- INFO: Beginning work on AHR... {November 12, 2007 5:41:19 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 5:44:29 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Aryl hydrocarbon receptor
| HGNCid = 348
| Symbol = AHR
| AltSymbols =;
| OMIM = 600253
| ECnumber =
| Homologene = 1224
| MGIid = 105043
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0004879 |text = ligand-dependent nuclear receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006950 |text = response to stress}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0009410 |text = response to xenobiotic stimulus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 196
| Hs_Ensembl = ENSG00000106546
| Hs_RefseqProtein = NP_001612
| Hs_RefseqmRNA = NM_001621
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 17304832
| Hs_GenLoc_end = 17349400
| Hs_Uniprot = P35869
| Mm_EntrezGene = 11622
| Mm_Ensembl = ENSMUSG00000019256
| Mm_RefseqmRNA = NM_013464
| Mm_RefseqProtein = NP_038492
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 36088776
| Mm_GenLoc_end = 36119695
| Mm_Uniprot = Q3U2B1
}}
}}
'''Aryl hydrocarbon receptor''', also known as '''AHR''', is a human [[gene]].
<!-- 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 ligand-activated transcription factor involved in the regulation of biological responses to planar aromatic hydrocarbons. This receptor has been shown to regulate xenobiotic-metabolizing enzymes such as cytochrome P450. Its ligands included a variety of aromatic hydrocarbons.<ref>{{cite web | title = Entrez Gene: AHR aryl hydrocarbon receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=196| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hahn ME |title=The aryl hydrocarbon receptor: a comparative perspective. |journal=Comp. Biochem. Physiol. C, Pharmacol. Toxicol. Endocrinol. |volume=121 |issue= 1-3 |pages= 23-53 |year= 1999 |pmid= 9972449 |doi= }}
*{{cite journal | author=Puga A, Xia Y, Elferink C |title=Role of the aryl hydrocarbon receptor in cell cycle regulation. |journal=Chem. Biol. Interact. |volume=141 |issue= 1-2 |pages= 117-30 |year= 2002 |pmid= 12213388 |doi= }}
*{{cite journal | author=Harper PA, Wong JY, Lam MS, Okey AB |title=Polymorphisms in the human AH receptor. |journal=Chem. Biol. Interact. |volume=141 |issue= 1-2 |pages= 161-87 |year= 2002 |pmid= 12213390 |doi= }}
*{{cite journal | author=Safe S, Wormke M, Samudio I |title=Mechanisms of inhibitory aryl hydrocarbon receptor-estrogen receptor crosstalk in human breast cancer cells. |journal=Journal of mammary gland biology and neoplasia |volume=5 |issue= 3 |pages= 295-306 |year= 2004 |pmid= 14973392 |doi= }}
*{{cite journal | author=Fujii-Kuriyama Y, Mimura J |title=Molecular mechanisms of AhR functions in the regulation of cytochrome P450 genes. |journal=Biochem. Biophys. Res. Commun. |volume=338 |issue= 1 |pages= 311-7 |year= 2005 |pmid= 16153594 |doi= 10.1016/j.bbrc.2005.08.162 }}
*{{cite journal | author=Ramadoss P, Marcus C, Perdew GH |title=Role of the aryl hydrocarbon receptor in drug metabolism. |journal=Expert opinion on drug metabolism & toxicology |volume=1 |issue= 1 |pages= 9-21 |year= 2006 |pmid= 16922649 |doi= 10.1517/17425255.1.1.9 }}
*{{cite journal | author=Yamaguchi Y, Kuo MT |title=Functional analysis of aryl hydrocarbon receptor nuclear translocator interactions with aryl hydrocarbon receptor in the yeast two-hybrid system. |journal=Biochem. Pharmacol. |volume=50 |issue= 8 |pages= 1295-302 |year= 1995 |pmid= 7488247 |doi= }}
*{{cite journal | author=Hayashi S, Watanabe J, Nakachi K, ''et al.'' |title=Interindividual difference in expression of human Ah receptor and related P450 genes. |journal=Carcinogenesis |volume=15 |issue= 5 |pages= 801-6 |year= 1994 |pmid= 7515333 |doi= }}
*{{cite journal | author=Kawajiri K, Watanabe J, Eguchi H, ''et al.'' |title=Polymorphisms of human Ah receptor gene are not involved in lung cancer. |journal=Pharmacogenetics |volume=5 |issue= 3 |pages= 151-8 |year= 1995 |pmid= 7550366 |doi= }}
*{{cite journal | author=Adams MD, Kerlavage AR, Fleischmann RD, ''et al.'' |title=Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. |journal=Nature |volume=377 |issue= 6547 Suppl |pages= 3-174 |year= 1995 |pmid= 7566098 |doi= }}
*{{cite journal | author=Lindebro MC, Poellinger L, Whitelaw ML |title=Protein-protein interaction via PAS domains: role of the PAS domain in positive and negative regulation of the bHLH/PAS dioxin receptor-Arnt transcription factor complex. |journal=EMBO J. |volume=14 |issue= 14 |pages= 3528-39 |year= 1995 |pmid= 7628454 |doi= }}
*{{cite journal | author=Abbott BD, Probst MR, Perdew GH |title=Immunohistochemical double-staining for Ah receptor and ARNT in human embryonic palatal shelves. |journal=Teratology |volume=50 |issue= 5 |pages= 361-6 |year= 1995 |pmid= 7716743 |doi= 10.1002/tera.1420500507 }}
*{{cite journal | author=Ema M, Matsushita N, Sogawa K, ''et al.'' |title=Human arylhydrocarbon receptor: functional expression and chromosomal assignment to 7p21. |journal=J. Biochem. |volume=116 |issue= 4 |pages= 845-51 |year= 1995 |pmid= 7883760 |doi= }}
*{{cite journal | author=Ema M, Ohe N, Suzuki M, ''et al.'' |title=Dioxin binding activities of polymorphic forms of mouse and human arylhydrocarbon receptors. |journal=J. Biol. Chem. |volume=269 |issue= 44 |pages= 27337-43 |year= 1994 |pmid= 7961644 |doi= }}
*{{cite journal | author=Chen HS, Perdew GH |title=Subunit composition of the heteromeric cytosolic aryl hydrocarbon receptor complex. |journal=J. Biol. Chem. |volume=269 |issue= 44 |pages= 27554-8 |year= 1994 |pmid= 7961671 |doi= }}
*{{cite journal | author=Eguchi H, Hayashi S, Watanabe J, ''et al.'' |title=Molecular cloning of the human AH receptor gene promoter. |journal=Biochem. Biophys. Res. Commun. |volume=203 |issue= 1 |pages= 615-22 |year= 1994 |pmid= 8074712 |doi= }}
*{{cite journal | author=Le Beau MM, Carver LA, Espinosa R, ''et al.'' |title=Chromosomal localization of the human AHR locus encoding the structural gene for the Ah receptor to 7p21-->p15. |journal=Cytogenet. Cell Genet. |volume=66 |issue= 3 |pages= 172-6 |year= 1994 |pmid= 8125016 |doi= }}
*{{cite journal | author=Dolwick KM, Schmidt JV, Carver LA, ''et al.'' |title=Cloning and expression of a human Ah receptor cDNA. |journal=Mol. Pharmacol. |volume=44 |issue= 5 |pages= 911-7 |year= 1994 |pmid= 8246913 |doi= }}
*{{cite journal | author=Whitelaw M, Pongratz I, Wilhelmsson A, ''et al.'' |title=Ligand-dependent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptor. |journal=Mol. Cell. Biol. |volume=13 |issue= 4 |pages= 2504-14 |year= 1993 |pmid= 8384309 |doi= }}
*{{cite journal | author=Itoh S, Kamataki T |title=Human Ah receptor cDNA: analysis for highly conserved sequences. |journal=Nucleic Acids Res. |volume=21 |issue= 15 |pages= 3578 |year= 1993 |pmid= 8393992 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on B2M... {November 12, 2007 5:45:27 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 5:46:07 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_B2M_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a1m.
| PDB = {{PDB2|1a1m}}, {{PDB2|1a1n}}, {{PDB2|1a1o}}, {{PDB2|1a6z}}, {{PDB2|1a9b}}, {{PDB2|1a9e}}, {{PDB2|1agb}}, {{PDB2|1agc}}, {{PDB2|1agd}}, {{PDB2|1age}}, {{PDB2|1agf}}, {{PDB2|1akj}}, {{PDB2|1ao7}}, {{PDB2|1b0g}}, {{PDB2|1b0r}}, {{PDB2|1bd2}}, {{PDB2|1c16}}, {{PDB2|1ce6}}, {{PDB2|1cg9}}, {{PDB2|1de4}}, {{PDB2|1duy}}, {{PDB2|1duz}}, {{PDB2|1e27}}, {{PDB2|1e28}}, {{PDB2|1eey}}, {{PDB2|1eez}}, {{PDB2|1efx}}, {{PDB2|1exu}}, {{PDB2|1gzp}}, {{PDB2|1gzq}}, {{PDB2|1hhg}}, {{PDB2|1hhh}}, {{PDB2|1hhi}}, {{PDB2|1hhj}}, {{PDB2|1hhk}}, {{PDB2|1hla}}, {{PDB2|1hsa}}, {{PDB2|1hsb}}, {{PDB2|1i1f}}, {{PDB2|1i1y}}, {{PDB2|1i4f}}, {{PDB2|1i7r}}, {{PDB2|1i7t}}, {{PDB2|1i7u}}, {{PDB2|1im3}}, {{PDB2|1im9}}, {{PDB2|1jf1}}, {{PDB2|1jgd}}, {{PDB2|1jge}}, {{PDB2|1jht}}, {{PDB2|1jnj}}, {{PDB2|1k5n}}, {{PDB2|1kpr}}, {{PDB2|1ktl}}, {{PDB2|1lds}}, {{PDB2|1lp9}}, {{PDB2|1m05}}, {{PDB2|1m6o}}, {{PDB2|1mhe}}, {{PDB2|1mi5}}, {{PDB2|1n2r}}, {{PDB2|1of2}}, {{PDB2|1oga}}, {{PDB2|1ogt}}, {{PDB2|1onq}}, {{PDB2|1p7q}}, {{PDB2|1py4}}, {{PDB2|1q94}}, {{PDB2|1qew}}, {{PDB2|1qlf}}, {{PDB2|1qqd}}, {{PDB2|1qr1}}, {{PDB2|1qrn}}, {{PDB2|1qse}}, {{PDB2|1qsf}}, {{PDB2|1qvo}}, {{PDB2|1r3h}}, {{PDB2|1s8d}}, {{PDB2|1s9w}}, {{PDB2|1s9x}}, {{PDB2|1s9y}}, {{PDB2|1sys}}, {{PDB2|1syv}}, {{PDB2|1t1w}}, {{PDB2|1t1x}}, {{PDB2|1t1y}}, {{PDB2|1t1z}}, {{PDB2|1t20}}, {{PDB2|1t21}}, {{PDB2|1t22}}, {{PDB2|1tmc}}, {{PDB2|1tvb}}, {{PDB2|1tvh}}, {{PDB2|1uqs}}, {{PDB2|1uxs}}, {{PDB2|1uxw}}, {{PDB2|1vgk}}, {{PDB2|1w0v}}, {{PDB2|1w0w}}, {{PDB2|1w72}}, {{PDB2|1x7q}}, {{PDB2|1xh3}}, {{PDB2|1xr8}}, {{PDB2|1xr9}}, {{PDB2|1xz0}}, {{PDB2|1ydp}}, {{PDB2|1ypz}}, {{PDB2|1zhk}}, {{PDB2|1zhl}}, {{PDB2|1zs8}}, {{PDB2|1zsd}}, {{PDB2|1zt4}}, {{PDB2|1zvs}}, {{PDB2|2a83}}, {{PDB2|2ak4}}, {{PDB2|2av1}}, {{PDB2|2av7}}, {{PDB2|2axf}}, {{PDB2|2axg}}, {{PDB2|2bck}}, {{PDB2|2bnq}}, {{PDB2|2bnr}}, {{PDB2|2bsr}}, {{PDB2|2bss}}, {{PDB2|2bst}}, {{PDB2|2bsu}}, {{PDB2|2bsv}}, {{PDB2|2bvo}}, {{PDB2|2bvp}}, {{PDB2|2bvq}}, {{PDB2|2c7u}}, {{PDB2|2cii}}, {{PDB2|2cik}}, {{PDB2|2clr}}, {{PDB2|2d31}}, {{PDB2|2d4d}}, {{PDB2|2d4f}}, {{PDB2|2dyp}}, {{PDB2|2esv}}, {{PDB2|2f53}}, {{PDB2|2f54}}, {{PDB2|2f74}}, {{PDB2|2f8o}}, {{PDB2|2fyy}}, {{PDB2|2fz3}}, {{PDB2|2git}}, {{PDB2|2gj6}}, {{PDB2|2h26}}, {{PDB2|2h6p}}, {{PDB2|2hjk}}, {{PDB2|2hjl}}, {{PDB2|2hla}}, {{PDB2|2hn7}}, {{PDB2|2nw3}}, {{PDB2|2nx5}}, {{PDB2|3hla}}
| Name = Beta-2-microglobulin
| HGNCid = 914
| Symbol = B2M
| AltSymbols =;
| OMIM = 109700
| ECnumber =
| Homologene = 2987
| MGIid = 88127
| GeneAtlas_image1 = PBB_GE_B2M_201891_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_B2M_216231_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0042612 |text = MHC class I protein complex}}
| Process = {{GNF_GO|id=GO:0002474 |text = antigen processing and presentation of peptide antigen via MHC class I}} {{GNF_GO|id=GO:0006955 |text = immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 567
| Hs_Ensembl = ENSG00000166710
| Hs_RefseqProtein = NP_004039
| Hs_RefseqmRNA = NM_004048
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 42790977
| Hs_GenLoc_end = 42797649
| Hs_Uniprot = P61769
| Mm_EntrezGene = 12010
| Mm_Ensembl = ENSMUSG00000060802
| Mm_RefseqmRNA = NM_009735
| Mm_RefseqProtein = NP_033865
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 121839127
| Mm_GenLoc_end = 121844524
| Mm_Uniprot = Q3U679
}}
}}
'''Beta-2-microglobulin''', also known as '''B2M''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Winchester JF, Salsberg JA, Levin NW |title=Beta-2 microglobulin in ESRD: an in-depth review. |journal=Advances in renal replacement therapy |volume=10 |issue= 4 |pages= 279-309 |year= 2004 |pmid= 14681859 |doi= }}
*{{cite journal | author=Krangel MS, Orr HT, Strominger JL |title=Assembly and maturation of HLA-A and HLA-B antigens in vivo. |journal=Cell |volume=18 |issue= 4 |pages= 979-91 |year= 1980 |pmid= 93026 |doi= }}
*{{cite journal | author=Okon M, Bray P, Vucelić D |title=1H NMR assignments and secondary structure of human beta 2-microglobulin in solution. |journal=Biochemistry |volume=31 |issue= 37 |pages= 8906-15 |year= 1992 |pmid= 1390678 |doi= }}
*{{cite journal | author=Guo HC, Jardetzky TS, Garrett TP, ''et al.'' |title=Different length peptides bind to HLA-Aw68 similarly at their ends but bulge out in the middle. |journal=Nature |volume=360 |issue= 6402 |pages= 364-6 |year= 1992 |pmid= 1448153 |doi= 10.1038/360364a0 }}
*{{cite journal | author=Gattoni-Celli S, Kirsch K, Timpane R, Isselbacher KJ |title=Beta 2-microglobulin gene is mutated in a human colon cancer cell line (HCT) deficient in the expression of HLA class I antigens on the cell surface. |journal=Cancer Res. |volume=52 |issue= 5 |pages= 1201-4 |year= 1992 |pmid= 1737380 |doi= }}
*{{cite journal | author=Saper MA, Bjorkman PJ, Wiley DC |title=Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolution. |journal=J. Mol. Biol. |volume=219 |issue= 2 |pages= 277-319 |year= 1991 |pmid= 2038058 |doi= }}
*{{cite journal | author=Caruana RJ, Lobel SA, Leffell MS, ''et al.'' |title=Tumor necrosis factor, interleukin-1 and beta 2-microglobulin levels in chronic hemodialysis patients. |journal=The International journal of artificial organs |volume=13 |issue= 12 |pages= 794-8 |year= 1991 |pmid= 2289831 |doi= }}
*{{cite journal | author=Connors LH, Shirahama T, Skinner M, ''et al.'' |title=In vitro formation of amyloid fibrils from intact beta 2-microglobulin. |journal=Biochem. Biophys. Res. Commun. |volume=131 |issue= 3 |pages= 1063-8 |year= 1985 |pmid= 2413854 |doi= }}
*{{cite journal | author=Hochman JH, Shimizu Y, DeMars R, Edidin M |title=Specific associations of fluorescent beta-2-microglobulin with cell surfaces. The affinity of different H-2 and HLA antigens for beta-2-microglobulin. |journal=J. Immunol. |volume=140 |issue= 7 |pages= 2322-9 |year= 1988 |pmid= 2450918 |doi= }}
*{{cite journal | author=Homma N, Gejyo F, Isemura M, Arakawa M |title=Collagen-binding affinity of beta-2-microglobulin, a preprotein of hemodialysis-associated amyloidosis. |journal=Nephron |volume=53 |issue= 1 |pages= 37-40 |year= 1989 |pmid= 2674742 |doi= }}
*{{cite journal | author=Bataille R, Grenier J, Commes T |title=In vitro production of beta 2 microglobulin by human myeloma cells. |journal=Cancer Invest. |volume=6 |issue= 3 |pages= 271-7 |year= 1988 |pmid= 3048575 |doi= }}
*{{cite journal | author=Hönig R, Marsen T, Schad S, ''et al.'' |title=Correlation of beta-2-microglobulin concentration changes to changes of distribution volume. |journal=The International journal of artificial organs |volume=11 |issue= 6 |pages= 459-64 |year= 1989 |pmid= 3060434 |doi= }}
*{{cite journal | author=Bjorkman PJ, Saper MA, Samraoui B, ''et al.'' |title=Structure of the human class I histocompatibility antigen, HLA-A2. |journal=Nature |volume=329 |issue= 6139 |pages= 506-12 |year= 1987 |pmid= 3309677 |doi= 10.1038/329506a0 }}
*{{cite journal | author=Güssow D, Rein R, Ginjaar I, ''et al.'' |title=The human beta 2-microglobulin gene. Primary structure and definition of the transcriptional unit. |journal=J. Immunol. |volume=139 |issue= 9 |pages= 3132-8 |year= 1987 |pmid= 3312414 |doi= }}
*{{cite journal | author=Cunningham BA, Wang JL, Berggård I, Peterson PA |title=The complete amino acid sequence of beta 2-microglobulin. |journal=Biochemistry |volume=12 |issue= 24 |pages= 4811-22 |year= 1974 |pmid= 4586824 |doi= }}
*{{cite journal | author=Suggs SV, Wallace RB, Hirose T, ''et al.'' |title=Use of synthetic oligonucleotides as hybridization probes: isolation of cloned cDNA sequences for human beta 2-microglobulin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=78 |issue= 11 |pages= 6613-7 |year= 1982 |pmid= 6171820 |doi= }}
*{{cite journal | author=Momoi T, Suzuki M, Titani K, ''et al.'' |title=Amino acid sequence of a modified beta 2-microglobulin in renal failure patient urine and long-term dialysis patient blood. |journal=Clin. Chim. Acta |volume=236 |issue= 2 |pages= 135-44 |year= 1995 |pmid= 7554280 |doi= }}
*{{cite journal | author=Collins EJ, Garboczi DN, Karpusas MN, Wiley DC |title=The three-dimensional structure of a class I major histocompatibility complex molecule missing the alpha 3 domain of the heavy chain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 4 |pages= 1218-21 |year= 1995 |pmid= 7862664 |doi= }}
*{{cite journal | author=Matoba R, Okubo K, Hori N, ''et al.'' |title=The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression. |journal=Gene |volume=146 |issue= 2 |pages= 199-207 |year= 1994 |pmid= 8076819 |doi= }}
*{{cite journal | author=Wang Z, Cao Y, Albino AP, ''et al.'' |title=Lack of HLA class I antigen expression by melanoma cells SK-MEL-33 caused by a reading frameshift in beta 2-microglobulin messenger RNA. |journal=J. Clin. Invest. |volume=91 |issue= 2 |pages= 684-92 |year= 1993 |pmid= 8432869 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CCNB1... {November 12, 2007 5:46:08 PM PST}
- SEARCH REDIRECT: Control Box Found: CCNB1 {November 12, 2007 5:46:45 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 12, 2007 5:46:47 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 12, 2007 5:46:47 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 12, 2007 5:46:47 PM PST}
- UPDATED: Updated protein page: CCNB1 {November 12, 2007 5:46:54 PM PST}
- INFO: Beginning work on CDK4... {November 12, 2007 5:46:55 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 5:47:15 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Cyclin-dependent kinase 4
| HGNCid = 1773
| Symbol = CDK4
| AltSymbols =; CMM3; MGC14458; PSK-J3
| OMIM = 123829
| ECnumber =
| Homologene = 55429
| MGIid = 88357
| GeneAtlas_image1 = PBB_GE_CDK4_202246_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004672 |text = protein kinase activity}} {{GNF_GO|id=GO:0004693 |text = cyclin-dependent protein 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}}
| Component = {{GNF_GO|id=GO:0000307 |text = cyclin-dependent protein kinase holoenzyme complex}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005667 |text = transcription factor complex}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0000082 |text = G1/S transition of mitotic cell cycle}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0042127 |text = regulation of cell proliferation}} {{GNF_GO|id=GO:0051301 |text = cell division}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1019
| Hs_Ensembl = ENSG00000135446
| Hs_RefseqProtein = NP_000066
| Hs_RefseqmRNA = NM_000075
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 56428272
| Hs_GenLoc_end = 56432431
| Hs_Uniprot = P11802
| Mm_EntrezGene = 12567
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_009870
| Mm_RefseqProtein = NP_034000
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Cyclin-dependent kinase 4''', also known as '''CDK4''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the Ser/Thr protein kinase family. This protein is highly similar to the gene products of S. cerevisiae cdc28 and S. pombe cdc2. It is a catalytic subunit of the protein kinase complex that is important for cell cycle G1 phase progression. The activity of this kinase is restricted to the G1-S phase, which is controlled by the regulatory subunits D-type cyclins and CDK inhibitor p16(INK4a). This kinase was shown to be responsible for the phosphorylation of retinoblastoma gene product (Rb). Mutations in this gene as well as in its related proteins including D-type cyclins, p16(INK4a) and Rb were all found to be associated with tumorigenesis of a variety of cancers. Multiple polyadenylation sites of this gene have been reported.<ref>{{cite web | title = Entrez Gene: CDK4 cyclin-dependent kinase 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1019| accessdate = }}</ref>
}}
==References==
{{reflist}}
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CRK... {November 12, 2007 5:47:15 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 5:48:02 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CRK_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1b07.
