leukemia inhibitory factor receptor (LIFR) gene is located within a cluster of cytokine receptor loci on mouse chromosome 15 and human chromosome 5p12-p13. |journal=Genomics |volume=18 |issue= 1 |pages= 148-50 |year= 1994 |pmid= 8276403 |doi= 10.1006/geno.1993.1441 }}
*{{cite journal | author=Sharkey AM, Dellow K, Blayney M, ''et al.'' |title=Stage-specific expression of cytokine and receptor messenger ribonucleic acids in human preimplantation embryos. |journal=Biol. Reprod. |volume=53 |issue= 4 |pages= 974-81 |year= 1996 |pmid= 8547494 |doi= }}
*{{cite journal | author=Kojima K, Kanzaki H, Iwai M, ''et al.'' |title=Expression of leukaemia inhibitory factor (LIF) receptor in human placenta: a possible role for LIF in the growth and differentiation of trophoblasts. |journal=Hum. Reprod. |volume=10 |issue= 7 |pages= 1907-11 |year= 1996 |pmid= 8583009 |doi= }}
*{{cite journal | author=Tomida M, Gotoh O |title=Structure of the gene encoding the human differentiation-stimulating factor/leukemia inhibitory factor receptor. |journal=J. Biochem. |volume=120 |issue= 1 |pages= 201-5 |year= 1997 |pmid= 8864865 |doi= }}
*{{cite journal | author=Wang Z, Melmed S |title=Identification of an upstream enhancer within a functional promoter of the human leukemia inhibitory factor receptor gene and its alternative promoter usage. |journal=J. Biol. Chem. |volume=272 |issue= 44 |pages= 27957-65 |year= 1997 |pmid= 9346946 |doi= }}
*{{cite journal | author=Tanaka M, Hara T, Copeland NG, ''et al.'' |title=Reconstitution of the functional mouse oncostatin M (OSM) receptor: molecular cloning of the mouse OSM receptor beta subunit. |journal=Blood |volume=93 |issue= 3 |pages= 804-15 |year= 1999 |pmid= 9920829 |doi= }}
*{{cite journal | author=Knight DA, Lydell CP, Zhou D, ''et al.'' |title=Leukemia inhibitory factor (LIF) and LIF receptor in human lung. Distribution and regulation of LIF release. |journal=Am. J. Respir. Cell Mol. Biol. |volume=20 |issue= 4 |pages= 834-41 |year= 1999 |pmid= 10101017 |doi= }}
*{{cite journal | author=Kakizawa T, Miyamoto T, Ichikawa K, ''et al.'' |title=Functional interaction between Oct-1 and retinoid X receptor. |journal=J. Biol. Chem. |volume=274 |issue= 27 |pages= 19103-8 |year= 1999 |pmid= 10383413 |doi= }}
*{{cite journal | author=Bartoe JL, Nathanson NM |title=Differential regulation of leukemia inhibitory factor-stimulated neuronal gene expression by protein phosphatases SHP-1 and SHP-2 through mitogen-activated protein kinase-dependent and -independent pathways. |journal=J. Neurochem. |volume=74 |issue= 5 |pages= 2021-32 |year= 2000 |pmid= 10800945 |doi= }}
*{{cite journal | author=Bamberger AM, Schulte HM, Wullbrand A, ''et al.'' |title=Expression of leukemia inhibitory factor (LIF) and LIF receptor (LIF-R) in the human adrenal cortex: implications for steroidogenesis. |journal=Mol. Cell. Endocrinol. |volume=162 |issue= 1-2 |pages= 145-9 |year= 2000 |pmid= 10854707 |doi= }}
*{{cite journal | author=Blanchard F, Duplomb L, Wang Y, ''et al.'' |title=Stimulation of leukemia inhibitory factor receptor degradation by extracellular signal-regulated kinase. |journal=J. Biol. Chem. |volume=275 |issue= 37 |pages= 28793-801 |year= 2000 |pmid= 10858440 |doi= 10.1074/jbc.M003986200 }}
*{{cite journal | author=Plun-Favreau H, Elson G, Chabbert M, ''et al.'' |title=The ciliary neurotrophic factor receptor alpha component induces the secretion of and is required for functional responses to cardiotrophin-like cytokine. |journal=EMBO J. |volume=20 |issue= 7 |pages= 1692-703 |year= 2001 |pmid= 11285233 |doi= 10.1093/emboj/20.7.1692 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MAP2K7... {November 18, 2007 11:11:17 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:11:48 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Mitogen-activated protein kinase kinase 7
| HGNCid = 6847
| Symbol = MAP2K7
| AltSymbols =; Jnkk2; MAPKK7; MKK7; PRKMK7
| OMIM = 603014
| ECnumber =
| Homologene = 56548
| MGIid = 1346871
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004708 |text = MAP kinase kinase activity}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0019901 |text = protein kinase binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006950 |text = response to stress}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0051403 |text = stress-activated MAPK cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5609
| Hs_Ensembl =
| Hs_RefseqProtein = NP_660186
| Hs_RefseqmRNA = NM_145185
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 26400
| Mm_Ensembl = ENSMUSG00000002948
| Mm_RefseqmRNA = NM_001042557
| Mm_RefseqProtein = NP_001036022
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 4238828
| Mm_GenLoc_end = 4251420
| Mm_Uniprot = Q8CE90
}}
}}
'''Mitogen-activated protein kinase kinase 7''', also known as '''MAP2K7''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MAP2K7 mitogen-activated protein kinase kinase 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5609| 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 dual specificity protein kinase that belongs to the MAP kinase kinase family. This kinase specifically activates MAPK8/JNK1 and MAPK9/JNK2, and this kinase itself is phosphorylated and activated by MAP kinase kinase kinases including MAP3K1/MEKK1, MAP3K2/MEKK2,MAP3K3/MEKK5, and MAP4K2/GCK. This kinase is involved in the signal transduction mediating the cell responses to proinflammatory cytokines, and environmental stresses. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found, but only one transcript variant has been supported and defined.<ref name="entrez">{{cite web | title = Entrez Gene: MAP2K7 mitogen-activated protein kinase kinase 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5609| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tournier C, Whitmarsh AJ, Cavanagh J, ''et al.'' |title=Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 14 |pages= 7337-42 |year= 1997 |pmid= 9207092 |doi= }}
*{{cite journal | author=Lu X, Nemoto S, Lin A |title=Identification of c-Jun NH2-terminal protein kinase (JNK)-activating kinase 2 as an activator of JNK but not p38. |journal=J. Biol. Chem. |volume=272 |issue= 40 |pages= 24751-4 |year= 1997 |pmid= 9312068 |doi= }}
*{{cite journal | author=Wu Z, Wu J, Jacinto E, Karin M |title=Molecular cloning and characterization of human JNKK2, a novel Jun NH2-terminal kinase-specific kinase. |journal=Mol. Cell. Biol. |volume=17 |issue= 12 |pages= 7407-16 |year= 1997 |pmid= 9372971 |doi= }}
*{{cite journal | author=Wang Y, Su B, Sah VP, ''et al.'' |title=Cardiac hypertrophy induced by mitogen-activated protein kinase kinase 7, a specific activator for c-Jun NH2-terminal kinase in ventricular muscle cells. |journal=J. Biol. Chem. |volume=273 |issue= 10 |pages= 5423-6 |year= 1998 |pmid= 9488659 |doi= }}
*{{cite journal | author=Foltz IN, Gerl RE, Wieler JS, ''et al.'' |title=Human mitogen-activated protein kinase kinase 7 (MKK7) is a highly conserved c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK) activated by environmental stresses and physiological stimuli. |journal=J. Biol. Chem. |volume=273 |issue= 15 |pages= 9344-51 |year= 1998 |pmid= 9535930 |doi= }}
*{{cite journal | author=Yang J, New L, Jiang Y, ''et al.'' |title=Molecular cloning and characterization of a human protein kinase that specifically activates c-Jun N-terminal kinase. |journal=Gene |volume=212 |issue= 1 |pages= 95-102 |year= 1998 |pmid= 9661668 |doi= }}
*{{cite journal | author=Merritt SE, Mata M, Nihalani D, ''et al.'' |title=The mixed lineage kinase DLK utilizes MKK7 and not MKK4 as substrate. |journal=J. Biol. Chem. |volume=274 |issue= 15 |pages= 10195-202 |year= 1999 |pmid= 10187804 |doi= }}
*{{cite journal | author=Deacon K, Blank JL |title=MEK kinase 3 directly activates MKK6 and MKK7, specific activators of the p38 and c-Jun NH2-terminal kinases. |journal=J. Biol. Chem. |volume=274 |issue= 23 |pages= 16604-10 |year= 1999 |pmid= 10347227 |doi= }}
*{{cite journal | author=Yasuda J, Whitmarsh AJ, Cavanagh J, ''et al.'' |title=The JIP group of mitogen-activated protein kinase scaffold proteins. |journal=Mol. Cell. Biol. |volume=19 |issue= 10 |pages= 7245-54 |year= 2000 |pmid= 10490659 |doi= }}
*{{cite journal | author=Kelkar N, Gupta S, Dickens M, Davis RJ |title=Interaction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3. |journal=Mol. Cell. Biol. |volume=20 |issue= 3 |pages= 1030-43 |year= 2000 |pmid= 10629060 |doi= }}
*{{cite journal | author=Cheng J, Yang J, Xia Y, ''et al.'' |title=Synergistic interaction of MEK kinase 2, c-Jun N-terminal kinase (JNK) kinase 2, and JNK1 results in efficient and specific JNK1 activation. |journal=Mol. Cell. Biol. |volume=20 |issue= 7 |pages= 2334-42 |year= 2000 |pmid= 10713157 |doi= }}
*{{cite journal | author=Negri S, Oberson A, Steinmann M, ''et al.'' |title=cDNA cloning and mapping of a novel islet-brain/JNK-interacting protein. |journal=Genomics |volume=64 |issue= 3 |pages= 324-30 |year= 2000 |pmid= 10756100 |doi= 10.1006/geno.2000.6129 }}
