- INFO: Beginning work on CASP10... {November 17, 2007 10:47:30 AM PST}
- SEARCH REDIRECT: Control Box Found: CASP10 {November 17, 2007 10:50:00 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 10:50:03 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 10:50:03 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 10:50:03 AM PST}
- UPDATED: Updated protein page: CASP10 {November 17, 2007 10:50:09 AM PST}
- INFO: Beginning work on CYP11A1... {November 17, 2007 10:50:09 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:50:59 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Cytochrome P450, family 11, subfamily A, polypeptide 1
| HGNCid = 2590
| Symbol = CYP11A1
| AltSymbols =; CYP11A; P450SCC
| OMIM = 118485
| ECnumber =
| Homologene = 37347
| MGIid = 88582
| GeneAtlas_image1 = PBB_GE_CYP11A1_204309_at_tn.png
| Function = {{GNF_GO|id=GO:0004497 |text = monooxygenase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0008386 |text = cholesterol monooxygenase (side-chain-cleaving) activity}} {{GNF_GO|id=GO:0019825 |text = oxygen binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006700 |text = C21-steroid hormone biosynthetic process}} {{GNF_GO|id=GO:0006702 |text = androgen biosynthetic process}} {{GNF_GO|id=GO:0008202 |text = steroid metabolic process}} {{GNF_GO|id=GO:0008203 |text = cholesterol metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1583
| Hs_Ensembl = ENSG00000140459
| Hs_RefseqProtein = NP_000772
| Hs_RefseqmRNA = NM_000781
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 72417193
| Hs_GenLoc_end = 72447134
| Hs_Uniprot = P05108
| Mm_EntrezGene = 13070
| Mm_Ensembl = ENSMUSG00000032323
| Mm_RefseqmRNA = XM_976231
| Mm_RefseqProtein = XP_981325
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 57813150
| Mm_GenLoc_end = 57825158
| Mm_Uniprot = Q6NV84
}}
}}
'''Cytochrome P450, family 11, subfamily A, polypeptide 1''', also known as '''CYP11A1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CYP11A1 cytochrome P450, family 11, subfamily A, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1583| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the mitochondrial inner membrane and catalyzes the conversion of cholesterol to pregnenolone, the first and rate-limiting step in the synthesis of the steroid hormones.<ref name="entrez">{{cite web | title = Entrez Gene: CYP11A1 cytochrome P450, family 11, subfamily A, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1583| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Helmberg A |title=Twin genes and endocrine disease: CYP21 and CYP11B genes. |journal=Acta Endocrinol. |volume=129 |issue= 2 |pages= 97-108 |year= 1993 |pmid= 8372604 |doi= }}
*{{cite journal | author=Papadopoulos V, Amri H, Boujrad N, ''et al.'' |title=Peripheral benzodiazepine receptor in cholesterol transport and steroidogenesis. |journal=Steroids |volume=62 |issue= 1 |pages= 21-8 |year= 1997 |pmid= 9029710 |doi= }}
*{{cite journal | author=Stocco DM |title=Intramitochondrial cholesterol transfer. |journal=Biochim. Biophys. Acta |volume=1486 |issue= 1 |pages= 184-97 |year= 2000 |pmid= 10856721 |doi= }}
*{{cite journal | author=Kristensen VN, Kure EH, Erikstein B, ''et al.'' |title=Genetic susceptibility and environmental estrogen-like compounds. |journal=Mutat. Res. |volume=482 |issue= 1-2 |pages= 77-82 |year= 2001 |pmid= 11535251 |doi= }}
*{{cite journal | author=Strauss JF |title=Some new thoughts on the pathophysiology and genetics of polycystic ovary syndrome. |journal=Ann. N. Y. Acad. Sci. |volume=997 |issue= |pages= 42-8 |year= 2004 |pmid= 14644808 |doi= }}
*{{cite journal | author=Guo IC, Shih MC, Lan HC, ''et al.'' |title=Transcriptional regulation of human CYP11A1 in gonads and adrenals. |journal=J. Biomed. Sci. |volume=14 |issue= 4 |pages= 509-15 |year= 2007 |pmid= 17594537 |doi= 10.1007/s11373-007-9177-z }}
*{{cite journal | author=Wada A, Waterman MR |title=Identification by site-directed mutagenesis of two lysine residues in cholesterol side chain cleavage cytochrome P450 that are essential for adrenodoxin binding. |journal=J. Biol. Chem. |volume=267 |issue= 32 |pages= 22877-82 |year= 1992 |pmid= 1429635 |doi= }}
*{{cite journal | author=Hu MC, Guo IC, Lin JH, Chung BC |title=Regulated expression of cytochrome P-450scc (cholesterol-side-chain cleavage enzyme) in cultured cell lines detected by antibody against bacterially expressed human protein. |journal=Biochem. J. |volume=274 ( Pt 3) |issue= |pages= 813-7 |year= 1991 |pmid= 1849407 |doi= }}
*{{cite journal | author=Sparkes RS, Klisak I, Miller WL |title=Regional mapping of genes encoding human steroidogenic enzymes: P450scc to 15q23-q24, adrenodoxin to 11q22; adrenodoxin reductase to 17q24-q25; and P450c17 to 10q24-q25. |journal=DNA Cell Biol. |volume=10 |issue= 5 |pages= 359-65 |year= 1991 |pmid= 1863359 |doi= }}
*{{cite journal | author=Coghlan VM, Vickery LE |title=Site-specific mutations in human ferredoxin that affect binding to ferredoxin reductase and cytochrome P450scc. |journal=J. Biol. Chem. |volume=266 |issue= 28 |pages= 18606-12 |year= 1991 |pmid= 1917982 |doi= }}
*{{cite journal | author=Matteson KJ, Chung BC, Urdea MS, Miller WL |title=Study of cholesterol side-chain cleavage (20,22 desmolase) deficiency causing congenital lipoid adrenal hyperplasia using bovine-sequence P450scc oligodeoxyribonucleotide probes. |journal=Endocrinology |volume=118 |issue= 4 |pages= 1296-305 |year= 1986 |pmid= 2419119 |doi= }}
*{{cite journal | author=Chung BC, Matteson KJ, Voutilainen R, ''et al.'' |title=Human cholesterol side-chain cleavage enzyme, P450scc: cDNA cloning, assignment of the gene to chromosome 15, and expression in the placenta. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 23 |pages= 8962-6 |year= 1987 |pmid= 3024157 |doi= }}
*{{cite journal | author=Morohashi K, Sogawa K, Omura T, Fujii-Kuriyama Y |title=Gene structure of human cytochrome P-450(SCC), cholesterol desmolase. |journal=J. Biochem. |volume=101 |issue= 4 |pages= 879-87 |year= 1987 |pmid= 3038854 |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=Gharani N, Waterworth DM, Batty S, ''et al.'' |title=Association of the steroid synthesis gene CYP11a with polycystic ovary syndrome and hyperandrogenism. |journal=Hum. Mol. Genet. |volume=6 |issue= 3 |pages= 397-402 |year= 1997 |pmid= 9147642 |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=Hukkanen J, Mäntylä M, Kangas L, ''et al.'' |title=Expression of cytochrome P450 genes encoding enzymes active in the metabolism of tamoxifen in human uterine endometrium. |journal=Pharmacol. Toxicol. |volume=82 |issue= 2 |pages= 93-7 |year= 1998 |pmid= 9498238 |doi= }}
*{{cite journal | author=Zhou Z, Shackleton CH, Pahwa S, ''et al.'' |title=Prominent sex steroid metabolism in human lymphocytes. |journal=Mol. Cell. Endocrinol. |volume=138 |issue= 1-2 |pages= 61-9 |year= 1998 |pmid= 9685215 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DEK... {November 17, 2007 11:02:56 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:03:17 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_DEK_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1q1v.
| PDB = {{PDB2|1q1v}}
| Name = DEK oncogene (DNA binding)
| HGNCid = 2768
| Symbol = DEK
| AltSymbols =; D6S231E
| OMIM = 125264
| ECnumber =
| Homologene = 2593
| MGIid = 1926209
| GeneAtlas_image1 = PBB_GE_DEK_200934_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003704 |text = specific RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}} {{GNF_GO|id=GO:0042393 |text = histone binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005786 |text = signal recognition particle, endoplasmic reticulum targeting}}
| Process = {{GNF_GO|id=GO:0006357 |text = regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006614 |text = SRP-dependent cotranslational protein targeting to membrane}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0019079 |text = viral genome replication}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7913
| Hs_Ensembl = ENSG00000124795
| Hs_RefseqProtein = NP_003463
| Hs_RefseqmRNA = NM_003472
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 18332392
| Hs_GenLoc_end = 18372750
| Hs_Uniprot = P35659
| Mm_EntrezGene = 110052
| Mm_Ensembl = ENSMUSG00000021377
| Mm_RefseqmRNA = NM_025900
| Mm_RefseqProtein = NP_080176
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 47095756
| Mm_GenLoc_end = 47117138
| Mm_Uniprot = Q3U4W4
}}
}}
'''DEK oncogene (DNA binding)''', also known as '''DEK''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DEK DEK oncogene (DNA binding)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7913| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a protein with one SAP domain. This protein binds to cruciform and superhelical DNA and induces positive supercoils into closed circular DNA and is also involved in splice site selection during mRNA processing. Chromosomal aberrations involving this region, increased expression of this gene and the presence of antibodies against this protein are all associated with various diseases.<ref name="entrez">{{cite web | title = Entrez Gene: DEK DEK oncogene (DNA binding)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7913| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=von Lindern M, Fornerod M, Soekarman N, ''et al.'' |title=Translocation t(6;9) in acute non-lymphocytic leukaemia results in the formation of a DEK-CAN fusion gene. |journal=Baillieres Clin. Haematol. |volume=5 |issue= 4 |pages= 857-79 |year= 1993 |pmid= 1308167 |doi= }}
*{{cite journal | author=Waldmann T, Scholten I, Kappes F, ''et al.'' |title=The DEK protein--an abundant and ubiquitous constituent of mammalian chromatin. |journal=Gene |volume=343 |issue= 1 |pages= 1-9 |year= 2005 |pmid= 15563827 |doi= 10.1016/j.gene.2004.08.029 }}
*{{cite journal | author=von Lindern M, Fornerod M, van Baal S, ''et al.'' |title=The translocation (6;9), associated with a specific subtype of acute myeloid leukemia, results in the fusion of two genes, dek and can, and the expression of a chimeric, leukemia-specific dek-can mRNA. |journal=Mol. Cell. Biol. |volume=12 |issue= 4 |pages= 1687-97 |year= 1992 |pmid= 1549122 |doi= }}
*{{cite journal | author=Denisenko ON, O'Neill B, Ostrowski J, ''et al.'' |title=Zik1, a transcriptional repressor that interacts with the heterogeneous nuclear ribonucleoprotein particle K protein. |journal=J. Biol. Chem. |volume=271 |issue= 44 |pages= 27701-6 |year= 1996 |pmid= 8910362 |doi= }}
*{{cite journal | author=Fu GK, Grosveld G, Markovitz DM |title=DEK, an autoantigen involved in a chromosomal translocation in acute myelogenous leukemia, binds to the HIV-2 enhancer. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 5 |pages= 1811-5 |year= 1997 |pmid= 9050861 |doi= }}
*{{cite journal | author=Murray KJ, Szer W, Grom AA, ''et al.'' |title=Antibodies to the 45 kDa DEK nuclear antigen in pauciarticular onset juvenile rheumatoid arthritis and iridocyclitis: selective association with MHC gene. |journal=J. Rheumatol. |volume=24 |issue= 3 |pages= 560-7 |year= 1997 |pmid= 9058666 |doi= }}
*{{cite journal | author=Forero L, Zwirner NW, Fink CW, ''et al.'' |title=Juvenile arthritis, HLA-A2 and binding of DEK oncogene-peptides. |journal=Hum. Immunol. |volume=59 |issue= 7 |pages= 443-50 |year= 1999 |pmid= 9684994 |doi= }}
*{{cite journal | author=Dong X, Michelis MA, Wang J, ''et al.'' |title=Autoantibodies to DEK oncoprotein in a patient with systemic lupus erythematosus and sarcoidosis. |journal=Arthritis Rheum. |volume=41 |issue= 8 |pages= 1505-10 |year= 1998 |pmid= 9704652 |doi= 10.1002/1529-0131(199808)41:8<1505::AID-ART23>3.0.CO;2-N }}
*{{cite journal | author=Wichmann I, Garcia-Lozano JR, Respaldiza N, ''et al.'' |title=Autoantibodies to transcriptional regulation proteins DEK and ALY in a patient with systemic lupus erythematosus. |journal=Hum. Immunol. |volume=60 |issue= 1 |pages= 57-62 |year= 1999 |pmid= 9952027 |doi= }}
*{{cite journal | author=Alexiadis V, Waldmann T, Andersen J, ''et al.'' |title=The protein encoded by the proto-oncogene DEK changes the topology of chromatin and reduces the efficiency of DNA replication in a chromatin-specific manner. |journal=Genes Dev. |volume=14 |issue= 11 |pages= 1308-12 |year= 2000 |pmid= 10837023 |doi= }}
*{{cite journal | author=McGarvey T, Rosonina E, McCracken S, ''et al.'' |title=The acute myeloid leukemia-associated protein, DEK, forms a splicing-dependent interaction with exon-product complexes. |journal=J. Cell Biol. |volume=150 |issue= 2 |pages= 309-20 |year= 2000 |pmid= 10908574 |doi= }}
*{{cite journal | author=Grottke C, Mantwill K, Dietel M, ''et al.'' |title=Identification of differentially expressed genes in human melanoma cells with acquired resistance to various antineoplastic drugs. |journal=Int. J. Cancer |volume=88 |issue= 4 |pages= 535-46 |year= 2000 |pmid= 11058868 |doi= }}
*{{cite journal | author=Le Hir H, Izaurralde E, Maquat LE, Moore MJ |title=The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions. |journal=EMBO J. |volume=19 |issue= 24 |pages= 6860-9 |year= 2001 |pmid= 11118221 |doi= 10.1093/emboj/19.24.6860 }}
*{{cite journal | author=Kappes F, Burger K, Baack M, ''et al.'' |title=Subcellular localization of the human proto-oncogene protein DEK. |journal=J. Biol. Chem. |volume=276 |issue= 28 |pages= 26317-23 |year= 2001 |pmid= 11333257 |doi= 10.1074/jbc.M100162200 }}
*{{cite journal | author=Waldmann T, Eckerich C, Baack M, Gruss C |title=The ubiquitous chromatin protein DEK alters the structure of DNA by introducing positive supercoils. |journal=J. Biol. Chem. |volume=277 |issue= 28 |pages= 24988-94 |year= 2002 |pmid= 11997399 |doi= 10.1074/jbc.M204045200 }}
*{{cite journal | author=Larramendy ML, Niini T, Elonen E, ''et al.'' |title=Overexpression of translocation-associated fusion genes of FGFRI, MYC, NPMI, and DEK, but absence of the translocations in acute myeloid leukemia. A microarray analysis. |journal=Haematologica |volume=87 |issue= 6 |pages= 569-77 |year= 2003 |pmid= 12031912 |doi= }}
*{{cite journal | author=Hollenbach AD, McPherson CJ, Mientjes EJ, ''et al.'' |title=Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek. |journal=J. Cell. Sci. |volume=115 |issue= Pt 16 |pages= 3319-30 |year= 2003 |pmid= 12140263 |doi= }}
*{{cite journal | author=Krithivas A, Fujimuro M, Weidner M, ''et al.'' |title=Protein interactions targeting the latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus to cell chromosomes. |journal=J. Virol. |volume=76 |issue= 22 |pages= 11596-604 |year= 2002 |pmid= 12388720 |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 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FASN... {November 17, 2007 10:51:36 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:52:40 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_FASN_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1xkt.