| PDB = {{PDB2|1b07}}, {{PDB2|1cka}}, {{PDB2|1ckb}}, {{PDB2|1ju5}}, {{PDB2|1m30}}, {{PDB2|1m3a}}, {{PDB2|1m3b}}, {{PDB2|1m3c}}, {{PDB2|2dvj}}, {{PDB2|2eyv}}, {{PDB2|2eyw}}, {{PDB2|2eyx}}, {{PDB2|2eyy}}, {{PDB2|2eyz}}, {{PDB2|2ggr}}
| Name = V-crk sarcoma virus CT10 oncogene homolog (avian)
| HGNCid = 2362
| Symbol = CRK
| AltSymbols =; CRKII
| OMIM = 164762
| ECnumber =
| Homologene = 81850
| MGIid = 88508
| GeneAtlas_image1 = PBB_GE_CRK_202224_at_tn.png
| GeneAtlas_image2 = PBB_GE_CRK_202225_at_tn.png
| GeneAtlas_image3 = PBB_GE_CRK_202226_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005070 |text = SH3/SH2 adaptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0042169 |text = SH2 domain binding}} {{GNF_GO|id=GO:0045309 |text = protein phosphorylated amino acid binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006357 |text = regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0030036 |text = actin cytoskeleton organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1398
| Hs_Ensembl = ENSG00000167193
| Hs_RefseqProtein = NP_005197
| Hs_RefseqmRNA = NM_005206
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 1270733
| Hs_GenLoc_end = 1306302
| Hs_Uniprot = P46108
| Mm_EntrezGene = 12928
| Mm_Ensembl = ENSMUSG00000017776
| Mm_RefseqmRNA = NM_133656
| Mm_RefseqProtein = NP_598417
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 75495505
| Mm_GenLoc_end = 75522289
| Mm_Uniprot = Q3TQV3
}}
}}
'''V-crk sarcoma virus CT10 oncogene homolog (avian)''', also known as '''CRK''', is a human [[gene]].
<!-- 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 an adapter protein family that binds to several tyrosine-phosphorylated proteins. The product of this gene has several SH2 and SH3 domains (src-homology domains) and is involved in several signaling pathways, recruiting cytoplasmic proteins in the vicinity of tyrosine kinase through SH2-phosphotyrosine interaction. The N-terminal SH2 domain of this protein functions as a positive regulator of transformation whereas the C-terminal SH3 domain functions as a negative regulator of transformation. Two alternative transcripts encoding different isoforms with distinct biological activity have been described.<ref>{{cite web | title = Entrez Gene: CRK v-crk sarcoma virus CT10 oncogene homolog (avian)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1398| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Feller SM, Ren R, Hanafusa H, Baltimore D |title=SH2 and SH3 domains as molecular adhesives: the interactions of Crk and Abl. |journal=Trends Biochem. Sci. |volume=19 |issue= 11 |pages= 453-8 |year= 1995 |pmid= 7855886 |doi= }}
*{{cite journal | author=Feller SM, Posern G, Voss J, ''et al.'' |title=Physiological signals and oncogenesis mediated through Crk family adapter proteins. |journal=J. Cell. Physiol. |volume=177 |issue= 4 |pages= 535-52 |year= 1999 |pmid= 10092207 |doi= 10.1002/(SICI)1097-4652(199812)177:4<535::AID-JCP5>3.0.CO;2-E }}
*{{cite journal | author=Pessin JE, Okada S |title=Insulin and EGF receptors integrate the Ras and Rap signaling pathways. |journal=Endocr. J. |volume=46 Suppl |issue= |pages= S11-6 |year= 2002 |pmid= 12054111 |doi= }}
*{{cite journal | author=Cicchetti P, Mayer BJ, Thiel G, Baltimore D |title=Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho. |journal=Science |volume=257 |issue= 5071 |pages= 803-6 |year= 1992 |pmid= 1379745 |doi= }}
*{{cite journal | author=Matsuda M, Tanaka S, Nagata S, ''et al.'' |title=Two species of human CRK cDNA encode proteins with distinct biological activities. |journal=Mol. Cell. Biol. |volume=12 |issue= 8 |pages= 3482-9 |year= 1992 |pmid= 1630456 |doi= }}
*{{cite journal | author=Mayer BJ, Hanafusa H |title=Association of the v-crk oncogene product with phosphotyrosine-containing proteins and protein kinase activity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 7 |pages= 2638-42 |year= 1990 |pmid= 1690891 |doi= }}
*{{cite journal | author=Anderson D, Koch CA, Grey L, ''et al.'' |title=Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors. |journal=Science |volume=250 |issue= 4983 |pages= 979-82 |year= 1990 |pmid= 2173144 |doi= }}
*{{cite journal | author=Schaller MD, Hildebrand JD, Shannon JD, ''et al.'' |title=Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src. |journal=Mol. Cell. Biol. |volume=14 |issue= 3 |pages= 1680-8 |year= 1994 |pmid= 7509446 |doi= }}
*{{cite journal | author=Hempstead BL, Birge RB, Fajardo JE, ''et al.'' |title=Expression of the v-crk oncogene product in PC12 cells results in rapid differentiation by both nerve growth factor- and epidermal growth factor-dependent pathways. |journal=Mol. Cell. Biol. |volume=14 |issue= 3 |pages= 1964-71 |year= 1994 |pmid= 7509449 |doi= }}
*{{cite journal | author=Tanaka S, Morishita T, Hashimoto Y, ''et al.'' |title=C3G, a guanine nucleotide-releasing protein expressed ubiquitously, binds to the Src homology 3 domains of CRK and GRB2/ASH proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 8 |pages= 3443-7 |year= 1994 |pmid= 7512734 |doi= }}
*{{cite journal | author=Calalb MB, Polte TR, Hanks SK |title=Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases. |journal=Mol. Cell. Biol. |volume=15 |issue= 2 |pages= 954-63 |year= 1995 |pmid= 7529876 |doi= }}
*{{cite journal | author=Teng KK, Lander H, Fajardo JE, ''et al.'' |title=v-Crk modulation of growth factor-induced PC12 cell differentiation involves the Src homology 2 domain of v-Crk and sustained activation of the Ras/mitogen-activated protein kinase pathway. |journal=J. Biol. Chem. |volume=270 |issue= 35 |pages= 20677-85 |year= 1995 |pmid= 7657647 |doi= }}
*{{cite journal | author=Schumacher C, Knudsen BS, Ohuchi T, ''et al.'' |title=The SH3 domain of Crk binds specifically to a conserved proline-rich motif in Eps15 and Eps15R. |journal=J. Biol. Chem. |volume=270 |issue= 25 |pages= 15341-7 |year= 1995 |pmid= 7797522 |doi= }}
*{{cite journal | author=Matsuda M, Hashimoto Y, Muroya K, ''et al.'' |title=CRK protein binds to two guanine nucleotide-releasing proteins for the Ras family and modulates nerve growth factor-induced activation of Ras in PC12 cells. |journal=Mol. Cell. Biol. |volume=14 |issue= 8 |pages= 5495-500 |year= 1994 |pmid= 8035825 |doi= }}
*{{cite journal | author=Feller SM, Knudsen B, Hanafusa H |title=c-Abl kinase regulates the protein binding activity of c-Crk. |journal=EMBO J. |volume=13 |issue= 10 |pages= 2341-51 |year= 1994 |pmid= 8194526 |doi= }}
*{{cite journal | author=Fioretos T, Heisterkamp N, Groffen J, ''et al.'' |title=CRK proto-oncogene maps to human chromosome band 17p13. |journal=Oncogene |volume=8 |issue= 10 |pages= 2853-5 |year= 1993 |pmid= 8378094 |doi= }}
*{{cite journal | author=Smit L, van der Horst G, Borst J |title=Sos, Vav, and C3G participate in B cell receptor-induced signaling pathways and differentially associate with Shc-Grb2, Crk, and Crk-L adaptors. |journal=J. Biol. Chem. |volume=271 |issue= 15 |pages= 8564-9 |year= 1996 |pmid= 8621483 |doi= }}
*{{cite journal | author=Beitner-Johnson D, Blakesley VA, Shen-Orr Z, ''et al.'' |title=The proto-oncogene product c-Crk associates with insulin receptor substrate-1 and 4PS. Modulation by insulin growth factor-I (IGF) and enhanced IGF-I signaling. |journal=J. Biol. Chem. |volume=271 |issue= 16 |pages= 9287-90 |year= 1996 |pmid= 8621590 |doi= }}
*{{cite journal | author=Hasegawa H, Kiyokawa E, Tanaka S, ''et al.'' |title=DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane. |journal=Mol. Cell. Biol. |volume=16 |issue= 4 |pages= 1770-6 |year= 1996 |pmid= 8657152 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CSNK2B... {November 12, 2007 5:48:02 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 5:48:33 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CSNK2B_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1jwh.
| PDB = {{PDB2|1jwh}}, {{PDB2|1qf8}}, {{PDB2|1rqf}}
| Name = Casein kinase 2, beta polypeptide
| HGNCid = 2460
| Symbol = CSNK2B
| AltSymbols =; CK2B; CK2N; CSK2B; G5A; MGC138222; MGC138224
| OMIM = 115441
| ECnumber =
| Homologene = 55572
| MGIid = 88548
| GeneAtlas_image1 = PBB_GE_CSNK2B_201390_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004682 |text = protein kinase CK2 activity}} {{GNF_GO|id=GO:0008605 |text = protein kinase CK2 regulator activity}} {{GNF_GO|id=GO:0016301 |text = kinase activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0005956 |text = protein kinase CK2 complex}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0016055 |text = Wnt receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1460
| Hs_Ensembl = ENSG00000206300
| Hs_RefseqProtein = NP_001311
| Hs_RefseqmRNA = NM_001320
| Hs_GenLoc_db =
| Hs_GenLoc_chr = c6_COX
| Hs_GenLoc_start = 31768327
| Hs_GenLoc_end = 31775955
| Hs_Uniprot = P67870
| Mm_EntrezGene = 13001
| Mm_Ensembl = ENSMUSG00000024387
| Mm_RefseqmRNA = NM_009975
| Mm_RefseqProtein = NP_034105
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 34724251
| Mm_GenLoc_end = 34729503
| Mm_Uniprot = P67871
}}
}}
'''Casein kinase 2, beta polypeptide''', also known as '''CSNK2B''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes the beta subunit of casein kinase II, a ubiquitous protein kinase which regulates metabolic pathways, signal transduction, transcription, translation, and replication. The enzyme is composed of three subunits, alpha, alpha prime and beta, which form a tetrameric holoenzyme. The alpha and alpha prime subunits are catalytic, while the beta subunit serves regulatory functions. The enzyme localizes to the endoplasmic reticulum and the Golgi apparatus.<ref>{{cite web | title = Entrez Gene: CSNK2B casein kinase 2, beta polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1460| accessdate = }}</ref>
}}
==References==
{{reflist}}
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CYP3A4... {November 12, 2007 5:48:34 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 5:49:31 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CYP3A4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1tqn.
| PDB = {{PDB2|1tqn}}, {{PDB2|1w0e}}, {{PDB2|1w0f}}, {{PDB2|1w0g}}, {{PDB2|2j0c}}, {{PDB2|2j0d}}
| Name = Cytochrome P450, family 3, subfamily A, polypeptide 4
| HGNCid = 2637
| Symbol = CYP3A4
| AltSymbols =; CYP3A; CP33; CP34; CYP3A3; HLP; MGC126680; NF-25; P450C3; P450PCN1
| OMIM = 124010
| ECnumber =
| Homologene = 88816
| MGIid =
| GeneAtlas_image1 = PBB_GE_CYP3A4_205999_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_CYP3A4_205998_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_CYP3A4_208367_x_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:0016712 |text = oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen}} {{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}} {{GNF_GO|id=GO:0050381 |text = unspecific monooxygenase activity}} {{GNF_GO|id=GO:0050591 |text = quinine 3-monooxygenase activity}} {{GNF_GO|id=GO:0050649 |text = testosterone 6-beta-hydroxylase activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0009986 |text = cell surface}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006805 |text = xenobiotic metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1576
| Hs_Ensembl = ENSG00000160868
| Hs_RefseqProtein = NP_059488
| Hs_RefseqmRNA = NM_017460
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 99083437
| Hs_GenLoc_end = 99219744
| Hs_Uniprot = P05184
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Cytochrome P450, family 3, subfamily A, polypeptide 4''', also known as '''CYP3A4''', is a human [[gene]].
<!-- 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, CYP3A4, 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 endoplasmic reticulum and its expression is induced by glucocorticoids and some pharmacological agents. This enzyme is involved in the metabolism of approximately half the drugs which are are used today, including acetaminophen, codeine, cyclosporin A, diazepam and erythromycin. The enzyme also metabolizes some steroids and carcinogens. This gene is part of a cluster of cytochrome P450 genes on chromosome 7q21.1. Previously another CYP3A gene, CYP3A3, was thought to exist; however, it is now thought that this sequence represents a transcript variant of CYP3A4.<ref>{{cite web | title = Entrez Gene: CYP3A4 cytochrome P450, family 3, subfamily A, polypeptide 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1576| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Smith G, Stubbins MJ, Harries LW, Wolf CR |title=Molecular genetics of the human cytochrome P450 monooxygenase superfamily. |journal=Xenobiotica |volume=28 |issue= 12 |pages= 1129-65 |year= 1999 |pmid= 9890157 |doi= }}
*{{cite journal | author=Guengerich FP |title=Cytochrome P-450 3A4: regulation and role in drug metabolism. |journal=Annu. Rev. Pharmacol. Toxicol. |volume=39 |issue= |pages= 1-17 |year= 1999 |pmid= 10331074 |doi= 10.1146/annurev.pharmtox.39.1.1 }}
*{{cite journal | author=Zhou S, Chan E, Pan SQ, ''et al.'' |title=Pharmacokinetic interactions of drugs with St John's wort. |journal=J. Psychopharmacol. (Oxford) |volume=18 |issue= 2 |pages= 262-76 |year= 2004 |pmid= 15260917 |doi= 10.1177/0269881104042632 }}
*{{cite journal | author=Lee SJ, Goldstein JA |title=Functionally defective or altered CYP3A4 and CYP3A5 single nucleotide polymorphisms and their detection with genotyping tests. |journal=Pharmacogenomics |volume=6 |issue= 4 |pages= 357-71 |year= 2006 |pmid= 16004554 |doi= 10.1517/14622416.6.4.357 }}
*{{cite journal | author=Inoue K, Inazawa J, Nakagawa H, ''et al.'' |title=Assignment of the human cytochrome P-450 nifedipine oxidase gene (CYP3A4) to chromosome 7 at band q22.1 by fluorescence in situ hybridization. |journal=Jpn. J. Hum. Genet. |volume=37 |issue= 2 |pages= 133-8 |year= 1992 |pmid= 1391968 |doi= }}
*{{cite journal | author=Bork RW, Muto T, Beaune PH, ''et al.'' |title=Characterization of mRNA species related to human liver cytochrome P-450 nifedipine oxidase and the regulation of catalytic activity. |journal=J. Biol. Chem. |volume=264 |issue= 2 |pages= 910-9 |year= 1989 |pmid= 2463251 |doi= }}
*{{cite journal | author=Shimada T, Guengerich FP |title=Evidence for cytochrome P-450NF, the nifedipine oxidase, being the principal enzyme involved in the bioactivation of aflatoxins in human liver. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 2 |pages= 462-5 |year= 1989 |pmid= 2492107 |doi= }}
*{{cite journal | author=Spurr NK, Gough AC, Stevenson K, Wolf CR |title=The human cytochrome P450 CYP3 locus: assignment to chromosome 7q22-qter. |journal=Hum. Genet. |volume=81 |issue= 2 |pages= 171-4 |year= 1989 |pmid= 2563251 |doi= }}
*{{cite journal | author=Komori M, Hashizume T, Ohi H, ''et al.'' |title=Cytochrome P-450 in human liver microsomes: high-performance liquid chromatographic isolation of three forms and their characterization. |journal=J. Biochem. |volume=104 |issue= 6 |pages= 912-6 |year= 1989 |pmid= 3243766 |doi= }}
*{{cite journal | author=Gonzalez FJ, Schmid BJ, Umeno M, ''et al.'' |title=Human P450PCN1: sequence, chromosome localization, and direct evidence through cDNA expression that P450PCN1 is nifedipine oxidase. |journal=DNA |volume=7 |issue= 2 |pages= 79-86 |year= 1988 |pmid= 3267210 |doi= }}
*{{cite journal | author=Molowa DT, Schuetz EG, Wrighton SA, ''et al.'' |title=Complete cDNA sequence of a cytochrome P-450 inducible by glucocorticoids in human liver. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 14 |pages= 5311-5 |year= 1986 |pmid= 3460094 |doi= }}
*{{cite journal | author=Beaune PH, Umbenhauer DR, Bork RW, ''et al.'' |title=Isolation and sequence determination of a cDNA clone related to human cytochrome P-450 nifedipine oxidase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 21 |pages= 8064-8 |year= 1986 |pmid= 3464943 |doi= }}
*{{cite journal | author=Watkins PB, Wrighton SA, Maurel P, ''et al.'' |title=Identification of an inducible form of cytochrome P-450 in human liver. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 18 |pages= 6310-4 |year= 1985 |pmid= 3898085 |doi= }}
*{{cite journal | author=Hashimoto H, Toide K, Kitamura R, ''et al.'' |title=Gene structure of CYP3A4, an adult-specific form of cytochrome P450 in human livers, and its transcriptional control. |journal=Eur. J. Biochem. |volume=218 |issue= 2 |pages= 585-95 |year= 1994 |pmid= 8269949 |doi= }}
*{{cite journal | author=Zhang H, Coville PF, Walker RJ, ''et al.'' |title=Evidence for involvement of human CYP3A in the 3-hydroxylation of quinine. |journal=British journal of clinical pharmacology |volume=43 |issue= 3 |pages= 245-52 |year= 1997 |pmid= 9088578 |doi= }}
*{{cite journal | author=Moody DE, Alburges ME, Parker RJ, ''et al.'' |title=The involvement of cytochrome P450 3A4 in the N-demethylation of L-alpha-acetylmethadol (LAAM), norLAAM, and methadone. |journal=Drug Metab. Dispos. |volume=25 |issue= 12 |pages= 1347-53 |year= 1998 |pmid= 9394023 |doi= }}
*{{cite journal | author=Zhao XJ, Kawashiro T, Ishizaki T |title=Mutual inhibition between quinine and etoposide by human liver microsomes. Evidence for cytochrome P4503A4 involvement in their major metabolic pathways. |journal=Drug Metab. Dispos. |volume=26 |issue= 2 |pages= 188-91 |year= 1998 |pmid= 9456308 |doi= }}
*{{cite journal | author=Felix CA, Walker AH, Lange BJ, ''et al.'' |title=Association of CYP3A4 genotype with treatment-related leukemia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 22 |pages= 13176-81 |year= 1998 |pmid= 9789061 |doi= }}
*{{cite journal | author=Korsmeyer KK, Davoll S, Figueiredo-Pereira ME, Correia MA |title=Proteolytic degradation of heme-modified hepatic cytochromes P450: A role for phosphorylation, ubiquitination, and the 26S proteasome? |journal=Arch. Biochem. Biophys. |volume=365 |issue= 1 |pages= 31-44 |year= 1999 |pmid= 10222036 |doi= 10.1006/abbi.1999.1138 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on EIF2AK2... {November 12, 2007 5:56:51 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 5:57:58 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_EIF2AK2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1qu6.