*{{cite journal | author=Karandikar M, Xu S, Cobb MH |title=MEKK1 binds raf-1 and the ERK2 cascade components. |journal=J. Biol. Chem. |volume=275 |issue= 51 |pages= 40120-7 |year= 2001 |pmid= 10969079 |doi= 10.1074/jbc.M005926200 }}
*{{cite journal | author=Fleming Y, Armstrong CG, Morrice N, ''et al.'' |title=Synergistic activation of stress-activated protein kinase 1/c-Jun N-terminal kinase (SAPK1/JNK) isoforms by mitogen-activated protein kinase kinase 4 (MKK4) and MKK7. |journal=Biochem. J. |volume=352 Pt 1 |issue= |pages= 145-54 |year= 2001 |pmid= 11062067 |doi= }}
*{{cite journal | author=Vitale G, Bernardi L, Napolitani G, ''et al.'' |title=Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor. |journal=Biochem. J. |volume=352 Pt 3 |issue= |pages= 739-45 |year= 2001 |pmid= 11104681 |doi= }}
*{{cite journal | author=Chayama K, Papst PJ, Garrington TP, ''et al.'' |title=Role of MEKK2-MEK5 in the regulation of TNF-alpha gene expression and MEKK2-MKK7 in the activation of c-Jun N-terminal kinase in mast cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 8 |pages= 4599-604 |year= 2001 |pmid= 11274363 |doi= 10.1073/pnas.081021898 }}
*{{cite journal | author=Acierno JS, Kennedy JC, Falardeau JL, ''et al.'' |title=A physical and transcript map of the MCOLN1 gene region on human chromosome 19p13.3-p13.2. |journal=Genomics |volume=73 |issue= 2 |pages= 203-10 |year= 2001 |pmid= 11318610 |doi= 10.1006/geno.2001.6526 }}
*{{cite journal | author=Tournier C, Dong C, Turner TK, ''et al.'' |title=MKK7 is an essential component of the JNK signal transduction pathway activated by proinflammatory cytokines. |journal=Genes Dev. |volume=15 |issue= 11 |pages= 1419-26 |year= 2001 |pmid= 11390361 |doi= 10.1101/gad.888501 }}
*{{cite journal | author=Gross EA, Callow MG, Waldbaum L, ''et al.'' |title=MRK, a mixed lineage kinase-related molecule that plays a role in gamma-radiation-induced cell cycle arrest. |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 13873-82 |year= 2002 |pmid= 11836244 |doi= 10.1074/jbc.M111994200 }}
*{{cite journal | author=Kawaguchi M, Onuchic LF, Huang SK |title=Activation of extracellular signal-regulated kinase (ERK)1/2, but not p38 and c-Jun N-terminal kinase, is involved in signaling of a novel cytokine, ML-1. |journal=J. Biol. Chem. |volume=277 |issue= 18 |pages= 15229-32 |year= 2002 |pmid= 11891214 |doi= 10.1074/jbc.C100641200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MCAM... {November 18, 2007 11:07:08 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:07:43 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| 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 = Melanoma cell adhesion molecule
| HGNCid = 6934
| Symbol = MCAM
| AltSymbols =; CD146; MUC18
| OMIM = 155735
| ECnumber =
| Homologene = 4742
| MGIid = 1933966
| GeneAtlas_image1 = PBB_GE_MCAM_211340_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_MCAM_209086_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_MCAM_209087_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0009653 |text = anatomical structure morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4162
| Hs_Ensembl = ENSG00000076706
| Hs_RefseqProtein = NP_006491
| Hs_RefseqmRNA = NM_006500
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 118684444
| Hs_GenLoc_end = 118693050
| Hs_Uniprot = P43121
| Mm_EntrezGene = 84004
| Mm_Ensembl = ENSMUSG00000032135
| Mm_RefseqmRNA = NM_023061
| Mm_RefseqProtein = NP_075548
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 43885666
| Mm_GenLoc_end = 43893719
| Mm_Uniprot = Q8R2Y2
}}
}}
'''Melanoma cell adhesion molecule''', also known as '''MCAM''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MCAM melanoma cell adhesion molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4162| 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=Johnson JP, Rothbächer U, Sers C |title=The progression associated antigen MUC18: a unique member of the immunoglobulin supergene family. |journal=Melanoma Res. |volume=3 |issue= 5 |pages= 337-40 |year= 1994 |pmid= 8292890 |doi= }}
*{{cite journal | author=Shih IM |title=The role of CD146 (Mel-CAM) in biology and pathology. |journal=J. Pathol. |volume=189 |issue= 1 |pages= 4-11 |year= 2000 |pmid= 10451481 |doi= 10.1002/(SICI)1096-9896(199909)189:1<4::AID-PATH332>3.0.CO;2-P }}
*{{cite journal | author=McGary EC, Lev DC, Bar-Eli M |title=Cellular adhesion pathways and metastatic potential of human melanoma. |journal=Cancer Biol. Ther. |volume=1 |issue= 5 |pages= 459-65 |year= 2003 |pmid= 12496470 |doi= }}
*{{cite journal | author=Lehmann JM, Riethmüller G, Johnson JP |title=MUC18, a marker of tumor progression in human melanoma, shows sequence similarity to the neural cell adhesion molecules of the immunoglobulin superfamily. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 24 |pages= 9891-5 |year= 1990 |pmid= 2602381 |doi= }}
*{{cite journal | author=Shih IM, Elder DE, Speicher D, ''et al.'' |title=Isolation and functional characterization of the A32 melanoma-associated antigen. |journal=Cancer Res. |volume=54 |issue= 9 |pages= 2514-20 |year= 1994 |pmid= 8162602 |doi= }}
*{{cite journal | author=Sers C, Kirsch K, Rothbächer U, ''et al.'' |title=Genomic organization of the melanoma-associated glycoprotein MUC18: implications for the evolution of the immunoglobulin domains. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 18 |pages= 8514-8 |year= 1993 |pmid= 8378324 |doi= }}
*{{cite journal | author=Bardin N, Francès V, Lesaule G, ''et al.'' |title=Identification of the S-Endo 1 endothelial-associated antigen. |journal=Biochem. Biophys. Res. Commun. |volume=218 |issue= 1 |pages= 210-6 |year= 1996 |pmid= 8573133 |doi= 10.1006/bbrc.1996.0037 }}
*{{cite journal | author=Pickl WF, Majdic O, Fischer GF, ''et al.'' |title=MUC18/MCAM (CD146), an activation antigen of human T lymphocytes. |journal=J. Immunol. |volume=158 |issue= 5 |pages= 2107-15 |year= 1997 |pmid= 9036955 |doi= }}
*{{cite journal | author=Bardin N, Francès V, Combes V, ''et al.'' |title=CD146: biosynthesis and production of a soluble form in human cultured endothelial cells. |journal=FEBS Lett. |volume=421 |issue= 1 |pages= 12-4 |year= 1998 |pmid= 9462829 |doi= }}
*{{cite journal | author=Schwarz MJ, Müller N, Körschenhausen D, ''et al.'' |title=Melanoma-associated adhesion molecule MUC18/MCAM (CD146) and transcriptional regulator mader in normal human CNS. |journal=Neuroimmunomodulation |volume=5 |issue= 5 |pages= 270-6 |year= 1998 |pmid= 9730695 |doi= }}
*{{cite journal | author=Anfosso F, Bardin N, Francès V, ''et al.'' |title=Activation of human endothelial cells via S-endo-1 antigen (CD146) stimulates the tyrosine phosphorylation of focal adhesion kinase p125(FAK). |journal=J. Biol. Chem. |volume=273 |issue= 41 |pages= 26852-6 |year= 1998 |pmid= 9756930 |doi= }}
*{{cite journal | author=Neidhart M, Wehrli R, Brühlmann P, ''et al.'' |title=Synovial fluid CD146 (MUC18), a marker for synovial membrane angiogenesis in rheumatoid arthritis. |journal=Arthritis Rheum. |volume=42 |issue= 4 |pages= 622-30 |year= 1999 |pmid= 10211875 |doi= 10.1002/1529-0131(199904)42:4<622::AID-ANR4>3.0.CO;2-Y }}
*{{cite journal | author=Taşman F, Dağdeviren A, Kendir B, ''et al.'' |title=Endothelial cell adhesion molecules in human dental pulp: a comparative immunohistochemical study on chronic periodontitis. |journal=Journal of endodontics |volume=25 |issue= 10 |pages= 664-7 |year= 2000 |pmid= 10687524 |doi= }}
*{{cite journal | author=Kuske MD, Johnson JP |title=Assignment of the human melanoma cell adhesion molecule gene (MCAM) to chromosome 11 band q23.3 by radiation hybrid mapping. |journal=Cytogenet. Cell Genet. |volume=87 |issue= 3-4 |pages= 258 |year= 2000 |pmid= 10702685 |doi= }}
*{{cite journal | author=Seftalioğlu A, Karakoç L |title=Expression of CD146 adhesion molecules (MUC18 or MCAM) in the thymic microenvironment. |journal=Acta Histochem. |volume=102 |issue= 1 |pages= 69-83 |year= 2000 |pmid= 10726166 |doi= 10.1078/0065-1281-00544 }}
*{{cite journal | author=Suzuki Y, Ishihara D, Sasaki M, ''et al.'' |title=Statistical analysis of the 5' untranslated region of human mRNA using "Oligo-Capped" cDNA libraries. |journal=Genomics |volume=64 |issue= 3 |pages= 286-97 |year= 2000 |pmid= 10756096 |doi= 10.1006/geno.2000.6076 }}
*{{cite journal | author=Anfosso F, Bardin N, Vivier E, ''et al.'' |title=Outside-in signaling pathway linked to CD146 engagement in human endothelial cells. |journal=J. Biol. Chem. |volume=276 |issue= 2 |pages= 1564-9 |year= 2001 |pmid= 11036077 |doi= 10.1074/jbc.M007065200 }}
*{{cite journal | author=Wu GJ, Varma VA, Wu MW, ''et al.'' |title=Expression of a human cell adhesion molecule, MUC18, in prostate cancer cell lines and tissues. |journal=Prostate |volume=48 |issue= 4 |pages= 305-15 |year= 2001 |pmid= 11536311 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NCF4... {November 18, 2007 11:08:20 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:08:59 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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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_NCF4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1h6h.