| PDB = {{PDB2|1xkt}}, {{PDB2|2cg5}}, {{PDB2|2jfd}}, {{PDB2|2jfk}}
| Name = Fatty acid synthase
| HGNCid = 3594
| Symbol = FASN
| AltSymbols =; FAS; MGC14367; MGC15706; OA-519
| OMIM = 600212
| ECnumber =
| Homologene = 55800
| MGIid = 95485
| GeneAtlas_image1 = PBB_GE_FASN_212218_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_FASN_217006_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003824 |text = catalytic activity}} {{GNF_GO|id=GO:0004313 |text = [acyl-carrier-protein] S-acetyltransferase activity}} {{GNF_GO|id=GO:0004314 |text = [acyl-carrier-protein] S-malonyltransferase activity}} {{GNF_GO|id=GO:0004315 |text = 3-oxoacyl-[acyl-carrier-protein] synthase activity}} {{GNF_GO|id=GO:0004316 |text = 3-oxoacyl-[acyl-carrier-protein] reductase activity}} {{GNF_GO|id=GO:0004317 |text = 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity}} {{GNF_GO|id=GO:0004319 |text = enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity}} {{GNF_GO|id=GO:0004320 |text = oleoyl-[acyl-carrier-protein] hydrolase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0010281 |text = acyl-ACP thioesterase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0016788 |text = hydrolase activity, acting on ester bonds}} {{GNF_GO|id=GO:0016829 |text = lyase activity}} {{GNF_GO|id=GO:0019901 |text = protein kinase binding}} {{GNF_GO|id=GO:0031177 |text = phosphopantetheine binding}} {{GNF_GO|id=GO:0048037 |text = cofactor binding}}
| Component = {{GNF_GO|id=GO:0042587 |text = glycogen granule}}
| Process = {{GNF_GO|id=GO:0006633 |text = fatty acid biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2194
| Hs_Ensembl = ENSG00000169710
| Hs_RefseqProtein = NP_004095
| Hs_RefseqmRNA = NM_004104
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 77629504
| Hs_GenLoc_end = 77649395
| Hs_Uniprot = P49327
| Mm_EntrezGene = 14104
| Mm_Ensembl = ENSMUSG00000025153
| Mm_RefseqmRNA = NM_007988
| Mm_RefseqProtein = NP_032014
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 120623167
| Mm_GenLoc_end = 120640332
| Mm_Uniprot = O89060
}}
}}
'''Fatty acid synthase''', also known as '''FASN''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FASN fatty acid synthase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2194| 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 enzyme encoded by this gene is a multifunctional protein. Its main function is to catalyze the synthesis of palmitate from acetyl-CoA and malonyl-CoA, in the presence of NADPH, into long-chain saturated fatty acids. In some cancer cell lines, this protein has been found to be fused with estrogen receptor-alpha (ER-alpha), in which the N-terminus of FAS is fused in-frame with the C-terminus of ER-alpha.<ref name="entrez">{{cite web | title = Entrez Gene: FASN fatty acid synthase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2194| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wakil SJ |title=Fatty acid synthase, a proficient multifunctional enzyme. |journal=Biochemistry |volume=28 |issue= 11 |pages= 4523-30 |year= 1989 |pmid= 2669958 |doi= }}
*{{cite journal | author=Baron A, Migita T, Tang D, Loda M |title=Fatty acid synthase: a metabolic oncogene in prostate cancer? |journal=J. Cell. Biochem. |volume=91 |issue= 1 |pages= 47-53 |year= 2004 |pmid= 14689581 |doi= 10.1002/jcb.10708 }}
*{{cite journal | author=Lejin D |title=[Viscosimetry in clinical practice] |journal=Med. Pregl. |volume=30 |issue= 9-10 |pages= 477-82 |year= 1978 |pmid= 600212 |doi= }}
*{{cite journal | author=Wronkowski Z |title=[Cancer diagnosis of the respiratory system] |journal=Pielȩgniarka i połozna |volume= |issue= 12 |pages= 7-8 |year= 1976 |pmid= 1044453 |doi= }}
*{{cite journal | author=Jayakumar A, Tai MH, Huang WY, ''et al.'' |title=Human fatty acid synthase: properties and molecular cloning. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 19 |pages= 8695-9 |year= 1995 |pmid= 7567999 |doi= }}
*{{cite journal | author=Semenkovich CF, Coleman T, Fiedorek FT |title=Human fatty acid synthase mRNA: tissue distribution, genetic mapping, and kinetics of decay after glucose deprivation. |journal=J. Lipid Res. |volume=36 |issue= 7 |pages= 1507-21 |year= 1995 |pmid= 7595075 |doi= }}
*{{cite journal | author=Jayakumar A, Chirala SS, Chinault AC, ''et al.'' |title=Isolation and chromosomal mapping of genomic clones encoding the human fatty acid synthase gene. |journal=Genomics |volume=23 |issue= 2 |pages= 420-4 |year= 1995 |pmid= 7835891 |doi= 10.1006/geno.1994.1518 }}
*{{cite journal | author=Kuhajda FP, Jenner K, Wood FD, ''et al.'' |title=Fatty acid synthesis: a potential selective target for antineoplastic therapy. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 14 |pages= 6379-83 |year= 1994 |pmid= 8022791 |doi= }}
*{{cite journal | author=Hsu MH, Chirala SS, Wakil SJ |title=Human fatty-acid synthase gene. Evidence for the presence of two promoters and their functional interaction. |journal=J. Biol. Chem. |volume=271 |issue= 23 |pages= 13584-92 |year= 1996 |pmid= 8662758 |doi= }}
*{{cite journal | author=Pizer ES, Kurman RJ, Pasternack GR, Kuhajda FP |title=Expression of fatty acid synthase is closely linked to proliferation and stromal decidualization in cycling endometrium. |journal=Int. J. Gynecol. Pathol. |volume=16 |issue= 1 |pages= 45-51 |year= 1997 |pmid= 8986532 |doi= }}
*{{cite journal | author=Jayakumar A, Chirala SS, Wakil SJ |title=Human fatty acid synthase: assembling recombinant halves of the fatty acid synthase subunit protein reconstitutes enzyme activity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 23 |pages= 12326-30 |year= 1997 |pmid= 9356448 |doi= }}
*{{cite journal | author=Kusakabe T, Maeda M, Hoshi N, ''et al.'' |title=Fatty acid synthase is expressed mainly in adult hormone-sensitive cells or cells with high lipid metabolism and in proliferating fetal cells. |journal=J. Histochem. Cytochem. |volume=48 |issue= 5 |pages= 613-22 |year= 2000 |pmid= 10769045 |doi= }}
*{{cite journal | author=Ye Q, Chung LW, Li S, Zhau HE |title=Identification of a novel FAS/ER-alpha fusion transcript expressed in human cancer cells. |journal=Biochim. Biophys. Acta |volume=1493 |issue= 3 |pages= 373-7 |year= 2000 |pmid= 11018265 |doi= }}
*{{cite journal | author=Rochat-Steiner V, Becker K, Micheau O, ''et al.'' |title=FIST/HIPK3: a Fas/FADD-interacting serine/threonine kinase that induces FADD phosphorylation and inhibits fas-mediated Jun NH(2)-terminal kinase activation. |journal=J. Exp. Med. |volume=192 |issue= 8 |pages= 1165-74 |year= 2000 |pmid= 11034606 |doi= }}
*{{cite journal | author=Chirala SS, Jayakumar A, Gu ZW, Wakil SJ |title=Human fatty acid synthase: role of interdomain in the formation of catalytically active synthase dimer. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 6 |pages= 3104-8 |year= 2001 |pmid= 11248039 |doi= 10.1073/pnas.051635998 }}
*{{cite journal | author=Brink J, Ludtke SJ, Yang CY, ''et al.'' |title=Quaternary structure of human fatty acid synthase by electron cryomicroscopy. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 1 |pages= 138-43 |year= 2002 |pmid= 11756679 |doi= 10.1073/pnas.012589499 }}
*{{cite journal | author=Joseph SB, Laffitte BA, Patel PH, ''et al.'' |title=Direct and indirect mechanisms for regulation of fatty acid synthase gene expression by liver X receptors. |journal=J. Biol. Chem. |volume=277 |issue= 13 |pages= 11019-25 |year= 2002 |pmid= 11790787 |doi= 10.1074/jbc.M111041200 }}
*{{cite journal | author=Ming D, Kong Y, Wakil SJ, ''et al.'' |title=Domain movements in human fatty acid synthase by quantized elastic deformational model. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 12 |pages= 7895-9 |year= 2002 |pmid= 12060737 |doi= 10.1073/pnas.112222299 }}
*{{cite journal | author=Field FJ, Born E, Murthy S, Mathur SN |title=Polyunsaturated fatty acids decrease the expression of sterol regulatory element-binding protein-1 in CaCo-2 cells: effect on fatty acid synthesis and triacylglycerol transport. |journal=Biochem. J. |volume=368 |issue= Pt 3 |pages= 855-64 |year= 2003 |pmid= 12213084 |doi= 10.1042/BJ20020731 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FBLN1... {November 17, 2007 10:50:59 AM PST}
- SEARCH REDIRECT: Control Box Found: FBLN1 {November 17, 2007 10:51:27 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 10:51:30 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 10:51:30 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 10:51:30 AM PST}
- UPDATED: Updated protein page: FBLN1 {November 17, 2007 10:51:36 AM PST}
- INFO: Beginning work on FCGR1A... {November 17, 2007 10:52:40 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:53:16 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Fc fragment of IgG, high affinity Ia, receptor (CD64)
| HGNCid = 3613
| Symbol = FCGR1A
| AltSymbols =; CD64; CD64A; FCRI; IGFR1
| OMIM = 146760
| ECnumber =
| Homologene = 475
| MGIid = 95498
| GeneAtlas_image1 = PBB_GE_FCGR1A_216950_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_FCGR1A_214511_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005057 |text = receptor signaling protein activity}} {{GNF_GO|id=GO:0019864 |text = IgG binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006911 |text = phagocytosis, engulfment}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2209
| Hs_Ensembl = ENSG00000150337
| Hs_RefseqProtein = NP_000557
| Hs_RefseqmRNA = NM_000566
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 148020870
| Hs_GenLoc_end = 148030698
| Hs_Uniprot = P12314
| Mm_EntrezGene = 14129
| Mm_Ensembl = ENSMUSG00000015947
| Mm_RefseqmRNA = NM_010186
| Mm_RefseqProtein = NP_034316
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 96368314
| Mm_GenLoc_end = 96379374
| Mm_Uniprot = P26151
}}
}}
'''Fc fragment of IgG, high affinity Ia, receptor (CD64)''', also known as '''FCGR1A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FCGR1A Fc fragment of IgG, high affinity Ia, receptor (CD64)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2209| 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=Monteiro RC, Van De Winkel JG |title=IgA Fc receptors. |journal=Annu. Rev. Immunol. |volume=21 |issue= |pages= 177-204 |year= 2003 |pmid= 12524384 |doi= 10.1146/annurev.immunol.21.120601.141011 }}
*{{cite journal | author=Ernst LK, van de Winkel JG, Chiu IM, Anderson CL |title=Three genes for the human high affinity Fc receptor for IgG (Fc gamma RI) encode four distinct transcription products. |journal=J. Biol. Chem. |volume=267 |issue= 22 |pages= 15692-700 |year= 1992 |pmid= 1379234 |doi= }}
*{{cite journal | author=Benech PD, Sastry K, Iyer RR, ''et al.'' |title=Definition of interferon gamma-response elements in a novel human Fc gamma receptor gene (Fc gamma RIb) and characterization of the gene structure. |journal=J. Exp. Med. |volume=176 |issue= 4 |pages= 1115-23 |year= 1992 |pmid= 1402657 |doi= }}
*{{cite journal | author=Porges AJ, Redecha PB, Doebele R, ''et al.'' |title=Novel Fc gamma receptor I family gene products in human mononuclear cells. |journal=J. Clin. Invest. |volume=90 |issue= 5 |pages= 2102-9 |year= 1992 |pmid= 1430234 |doi= }}
*{{cite journal | author=van de Winkel JG, Ernst LK, Anderson CL, Chiu IM |title=Gene organization of the human high affinity receptor for IgG, Fc gamma RI (CD64). Characterization and evidence for a second gene. |journal=J. Biol. Chem. |volume=266 |issue= 20 |pages= 13449-55 |year= 1991 |pmid= 1830050 |doi= }}
*{{cite journal | author=Eizuru Y, Minamishima Y |title=Induction of Fc (IgG) receptor(s) by simian cytomegaloviruses in human embryonic lung fibroblasts. |journal=Intervirology |volume=29 |issue= 6 |pages= 339-45 |year= 1989 |pmid= 2852656 |doi= }}
*{{cite journal | author=Allen JM, Seed B |title=Isolation and expression of functional high-affinity Fc receptor complementary DNAs. |journal=Science |volume=243 |issue= 4889 |pages= 378-81 |year= 1989 |pmid= 2911749 |doi= }}
*{{cite journal | author=Allen JM, Seed B |title=Nucleotide sequence of three cDNAs for the human high affinity Fc receptor (FcRI). |journal=Nucleic Acids Res. |volume=16 |issue= 24 |pages= 11824 |year= 1989 |pmid= 2974947 |doi= }}
*{{cite journal | author=Indik ZK, Hunter S, Huang MM, ''et al.'' |title=The high affinity Fc gamma receptor (CD64) induces phagocytosis in the absence of its cytoplasmic domain: the gamma subunit of Fc gamma RIIIA imparts phagocytic function to Fc gamma RI. |journal=Exp. Hematol. |volume=22 |issue= 7 |pages= 599-606 |year= 1994 |pmid= 7516890 |doi= }}
*{{cite journal | author=Valerius T, Repp R, de Wit TP, ''et al.'' |title=Involvement of the high-affinity receptor for IgG (Fc gamma RI; CD64) in enhanced tumor cell cytotoxicity of neutrophils during granulocyte colony-stimulating factor therapy. |journal=Blood |volume=82 |issue= 3 |pages= 931-9 |year= 1993 |pmid= 7687898 |doi= }}
*{{cite journal | author=Wang AV, Scholl PR, Geha RS |title=Physical and functional association of the high affinity immunoglobulin G receptor (Fc gamma RI) with the kinases Hck and Lyn. |journal=J. Exp. Med. |volume=180 |issue= 3 |pages= 1165-70 |year= 1994 |pmid= 8064233 |doi= }}
*{{cite journal | author=Takai S, Kasama M, Yamada K, ''et al.'' |title=Human high-affinity Fc gamma RI (CD64) gene mapped to chromosome 1q21.2-q21.3 by fluorescence in situ hybridization. |journal=Hum. Genet. |volume=93 |issue= 1 |pages= 13-5 |year= 1994 |pmid= 8270248 |doi= }}
*{{cite journal | author=Morton HC, van den Herik-Oudijk IE, Vossebeld P, ''et al.'' |title=Functional association between the human myeloid immunoglobulin A Fc receptor (CD89) and FcR gamma chain. Molecular basis for CD89/FcR gamma chain association. |journal=J. Biol. Chem. |volume=270 |issue= 50 |pages= 29781-7 |year= 1996 |pmid= 8530370 |doi= }}
*{{cite journal | author=Maresco DL, Chang E, Theil KS, ''et al.'' |title=The three genes of the human FCGR1 gene family encoding Fc gamma RI flank the centromere of chromosome 1 at 1p12 and 1q21. |journal=Cytogenet. Cell Genet. |volume=73 |issue= 3 |pages= 157-63 |year= 1996 |pmid= 8697799 |doi= }}
*{{cite journal | author=De SK, Venkateshan CN, Seth P, ''et al.'' |title=Adenovirus-mediated human immunodeficiency virus-1 Nef expression in human monocytes/macrophages and effect of Nef on downmodulation of Fcgamma receptors and expression of monokines. |journal=Blood |volume=91 |issue= 6 |pages= 2108-17 |year= 1998 |pmid= 9490697 |doi= }}
*{{cite journal | author=Maresco DL, Blue LE, Culley LL, ''et al.'' |title=Localization of FCGR1 encoding Fcgamma receptor class I in primates: molecular evidence for two pericentric inversions during the evolution of human chromosome 1. |journal=Cytogenet. Cell Genet. |volume=82 |issue= 1-2 |pages= 71-4 |year= 1998 |pmid= 9763663 |doi= }}
*{{cite journal | author=Kyono WT, de Jong R, Park RK, ''et al.'' |title=Differential interaction of Crkl with Cbl or C3G, Hef-1, and gamma subunit immunoreceptor tyrosine-based activation motif in signaling of myeloid high affinity Fc receptor for IgG (Fc gamma RI). |journal=J. Immunol. |volume=161 |issue= 10 |pages= 5555-63 |year= 1998 |pmid= 9820532 |doi= }}
*{{cite journal | author=Fanger NA, Cosman D, Peterson L, ''et al.'' |title=The MHC class I binding proteins LIR-1 and LIR-2 inhibit Fc receptor-mediated signaling in monocytes. |journal=Eur. J. Immunol. |volume=28 |issue= 11 |pages= 3423-34 |year= 1998 |pmid= 9842885 |doi= }}
*{{cite journal | author=Gorgani NN, Altin JG, Parish CR |title=Histidine-rich glycoprotein regulates the binding of monomeric IgG and immune complexes to monocytes. |journal=Int. Immunol. |volume=11 |issue= 8 |pages= 1275-82 |year= 1999 |pmid= 10421785 |doi= }}
*{{cite journal | author=Tridandapani S, Lyden TW, Smith JL, ''et al.'' |title=The adapter protein LAT enhances fcgamma receptor-mediated signal transduction in myeloid cells. |journal=J. Biol. Chem. |volume=275 |issue= 27 |pages= 20480-7 |year= 2000 |pmid= 10781611 |doi= 10.1074/jbc.M909462199 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FECH... {November 17, 2007 10:53:16 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:53:43 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_FECH_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hrk.