| PDB = {{PDB2|1qu6}}, {{PDB2|2a19}}, {{PDB2|2a1a}}
| Name = Eukaryotic translation initiation factor 2-alpha kinase 2
| HGNCid = 9437
| Symbol = EIF2AK2
| AltSymbols =; EIF2AK1; MGC126524; PKR; PRKR
| OMIM = 176871
| ECnumber =
| Homologene = 48134
| MGIid = 1353449
| GeneAtlas_image1 = PBB_GE_EIF2AK2_204211_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_EIF2AK2_213294_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003725 |text = double-stranded RNA binding}} {{GNF_GO|id=GO:0004672 |text = protein kinase activity}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004694 |text = eukaryotic translation initiation factor 2alpha kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008601 |text = protein phosphatase type 2A regulator activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}}
| Process = {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006412 |text = translation}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006926 |text = virus-infected cell apoptosis}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0009615 |text = response to virus}} {{GNF_GO|id=GO:0030968 |text = unfolded protein response}} {{GNF_GO|id=GO:0046777 |text = protein amino acid autophosphorylation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5610
| Hs_Ensembl = ENSG00000055332
| Hs_RefseqProtein = NP_002750
| Hs_RefseqmRNA = NM_002759
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 37179857
| Hs_GenLoc_end = 37405184
| Hs_Uniprot = P19525
| Mm_EntrezGene = 19106
| Mm_Ensembl = ENSMUSG00000024079
| Mm_RefseqmRNA = NM_011163
| Mm_RefseqProtein = NP_035293
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 78757622
| Mm_GenLoc_end = 78787630
| Mm_Uniprot = Q78E06
}}
}}
'''Eukaryotic translation initiation factor 2-alpha kinase 2''', also known as '''EIF2AK2''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Williams BR |title=PKR; a sentinel kinase for cellular stress. |journal=Oncogene |volume=18 |issue= 45 |pages= 6112-20 |year= 1999 |pmid= 10557102 |doi= 10.1038/sj.onc.1203127 }}
*{{cite journal | author=García MA, Meurs EF, Esteban M |title=The dsRNA protein kinase PKR: virus and cell control. |journal=Biochimie |volume=89 |issue= 6-7 |pages= 799-811 |year= 2007 |pmid= 17451862 |doi= 10.1016/j.biochi.2007.03.001 }}
*{{cite journal | author=Feng GS, Chong K, Kumar A, Williams BR |title=Identification of double-stranded RNA-binding domains in the interferon-induced double-stranded RNA-activated p68 kinase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 12 |pages= 5447-51 |year= 1992 |pmid= 1351683 |doi= }}
*{{cite journal | author=Thomis DC, Doohan JP, Samuel CE |title=Mechanism of interferon action: cDNA structure, expression, and regulation of the interferon-induced, RNA-dependent P1/eIF-2 alpha protein kinase from human cells. |journal=Virology |volume=188 |issue= 1 |pages= 33-46 |year= 1992 |pmid= 1373553 |doi= }}
*{{cite journal | author=McCormack SJ, Thomis DC, Samuel CE |title=Mechanism of interferon action: identification of a RNA binding domain within the N-terminal region of the human RNA-dependent P1/eIF-2 alpha protein kinase. |journal=Virology |volume=188 |issue= 1 |pages= 47-56 |year= 1992 |pmid= 1373554 |doi= }}
*{{cite journal | author=Mellor H, Proud CG |title=A synthetic peptide substrate for initiation factor-2 kinases. |journal=Biochem. Biophys. Res. Commun. |volume=178 |issue= 2 |pages= 430-7 |year= 1991 |pmid= 1677563 |doi= }}
*{{cite journal | author=Meurs E, Chong K, Galabru J, ''et al.'' |title=Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon. |journal=Cell |volume=62 |issue= 2 |pages= 379-90 |year= 1990 |pmid= 1695551 |doi= }}
*{{cite journal | author=Silverman RH, Sengupta DN |title=Translational regulation by HIV leader RNA, TAT, and interferon-inducible enzymes. |journal=J. Exp. Pathol. |volume=5 |issue= 2 |pages= 69-77 |year= 1991 |pmid= 1708818 |doi= }}
*{{cite journal | author=Roy S, Katze MG, Parkin NT, ''et al.'' |title=Control of the interferon-induced 68-kilodalton protein kinase by the HIV-1 tat gene product. |journal=Science |volume=247 |issue= 4947 |pages= 1216-9 |year= 1990 |pmid= 2180064 |doi= }}
*{{cite journal | author=McMillan NA, Chun RF, Siderovski DP, ''et al.'' |title=HIV-1 Tat directly interacts with the interferon-induced, double-stranded RNA-dependent kinase, PKR. |journal=Virology |volume=213 |issue= 2 |pages= 413-24 |year= 1996 |pmid= 7491766 |doi= 10.1006/viro.1995.0014 }}
*{{cite journal | author=Cosentino GP, Venkatesan S, Serluca FC, ''et al.'' |title=Double-stranded-RNA-dependent protein kinase and TAR RNA-binding protein form homo- and heterodimers in vivo. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 21 |pages= 9445-9 |year= 1995 |pmid= 7568151 |doi= }}
*{{cite journal | author=Barber GN, Edelhoff S, Katze MG, Disteche CM |title=Chromosomal assignment of the interferon-inducible double-stranded RNA-dependent protein kinase (PRKR) to human chromosome 2p21-p22 and mouse chromosome 17 E2. |journal=Genomics |volume=16 |issue= 3 |pages= 765-7 |year= 1993 |pmid= 7686883 |doi= 10.1006/geno.1993.1262 }}
*{{cite journal | author=Squire J, Meurs EF, Chong KL, ''et al.'' |title=Localization of the human interferon-induced, ds-RNA activated p68 kinase gene (PRKR) to chromosome 2p21-p22. |journal=Genomics |volume=16 |issue= 3 |pages= 768-70 |year= 1993 |pmid= 7686884 |doi= 10.1006/geno.1993.1263 }}
*{{cite journal | author=Prigmore E, Ahmed S, Best A, ''et al.'' |title=A 68-kDa kinase and NADPH oxidase component p67phox are targets for Cdc42Hs and Rac1 in neutrophils. |journal=J. Biol. Chem. |volume=270 |issue= 18 |pages= 10717-22 |year= 1995 |pmid= 7738010 |doi= }}
*{{cite journal | author=Barber GN, Wambach M, Wong ML, ''et al.'' |title=Translational regulation by the interferon-induced double-stranded-RNA-activated 68-kDa protein kinase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 10 |pages= 4621-5 |year= 1993 |pmid= 8099444 |doi= }}
*{{cite journal | author=Polyak SJ, Tang N, Wambach M, ''et al.'' |title=The P58 cellular inhibitor complexes with the interferon-induced, double-stranded RNA-dependent protein kinase, PKR, to regulate its autophosphorylation and activity. |journal=J. Biol. Chem. |volume=271 |issue= 3 |pages= 1702-7 |year= 1996 |pmid= 8576172 |doi= }}
*{{cite journal | author=Chen ZJ, Parent L, Maniatis T |title=Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity. |journal=Cell |volume=84 |issue= 6 |pages= 853-62 |year= 1996 |pmid= 8601309 |doi= }}
*{{cite journal | author=Kuhen KL, Shen X, Carlisle ER, ''et al.'' |title=Structural organization of the human gene (PKR) encoding an interferon-inducible RNA-dependent protein kinase (PKR) and differences from its mouse homolog. |journal=Genomics |volume=36 |issue= 1 |pages= 197-201 |year= 1997 |pmid= 8812437 |doi= 10.1006/geno.1996.0446 }}
*{{cite journal | author=Taylor DR, Lee SB, Romano PR, ''et al.'' |title=Autophosphorylation sites participate in the activation of the double-stranded-RNA-activated protein kinase PKR. |journal=Mol. Cell. Biol. |volume=16 |issue= 11 |pages= 6295-302 |year= 1996 |pmid= 8887659 |doi= }}
*{{cite journal | author=Kuhen KL, Shen X, Samuel CE |title=Mechanism of interferon action sequence of the human interferon-inducible RNA-dependent protein kinase (PKR) deduced from genomic clones. |journal=Gene |volume=178 |issue= 1-2 |pages= 191-3 |year= 1996 |pmid= 8921913 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on F2R... {November 12, 2007 5:49:31 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 5:50:25 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Coagulation factor II (thrombin) receptor
| HGNCid = 3537
| Symbol = F2R
| AltSymbols =; CF2R; HTR; PAR1; TR
| OMIM = 187930
| ECnumber =
| Homologene = 1510
| MGIid = 101802
| GeneAtlas_image1 = PBB_GE_F2R_203989_x_at_tn.png
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0015057 |text = thrombin receptor activity}}
| Component = {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006919 |text = caspase activation}} {{GNF_GO|id=GO:0006928 |text = cell motility}} {{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:0007260 |text = tyrosine phosphorylation of STAT protein}} {{GNF_GO|id=GO:0007262 |text = STAT protein nuclear translocation}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}} {{GNF_GO|id=GO:0009611 |text = response to wounding}} {{GNF_GO|id=GO:0009653 |text = anatomical structure morphogenesis}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2149
| Hs_Ensembl = ENSG00000181104
| Hs_RefseqProtein = NP_001983
| Hs_RefseqmRNA = NM_001992
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 76047542
| Hs_GenLoc_end = 76067054
| Hs_Uniprot = P25116
| Mm_EntrezGene = 14062
| Mm_Ensembl = ENSMUSG00000048376
| Mm_RefseqmRNA = NM_010169
| Mm_RefseqProtein = NP_034299
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 96702488
| Mm_GenLoc_end = 96719173
| Mm_Uniprot = Q3UK34
}}
}}
'''Coagulation factor II (thrombin) receptor''', also known as '''F2R''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Coagulation factor II receptor is a 7-transmembrane receptor involved in the regulation of thrombotic response. Proteolytic cleavage leads to the activation of the receptor. F2R is a G-protein coupled receptor family member.<ref>{{cite web | title = Entrez Gene: F2R coagulation factor II (thrombin) receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2149| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Coughlin SR, Vu TK, Hung DT, Wheaton VI |title=Characterization of a functional thrombin receptor. Issues and opportunities. |journal=J. Clin. Invest. |volume=89 |issue= 2 |pages= 351-5 |year= 1992 |pmid= 1310691 |doi= }}
*{{cite journal | author=Howell DC, Laurent GJ, Chambers RC |title=Role of thrombin and its major cellular receptor, protease-activated receptor-1, in pulmonary fibrosis. |journal=Biochem. Soc. Trans. |volume=30 |issue= 2 |pages= 211-6 |year= 2002 |pmid= 12023853 |doi= 10.1042/ }}
*{{cite journal | author=Tellez C, Bar-Eli M |title=Role and regulation of the thrombin receptor (PAR-1) in human melanoma. |journal=Oncogene |volume=22 |issue= 20 |pages= 3130-7 |year= 2003 |pmid= 12789289 |doi= 10.1038/sj.onc.1206453 }}
*{{cite journal | author=Remillard CV, Yuan JX |title=PGE2 and PAR-1 in pulmonary fibrosis: a case of biting the hand that feeds you? |journal=Am. J. Physiol. Lung Cell Mol. Physiol. |volume=288 |issue= 5 |pages= L789-92 |year= 2005 |pmid= 15821019 |doi= 10.1152/ajplung.00016.2005 }}
*{{cite journal | author=Leger AJ, Covic L, Kuliopulos A |title=Protease-activated receptors in cardiovascular diseases. |journal=Circulation |volume=114 |issue= 10 |pages= 1070-7 |year= 2006 |pmid= 16952995 |doi= 10.1161/CIRCULATIONAHA.105.574830 }}
*{{cite journal | author=Traynelis SF, Trejo J |title=Protease-activated receptor signaling: new roles and regulatory mechanisms. |journal=Curr. Opin. Hematol. |volume=14 |issue= 3 |pages= 230-5 |year= 2007 |pmid= 17414212 |doi= 10.1097/MOH.0b013e3280dce568 }}
*{{cite journal | author=Vu TK, Hung DT, Wheaton VI, Coughlin SR |title=Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. |journal=Cell |volume=64 |issue= 6 |pages= 1057-68 |year= 1991 |pmid= 1672265 |doi= }}
*{{cite journal | author=Wojtukiewicz MZ, Tang DG, Ben-Josef E, ''et al.'' |title=Solid tumor cells express functional "tethered ligand" thrombin receptor. |journal=Cancer Res. |volume=55 |issue= 3 |pages= 698-704 |year= 1995 |pmid= 7834643 |doi= }}
*{{cite journal | author=Hein L, Ishii K, Coughlin SR, Kobilka BK |title=Intracellular targeting and trafficking of thrombin receptors. A novel mechanism for resensitization of a G protein-coupled receptor. |journal=J. Biol. Chem. |volume=269 |issue= 44 |pages= 27719-26 |year= 1994 |pmid= 7961693 |doi= }}
*{{cite journal | author=Mathews II, Padmanabhan KP, Ganesh V, ''et al.'' |title=Crystallographic structures of thrombin complexed with thrombin receptor peptides: existence of expected and novel binding modes. |journal=Biochemistry |volume=33 |issue= 11 |pages= 3266-79 |year= 1994 |pmid= 8136362 |doi= }}
*{{cite journal | author=Offermanns S, Laugwitz KL, Spicher K, Schultz G |title=G proteins of the G12 family are activated via thromboxane A2 and thrombin receptors in human platelets. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 2 |pages= 504-8 |year= 1994 |pmid= 8290554 |doi= }}
*{{cite journal | author=Hoffman M, Church FC |title=Response of blood leukocytes to thrombin receptor peptides. |journal=J. Leukoc. Biol. |volume=54 |issue= 2 |pages= 145-51 |year= 1993 |pmid= 8395550 |doi= }}
*{{cite journal | author=Bahou WF, Nierman WC, Durkin AS, ''et al.'' |title=Chromosomal assignment of the human thrombin receptor gene: localization to region q13 of chromosome 5. |journal=Blood |volume=82 |issue= 5 |pages= 1532-7 |year= 1993 |pmid= 8395910 |doi= }}
*{{cite journal | author=Schmidt VA, Vitale E, Bahou WF |title=Genomic cloning and characterization of the human thrombin receptor gene. Structural similarity to the proteinase activated receptor-2 gene. |journal=J. Biol. Chem. |volume=271 |issue= 16 |pages= 9307-12 |year= 1996 |pmid= 8621593 |doi= }}
*{{cite journal | author=Li F, Baykal D, Horaist C, ''et al.'' |title=Cloning and identification of regulatory sequences of the human thrombin receptor gene. |journal=J. Biol. Chem. |volume=271 |issue= 42 |pages= 26320-8 |year= 1996 |pmid= 8824285 |doi= }}
*{{cite journal | author=Shapiro MJ, Trejo J, Zeng D, Coughlin SR |title=Role of the thrombin receptor's cytoplasmic tail in intracellular trafficking. Distinct determinants for agonist-triggered versus tonic internalization and intracellular localization. |journal=J. Biol. Chem. |volume=271 |issue= 51 |pages= 32874-80 |year= 1997 |pmid= 8955127 |doi= }}
*{{cite journal | author=Ogino Y, Tanaka K, Shimizu N |title=Direct evidence for two distinct G proteins coupling with thrombin receptors in human neuroblastoma SH-EP cells. |journal=Eur. J. Pharmacol. |volume=316 |issue= 1 |pages= 105-9 |year= 1997 |pmid= 8982657 |doi= }}
*{{cite journal | author=Molino M, Bainton DF, Hoxie JA, ''et al.'' |title=Thrombin receptors on human platelets. Initial localization and subsequent redistribution during platelet activation. |journal=J. Biol. Chem. |volume=272 |issue= 9 |pages= 6011-7 |year= 1997 |pmid= 9038223 |doi= }}
*{{cite journal | author=Renesto P, Si-Tahar M, Moniatte M, ''et al.'' |title=Specific inhibition of thrombin-induced cell activation by the neutrophil proteinases elastase, cathepsin G, and proteinase 3: evidence for distinct cleavage sites within the aminoterminal domain of the thrombin receptor. |journal=Blood |volume=89 |issue= 6 |pages= 1944-53 |year= 1997 |pmid= 9058715 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FGA... {November 12, 2007 5:50:25 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 5:51:06 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_FGA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1fza.
| PDB = {{PDB2|1fza}}, {{PDB2|1fzb}}, {{PDB2|1fzc}}, {{PDB2|1fzd}}, {{PDB2|1fze}}, {{PDB2|1fzf}}, {{PDB2|1fzg}}, {{PDB2|1lt9}}, {{PDB2|1ltj}}, {{PDB2|1n86}}, {{PDB2|1n8e}}, {{PDB2|1re3}}, {{PDB2|1re4}}, {{PDB2|1rf0}}, {{PDB2|1rf1}}, {{PDB2|2a45}}, {{PDB2|2ffd}}, {{PDB2|2h43}}, {{PDB2|2hod}}, {{PDB2|2hpc}}, {{PDB2|2oyh}}, {{PDB2|2oyi}}
| Name = Fibrinogen alpha chain
| HGNCid = 3661
| Symbol = FGA
| AltSymbols =; Fib2; MGC119422; MGC119423; MGC119425
| OMIM = 134820
| ECnumber =
| Homologene = 428
| MGIid = 1316726
| GeneAtlas_image1 = PBB_GE_FGA_205650_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_FGA_205649_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0030674 |text = protein binding, bridging}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005577 |text = fibrinogen complex}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0008217 |text = blood pressure regulation}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0030168 |text = platelet activation}} {{GNF_GO|id=GO:0051258 |text = protein polymerization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2243
| Hs_Ensembl = ENSG00000171560
| Hs_RefseqProtein = NP_000499
| Hs_RefseqmRNA = NM_000508
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 155723730
| Hs_GenLoc_end = 155731347
| Hs_Uniprot = P02671
| Mm_EntrezGene = 14161
| Mm_Ensembl = ENSMUSG00000028001
| Mm_RefseqmRNA = NM_010196
| Mm_RefseqProtein = NP_034326
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 83112081
| Mm_GenLoc_end = 83118197
| Mm_Uniprot =
}}
}}
'''Fibrinogen alpha chain''', also known as '''FGA''', is a human [[gene]].