| PDB = {{PDB2|1h6h}}, {{PDB2|1oey}}, {{PDB2|1w6x}}, {{PDB2|1w70}}, {{PDB2|1z9q}}, {{PDB2|2dyb}}
| Name = Neutrophil cytosolic factor 4, 40kDa
| HGNCid = 7662
| Symbol = NCF4
| AltSymbols =; MGC3810; NCF; P40PHOX; SH3PXD4
| OMIM = 601488
| ECnumber =
| Homologene = 525
| MGIid = 109186
| GeneAtlas_image1 = PBB_GE_NCF4_207677_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_NCF4_205147_x_at_tn.png
| Function = {{GNF_GO|id=GO:0035091 |text = phosphoinositide binding}} {{GNF_GO|id=GO:0046983 |text = protein dimerization activity}}
| Component = {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0043020 |text = NADPH oxidase complex}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007154 |text = cell communication}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4689
| Hs_Ensembl = ENSG00000100365
| Hs_RefseqProtein = NP_000622
| Hs_RefseqmRNA = NM_000631
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 35586976
| Hs_GenLoc_end = 35604003
| Hs_Uniprot = Q15080
| Mm_EntrezGene = 17972
| Mm_Ensembl = ENSMUSG00000071715
| Mm_RefseqmRNA = NM_008677
| Mm_RefseqProtein = NP_032703
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 78072089
| Mm_GenLoc_end = 78089829
| Mm_Uniprot = Q3TBC6
}}
}}
'''Neutrophil cytosolic factor 4, 40kDa''', also known as '''NCF4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NCF4 neutrophil cytosolic factor 4, 40kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4689| 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 cytosolic regulatory component of the superoxide-producing phagocyte NADPH-oxidase, a multicomponent enzyme system important for host defense. This protein is preferentially expressed in cells of myeloid lineage. It interacts primarily with neutrophil cytosolic factor 2 (NCF2/p67-phox) to form a complex with neutrophil cytosolic factor 1 (NCF1/p47-phox), which further interacts with the small G protein RAC1 and translocates to the membrane upon cell stimulation. This complex then activates flavocytochrome b, the membrane-integrated catalytic core of the enzyme system. The PX domain of this protein can bind phospholipid products of the PI(3) kinase, which suggests its role in PI(3) kinase-mediated signaling events. The phosphorylation of this protein was found to negatively regulate the enzyme activity. Alternatively spliced transcript variants encoding distinct isoforms have been observed.<ref name="entrez">{{cite web | title = Entrez Gene: NCF4 neutrophil cytosolic factor 4, 40kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4689| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Matute JD, Arias AA, Dinauer MC, Patiño PJ |title=p40phox: the last NADPH oxidase subunit. |journal=Blood Cells Mol. Dis. |volume=35 |issue= 2 |pages= 291-302 |year= 2006 |pmid= 16102984 |doi= 10.1016/j.bcmd.2005.06.010 }}
*{{cite journal | author=Jones JH |title=The essence of operating room nursing. Paramedical personnel. |journal=The Australasian nurses journal |volume=7 |issue= 1 |pages= 44-5, 63-4 |year= 1977 |pmid= 243433 |doi= }}
*{{cite journal | author=Leto TL, Adams AG, de Mendez I |title=Assembly of the phagocyte NADPH oxidase: binding of Src homology 3 domains to proline-rich targets. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 22 |pages= 10650-4 |year= 1994 |pmid= 7938008 |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=Tsunawaki S, Mizunari H, Nagata M, ''et al.'' |title=A novel cytosolic component, p40phox, of respiratory burst oxidase associates with p67phox and is absent in patients with chronic granulomatous disease who lack p67phox. |journal=Biochem. Biophys. Res. Commun. |volume=199 |issue= 3 |pages= 1378-87 |year= 1994 |pmid= 8147882 |doi= 10.1006/bbrc.1994.1383 }}
*{{cite journal | author=Wientjes FB, Hsuan JJ, Totty NF, Segal AW |title=p40phox, a third cytosolic component of the activation complex of the NADPH oxidase to contain src homology 3 domains. |journal=Biochem. J. |volume=296 ( Pt 3) |issue= |pages= 557-61 |year= 1994 |pmid= 8280052 |doi= }}
*{{cite journal | author=Dusi S, Donini M, Rossi F |title=Mechanisms of NADPH oxidase activation: translocation of p40phox, Rac1 and Rac2 from the cytosol to the membranes in human neutrophils lacking p47phox or p67phox. |journal=Biochem. J. |volume=314 ( Pt 2) |issue= |pages= 409-12 |year= 1996 |pmid= 8670049 |doi= }}
*{{cite journal | author=Zhan S, Vazquez N, Zhan S, ''et al.'' |title=Genomic structure, chromosomal localization, start of transcription, and tissue expression of the human p40-phox, a new component of the nicotinamide adenine dinucleotide phosphate-oxidase complex. |journal=Blood |volume=88 |issue= 7 |pages= 2714-21 |year= 1996 |pmid= 8839867 |doi= }}
*{{cite journal | author=Someya A, Nagaoka I, Nunoi H, Yamashita T |title=Translocation of guinea pig p40-phox during activation of NADPH oxidase. |journal=Biochim. Biophys. Acta |volume=1277 |issue= 3 |pages= 217-25 |year= 1997 |pmid= 8982388 |doi= }}
*{{cite journal | author=Sathyamoorthy M, de Mendez I, Adams AG, Leto TL |title=p40(phox) down-regulates NADPH oxidase activity through interactions with its SH3 domain. |journal=J. Biol. Chem. |volume=272 |issue= 14 |pages= 9141-6 |year= 1997 |pmid= 9083043 |doi= }}
*{{cite journal | author=Grogan A, Reeves E, Keep N, ''et al.'' |title=Cytosolic phox proteins interact with and regulate the assembly of coronin in neutrophils. |journal=J. Cell. Sci. |volume=110 ( Pt 24) |issue= |pages= 3071-81 |year= 1998 |pmid= 9365277 |doi= }}
*{{cite journal | author=Fuchs A, Bouin AP, Rabilloud T, Vignais PV |title=The 40-kDa component of the phagocyte NADPH oxidase (p40phox) is phosphorylated during activation in differentiated HL60 cells. |journal=Eur. J. Biochem. |volume=249 |issue= 2 |pages= 531-9 |year= 1997 |pmid= 9370364 |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=Bouin AP, Grandvaux N, Vignais PV, Fuchs A |title=p40(phox) is phosphorylated on threonine 154 and serine 315 during activation of the phagocyte NADPH oxidase. Implication of a protein kinase c-type kinase in the phosphorylation process. |journal=J. Biol. Chem. |volume=273 |issue= 46 |pages= 30097-103 |year= 1998 |pmid= 9804763 |doi= }}
*{{cite journal | author=Grandvaux N, Grizot S, Vignais PV, Dagher MC |title=The Ku70 autoantigen interacts with p40phox in B lymphocytes. |journal=J. Cell. Sci. |volume=112 ( Pt 4) |issue= |pages= 503-13 |year= 1999 |pmid= 9914162 |doi= }}
*{{cite journal | author=Nishiyama A, Ohno T, Iwata S, ''et al.'' |title=Demonstration of the interaction of thioredoxin with p40phox, a phagocyte oxidase component, using a yeast two-hybrid system. |journal=Immunol. Lett. |volume=68 |issue= 1 |pages= 155-9 |year= 1999 |pmid= 10397171 |doi= }}
*{{cite journal | author=Hasebe T, Someya A, Nagaoka I |title=Identification of a splice variant mRNA of p40phox, an NADPH oxidase component of phagocytes. |journal=FEBS Lett. |volume=455 |issue= 3 |pages= 257-61 |year= 1999 |pmid= 10437784 |doi= }}
*{{cite journal | author=Dunham I, Shimizu N, Roe BA, ''et al.'' |title=The DNA sequence of human chromosome 22. |journal=Nature |volume=402 |issue= 6761 |pages= 489-95 |year= 1999 |pmid= 10591208 |doi= 10.1038/990031 }}
*{{cite journal | author=Vergnaud S, Paclet MH, El Benna J, ''et al.'' |title=Complementation of NADPH oxidase in p67-phox-deficient CGD patients p67-phox/p40-phox interaction. |journal=Eur. J. Biochem. |volume=267 |issue= 4 |pages= 1059-67 |year= 2000 |pmid= 10672014 |doi= }}
*{{cite journal | author=Grizot S, Grandvaux N, Fieschi F, ''et al.'' |title=Small angle neutron scattering and gel filtration analyses of neutrophil NADPH oxidase cytosolic factors highlight the role of the C-terminal end of p47phox in the association with p40phox. |journal=Biochemistry |volume=40 |issue= 10 |pages= 3127-33 |year= 2001 |pmid= 11258927 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ND3... {November 18, 2007 11:07:43 AM PST}
- SEARCH REDIRECT: Control Box Found: ND3 {November 18, 2007 11:08:10 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:08:13 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:08:13 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:08:13 AM PST}
- UPDATED: Updated protein page: ND3 {November 18, 2007 11:08:20 AM PST}
- INFO: Beginning work on NOTCH2... {November 18, 2007 11:08:59 AM PST}
- SEARCH REDIRECT: Control Box Found: NOTCH2 {November 18, 2007 11:09:40 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:09:41 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:09:41 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:09:41 AM PST}
- UPDATED: Updated protein page: NOTCH2 {November 18, 2007 11:09:48 AM PST}
- INFO: Beginning work on PAX5... {November 18, 2007 11:10:43 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:11:17 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PAX5_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1k78.