| PDB = {{PDB2|1hrk}}, {{PDB2|2hrc}}, {{PDB2|2hre}}
| Name = Ferrochelatase (protoporphyria)
| HGNCid = 3647
| Symbol = FECH
| AltSymbols =; EPP; FCE
| OMIM = 177000
| ECnumber =
| Homologene = 113
| MGIid = 95513
| GeneAtlas_image1 = PBB_GE_FECH_203116_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_FECH_203115_at_tn.png
| Function = {{GNF_GO|id=GO:0004325 |text = ferrochelatase activity}} {{GNF_GO|id=GO:0008198 |text = ferrous iron binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0051537 |text = 2 iron, 2 sulfur cluster binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}}
| Process = {{GNF_GO|id=GO:0006091 |text = generation of precursor metabolites and energy}} {{GNF_GO|id=GO:0006783 |text = heme biosynthetic process}} {{GNF_GO|id=GO:0009416 |text = response to light stimulus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2235
| Hs_Ensembl = ENSG00000066926
| Hs_RefseqProtein = NP_000131
| Hs_RefseqmRNA = NM_000140
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 18
| Hs_GenLoc_start = 53366535
| Hs_GenLoc_end = 53404988
| Hs_Uniprot = P22830
| Mm_EntrezGene = 14151
| Mm_Ensembl = ENSMUSG00000024588
| Mm_RefseqmRNA = XM_001000060
| Mm_RefseqProtein = XP_001000060
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 18
| Mm_GenLoc_start = 64581919
| Mm_GenLoc_end = 64614435
| Mm_Uniprot = Q3UC49
}}
}}
'''Ferrochelatase (protoporphyria)''', also known as '''FECH''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FECH ferrochelatase (protoporphyria)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2235| 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 = Ferrochelatase is localized to the mitochondrion where it catalyzes the insertion of the ferrous form of iron into protoporphyrin IX in the heme synthesis pathway. Defects in ferrochelatase are associated with protoporphyria. Two transcript variants encoding different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: FECH ferrochelatase (protoporphyria)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2235| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Cox TM |title=Erythropoietic protoporphyria. |journal=J. Inherit. Metab. Dis. |volume=20 |issue= 2 |pages= 258-69 |year= 1997 |pmid= 9211198 |doi= }}
*{{cite journal | author=Buller RE, Schrader WT, O'Maller BW |title=Steroids and the practical aspects of performing binding studies. |journal=J. Steroid Biochem. |volume=7 |issue= 5 |pages= 321-6 |year= 1976 |pmid= 180343 |doi= }}
*{{cite journal | author=Bonkowsky HL, Bloomer JR, Ebert PS, Mahoney MJ |title=Heme synthetase deficiency in human protoporphyria. Demonstration of the defect in liver and cultured skin fibroblasts. |journal=J. Clin. Invest. |volume=56 |issue= 5 |pages= 1139-48 |year= 1976 |pmid= 1184741 |doi= }}
*{{cite journal | author=Brenner DA, Didier JM, Frasier F, ''et al.'' |title=A molecular defect in human protoporphyria. |journal=Am. J. Hum. Genet. |volume=50 |issue= 6 |pages= 1203-10 |year= 1992 |pmid= 1376018 |doi= }}
*{{cite journal | author=Nakahashi Y, Fujita H, Taketani S, ''et al.'' |title=The molecular defect of ferrochelatase in a patient with erythropoietic protoporphyria. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 1 |pages= 281-5 |year= 1992 |pmid= 1729699 |doi= }}
*{{cite journal | author=Lamoril J, Boulechfar S, de Verneuil H, ''et al.'' |title=Human erythropoietic protoporphyria: two point mutations in the ferrochelatase gene. |journal=Biochem. Biophys. Res. Commun. |volume=181 |issue= 2 |pages= 594-9 |year= 1992 |pmid= 1755842 |doi= }}
*{{cite journal | author=Diep A, Li C, Klisak I, ''et al.'' |title=Assignment of the gene for cyclic AMP-response element binding protein 2 (CREB2) to human chromosome 2q24.1-q32. |journal=Genomics |volume=11 |issue= 4 |pages= 1161-3 |year= 1992 |pmid= 1838349 |doi= }}
*{{cite journal | author=Nakahashi Y, Taketani S, Okuda M, ''et al.'' |title=Molecular cloning and sequence analysis of cDNA encoding human ferrochelatase. |journal=Biochem. Biophys. Res. Commun. |volume=173 |issue= 2 |pages= 748-55 |year= 1991 |pmid= 2260980 |doi= }}
*{{cite journal | author=Rossi E, Attwood PV, Garcia-Webb P, Costin KA |title=Inhibition of human lymphocyte ferrochelatase activity by hemin. |journal=Biochim. Biophys. Acta |volume=1038 |issue= 3 |pages= 375-81 |year= 1990 |pmid= 2340297 |doi= }}
*{{cite journal | author=Polson RJ, Lim CK, Rolles K, ''et al.'' |title=The effect of liver transplantation in a 13-year-old boy with erythropoietic protoporphyria. |journal=Transplantation |volume=46 |issue= 3 |pages= 386-9 |year= 1988 |pmid= 3047929 |doi= }}
*{{cite journal | author=Bonkovsky HL, Schned AR |title=Fatal liver failure in protoporphyria. Synergism between ethanol excess and the genetic defect. |journal=Gastroenterology |volume=90 |issue= 1 |pages= 191-201 |year= 1986 |pmid= 3940245 |doi= }}
*{{cite journal | author=Prasad AR, Dailey HA |title=Effect of cellular location on the function of ferrochelatase. |journal=J. Biol. Chem. |volume=270 |issue= 31 |pages= 18198-200 |year= 1995 |pmid= 7629135 |doi= }}
*{{cite journal | author=Sarkany RP, Alexander GJ, Cox TM |title=Recessive inheritance of erythropoietic protoporphyria with liver failure. |journal=Lancet |volume=343 |issue= 8910 |pages= 1394-6 |year= 1994 |pmid= 7910885 |doi= }}
*{{cite journal | author=Tugores A, Magness ST, Brenner DA |title=A single promoter directs both housekeeping and erythroid preferential expression of the human ferrochelatase gene. |journal=J. Biol. Chem. |volume=269 |issue= 49 |pages= 30789-97 |year= 1995 |pmid= 7983009 |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=Dailey HA, Sellers VM, Dailey TA |title=Mammalian ferrochelatase. Expression and characterization of normal and two human protoporphyric ferrochelatases. |journal=J. Biol. Chem. |volume=269 |issue= 1 |pages= 390-5 |year= 1994 |pmid= 8276824 |doi= }}
*{{cite journal | author=Wang X, Poh-Fitzpatrick M, Carriero D, ''et al.'' |title=A novel mutation in erythropoietic protoporphyria: an aberrant ferrochelatase mRNA caused by exon skipping during RNA splicing. |journal=Biochim. Biophys. Acta |volume=1181 |issue= 2 |pages= 198-200 |year= 1993 |pmid= 8481408 |doi= }}
*{{cite journal | author=Nakahashi Y, Miyazaki H, Kadota Y, ''et al.'' |title=Molecular defect in human erythropoietic protoporphyria with fatal liver failure. |journal=Hum. Genet. |volume=91 |issue= 4 |pages= 303-6 |year= 1993 |pmid= 8500787 |doi= }}
*{{cite journal | author=Imoto S, Tanizawa Y, Sato Y, ''et al.'' |title=A novel mutation in the ferrochelatase gene associated with erythropoietic protoporphyria. |journal=Br. J. Haematol. |volume=94 |issue= 1 |pages= 191-7 |year= 1996 |pmid= 8757534 |doi= }}
*{{cite journal | author=Crouse BR, Sellers VM, Finnegan MG, ''et al.'' |title=Site-directed mutagenesis and spectroscopic characterization of human ferrochelatase: identification of residues coordinating the [2Fe-2S] cluster. |journal=Biochemistry |volume=35 |issue= 50 |pages= 16222-9 |year= 1997 |pmid= 8973195 |doi= 10.1021/bi9620114 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GGA1... {November 17, 2007 11:03:59 AM PST}
- SEARCH REDIRECT: Control Box Found: GGA1 {November 17, 2007 11:04:23 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:04:24 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:04:24 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:04:24 AM PST}
- UPDATED: Updated protein page: GGA1 {November 17, 2007 11:04:32 AM PST}
- INFO: Beginning work on GNAI3... {November 17, 2007 10:53:43 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:54:17 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_GNAI3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1agr.
| PDB = {{PDB2|1agr}}, {{PDB2|1as0}}, {{PDB2|1as2}}, {{PDB2|1as3}}, {{PDB2|1bh2}}, {{PDB2|1bof}}, {{PDB2|1cip}}, {{PDB2|1gdd}}, {{PDB2|1gfi}}, {{PDB2|1gg2}}, {{PDB2|1gia}}, {{PDB2|1gil}}, {{PDB2|1git}}, {{PDB2|1gp2}}, {{PDB2|1kjy}}, {{PDB2|1svk}}, {{PDB2|1svs}}, {{PDB2|1y3a}}, {{PDB2|2g83}}, {{PDB2|2gtp}}, {{PDB2|2hlb}}, {{PDB2|2ihb}}, {{PDB2|2ik8}}, {{PDB2|2ode}}
| Name = Guanine nucleotide binding protein (G protein), alpha inhibiting activity polypeptide 3
| HGNCid = 4387
| Symbol = GNAI3
| AltSymbols =; 87U6; FLJ26559
| OMIM = 139370
| ECnumber =
| Homologene = 55975
| MGIid = 95773
| GeneAtlas_image1 = PBB_GE_GNAI3_201180_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_GNAI3_201179_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_GNAI3_201181_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:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007194 |text = negative regulation of adenylate cyclase activity}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2773
| Hs_Ensembl = ENSG00000065135
| Hs_RefseqProtein = NP_006487
| Hs_RefseqmRNA = NM_006496
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 109892756
| Hs_GenLoc_end = 109938498
| Hs_Uniprot = P08754
| Mm_EntrezGene = 14679
| Mm_Ensembl = ENSMUSG00000000001
| Mm_RefseqmRNA = NM_010306
| Mm_RefseqProtein = NP_034436
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 108235337
| Mm_GenLoc_end = 108274202
| Mm_Uniprot = Q3TJH1
}}
}}
'''Guanine nucleotide binding protein (G protein), alpha inhibiting activity polypeptide 3''', also known as '''GNAI3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GNAI3 guanine nucleotide binding protein (G protein), alpha inhibiting activity polypeptide 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2773| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Downes GB, Gautam N |title=The G protein subunit gene families. |journal=Genomics |volume=62 |issue= 3 |pages= 544-52 |year= 2000 |pmid= 10644457 |doi= 10.1006/geno.1999.5992 }}
*{{cite journal | author=Sidhu A, Niznik HB |title=Coupling of dopamine receptor subtypes to multiple and diverse G proteins. |journal=Int. J. Dev. Neurosci. |volume=18 |issue= 7 |pages= 669-77 |year= 2000 |pmid= 10978845 |doi= }}
*{{cite journal | author=Jiang M, Pandey S, Tran VT, Fong HK |title=Guanine nucleotide-binding regulatory proteins in retinal pigment epithelial cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 9 |pages= 3907-11 |year= 1991 |pmid= 1902575 |doi= }}
*{{cite journal | author=Carty DJ, Padrell E, Codina J, ''et al.'' |title=Distinct guanine nucleotide binding and release properties of the three Gi proteins. |journal=J. Biol. Chem. |volume=265 |issue= 11 |pages= 6268-73 |year= 1990 |pmid= 2108158 |doi= }}
*{{cite journal | author=Suki WN, Abramowitz J, Mattera R, ''et al.'' |title=The human genome encodes at least three non-allellic G proteins with alpha i-type subunits. |journal=FEBS Lett. |volume=220 |issue= 1 |pages= 187-92 |year= 1987 |pmid= 2440724 |doi= }}
*{{cite journal | author=Codina J, Olate J, Abramowitz J, ''et al.'' |title=Alpha i-3 cDNA encodes the alpha subunit of Gk, the stimulatory G protein of receptor-regulated K+ channels. |journal=J. Biol. Chem. |volume=263 |issue= 14 |pages= 6746-50 |year= 1988 |pmid= 2452165 |doi= }}
*{{cite journal | author=Itoh H, Toyama R, Kozasa T, ''et al.'' |title=Presence of three distinct molecular species of Gi protein alpha subunit. Structure of rat cDNAs and human genomic DNAs. |journal=J. Biol. Chem. |volume=263 |issue= 14 |pages= 6656-64 |year= 1988 |pmid= 2834384 |doi= }}
*{{cite journal | author=Didsbury JR, Snyderman R |title=Molecular cloning of a new human G protein. Evidence for two Gi alpha-like protein families. |journal=FEBS Lett. |volume=219 |issue= 1 |pages= 259-63 |year= 1987 |pmid= 3109953 |doi= }}
*{{cite journal | author=Beals CR, Wilson CB, Perlmutter RM |title=A small multigene family encodes Gi signal-transduction proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 22 |pages= 7886-90 |year= 1987 |pmid= 3120178 |doi= }}
*{{cite journal | author=Kim SY, Ang SL, Bloch DB, ''et al.'' |title=Identification of cDNA encoding an additional alpha subunit of a human GTP-binding protein: expression of three alpha i subtypes in human tissues and cell lines. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 12 |pages= 4153-7 |year= 1988 |pmid= 3132707 |doi= }}
*{{cite journal | author=Migeon JC, Thomas SL, Nathanson NM |title=Differential coupling of m2 and m4 muscarinic receptors to inhibition of adenylyl cyclase by Gi alpha and G(o)alpha subunits. |journal=J. Biol. Chem. |volume=270 |issue= 27 |pages= 16070-4 |year= 1995 |pmid= 7608168 |doi= }}
*{{cite journal | author=Raymond JR, Olsen CL, Gettys TW |title=Cell-specific physical and functional coupling of human 5-HT1A receptors to inhibitory G protein alpha-subunits and lack of coupling to Gs alpha. |journal=Biochemistry |volume=32 |issue= 41 |pages= 11064-73 |year= 1993 |pmid= 8218170 |doi= }}
*{{cite journal | author=Wu D, LaRosa GJ, Simon MI |title=G protein-coupled signal transduction pathways for interleukin-8. |journal=Science |volume=261 |issue= 5117 |pages= 101-3 |year= 1993 |pmid= 8316840 |doi= }}
*{{cite journal | author=Europe-Finner GN, Phaneuf S, Watson SP, López Bernal A |title=Identification and expression of G-proteins in human myometrium: up-regulation of G alpha s in pregnancy. |journal=Endocrinology |volume=132 |issue= 6 |pages= 2484-90 |year= 1993 |pmid= 8504751 |doi= }}
*{{cite journal | author=De Vries L, Mousli M, Wurmser A, Farquhar MG |title=GAIP, a protein that specifically interacts with the trimeric G protein G alpha i3, is a member of a protein family with a highly conserved core domain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 25 |pages= 11916-20 |year= 1996 |pmid= 8524874 |doi= }}
*{{cite journal | author=Laugwitz KL, Allgeier A, Offermanns S, ''et al.'' |title=The human thyrotropin receptor: a heptahelical receptor capable of stimulating members of all four G protein families. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 1 |pages= 116-20 |year= 1996 |pmid= 8552586 |doi= }}
*{{cite journal | author=Lee MJ, Evans M, Hla T |title=The inducible G protein-coupled receptor edg-1 signals via the G(i)/mitogen-activated protein kinase pathway. |journal=J. Biol. Chem. |volume=271 |issue= 19 |pages= 11272-9 |year= 1996 |pmid= 8626678 |doi= }}
*{{cite journal | author=Solomon KR, Rudd CE, Finberg RW |title=The association between glycosylphosphatidylinositol-anchored proteins and heterotrimeric G protein alpha subunits in lymphocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 12 |pages= 6053-8 |year= 1996 |pmid= 8650218 |doi= }}
*{{cite journal | author=Zhang J, Pratt RE |title=The AT2 receptor selectively associates with Gialpha2 and Gialpha3 in the rat fetus. |journal=J. Biol. Chem. |volume=271 |issue= 25 |pages= 15026-33 |year= 1996 |pmid= 8663053 |doi= }}
*{{cite journal | author=Hunt TW, Fields TA, Casey PJ, Peralta EG |title=RGS10 is a selective activator of G alpha i GTPase activity. |journal=Nature |volume=383 |issue= 6596 |pages= 175-7 |year= 1996 |pmid= 8774883 |doi= 10.1038/383175a0 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MAP2... {November 17, 2007 10:55:40 AM PST}
- SEARCH REDIRECT: Control Box Found: MAP2 {November 17, 2007 10:56:21 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 10:56:23 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 10:56:23 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 10:56:23 AM PST}