<!-- 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 the alpha component of fibrinogen, a blood-borne glycoprotein comprised of three pairs of nonidentical polypeptide chains. Following vascular injury, fibrinogen is cleaved by thrombin to form fibrin which is the most abundant component of blood clots. In addition, various cleavage products of fibrinogen and fibrin regulate cell adhesion and spreading, display vasoconstrictor and chemotactic activities, and are mitogens for several cell types. Mutations in this gene lead to several disorders, including dysfibrinogenemia, hypofibrinogenemia, afibrinogenemia and renal amyloidosis. Alternative splicing results in two isoforms which vary in the carboxy-terminus.<ref>{{cite web | title = Entrez Gene: FGA fibrinogen alpha chain| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2243| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Doolittle RF |title=Fibrinogen and fibrin. |journal=Annu. Rev. Biochem. |volume=53 |issue= |pages= 195-229 |year= 1984 |pmid= 6383194 |doi= 10.1146/annurev.bi.53.070184.001211 }}
*{{cite journal | author=Galanakis DK |title=Inherited dysfibrinogenemia: emerging abnormal structure associations with pathologic and nonpathologic dysfunctions. |journal=Semin. Thromb. Hemost. |volume=19 |issue= 4 |pages= 386-95 |year= 1994 |pmid= 8140431 |doi= }}
*{{cite journal | author=Herrick S, Blanc-Brude O, Gray A, Laurent G |title=Fibrinogen. |journal=Int. J. Biochem. Cell Biol. |volume=31 |issue= 7 |pages= 741-6 |year= 1999 |pmid= 10467729 |doi= }}
*{{cite journal | author=Bennett JS |title=Platelet-fibrinogen interactions. |journal=Ann. N. Y. Acad. Sci. |volume=936 |issue= |pages= 340-54 |year= 2001 |pmid= 11460491 |doi= }}
*{{cite journal | author=Redman CM, Xia H |title=Fibrinogen biosynthesis. Assembly, intracellular degradation, and association with lipid synthesis and secretion. |journal=Ann. N. Y. Acad. Sci. |volume=936 |issue= |pages= 480-95 |year= 2001 |pmid= 11460506 |doi= }}
*{{cite journal | author=Matsuda M, Sugo T |title=Structure and function of human fibrinogen inferred from dysfibrinogens. |journal=Int. J. Hematol. |volume=76 Suppl 1 |issue= |pages= 352-60 |year= 2003 |pmid= 12430881 |doi= }}
*{{cite journal | author=Everse SJ |title=New insights into fibrin (ogen) structure and function. |journal=Vox Sang. |volume=83 Suppl 1 |issue= |pages= 375-82 |year= 2003 |pmid= 12617173 |doi= }}
*{{cite journal | author=Scott EM, Ariëns RA, Grant PJ |title=Genetic and environmental determinants of fibrin structure and function: relevance to clinical disease. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=24 |issue= 9 |pages= 1558-66 |year= 2005 |pmid= 15217804 |doi= 10.1161/01.ATV.0000136649.83297.bf }}
*{{cite journal | author=Lord ST |title=Fibrinogen and fibrin: scaffold proteins in hemostasis. |journal=Curr. Opin. Hematol. |volume=14 |issue= 3 |pages= 236-41 |year= 2007 |pmid= 17414213 |doi= 10.1097/MOH.0b013e3280dce58c }}
*{{cite journal | author=Cottrell BA, Strong DD, Watt KW, Doolittle RF |title=Amino acid sequence studies on the alpha chain of human fibrinogen. Exact location of cross-linking acceptor sites. |journal=Biochemistry |volume=18 |issue= 24 |pages= 5405-10 |year= 1980 |pmid= 518845 |doi= }}
*{{cite journal | author=Watt KW, Cottrell BA, Strong DD, Doolittle RF |title=Amino acid sequence studies on the alpha chain of human fibrinogen. Overlapping sequences providing the complete sequence. |journal=Biochemistry |volume=18 |issue= 24 |pages= 5410-6 |year= 1980 |pmid= 518846 |doi= }}
*{{cite journal | author=Fretto LJ, Ferguson EW, Steinman HM, McKee PA |title=Localization of the alpha-chain cross-link acceptor sites of human fibrin. |journal=J. Biol. Chem. |volume=253 |issue= 7 |pages= 2184-95 |year= 1978 |pmid= 632262 |doi= }}
*{{cite journal | author=Blombäck B, Hessel B, Hogg D |title=Disulfide bridges in nh2 -terminal part of human fibrinogen. |journal=Thromb. Res. |volume=8 |issue= 5 |pages= 639-58 |year= 1976 |pmid= 936108 |doi= }}
*{{cite journal | author=Koopman J, Haverkate F, Grimbergen J, ''et al.'' |title=Fibrinogen Marburg: a homozygous case of dysfibrinogenemia, lacking amino acids A alpha 461-610 (Lys 461 AAA-->stop TAA). |journal=Blood |volume=80 |issue= 8 |pages= 1972-9 |year= 1992 |pmid= 1391954 |doi= }}
*{{cite journal | author=Fu Y, Weissbach L, Plant PW, ''et al.'' |title=Carboxy-terminal-extended variant of the human fibrinogen alpha subunit: a novel exon conferring marked homology to beta and gamma subunits. |journal=Biochemistry |volume=31 |issue= 48 |pages= 11968-72 |year= 1993 |pmid= 1457396 |doi= }}
*{{cite journal | author=Martin PD, Robertson W, Turk D, ''et al.'' |title=The structure of residues 7-16 of the A alpha-chain of human fibrinogen bound to bovine thrombin at 2.3-A resolution. |journal=J. Biol. Chem. |volume=267 |issue= 11 |pages= 7911-20 |year= 1992 |pmid= 1560020 |doi= }}
*{{cite journal | author=Stubbs MT, Oschkinat H, Mayr I, ''et al.'' |title=The interaction of thrombin with fibrinogen. A structural basis for its specificity. |journal=Eur. J. Biochem. |volume=206 |issue= 1 |pages= 187-95 |year= 1992 |pmid= 1587268 |doi= }}
*{{cite journal | author=Maekawa H, Yamazumi K, Muramatsu S, ''et al.'' |title=Fibrinogen Lima: a homozygous dysfibrinogen with an A alpha-arginine-141 to serine substitution associated with extra N-glycosylation at A alpha-asparagine-139. Impaired fibrin gel formation but normal fibrin-facilitated plasminogen activation catalyzed by tissue-type plasminogen activator. |journal=J. Clin. Invest. |volume=90 |issue= 1 |pages= 67-76 |year= 1992 |pmid= 1634621 |doi= }}
*{{cite journal | author=Maekawa H, Yamazumi K, Muramatsu S, ''et al.'' |title=An A alpha Ser-434 to N-glycosylated Asn substitution in a dysfibrinogen, fibrinogen Caracas II, characterized by impaired fibrin gel formation. |journal=J. Biol. Chem. |volume=266 |issue= 18 |pages= 11575-81 |year= 1991 |pmid= 1675636 |doi= }}
*{{cite journal | author=Wu C, Chung AE |title=Potential role of entactin in hemostasis. Specific interaction of entactin with fibrinogen A alpha and B beta chains. |journal=J. Biol. Chem. |volume=266 |issue= 28 |pages= 18802-7 |year= 1991 |pmid= 1680863 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GP1BA... {November 12, 2007 5:51:06 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 5:51:47 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_GP1BA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1gwb.
| PDB = {{PDB2|1gwb}}, {{PDB2|1m0z}}, {{PDB2|1m10}}, {{PDB2|1ook}}, {{PDB2|1p8v}}, {{PDB2|1p9a}}, {{PDB2|1qyy}}, {{PDB2|1sq0}}, {{PDB2|1u0n}}
| Name = Glycoprotein Ib (platelet), alpha polypeptide
| HGNCid = 4439
| Symbol = GP1BA
| AltSymbols =; BSS; CD42B; CD42b-alpha; GP1B; MGC34595
| OMIM = 606672
| ECnumber =
| Homologene = 143
| MGIid = 1333744
| GeneAtlas_image1 = PBB_GE_GP1BA_207389_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0015057 |text = thrombin receptor activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0000902 |text = cell morphogenesis}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0030168 |text = platelet activation}} {{GNF_GO|id=GO:0030193 |text = regulation of blood coagulation}} {{GNF_GO|id=GO:0042730 |text = fibrinolysis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2811
| Hs_Ensembl = ENSG00000185245
| Hs_RefseqProtein = NP_000164
| Hs_RefseqmRNA = NM_000173
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 4776680
| Hs_GenLoc_end = 4778599
| Hs_Uniprot = P07359
| Mm_EntrezGene = 14723
| Mm_Ensembl = ENSMUSG00000050675
| Mm_RefseqmRNA = NM_010326
| Mm_RefseqProtein = NP_034456
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 70455317
| Mm_GenLoc_end = 70458253
| Mm_Uniprot = O35930
}}
}}
'''Glycoprotein Ib (platelet), alpha polypeptide''', also known as '''GP1BA''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Glycoprotein Ib (GP Ib) is a platelet surface membrane glycoprotein composed of a heterodimer, an alpha chain and a beta chain, that are linked by disulfide bonds. The Gp Ib functions as a receptor for von Willebrand factor (VWF). The complete receptor complex includes noncovalent association of the alpha and beta subunits with platelet glycoprotein IX and platelet glycoprotein V. The binding of the GP Ib-IX-V complex to VWF facilitates initial platelet adhesion to vascular subendothelium after vascular injury, and also initiates signaling events within the platelet that lead to enhanced platelet activation, thrombosis, and hemostasis. This gene encodes the alpha subunit. Several polymorphisms and mutations have been described in this gene, some of which are the cause of Bernard-Soulier syndromes and platelet-type von Willebrand disease.<ref>{{cite web | title = Entrez Gene: GP1BA glycoprotein Ib (platelet), alpha polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2811| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kunishima S, Kamiya T, Saito H |title=Genetic abnormalities of Bernard-Soulier syndrome. |journal=Int. J. Hematol. |volume=76 |issue= 4 |pages= 319-27 |year= 2003 |pmid= 12463594 |doi= }}
*{{cite journal | author=Du X |title=Signaling and regulation of the platelet glycoprotein Ib-IX-V complex. |journal=Curr. Opin. Hematol. |volume=14 |issue= 3 |pages= 262-9 |year= 2007 |pmid= 17414217 |doi= 10.1097/MOH.0b013e3280dce51a }}
*{{cite journal | author=Clemetson KJ |title=A short history of platelet glycoprotein Ib complex. |journal=Thromb. Haemost. |volume=98 |issue= 1 |pages= 63-8 |year= 2007 |pmid= 17597992 |doi= }}
*{{cite journal | author=López JA, Ludwig EH, McCarthy BJ |title=Polymorphism of human glycoprotein Ib alpha results from a variable number of tandem repeats of a 13-amino acid sequence in the mucin-like macroglycopeptide region. Structure/function implications. |journal=J. Biol. Chem. |volume=267 |issue= 14 |pages= 10055-61 |year= 1992 |pmid= 1577776 |doi= }}
*{{cite journal | author=Murata M, Furihata K, Ishida F, ''et al.'' |title=Genetic and structural characterization of an amino acid dimorphism in glycoprotein Ib alpha involved in platelet transfusion refractoriness. |journal=Blood |volume=79 |issue= 11 |pages= 3086-90 |year= 1992 |pmid= 1586750 |doi= }}
*{{cite journal | author=Girma JP, Takahashi Y, Yoshioka A, ''et al.'' |title=Ristocetin and botrocetin involve two distinct domains of von Willebrand factor for binding to platelet membrane glycoprotein Ib. |journal=Thromb. Haemost. |volume=64 |issue= 2 |pages= 326-32 |year= 1991 |pmid= 1702906 |doi= }}
*{{cite journal | author=Miller JL, Lyle VA, Cunningham D |title=Mutation of leucine-57 to phenylalanine in a platelet glycoprotein Ib alpha leucine tandem repeat occurring in patients with an autosomal dominant variant of Bernard-Soulier disease. |journal=Blood |volume=79 |issue= 2 |pages= 439-46 |year= 1992 |pmid= 1730088 |doi= }}
*{{cite journal | author=Modderman PW, Admiraal LG, Sonnenberg A, von dem Borne AE |title=Glycoproteins V and Ib-IX form a noncovalent complex in the platelet membrane. |journal=J. Biol. Chem. |volume=267 |issue= 1 |pages= 364-9 |year= 1992 |pmid= 1730602 |doi= }}
*{{cite journal | author=Miller JL, Cunningham D, Lyle VA, Finch CN |title=Mutation in the gene encoding the alpha chain of platelet glycoprotein Ib in platelet-type von Willebrand disease. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 11 |pages= 4761-5 |year= 1991 |pmid= 2052556 |doi= }}
*{{cite journal | author=Hess D, Schaller J, Rickli EE, Clemetson KJ |title=Identification of the disulphide bonds in human platelet glycocalicin. |journal=Eur. J. Biochem. |volume=199 |issue= 2 |pages= 389-93 |year= 1991 |pmid= 2070794 |doi= }}
*{{cite journal | author=Du X, Beutler L, Ruan C, ''et al.'' |title=Glycoprotein Ib and glycoprotein IX are fully complexed in the intact platelet membrane. |journal=Blood |volume=69 |issue= 5 |pages= 1524-7 |year= 1987 |pmid= 2436691 |doi= }}
*{{cite journal | author=Andrews RK, Booth WJ, Gorman JJ, ''et al.'' |title=Purification of botrocetin from Bothrops jararaca venom. Analysis of the botrocetin-mediated interaction between von Willebrand factor and the human platelet membrane glycoprotein Ib-IX complex. |journal=Biochemistry |volume=28 |issue= 21 |pages= 8317-26 |year= 1990 |pmid= 2557900 |doi= }}
*{{cite journal | author=Wenger RH, Wicki AN, Kieffer N, ''et al.'' |title=The 5' flanking region and chromosomal localization of the gene encoding human platelet membrane glycoprotein Ib alpha. |journal=Gene |volume=85 |issue= 2 |pages= 517-24 |year= 1990 |pmid= 2628181 |doi= }}
*{{cite journal | author=Wenger RH, Kieffer N, Wicki AN, Clemetson KJ |title=Structure of the human blood platelet membrane glycoprotein Ib alpha gene. |journal=Biochem. Biophys. Res. Commun. |volume=156 |issue= 1 |pages= 389-95 |year= 1988 |pmid= 2845978 |doi= }}
*{{cite journal | author=Wicki AN, Clemetson KJ |title=Structure and function of platelet membrane glycoproteins Ib and V. Effects of leukocyte elastase and other proteases on platelets response to von Willebrand factor and thrombin. |journal=Eur. J. Biochem. |volume=153 |issue= 1 |pages= 1-11 |year= 1985 |pmid= 2933256 |doi= }}
*{{cite journal | author=Adelman B, Michelson AD, Greenberg J, Handin RI |title=Proteolysis of platelet glycoprotein Ib by plasmin is facilitated by plasmin lysine-binding regions. |journal=Blood |volume=68 |issue= 6 |pages= 1280-4 |year= 1987 |pmid= 2946332 |doi= }}
*{{cite journal | author=Lopez JA, Chung DW, Fujikawa K, ''et al.'' |title=Cloning of the alpha chain of human platelet glycoprotein Ib: a transmembrane protein with homology to leucine-rich alpha 2-glycoprotein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 16 |pages= 5615-9 |year= 1987 |pmid= 3303030 |doi= }}
*{{cite journal | author=Lopez JA, Chung DW, Fujikawa K, ''et al.'' |title=The alpha and beta chains of human platelet glycoprotein Ib are both transmembrane proteins containing a leucine-rich amino acid sequence. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 7 |pages= 2135-9 |year= 1988 |pmid= 3353370 |doi= }}
*{{cite journal | author=Titani K, Takio K, Handa M, Ruggeri ZM |title=Amino acid sequence of the von Willebrand factor-binding domain of platelet membrane glycoprotein Ib. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 16 |pages= 5610-4 |year= 1987 |pmid= 3497398 |doi= }}
*{{cite journal | author=Harmon JT, Jamieson GA |title=The glycocalicin portion of platelet glycoprotein Ib expresses both high and moderate affinity receptor sites for thrombin. A soluble radioreceptor assay for the interaction of thrombin with platelets. |journal=J. Biol. Chem. |volume=261 |issue= 28 |pages= 13224-9 |year= 1986 |pmid= 3759960 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HBG1... {November 12, 2007 5:51:47 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 5:52:27 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_HBG1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1fdh.
| PDB = {{PDB2|1fdh}}, {{PDB2|1i3d}}, {{PDB2|1i3e}}
| Name = Hemoglobin, gamma A
| HGNCid = 4831
| Symbol = HBG1
| AltSymbols =; HBGA; HBGR; HSGGL1; PRO2979
| OMIM = 142200
| ECnumber =
| Homologene = 73883
| MGIid = 96024
| Function = {{GNF_GO|id=GO:0005344 |text = oxygen transporter activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0019825 |text = oxygen binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005833 |text = hemoglobin complex}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0015671 |text = oxygen transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3047
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000550
| Hs_RefseqmRNA = NM_000559
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 15132
| Mm_Ensembl = ENSMUSG00000052217
| Mm_RefseqmRNA = XM_993220
| Mm_RefseqProtein = XP_998314
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 103715459
| Mm_GenLoc_end = 103716983
| Mm_Uniprot = Q3TUN7
}}
}}
'''Hemoglobin, gamma A''', also known as '''HBG1''', is a human [[gene]].
<!-- 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 gamma globin genes (HBG1 and HBG2) are normally expressed in the fetal liver, spleen and bone marrow. Two gamma chains together with two alpha chains constitute fetal hemoglobin (HbF) which is normally replaced by adult hemoglobin (HbA) at birth. In some beta-thalassemias and related conditions, gamma chain production continues into adulthood. The two types of gamma chains differ at residue 136 where glycine is found in the G-gamma product (HBG2) and alanine is found in the A-gamma product (HBG1). The former is predominant at birth. The order of the genes in the beta-globin cluster is: 5'-epsilon -- gamma-G -- gamma-A -- delta -- beta--3'.<ref>{{cite web | title = Entrez Gene: HBG1 hemoglobin, gamma A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3047| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Huisman TH, Kutlar F, Gu LH |title=Gamma chain abnormalities and gamma-globin gene rearrangements in newborn babies of various populations. |journal=Hemoglobin |volume=15 |issue= 5 |pages= 349-79 |year= 1992 |pmid= 1802881 |doi= }}
*{{cite journal | author=Gelinas R, Yagi M, Endlich B, ''et al.'' |title=Sequences of G gamma, A gamma, and beta genes of the Greek (A gamma) HPFH mutant: evidence for a distal CCAAT box mutation in the A gamma gene. |journal=Prog. Clin. Biol. Res. |volume=191 |issue= |pages= 125-39 |year= 1985 |pmid= 2413469 |doi= }}
*{{cite journal | author=Higgs DR, Vickers MA, Wilkie AO, ''et al.'' |title=A review of the molecular genetics of the human alpha-globin gene cluster. |journal=Blood |volume=73 |issue= 5 |pages= 1081-104 |year= 1989 |pmid= 2649166 |doi= }}
*{{cite journal | author=Giardina B, Messana I, Scatena R, Castagnola M |title=The multiple functions of hemoglobin. |journal=Crit. Rev. Biochem. Mol. Biol. |volume=30 |issue= 3 |pages= 165-96 |year= 1995 |pmid= 7555018 |doi= }}
*{{cite journal | author=Anderson NL, Anderson NG |title=The human plasma proteome: history, character, and diagnostic prospects. |journal=Mol. Cell Proteomics |volume=1 |issue= 11 |pages= 845-67 |year= 2003 |pmid= 12488461 |doi= }}
*{{cite journal | author=Chang JC, Kan YW |title=beta 0 thalassemia, a nonsense mutation in man. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=76 |issue= 6 |pages= 2886-9 |year= 1979 |pmid= 88735 |doi= }}
*{{cite journal | author=Saglio G, Ricco G, Mazza U, ''et al.'' |title=Human T gamma globin chain is a variant of A gamma chain (A gamma Sardinia). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=76 |issue= 7 |pages= 3420-4 |year= 1979 |pmid= 291015 |doi= }}
*{{cite journal | author=Poon R, Kan YW, Boyer HW |title=Sequence of the 3'-noncoding and adjacent coding regions of human gamma-globin mRNA. |journal=Nucleic Acids Res. |volume=5 |issue= 12 |pages= 4625-30 |year= 1979 |pmid= 318163 |doi= }}
*{{cite journal | author=Grifoni V, Kamuzora H, Lehmann H, Charlesworth D |title=A new Hb variant: Hb F Sardinia gamma75(E19) isoleucine leads to threonine found in a family with Hb G Philadelphia, beta-chain deficiency and a Lepore-like haemoglobin indistinguishable from Hb A2. |journal=Acta Haematol. |volume=53 |issue= 6 |pages= 347-55 |year= 1975 |pmid= 808940 |doi= }}
*{{cite journal | author=Proudfoot NJ, Brownlee GG |title=3' non-coding region sequences in eukaryotic messenger RNA. |journal=Nature |volume=263 |issue= 5574 |pages= 211-4 |year= 1976 |pmid= 822353 |doi= }}
*{{cite journal | author=Marotta CA, Forget BG, Cohne-Solal M, ''et al.'' |title=Human beta-globin messenger RNA. I. Nucleotide sequences derived from complementary RNA. |journal=J. Biol. Chem. |volume=252 |issue= 14 |pages= 5019-31 |year= 1977 |pmid= 873928 |doi= }}
*{{cite journal | author=Frier JA, Perutz MF |title=Structure of human foetal deoxyhaemoglobin. |journal=J. Mol. Biol. |volume=112 |issue= 1 |pages= 97-112 |year= 1977 |pmid= 881729 |doi= }}
*{{cite journal | author=Ahern E, Holder W, Ahern V, ''et al.'' |title=Haemoglobin F Victoria Jubilee (alpha 2 A gamma 2 80 Asp-Try). |journal=Biochim. Biophys. Acta |volume=393 |issue= 1 |pages= 188-94 |year= 1975 |pmid= 1138921 |doi= }}
*{{cite journal | author=Waye JS, Cai SP, Eng B, ''et al.'' |title=Clinical course and molecular characterization of a compound heterozygote for sickle hemoglobin and hemoglobin Kenya. |journal=Am. J. Hematol. |volume=41 |issue= 4 |pages= 289-91 |year= 1993 |pmid= 1283810 |doi= }}
*{{cite journal | author=Bailey WJ, Hayasaka K, Skinner CG, ''et al.'' |title=Reexamination of the African hominoid trichotomy with additional sequences from the primate beta-globin gene cluster. |journal=Mol. Phylogenet. Evol. |volume=1 |issue= 2 |pages= 97-135 |year= 1994 |pmid= 1342932 |doi= }}
*{{cite journal | author=Gottardi E, Losekoot M, Fodde R, ''et al.'' |title=Rapid identification by denaturing gradient gel electrophoresis of mutations in the gamma-globin gene promoters in non-deletion type HPFH. |journal=Br. J. Haematol. |volume=80 |issue= 4 |pages= 533-8 |year= 1992 |pmid= 1374633 |doi= }}
*{{cite journal | author=Berry M, Grosveld F, Dillon N |title=A single point mutation is the cause of the Greek form of hereditary persistence of fetal haemoglobin. |journal=Nature |volume=358 |issue= 6386 |pages= 499-502 |year= 1992 |pmid= 1379347 |doi= 10.1038/358499a0 }}
*{{cite journal | author=Loudianos G, Moi P, Lavinha J, ''et al.'' |title=Normal delta-globin gene sequences in Sardinian nondeletional delta beta-thalassemia. |journal=Hemoglobin |volume=16 |issue= 6 |pages= 503-9 |year= 1993 |pmid= 1487421 |doi= }}
*{{cite journal | author=Fucharoen S, Shimizu K, Fukumaki Y |title=A novel C-T transition within the distal CCAAT motif of the G gamma-globin gene in the Japanese HPFH: implication of factor binding in elevated fetal globin expression. |journal=Nucleic Acids Res. |volume=18 |issue= 17 |pages= 5245-53 |year= 1990 |pmid= 1698280 |doi= }}
*{{cite journal | author=Plaseska D, Kutlar F, Wilson JB, ''et al.'' |title=Hb F-Jiangsu, the first gamma chain variant with a valine----methionine substitution: alpha 2A gamma 2 134(H12)Val----Met. |journal=Hemoglobin |volume=14 |issue= 2 |pages= 177-83 |year= 1991 |pmid= 1703137 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HCK... {November 12, 2007 5:52:27 PM PST}
- SEARCH REDIRECT: Control Box Found: HCK {November 12, 2007 5:53:03 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 12, 2007 5:53:04 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 12, 2007 5:53:04 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 12, 2007 5:53:04 PM PST}
- UPDATED: Updated protein page: HCK {November 12, 2007 5:53:10 PM PST}
- INFO: Beginning work on HSPD1... {November 12, 2007 5:53:11 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 5:53:58 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Heat shock 60kDa protein 1 (chaperonin)
| HGNCid = 5261
| Symbol = HSPD1
| AltSymbols =; CPN60; GROEL; HSP60; HSP65; HuCHA60; SPG13
| OMIM = 118190
| ECnumber =
| Homologene = 86105
| MGIid = 96242
| GeneAtlas_image1 = PBB_GE_HSPD1_200807_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_HSPD1_200806_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0051082 |text = unfolded protein binding}} {{GNF_GO|id=GO:0051087 |text = chaperone binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}}
| Process = {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0006986 |text = response to unfolded protein}} {{GNF_GO|id=GO:0030150 |text = protein import into mitochondrial matrix}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}} {{GNF_GO|id=GO:0044267 |text = cellular protein metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3329
| Hs_Ensembl = ENSG00000144381
| Hs_RefseqProtein = NP_002147
| Hs_RefseqmRNA = NM_002156
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 198059555
| Hs_GenLoc_end = 198073243
| Hs_Uniprot = P10809
| Mm_EntrezGene = 15510
| Mm_Ensembl = ENSMUSG00000025980
| Mm_RefseqmRNA = NM_010477
| Mm_RefseqProtein = NP_034607
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 55022380
| Mm_GenLoc_end = 55032390
| Mm_Uniprot = Q3KQP2
}}
}}
'''Heat shock 60kDa protein 1 (chaperonin)''', also known as '''HSPD1''', is a human [[gene]].