| PDB = {{PDB2|1k78}}, {{PDB2|1mdm}}
| Name = Paired box gene 5 (B-cell lineage specific activator)
| HGNCid = 8619
| Symbol = PAX5
| AltSymbols =; BSAP
| OMIM = 167414
| ECnumber =
| Homologene = 56419
| MGIid = 97489
| GeneAtlas_image1 = PBB_GE_PAX5_206802_at_tn.png
| GeneAtlas_image2 = PBB_GE_PAX5_221969_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006959 |text = humoral immune response}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007283 |text = spermatogenesis}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5079
| Hs_Ensembl = ENSG00000196092
| Hs_RefseqProtein = NP_057953
| Hs_RefseqmRNA = NM_016734
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 36823272
| Hs_GenLoc_end = 37024476
| Hs_Uniprot = Q02548
| Mm_EntrezGene = 18507
| Mm_Ensembl = ENSMUSG00000014030
| Mm_RefseqmRNA = NM_008782
| Mm_RefseqProtein = NP_032808
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 44552606
| Mm_GenLoc_end = 44731762
| Mm_Uniprot = Q02650
}}
}}
'''Paired box gene 5 (B-cell lineage specific activator)''', also known as '''PAX5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PAX5 paired box gene 5 (B-cell lineage specific activator)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5079| 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 PAX5 gene is a member of the paired box (PAX) family of transcription factors. The central feature of this gene family is a novel, highly conserved DNA-binding motif, known as the paired box. The PAX proteins are important regulators in early development, and alterations in the expression of their genes are thought to contribute to neoplastic transformation. The PAX5 gene encodes the B-cell lineage specific activator protein (BSAP) that is expressed at early, but not late stages of B-cell differentiation. Its expression has also been detected in developing CNS and testis, therefore, PAX5 gene product may not only play an important role in B-cell differentiation, but also in neural development and spermatogenesis. The PAX5 gene is located in chromosome 9p13 region, which is involved in t(9;14)(p13;q32) translocations recurring in small lymphocytic lymphomas of the plasmacytoid subtype, and in derived large-cell lymphomas. This translocation brings the potent E-mu enhancer of the IgH gene into close proximity of the PAX5 promoters, suggesting that the deregulation of PAX5 gene transcription contributes to the pathogenesis of these lymphomas. A transcript variant arising as a consequence of alternative promoter usage, and containing a different coding exon 1(B), has been described, however, its full-length nature is not known.<ref name="entrez">{{cite web | title = Entrez Gene: PAX5 paired box gene 5 (B-cell lineage specific activator)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5079| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hagman J, Wheat W, Fitzsimmons D, ''et al.'' |title=Pax-5/BSAP: regulator of specific gene expression and differentiation in B lymphocytes. |journal=Curr. Top. Microbiol. Immunol. |volume=245 |issue= 1 |pages= 169-94 |year= 1999 |pmid= 10533313 |doi= }}
*{{cite journal | author=Calame KL, Lin KI, Tunyaplin C |title=Regulatory mechanisms that determine the development and function of plasma cells. |journal=Annu. Rev. Immunol. |volume=21 |issue= |pages= 205-30 |year= 2003 |pmid= 12524387 |doi= 10.1146/annurev.immunol.21.120601.141138 }}
*{{cite journal | author=Carotta S, Holmes ML, Pridans C, Nutt SL |title=Pax5 maintains cellular identity by repressing gene expression throughout B cell differentiation. |journal=Cell Cycle |volume=5 |issue= 21 |pages= 2452-6 |year= 2007 |pmid= 17102626 |doi= }}
*{{cite journal | author=Adams B, Dörfler P, Aguzzi A, ''et al.'' |title=Pax-5 encodes the transcription factor BSAP and is expressed in B lymphocytes, the developing CNS, and adult testis. |journal=Genes Dev. |volume=6 |issue= 9 |pages= 1589-607 |year= 1992 |pmid= 1516825 |doi= }}
*{{cite journal | author=Stapleton P, Weith A, Urbánek P, ''et al.'' |title=Chromosomal localization of seven PAX genes and cloning of a novel family member, PAX-9. |journal=Nat. Genet. |volume=3 |issue= 4 |pages= 292-8 |year= 1995 |pmid= 7981748 |doi= 10.1038/ng0493-292 }}
*{{cite journal | author=Pilz AJ, Povey S, Gruss P, Abbott CM |title=Mapping of the human homologs of the murine paired-box-containing genes. |journal=Mamm. Genome |volume=4 |issue= 2 |pages= 78-82 |year= 1993 |pmid= 8431641 |doi= }}
*{{cite journal | author=Busslinger M, Klix N, Pfeffer P, ''et al.'' |title=Deregulation of PAX-5 by translocation of the Emu enhancer of the IgH locus adjacent to two alternative PAX-5 promoters in a diffuse large-cell lymphoma. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 12 |pages= 6129-34 |year= 1996 |pmid= 8650231 |doi= }}
*{{cite journal | author=Iida S, Rao PH, Nallasivam P, ''et al.'' |title=The t(9;14)(p13;q32) chromosomal translocation associated with lymphoplasmacytoid lymphoma involves the PAX-5 gene. |journal=Blood |volume=88 |issue= 11 |pages= 4110-7 |year= 1996 |pmid= 8943844 |doi= }}
*{{cite journal | author=Kaneko H, Ariyasu T, Inoue R, ''et al.'' |title=Expression of Pax5 gene in human haematopoietic cells and tissues: comparison with immunodeficient donors. |journal=Clin. Exp. Immunol. |volume=111 |issue= 2 |pages= 339-44 |year= 1998 |pmid= 9486401 |doi= }}
*{{cite journal | author=Verkoczy LK, Berinstein NL |title=Isolation of genes negatively or positively co-expressed with human recombination activating gene 1 (RAG1) by differential display PCR (DD RT-PCR). |journal=Nucleic Acids Res. |volume=26 |issue= 19 |pages= 4497-507 |year= 1998 |pmid= 9742255 |doi= }}
*{{cite journal | author=Wheat W, Fitzsimmons D, Lennox H, ''et al.'' |title=The highly conserved beta-hairpin of the paired DNA-binding domain is required for assembly of Pax-Ets ternary complexes. |journal=Mol. Cell. Biol. |volume=19 |issue= 3 |pages= 2231-41 |year= 1999 |pmid= 10022910 |doi= }}
*{{cite journal | author=Eberhard D, Busslinger M |title=The partial homeodomain of the transcription factor Pax-5 (BSAP) is an interaction motif for the retinoblastoma and TATA-binding proteins. |journal=Cancer Res. |volume=59 |issue= 7 Suppl |pages= 1716s-1724s; discussion 1724s-1725s |year= 1999 |pmid= 10197586 |doi= }}
*{{cite journal | author=Libermann TA, Pan Z, Akbarali Y, ''et al.'' |title=AML1 (CBFalpha2) cooperates with B cell-specific activating protein (BSAP/PAX5) in activation of the B cell-specific BLK gene promoter. |journal=J. Biol. Chem. |volume=274 |issue= 35 |pages= 24671-6 |year= 1999 |pmid= 10455134 |doi= }}
*{{cite journal | author=Nutt SL, Heavey B, Rolink AG, Busslinger M |title=Commitment to the B-lymphoid lineage depends on the transcription factor Pax5. |journal=Nature |volume=401 |issue= 6753 |pages= 556-62 |year= 1999 |pmid= 10524622 |doi= 10.1038/44076 }}
*{{cite journal | author=Rolink AG, Nutt SL, Melchers F, Busslinger M |title=Long-term in vivo reconstitution of T-cell development by Pax5-deficient B-cell progenitors. |journal=Nature |volume=401 |issue= 6753 |pages= 603-6 |year= 1999 |pmid= 10524629 |doi= 10.1038/44164 }}
*{{cite journal | author=Kovac CR, Emelyanov A, Singh M, ''et al.'' |title=BSAP (Pax5)-importin alpha 1 (Rch1) interaction identifies a nuclear localization sequence. |journal=J. Biol. Chem. |volume=275 |issue= 22 |pages= 16752-7 |year= 2000 |pmid= 10748034 |doi= 10.1074/jbc.M001551200 }}
*{{cite journal | author=Eberhard D, Jiménez G, Heavey B, Busslinger M |title=Transcriptional repression by Pax5 (BSAP) through interaction with corepressors of the Groucho family. |journal=EMBO J. |volume=19 |issue= 10 |pages= 2292-303 |year= 2000 |pmid= 10811620 |doi= 10.1093/emboj/19.10.2292 }}
*{{cite journal | author=Roberts EC, Deed RW, Inoue T, ''et al.'' |title=Id helix-loop-helix proteins antagonize pax transcription factor activity by inhibiting DNA binding. |journal=Mol. Cell. Biol. |volume=21 |issue= 2 |pages= 524-33 |year= 2001 |pmid= 11134340 |doi= 10.1128/MCB.21.2.524-533.2001 }}
*{{cite journal | author=Pasqualucci L, Neumeister P, Goossens T, ''et al.'' |title=Hypermutation of multiple proto-oncogenes in B-cell diffuse large-cell lymphomas. |journal=Nature |volume=412 |issue= 6844 |pages= 341-6 |year= 2001 |pmid= 11460166 |doi= 10.1038/35085588 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PRDX1... {November 18, 2007 11:09:48 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:10:43 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| 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_PRDX1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1qq2.