- UPDATED: Updated protein page: MAP2 {November 17, 2007 10:56:29 AM PST}
- INFO: Beginning work on MYO7A... {November 17, 2007 10:56:29 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:57:01 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 = Myosin VIIA
| HGNCid = 7606
| Symbol = MYO7A
| AltSymbols =; DFNA11; DFNB2; MYU7A; NSRD2; USH1B
| OMIM = 276903
| ECnumber =
| Homologene = 219
| MGIid = 104510
| Function = {{GNF_GO|id=GO:0000146 |text = microfilament motor activity}} {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005488 |text = binding}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0046983 |text = protein dimerization activity}}
| Component = {{GNF_GO|id=GO:0001750 |text = photoreceptor outer segment}} {{GNF_GO|id=GO:0001917 |text = photoreceptor inner segment}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005765 |text = lysosomal membrane}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005929 |text = cilium}} {{GNF_GO|id=GO:0016324 |text = apical plasma membrane}} {{GNF_GO|id=GO:0016459 |text = myosin complex}} {{GNF_GO|id=GO:0042470 |text = melanosome}} {{GNF_GO|id=GO:0045202 |text = synapse}}
| Process = {{GNF_GO|id=GO:0001845 |text = phagolysosome formation}} {{GNF_GO|id=GO:0007040 |text = lysosome organization and biogenesis}} {{GNF_GO|id=GO:0007601 |text = visual perception}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0030030 |text = cell projection organization and biogenesis}} {{GNF_GO|id=GO:0030048 |text = actin filament-based movement}} {{GNF_GO|id=GO:0035058 |text = sensory cilium biogenesis}} {{GNF_GO|id=GO:0042472 |text = inner ear morphogenesis}} {{GNF_GO|id=GO:0042491 |text = auditory receptor cell differentiation}} {{GNF_GO|id=GO:0048563 |text = post-embryonic organ morphogenesis}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}} {{GNF_GO|id=GO:0051875 |text = pigment granule localization}} {{GNF_GO|id=GO:0051904 |text = pigment granule transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4647
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000251
| Hs_RefseqmRNA = NM_000260
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 17921
| Mm_Ensembl = ENSMUSG00000030761
| Mm_RefseqmRNA = NM_008663
| Mm_RefseqProtein = NP_032689
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 97926593
| Mm_GenLoc_end = 97984444
| Mm_Uniprot = P97479
}}
}}
'''Myosin VIIA''', also known as '''MYO7A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MYO7A myosin VIIA| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4647| 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=Wolfrum U |title=The cellular function of the usher gene product myosin VIIa is specified by its ligands. |journal=Adv. Exp. Med. Biol. |volume=533 |issue= |pages= 133-42 |year= 2004 |pmid= 15180257 |doi= }}
*{{cite journal | author=Kimberling WJ, Möller CG, Davenport S, ''et al.'' |title=Linkage of Usher syndrome type I gene (USH1B) to the long arm of chromosome 11. |journal=Genomics |volume=14 |issue= 4 |pages= 988-94 |year= 1993 |pmid= 1478677 |doi= }}
*{{cite journal | author=Hasson T, Heintzelman MB, Santos-Sacchi J, ''et al.'' |title=Expression in cochlea and retina of myosin VIIa, the gene product defective in Usher syndrome type 1B. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 21 |pages= 9815-9 |year= 1995 |pmid= 7568224 |doi= }}
*{{cite journal | author=Weil D, Blanchard S, Kaplan J, ''et al.'' |title=Defective myosin VIIA gene responsible for Usher syndrome type 1B. |journal=Nature |volume=374 |issue= 6517 |pages= 60-1 |year= 1995 |pmid= 7870171 |doi= 10.1038/374060a0 }}
*{{cite journal | author=Guilford P, Ayadi H, Blanchard S, ''et al.'' |title=A human gene responsible for neurosensory, non-syndromic recessive deafness is a candidate homologue of the mouse sh-1 gene. |journal=Hum. Mol. Genet. |volume=3 |issue= 6 |pages= 989-93 |year= 1994 |pmid= 7951250 |doi= }}
*{{cite journal | author=Bement WM, Hasson T, Wirth JA, ''et al.'' |title=Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 14 |pages= 6549-53 |year= 1994 |pmid= 8022818 |doi= }}
*{{cite journal | author=Wagenaar M, ter Rahe B, van Aarem A, ''et al.'' |title=Clinical findings in obligate carriers of type I Usher syndrome. |journal=Am. J. Med. Genet. |volume=59 |issue= 3 |pages= 375-9 |year= 1996 |pmid= 8599365 |doi= 10.1002/ajmg.1320590319 }}
*{{cite journal | author=Weil D, Levy G, Sahly I, ''et al.'' |title=Human myosin VIIA responsible for the Usher 1B syndrome: a predicted membrane-associated motor protein expressed in developing sensory epithelia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 8 |pages= 3232-7 |year= 1996 |pmid= 8622919 |doi= }}
*{{cite journal | author=Tamagawa Y, Kitamura K, Ishida T, ''et al.'' |title=A gene for a dominant form of non-syndromic sensorineural deafness (DFNA11) maps within the region containing the DFNB2 recessive deafness gene. |journal=Hum. Mol. Genet. |volume=5 |issue= 6 |pages= 849-52 |year= 1996 |pmid= 8776602 |doi= }}
*{{cite journal | author=el-Amraoui A, Sahly I, Picaud S, ''et al.'' |title=Human Usher 1B/mouse shaker-1: the retinal phenotype discrepancy explained by the presence/absence of myosin VIIA in the photoreceptor cells. |journal=Hum. Mol. Genet. |volume=5 |issue= 8 |pages= 1171-8 |year= 1997 |pmid= 8842737 |doi= }}
*{{cite journal | author=Hasson T, Skowron JF, Gilbert DJ, ''et al.'' |title=Mapping of unconventional myosins in mouse and human. |journal=Genomics |volume=36 |issue= 3 |pages= 431-9 |year= 1997 |pmid= 8884266 |doi= 10.1006/geno.1996.0488 }}
*{{cite journal | author=Chen ZY, Hasson T, Kelley PM, ''et al.'' |title=Molecular cloning and domain structure of human myosin-VIIa, the gene product defective in Usher syndrome 1B. |journal=Genomics |volume=36 |issue= 3 |pages= 440-8 |year= 1997 |pmid= 8884267 |doi= 10.1006/geno.1996.0489 }}
*{{cite journal | author=Weston MD, Kelley PM, Overbeck LD, ''et al.'' |title=Myosin VIIA mutation screening in 189 Usher syndrome type 1 patients. |journal=Am. J. Hum. Genet. |volume=59 |issue= 5 |pages= 1074-83 |year= 1996 |pmid= 8900236 |doi= }}
*{{cite journal | author=Lévy G, Levi-Acobas F, Blanchard S, ''et al.'' |title=Myosin VIIA gene: heterogeneity of the mutations responsible for Usher syndrome type IB. |journal=Hum. Mol. Genet. |volume=6 |issue= 1 |pages= 111-6 |year= 1997 |pmid= 9002678 |doi= }}
*{{cite journal | author=Kelley PM, Weston MD, Chen ZY, ''et al.'' |title=The genomic structure of the gene defective in Usher syndrome type Ib (MYO7A). |journal=Genomics |volume=40 |issue= 1 |pages= 73-9 |year= 1997 |pmid= 9070921 |doi= 10.1006/geno.1996.4545 }}
*{{cite journal | author=Liu XZ, Walsh J, Mburu P, ''et al.'' |title=Mutations in the myosin VIIA gene cause non-syndromic recessive deafness. |journal=Nat. Genet. |volume=16 |issue= 2 |pages= 188-90 |year= 1997 |pmid= 9171832 |doi= 10.1038/ng0697-188 }}
*{{cite journal | author=Weil D, Küssel P, Blanchard S, ''et al.'' |title=The autosomal recessive isolated deafness, DFNB2, and the Usher 1B syndrome are allelic defects of the myosin-VIIA gene. |journal=Nat. Genet. |volume=16 |issue= 2 |pages= 191-3 |year= 1997 |pmid= 9171833 |doi= 10.1038/ng0697-191 }}
*{{cite journal | author=Liu XZ, Walsh J, Tamagawa Y, ''et al.'' |title=Autosomal dominant non-syndromic deafness caused by a mutation in the myosin VIIA gene. |journal=Nat. Genet. |volume=17 |issue= 3 |pages= 268-9 |year= 1997 |pmid= 9354784 |doi= 10.1038/ng1197-268 }}
*{{cite journal | author=Adato A, Weil D, Kalinski H, ''et al.'' |title=Mutation profile of all 49 exons of the human myosin VIIA gene, and haplotype analysis, in Usher 1B families from diverse origins. |journal=Am. J. Hum. Genet. |volume=61 |issue= 4 |pages= 813-21 |year= 1997 |pmid= 9382091 |doi= }}
*{{cite journal | author=Liu XZ, Hope C, Walsh J, ''et al.'' |title=Mutations in the myosin VIIA gene cause a wide phenotypic spectrum, including atypical Usher syndrome. |journal=Am. J. Hum. Genet. |volume=63 |issue= 3 |pages= 909-12 |year= 1998 |pmid= 9718356 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NR4A2... {November 17, 2007 10:57:01 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:57:41 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_NR4A2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cit.
| PDB = {{PDB2|1cit}}, {{PDB2|1ovl}}
| Name = Nuclear receptor subfamily 4, group A, member 2
| HGNCid = 7981
| Symbol = NR4A2
| AltSymbols =; RNR1; HZF-3; NOT; NURR1; TINUR
| OMIM = 601828
| ECnumber =
| Homologene = 4509
| MGIid = 1352456
| GeneAtlas_image1 = PBB_GE_NR4A2_216248_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_NR4A2_204621_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_NR4A2_204622_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003707 |text = steroid hormone receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0019735 |text = antimicrobial humoral response}} {{GNF_GO|id=GO:0030182 |text = neuron differentiation}} {{GNF_GO|id=GO:0042053 |text = regulation of dopamine metabolic process}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4929
| Hs_Ensembl = ENSG00000153234
| Hs_RefseqProtein = NP_006177
| Hs_RefseqmRNA = NM_006186
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 156889194
| Hs_GenLoc_end = 156897474
| Hs_Uniprot = P43354
| Mm_EntrezGene = 18227
| Mm_Ensembl = ENSMUSG00000026826
| Mm_RefseqmRNA = NM_013613
| Mm_RefseqProtein = NP_038641
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 56922903
| Mm_GenLoc_end = 56939527
| Mm_Uniprot = Q3TYI4
}}
}}
'''Nuclear receptor subfamily 4, group A, member 2''', also known as '''NR4A2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NR4A2 nuclear receptor subfamily 4, group A, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4929| 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 steroid-thyroid hormone-retinoid receptor superfamily. The encoded protein may act as a transcription factor. Mutations in this gene have been associated with disorders related to dopaminergic dysfunction, including Parkinson disease, schizophernia, and manic depression. Misregulation of this gene may be associated with rheumatoid arthritis. Four transcript variants encoding four distinct isoforms have been identified for this gene. Additional alternate splice variants may exist, but their full length nature has not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: NR4A2 nuclear receptor subfamily 4, group A, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4929| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Le W, Appel SH |title=Mutant genes responsible for Parkinson's disease. |journal=Current opinion in pharmacology |volume=4 |issue= 1 |pages= 79-84 |year= 2004 |pmid= 15018843 |doi= 10.1016/j.coph.2003.09.005 }}
*{{cite journal | author=Wedler B, Wüstenberg PW, Naumann G |title=[Treatment of hypertonus in diabetes mellitus] |journal=Zeitschrift für die gesamte innere Medizin und ihre Grenzgebiete |volume=30 |issue= 13 |pages= 437-42 |year= 1976 |pmid= 4929 |doi= }}
*{{cite journal | author=Perlmann T, Jansson L |title=A novel pathway for vitamin A signaling mediated by RXR heterodimerization with NGFI-B and NURR1. |journal=Genes Dev. |volume=9 |issue= 7 |pages= 769-82 |year= 1995 |pmid= 7705655 |doi= }}
*{{cite journal | author=Okabe T, Takayanagi R, Imasaki K, ''et al.'' |title=cDNA cloning of a NGFI-B/nur77-related transcription factor from an apoptotic human T cell line. |journal=J. Immunol. |volume=154 |issue= 8 |pages= 3871-9 |year= 1995 |pmid= 7706727 |doi= }}
*{{cite journal | author=Forman BM, Umesono K, Chen J, Evans RM |title=Unique response pathways are established by allosteric interactions among nuclear hormone receptors. |journal=Cell |volume=81 |issue= 4 |pages= 541-50 |year= 1995 |pmid= 7758108 |doi= }}
*{{cite journal | author=Mages HW, Rilke O, Bravo R, ''et al.'' |title=NOT, a human immediate-early response gene closely related to the steroid/thyroid hormone receptor NAK1/TR3. |journal=Mol. Endocrinol. |volume=8 |issue= 11 |pages= 1583-91 |year= 1995 |pmid= 7877627 |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=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=Torii T, Kawarai T, Nakamura S, Kawakami H |title=Organization of the human orphan nuclear receptor Nurr1 gene. |journal=Gene |volume=230 |issue= 2 |pages= 225-32 |year= 1999 |pmid= 10216261 |doi= }}
*{{cite journal | author=Ichinose H, Ohye T, Suzuki T, ''et al.'' |title=Molecular cloning of the human Nurr1 gene: characterization of the human gene and cDNAs. |journal=Gene |volume=230 |issue= 2 |pages= 233-9 |year= 1999 |pmid= 10216262 |doi= }}
*{{cite journal | author=Chen YH, Tsai MT, Shaw CK, Chen CH |title=Mutation analysis of the human NR4A2 gene, an essential gene for midbrain dopaminergic neurogenesis, in schizophrenic patients. |journal=Am. J. Med. Genet. |volume=105 |issue= 8 |pages= 753-7 |year= 2002 |pmid= 11803525 |doi= }}
*{{cite journal | author=Ishiguro H, Okubo Y, Ohtsuki T, ''et al.'' |title=Mutation analysis of the retinoid X receptor beta, nuclear-related receptor 1, and peroxisome proliferator-activated receptor alpha genes in schizophrenia and alcohol dependence: possible haplotype association of nuclear-related receptor 1 gene to alcohol dependence. |journal=Am. J. Med. Genet. |volume=114 |issue= 1 |pages= 15-23 |year= 2002 |pmid= 11840500 |doi= }}
*{{cite journal | author=McEvoy AN, Murphy EA, Ponnio T, ''et al.'' |title=Activation of nuclear orphan receptor NURR1 transcription by NF-kappa B and cyclic adenosine 5'-monophosphate response element-binding protein in rheumatoid arthritis synovial tissue. |journal=J. Immunol. |volume=168 |issue= 6 |pages= 2979-87 |year= 2002 |pmid= 11884470 |doi= }}
*{{cite journal | author=Xu PY, Liang R, Jankovic J, ''et al.'' |title=Association of homozygous 7048G7049 variant in the intron six of Nurr1 gene with Parkinson's disease. |journal=Neurology |volume=58 |issue= 6 |pages= 881-4 |year= 2002 |pmid= 11914402 |doi= }}
*{{cite journal | author=Bannon MJ, Pruetz B, Manning-Bog AB, ''et al.'' |title=Decreased expression of the transcription factor NURR1 in dopamine neurons of cocaine abusers. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 9 |pages= 6382-5 |year= 2002 |pmid= 11959923 |doi= 10.1073/pnas.092654299 }}
*{{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=Le WD, Xu P, Jankovic J, ''et al.'' |title=Mutations in NR4A2 associated with familial Parkinson disease. |journal=Nat. Genet. |volume=33 |issue= 1 |pages= 85-9 |year= 2003 |pmid= 12496759 |doi= 10.1038/ng1066 }}
*{{cite journal | author=Satoh J, Kuroda Y |title=The constitutive and inducible expression of Nurr1, a key regulator of dopaminergic neuronal differentiation, in human neural and non-neural cell lines. |journal=Neuropathology : official journal of the Japanese Society of Neuropathology |volume=22 |issue= 4 |pages= 219-32 |year= 2003 |pmid= 12564761 |doi= }}
*{{cite journal | author=Iwayama-Shigeno Y, Yamada K, Toyota T, ''et al.'' |title=Distribution of haplotypes derived from three common variants of the NR4A2 gene in Japanese patients with schizophrenia. |journal=Am. J. Med. Genet. B Neuropsychiatr. Genet. |volume=118 |issue= 1 |pages= 20-4 |year= 2003 |pmid= 12627459 |doi= 10.1002/ajmg.b.10053 }}