<!-- 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 chaperonin family. The encoded mitochondrial protein may function as a signaling molecule in the innate immune system. This protein is essential for the folding and assembly of newly imported proteins in the mitochondria. This gene is adjacent to a related family member and the region between the 2 genes functions as a bidirectional promoter. Two pseudogenes, both located on chromosome 8, have been associated with this gene. Two transcript variants encoding the same protein have been identified for this gene. Mutations associated with this gene cause autosomal recessive spastic paraplegia 13.<ref>{{cite web | title = Entrez Gene: HSPD1 heat shock 60kDa protein 1 (chaperonin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3329| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tabibzadeh S, Broome J |title=Heat shock proteins in human endometrium throughout the menstrual cycle. |journal=Infectious diseases in obstetrics and gynecology |volume=7 |issue= 1-2 |pages= 5-9 |year= 1999 |pmid= 10231001 |doi= }}
*{{cite journal | author=Schäfer C, Williams JA |title=Stress kinases and heat shock proteins in the pancreas: possible roles in normal function and disease. |journal=J. Gastroenterol. |volume=35 |issue= 1 |pages= 1-9 |year= 2000 |pmid= 10632533 |doi= }}
*{{cite journal | author=Moseley P |title=Stress proteins and the immune response. |journal=Immunopharmacology |volume=48 |issue= 3 |pages= 299-302 |year= 2000 |pmid= 10960671 |doi= }}
*{{cite journal | author=Liu Y, Steinacker JM |title=Changes in skeletal muscle heat shock proteins: pathological significance. |journal=Front. Biosci. |volume=6 |issue= |pages= D12-25 |year= 2001 |pmid= 11145923 |doi= }}
*{{cite journal | author=Van Maele B, Debyser Z |title=HIV-1 integration: an interplay between HIV-1 integrase, cellular and viral proteins. |journal=AIDS reviews |volume=7 |issue= 1 |pages= 26-43 |year= 2005 |pmid= 15875659 |doi= }}
*{{cite journal | author=Hochstrasser DF, Frutiger S, Paquet N, ''et al.'' |title=Human liver protein map: a reference database established by microsequencing and gel comparison. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 992-1001 |year= 1993 |pmid= 1286669 |doi= }}
*{{cite journal | author=Ikawa S, Weinberg RA |title=An interaction between p21ras and heat shock protein hsp60, a chaperonin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 6 |pages= 2012-6 |year= 1992 |pmid= 1347942 |doi= }}
*{{cite journal | author=Brudzynski K, Martinez V, Gupta RS |title=Immunocytochemical localization of heat-shock protein 60-related protein in beta-cell secretory granules and its altered distribution in non-obese diabetic mice. |journal=Diabetologia |volume=35 |issue= 4 |pages= 316-24 |year= 1992 |pmid= 1516759 |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=Singh B, Patel HV, Ridley RG, ''et al.'' |title=Mitochondrial import of the human chaperonin (HSP60) protein. |journal=Biochem. Biophys. Res. Commun. |volume=169 |issue= 2 |pages= 391-6 |year= 1990 |pmid= 1972619 |doi= }}
*{{cite journal | author=Venner TJ, Singh B, Gupta RS |title=Nucleotide sequences and novel structural features of human and Chinese hamster hsp60 (chaperonin) gene families. |journal=DNA Cell Biol. |volume=9 |issue= 8 |pages= 545-52 |year= 1991 |pmid= 1980192 |doi= }}
*{{cite journal | author=Ward LD, Hong J, Whitehead RH, Simpson RJ |title=Development of a database of amino acid sequences for human colon carcinoma proteins separated by two-dimensional polyacrylamide gel electrophoresis. |journal=Electrophoresis |volume=11 |issue= 10 |pages= 883-91 |year= 1991 |pmid= 2079031 |doi= 10.1002/elps.1150111019 }}
*{{cite journal | author=Jindal S, Dudani AK, Singh B, ''et al.'' |title=Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonins and to the 65-kilodalton mycobacterial antigen. |journal=Mol. Cell. Biol. |volume=9 |issue= 5 |pages= 2279-83 |year= 1989 |pmid= 2568584 |doi= }}
*{{cite journal | author=Waldinger D, Eckerskorn C, Lottspeich F, Cleve H |title=Amino-acid sequence homology of a polymorphic cellular protein from human lymphocytes and the chaperonins from Escherichia coli (groEL) and chloroplasts (Rubisco-binding protein). |journal=Biol. Chem. Hoppe-Seyler |volume=369 |issue= 10 |pages= 1185-9 |year= 1989 |pmid= 2907406 |doi= }}
*{{cite journal | author=Kreisel W, Hildebrandt H, Schiltz E, ''et al.'' |title=Immuno-gold electron microscopical detection of heat shock protein 60 (hsp60) in mitochondria of rat hepatocytes and myocardiocytes. |journal=Acta Histochem. |volume=96 |issue= 1 |pages= 51-62 |year= 1994 |pmid= 7518175 |doi= }}
*{{cite journal | author=Corbett JM, Wheeler CH, Baker CS, ''et al.'' |title=The human myocardial two-dimensional gel protein database: update 1994. |journal=Electrophoresis |volume=15 |issue= 11 |pages= 1459-65 |year= 1995 |pmid= 7895732 |doi= }}
*{{cite journal | author=Baca-Estrada ME, Gupta RS, Stead RH, Croitoru K |title=Intestinal expression and cellular immune responses to human heat-shock protein 60 in Crohn's disease. |journal=Dig. Dis. Sci. |volume=39 |issue= 3 |pages= 498-506 |year= 1994 |pmid= 7907543 |doi= }}
*{{cite journal | author=Vélez-Granell CS, Arias AE, Torres-Ruíz JA, Bendayan M |title=Molecular chaperones in pancreatic tissue: the presence of cpn10, cpn60 and hsp70 in distinct compartments along the secretory pathway of the acinar cells. |journal=J. Cell. Sci. |volume=107 ( Pt 3) |issue= |pages= 539-49 |year= 1994 |pmid= 7911805 |doi= }}
*{{cite journal | author=Mayhew M, da Silva AC, Martin J, ''et al.'' |title=Protein folding in the central cavity of the GroEL-GroES chaperonin complex. |journal=Nature |volume=379 |issue= 6564 |pages= 420-6 |year= 1996 |pmid= 8559246 |doi= 10.1038/379420a0 }}
*{{cite journal | author=Tabibzadeh S, Kong QF, Satyaswaroop PG, Babaknia A |title=Heat shock proteins in human endometrium throughout the menstrual cycle. |journal=Hum. Reprod. |volume=11 |issue= 3 |pages= 633-40 |year= 1996 |pmid= 8671282 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LEPR... {November 12, 2007 5:53:58 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 5:54:36 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Leptin receptor
| HGNCid = 6554
| Symbol = LEPR
| AltSymbols =; CD295; OBR
| OMIM = 601007
| ECnumber =
| Homologene = 1731
| MGIid = 104993
| Function = {{GNF_GO|id=GO:0004896 |text = hematopoietin/interferon-class (D200-domain) cytokine receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006112 |text = energy reserve metabolic process}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3953
| Hs_Ensembl =
| Hs_RefseqProtein = NP_001003679
| Hs_RefseqmRNA = NM_001003679
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 16847
| Mm_Ensembl = ENSMUSG00000057722
| Mm_RefseqmRNA = NM_010704
| Mm_RefseqProtein = NP_034834
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 101215336
| Mm_GenLoc_end = 101313489
| Mm_Uniprot = P48356
}}
}}
'''Leptin receptor''', also known as '''LEPR''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Leptin (LEP; MIM 164160), an adipocyte-specific hormone that regulates adipose-tissue mass through hypothalamic effects on satiety and energy expenditure, acts through the leptin receptor (LEPR), a single-transmembrane-domain receptor of the cytokine receptor family.[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: LEPR leptin receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3953| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Heshka JT, Jones PJ |title=A role for dietary fat in leptin receptor, OB-Rb, function. |journal=Life Sci. |volume=69 |issue= 9 |pages= 987-1003 |year= 2001 |pmid= 11508653 |doi= }}
*{{cite journal | author=Tartaglia LA, Dembski M, Weng X, ''et al.'' |title=Identification and expression cloning of a leptin receptor, OB-R. |journal=Cell |volume=83 |issue= 7 |pages= 1263-71 |year= 1996 |pmid= 8548812 |doi= }}
*{{cite journal | author=Chen H, Charlat O, Tartaglia LA, ''et al.'' |title=Evidence that the diabetes gene encodes the leptin receptor: identification of a mutation in the leptin receptor gene in db/db mice. |journal=Cell |volume=84 |issue= 3 |pages= 491-5 |year= 1996 |pmid= 8608603 |doi= }}
*{{cite journal | author=Cioffi JA, Shafer AW, Zupancic TJ, ''et al.'' |title=Novel B219/OB receptor isoforms: possible role of leptin in hematopoiesis and reproduction. |journal=Nat. Med. |volume=2 |issue= 5 |pages= 585-9 |year= 1996 |pmid= 8616721 |doi= }}
*{{cite journal | author=Considine RV, Considine EL, Williams CJ, ''et al.'' |title=The hypothalamic leptin receptor in humans: identification of incidental sequence polymorphisms and absence of the db/db mouse and fa/fa rat mutations. |journal=Diabetes |volume=45 |issue= 7 |pages= 992-4 |year= 1996 |pmid= 8666155 |doi= }}
*{{cite journal | author=Chung WK, Power-Kehoe L, Chua M, Leibel RL |title=Mapping of the OB receptor to 1p in a region of nonconserved gene order from mouse and rat to human. |journal=Genome Res. |volume=6 |issue= 5 |pages= 431-8 |year= 1996 |pmid= 8743992 |doi= }}
*{{cite journal | author=Bennett BD, Solar GP, Yuan JQ, ''et al.'' |title=A role for leptin and its cognate receptor in hematopoiesis. |journal=Curr. Biol. |volume=6 |issue= 9 |pages= 1170-80 |year= 1997 |pmid= 8805376 |doi= }}
*{{cite journal | author=Winick JD, Stoffel M, Friedman JM |title=Identification of microsatellite markers linked to the human leptin receptor gene on chromosome 1. |journal=Genomics |volume=36 |issue= 1 |pages= 221-2 |year= 1997 |pmid= 8812446 |doi= 10.1006/geno.1996.0455 }}
*{{cite journal | author=Luoh SM, Di Marco F, Levin N, ''et al.'' |title=Cloning and characterization of a human leptin receptor using a biologically active leptin immunoadhesin. |journal=J. Mol. Endocrinol. |volume=18 |issue= 1 |pages= 77-85 |year= 1997 |pmid= 9061609 |doi= }}
*{{cite journal | author=Echwald SM, Sørensen TD, Sørensen TI, ''et al.'' |title=Amino acid variants in the human leptin receptor: lack of association to juvenile onset obesity. |journal=Biochem. Biophys. Res. Commun. |volume=233 |issue= 1 |pages= 248-52 |year= 1997 |pmid= 9144432 |doi= 10.1006/bbrc.1997.6430 }}
*{{cite journal | author=Thompson DB, Ravussin E, Bennett PH, Bogardus C |title=Structure and sequence variation at the human leptin receptor gene in lean and obese Pima Indians. |journal=Hum. Mol. Genet. |volume=6 |issue= 5 |pages= 675-9 |year= 1997 |pmid= 9158141 |doi= }}
*{{cite journal | author=Gotoda T, Manning BS, Goldstone AP, ''et al.'' |title=Leptin receptor gene variation and obesity: lack of association in a white British male population. |journal=Hum. Mol. Genet. |volume=6 |issue= 6 |pages= 869-76 |year= 1997 |pmid= 9175732 |doi= }}
*{{cite journal | author=Bailleul B, Akerblom I, Strosberg AD |title=The leptin receptor promoter controls expression of a second distinct protein. |journal=Nucleic Acids Res. |volume=25 |issue= 14 |pages= 2752-8 |year= 1997 |pmid= 9207021 |doi= }}
*{{cite journal | author=Chung WK, Power-Kehoe L, Chua M, ''et al.'' |title=Exonic and intronic sequence variation in the human leptin receptor gene (LEPR). |journal=Diabetes |volume=46 |issue= 9 |pages= 1509-11 |year= 1997 |pmid= 9287054 |doi= }}
*{{cite journal | author=Bjørbaek C, Uotani S, da Silva B, Flier JS |title=Divergent signaling capacities of the long and short isoforms of the leptin receptor. |journal=J. Biol. Chem. |volume=272 |issue= 51 |pages= 32686-95 |year= 1998 |pmid= 9405487 |doi= }}
*{{cite journal | author=Clément K, Vaisse C, Lahlou N, ''et al.'' |title=A mutation in the human leptin receptor gene causes obesity and pituitary dysfunction. |journal=Nature |volume=392 |issue= 6674 |pages= 398-401 |year= 1998 |pmid= 9537324 |doi= 10.1038/32911 }}
*{{cite journal | author=Carpenter LR, Farruggella TJ, Symes A, ''et al.'' |title=Enhancing leptin response by preventing SH2-containing phosphatase 2 interaction with Ob receptor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 11 |pages= 6061-6 |year= 1998 |pmid= 9600917 |doi= }}
*{{cite journal | author=Kielar D, Clark JS, Ciechanowicz A, ''et al.'' |title=Leptin receptor isoforms expressed in human adipose tissue. |journal=Metab. Clin. Exp. |volume=47 |issue= 7 |pages= 844-7 |year= 1998 |pmid= 9667233 |doi= }}
*{{cite journal | author=Haniu M, Arakawa T, Bures EJ, ''et al.'' |title=Human leptin receptor. Determination of disulfide structure and N-glycosylation sites of the extracellular domain. |journal=J. Biol. Chem. |volume=273 |issue= 44 |pages= 28691-9 |year= 1998 |pmid= 9786864 |doi= }}
*{{cite journal | author=Haft CR, de la Luz Sierra M, Barr VA, ''et al.'' |title=Identification of a family of sorting nexin molecules and characterization of their association with receptors. |journal=Mol. Cell. Biol. |volume=18 |issue= 12 |pages= 7278-87 |year= 1998 |pmid= 9819414 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MPO... {November 12, 2007 5:54:36 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 5:55:05 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_MPO_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cxp.
| PDB = {{PDB2|1cxp}}, {{PDB2|1d2v}}, {{PDB2|1d5l}}, {{PDB2|1d7w}}, {{PDB2|1dnu}}, {{PDB2|1dnw}}, {{PDB2|1mhl}}, {{PDB2|1myp}}
| Name = Myeloperoxidase
| HGNCid = 7218
| Symbol = MPO
| AltSymbols =;
| OMIM = 606989
| ECnumber =
| Homologene = 55450
| MGIid = 97137
| GeneAtlas_image1 = PBB_GE_MPO_203948_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_MPO_203949_at_tn.png
| Function = {{GNF_GO|id=GO:0003682 |text = chromatin binding}} {{GNF_GO|id=GO:0004601 |text = peroxidase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005764 |text = lysosome}}
| Process = {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0006952 |text = defense response}} {{GNF_GO|id=GO:0006979 |text = response to oxidative stress}} {{GNF_GO|id=GO:0042744 |text = hydrogen peroxide catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4353
| Hs_Ensembl = ENSG00000005381
| Hs_RefseqProtein = NP_000241
| Hs_RefseqmRNA = NM_000250
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 53702201
| Hs_GenLoc_end = 53713281
| Hs_Uniprot = P05164
| Mm_EntrezGene = 17523
| Mm_Ensembl = ENSMUSG00000009350
| Mm_RefseqmRNA = NM_010824
| Mm_RefseqProtein = NP_034954
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 87609776
| Mm_GenLoc_end = 87620592
| Mm_Uniprot = Q571G0
}}
}}
'''Myeloperoxidase''', also known as '''MPO''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Myeloperoxidase (MPO) is a heme protein synthesized during myeloid differentiation that constitutes the major component of neutrophil azurophilic granules. Produced as a single chain precursor, myeloperoxidase is subsequently cleaved into a light and heavy chain. The mature myeloperoxidase is a tetramer composed of 2 light chains and 2 heavy chains. This enzyme produces hypohalous acids central to the microbicidal activity of netrophils.<ref>{{cite web | title = Entrez Gene: MPO myeloperoxidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4353| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Arnhold J |title=Properties, functions, and secretion of human myeloperoxidase. |journal=Biochemistry Mosc. |volume=69 |issue= 1 |pages= 4-9 |year= 2004 |pmid= 14972011 |doi= }}
*{{cite journal | author=Suzuki K, Okazaki T |title=Contribution of myeloperoxidase in vasculitis development. |journal=Jpn. J. Infect. Dis. |volume=57 |issue= 5 |pages= S2-3 |year= 2005 |pmid= 15507759 |doi= }}
*{{cite journal | author=Nicholls SJ, Hazen SL |title=The role of myeloperoxidase in the pathogenesis of coronary artery disease. |journal=Jpn. J. Infect. Dis. |volume=57 |issue= 5 |pages= S21-2 |year= 2005 |pmid= 15507760 |doi= }}
*{{cite journal | author=Nauseef WM |title=Lessons from MPO deficiency about functionally important structural features. |journal=Jpn. J. Infect. Dis. |volume=57 |issue= 5 |pages= S4-5 |year= 2005 |pmid= 15507769 |doi= }}
*{{cite journal | author=Williams J, Hewins P, Savage C |title=The influence of autoantibodies to myeloperoxidase on neutrophil function and intracellular signaling. |journal=Jpn. J. Infect. Dis. |volume=57 |issue= 5 |pages= S5-6 |year= 2005 |pmid= 15507770 |doi= }}
*{{cite journal | author=Schmitt WH |title=Newer insights into the aetiology and pathogenesis of myeloperoxidase associated autoimmunity. |journal=Jpn. J. Infect. Dis. |volume=57 |issue= 5 |pages= S7-8 |year= 2005 |pmid= 15507771 |doi= }}
*{{cite journal | author=Taioli E, Benhamou S, Bouchardy C, ''et al.'' |title=Myeloperoxidase G-463A polymorphism and lung cancer: a HuGE genetic susceptibility to environmental carcinogens pooled analysis. |journal=Genet. Med. |volume=9 |issue= 2 |pages= 67-73 |year= 2007 |pmid= 17304047 |doi= 10.1097/GIM.0b013e31803068b1 }}
*{{cite journal | author=Zeng J, Fenna RE |title=X-ray crystal structure of canine myeloperoxidase at 3 A resolution. |journal=J. Mol. Biol. |volume=226 |issue= 1 |pages= 185-207 |year= 1992 |pmid= 1320128 |doi= }}
*{{cite journal | author=Taylor KL, Pohl J, Kinkade JM |title=Unique autolytic cleavage of human myeloperoxidase. Implications for the involvement of active site MET409. |journal=J. Biol. Chem. |volume=267 |issue= 35 |pages= 25282-8 |year= 1993 |pmid= 1334087 |doi= }}
*{{cite journal | author=Srivastava CH, Rado TA, Bauerle D, Broxmeyer HE |title=Regulation of human bone marrow lactoferrin and myeloperoxidase gene expression by tumor necrosis factor-alpha. |journal=J. Immunol. |volume=146 |issue= 3 |pages= 1014-9 |year= 1991 |pmid= 1703177 |doi= }}
*{{cite journal | author=Yamada M, Hur SJ, Toda H |title=Isolation and characterization of extracellular myeloperoxidase precursor in HL-60 cell cultures. |journal=Biochem. Biophys. Res. Commun. |volume=166 |issue= 2 |pages= 852-9 |year= 1990 |pmid= 2154223 |doi= }}
*{{cite journal | author=Morishita K, Tsuchiya M, Asano S, ''et al.'' |title=Chromosomal gene structure of human myeloperoxidase and regulation of its expression by granulocyte colony-stimulating factor. |journal=J. Biol. Chem. |volume=262 |issue= 31 |pages= 15208-13 |year= 1987 |pmid= 2444596 |doi= }}
*{{cite journal | author=Johnson K, Gemperlein I, Hudson S, ''et al.'' |title=Complete nucleotide sequence of the human myeloperoxidase gene. |journal=Nucleic Acids Res. |volume=17 |issue= 19 |pages= 7985-6 |year= 1989 |pmid= 2552418 |doi= }}
*{{cite journal | author=Nauseef WM |title=Posttranslational processing of a human myeloid lysosomal protein, myeloperoxidase. |journal=Blood |volume=70 |issue= 4 |pages= 1143-50 |year= 1987 |pmid= 2820530 |doi= }}
*{{cite journal | author=Murao S, Stevens FJ, Ito A, Huberman E |title=Myeloperoxidase: a myeloid cell nuclear antigen with DNA-binding properties. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 4 |pages= 1232-6 |year= 1988 |pmid= 2829220 |doi= }}
*{{cite journal | author=Yamada M, Hur SJ, Hashinaka K, ''et al.'' |title=Isolation and characterization of a cDNA coding for human myeloperoxidase. |journal=Arch. Biochem. Biophys. |volume=255 |issue= 1 |pages= 147-55 |year= 1987 |pmid= 2884926 |doi= }}
*{{cite journal | author=Hashinaka K, Nishio C, Hur SJ, ''et al.'' |title=Multiple species of myeloperoxidase messenger RNAs produced by alternative splicing and differential polyadenylation. |journal=Biochemistry |volume=27 |issue= 16 |pages= 5906-14 |year= 1989 |pmid= 2903767 |doi= }}
*{{cite journal | author=Morishita K, Kubota N, Asano S, ''et al.'' |title=Molecular cloning and characterization of cDNA for human myeloperoxidase. |journal=J. Biol. Chem. |volume=262 |issue= 8 |pages= 3844-51 |year= 1987 |pmid= 3029127 |doi= }}
*{{cite journal | author=Johnson KR, Nauseef WM, Care A, ''et al.'' |title=Characterization of cDNA clones for human myeloperoxidase: predicted amino acid sequence and evidence for multiple mRNA species. |journal=Nucleic Acids Res. |volume=15 |issue= 5 |pages= 2013-28 |year= 1987 |pmid= 3031585 |doi= }}
*{{cite journal | author=Seto P, Hirayu H, Magnusson RP, ''et al.'' |title=Isolation of a complementary DNA clone for thyroid microsomal antigen. Homology with the gene for thyroid peroxidase. |journal=J. Clin. Invest. |volume=80 |issue= 4 |pages= 1205-8 |year= 1987 |pmid= 3654979 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PCAF... {November 12, 2007 6:02:22 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 6:03:16 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PCAF_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cm0.