| PDB = {{PDB2|1qq2}}
| Name = Peroxiredoxin 1
| HGNCid = 9352
| Symbol = PRDX1
| AltSymbols =; MSP23; NKEFA; PAG; PAGA; PAGB; TDPX2
| OMIM = 176763
| ECnumber =
| Homologene = 21685
| MGIid = 99523
| GeneAtlas_image1 = PBB_GE_PRDX1_208680_at_tn.png
| Function = {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0051920 |text = peroxiredoxin activity}}
| Component =
| Process = {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5052
| Hs_Ensembl = ENSG00000117450
| Hs_RefseqProtein = NP_002565
| Hs_RefseqmRNA = NM_002574
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 45749295
| Hs_GenLoc_end = 45760215
| Hs_Uniprot = Q06830
| Mm_EntrezGene = 18477
| Mm_Ensembl = ENSMUSG00000028691
| Mm_RefseqmRNA = NM_011034
| Mm_RefseqProtein = NP_035164
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 116183531
| Mm_GenLoc_end = 116197932
| Mm_Uniprot = Q3U9J9
}}
}}
'''Peroxiredoxin 1''', also known as '''PRDX1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRDX1 peroxiredoxin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5052| 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 peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. The encoded protein may play an antioxidant protective role in cells, and may contribute to the antiviral activity of CD8(+) T-cells. This protein may have a proliferative effect and play a role in cancer development or progression. Three transcript variants encoding the same protein have been identified for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: PRDX1 peroxiredoxin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5052| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wood ZA, Schröder E, Robin Harris J, Poole LB |title=Structure, mechanism and regulation of peroxiredoxins. |journal=Trends Biochem. Sci. |volume=28 |issue= 1 |pages= 32-40 |year= 2003 |pmid= 12517450 |doi= }}
*{{cite journal | author=Sauri H, Butterfield L, Kim A, Shau H |title=Antioxidant function of recombinant human natural killer enhancing factor. |journal=Biochem. Biophys. Res. Commun. |volume=208 |issue= 3 |pages= 964-9 |year= 1995 |pmid= 7702627 |doi= }}
*{{cite journal | author=Shau H, Butterfield LH, Chiu R, Kim A |title=Cloning and sequence analysis of candidate human natural killer-enhancing factor genes. |journal=Immunogenetics |volume=40 |issue= 2 |pages= 129-34 |year= 1994 |pmid= 8026862 |doi= }}
*{{cite journal | author=Kawai S, Takeshita S, Okazaki M, ''et al.'' |title=Cloning and characterization of OSF-3, a new member of the MER5 family, expressed in mouse osteoblastic cells. |journal=J. Biochem. |volume=115 |issue= 4 |pages= 641-3 |year= 1994 |pmid= 8089076 |doi= }}
*{{cite journal | author=Shau H, Kim A |title=Identification of natural killer enhancing factor as a major antioxidant in human red blood cells. |journal=Biochem. Biophys. Res. Commun. |volume=199 |issue= 1 |pages= 83-8 |year= 1994 |pmid= 8123050 |doi= }}
*{{cite journal | author=Prospéri MT, Apiou F, Dutrillaux B, Goubin G |title=Organization and chromosomal assignment of two human PAG gene loci: PAGA encoding a functional gene and PAGB a processed pseudogene. |journal=Genomics |volume=19 |issue= 2 |pages= 236-41 |year= 1994 |pmid= 8188254 |doi= 10.1006/geno.1994.1053 }}
*{{cite journal | author=Prospéri MT, Ferbus D, Karczinski I, Goubin G |title=A human cDNA corresponding to a gene overexpressed during cell proliferation encodes a product sharing homology with amoebic and bacterial proteins. |journal=J. Biol. Chem. |volume=268 |issue= 15 |pages= 11050-6 |year= 1993 |pmid= 8496166 |doi= }}
*{{cite journal | author=Wen ST, Van Etten RA |title=The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity. |journal=Genes Dev. |volume=11 |issue= 19 |pages= 2456-67 |year= 1997 |pmid= 9334312 |doi= }}
*{{cite journal | author=Jin DY, Chae HZ, Rhee SG, Jeang KT |title=Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation. |journal=J. Biol. Chem. |volume=272 |issue= 49 |pages= 30952-61 |year= 1998 |pmid= 9388242 |doi= }}
*{{cite journal | author=Outinen PA, Sood SK, Pfeifer SI, ''et al.'' |title=Homocysteine-induced endoplasmic reticulum stress and growth arrest leads to specific changes in gene expression in human vascular endothelial cells. |journal=Blood |volume=94 |issue= 3 |pages= 959-67 |year= 1999 |pmid= 10419887 |doi= }}
*{{cite journal | author=Yanagawa T, Ishikawa T, Ishii T, ''et al.'' |title=Peroxiredoxin I expression in human thyroid tumors. |journal=Cancer Lett. |volume=145 |issue= 1-2 |pages= 127-32 |year= 1999 |pmid= 10530780 |doi= }}
*{{cite journal | author=Noh DY, Ahn SJ, Lee RA, ''et al.'' |title=Overexpression of peroxiredoxin in human breast cancer. |journal=Anticancer Res. |volume=21 |issue= 3B |pages= 2085-90 |year= 2001 |pmid= 11497302 |doi= }}
*{{cite journal | author=Xu XR, Huang J, Xu ZG, ''et al.'' |title=Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 26 |pages= 15089-94 |year= 2002 |pmid= 11752456 |doi= 10.1073/pnas.241522398 }}
*{{cite journal | author=Kim SH, Fountoulakis M, Cairns N, Lubec G |title=Protein levels of human peroxiredoxin subtypes in brains of patients with Alzheimer's disease and Down syndrome. |journal=J. Neural Transm. Suppl. |volume= |issue= 61 |pages= 223-35 |year= 2002 |pmid= 11771746 |doi= }}
*{{cite journal | author=Rabilloud T, Heller M, Gasnier F, ''et al.'' |title=Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site. |journal=J. Biol. Chem. |volume=277 |issue= 22 |pages= 19396-401 |year= 2002 |pmid= 11904290 |doi= 10.1074/jbc.M106585200 }}
*{{cite journal | author=Chang TS, Jeong W, Choi SY, ''et al.'' |title=Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation. |journal=J. Biol. Chem. |volume=277 |issue= 28 |pages= 25370-6 |year= 2002 |pmid= 11986303 |doi= 10.1074/jbc.M110432200 }}
*{{cite journal | author=Wagner E, Luche S, Penna L, ''et al.'' |title=A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress. |journal=Biochem. J. |volume=366 |issue= Pt 3 |pages= 777-85 |year= 2002 |pmid= 12059788 |doi= 10.1042/BJ20020525 }}
*{{cite journal | author=Shen C, Nathan C |title=Nonredundant antioxidant defense by multiple two-cysteine peroxiredoxins in human prostate cancer cells. |journal=Mol. Med. |volume=8 |issue= 2 |pages= 95-102 |year= 2002 |pmid= 12080185 |doi= }}
*{{cite journal | author=Yang KS, Kang SW, Woo HA, ''et al.'' |title=Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid. |journal=J. Biol. Chem. |volume=277 |issue= 41 |pages= 38029-36 |year= 2002 |pmid= 12161445 |doi= 10.1074/jbc.M206626200 }}
*{{cite journal | author=Geiben-Lynn R, Kursar M, Brown NV, ''et al.'' |title=HIV-1 antiviral activity of recombinant natural killer cell enhancing factors, NKEF-A and NKEF-B, members of the peroxiredoxin family. |journal=J. Biol. Chem. |volume=278 |issue= 3 |pages= 1569-74 |year= 2003 |pmid= 12421812 |doi= 10.1074/jbc.M209964200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PRKAG2... {November 18, 2007 11:16:12 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:16:57 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Protein kinase, AMP-activated, gamma 2 non-catalytic subunit
| HGNCid = 9386
| Symbol = PRKAG2
| AltSymbols =; AAKG; AAKG2; CMH6; H91620p; WPWS
| OMIM = 602743
| ECnumber =
| Homologene = 81846
| MGIid = 1336153
| GeneAtlas_image1 = PBB_GE_PRKAG2_218292_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}}
| Process = {{GNF_GO|id=GO:0006633 |text = fatty acid biosynthetic process}} {{GNF_GO|id=GO:0006695 |text = cholesterol biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 51422
| Hs_Ensembl = ENSG00000106617
| Hs_RefseqProtein = NP_001035723
| Hs_RefseqmRNA = NM_001040633
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 150884960
| Hs_GenLoc_end = 151204728
| Hs_Uniprot = Q9UGJ0
| Mm_EntrezGene = 108099
| Mm_Ensembl = ENSMUSG00000028944
| Mm_RefseqmRNA = NM_145401
| Mm_RefseqProtein = NP_663376
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 24372813
| Mm_GenLoc_end = 24610495
| Mm_Uniprot = Q3TMN8
}}
}}
'''Protein kinase, AMP-activated, gamma 2 non-catalytic subunit''', also known as '''PRKAG2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRKAG2 protein kinase, AMP-activated, gamma 2 non-catalytic subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51422| 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 = AMP-activated protein kinase (AMPK) is a heterotrimeric protein composed of a catalytic alpha subunit, a noncatalytic beta subunit, and a noncatalytic regulatory gamma subunit. Various forms of each of these subunits exist, encoded by different genes. AMPK is an important energy-sensing enzyme that monitors cellular energy status and functions by inactivating key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. This gene is a member of the AMPK gamma subunit family and encodes a protein with four cystathionine beta-synthase domains. Mutations in this gene have been associated with ventricular pre-excitation (Wolff-Parkinson-White syndrome), progressive conduction system disease and cardiac hypertrophy. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.<ref name="entrez">{{cite web | title = Entrez Gene: PRKAG2 protein kinase, AMP-activated, gamma 2 non-catalytic subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51422| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Gollob MH, Green MS, Tang AS, Roberts R |title=PRKAG2 cardiac syndrome: familial ventricular preexcitation, conduction system disease, and cardiac hypertrophy. |journal=Curr. Opin. Cardiol. |volume=17 |issue= 3 |pages= 229-34 |year= 2002 |pmid= 12015471 |doi= }}
*{{cite journal | author=Gollob MH |title=Glycogen storage disease as a unifying mechanism of disease in the PRKAG2 cardiac syndrome. |journal=Biochem. Soc. Trans. |volume=31 |issue= Pt 1 |pages= 228-31 |year= 2003 |pmid= 12546691 |doi= 10.1042/ }}
*{{cite journal | author=Hofmann B, Nishanian P, Baldwin RL, ''et al.'' |title=HIV inhibits the early steps of lymphocyte activation, including initiation of inositol phospholipid metabolism. |journal=J. Immunol. |volume=145 |issue= 11 |pages= 3699-705 |year= 1991 |pmid= 1978848 |doi= }}
*{{cite journal | author=MacRae CA, Ghaisas N, Kass S, ''et al.'' |title=Familial Hypertrophic cardiomyopathy with Wolff-Parkinson-White syndrome maps to a locus on chromosome 7q3. |journal=J. Clin. Invest. |volume=96 |issue= 3 |pages= 1216-20 |year= 1995 |pmid= 7657794 |doi= }}
*{{cite journal | author=Hofmann B, Nishanian P, Nguyen T, ''et al.'' |title=Human immunodeficiency virus proteins induce the inhibitory cAMP/protein kinase A pathway in normal lymphocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 14 |pages= 6676-80 |year= 1993 |pmid= 7688126 |doi= }}