*{{cite journal | author=Kim KS, Kim CH, Hwang DY, ''et al.'' |title=Orphan nuclear receptor Nurr1 directly transactivates the promoter activity of the tyrosine hydroxylase gene in a cell-specific manner. |journal=J. Neurochem. |volume=85 |issue= 3 |pages= 622-34 |year= 2003 |pmid= 12694388 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NUP62... {November 17, 2007 11:03:17 AM PST}
- SEARCH REDIRECT: Control Box Found: NUP62 {November 17, 2007 11:03:47 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:03:51 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:03:51 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:03:51 AM PST}
- UPDATED: Updated protein page: NUP62 {November 17, 2007 11:03:59 AM PST}
- INFO: Beginning work on PDHA1... {November 17, 2007 10:57:41 AM PST}
- SEARCH REDIRECT: Control Box Found: PDHA1 {November 17, 2007 10:58:21 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 10:58:22 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 10:58:22 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 10:58:22 AM PST}
- UPDATED: Updated protein page: PDHA1 {November 17, 2007 10:58:29 AM PST}
- INFO: Beginning work on PHB... {November 17, 2007 10:58:51 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:59:15 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| 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 = Prohibitin
| HGNCid = 8912
| Symbol = PHB
| AltSymbols =;
| OMIM = 176705
| ECnumber =
| Homologene = 1980
| MGIid = 97572
| GeneAtlas_image1 = PBB_GE_PHB_200658_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PHB_200659_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016563 |text = transcription activator activity}} {{GNF_GO|id=GO:0016564 |text = transcription repressor activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005654 |text = nucleoplasm}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005743 |text = mitochondrial inner membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006260 |text = DNA replication}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0016481 |text = negative regulation of transcription}} {{GNF_GO|id=GO:0016575 |text = histone deacetylation}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5245
| Hs_Ensembl = ENSG00000167085
| Hs_RefseqProtein = NP_002625
| Hs_RefseqmRNA = NM_002634
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 44836419
| Hs_GenLoc_end = 44847241
| Hs_Uniprot = P35232
| Mm_EntrezGene = 18673
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_008831
| Mm_RefseqProtein = NP_032857
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Prohibitin''', also known as '''PHB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PHB prohibitin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5245| 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 = Prohibitin is an evolutionarily conserved gene that is ubiquitously expressed. It is thought to be a negative regulator of cell proliferation and may be a tumor suppressor. Mutations in PHB have been linked to sporadic breast cancer. Prohibitin is expressed as two transcripts with varying lengths of 3' untranslated region. The longer transcript is present at higher levels in proliferating tissues and cells, suggesting that this longer 3' untranslated region may function as a trans-acting regulatory RNA.<ref name="entrez">{{cite web | title = Entrez Gene: PHB prohibitin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5245| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=McClung JK, Jupe ER, Liu XT, Dell'Orco RT |title=Prohibitin: potential role in senescence, development, and tumor suppression. |journal=Exp. Gerontol. |volume=30 |issue= 2 |pages= 99-124 |year= 1996 |pmid= 8591812 |doi= }}
*{{cite journal | author=Dell'Orco RT, McClung JK, Jupe ER, Liu XT |title=Prohibitin and the senescent phenotype. |journal=Exp. Gerontol. |volume=31 |issue= 1-2 |pages= 245-52 |year= 1996 |pmid= 8706794 |doi= }}
*{{cite journal | author=Mishra S, Murphy LC, Nyomba BL, Murphy LJ |title=Prohibitin: a potential target for new therapeutics. |journal=Trends in molecular medicine |volume=11 |issue= 4 |pages= 192-7 |year= 2005 |pmid= 15823758 |doi= 10.1016/j.molmed.2005.02.004 }}
*{{cite journal | author=Rajalingam K, Rudel T |title=Ras-Raf signaling needs prohibitin. |journal=Cell Cycle |volume=4 |issue= 11 |pages= 1503-5 |year= 2007 |pmid= 16294014 |doi= }}
*{{cite journal | author=Sato T, Saito H, Swensen J, ''et al.'' |title=The human prohibitin gene located on chromosome 17q21 is mutated in sporadic breast cancer. |journal=Cancer Res. |volume=52 |issue= 6 |pages= 1643-6 |year= 1992 |pmid= 1540973 |doi= }}
*{{cite journal | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi= }}
*{{cite journal | author=White JJ, Ledbetter DH, Eddy RL, ''et al.'' |title=Assignment of the human prohibitin gene (PHB) to chromosome 17 and identification of a DNA polymorphism. |journal=Genomics |volume=11 |issue= 1 |pages= 228-30 |year= 1992 |pmid= 1684951 |doi= }}
*{{cite journal | author=Altus MS, Wood CM, Stewart DA, ''et al.'' |title=Regions of evolutionary conservation between the rat and human prohibitin-encoding genes. |journal=Gene |volume=158 |issue= 2 |pages= 291-4 |year= 1995 |pmid= 7607556 |doi= }}
*{{cite journal | author=Ikonen E, Fiedler K, Parton RG, Simons K |title=Prohibitin, an antiproliferative protein, is localized to mitochondria. |journal=FEBS Lett. |volume=358 |issue= 3 |pages= 273-7 |year= 1995 |pmid= 7843414 |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=Sato T, Sakamoto T, Takita K, ''et al.'' |title=The human prohibitin (PHB) gene family and its somatic mutations in human tumors. |journal=Genomics |volume=17 |issue= 3 |pages= 762-4 |year= 1993 |pmid= 8244394 |doi= }}
*{{cite journal | author=Jupe ER, Liu XT, Kiehlbauch JL, ''et al.'' |title=The 3' untranslated region of prohibitin and cellular immortalization. |journal=Exp. Cell Res. |volume=224 |issue= 1 |pages= 128-35 |year= 1996 |pmid= 8612677 |doi= 10.1006/excr.1996.0120 }}
*{{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=Rasmussen RK, Ji H, Eddes JS, ''et al.'' |title=Two-dimensional electrophoretic analysis of mixed lineage kinase 2 N-terminal domain binding proteins. |journal=Electrophoresis |volume=19 |issue= 5 |pages= 809-17 |year= 1998 |pmid= 9629920 |doi= 10.1002/elps.1150190535 }}
*{{cite journal | author=Wang S, Nath N, Adlam M, Chellappan S |title=Prohibitin, a potential tumor suppressor, interacts with RB and regulates E2F function. |journal=Oncogene |volume=18 |issue= 23 |pages= 3501-10 |year= 1999 |pmid= 10376528 |doi= 10.1038/sj.onc.1202684 }}
*{{cite journal | author=Wang S, Nath N, Fusaro G, Chellappan S |title=Rb and prohibitin target distinct regions of E2F1 for repression and respond to different upstream signals. |journal=Mol. Cell. Biol. |volume=19 |issue= 11 |pages= 7447-60 |year= 1999 |pmid= 10523633 |doi= }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
*{{cite journal | author=Coates PJ, Nenutil R, McGregor A, ''et al.'' |title=Mammalian prohibitin proteins respond to mitochondrial stress and decrease during cellular senescence. |journal=Exp. Cell Res. |volume=265 |issue= 2 |pages= 262-73 |year= 2001 |pmid= 11302691 |doi= 10.1006/excr.2001.5166 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PIM1... {November 17, 2007 10:59:15 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:59:43 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_PIM1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1xqz.
| PDB = {{PDB2|1xqz}}, {{PDB2|1xr1}}, {{PDB2|1xws}}, {{PDB2|1yhs}}, {{PDB2|1yi3}}, {{PDB2|1yi4}}, {{PDB2|1ywv}}, {{PDB2|1yxs}}, {{PDB2|1yxt}}, {{PDB2|1yxu}}, {{PDB2|1yxv}}, {{PDB2|1yxx}}, {{PDB2|2bik}}, {{PDB2|2bil}}, {{PDB2|2bzh}}, {{PDB2|2bzi}}, {{PDB2|2bzj}}, {{PDB2|2bzk}}, {{PDB2|2c3i}}, {{PDB2|2j2i}}, {{PDB2|2o3p}}, {{PDB2|2o63}}, {{PDB2|2o64}}, {{PDB2|2o65}}, {{PDB2|2obj}}, {{PDB2|2oi4}}
| Name = Pim-1 oncogene
| HGNCid = 8986
| Symbol = PIM1
| AltSymbols =; PIM
| OMIM = 164960
| ECnumber =
| Homologene = 11214
| MGIid = 97584
| GeneAtlas_image1 = PBB_GE_PIM1_209193_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine 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:0030145 |text = manganese ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion 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:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0043066 |text = negative regulation of apoptosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5292
| Hs_Ensembl = ENSG00000137193
| Hs_RefseqProtein = NP_002639
| Hs_RefseqmRNA = NM_002648
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 37245957
| Hs_GenLoc_end = 37251180
| Hs_Uniprot = P11309
| Mm_EntrezGene = 18712
| Mm_Ensembl = ENSMUSG00000024014
| Mm_RefseqmRNA = XM_991765
| Mm_RefseqProtein = XP_996859
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 29217824
| Mm_GenLoc_end = 29222496
| Mm_Uniprot = Q3TYQ0
}}
}}
'''Pim-1 oncogene''', also known as '''PIM1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PIM1 pim-1 oncogene| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5292| 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 protooncogene PIM1 encodes a protein kinase upregulated in prostate cancer.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: PIM1 pim-1 oncogene| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5292| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ragoussis J, Senger G, Mockridge I, ''et al.'' |title=A testis-expressed Zn finger gene (ZNF76) in human 6p21.3 centromeric to the MHC is closely linked to the human homolog of the t-complex gene tcp-11. |journal=Genomics |volume=14 |issue= 3 |pages= 673-9 |year= 1992 |pmid= 1427894 |doi= }}
*{{cite journal | author=Saris CJ, Domen J, Berns A |title=The pim-1 oncogene encodes two related protein-serine/threonine kinases by alternative initiation at AUG and CUG. |journal=EMBO J. |volume=10 |issue= 3 |pages= 655-64 |year= 1991 |pmid= 1825810 |doi= }}
*{{cite journal | author=Reeves R, Spies GA, Kiefer M, ''et al.'' |title=Primary structure of the putative human oncogene, pim-1. |journal=Gene |volume=90 |issue= 2 |pages= 303-7 |year= 1990 |pmid= 2205533 |doi= }}
*{{cite journal | author=Amson R, Sigaux F, Przedborski S, ''et al.'' |title=The human protooncogene product p33pim is expressed during fetal hematopoiesis and in diverse leukemias. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 22 |pages= 8857-61 |year= 1989 |pmid= 2682662 |doi= }}
*{{cite journal | author=Telerman A, Amson R, Zakut-Houri R, Givol D |title=Identification of the human pim-1 gene product as a 33-kilodalton cytoplasmic protein with tyrosine kinase activity. |journal=Mol. Cell. Biol. |volume=8 |issue= 4 |pages= 1498-503 |year= 1988 |pmid= 2837645 |doi= }}
*{{cite journal | author=Domen J, Von Lindern M, Hermans A, ''et al.'' |title=Comparison of the human and mouse PIM-1 cDNAs: nucleotide sequence and immunological identification of the in vitro synthesized PIM-1 protein. |journal=Oncogene Res. |volume=1 |issue= 1 |pages= 103-12 |year= 1988 |pmid= 3329709 |doi= }}
*{{cite journal | author=Meeker TC, Nagarajan L, ar-Rushdi A, Croce CM |title=Cloning and characterization of the human PIM-1 gene: a putative oncogene related to the protein kinases. |journal=J. Cell. Biochem. |volume=35 |issue= 2 |pages= 105-12 |year= 1988 |pmid= 3429489 |doi= 10.1002/jcb.240350204 }}
*{{cite journal | author=Zakut-Houri R, Hazum S, Givol D, Telerman A |title=The cDNA sequence and gene analysis of the human pim oncogene. |journal=Gene |volume=54 |issue= 1 |pages= 105-11 |year= 1987 |pmid= 3475233 |doi= }}
*{{cite journal | author=Leverson JD, Koskinen PJ, Orrico FC, ''et al.'' |title=Pim-1 kinase and p100 cooperate to enhance c-Myb activity. |journal=Mol. Cell |volume=2 |issue= 4 |pages= 417-25 |year= 1998 |pmid= 9809063 |doi= }}
*{{cite journal | author=Mochizuki T, Kitanaka C, Noguchi K, ''et al.'' |title=Physical and functional interactions between Pim-1 kinase and Cdc25A phosphatase. Implications for the Pim-1-mediated activation of the c-Myc signaling pathway. |journal=J. Biol. Chem. |volume=274 |issue= 26 |pages= 18659-66 |year= 1999 |pmid= 10373478 |doi= }}
*{{cite journal | author=Koike N, Maita H, Taira T, ''et al.'' |title=Identification of heterochromatin protein 1 (HP1) as a phosphorylation target by Pim-1 kinase and the effect of phosphorylation on the transcriptional repression function of HP1(1). |journal=FEBS Lett. |volume=467 |issue= 1 |pages= 17-21 |year= 2000 |pmid= 10664448 |doi= }}
*{{cite journal | author=Maita H, Harada Y, Nagakubo D, ''et al.'' |title=PAP-1, a novel target protein of phosphorylation by pim-1 kinase. |journal=Eur. J. Biochem. |volume=267 |issue= 16 |pages= 5168-78 |year= 2000 |pmid= 10931201 |doi= }}
*{{cite journal | author=Mizuno K, Shirogane T, Shinohara A, ''et al.'' |title=Regulation of Pim-1 by Hsp90. |journal=Biochem. Biophys. Res. Commun. |volume=281 |issue= 3 |pages= 663-9 |year= 2001 |pmid= 11237709 |doi= 10.1006/bbrc.2001.4405 }}
*{{cite journal | author=Parks WT, Frank DB, Huff C, ''et al.'' |title=Sorting nexin 6, a novel SNX, interacts with the transforming growth factor-beta family of receptor serine-threonine kinases. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 19332-9 |year= 2001 |pmid= 11279102 |doi= 10.1074/jbc.M100606200 }}
*{{cite journal | author=Wang Z, Bhattacharya N, Meyer MK, ''et al.'' |title=Pim-1 negatively regulates the activity of PTP-U2S phosphatase and influences terminal differentiation and apoptosis of monoblastoid leukemia cells. |journal=Arch. Biochem. Biophys. |volume=390 |issue= 1 |pages= 9-18 |year= 2001 |pmid= 11368509 |doi= 10.1006/abbi.2001.2370 }}
*{{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 }}
*{{cite journal | author=Ishibashi Y, Maita H, Yano M, ''et al.'' |title=Pim-1 translocates sorting nexin 6/TRAF4-associated factor 2 from cytoplasm to nucleus. |journal=FEBS Lett. |volume=506 |issue= 1 |pages= 33-8 |year= 2001 |pmid= 11591366 |doi= }}
*{{cite journal | author=Rainio EM, Sandholm J, Koskinen PJ |title=Cutting edge: Transcriptional activity of NFATc1 is enhanced by the Pim-1 kinase. |journal=J. Immunol. |volume=168 |issue= 4 |pages= 1524-7 |year= 2002 |pmid= 11823475 |doi= }}
*{{cite journal | author=Nieborowska-Skorska M, Hoser G, Kossev P, ''et al.'' |title=Complementary functions of the antiapoptotic protein A1 and serine/threonine kinase pim-1 in the BCR/ABL-mediated leukemogenesis. |journal=Blood |volume=99 |issue= 12 |pages= 4531-9 |year= 2002 |pmid= 12036885 |doi= }}
*{{cite journal | author=Bhattacharya N, Wang Z, Davitt C, ''et al.'' |title=Pim-1 associates with protein complexes necessary for mitosis. |journal=Chromosoma |volume=111 |issue= 2 |pages= 80-95 |year= 2003 |pmid= 12111331 |doi= 10.1007/s00412-002-0192-6 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PRKAA2... {November 17, 2007 10:59:43 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:00:28 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_PRKAA2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2h6d.