| PDB = {{PDB2|1cm0}}, {{PDB2|1jm4}}, {{PDB2|1n72}}, {{PDB2|1wug}}, {{PDB2|1wum}}, {{PDB2|1zs5}}
| Name = P300/CBP-associated factor
| HGNCid = 8638
| Symbol = PCAF
| AltSymbols =; P; CAF; P/CAF
| OMIM = 602303
| ECnumber =
| Homologene = 20834
| MGIid = 1343094
| GeneAtlas_image1 = PBB_GE_PCAF_203845_at_tn.png
| Function = {{GNF_GO|id=GO:0003712 |text = transcription cofactor activity}} {{GNF_GO|id=GO:0004402 |text = histone acetyltransferase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008080 |text = N-acetyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0042826 |text = histone deacetylase binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006338 |text = chromatin remodeling}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006473 |text = protein amino acid acetylation}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007050 |text = cell cycle arrest}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8850
| Hs_Ensembl = ENSG00000114166
| Hs_RefseqProtein = XP_001130666
| Hs_RefseqmRNA = XM_001130666
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 20056528
| Hs_GenLoc_end = 20170887
| Hs_Uniprot = Q92831
| Mm_EntrezGene = 18519
| Mm_Ensembl = ENSMUSG00000000708
| Mm_RefseqmRNA = XM_001003318
| Mm_RefseqProtein = XP_001003318
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 53032244
| Mm_GenLoc_end = 53137649
| Mm_Uniprot =
}}
}}
'''P300/CBP-associated factor''', also known as '''PCAF''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = CBP and p300 are large nuclear proteins that bind to many sequence-specific factors involved in cell growth and/or differentiation, including c-jun and the adenoviral oncoprotein E1A. The protein encoded by this gene associates with p300/CBP. It has in vitro and in vivo binding activity with CBP and p300, and competes with E1A for binding sites in p300/CBP. It has histone acetyl transferase activity with core histones and nucleosome core particles, indicating that this protein plays a direct role in transcriptional regulation.<ref>{{cite web | title = Entrez Gene: PCAF p300/CBP-associated factor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8850| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Marcello A, Zoppé M, Giacca M |title=Multiple modes of transcriptional regulation by the HIV-1 Tat transactivator. |journal=IUBMB Life |volume=51 |issue= 3 |pages= 175-81 |year= 2002 |pmid= 11547919 |doi= }}
*{{cite journal | author=Ott M, Dorr A, Hetzer-Egger C, ''et al.'' |title=Tat acetylation: a regulatory switch between early and late phases in HIV transcription elongation. |journal=Novartis Found. Symp. |volume=259 |issue= |pages= 182-93; discussion 193-6, 223-5 |year= 2004 |pmid= 15171254 |doi= }}
*{{cite journal | author=Liou LY, Herrmann CH, Rice AP |title=HIV-1 infection and regulation of Tat function in macrophages. |journal=Int. J. Biochem. Cell Biol. |volume=36 |issue= 9 |pages= 1767-75 |year= 2005 |pmid= 15183343 |doi= 10.1016/j.biocel.2004.02.018 }}
*{{cite journal | author=Gibellini D, Vitone F, Schiavone P, Re MC |title=HIV-1 tat protein and cell proliferation and survival: a brief review. |journal=New Microbiol. |volume=28 |issue= 2 |pages= 95-109 |year= 2005 |pmid= 16035254 |doi= }}
*{{cite journal | author=Hetzer C, Dormeyer W, Schnölzer M, Ott M |title=Decoding Tat: the biology of HIV Tat posttranslational modifications. |journal=Microbes Infect. |volume=7 |issue= 13 |pages= 1364-9 |year= 2006 |pmid= 16046164 |doi= 10.1016/j.micinf.2005.06.003 }}
*{{cite journal | author=Peruzzi F |title=The multiple functions of HIV-1 Tat: proliferation versus apoptosis. |journal=Front. Biosci. |volume=11 |issue= |pages= 708-17 |year= 2006 |pmid= 16146763 |doi= }}
*{{cite journal | author=Stevens M, De Clercq E, Balzarini J |title=The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention. |journal=Med Res Rev |volume=26 |issue= 5 |pages= 595-625 |year= 2007 |pmid= 16838299 |doi= 10.1002/med.20081 }}
*{{cite journal | author=Harrich D, McMillan N, Munoz L, ''et al.'' |title=Will diverse Tat interactions lead to novel antiretroviral drug targets? |journal=Current drug targets |volume=7 |issue= 12 |pages= 1595-606 |year= 2007 |pmid= 17168834 |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=Yang XJ, Ogryzko VV, Nishikawa J, ''et al.'' |title=A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. |journal=Nature |volume=382 |issue= 6589 |pages= 319-24 |year= 1996 |pmid= 8684459 |doi= 10.1038/382319a0 }}
*{{cite journal | author=Ogryzko VV, Schiltz RL, Russanova V, ''et al.'' |title=The transcriptional coactivators p300 and CBP are histone acetyltransferases. |journal=Cell |volume=87 |issue= 5 |pages= 953-9 |year= 1997 |pmid= 8945521 |doi= }}
*{{cite journal | author=Jenster G, Spencer TE, Burcin MM, ''et al.'' |title=Steroid receptor induction of gene transcription: a two-step model. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 15 |pages= 7879-84 |year= 1997 |pmid= 9223281 |doi= }}
*{{cite journal | author=Chen H, Lin RJ, Schiltz RL, ''et al.'' |title=Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. |journal=Cell |volume=90 |issue= 3 |pages= 569-80 |year= 1997 |pmid= 9267036 |doi= }}
*{{cite journal | author=Spencer TE, Jenster G, Burcin MM, ''et al.'' |title=Steroid receptor coactivator-1 is a histone acetyltransferase. |journal=Nature |volume=389 |issue= 6647 |pages= 194-8 |year= 1997 |pmid= 9296499 |doi= 10.1038/38304 }}
*{{cite journal | author=Takeshita A, Cardona GR, Koibuchi N, ''et al.'' |title=TRAM-1, A novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1. |journal=J. Biol. Chem. |volume=272 |issue= 44 |pages= 27629-34 |year= 1997 |pmid= 9346901 |doi= }}
*{{cite journal | author=Korzus E, Torchia J, Rose DW, ''et al.'' |title=Transcription factor-specific requirements for coactivators and their acetyltransferase functions. |journal=Science |volume=279 |issue= 5351 |pages= 703-7 |year= 1998 |pmid= 9445475 |doi= }}
*{{cite journal | author=Puri PL, Sartorelli V, Yang XJ, ''et al.'' |title=Differential roles of p300 and PCAF acetyltransferases in muscle differentiation. |journal=Mol. Cell |volume=1 |issue= 1 |pages= 35-45 |year= 1998 |pmid= 9659901 |doi= }}
*{{cite journal | author=Ogryzko VV, Kotani T, Zhang X, ''et al.'' |title=Histone-like TAFs within the PCAF histone acetylase complex. |journal=Cell |volume=94 |issue= 1 |pages= 35-44 |year= 1998 |pmid= 9674425 |doi= }}
*{{cite journal | author=Randhawa GS, Bell DW, Testa JR, Feinberg AP |title=Identification and mapping of human histone acetylation modifier gene homologues. |journal=Genomics |volume=51 |issue= 2 |pages= 262-9 |year= 1998 |pmid= 9722949 |doi= 10.1006/geno.1998.5370 }}
*{{cite journal | author=Benkirane M, Chun RF, Xiao H, ''et al.'' |title=Activation of integrated provirus requires histone acetyltransferase. p300 and P/CAF are coactivators for HIV-1 Tat. |journal=J. Biol. Chem. |volume=273 |issue= 38 |pages= 24898-905 |year= 1998 |pmid= 9733796 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PIK3CA... {November 12, 2007 5:56:05 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 5:56:50 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Phosphoinositide-3-kinase, catalytic, alpha polypeptide
| HGNCid = 8975
| Symbol = PIK3CA
| AltSymbols =; MGC142161; MGC142163; PI3K; p110-alpha
| OMIM = 171834
| ECnumber =
| Homologene = 21249
| MGIid = 1206581
| GeneAtlas_image1 = PBB_GE_PIK3CA_204369_at_tn.png
| Function = {{GNF_GO|id=GO:0004428 |text = inositol or phosphatidylinositol kinase activity}} {{GNF_GO|id=GO:0016303 |text = 1-phosphatidylinositol-3-kinase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0043560 |text = insulin receptor substrate binding}} {{GNF_GO|id=GO:0046934 |text = phosphatidylinositol-4,5-bisphosphate 3-kinase activity}}
| Component = {{GNF_GO|id=GO:0005942 |text = phosphoinositide 3-kinase complex}} {{GNF_GO|id=GO:0030027 |text = lamellipodium}}
| Process = {{GNF_GO|id=GO:0006006 |text = glucose metabolic process}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0040014 |text = regulation of body size}} {{GNF_GO|id=GO:0043491 |text = protein kinase B signaling cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5290
| Hs_Ensembl = ENSG00000121879
| Hs_RefseqProtein = NP_006209
| Hs_RefseqmRNA = NM_006218
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 180349005
| Hs_GenLoc_end = 180435189
| Hs_Uniprot = P42336
| Mm_EntrezGene = 18706
| Mm_Ensembl = ENSMUSG00000027665
| Mm_RefseqmRNA = NM_008839
| Mm_RefseqProtein = NP_032865
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 32627755
| Mm_GenLoc_end = 32654380
| Mm_Uniprot = Q0VGQ5
}}
}}
'''Phosphoinositide-3-kinase, catalytic, alpha polypeptide''', also known as '''PIK3CA''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Phosphatidylinositol 3-kinase is composed of an 85 kDa regulatory subunit and a 110 kDa catalytic subunit. The protein encoded by this gene represents the catalytic subunit, which uses ATP to phosphorylate PtdIns, PtdIns4P and PtdIns(4,5)P2. This gene has been found to be oncogenic and has been implicated in cervical cancers.<ref>{{cite web | title = Entrez Gene: PIK3CA phosphoinositide-3-kinase, catalytic, alpha polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5290| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Katada T, Kurosu H, Okada T, ''et al.'' |title=Synergistic activation of a family of phosphoinositide 3-kinase via G-protein coupled and tyrosine kinase-related receptors. |journal=Chem. Phys. Lipids |volume=98 |issue= 1-2 |pages= 79-86 |year= 1999 |pmid= 10358930 |doi= }}
*{{cite journal | author=Lee C, Liu QH, Tomkowicz B, ''et al.'' |title=Macrophage activation through CCR5- and CXCR4-mediated gp120-elicited signaling pathways. |journal=J. Leukoc. Biol. |volume=74 |issue= 5 |pages= 676-82 |year= 2004 |pmid= 12960231 |doi= 10.1189/jlb.0503206 }}
*{{cite journal | author=Bader AG, Kang S, Zhao L, Vogt PK |title=Oncogenic PI3K deregulates transcription and translation. |journal=Nat. Rev. Cancer |volume=5 |issue= 12 |pages= 921-9 |year= 2005 |pmid= 16341083 |doi= 10.1038/nrc1753 }}
*{{cite journal | author=Liu Z, Roberts TM |title=Human tumor mutants in the p110alpha subunit of PI3K. |journal=Cell Cycle |volume=5 |issue= 7 |pages= 675-7 |year= 2006 |pmid= 16627990 |doi= }}
*{{cite journal | author=Hiles ID, Otsu M, Volinia S, ''et al.'' |title=Phosphatidylinositol 3-kinase: structure and expression of the 110 kd catalytic subunit. |journal=Cell |volume=70 |issue= 3 |pages= 419-29 |year= 1992 |pmid= 1322797 |doi= }}
*{{cite journal | author=Carpenter CL, Duckworth BC, Auger KR, ''et al.'' |title=Purification and characterization of phosphoinositide 3-kinase from rat liver. |journal=J. Biol. Chem. |volume=265 |issue= 32 |pages= 19704-11 |year= 1991 |pmid= 2174051 |doi= }}
*{{cite journal | author=Volinia S, Hiles I, Ormondroyd E, ''et al.'' |title=Molecular cloning, cDNA sequence, and chromosomal localization of the human phosphatidylinositol 3-kinase p110 alpha (PIK3CA) gene. |journal=Genomics |volume=24 |issue= 3 |pages= 472-7 |year= 1995 |pmid= 7713498 |doi= }}
*{{cite journal | author=Kodaki T, Woscholski R, Hallberg B, ''et al.'' |title=The activation of phosphatidylinositol 3-kinase by Ras. |journal=Curr. Biol. |volume=4 |issue= 9 |pages= 798-806 |year= 1995 |pmid= 7820549 |doi= }}
*{{cite journal | author=Woscholski R, Dhand R, Fry MJ, ''et al.'' |title=Biochemical characterization of the free catalytic p110 alpha and the complexed heterodimeric p110 alpha.p85 alpha forms of the mammalian phosphatidylinositol 3-kinase. |journal=J. Biol. Chem. |volume=269 |issue= 40 |pages= 25067-72 |year= 1994 |pmid= 7929193 |doi= }}
*{{cite journal | author=von Willebrand M, Baier G, Couture C, ''et al.'' |title=Activation of phosphatidylinositol-3-kinase in Jurkat T cells depends on the presence of the p56lck tyrosine kinase. |journal=Eur. J. Immunol. |volume=24 |issue= 1 |pages= 234-8 |year= 1994 |pmid= 8020561 |doi= }}
*{{cite journal | author=Graziani A, Galimi F, Medico E, ''et al.'' |title=The HIV-1 nef protein interferes with phosphatidylinositol 3-kinase activation 1. |journal=J. Biol. Chem. |volume=271 |issue= 12 |pages= 6590-3 |year= 1996 |pmid= 8636073 |doi= }}
*{{cite journal | author=Salgia R, Sattler M, Pisick E, ''et al.'' |title=p210BCR/ABL induces formation of complexes containing focal adhesion proteins and the protooncogene product p120c-Cbl. |journal=Exp. Hematol. |volume=24 |issue= 2 |pages= 310-3 |year= 1996 |pmid= 8641358 |doi= }}
*{{cite journal | author=Liu YC, Elly C, Yoshida H, ''et al.'' |title=Activation-modulated association of 14-3-3 proteins with Cbl in T cells. |journal=J. Biol. Chem. |volume=271 |issue= 24 |pages= 14591-5 |year= 1996 |pmid= 8663231 |doi= }}
*{{cite journal | author=Rodriguez-Viciana P, Warne PH, Vanhaesebroeck B, ''et al.'' |title=Activation of phosphoinositide 3-kinase by interaction with Ras and by point mutation. |journal=EMBO J. |volume=15 |issue= 10 |pages= 2442-51 |year= 1996 |pmid= 8665852 |doi= }}
*{{cite journal | author=Domin J, Dhand R, Waterfield MD |title=Binding to the platelet-derived growth factor receptor transiently activates the p85alpha-p110alpha phosphoinositide 3-kinase complex in vivo. |journal=J. Biol. Chem. |volume=271 |issue= 35 |pages= 21614-21 |year= 1996 |pmid= 8702949 |doi= }}
*{{cite journal | author=Milani D, Mazzoni M, Borgatti P, ''et al.'' |title=Extracellular human immunodeficiency virus type-1 Tat protein activates phosphatidylinositol 3-kinase in PC12 neuronal cells. |journal=J. Biol. Chem. |volume=271 |issue= 38 |pages= 22961-4 |year= 1996 |pmid= 8798481 |doi= }}
*{{cite journal | author=Stirdivant SM, Ahern J, Conroy RR, ''et al.'' |title=Cloning and mutagenesis of the p110 alpha subunit of human phosphoinositide 3'-hydroxykinase. |journal=Bioorg. Med. Chem. |volume=5 |issue= 1 |pages= 65-74 |year= 1997 |pmid= 9043658 |doi= }}
*{{cite journal | author=Vanhaesebroeck B, Welham MJ, Kotani K, ''et al.'' |title=P110delta, a novel phosphoinositide 3-kinase in leukocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 9 |pages= 4330-5 |year= 1997 |pmid= 9113989 |doi= }}
*{{cite journal | author=Rodriguez-Viciana P, Warne PH, Khwaja A, ''et al.'' |title=Role of phosphoinositide 3-OH kinase in cell transformation and control of the actin cytoskeleton by Ras. |journal=Cell |volume=89 |issue= 3 |pages= 457-67 |year= 1997 |pmid= 9150145 |doi= }}
*{{cite journal | author=Garcia A |title=Expression of HIV-1 nef decreases basal phosphatidyl-inositol 3-kinase activity. |journal=C. R. Acad. Sci. III, Sci. Vie |volume=320 |issue= 6 |pages= 505-8 |year= 1997 |pmid= 9247029 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RAD51... {November 12, 2007 5:57:58 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 5:58:53 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_RAD51_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1b22.