*{{cite journal | author=Hofmann B, Nishanian P, Fan J, ''et al.'' |title=HIV Gag p17 protein impairs proliferation of normal lymphocytes in vitro. |journal=AIDS |volume=8 |issue= 7 |pages= 1016-7 |year= 1994 |pmid= 7946090 |doi= }}
*{{cite journal | author=Stapleton D, Mitchelhill KI, Gao G, ''et al.'' |title=Mammalian AMP-activated protein kinase subfamily. |journal=J. Biol. Chem. |volume=271 |issue= 2 |pages= 611-4 |year= 1996 |pmid= 8557660 |doi= }}
*{{cite journal | author=Gao G, Fernandez CS, Stapleton D, ''et al.'' |title=Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-activated protein kinase. |journal=J. Biol. Chem. |volume=271 |issue= 15 |pages= 8675-81 |year= 1996 |pmid= 8621499 |doi= }}
*{{cite journal | author=Swingler S, Gallay P, Camaur D, ''et al.'' |title=The Nef protein of human immunodeficiency virus type 1 enhances serine phosphorylation of the viral matrix. |journal=J. Virol. |volume=71 |issue= 6 |pages= 4372-7 |year= 1997 |pmid= 9151826 |doi= }}
*{{cite journal | author=Stapleton D, Woollatt E, Mitchelhill KI, ''et al.'' |title=AMP-activated protein kinase isoenzyme family: subunit structure and chromosomal location. |journal=FEBS Lett. |volume=409 |issue= 3 |pages= 452-6 |year= 1997 |pmid= 9224708 |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=Zidovetzki R, Wang JL, Chen P, ''et al.'' |title=Human immunodeficiency virus Tat protein induces interleukin 6 mRNA expression in human brain endothelial cells via protein kinase C- and cAMP-dependent protein kinase pathways. |journal=AIDS Res. Hum. Retroviruses |volume=14 |issue= 10 |pages= 825-33 |year= 1998 |pmid= 9671211 |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= |title=Toward a complete human genome sequence. |journal=Genome Res. |volume=8 |issue= 11 |pages= 1097-108 |year= 1999 |pmid= 9847074 |doi= }}
*{{cite journal | author=Cheung PC, Salt IP, Davies SP, ''et al.'' |title=Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding. |journal=Biochem. J. |volume=346 Pt 3 |issue= |pages= 659-69 |year= 2000 |pmid= 10698692 |doi= }}
*{{cite journal | author=Lang T, Yu L, Tu Q, ''et al.'' |title=Molecular cloning, genomic organization, and mapping of PRKAG2, a heart abundant gamma2 subunit of 5'-AMP-activated protein kinase, to human chromosome 7q36. |journal=Genomics |volume=70 |issue= 2 |pages= 258-63 |year= 2001 |pmid= 11112354 |doi= 10.1006/geno.2000.6376 }}
*{{cite journal | author=Blair E, Redwood C, Ashrafian H, ''et al.'' |title=Mutations in the gamma(2) subunit of AMP-activated protein kinase cause familial hypertrophic cardiomyopathy: evidence for the central role of energy compromise in disease pathogenesis. |journal=Hum. Mol. Genet. |volume=10 |issue= 11 |pages= 1215-20 |year= 2001 |pmid= 11371514 |doi= }}
*{{cite journal | author=Gollob MH, Green MS, Tang AS, ''et al.'' |title=Identification of a gene responsible for familial Wolff-Parkinson-White syndrome. |journal=N. Engl. J. Med. |volume=344 |issue= 24 |pages= 1823-31 |year= 2001 |pmid= 11407343 |doi= }}
*{{cite journal | author=Hamilton SR, Stapleton D, O'Donnell JB, ''et al.'' |title=An activating mutation in the gamma1 subunit of the AMP-activated protein kinase. |journal=FEBS Lett. |volume=500 |issue= 3 |pages= 163-8 |year= 2001 |pmid= 11445078 |doi= }}
*{{cite journal | author=Gollob MH, Seger JJ, Gollob TN, ''et al.'' |title=Novel PRKAG2 mutation responsible for the genetic syndrome of ventricular preexcitation and conduction system disease with childhood onset and absence of cardiac hypertrophy. |journal=Circulation |volume=104 |issue= 25 |pages= 3030-3 |year= 2002 |pmid= 11748095 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PTGER4... {November 18, 2007 11:11:48 AM PST}
- SEARCH REDIRECT: Control Box Found: PTGER4 {November 18, 2007 11:12:14 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:12:17 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:12:17 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:12:17 AM PST}
- UPDATED: Updated protein page: PTGER4 {November 18, 2007 11:12:24 AM PST}
- INFO: Beginning work on PURA... {November 18, 2007 11:12:24 AM PST}
- SEARCH REDIRECT: Control Box Found: PURA {November 18, 2007 11:13:23 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:13:27 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:13:27 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:13:27 AM PST}
- UPDATED: Updated protein page: PURA {November 18, 2007 11:13:33 AM PST}
- INFO: Beginning work on PYGM... {November 18, 2007 11:13:34 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:13:54 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PYGM_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a8i.
| PDB = {{PDB2|1a8i}}, {{PDB2|1abb}}, {{PDB2|1axr}}, {{PDB2|1b4d}}, {{PDB2|1bx3}}, {{PDB2|1c50}}, {{PDB2|1c8k}}, {{PDB2|1c8l}}, {{PDB2|1e1y}}, {{PDB2|1fs4}}, {{PDB2|1ftq}}, {{PDB2|1ftw}}, {{PDB2|1fty}}, {{PDB2|1fu4}}, {{PDB2|1fu7}}, {{PDB2|1fu8}}, {{PDB2|1gfz}}, {{PDB2|1gg8}}, {{PDB2|1ggn}}, {{PDB2|1gpa}}, {{PDB2|1gpb}}, {{PDB2|1gpy}}, {{PDB2|1h5u}}, {{PDB2|1hlf}}, {{PDB2|1k06}}, {{PDB2|1k08}}, {{PDB2|1kti}}, {{PDB2|1lwn}}, {{PDB2|1lwo}}, {{PDB2|1noi}}, {{PDB2|1noj}}, {{PDB2|1nok}}, {{PDB2|1p29}}, {{PDB2|1p2b}}, {{PDB2|1p2d}}, {{PDB2|1p2g}}, {{PDB2|1p4g}}, {{PDB2|1p4h}}, {{PDB2|1p4j}}, {{PDB2|1pyg}}, {{PDB2|1uzu}}, {{PDB2|1wut}}, {{PDB2|1wuy}}, {{PDB2|1wv0}}, {{PDB2|1wv1}}, {{PDB2|1ww2}}, {{PDB2|1ww3}}, {{PDB2|1xc7}}, {{PDB2|1xkx}}, {{PDB2|1xl0}}, {{PDB2|1xl1}}, {{PDB2|1z62}}, {{PDB2|1z6p}}, {{PDB2|1z6q}}, {{PDB2|1z8d}}, {{PDB2|2amv}}, {{PDB2|2f3p}}, {{PDB2|2f3q}}, {{PDB2|2f3s}}, {{PDB2|2f3u}}, {{PDB2|2fet}}, {{PDB2|2ff5}}, {{PDB2|2ffr}}, {{PDB2|2g9q}}, {{PDB2|2g9r}}, {{PDB2|2g9u}}, {{PDB2|2g9v}}, {{PDB2|2gj4}}, {{PDB2|2gm9}}, {{PDB2|2gpa}}, {{PDB2|2gpb}}, {{PDB2|2gpn}}, {{PDB2|2ieg}}, {{PDB2|2iei}}, {{PDB2|2pri}}, {{PDB2|2prj}}, {{PDB2|2skc}}, {{PDB2|2skd}}, {{PDB2|2ske}}, {{PDB2|3amv}}, {{PDB2|3gpb}}, {{PDB2|4gpb}}, {{PDB2|5gpb}}, {{PDB2|6gpb}}, {{PDB2|7gpb}}, {{PDB2|8gpb}}, {{PDB2|9gpb}}
| Name = Phosphorylase, glycogen; muscle (McArdle syndrome, glycogen storage disease type V)
| HGNCid = 9726
| Symbol = PYGM
| AltSymbols =;
| OMIM = 608455
| ECnumber =
| Homologene = 2145
| MGIid = 97830
| GeneAtlas_image1 = PBB_GE_PYGM_205577_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0008184 |text = glycogen phosphorylase activity}} {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}} {{GNF_GO|id=GO:0030170 |text = pyridoxal phosphate binding}}
| Component =
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0005980 |text = glycogen catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5837
| Hs_Ensembl = ENSG00000068976
| Hs_RefseqProtein = NP_005600
| Hs_RefseqmRNA = NM_005609
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 64270437
| Hs_GenLoc_end = 64284763
| Hs_Uniprot = P11217
| Mm_EntrezGene = 19309
| Mm_Ensembl = ENSMUSG00000032648
| Mm_RefseqmRNA = NM_011224
| Mm_RefseqProtein = NP_035354
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 6384429
| Mm_GenLoc_end = 6398459
| Mm_Uniprot = Q9CTZ0
}}
}}
'''Phosphorylase, glycogen; muscle (McArdle syndrome, glycogen storage disease type V)''', also known as '''PYGM''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PYGM phosphorylase, glycogen; muscle (McArdle syndrome, glycogen storage disease type V)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5837| 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 = Glycogen phosphorylase (EC 2.4.1.1) catalyzes and regulates the breakdown of glycogen to glucose-1-phosphate.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: PYGM phosphorylase, glycogen; muscle (McArdle syndrome, glycogen storage disease type V)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5837| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Carty TJ, Tu J-I , Graves DJ |title=Regulation of glycogen phosphorylase. Role of the peptide region surrounding the phosphoserine residue in determining enzyme properties. |journal=J. Biol. Chem. |volume=250 |issue= 13 |pages= 4980-5 |year= 1975 |pmid= 1150650 |doi= }}
*{{cite journal | author=Lebo RV, Anderson LA, DiMauro S, ''et al.'' |title=Rare McArdle disease locus polymorphic site on 11q13 contains CpG sequence. |journal=Hum. Genet. |volume=86 |issue= 1 |pages= 17-24 |year= 1991 |pmid= 1701414 |doi= }}
*{{cite journal | author=Sarova-Pinhas I, Sadeh M |title=McArdle disease in a Druze family. |journal=Isr. J. Med. Sci. |volume=25 |issue= 2 |pages= 64-8 |year= 1989 |pmid= 2703328 |doi= }}
*{{cite journal | author=Burke J, Hwang P, Anderson L, ''et al.'' |title=Intron/exon structure of the human gene for the muscle isozyme of glycogen phosphorylase. |journal=Proteins |volume=2 |issue= 3 |pages= 177-87 |year= 1988 |pmid= 3447177 |doi= 10.1002/prot.340020303 }}
*{{cite journal | author=Gautron S, Daegelen D, Mennecier F, ''et al.'' |title=Molecular mechanisms of McArdle's disease (muscle glycogen phosphorylase deficiency). RNA and DNA analysis. |journal=J. Clin. Invest. |volume=79 |issue= 1 |pages= 275-81 |year= 1987 |pmid= 3466902 |doi= }}
*{{cite journal | author=Hwang PK, See YP, Vincentini AM, ''et al.'' |title=Comparative sequence analysis of rat, rabbit, and human muscle glycogen phosphorylase cDNAs. |journal=Eur. J. Biochem. |volume=152 |issue= 2 |pages= 267-74 |year= 1985 |pmid= 3840433 |doi= }}
*{{cite journal | author=Daegelen-Proux D, Kahn A, Marie J, Dreyfus JC |title=Research on molecular mechanisms of McArdle's disease (muscle glycogen phosphorylase deficiency). Use of new protein mapping and immunological techniques. |journal=Ann. Hum. Genet. |volume=45 |issue= Pt 2 |pages= 113-20 |year= 1982 |pmid= 6797345 |doi= }}
*{{cite journal | author=Tsujino S, Shanske S, Nonaka I, DiMauro S |title=The molecular genetic basis of myophosphorylase deficiency (McArdle's disease). |journal=Muscle Nerve |volume=3 |issue= |pages= S23-7 |year= 1995 |pmid= 7603523 |doi= }}
*{{cite journal | author=Cuenda A, Nogues M, Henao F, Gutiérrez-Merino C |title=Interaction between glycogen phosphorylase and sarcoplasmic reticulum membranes and its functional implications. |journal=J. Biol. Chem. |volume=270 |issue= 20 |pages= 11998-2004 |year= 1995 |pmid= 7744850 |doi= }}
*{{cite journal | author=Froman BE, Herrick KR, Gorin FA |title=Regulation of the rat muscle glycogen phosphorylase-encoding gene during muscle cell development. |journal=Gene |volume=149 |issue= 2 |pages= 245-52 |year= 1994 |pmid= 7958997 |doi= }}
*{{cite journal | author=Tsujino S, Shanske S, DiMauro S |title=Molecular genetic heterogeneity of myophosphorylase deficiency (McArdle's disease). |journal=N. Engl. J. Med. |volume=329 |issue= 4 |pages= 241-5 |year= 1993 |pmid= 8316268 |doi= }}