| PDB = {{PDB2|2h6d}}
| Name = Protein kinase, AMP-activated, alpha 2 catalytic subunit
| HGNCid = 9377
| Symbol = PRKAA2
| AltSymbols =; AMPK; AMPK2; PRKAA
| OMIM = 600497
| ECnumber =
| Homologene = 4551
| MGIid = 1336173
| GeneAtlas_image1 = PBB_GE_PRKAA2_207709_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006633 |text = fatty acid biosynthetic process}} {{GNF_GO|id=GO:0006695 |text = cholesterol biosynthetic process}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5563
| Hs_Ensembl = ENSG00000162409
| Hs_RefseqProtein = NP_006243
| Hs_RefseqmRNA = NM_006252
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 56883583
| Hs_GenLoc_end = 56953596
| Hs_Uniprot = P54646
| Mm_EntrezGene = 108079
| Mm_Ensembl = ENSMUSG00000028518
| Mm_RefseqmRNA = NM_178143
| Mm_RefseqProtein = NP_835279
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 104532922
| Mm_GenLoc_end = 104607801
| Mm_Uniprot = Q8BRK8
}}
}}
'''Protein kinase, AMP-activated, alpha 2 catalytic subunit''', also known as '''PRKAA2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRKAA2 protein kinase, AMP-activated, alpha 2 catalytic subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5563| 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 catalytic subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. Studies of the mouse counterpart suggest that this catalytic subunit may control whole-body insulin sensitivity and is necessary for maintaining myocardial energy homeostasis during ischemia.<ref name="entrez">{{cite web | title = Entrez Gene: PRKAA2 protein kinase, AMP-activated, alpha 2 catalytic subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5563| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hardie DG, MacKintosh RW |title=AMP-activated protein kinase--an archetypal protein kinase cascade? |journal=Bioessays |volume=14 |issue= 10 |pages= 699-704 |year= 1995 |pmid= 1365882 |doi= 10.1002/bies.950141011 }}
*{{cite journal | author=Hardie DG |title=Regulation of fatty acid and cholesterol metabolism by the AMP-activated protein kinase. |journal=Biochim. Biophys. Acta |volume=1123 |issue= 3 |pages= 231-8 |year= 1992 |pmid= 1536860 |doi= }}
*{{cite journal | author=Carling D |title=The AMP-activated protein kinase cascade--a unifying system for energy control. |journal=Trends Biochem. Sci. |volume=29 |issue= 1 |pages= 18-24 |year= 2004 |pmid= 14729328 |doi= }}
*{{cite journal | author=Aguan K, Scott J, See CG, Sarkar NH |title=Characterization and chromosomal localization of the human homologue of a rat AMP-activated protein kinase-encoding gene: a major regulator of lipid metabolism in mammals. |journal=Gene |volume=149 |issue= 2 |pages= 345-50 |year= 1994 |pmid= 7959015 |doi= }}
*{{cite journal | author=Beri RK, Marley AE, See CG, ''et al.'' |title=Molecular cloning, expression and chromosomal localisation of human AMP-activated protein kinase. |journal=FEBS Lett. |volume=356 |issue= 1 |pages= 117-21 |year= 1995 |pmid= 7988703 |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=Vavvas D, Apazidis A, Saha AK, ''et al.'' |title=Contraction-induced changes in acetyl-CoA carboxylase and 5'-AMP-activated kinase in skeletal muscle. |journal=J. Biol. Chem. |volume=272 |issue= 20 |pages= 13255-61 |year= 1997 |pmid= 9148944 |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=Stein SC, Woods A, Jones NA, ''et al.'' |title=The regulation of AMP-activated protein kinase by phosphorylation. |journal=Biochem. J. |volume=345 Pt 3 |issue= |pages= 437-43 |year= 2000 |pmid= 10642499 |doi= }}
*{{cite journal | author=da Silva Xavier G, Leclerc I, Salt IP, ''et al.'' |title=Role of AMP-activated protein kinase in the regulation by glucose of islet beta cell gene expression. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 8 |pages= 4023-8 |year= 2000 |pmid= 10760274 |doi= }}
*{{cite journal | author=Mu J, Brozinick JT, Valladares O, ''et al.'' |title=A role for AMP-activated protein kinase in contraction- and hypoxia-regulated glucose transport in skeletal muscle. |journal=Mol. Cell |volume=7 |issue= 5 |pages= 1085-94 |year= 2001 |pmid= 11389854 |doi= }}
*{{cite journal | author=Minokoshi Y, Kim YB, Peroni OD, ''et al.'' |title=Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase. |journal=Nature |volume=415 |issue= 6869 |pages= 339-43 |year= 2002 |pmid= 11797013 |doi= 10.1038/415339a }}
*{{cite journal | author=Dubbelhuis PF, Meijer AJ |title=Hepatic amino acid-dependent signaling is under the control of AMP-dependent protein kinase. |journal=FEBS Lett. |volume=521 |issue= 1-3 |pages= 39-42 |year= 2002 |pmid= 12067722 |doi= }}
*{{cite journal | author=Esumi H, Izuishi K, Kato K, ''et al.'' |title=Hypoxia and nitric oxide treatment confer tolerance to glucose starvation in a 5'-AMP-activated protein kinase-dependent manner. |journal=J. Biol. Chem. |volume=277 |issue= 36 |pages= 32791-8 |year= 2002 |pmid= 12091379 |doi= 10.1074/jbc.M112270200 }}
*{{cite journal | author=Nielsen JN, Mustard KJ, Graham DA, ''et al.'' |title=5'-AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle. |journal=J. Appl. Physiol. |volume=94 |issue= 2 |pages= 631-41 |year= 2003 |pmid= 12391032 |doi= 10.1152/japplphysiol.00642.2002 }}
*{{cite journal | author=Wojtaszewski JF, Mourtzakis M, Hillig T, ''et al.'' |title=Dissociation of AMPK activity and ACCbeta phosphorylation in human muscle during prolonged exercise. |journal=Biochem. Biophys. Res. Commun. |volume=298 |issue= 3 |pages= 309-16 |year= 2002 |pmid= 12413941 |doi= }}
*{{cite journal | author=Hallows KR, McCane JE, Kemp BE, ''et al.'' |title=Regulation of channel gating by AMP-activated protein kinase modulates cystic fibrosis transmembrane conductance regulator activity in lung submucosal cells. |journal=J. Biol. Chem. |volume=278 |issue= 2 |pages= 998-1004 |year= 2003 |pmid= 12427743 |doi= 10.1074/jbc.M210621200 }}
*{{cite journal | author=Zong H, Ren JM, Young LH, ''et al.'' |title=AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 25 |pages= 15983-7 |year= 2003 |pmid= 12444247 |doi= 10.1073/pnas.252625599 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PRMT1... {November 17, 2007 10:54:17 AM PST}
- SEARCH REDIRECT: Control Box Found: PRMT1 {November 17, 2007 10:54:49 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 10:54:51 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 10:54:51 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 10:54:51 AM PST}
- UPDATED: Updated protein page: PRMT1 {November 17, 2007 10:54:57 AM PST}
- INFO: Beginning work on SH2D1A... {November 17, 2007 10:54:57 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:55:40 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_SH2D1A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1d1z.
| PDB = {{PDB2|1d1z}}, {{PDB2|1d4t}}, {{PDB2|1d4w}}, {{PDB2|1ka6}}, {{PDB2|1ka7}}, {{PDB2|1m27}}
| Name = SH2 domain protein 1A, Duncan's disease (lymphoproliferative syndrome)
| HGNCid = 10820
| Symbol = SH2D1A
| AltSymbols =; SAP; DSHP; EBVS; IMD5; LYP; MTCP1; XLP; XLPD
| OMIM = 300490
| ECnumber =
| Homologene = 1762
| MGIid = 1328352
| GeneAtlas_image1 = PBB_GE_SH2D1A_210116_at_tn.png
| GeneAtlas_image2 = PBB_GE_SH2D1A_211209_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_SH2D1A_211210_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005070 |text = SH3/SH2 adaptor activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006959 |text = humoral immune response}} {{GNF_GO|id=GO:0006968 |text = cellular defense response}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4068
| Hs_Ensembl = ENSG00000183918
| Hs_RefseqProtein = NP_002342
| Hs_RefseqmRNA = NM_002351
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 123307875
| Hs_GenLoc_end = 123334686
| Hs_Uniprot = O60880
| Mm_EntrezGene = 20400
| Mm_Ensembl = ENSMUSG00000005696
| Mm_RefseqmRNA = XM_903301
| Mm_RefseqProtein = XP_908394
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 38747189
| Mm_GenLoc_end = 38766724
| Mm_Uniprot = Q544F1
}}
}}
'''SH2 domain protein 1A, Duncan's disease (lymphoproliferative syndrome)''', also known as '''SH2D1A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SH2D1A SH2 domain protein 1A, Duncan's disease (lymphoproliferative syndrome)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4068| 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=Sumegi J, Seemayer TA, Huang D, ''et al.'' |title=A spectrum of mutations in SH2D1A that causes X-linked lymphoproliferative disease and other Epstein-Barr virus-associated illnesses. |journal=Leuk. Lymphoma |volume=43 |issue= 6 |pages= 1189-201 |year= 2003 |pmid= 12152986 |doi= }}
*{{cite journal | author=Engel P, Eck MJ, Terhorst C |title=The SAP and SLAM families in immune responses and X-linked lymphoproliferative disease. |journal=Nat. Rev. Immunol. |volume=3 |issue= 10 |pages= 813-21 |year= 2003 |pmid= 14523387 |doi= 10.1038/nri1202 }}
*{{cite journal | author=Stern MH, Soulier J, Rosenzwajg M, ''et al.'' |title=MTCP-1: a novel gene on the human chromosome Xq28 translocated to the T cell receptor alpha/delta locus in mature T cell proliferations. |journal=Oncogene |volume=8 |issue= 9 |pages= 2475-83 |year= 1993 |pmid= 8361760 |doi= }}
*{{cite journal | author=Skare J, Wu BL, Madan S, ''et al.'' |title=Characterization of three overlapping deletions causing X-linked lymphoproliferative disease. |journal=Genomics |volume=16 |issue= 1 |pages= 254-5 |year= 1993 |pmid= 8387453 |doi= }}
*{{cite journal | author=Coffey AJ, Brooksbank RA, Brandau O, ''et al.'' |title=Host response to EBV infection in X-linked lymphoproliferative disease results from mutations in an SH2-domain encoding gene. |journal=Nat. Genet. |volume=20 |issue= 2 |pages= 129-35 |year= 1998 |pmid= 9771704 |doi= 10.1038/2424 }}
*{{cite journal | author=Sayos J, Wu C, Morra M, ''et al.'' |title=The X-linked lymphoproliferative-disease gene product SAP regulates signals induced through the co-receptor SLAM. |journal=Nature |volume=395 |issue= 6701 |pages= 462-9 |year= 1998 |pmid= 9774102 |doi= 10.1038/26683 }}
*{{cite journal | author=Nichols KE, Harkin DP, Levitz S, ''et al.'' |title=Inactivating mutations in an SH2 domain-encoding gene in X-linked lymphoproliferative syndrome. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 23 |pages= 13765-70 |year= 1998 |pmid= 9811875 |doi= }}
*{{cite journal | author=Poy F, Yaffe MB, Sayos J, ''et al.'' |title=Crystal structures of the XLP protein SAP reveal a class of SH2 domains with extended, phosphotyrosine-independent sequence recognition. |journal=Mol. Cell |volume=4 |issue= 4 |pages= 555-61 |year= 1999 |pmid= 10549287 |doi= }}
*{{cite journal | author=Li SC, Gish G, Yang D, ''et al.'' |title=Novel mode of ligand binding by the SH2 domain of the human XLP disease gene product SAP/SH2D1A. |journal=Curr. Biol. |volume=9 |issue= 23 |pages= 1355-62 |year= 2000 |pmid= 10607564 |doi= }}
*{{cite journal | author=Sylla BS, Murphy K, Cahir-McFarland E, ''et al.'' |title=The X-linked lymphoproliferative syndrome gene product SH2D1A associates with p62dok (Dok1) and activates NF-kappa B. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 13 |pages= 7470-5 |year= 2000 |pmid= 10852966 |doi= 10.1073/pnas.130193097 }}
*{{cite journal | author=Benoit L, Wang X, Pabst HF, ''et al.'' |title=Defective NK cell activation in X-linked lymphoproliferative disease. |journal=J. Immunol. |volume=165 |issue= 7 |pages= 3549-53 |year= 2000 |pmid= 11034354 |doi= }}
*{{cite journal | author=Nagy N, Cerboni C, Mattsson K, ''et al.'' |title=SH2D1A and SLAM protein expression in human lymphocytes and derived cell lines. |journal=Int. J. Cancer |volume=88 |issue= 3 |pages= 439-47 |year= 2000 |pmid= 11054674 |doi= }}
*{{cite journal | author=Shlapatska LM, Mikhalap SV, Berdova AG, ''et al.'' |title=CD150 association with either the SH2-containing inositol phosphatase or the SH2-containing protein tyrosine phosphatase is regulated by the adaptor protein SH2D1A. |journal=J. Immunol. |volume=166 |issue= 9 |pages= 5480-7 |year= 2001 |pmid= 11313386 |doi= }}
*{{cite journal | author=Sayós J, Martín M, Chen A, ''et al.'' |title=Cell surface receptors Ly-9 and CD84 recruit the X-linked lymphoproliferative disease gene product SAP. |journal=Blood |volume=97 |issue= 12 |pages= 3867-74 |year= 2001 |pmid= 11389028 |doi= }}
*{{cite journal | author=Morra M, Simarro-Grande M, Martin M, ''et al.'' |title=Characterization of SH2D1A missense mutations identified in X-linked lymphoproliferative disease patients. |journal=J. Biol. Chem. |volume=276 |issue= 39 |pages= 36809-16 |year= 2001 |pmid= 11477068 |doi= 10.1074/jbc.M101305200 }}
*{{cite journal | author=Latour S, Gish G, Helgason CD, ''et al.'' |title=Regulation of SLAM-mediated signal transduction by SAP, the X-linked lymphoproliferative gene product. |journal=Nat. Immunol. |volume=2 |issue= 8 |pages= 681-90 |year= 2001 |pmid= 11477403 |doi= 10.1038/90615 }}
*{{cite journal | author=Bottino C, Falco M, Parolini S, ''et al.'' |title=NTB-A [correction of GNTB-A], a novel SH2D1A-associated surface molecule contributing to the inability of natural killer cells to kill Epstein-Barr virus-infected B cells in X-linked lymphoproliferative disease. |journal=J. Exp. Med. |volume=194 |issue= 3 |pages= 235-46 |year= 2001 |pmid= 11489943 |doi= }}
*{{cite journal | author=Liu A, Klein G, Bandobashi K, ''et al.'' |title=SH2D1A expression reflects activation of T and NK cells in cord blood lymphocytes infected with EBV and treated with the immunomodulator PSK. |journal=Immunol. Lett. |volume=80 |issue= 3 |pages= 181-8 |year= 2002 |pmid= 11803050 |doi= }}
*{{cite journal | author=Howie D, Simarro M, Sayos J, ''et al.'' |title=Molecular dissection of the signaling and costimulatory functions of CD150 (SLAM): CD150/SAP binding and CD150-mediated costimulation. |journal=Blood |volume=99 |issue= 3 |pages= 957-65 |year= 2002 |pmid= 11806999 |doi= }}
*{{cite journal | author=Aoukaty A, Tan R |title=Association of the X-linked lymphoproliferative disease gene product SAP/SH2D1A with 2B4, a natural killer cell-activating molecule, is dependent on phosphoinositide 3-kinase. |journal=J. Biol. Chem. |volume=277 |issue= 15 |pages= 13331-7 |year= 2002 |pmid= 11815622 |doi= 10.1074/jbc.M112029200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SLC19A1... {November 17, 2007 11:00:28 AM PST}
- SEARCH REDIRECT: Control Box Found: SLC19A1 {November 17, 2007 11:01:08 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:01:11 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:01:11 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:01:11 AM PST}
- UPDATED: Updated protein page: SLC19A1 {November 17, 2007 11:01:18 AM PST}
- INFO: Beginning work on SLC25A4... {November 17, 2007 10:46:31 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:47:30 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_SLC25A4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1okc.