| PDB = {{PDB2|1b22}}, {{PDB2|1n0w}}
| Name = RAD51 homolog (RecA homolog, E. coli) (S. cerevisiae)
| HGNCid = 9817
| Symbol = RAD51
| AltSymbols =; BRCC5; HRAD51; HsRad51; HsT16930; RAD51A; RECA
| OMIM = 179617
| ECnumber =
| Homologene = 2155
| MGIid = 97890
| GeneAtlas_image1 = PBB_GE_RAD51_205024_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_RAD51_205023_at_tn.png
| Function = {{GNF_GO|id=GO:0000150 |text = recombinase activity}} {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003684 |text = damaged DNA binding}} {{GNF_GO|id=GO:0003690 |text = double-stranded DNA binding}} {{GNF_GO|id=GO:0003697 |text = single-stranded DNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008094 |text = DNA-dependent ATPase activity}} {{GNF_GO|id=GO:0016887 |text = ATPase activity}} {{GNF_GO|id=GO:0017111 |text = nucleoside-triphosphatase activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}} {{GNF_GO|id=GO:0043142 |text = single-stranded DNA-dependent ATPase activity}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}}
| Component = {{GNF_GO|id=GO:0000795 |text = synaptonemal complex}} {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0000724 |text = double-strand break repair via homologous recombination}} {{GNF_GO|id=GO:0006268 |text = DNA unwinding during replication}} {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006312 |text = mitotic recombination}} {{GNF_GO|id=GO:0007126 |text = meiosis}} {{GNF_GO|id=GO:0007131 |text = meiotic recombination}} {{GNF_GO|id=GO:0051106 |text = positive regulation of DNA ligation}} {{GNF_GO|id=GO:0051260 |text = protein homooligomerization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5888
| Hs_Ensembl = ENSG00000051180
| Hs_RefseqProtein = NP_002866
| Hs_RefseqmRNA = NM_002875
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 38774661
| Hs_GenLoc_end = 38811646
| Hs_Uniprot = Q06609
| Mm_EntrezGene = 19361
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_011234
| Mm_RefseqProtein = NP_035364
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''RAD51 homolog (RecA homolog, E. coli) (S. cerevisiae)''', also known as '''RAD51''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the RAD51 protein family. RAD51 family members are highly similar to bacterial RecA and Saccharomyces cerevisiae Rad51, and are known to be involved in the homologous recombination and repair of DNA. This protein can interact with the ssDNA-binding protein RPA and RAD52, and it is thought to play roles in homologous pairing and strand transfer of DNA. This protein is also found to interact with BRCA1 and BRCA2, which may be important for the cellular response to DNA damage. BRCA2 is shown to regulate both the intracellular localization and DNA-binding ability of this protein. Loss of these controls following BRCA2 inactivation may be a key event leading to genomic instability and tumorigenesis. Two alternatively spliced transcript variants of this gene, which encode distinct proteins, have been reported. Transcript variants utilizing alternative polyA signals exist.<ref>{{cite web | title = Entrez Gene: RAD51 RAD51 homolog (RecA homolog, E. coli) (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5888| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Daniel DC |title=Highlight: BRCA1 and BRCA2 proteins in breast cancer. |journal=Microsc. Res. Tech. |volume=59 |issue= 1 |pages= 68-83 |year= 2002 |pmid= 12242698 |doi= 10.1002/jemt.10178 }}
*{{cite journal | author=Henning W, Stürzbecher HW |title=Homologous recombination and cell cycle checkpoints: Rad51 in tumour progression and therapy resistance. |journal=Toxicology |volume=193 |issue= 1-2 |pages= 91-109 |year= 2003 |pmid= 14599770 |doi= }}
*{{cite journal | author=Hasselbach L, Haase S, Fischer D, ''et al.'' |title=Characterisation of the promoter region of the human DNA-repair gene Rad51. |journal=Eur. J. Gynaecol. Oncol. |volume=26 |issue= 6 |pages= 589-98 |year= 2006 |pmid= 16398215 |doi= }}
*{{cite journal | author=Benson FE, Stasiak A, West SC |title=Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA. |journal=EMBO J. |volume=13 |issue= 23 |pages= 5764-71 |year= 1995 |pmid= 7988572 |doi= }}
*{{cite journal | author=Takahashi E, Matsuda Y, Hori T, ''et al.'' |title=Chromosome mapping of the human (RECA) and mouse (Reca) homologs of the yeast RAD51 and Escherichia coli recA genes to human (15q15.1) and mouse (2F1) chromosomes by direct R-banding fluorescence in situ hybridization. |journal=Genomics |volume=19 |issue= 2 |pages= 376-8 |year= 1994 |pmid= 8188269 |doi= }}
*{{cite journal | author=Shinohara A, Ogawa H, Matsuda Y, ''et al.'' |title=Cloning of human, mouse and fission yeast recombination genes homologous to RAD51 and recA. |journal=Nat. Genet. |volume=4 |issue= 3 |pages= 239-43 |year= 1993 |pmid= 8358431 |doi= 10.1038/ng0793-239 }}
*{{cite journal | author=Yoshimura Y, Morita T, Yamamoto A, Matsushiro A |title=Cloning and sequence of the human RecA-like gene cDNA. |journal=Nucleic Acids Res. |volume=21 |issue= 7 |pages= 1665 |year= 1993 |pmid= 8479919 |doi= }}
*{{cite journal | author=Kovalenko OV, Plug AW, Haaf T, ''et al.'' |title=Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 7 |pages= 2958-63 |year= 1996 |pmid= 8610150 |doi= }}
*{{cite journal | author=Stürzbecher HW, Donzelmann B, Henning W, ''et al.'' |title=p53 is linked directly to homologous recombination processes via RAD51/RecA protein interaction. |journal=EMBO J. |volume=15 |issue= 8 |pages= 1992-2002 |year= 1996 |pmid= 8617246 |doi= }}
*{{cite journal | author=Wang XW, Vermeulen W, Coursen JD, ''et al.'' |title=The XPB and XPD DNA helicases are components of the p53-mediated apoptosis pathway. |journal=Genes Dev. |volume=10 |issue= 10 |pages= 1219-32 |year= 1996 |pmid= 8675009 |doi= }}
*{{cite journal | author=Flygare J, Benson F, Hellgren D |title=Expression of the human RAD51 gene during the cell cycle in primary human peripheral blood lymphocytes. |journal=Biochim. Biophys. Acta |volume=1312 |issue= 3 |pages= 231-6 |year= 1996 |pmid= 8703992 |doi= }}
*{{cite journal | author=Shen Z, Pardington-Purtymun PE, Comeaux JC, ''et al.'' |title=UBL1, a human ubiquitin-like protein associating with human RAD51/RAD52 proteins. |journal=Genomics |volume=36 |issue= 2 |pages= 271-9 |year= 1997 |pmid= 8812453 |doi= 10.1006/geno.1996.0462 }}
*{{cite journal | author=Li MJ, Peakman MC, Golub EI, ''et al.'' |title=Rad51 expression and localization in B cells carrying out class switch recombination. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 19 |pages= 10222-7 |year= 1996 |pmid= 8816780 |doi= }}
*{{cite journal | author=Shen Z, Pardington-Purtymun PE, Comeaux JC, ''et al.'' |title=Associations of UBE2I with RAD52, UBL1, p53, and RAD51 proteins in a yeast two-hybrid system. |journal=Genomics |volume=37 |issue= 2 |pages= 183-6 |year= 1997 |pmid= 8921390 |doi= 10.1006/geno.1996.0540 }}
*{{cite journal | author=Baumann P, Benson FE, West SC |title=Human Rad51 protein promotes ATP-dependent homologous pairing and strand transfer reactions in vitro. |journal=Cell |volume=87 |issue= 4 |pages= 757-66 |year= 1997 |pmid= 8929543 |doi= }}
*{{cite journal | author=Scully R, Chen J, Plug A, ''et al.'' |title=Association of BRCA1 with Rad51 in mitotic and meiotic cells. |journal=Cell |volume=88 |issue= 2 |pages= 265-75 |year= 1997 |pmid= 9008167 |doi= }}
*{{cite journal | author=Cujec TP, Cho H, Maldonado E, ''et al.'' |title=The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme. |journal=Mol. Cell. Biol. |volume=17 |issue= 4 |pages= 1817-23 |year= 1997 |pmid= 9121429 |doi= }}
*{{cite journal | author=Sharan SK, Morimatsu M, Albrecht U, ''et al.'' |title=Embryonic lethality and radiation hypersensitivity mediated by Rad51 in mice lacking Brca2. |journal=Nature |volume=386 |issue= 6627 |pages= 804-10 |year= 1997 |pmid= 9126738 |doi= 10.1038/386804a0 }}
*{{cite journal | author=Mizuta R, LaSalle JM, Cheng HL, ''et al.'' |title=RAB22 and RAB163/mouse BRCA2: proteins that specifically interact with the RAD51 protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 13 |pages= 6927-32 |year= 1997 |pmid= 9192668 |doi= }}
*{{cite journal | author=Golub EI, Kovalenko OV, Gupta RC, ''et al.'' |title=Interaction of human recombination proteins Rad51 and Rad54. |journal=Nucleic Acids Res. |volume=25 |issue= 20 |pages= 4106-10 |year= 1997 |pmid= 9321665 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SERPINC1... {November 12, 2007 5:44:31 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 5:45:27 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_SERPINC1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ant.
| PDB = {{PDB2|1ant}}, {{PDB2|1ath}}, {{PDB2|1azx}}, {{PDB2|1br8}}, {{PDB2|1dzg}}, {{PDB2|1dzh}}, {{PDB2|1e03}}, {{PDB2|1e04}}, {{PDB2|1e05}}, {{PDB2|1jvq}}, {{PDB2|1lk6}}, {{PDB2|1nq9}}, {{PDB2|1oyh}}, {{PDB2|1r1l}}, {{PDB2|1sr5}}, {{PDB2|1t1f}}, {{PDB2|1tb6}}, {{PDB2|2ant}}, {{PDB2|2b4x}}, {{PDB2|2b5t}}, {{PDB2|2beh}}, {{PDB2|2gd4}}
| Name = Serpin peptidase inhibitor, clade C (antithrombin), member 1
| HGNCid = 775
| Symbol = SERPINC1
| AltSymbols =; AT3; ATIII; MGC22579
| OMIM = 107300
| ECnumber =
| Homologene = 20139
| MGIid = 88095
| GeneAtlas_image1 = PBB_GE_SERPINC1_210049_at_tn.png
| Function = {{GNF_GO|id=GO:0004867 |text = serine-type endopeptidase inhibitor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008201 |text = heparin binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0007596 |text = blood coagulation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 462
| Hs_Ensembl = ENSG00000117601
| Hs_RefseqProtein = NP_000479
| Hs_RefseqmRNA = NM_000488
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 172139562
| Hs_GenLoc_end = 172153139
| Hs_Uniprot = P01008
| Mm_EntrezGene = 11905
| Mm_Ensembl = ENSMUSG00000026715
| Mm_RefseqmRNA = NM_080844
| Mm_RefseqProtein = NP_543120
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 162815323
| Mm_GenLoc_end = 162839687
| Mm_Uniprot = Q543J5
}}
}}
'''Serpin peptidase inhibitor, clade C (antithrombin), member 1''', also known as '''SERPINC1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Blajchman MA, Austin RC, Fernandez-Rachubinski F, Sheffield WP |title=Molecular basis of inherited human antithrombin deficiency. |journal=Blood |volume=80 |issue= 9 |pages= 2159-71 |year= 1992 |pmid= 1421387 |doi= }}
*{{cite journal | author=Mourey L, Samama JP, Delarue M, ''et al.'' |title=Antithrombin III: structural and functional aspects. |journal=Biochimie |volume=72 |issue= 8 |pages= 599-608 |year= 1991 |pmid= 2126464 |doi= }}
*{{cite journal | author=Hultin MB, McKay J, Abildgaard U |title=Antithrombin Oslo: type Ib classification of the first reported antithrombin-deficient family, with a review of hereditary antithrombin variants. |journal=Thromb. Haemost. |volume=59 |issue= 3 |pages= 468-73 |year= 1988 |pmid= 3055413 |doi= }}
*{{cite journal | author=Stein PE, Carrell RW |title=What do dysfunctional serpins tell us about molecular mobility and disease? |journal=Nat. Struct. Biol. |volume=2 |issue= 2 |pages= 96-113 |year= 1995 |pmid= 7749926 |doi= }}
*{{cite journal | author=Perry DJ, Carrell RW |title=Molecular genetics of human antithrombin deficiency. |journal=Hum. Mutat. |volume=7 |issue= 1 |pages= 7-22 |year= 1996 |pmid= 8664906 |doi= 10.1002/(SICI)1098-1004(1996)7:1<7::AID-HUMU2>3.0.CO;2-B }}
*{{cite journal | author=Lane DA, Bayston T, Olds RJ, ''et al.'' |title=Antithrombin mutation database: 2nd (1997) update. For the Plasma Coagulation Inhibitors Subcommittee of the Scientific and Standardization Committee of the International Society on Thrombosis and Haemostasis. |journal=Thromb. Haemost. |volume=77 |issue= 1 |pages= 197-211 |year= 1997 |pmid= 9031473 |doi= }}
*{{cite journal | author=Kuhle S, Lane DA, Jochmanns K, ''et al.'' |title=Homozygous antithrombin deficiency type II (99 Leu to Phe mutation) and childhood thromboembolism. |journal=Thromb. Haemost. |volume=86 |issue= 4 |pages= 1007-11 |year= 2002 |pmid= 11686316 |doi= }}
*{{cite journal | author=Witt I |title=[Molecular biological basis and diagnosis of hereditary defect of antithrombin III, protein c and protein S] |journal=Hamostaseologie |volume=22 |issue= 2 |pages= 14-24 |year= 2002 |pmid= 12193972 |doi= 10.1267/Hamo02020057 }}
*{{cite journal | author=Wiedermann CJ |title=Clinical review: molecular mechanisms underlying the role of antithrombin in sepsis. |journal=Critical care (London, England) |volume=10 |issue= 1 |pages= 209 |year= 2006 |pmid= 16542481 |doi= 10.1186/cc4822 }}
*{{cite journal | author=Abildgaard U |title=Antithrombin--early prophecies and present challenges. |journal=Thromb. Haemost. |volume=98 |issue= 1 |pages= 97-104 |year= 2007 |pmid= 17597998 |doi= }}
*{{cite journal | author=Labarrere CA, Pitts D, Halbrook H, Faulk WP |title=Natural anticoagulant pathways in normal and transplanted human hearts. |journal=J. Heart Lung Transplant. |volume=11 |issue= 2 Pt 1 |pages= 342-7 |year= 1992 |pmid= 1315572 |doi= }}
*{{cite journal | author=Daly M, Perry DJ, Harper PL, ''et al.'' |title=Insertions/deletions in the antithrombin gene: 3 mutations associated with non-expression. |journal=Thromb. Haemost. |volume=67 |issue= 5 |pages= 521-5 |year= 1992 |pmid= 1325679 |doi= }}
*{{cite journal | author=White D, Abraham G, Carter C, ''et al.'' |title=A novel missense mutation in the antithrombin III gene (Ala387-->Val) causing recurrent venous thrombosis. |journal=Hum. Genet. |volume=90 |issue= 4 |pages= 472-3 |year= 1993 |pmid= 1483709 |doi= }}
*{{cite journal | author=Blajchman MA, Fernandez-Rachubinski F, Sheffield WP, ''et al.'' |title=Antithrombin-III-Stockholm: a codon 392 (Gly----Asp) mutation with normal heparin binding and impaired serine protease reactivity. |journal=Blood |volume=79 |issue= 6 |pages= 1428-34 |year= 1992 |pmid= 1547341 |doi= }}
*{{cite journal | author=Grundy CB, Holding S, Millar DS, ''et al.'' |title=A novel missense mutation in the antithrombin III gene (Ser349----Pro) causing recurrent venous thrombosis. |journal=Hum. Genet. |volume=88 |issue= 6 |pages= 707-8 |year= 1992 |pmid= 1551681 |doi= }}
*{{cite journal | author=Olds RJ, Lane DA, Boisclair M, ''et al.'' |title=Antithrombin Budapest 3. An antithrombin variant with reduced heparin affinity resulting from the substitution L99F. |journal=FEBS Lett. |volume=300 |issue= 3 |pages= 241-6 |year= 1992 |pmid= 1555650 |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=Olds RJ, Lane DA, Ireland H, ''et al.'' |title=A common point mutation producing type 1A antithrombin III deficiency: AT129 CGA to TGA (Arg to Stop). |journal=Thromb. Res. |volume=64 |issue= 5 |pages= 621-5 |year= 1992 |pmid= 1808766 |doi= }}
*{{cite journal | author=Grundy CB, Thomas F, Millar DS, ''et al.'' |title=Recurrent deletion in the human antithrombin III gene. |journal=Blood |volume=78 |issue= 4 |pages= 1027-32 |year= 1991 |pmid= 1868237 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TNFRSF11B... {November 12, 2007 5:55:05 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 5:56:04 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Tumor necrosis factor receptor superfamily, member 11b (osteoprotegerin)
| HGNCid = 11909
| Symbol = TNFRSF11B
| AltSymbols =; OCIF; OPG; MGC29565; TR1
| OMIM = 602643
| ECnumber =
| Homologene = 1912
| MGIid = 109587
| GeneAtlas_image1 = PBB_GE_TNFRSF11B_204932_at_tn.png
| GeneAtlas_image2 = PBB_GE_TNFRSF11B_204933_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}}
| Process = {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0042489 |text = negative regulation of odontogenesis (sensu Vertebrata)}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4982
| Hs_Ensembl = ENSG00000164761
| Hs_RefseqProtein = NP_002537
| Hs_RefseqmRNA = NM_002546
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 120004978
| Hs_GenLoc_end = 120033492
| Hs_Uniprot = O00300
| Mm_EntrezGene = 18383
| Mm_Ensembl = ENSMUSG00000063727
| Mm_RefseqmRNA = NM_008764
| Mm_RefseqProtein = NP_032790
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 54080702
| Mm_GenLoc_end = 54108567
| Mm_Uniprot = Q3UK97
}}
}}
'''Tumor necrosis factor receptor superfamily, member 11b (osteoprotegerin)''', also known as '''TNFRSF11B''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the TNF-receptor superfamily. This protein is an osteoblast-secreted decoy receptor that functions as a negative regulator of bone resorption. This protein specifically binds to its ligand, osteoprotegerin ligand (TNFSF11/OPGL), both of which are key extracellular regulators of osteoclast development. Studies of the mouse counterpart also suggest this protein and its ligand play a role in lymph-node organogenesis and vascular calcification. Alternatively spliced transcript variants of this gene have been reported, but their full length nature has not been determined.<ref>{{cite web | title = Entrez Gene: TNFRSF11B tumor necrosis factor receptor superfamily, member 11b (osteoprotegerin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4982| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hofbauer LC, Neubauer A, Heufelder AE |title=Receptor activator of nuclear factor-kappaB ligand and osteoprotegerin: potential implications for the pathogenesis and treatment of malignant bone diseases. |journal=Cancer |volume=92 |issue= 3 |pages= 460-70 |year= 2001 |pmid= 11505389 |doi= }}
*{{cite journal | author=Buckley KA, Fraser WD |title=Receptor activator for nuclear factor kappaB ligand and osteoprotegerin: regulators of bone physiology and immune responses/potential therapeutic agents and biochemical markers. |journal=Ann. Clin. Biochem. |volume=39 |issue= Pt 6 |pages= 551-6 |year= 2003 |pmid= 12564836 |doi= }}
*{{cite journal | author=Kimberley FC, Screaton GR |title=Following a TRAIL: update on a ligand and its five receptors. |journal=Cell Res. |volume=14 |issue= 5 |pages= 359-72 |year= 2005 |pmid= 15538968 |doi= 10.1038/sj.cr.7290236 }}
*{{cite journal | author=Collin-Osdoby P |title=Regulation of vascular calcification by osteoclast regulatory factors RANKL and osteoprotegerin. |journal=Circ. Res. |volume=95 |issue= 11 |pages= 1046-57 |year= 2005 |pmid= 15564564 |doi= 10.1161/01.RES.0000149165.99974.12 }}
*{{cite journal | author=Whyte MP, Mumm S |title=Heritable disorders of the RANKL/OPG/RANK signaling pathway. |journal=Journal of musculoskeletal & neuronal interactions |volume=4 |issue= 3 |pages= 254-67 |year= 2005 |pmid= 15615493 |doi= }}
*{{cite journal | author=Anandarajah AP, Schwarz EM |title=Anti-RANKL therapy for inflammatory bone disorders: Mechanisms and potential clinical applications. |journal=J. Cell. Biochem. |volume=97 |issue= 2 |pages= 226-32 |year= 2006 |pmid= 16240334 |doi= 10.1002/jcb.20674 }}
*{{cite journal | author=Baud'huin M, Duplomb L, Ruiz Velasco C, ''et al.'' |title=Key roles of the OPG-RANK-RANKL system in bone oncology. |journal=Expert Rev Anticancer Ther |volume=7 |issue= 2 |pages= 221-32 |year= 2007 |pmid= 17288531 |doi= 10.1586/14737140.7.2.221 }}
*{{cite journal | author=Boyce BF, Xing L |title=Biology of RANK, RANKL, and osteoprotegerin. |journal=Arthritis Res. Ther. |volume=9 Suppl 1 |issue= |pages= S1 |year= 2007 |pmid= 17634140 |doi= 10.1186/ar2165 }}
*{{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=Simonet WS, Lacey DL, Dunstan CR, ''et al.'' |title=Osteoprotegerin: a novel secreted protein involved in the regulation of bone density. |journal=Cell |volume=89 |issue= 2 |pages= 309-19 |year= 1997 |pmid= 9108485 |doi= }}
*{{cite journal | author=Tsuda E, Goto M, Mochizuki S, ''et al.'' |title=Isolation of a novel cytokine from human fibroblasts that specifically inhibits osteoclastogenesis. |journal=Biochem. Biophys. Res. Commun. |volume=234 |issue= 1 |pages= 137-42 |year= 1997 |pmid= 9168977 |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=Tan KB, Harrop J, Reddy M, ''et al.'' |title=Characterization of a novel TNF-like ligand and recently described TNF ligand and TNF receptor superfamily genes and their constitutive and inducible expression in hematopoietic and non-hematopoietic cells. |journal=Gene |volume=204 |issue= 1-2 |pages= 35-46 |year= 1998 |pmid= 9434163 |doi= }}
*{{cite journal | author=Yamaguchi K, Kinosaki M, Goto M, ''et al.'' |title=Characterization of structural domains of human osteoclastogenesis inhibitory factor. |journal=J. Biol. Chem. |volume=273 |issue= 9 |pages= 5117-23 |year= 1998 |pmid= 9478964 |doi= }}
*{{cite journal | author=Yasuda H, Shima N, Nakagawa N, ''et al.'' |title=Identity of osteoclastogenesis inhibitory factor (OCIF) and osteoprotegerin (OPG): a mechanism by which OPG/OCIF inhibits osteoclastogenesis in vitro. |journal=Endocrinology |volume=139 |issue= 3 |pages= 1329-37 |year= 1998 |pmid= 9492069 |doi= }}
*{{cite journal | author=Yasuda H, Shima N, Nakagawa N, ''et al.'' |title=Osteoclast differentiation factor is a ligand for osteoprotegerin/osteoclastogenesis-inhibitory factor and is identical to TRANCE/RANKL. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 7 |pages= 3597-602 |year= 1998 |pmid= 9520411 |doi= }}
*{{cite journal | author=Tomoyasu A, Goto M, Fujise N, ''et al.'' |title=Characterization of monomeric and homodimeric forms of osteoclastogenesis inhibitory factor. |journal=Biochem. Biophys. Res. Commun. |volume=245 |issue= 2 |pages= 382-7 |year= 1998 |pmid= 9571159 |doi= }}
*{{cite journal | author=Bucay N, Sarosi I, Dunstan CR, ''et al.'' |title=osteoprotegerin-deficient mice develop early onset osteoporosis and arterial calcification. |journal=Genes Dev. |volume=12 |issue= 9 |pages= 1260-8 |year= 1998 |pmid= 9573043 |doi= }}
*{{cite journal | author=Emery JG, McDonnell P, Burke MB, ''et al.'' |title=Osteoprotegerin is a receptor for the cytotoxic ligand TRAIL. |journal=J. Biol. Chem. |volume=273 |issue= 23 |pages= 14363-7 |year= 1998 |pmid= 9603945 |doi= }}
*{{cite journal | author=Morinaga T, Nakagawa N, Yasuda H, ''et al.'' |title=Cloning and characterization of the gene encoding human osteoprotegerin/osteoclastogenesis-inhibitory factor. |journal=Eur. J. Biochem. |volume=254 |issue= 3 |pages= 685-91 |year= 1998 |pmid= 9688283 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on UBE2I... {November 12, 2007 5:58:54 PM PST}
- SEARCH REDIRECT: Control Box Found: UBE2I {November 12, 2007 5:59:20 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 12, 2007 5:59:21 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 12, 2007 5:59:21 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 12, 2007 5:59:21 PM PST}
- UPDATED: Updated protein page: UBE2I {November 12, 2007 5:59:28 PM PST}
- INFO: Beginning work on VAV1... {November 12, 2007 5:59:28 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 6:00:53 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_VAV1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1k1z.