*{{cite journal | author=Tsujino S, Shanske S, Martinuzzi A, ''et al.'' |title=Two novel missense mutations (E654K, L396P) in Caucasian patients with myophosphorylase deficiency (McArdle's disease). |journal=Hum. Mutat. |volume=6 |issue= 3 |pages= 276-7 |year= 1996 |pmid= 8535454 |doi= 10.1002/humu.1380060318 }}
*{{cite journal | author=Vorgerd M, Kubisch C, Burwinkel B, ''et al.'' |title=Mutation analysis in myophosphorylase deficiency (McArdle's disease). |journal=Ann. Neurol. |volume=43 |issue= 3 |pages= 326-31 |year= 1998 |pmid= 9506549 |doi= 10.1002/ana.410430310 }}
*{{cite journal | author=Kubisch C, Wicklein EM, Jentsch TJ |title=Molecular diagnosis of McArdle disease: revised genomic structure of the myophosphorylase gene and identification of a novel mutation. |journal=Hum. Mutat. |volume=12 |issue= 1 |pages= 27-32 |year= 1998 |pmid= 9633816 |doi= 10.1002/(SICI)1098-1004(1998)12:1<27::AID-HUMU4>3.0.CO;2-# }}
*{{cite journal | author=Andreu AL, Bruno C, Tamburino L, ''et al.'' |title=A new mutation in the myophosphorylase gene (Asn684Tyr) in a Spanish patient with McArdle's disease. |journal=Neuromuscul. Disord. |volume=9 |issue= 3 |pages= 171-3 |year= 1999 |pmid= 10382911 |doi= }}
*{{cite journal | author=Rubio JC, Martín MA, García A, ''et al.'' |title=McArdle's disease associated with homozygosity for the missense mutation Gly204Ser of the myophosphorylase gene in a Spanish patient. |journal=Neuromuscul. Disord. |volume=9 |issue= 3 |pages= 174-5 |year= 1999 |pmid= 10382912 |doi= }}
*{{cite journal | author=Gamez J, Fernandez R, Bruno C, ''et al.'' |title=A new mutation in the regulatory domain of the myophosphorylase gene affecting protein dimer contact. |journal=Muscle Nerve |volume=22 |issue= 8 |pages= 1136-8 |year= 2002 |pmid= 10417800 |doi= }}
*{{cite journal | author=Rubio JC, Martín MA, Campos Y, ''et al.'' |title=A missense mutation W797R in the myophosphorylase gene in a Spanish patient with McArdle's disease. |journal=Muscle Nerve |volume=23 |issue= 1 |pages= 129-31 |year= 2000 |pmid= 10590419 |doi= }}
*{{cite journal | author=Fernández R, Navarro C, Andreu AL, ''et al.'' |title=A novel missense mutation (W797R) in the myophosphorylase gene in Spanish patients with McArdle disease. |journal=Arch. Neurol. |volume=57 |issue= 2 |pages= 217-9 |year= 2000 |pmid= 10681080 |doi= }}
*{{cite journal | author=Rubio JC, Martín MA, Campos Y, ''et al.'' |title=A missense mutation T487N in the myophosphorylase gene in a Spanish patient with McArdle's disease. |journal=Neuromuscul. Disord. |volume=10 |issue= 2 |pages= 138-40 |year= 2000 |pmid= 10714589 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RAD17... {November 18, 2007 11:13:54 AM PST}
- SEARCH REDIRECT: Control Box Found: RAD17 {November 18, 2007 11:14:37 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:14:41 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:14:41 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:14:41 AM PST}
- UPDATED: Updated protein page: RAD17 {November 18, 2007 11:14:48 AM PST}
- INFO: Beginning work on RAP1GAP... {November 18, 2007 11:14:48 AM PST}
- SEARCH REDIRECT: Control Box Found: RAP1GAP {November 18, 2007 11:15:19 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:15:20 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:15:20 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:15:20 AM PST}
- UPDATED: Updated protein page: RAP1GAP {November 18, 2007 11:15:26 AM PST}
- INFO: Beginning work on RHOC... {November 18, 2007 11:00:15 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:01:20 AM PST}
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{{PBB_Controls
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| update_protein_box = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_RHOC_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a2b.
| PDB = {{PDB2|1a2b}}, {{PDB2|1cc0}}, {{PDB2|1cxz}}, {{PDB2|1dpf}}, {{PDB2|1ftn}}, {{PDB2|1kmq}}, {{PDB2|1lb1}}, {{PDB2|1ow3}}, {{PDB2|1s1c}}, {{PDB2|1tx4}}, {{PDB2|1x86}}, {{PDB2|1xcg}}, {{PDB2|1z2c}}, {{PDB2|2gcn}}, {{PDB2|2gco}}, {{PDB2|2gcp}}
| Name = Ras homolog gene family, member C
| HGNCid = 669
| Symbol = RHOC
| AltSymbols =; ARH9; ARHC; H9; MGC1448; MGC61427; RHOH9
| OMIM = 165380
| ECnumber =
| Homologene = 56380
| MGIid = 106028
| GeneAtlas_image1 = PBB_GE_RHOC_200885_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 389
| Hs_Ensembl = ENSG00000155366
| Hs_RefseqProtein = NP_001036143
| Hs_RefseqmRNA = NM_001042678
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 113045251
| Hs_GenLoc_end = 113051579
| Hs_Uniprot = P08134
| Mm_EntrezGene = 11853
| Mm_Ensembl = ENSMUSG00000002233
| Mm_RefseqmRNA = NM_007484
| Mm_RefseqProtein = NP_031510
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 104917090
| Mm_GenLoc_end = 104922515
| Mm_Uniprot = Q62159
}}
}}
'''Ras homolog gene family, member C''', also known as '''RHOC''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RHOC ras homolog gene family, member C| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=389| 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 Rho family of small GTPases, which cycle between inactive GDP-bound and active GTP-bound states and function as molecular switches in signal transduction cascades. Rho proteins promote reorganization of the actin cytoskeleton and regulate cell shape, attachment, and motility. The protein encoded by this gene is prenylated at its C-terminus, and localizes to the cytoplasm and plasma membrane. It is thought to be important in cell locomotion. Overexpression of this gene is associated with tumor cell proliferation and metastasis. Multiple alternatively spliced variants, encoding the same protein, have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: RHOC ras homolog gene family, member C| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=389| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wennerberg K, Der CJ |title=Rho-family GTPases: it's not only Rac and Rho (and I like it). |journal=J. Cell. Sci. |volume=117 |issue= Pt 8 |pages= 1301-12 |year= 2004 |pmid= 15020670 |doi= 10.1242/jcs.01118 }}
*{{cite journal | author=Wheeler AP, Ridley AJ |title=Why three Rho proteins? RhoA, RhoB, RhoC, and cell motility. |journal=Exp. Cell Res. |volume=301 |issue= 1 |pages= 43-9 |year= 2004 |pmid= 15501444 |doi= 10.1016/j.yexcr.2004.08.012 }}
*{{cite journal | author=Adamson P, Paterson HF, Hall A |title=Intracellular localization of the P21rho proteins. |journal=J. Cell Biol. |volume=119 |issue= 3 |pages= 617-27 |year= 1992 |pmid= 1383236 |doi= }}
*{{cite journal | author=Chardin P, Madaule P, Tavitian A |title=Coding sequence of human rho cDNAs clone 6 and clone 9. |journal=Nucleic Acids Res. |volume=16 |issue= 6 |pages= 2717 |year= 1988 |pmid= 3283705 |doi= }}
*{{cite journal | author=Madaule P, Axel R |title=A novel ras-related gene family. |journal=Cell |volume=41 |issue= 1 |pages= 31-40 |year= 1985 |pmid= 3888408 |doi= }}
*{{cite journal | author=Fagan KP, Oliveira L, Pittler SJ |title=Sequence of rho small GTP-binding protein cDNAs from human retina and identification of novel 5' end cloning artifacts. |journal=Exp. Eye Res. |volume=59 |issue= 2 |pages= 235-7 |year= 1995 |pmid= 7835413 |doi= 10.1006/exer.1994.1102 }}
*{{cite journal | author=Bokoch GM, Bohl BP, Chuang TH |title=Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins. |journal=J. Biol. Chem. |volume=269 |issue= 50 |pages= 31674-9 |year= 1995 |pmid= 7989340 |doi= }}
*{{cite journal | author=Morris SW, Valentine MB, Kirstein MN, Huebner K |title=Reassignment of the human ARH9 RAS-related gene to chromosome 1p13-p21. |journal=Genomics |volume=15 |issue= 3 |pages= 677-9 |year= 1993 |pmid= 8468062 |doi= 10.1006/geno.1993.1124 }}
*{{cite journal | author=Madaule P, Furuyashiki T, Reid T, ''et al.'' |title=A novel partner for the GTP-bound forms of rho and rac. |journal=FEBS Lett. |volume=377 |issue= 2 |pages= 243-8 |year= 1996 |pmid= 8543060 |doi= }}
*{{cite journal | author=Reid T, Furuyashiki T, Ishizaki T, ''et al.'' |title=Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain. |journal=J. Biol. Chem. |volume=271 |issue= 23 |pages= 13556-60 |year= 1996 |pmid= 8662891 |doi= }}
*{{cite journal | author=Leung T, Chen XQ, Manser E, Lim L |title=The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton. |journal=Mol. Cell. Biol. |volume=16 |issue= 10 |pages= 5313-27 |year= 1996 |pmid= 8816443 |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=Maekawa M, Ishizaki T, Boku S, ''et al.'' |title=Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase. |journal=Science |volume=285 |issue= 5429 |pages= 895-8 |year= 1999 |pmid= 10436159 |doi= }}
*{{cite journal | author=Clark EA, Golub TR, Lander ES, Hynes RO |title=Genomic analysis of metastasis reveals an essential role for RhoC. |journal=Nature |volume=406 |issue= 6795 |pages= 532-5 |year= 2000 |pmid= 10952316 |doi= 10.1038/35020106 }}
*{{cite journal | author=Diviani D, Soderling J, Scott JD |title=AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho-mediated stress fiber formation. |journal=J. Biol. Chem. |volume=276 |issue= 47 |pages= 44247-57 |year= 2001 |pmid= 11546812 |doi= 10.1074/jbc.M106629200 }}
*{{cite journal | author=Kleer CG, van Golen KL, Zhang Y, ''et al.'' |title=Characterization of RhoC expression in benign and malignant breast disease: a potential new marker for small breast carcinomas with metastatic ability. |journal=Am. J. Pathol. |volume=160 |issue= 2 |pages= 579-84 |year= 2002 |pmid= 11839578 |doi= }}
*{{cite journal | author=van Golen KL, Bao LW, Pan Q, ''et al.'' |title=Mitogen activated protein kinase pathway is involved in RhoC GTPase induced motility, invasion and angiogenesis in inflammatory breast cancer. |journal=Clin. Exp. Metastasis |volume=19 |issue= 4 |pages= 301-11 |year= 2002 |pmid= 12090470 |doi= }}
*{{cite journal | author=Arthur WT, Ellerbroek SM, Der CJ, ''et al.'' |title=XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not RhoC. |journal=J. Biol. Chem. |volume=277 |issue= 45 |pages= 42964-72 |year= 2003 |pmid= 12221096 |doi= 10.1074/jbc.M207401200 }}
*{{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=Shao F, Dixon JE |title=YopT is a cysteine protease cleaving Rho family GTPases. |journal=Adv. Exp. Med. Biol. |volume=529 |issue= |pages= 79-84 |year= 2003 |pmid= 12756732 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SERPIND1... {November 18, 2007 11:02:08 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:03:03 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_SERPIND1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1jmj.