| PDB = {{PDB2|1okc}}, {{PDB2|2c3e}}
| Name = Solute carrier family 25 (mitochondrial carrier; adenine nucleotide translocator), member 4
| HGNCid = 10990
| Symbol = SLC25A4
| AltSymbols =; ANT; ANT1; PEO2; PEO3; T1
| OMIM = 103220
| ECnumber =
| Homologene = 36058
| MGIid = 1353495
| GeneAtlas_image1 = PBB_GE_SLC25A4_202825_at_tn.png
| Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005488 |text = binding}} {{GNF_GO|id=GO:0015207 |text = adenine transmembrane transporter activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005743 |text = mitochondrial inner membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0000002 |text = mitochondrial genome maintenance}} {{GNF_GO|id=GO:0006091 |text = generation of precursor metabolites and energy}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006839 |text = mitochondrial transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 291
| Hs_Ensembl = ENSG00000151729
| Hs_RefseqProtein = NP_001142
| Hs_RefseqmRNA = NM_001151
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 186301392
| Hs_GenLoc_end = 186305418
| Hs_Uniprot = P12235
| Mm_EntrezGene = 11739
| Mm_Ensembl = ENSMUSG00000031633
| Mm_RefseqmRNA = XM_134169
| Mm_RefseqProtein = XP_134169
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 47705991
| Mm_GenLoc_end = 47709847
| Mm_Uniprot = Q8BVI9
}}
}}
'''Solute carrier family 25 (mitochondrial carrier; adenine nucleotide translocator), member 4''', also known as '''SLC25A4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SLC25A4 solute carrier family 25 (mitochondrial carrier; adenine nucleotide translocator), member 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=291| 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=Vieira HL, Haouzi D, El Hamel C, ''et al.'' |title=Permeabilization of the mitochondrial inner membrane during apoptosis: impact of the adenine nucleotide translocator. |journal=Cell Death Differ. |volume=7 |issue= 12 |pages= 1146-54 |year= 2001 |pmid= 11175251 |doi= 10.1038/sj.cdd.4400778 }}
*{{cite journal | author=Ferri KF, Jacotot E, Blanco J, ''et al.'' |title=Mitochondrial control of cell death induced by HIV-1-encoded proteins. |journal=Ann. N. Y. Acad. Sci. |volume=926 |issue= |pages= 149-64 |year= 2001 |pmid= 11193032 |doi= }}
*{{cite journal | author=Kino T, Pavlakis GN |title=Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1. |journal=DNA Cell Biol. |volume=23 |issue= 4 |pages= 193-205 |year= 2004 |pmid= 15142377 |doi= 10.1089/104454904773819789 }}
*{{cite journal | author=Andersen JL, Planelles V |title=The role of Vpr in HIV-1 pathogenesis. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 43-51 |year= 2005 |pmid= 15638722 |doi= }}
*{{cite journal | author=Le Rouzic E, Benichou S |title=The Vpr protein from HIV-1: distinct roles along the viral life cycle. |journal=Retrovirology |volume=2 |issue= |pages= 11 |year= 2006 |pmid= 15725353 |doi= 10.1186/1742-4690-2-11 }}
*{{cite journal | author=Zhao RY, Bukrinsky M, Elder RT |title=HIV-1 viral protein R (Vpr) & host cellular responses. |journal=Indian J. Med. Res. |volume=121 |issue= 4 |pages= 270-86 |year= 2005 |pmid= 15817944 |doi= }}
*{{cite journal | author=Muthumani K, Choo AY, Premkumar A, ''et al.'' |title=Human immunodeficiency virus type 1 (HIV-1) Vpr-regulated cell death: insights into mechanism. |journal=Cell Death Differ. |volume=12 Suppl 1 |issue= |pages= 962-70 |year= 2006 |pmid= 15832179 |doi= 10.1038/sj.cdd.4401583 }}
*{{cite journal | author=Li L, Li HS, Pauza CD, ''et al.'' |title=Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions. |journal=Cell Res. |volume=15 |issue= 11-12 |pages= 923-34 |year= 2006 |pmid= 16354571 |doi= 10.1038/sj.cr.7290370 }}
*{{cite journal | author=Moon HS, Yang JS |title=Role of HIV Vpr as a regulator of apoptosis and an effector on bystander cells. |journal=Mol. Cells |volume=21 |issue= 1 |pages= 7-20 |year= 2006 |pmid= 16511342 |doi= }}
*{{cite journal | author=Fan YS, Yang HM, Lin CC |title=Assignment of the human muscle adenine nucleotide translocator gene (ANT1) to 4q35 by fluorescence in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=60 |issue= 1 |pages= 29-30 |year= 1992 |pmid= 1582253 |doi= }}
*{{cite journal | author=Cozens AL, Runswick MJ, Walker JE |title=DNA sequences of two expressed nuclear genes for human mitochondrial ADP/ATP translocase. |journal=J. Mol. Biol. |volume=206 |issue= 2 |pages= 261-80 |year= 1989 |pmid= 2541251 |doi= }}
*{{cite journal | author=Li K, Warner CK, Hodge JA, ''et al.'' |title=A human muscle adenine nucleotide translocator gene has four exons, is located on chromosome 4, and is differentially expressed. |journal=J. Biol. Chem. |volume=264 |issue= 24 |pages= 13998-4004 |year= 1989 |pmid= 2547778 |doi= }}
*{{cite journal | author=Neckelmann N, Li K, Wade RP, ''et al.'' |title=cDNA sequence of a human skeletal muscle ADP/ATP translocator: lack of a leader peptide, divergence from a fibroblast translocator cDNA, and coevolution with mitochondrial DNA genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 21 |pages= 7580-4 |year= 1987 |pmid= 2823266 |doi= }}
*{{cite journal | author=Houldsworth J, Attardi G |title=Two distinct genes for ADP/ATP translocase are expressed at the mRNA level in adult human liver. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 2 |pages= 377-81 |year= 1988 |pmid= 2829183 |doi= }}
*{{cite journal | author=Wijmenga C, Winokur ST, Padberg GW, ''et al.'' |title=The human skeletal muscle adenine nucleotide translocator gene maps to chromosome 4q35 in the region of the facioscapulohumeral muscular dystrophy locus. |journal=Hum. Genet. |volume=92 |issue= 2 |pages= 198-203 |year= 1993 |pmid= 8103757 |doi= }}
*{{cite journal | author=Bakker HD, Scholte HR, Van den Bogert C, ''et al.'' |title=Deficiency of the adenine nucleotide translocator in muscle of a patient with myopathy and lactic acidosis: a new mitochondrial defect. |journal=Pediatr. Res. |volume=33 |issue= 4 Pt 1 |pages= 412-7 |year= 1993 |pmid= 8479824 |doi= }}
*{{cite journal | author=Kaukonen JA, Amati P, Suomalainen A, ''et al.'' |title=An autosomal locus predisposing to multiple deletions of mtDNA on chromosome 3p. |journal=Am. J. Hum. Genet. |volume=58 |issue= 4 |pages= 763-9 |year= 1996 |pmid= 8644740 |doi= }}
*{{cite journal | author=Marzo I, Brenner C, Zamzami N, ''et al.'' |title=Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis. |journal=Science |volume=281 |issue= 5385 |pages= 2027-31 |year= 1998 |pmid= 9748162 |doi= }}
*{{cite journal | author=Kaukonen J, Zeviani M, Comi GP, ''et al.'' |title=A third locus predisposing to multiple deletions of mtDNA in autosomal dominant progressive external ophthalmoplegia. |journal=Am. J. Hum. Genet. |volume=65 |issue= 1 |pages= 256-61 |year= 1999 |pmid= 10364542 |doi= }}
*{{cite journal | author=Jacotot E, Ravagnan L, Loeffler M, ''et al.'' |title=The HIV-1 viral protein R induces apoptosis via a direct effect on the mitochondrial permeability transition pore. |journal=J. Exp. Med. |volume=191 |issue= 1 |pages= 33-46 |year= 2000 |pmid= 10620603 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SLC26A4... {November 17, 2007 10:58:29 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 10:58:51 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Solute carrier family 26, member 4
| HGNCid = 8818
| Symbol = SLC26A4
| AltSymbols =; DFNB4; PDS
| OMIM = 605646
| ECnumber =
| Homologene = 20132
| MGIid = 1346029
| GeneAtlas_image1 = PBB_GE_SLC26A4_206529_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0008271 |text = secondary active sulfate transmembrane transporter activity}} {{GNF_GO|id=GO:0015108 |text = chloride transmembrane transporter activity}} {{GNF_GO|id=GO:0015111 |text = iodide transmembrane transporter activity}} {{GNF_GO|id=GO:0031404 |text = chloride ion binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0008272 |text = sulfate transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5172
| Hs_Ensembl = ENSG00000091137
| Hs_RefseqProtein = NP_000432
| Hs_RefseqmRNA = NM_000441
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 107088316
| Hs_GenLoc_end = 107145490
| Hs_Uniprot = O43511
| Mm_EntrezGene = 23985
| Mm_Ensembl = ENSMUSG00000020651
| Mm_RefseqmRNA = NM_011867
| Mm_RefseqProtein = NP_035997
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 32101856
| Mm_GenLoc_end = 32145728
| Mm_Uniprot = Q9R155
}}
}}
'''Solute carrier family 26, member 4''', also known as '''SLC26A4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SLC26A4 solute carrier family 26, member 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5172| 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 = Mutations in this gene are associated with Pendred syndrome, the most common form of syndromic deafness, an autosomal-recessive disease. It is highly homologous to the SLC26A3 gene; they have similar genomic structures and this gene is located 3' of the SLC26A3 gene. The encoded protein has homology to sulfate transporters.<ref name="entrez">{{cite web | title = Entrez Gene: SLC26A4 solute carrier family 26, member 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5172| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Markovich D |title=Physiological roles and regulation of mammalian sulfate transporters. |journal=Physiol. Rev. |volume=81 |issue= 4 |pages= 1499-533 |year= 2001 |pmid= 11581495 |doi= }}
*{{cite journal | author=Baldwin CT, Weiss S, Farrer LA, ''et al.'' |title=Linkage of congenital, recessive deafness (DFNB4) to chromosome 7q31 and evidence for genetic heterogeneity in the Middle Eastern Druze population. |journal=Hum. Mol. Genet. |volume=4 |issue= 9 |pages= 1637-42 |year= 1996 |pmid= 8541853 |doi= }}
*{{cite journal | author=Coyle B, Coffey R, Armour JA, ''et al.'' |title=Pendred syndrome (goitre and sensorineural hearing loss) maps to chromosome 7 in the region containing the nonsyndromic deafness gene DFNB4. |journal=Nat. Genet. |volume=12 |issue= 4 |pages= 421-3 |year= 1996 |pmid= 8630497 |doi= 10.1038/ng0496-421 }}
*{{cite journal | author=Sheffield VC, Kraiem Z, Beck JC, ''et al.'' |title=Pendred syndrome maps to chromosome 7q21-34 and is caused by an intrinsic defect in thyroid iodine organification. |journal=Nat. Genet. |volume=12 |issue= 4 |pages= 424-6 |year= 1996 |pmid= 8630498 |doi= 10.1038/ng0496-424 }}
*{{cite journal | author=Gausden E, Armour JA, Coyle B, ''et al.'' |title=Thyroid peroxidase: evidence for disease gene exclusion in Pendred's syndrome. |journal=Clin. Endocrinol. (Oxf) |volume=44 |issue= 4 |pages= 441-6 |year= 1996 |pmid= 8706311 |doi= }}
*{{cite journal | author=Coucke P, Van Camp G, Demirhan O, ''et al.'' |title=The gene for Pendred syndrome is located between D7S501 and D7S692 in a 1.7-cM region on chromosome 7q. |journal=Genomics |volume=40 |issue= 1 |pages= 48-54 |year= 1997 |pmid= 9070918 |doi= 10.1006/geno.1996.4541 }}
*{{cite journal | author=Everett LA, Glaser B, Beck JC, ''et al.'' |title=Pendred syndrome is caused by mutations in a putative sulphate transporter gene (PDS). |journal=Nat. Genet. |volume=17 |issue= 4 |pages= 411-22 |year= 1997 |pmid= 9398842 |doi= 10.1038/ng1297-411 }}
*{{cite journal | author=Li XC, Everett LA, Lalwani AK, ''et al.'' |title=A mutation in PDS causes non-syndromic recessive deafness. |journal=Nat. Genet. |volume=18 |issue= 3 |pages= 215-7 |year= 1998 |pmid= 9500541 |doi= 10.1038/ng0398-215 }}
*{{cite journal | author=Van Hauwe P, Everett LA, Coucke P, ''et al.'' |title=Two frequent missense mutations in Pendred syndrome. |journal=Hum. Mol. Genet. |volume=7 |issue= 7 |pages= 1099-104 |year= 1999 |pmid= 9618166 |doi= }}
*{{cite journal | author=Coyle B, Reardon W, Herbrick JA, ''et al.'' |title=Molecular analysis of the PDS gene in Pendred syndrome. |journal=Hum. Mol. Genet. |volume=7 |issue= 7 |pages= 1105-12 |year= 1999 |pmid= 9618167 |doi= }}
*{{cite journal | author=Usami S, Abe S, Weston MD, ''et al.'' |title=Non-syndromic hearing loss associated with enlarged vestibular aqueduct is caused by PDS mutations. |journal=Hum. Genet. |volume=104 |issue= 2 |pages= 188-92 |year= 1999 |pmid= 10190331 |doi= }}
*{{cite journal | author=Scott DA, Wang R, Kreman TM, ''et al.'' |title=The Pendred syndrome gene encodes a chloride-iodide transport protein. |journal=Nat. Genet. |volume=21 |issue= 4 |pages= 440-3 |year= 1999 |pmid= 10192399 |doi= 10.1038/7783 }}
*{{cite journal | author=Masmoudi S, Charfedine I, Hmani M, ''et al.'' |title=Pendred syndrome: phenotypic variability in two families carrying the same PDS missense mutation. |journal=Am. J. Med. Genet. |volume=90 |issue= 1 |pages= 38-44 |year= 2000 |pmid= 10602116 |doi= }}
*{{cite journal | author=Reardon W, OMahoney CF, Trembath R, ''et al.'' |title=Enlarged vestibular aqueduct: a radiological marker of pendred syndrome, and mutation of the PDS gene. |journal=QJM : monthly journal of the Association of Physicians |volume=93 |issue= 2 |pages= 99-104 |year= 2000 |pmid= 10700480 |doi= }}
*{{cite journal | author=Bogazzi F, Raggi F, Ultimieri F, ''et al.'' |title=A novel mutation in the pendrin gene associated with Pendred's syndrome. |journal=Clin. Endocrinol. (Oxf) |volume=52 |issue= 3 |pages= 279-85 |year= 2000 |pmid= 10718825 |doi= }}
*{{cite journal | author=Bidart JM, Mian C, Lazar V, ''et al.'' |title=Expression of pendrin and the Pendred syndrome (PDS) gene in human thyroid tissues. |journal=J. Clin. Endocrinol. Metab. |volume=85 |issue= 5 |pages= 2028-33 |year= 2000 |pmid= 10843192 |doi= }}
*{{cite journal | author=Adato A, Raskin L, Petit C, Bonne-Tamir B |title=Deafness heterogeneity in a Druze isolate from the Middle East: novel OTOF and PDS mutations, low prevalence of GJB2 35delG mutation and indication for a new DFNB locus. |journal=Eur. J. Hum. Genet. |volume=8 |issue= 6 |pages= 437-42 |year= 2000 |pmid= 10878664 |doi= 10.1038/sj.ejhg.5200489 }}
*{{cite journal | author=Lohi H, Kujala M, Kerkelä E, ''et al.'' |title=Mapping of five new putative anion transporter genes in human and characterization of SLC26A6, a candidate gene for pancreatic anion exchanger. |journal=Genomics |volume=70 |issue= 1 |pages= 102-12 |year= 2001 |pmid= 11087667 |doi= 10.1006/geno.2000.6355 }}
*{{cite journal | author=Royaux IE, Wall SM, Karniski LP, ''et al.'' |title=Pendrin, encoded by the Pendred syndrome gene, resides in the apical region of renal intercalated cells and mediates bicarbonate secretion. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 7 |pages= 4221-6 |year= 2001 |pmid= 11274445 |doi= 10.1073/pnas.071516798 }}
*{{cite journal | author=Campbell C, Cucci RA, Prasad S, ''et al.'' |title=Pendred syndrome, DFNB4, and PDS/SLC26A4 identification of eight novel mutations and possible genotype-phenotype correlations. |journal=Hum. Mutat. |volume=17 |issue= 5 |pages= 403-11 |year= 2001 |pmid= 11317356 |doi= 10.1002/humu.1116 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SOD3... {November 17, 2007 11:01:18 AM PST}
- SEARCH REDIRECT: Control Box Found: SOD3 {November 17, 2007 11:01:42 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:01:45 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:01:45 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:01:45 AM PST}
- UPDATED: Updated protein page: SOD3 {November 17, 2007 11:01:52 AM PST}
- INFO: Beginning work on VIP... {November 17, 2007 11:01:52 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:02:18 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 = Vasoactive intestinal peptide
| HGNCid = 12693
| Symbol = VIP
| AltSymbols =; MGC13587; PHM27
| OMIM = 192320
| ECnumber =
| Homologene = 2539
| MGIid = 98933
| GeneAtlas_image1 = PBB_GE_VIP_206577_at_tn.png
| Function = {{GNF_GO|id=GO:0005179 |text = hormone activity}} {{GNF_GO|id=GO:0005184 |text = neuropeptide hormone activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}}
| Process = {{GNF_GO|id=GO:0006936 |text = muscle contraction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007589 |text = fluid secretion}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7432
| Hs_Ensembl = ENSG00000146469
| Hs_RefseqProtein = NP_003372
| Hs_RefseqmRNA = NM_003381
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 153113626
| Hs_GenLoc_end = 153122593
| Hs_Uniprot = P01282
| Mm_EntrezGene = 22353
| Mm_Ensembl = ENSMUSG00000019772
| Mm_RefseqmRNA = NM_011702
| Mm_RefseqProtein = NP_035832
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 4698927
| Mm_GenLoc_end = 4707323
| Mm_Uniprot = P32648
}}
}}
'''Vasoactive intestinal peptide''', also known as '''VIP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: VIP vasoactive intestinal peptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7432| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene belongs to the glucagon family. It stimulates myocardial contractility, causes vasodilation, increases glycogenolysis, lowers arterial blood pressure and relaxes the smooth muscle of trachea, stomach and gall bladder. Alternative splicing occurs at this locus and two transcript variants encoding distinct isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: VIP vasoactive intestinal peptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7432| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Fahrenkrug J |title=Gut/brain peptides in the genital tract: VIP and PACAP. |journal=Scand. J. Clin. Lab. Invest. Suppl. |volume=234 |issue= |pages= 35-9 |year= 2002 |pmid= 11713978 |doi= }}
*{{cite journal | author=Delgado M, Pozo D, Ganea D |title=The significance of vasoactive intestinal peptide in immunomodulation. |journal=Pharmacol. Rev. |volume=56 |issue= 2 |pages= 249-90 |year= 2004 |pmid= 15169929 |doi= 10.1124/pr.56.2.7 }}
*{{cite journal | author=Conconi MT, Spinazzi R, Nussdorfer GG |title=Endogenous ligands of PACAP/VIP receptors in the autocrine-paracrine regulation of the adrenal gland. |journal=Int. Rev. Cytol. |volume=249 |issue= |pages= 1-51 |year= 2006 |pmid= 16697281 |doi= 10.1016/S0074-7696(06)49001-X }}
*{{cite journal | author=Hill JM |title=Vasoactive intestinal peptide in neurodevelopmental disorders: therapeutic potential. |journal=Curr. Pharm. Des. |volume=13 |issue= 11 |pages= 1079-89 |year= 2007 |pmid= 17430171 |doi= }}
*{{cite journal | author=Gonzalez-Rey E, Varela N, Chorny A, Delgado M |title=Therapeutical approaches of vasoactive intestinal peptide as a pleiotropic immunomodulator. |journal=Curr. Pharm. Des. |volume=13 |issue= 11 |pages= 1113-39 |year= 2007 |pmid= 17430175 |doi= }}
*{{cite journal | author= |title=[Quaternary structure of rabbit skeletal muscle glycogen synthetase] |journal=Dokl. Akad. Nauk SSSR |volume=222 |issue= 4 |pages= 997-1000 |year= 1975 |pmid= 807467 |doi= }}
*{{cite journal | author=Kitamura K, Kangawa K, Kawamoto M, ''et al.'' |title=Isolation and characterization of peptides which act on rat platelets, from a pheochromocytoma. |journal=Biochem. Biophys. Res. Commun. |volume=185 |issue= 1 |pages= 134-41 |year= 1992 |pmid= 1318039 |doi= }}
*{{cite journal | author=Glowa JR, Panlilio LV, Brenneman DE, ''et al.'' |title=Learning impairment following intracerebral administration of the HIV envelope protein gp120 or a VIP antagonist. |journal=Brain Res. |volume=570 |issue= 1-2 |pages= 49-53 |year= 1992 |pmid= 1617429 |doi= }}
*{{cite journal | author=Theriault Y, Boulanger Y, St-Pierre S |title=Structural determination of the vasoactive intestinal peptide by two-dimensional H-NMR spectroscopy. |journal=Biopolymers |volume=31 |issue= 4 |pages= 459-64 |year= 1991 |pmid= 1863695 |doi= 10.1002/bip.360310411 }}
*{{cite journal | author=Gozes I, Giladi E, Shani Y |title=Vasoactive intestinal peptide gene: putative mechanism of information storage at the RNA level. |journal=J. Neurochem. |volume=48 |issue= 4 |pages= 1136-41 |year= 1987 |pmid= 2434617 |doi= }}
*{{cite journal | author=Yamagami T, Ohsawa K, Nishizawa M, ''et al.'' |title=Complete nucleotide sequence of human vasoactive intestinal peptide/PHM-27 gene and its inducible promoter. |journal=Ann. N. Y. Acad. Sci. |volume=527 |issue= |pages= 87-102 |year= 1988 |pmid= 2839091 |doi= }}
*{{cite journal | author=Bodner M, Fridkin M, Gozes I |title=Coding sequences for vasoactive intestinal peptide and PHM-27 peptide are located on two adjacent exons in the human genome. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 11 |pages= 3548-51 |year= 1985 |pmid= 2987932 |doi= }}
*{{cite journal | author=DeLamarter JF, Buell GN, Kawashima E, ''et al.'' |title=Vasoactive intestinal peptide: expression of the prohormone in bacterial cells. |journal=Peptides |volume=6 Suppl 1 |issue= |pages= 95-102 |year= 1985 |pmid= 2995945 |doi= }}
*{{cite journal | author=Linder S, Barkhem T, Norberg A, ''et al.'' |title=Structure and expression of the gene encoding the vasoactive intestinal peptide precursor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 2 |pages= 605-9 |year= 1987 |pmid= 3025882 |doi= }}
*{{cite journal | author=Gotoh E, Yamagami T, Yamamoto H, Okamoto H |title=Chromosomal assignment of human VIP/PHM-27 gene to 6q26----q27 region by spot blot hybridization and in situ hybridization. |journal=Biochem. Int. |volume=17 |issue= 3 |pages= 555-62 |year= 1989 |pmid= 3202886 |doi= }}
*{{cite journal | author=Yiangou Y, Di Marzo V, Spokes RA, ''et al.'' |title=Isolation, characterization, and pharmacological actions of peptide histidine valine 42, a novel prepro-vasoactive intestinal peptide-derived peptide. |journal=J. Biol. Chem. |volume=262 |issue= 29 |pages= 14010-3 |year= 1987 |pmid= 3654650 |doi= }}
*{{cite journal | author=Gozes I, Bodner M, Shani Y, Fridkin M |title=Structure and expression of the vasoactive intestinal peptide (VIP) gene in a human tumor. |journal=Peptides |volume=7 Suppl 1 |issue= |pages= 1-6 |year= 1986 |pmid= 3748844 |doi= }}
*{{cite journal | author=Tsukada T, Horovitch SJ, Montminy MR, ''et al.'' |title=Structure of the human vasoactive intestinal polypeptide gene. |journal=DNA |volume=4 |issue= 4 |pages= 293-300 |year= 1985 |pmid= 3899557 |doi= }}
*{{cite journal | author=Heinz-Erian P, Dey RD, Flux M, Said SI |title=Deficient vasoactive intestinal peptide innervation in the sweat glands of cystic fibrosis patients. |journal=Science |volume=229 |issue= 4720 |pages= 1407-8 |year= 1985 |pmid= 4035357 |doi= }}
*{{cite journal | author=Bloom SR, Christofides ND, Delamarter J, ''et al.'' |title=Diarrhoea in vipoma patients associated with cosecretion of a second active peptide (peptide histidine isoleucine) explained by single coding gene. |journal=Lancet |volume=2 |issue= 8360 |pages= 1163-5 |year= 1984 |pmid= 6139527 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on VIPR1... {November 17, 2007 11:02:18 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:02:56 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 = Vasoactive intestinal peptide receptor 1
| HGNCid = 12694
| Symbol = VIPR1
| AltSymbols =; II; FLJ41949; HVR1; PACAP-R-2; RDC1; VAPC1; VIPR; VIRG; VPAC1
| OMIM = 192321
| ECnumber =
| Homologene = 3399
| MGIid = 109272
| GeneAtlas_image1 = PBB_GE_VIPR1_205019_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004930 |text = G-protein coupled receptor activity}} {{GNF_GO|id=GO:0004999 |text = vasoactive intestinal polypeptide receptor activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006936 |text = muscle contraction}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007187 |text = G-protein signaling, coupled to cyclic nucleotide second messenger}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007586 |text = digestion}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7433
| Hs_Ensembl = ENSG00000114812
| Hs_RefseqProtein = NP_004615
| Hs_RefseqmRNA = NM_004624
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 42519121
| Hs_GenLoc_end = 42554064
| Hs_Uniprot = P32241
| Mm_EntrezGene = 22354
| Mm_Ensembl = ENSMUSG00000032528
| Mm_RefseqmRNA = NM_011703
| Mm_RefseqProtein = NP_035833
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 121491414
| Mm_GenLoc_end = 121519332
| Mm_Uniprot = P97751
}}
}}
'''Vasoactive intestinal peptide receptor 1''', also known as '''VIPR1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: VIPR1 vasoactive intestinal peptide receptor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7433| 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 receptor for vasoactive intestinal peptide, a small neuropeptide. Vasoactive intestinal peptide is involved in smooth muscle relaxation, exocrine and endocrine secretion, and water and ion flux in lung and intestinal epithelia. Its actions are effected through integral membrane receptors associated with a guanine nucleotide binding protein which activates adenylate cyclase.<ref name="entrez">{{cite web | title = Entrez Gene: VIPR1 vasoactive intestinal peptide receptor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7433| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author= |title=[Quaternary structure of rabbit skeletal muscle glycogen synthetase] |journal=Dokl. Akad. Nauk SSSR |volume=222 |issue= 4 |pages= 997-1000 |year= 1975 |pmid= 807467 |doi= }}
*{{cite journal | author=Sreedharan SP, Huang JX, Cheung MC, Goetzl EJ |title=Structure, expression, and chromosomal localization of the type I human vasoactive intestinal peptide receptor gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 7 |pages= 2939-43 |year= 1995 |pmid= 7708752 |doi= }}
*{{cite journal | author=Couvineau A, Gaudin P, Maoret JJ, ''et al.'' |title=Highly conserved aspartate 68, tryptophane 73 and glycine 109 in the N-terminal extracellular domain of the human VIP receptor are essential for its ability to bind VIP. |journal=Biochem. Biophys. Res. Commun. |volume=206 |issue= 1 |pages= 246-52 |year= 1995 |pmid= 7818527 |doi= }}
*{{cite journal | author=Gagnon AW, Aiyar N, Elshourbagy NA |title=Molecular cloning and functional characterization of a human liver vasoactive intestinal peptide receptor. |journal=Cell. Signal. |volume=6 |issue= 3 |pages= 321-33 |year= 1994 |pmid= 7917790 |doi= }}
*{{cite journal | author=Sreedharan SP, Patel DR, Xia M, ''et al.'' |title=Human vasoactive intestinal peptide1 receptors expressed by stable transfectants couple to two distinct signaling pathways. |journal=Biochem. Biophys. Res. Commun. |volume=203 |issue= 1 |pages= 141-8 |year= 1994 |pmid= 8074647 |doi= }}
*{{cite journal | author=Couvineau A, Rouyer-Fessard C, Darmoul D, ''et al.'' |title=Human intestinal VIP receptor: cloning and functional expression of two cDNA encoding proteins with different N-terminal domains. |journal=Biochem. Biophys. Res. Commun. |volume=200 |issue= 2 |pages= 769-76 |year= 1994 |pmid= 8179610 |doi= }}
*{{cite journal | author=Moody TW, Zia F, Draoui M, ''et al.'' |title=A vasoactive intestinal peptide antagonist inhibits non-small cell lung cancer growth. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 10 |pages= 4345-9 |year= 1993 |pmid= 8389448 |doi= }}
*{{cite journal | author=Sreedharan SP, Patel DR, Huang JX, Goetzl EJ |title=Cloning and functional expression of a human neuroendocrine vasoactive intestinal peptide receptor. |journal=Biochem. Biophys. Res. Commun. |volume=193 |issue= 2 |pages= 546-53 |year= 1993 |pmid= 8390245 |doi= 10.1006/bbrc.1993.1658 }}
*{{cite journal | author=Couvineau A, Fabre C, Gaudin P, ''et al.'' |title=Mutagenesis of N-glycosylation sites in the human vasoactive intestinal peptide 1 receptor. Evidence that asparagine 58 or 69 is crucial for correct delivery of the receptor to plasma membrane. |journal=Biochemistry |volume=35 |issue= 6 |pages= 1745-52 |year= 1996 |pmid= 8639654 |doi= 10.1021/bi952022h }}
*{{cite journal | author=Pozo D, Guerrero JM, Segura JJ, Calvo JR |title=Thymosin alpha 1 interacts with the VIP receptor-effector system in rat and mouse immunocompetent cells. |journal=Immunopharmacology |volume=34 |issue= 2-3 |pages= 113-23 |year= 1997 |pmid= 8886855 |doi= }}
*{{cite journal | author=Couvineau A, Maoret JJ, Rouyer-Fessard C, ''et al.'' |title=Cloning and functional characterization of the human VIP1/PACAP receptor promoter. |journal=Ann. N. Y. Acad. Sci. |volume=865 |issue= |pages= 59-63 |year= 1999 |pmid= 9927997 |doi= }}
*{{cite journal | author=Knudsen SM, Tams JW, Wulff BS, Fahrenkrug J |title=Importance of conserved cysteines in the extracellular loops of human PACAP/VIP1 receptor for ligand binding and stimulation of cAMP production. |journal=Ann. N. Y. Acad. Sci. |volume=865 |issue= |pages= 259-65 |year= 1999 |pmid= 9928020 |doi= }}
*{{cite journal | author=Marie J, Wakkach A, Coudray A, ''et al.'' |title=Functional expression of receptors for calcitonin gene-related peptide, calcitonin, and vasoactive intestinal peptide in the human thymus and thymomas from myasthenia gravis patients. |journal=J. Immunol. |volume=162 |issue= 4 |pages= 2103-12 |year= 1999 |pmid= 9973484 |doi= }}
*{{cite journal | author=Mimuro H, Suzuki T, Suetsugu S, ''et al.'' |title=Profilin is required for sustaining efficient intra- and intercellular spreading of Shigella flexneri. |journal=J. Biol. Chem. |volume=275 |issue= 37 |pages= 28893-901 |year= 2000 |pmid= 10867004 |doi= 10.1074/jbc.M003882200 }}
*{{cite journal | author=Nicole P, Maoret JJ, Couvineau A, ''et al.'' |title=Tryptophan 67 in the human VPAC(1) receptor: crucial role for VIP binding. |journal=Biochem. Biophys. Res. Commun. |volume=276 |issue= 2 |pages= 654-9 |year= 2000 |pmid= 11027527 |doi= 10.1006/bbrc.2000.3375 }}
*{{cite journal | author=Bajo AM, Juarranz MG, Valenzuela P, ''et al.'' |title=Expression of vasoactive intestinal peptide (VIP) receptors in human uterus. |journal=Peptides |volume=21 |issue= 9 |pages= 1383-8 |year= 2001 |pmid= 11072126 |doi= }}
*{{cite journal | author=Lara-Marquez M, O'Dorisio M, O'Dorisio T, ''et al.'' |title=Selective gene expression and activation-dependent regulation of vasoactive intestinal peptide receptor type 1 and type 2 in human T cells. |journal=J. Immunol. |volume=166 |issue= 4 |pages= 2522-30 |year= 2001 |pmid= 11160313 |doi= }}
*{{cite journal | author=Martin Shreeve S |title=Identification of G-proteins coupling to the vasoactive intestinal peptide receptor VPAC(1) using immunoaffinity chromatography: evidence for precoupling. |journal=Biochem. Biophys. Res. Commun. |volume=290 |issue= 4 |pages= 1300-7 |year= 2002 |pmid= 11812005 |doi= 10.1006/bbrc.2002.6342 }}
*{{cite journal | author=Dorsam G, Goetzl EJ |title=Vasoactive intestinal peptide receptor-1 (VPAC-1) is a novel gene target of the hemolymphopoietic transcription factor Ikaros. |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 13488-93 |year= 2002 |pmid= 11812772 |doi= 10.1074/jbc.M107922200 }}
*{{cite journal | author=Branch DR, Valenta LJ, Yousefi S, ''et al.'' |title=VPAC1 is a cellular neuroendocrine receptor expressed on T cells that actively facilitates productive HIV-1 infection. |journal=AIDS |volume=16 |issue= 3 |pages= 309-19 |year= 2002 |pmid= 11834941 |doi= }}
}}
{{refend}}
{{protein-stub}}
end log.