| PDB = {{PDB2|1jmj}}, {{PDB2|1jmo}}
| Name = Serpin peptidase inhibitor, clade D (heparin cofactor), member 1
| HGNCid = 4838
| Symbol = SERPIND1
| AltSymbols =; D22S673; HC2; HCF2; HCII; HLS2; LS2
| OMIM = 142360
| ECnumber =
| Homologene = 36018
| MGIid = 96051
| GeneAtlas_image1 = PBB_GE_SERPIND1_205576_at_tn.png
| Function = {{GNF_GO|id=GO:0004867 |text = serine-type endopeptidase inhibitor activity}} {{GNF_GO|id=GO:0008201 |text = heparin binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3053
| Hs_Ensembl = ENSG00000099937
| Hs_RefseqProtein = NP_000176
| Hs_RefseqmRNA = NM_000185
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 19458383
| Hs_GenLoc_end = 19472008
| Hs_Uniprot = P05546
| Mm_EntrezGene = 15160
| Mm_Ensembl = ENSMUSG00000022766
| Mm_RefseqmRNA = NM_008223
| Mm_RefseqProtein = NP_032249
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 17244978
| Mm_GenLoc_end = 17257137
| Mm_Uniprot = Q5FW62
}}
}}
'''Serpin peptidase inhibitor, clade D (heparin cofactor), member 1''', also known as '''SERPIND1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SERPIND1 serpin peptidase inhibitor, clade D (heparin cofactor), member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3053| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The product encoded by this gene is a serine proteinase inhibitor which rapidly inhibits thrombin in the presence of dermatan sulfate or heparin. The gene contains five exons and four introns. This protein shares homology with antithrombin III and other members of the alpha 1-antitrypsin superfamily. Mutations in this gene are associated with heparin cofactor II deficiency.<ref name="entrez">{{cite web | title = Entrez Gene: SERPIND1 serpin peptidase inhibitor, clade D (heparin cofactor), member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3053| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Uszyński M |title=Tissue anticoagulants in the human placenta: preliminary study with a heparin-like anticoagulant and review of the literature. |journal=Gynecol. Obstet. Invest. |volume=32 |issue= 3 |pages= 129-33 |year= 1992 |pmid= 1836773 |doi= }}
*{{cite journal | author=Pizzo SV |title=Serpin receptor 1: a hepatic receptor that mediates the clearance of antithrombin III-proteinase complexes. |journal=Am. J. Med. |volume=87 |issue= 3B |pages= 10S-14S |year= 1989 |pmid= 2552799 |doi= }}
*{{cite journal | author=Herzog R, Lutz S, Blin N, ''et al.'' |title=Complete nucleotide sequence of the gene for human heparin cofactor II and mapping to chromosomal band 22q11. |journal=Biochemistry |volume=30 |issue= 5 |pages= 1350-7 |year= 1991 |pmid= 1671335 |doi= }}
*{{cite journal | author=Van Deerlin VM, Tollefsen DM |title=The N-terminal acidic domain of heparin cofactor II mediates the inhibition of alpha-thrombin in the presence of glycosaminoglycans. |journal=J. Biol. Chem. |volume=266 |issue= 30 |pages= 20223-31 |year= 1991 |pmid= 1939083 |doi= }}
*{{cite journal | author=Church FC, Pratt CW, Hoffman M |title=Leukocyte chemoattractant peptides from the serpin heparin cofactor II. |journal=J. Biol. Chem. |volume=266 |issue= 2 |pages= 704-9 |year= 1991 |pmid= 1985958 |doi= }}
*{{cite journal | author=Blinder MA, Tollefsen DM |title=Site-directed mutagenesis of arginine 103 and lysine 185 in the proposed glycosaminoglycan-binding site of heparin cofactor II. |journal=J. Biol. Chem. |volume=265 |issue= 1 |pages= 286-91 |year= 1990 |pmid= 2104620 |doi= }}
*{{cite journal | author=Pratt CW, Tobin RB, Church FC |title=Interaction of heparin cofactor II with neutrophil elastase and cathepsin G. |journal=J. Biol. Chem. |volume=265 |issue= 11 |pages= 6092-7 |year= 1990 |pmid= 2318847 |doi= }}
*{{cite journal | author=Blinder MA, Andersson TR, Abildgaard U, Tollefsen DM |title=Heparin cofactor IIOslo. Mutation of Arg-189 to His decreases the affinity for dermatan sulfate. |journal=J. Biol. Chem. |volume=264 |issue= 9 |pages= 5128-33 |year= 1989 |pmid= 2647747 |doi= }}
*{{cite journal | author=Hortin GL, Tollefsen DM, Benutto BM |title=Antithrombin activity of a peptide corresponding to residues 54-75 of heparin cofactor II. |journal=J. Biol. Chem. |volume=264 |issue= 24 |pages= 13979-82 |year= 1989 |pmid= 2760054 |doi= }}
*{{cite journal | author=Ragg H, Preibisch G |title=Structure and expression of the gene coding for the human serpin hLS2. |journal=J. Biol. Chem. |volume=263 |issue= 24 |pages= 12129-34 |year= 1988 |pmid= 2841345 |doi= }}
*{{cite journal | author=Blinder MA, Marasa JC, Reynolds CH, ''et al.'' |title=Heparin cofactor II: cDNA sequence, chromosome localization, restriction fragment length polymorphism, and expression in Escherichia coli. |journal=Biochemistry |volume=27 |issue= 2 |pages= 752-9 |year= 1988 |pmid= 2894851 |doi= }}
*{{cite journal | author=Ragg H |title=A new member of the plasma protease inhibitor gene family. |journal=Nucleic Acids Res. |volume=14 |issue= 2 |pages= 1073-88 |year= 1986 |pmid= 3003690 |doi= }}
*{{cite journal | author=Hiramoto SA, Cunningham DD |title=Effects of fibroblasts and endothelial cells on inactivation of target proteases by protease nexin-1, heparin cofactor II, and C1-inhibitor. |journal=J. Cell. Biochem. |volume=36 |issue= 3 |pages= 199-207 |year= 1988 |pmid= 3379101 |doi= 10.1002/jcb.240360302 }}
*{{cite journal | author=Inhorn RC, Tollefsen DM |title=Isolation and characterization of a partial cDNA clone for heparin cofactor II1. |journal=Biochem. Biophys. Res. Commun. |volume=137 |issue= 1 |pages= 431-6 |year= 1986 |pmid= 3755044 |doi= }}
*{{cite journal | author=Hortin G, Tollefsen DM, Strauss AW |title=Identification of two sites of sulfation of human heparin cofactor II. |journal=J. Biol. Chem. |volume=261 |issue= 34 |pages= 15827-30 |year= 1987 |pmid= 3782093 |doi= }}
*{{cite journal | author=Griffith MJ, Noyes CM, Tyndall JA, Church FC |title=Structural evidence for leucine at the reactive site of heparin cofactor II. |journal=Biochemistry |volume=24 |issue= 24 |pages= 6777-82 |year= 1986 |pmid= 3907702 |doi= }}
*{{cite journal | author=Liu L, Dewar L, Song Y, ''et al.'' |title=Inhibition of thrombin by antithrombin III and heparin cofactor II in vivo. |journal=Thromb. Haemost. |volume=73 |issue= 3 |pages= 405-12 |year= 1995 |pmid= 7545318 |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= }}
}}
{{refend}}
{{protein-stub}}
end log.