| PDB = {{PDB2|1k1z}}
| Name = Vav 1 oncogene
| HGNCid = 12657
| Symbol = VAV1
| AltSymbols =; VAV
| OMIM = 164875
| ECnumber =
| Homologene = 3961
| MGIid = 98923
| GeneAtlas_image1 = PBB_GE_VAV1_206219_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005085 |text = guanyl-nucleotide exchange factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0019992 |text = diacylglycerol binding}} {{GNF_GO|id=GO:0030676 |text = Rac guanyl-nucleotide exchange factor activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006909 |text = phagocytosis}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0035023 |text = regulation of Rho protein signal transduction}} {{GNF_GO|id=GO:0042110 |text = T cell activation}} {{GNF_GO|id=GO:0043087 |text = regulation of GTPase activity}} {{GNF_GO|id=GO:0045785 |text = positive regulation of cell adhesion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7409
| Hs_Ensembl = ENSG00000141968
| Hs_RefseqProtein = NP_005419
| Hs_RefseqmRNA = NM_005428
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 6723722
| Hs_GenLoc_end = 6808371
| Hs_Uniprot = P15498
| Mm_EntrezGene = 22324
| Mm_Ensembl = ENSMUSG00000034116
| Mm_RefseqmRNA = XM_980038
| Mm_RefseqProtein = XP_985132
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 56964450
| Mm_GenLoc_end = 57013288
| Mm_Uniprot = Q3TXC4
}}
}}
'''Vav 1 oncogene''', also known as '''VAV1''', is a human [[gene]].
<!-- 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 proto-oncogene is a member of the Dbl family of guanine nucleotide exchange factors (GEF) for the Rho family of GTP binding proteins. The protein is important in hematopoiesis, playing a role in T-cell and B-cell development and activation. This particular GEF has been identified as the specific binding partner of Nef proteins from HIV-1. Coexpression and binding of these partners initiates profound morphological changes, cytoskeletal rearrangements and the JNK/SAPK signaling cascade, leading to increased levels of viral transcription and replication.<ref>{{cite web | title = Entrez Gene: VAV1 vav 1 oncogene| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7409| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Romero F, Fischer S |title=Structure and function of vav. |journal=Cell. Signal. |volume=8 |issue= 8 |pages= 545-53 |year= 1997 |pmid= 9115846 |doi= }}
*{{cite journal | author=Bustelo XR |title=Regulatory and signaling properties of the Vav family. |journal=Mol. Cell. Biol. |volume=20 |issue= 5 |pages= 1461-77 |year= 2000 |pmid= 10669724 |doi= }}
*{{cite journal | author=Geyer M, Fackler OT, Peterlin BM |title=Structure--function relationships in HIV-1 Nef. |journal=EMBO Rep. |volume=2 |issue= 7 |pages= 580-5 |year= 2001 |pmid= 11463741 |doi= 10.1093/embo-reports/kve141 }}
*{{cite journal | author=Greenway AL, Holloway G, McPhee DA, ''et al.'' |title=HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication. |journal=J. Biosci. |volume=28 |issue= 3 |pages= 323-35 |year= 2004 |pmid= 12734410 |doi= }}
*{{cite journal | author=Anderson JL, Hope TJ |title=HIV accessory proteins and surviving the host cell. |journal=Current HIV/AIDS reports |volume=1 |issue= 1 |pages= 47-53 |year= 2005 |pmid= 16091223 |doi= }}
*{{cite journal | author=Stove V, Verhasselt B |title=Modelling thymic HIV-1 Nef effects. |journal=Curr. HIV Res. |volume=4 |issue= 1 |pages= 57-64 |year= 2006 |pmid= 16454711 |doi= }}
*{{cite journal | author=Katzav S |title=Flesh and blood: the story of Vav1, a gene that signals in hematopoietic cells but can be transforming in human malignancies. |journal=Cancer Lett. |volume=255 |issue= 2 |pages= 241-54 |year= 2007 |pmid= 17590270 |doi= 10.1016/j.canlet.2007.04.015 }}
*{{cite journal | author=Bustelo XR, Barbacid M |title=Tyrosine phosphorylation of the vav proto-oncogene product in activated B cells. |journal=Science |volume=256 |issue= 5060 |pages= 1196-9 |year= 1992 |pmid= 1375396 |doi= }}
*{{cite journal | author=Adams JM, Houston H, Allen J, ''et al.'' |title=The hematopoietically expressed vav proto-oncogene shares homology with the dbl GDP-GTP exchange factor, the bcr gene and a yeast gene (CDC24) involved in cytoskeletal organization. |journal=Oncogene |volume=7 |issue= 4 |pages= 611-8 |year= 1992 |pmid= 1565462 |doi= }}
*{{cite journal | author=Katzav S, Cleveland JL, Heslop HE, Pulido D |title=Loss of the amino-terminal helix-loop-helix domain of the vav proto-oncogene activates its transforming potential. |journal=Mol. Cell. Biol. |volume=11 |issue= 4 |pages= 1912-20 |year= 1991 |pmid= 2005887 |doi= }}
*{{cite journal | author=Coppola J, Bryant S, Koda T, ''et al.'' |title=Mechanism of activation of the vav protooncogene. |journal=Cell Growth Differ. |volume=2 |issue= 2 |pages= 95-105 |year= 1991 |pmid= 2069873 |doi= }}
*{{cite journal | author=Katzav S, Martin-Zanca D, Barbacid M |title=vav, a novel human oncogene derived from a locus ubiquitously expressed in hematopoietic cells. |journal=EMBO J. |volume=8 |issue= 8 |pages= 2283-90 |year= 1989 |pmid= 2477241 |doi= }}
*{{cite journal | author=Ramos-Morales F, Romero F, Schweighoffer F, ''et al.'' |title=The proline-rich region of Vav binds to Grb2 and Grb3-3. |journal=Oncogene |volume=11 |issue= 8 |pages= 1665-9 |year= 1995 |pmid= 7478592 |doi= }}
*{{cite journal | author=Weng WK, Jarvis L, LeBien TW |title=Signaling through CD19 activates Vav/mitogen-activated protein kinase pathway and induces formation of a CD19/Vav/phosphatidylinositol 3-kinase complex in human B cell precursors. |journal=J. Biol. Chem. |volume=269 |issue= 51 |pages= 32514-21 |year= 1995 |pmid= 7528218 |doi= }}
*{{cite journal | author=Matsuguchi T, Inhorn RC, Carlesso N, ''et al.'' |title=Tyrosine phosphorylation of p95Vav in myeloid cells is regulated by GM-CSF, IL-3 and steel factor and is constitutively increased by p210BCR/ABL. |journal=EMBO J. |volume=14 |issue= 2 |pages= 257-65 |year= 1995 |pmid= 7530656 |doi= }}
*{{cite journal | author=Uddin S, Katzav S, White MF, Platanias LC |title=Insulin-dependent tyrosine phosphorylation of the vav protooncogene product in cells of hematopoietic origin. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7712-6 |year= 1995 |pmid= 7535775 |doi= }}
*{{cite journal | author=Machide M, Mano H, Todokoro K |title=Interleukin 3 and erythropoietin induce association of Vav with Tec kinase through Tec homology domain. |journal=Oncogene |volume=11 |issue= 4 |pages= 619-25 |year= 1995 |pmid= 7651724 |doi= }}
*{{cite journal | author=Clevenger CV, Ngo W, Sokol DL, ''et al.'' |title=Vav is necessary for prolactin-stimulated proliferation and is translocated into the nucleus of a T-cell line. |journal=J. Biol. Chem. |volume=270 |issue= 22 |pages= 13246-53 |year= 1995 |pmid= 7768923 |doi= }}
*{{cite journal | author=Katzav S, Sutherland M, Packham G, ''et al.'' |title=The protein tyrosine kinase ZAP-70 can associate with the SH2 domain of proto-Vav. |journal=J. Biol. Chem. |volume=269 |issue= 51 |pages= 32579-85 |year= 1995 |pmid= 7798261 |doi= }}
*{{cite journal | author=Ye ZS, Baltimore D |title=Binding of Vav to Grb2 through dimerization of Src homology 3 domains. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 26 |pages= 12629-33 |year= 1995 |pmid= 7809090 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on XRCC1... {November 12, 2007 6:00:53 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 6:01:33 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_XRCC1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cdz.
| PDB = {{PDB2|1cdz}}, {{PDB2|1xna}}, {{PDB2|1xnt}}, {{PDB2|2d8m}}
| Name = X-ray repair complementing defective repair in Chinese hamster cells 1
| HGNCid = 12828
| Symbol = XRCC1
| AltSymbols =; RCC
| OMIM = 194360
| ECnumber =
| Homologene = 31368
| MGIid = 99137
| GeneAtlas_image1 = PBB_GE_XRCC1_203655_at_tn.png
| Function = {{GNF_GO|id=GO:0003684 |text = damaged DNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0000012 |text = single strand break repair}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7515
| Hs_Ensembl = ENSG00000073050
| Hs_RefseqProtein = NP_006288
| Hs_RefseqmRNA = NM_006297
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 48739032
| Hs_GenLoc_end = 48771998
| Hs_Uniprot = P18887
| Mm_EntrezGene = 22594
| Mm_Ensembl = ENSMUSG00000051768
| Mm_RefseqmRNA = NM_009532
| Mm_RefseqProtein = NP_033558
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 24255049
| Mm_GenLoc_end = 24282200
| Mm_Uniprot = Q3TGI0
}}
}}
'''X-ray repair complementing defective repair in Chinese hamster cells 1''', also known as '''XRCC1''', is a human [[gene]].
<!-- 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 involved in the efficient repair of DNA single-strand breaks formed by exposure to ionizing radiation and alkylating agents. This protein interacts with DNA ligase III, polymerase beta and poly (ADP-ribose) polymerase to participate in the base excision repair pathway. It may play a role in DNA processing during meiogenesis and recombination in germ cells. A rare microsatellite polymorphism in this gene is associated with cancer in patients of varying radiosensitivity.<ref>{{cite web | title = Entrez Gene: XRCC1 X-ray repair complementing defective repair in Chinese hamster cells 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7515| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hung RJ, Hall J, Brennan P, Boffetta P |title=Genetic polymorphisms in the base excision repair pathway and cancer risk: a HuGE review. |journal=Am. J. Epidemiol. |volume=162 |issue= 10 |pages= 925-42 |year= 2006 |pmid= 16221808 |doi= 10.1093/aje/kwi318 }}
*{{cite journal | author=Thompson LH, Brookman KW, Jones NJ, ''et al.'' |title=Molecular cloning of the human XRCC1 gene, which corrects defective DNA strand break repair and sister chromatid exchange. |journal=Mol. Cell. Biol. |volume=10 |issue= 12 |pages= 6160-71 |year= 1991 |pmid= 2247054 |doi= }}
*{{cite journal | author=Thompson LH, Bachinski LL, Stallings RL, ''et al.'' |title=Complementation of repair gene mutations on the hemizygous chromosome 9 in CHO: a third repair gene on human chromosome 19. |journal=Genomics |volume=5 |issue= 4 |pages= 670-9 |year= 1990 |pmid= 2591959 |doi= }}
*{{cite journal | author=Gyapay G, Morissette J, Vignal A, ''et al.'' |title=The 1993-94 Généthon human genetic linkage map. |journal=Nat. Genet. |volume=7 |issue= 2 Spec No |pages= 246-339 |year= 1994 |pmid= 7545953 |doi= 10.1038/ng0694supp-246 }}
*{{cite journal | author=Wei Q, Xu X, Cheng L, ''et al.'' |title=Simultaneous amplification of four DNA repair genes and beta-actin in human lymphocytes by multiplex reverse transcriptase-PCR. |journal=Cancer Res. |volume=55 |issue= 21 |pages= 5025-9 |year= 1995 |pmid= 7585546 |doi= }}
*{{cite journal | author=Lamerdin JE, Montgomery MA, Stilwagen SA, ''et al.'' |title=Genomic sequence comparison of the human and mouse XRCC1 DNA repair gene regions. |journal=Genomics |volume=25 |issue= 2 |pages= 547-54 |year= 1995 |pmid= 7789989 |doi= }}
*{{cite journal | author=Caldecott KW, McKeown CK, Tucker JD, ''et al.'' |title=An interaction between the mammalian DNA repair protein XRCC1 and DNA ligase III. |journal=Mol. Cell. Biol. |volume=14 |issue= 1 |pages= 68-76 |year= 1994 |pmid= 8264637 |doi= }}
*{{cite journal | author=Trask B, Fertitta A, Christensen M, ''et al.'' |title=Fluorescence in situ hybridization mapping of human chromosome 19: cytogenetic band location of 540 cosmids and 70 genes or DNA markers. |journal=Genomics |volume=15 |issue= 1 |pages= 133-45 |year= 1993 |pmid= 8432525 |doi= }}
*{{cite journal | author=Kubota Y, Nash RA, Klungland A, ''et al.'' |title=Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein. |journal=EMBO J. |volume=15 |issue= 23 |pages= 6662-70 |year= 1997 |pmid= 8978692 |doi= }}
*{{cite journal | author=Nash RA, Caldecott KW, Barnes DE, Lindahl T |title=XRCC1 protein interacts with one of two distinct forms of DNA ligase III. |journal=Biochemistry |volume=36 |issue= 17 |pages= 5207-11 |year= 1997 |pmid= 9136882 |doi= 10.1021/bi962281m }}
*{{cite journal | author=Shen MR, Jones IM, Mohrenweiser H |title=Nonconservative amino acid substitution variants exist at polymorphic frequency in DNA repair genes in healthy humans. |journal=Cancer Res. |volume=58 |issue= 4 |pages= 604-8 |year= 1998 |pmid= 9485007 |doi= }}
*{{cite journal | author=Price EA, Bourne SL, Radbourne R, ''et al.'' |title=Rare microsatellite polymorphisms in the DNA repair genes XRCC1, XRCC3 and XRCC5 associated with cancer in patients of varying radiosensitivity. |journal=Somat. Cell Mol. Genet. |volume=23 |issue= 4 |pages= 237-47 |year= 1998 |pmid= 9542526 |doi= }}
*{{cite journal | author=Masson M, Niedergang C, Schreiber V, ''et al.'' |title=XRCC1 is specifically associated with poly(ADP-ribose) polymerase and negatively regulates its activity following DNA damage. |journal=Mol. Cell. Biol. |volume=18 |issue= 6 |pages= 3563-71 |year= 1998 |pmid= 9584196 |doi= }}
*{{cite journal | author=Taylor RM, Wickstead B, Cronin S, Caldecott KW |title=Role of a BRCT domain in the interaction of DNA ligase III-alpha with the DNA repair protein XRCC1. |journal=Curr. Biol. |volume=8 |issue= 15 |pages= 877-80 |year= 1998 |pmid= 9705932 |doi= }}
*{{cite journal | author=Zhou ZQ, Walter CA |title=Cloning and characterization of the promoter of baboon XRCC1, a gene involved in DNA strand-break repair. |journal=Somat. Cell Mol. Genet. |volume=24 |issue= 1 |pages= 23-39 |year= 1998 |pmid= 9776979 |doi= }}
*{{cite journal | author=Taylor RM, Moore DJ, Whitehouse J, ''et al.'' |title=A cell cycle-specific requirement for the XRCC1 BRCT II domain during mammalian DNA strand break repair. |journal=Mol. Cell. Biol. |volume=20 |issue= 2 |pages= 735-40 |year= 2000 |pmid= 10611252 |doi= }}
*{{cite journal | author=Marintchev A, Robertson A, Dimitriadis EK, ''et al.'' |title=Domain specific interaction in the XRCC1-DNA polymerase beta complex. |journal=Nucleic Acids Res. |volume=28 |issue= 10 |pages= 2049-59 |year= 2000 |pmid= 10773072 |doi= }}
*{{cite journal | author=Duell EJ, Wiencke JK, Cheng TJ, ''et al.'' |title=Polymorphisms in the DNA repair genes XRCC1 and ERCC2 and biomarkers of DNA damage in human blood mononuclear cells. |journal=Carcinogenesis |volume=21 |issue= 5 |pages= 965-71 |year= 2000 |pmid= 10783319 |doi= }}
*{{cite journal | author=Whitehouse CJ, Taylor RM, Thistlethwaite A, ''et al.'' |title=XRCC1 stimulates human polynucleotide kinase activity at damaged DNA termini and accelerates DNA single-strand break repair. |journal=Cell |volume=104 |issue= 1 |pages= 107-17 |year= 2001 |pmid= 11163244 |doi= }}
*{{cite journal | author=Dulic A, Bates PA, Zhang X, ''et al.'' |title=BRCT domain interactions in the heterodimeric DNA repair protein XRCC1-DNA ligase III. |journal=Biochemistry |volume=40 |issue= 20 |pages= 5906-13 |year= 2001 |pmid= 11352725 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ZAP70... {November 12, 2007 6:01:33 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 6:02:22 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ZAP70_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1m61.
| PDB = {{PDB2|1m61}}, {{PDB2|1u59}}, {{PDB2|2oq1}}, {{PDB2|2ozo}}
| Name = Zeta-chain (TCR) associated protein kinase 70kDa
| HGNCid = 12858
| Symbol = ZAP70
| AltSymbols =; SRK; STD; TZK; ZAP-70
| OMIM = 176947
| ECnumber =
| Homologene = 839
| MGIid = 99613
| GeneAtlas_image1 = PBB_GE_ZAP70_214032_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:0004713 |text = protein-tyrosine kinase activity}} {{GNF_GO|id=GO:0004715 |text = non-membrane spanning protein tyrosine kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0042101 |text = T cell receptor complex}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007243 |text = protein kinase cascade}} {{GNF_GO|id=GO:0045059 |text = positive thymic T cell selection}} {{GNF_GO|id=GO:0045582 |text = positive regulation of T cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7535
| Hs_Ensembl = ENSG00000115085
| Hs_RefseqProtein = NP_001070
| Hs_RefseqmRNA = NM_001079
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 97696461
| Hs_GenLoc_end = 97722755
| Hs_Uniprot = P43403
| Mm_EntrezGene = 22637
| Mm_Ensembl = ENSMUSG00000026117
| Mm_RefseqmRNA = NM_009539
| Mm_RefseqProtein = NP_033565
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 36706371
| Mm_GenLoc_end = 36727362
| Mm_Uniprot = P97455
}}
}}
'''Zeta-chain (TCR) associated protein kinase 70kDa''', also known as '''ZAP70''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Orchard J, Ibbotson R, Best G, ''et al.'' |title=ZAP-70 in B cell malignancies. |journal=Leuk. Lymphoma |volume=46 |issue= 12 |pages= 1689-98 |year= 2006 |pmid= 16263570 |doi= 10.1080/09638280500260079 }}
*{{cite journal | author=Hamblin AD, Hamblin TJ |title=Functional and prognostic role of ZAP-70 in chronic lymphocytic leukaemia. |journal=Expert Opin. Ther. Targets |volume=9 |issue= 6 |pages= 1165-78 |year= 2006 |pmid= 16300468 |doi= 10.1517/14728222.9.6.1165 }}
*{{cite journal | author=Chan AC, Iwashima M, Turck CW, Weiss A |title=ZAP-70: a 70 kd protein-tyrosine kinase that associates with the TCR zeta chain. |journal=Cell |volume=71 |issue= 4 |pages= 649-62 |year= 1992 |pmid= 1423621 |doi= }}
*{{cite journal | author=Goldman F, Jensen WA, Johnson GL, ''et al.'' |title=gp120 ligation of CD4 induces p56lck activation and TCR desensitization independent of TCR tyrosine phosphorylation. |journal=J. Immunol. |volume=153 |issue= 7 |pages= 2905-17 |year= 1994 |pmid= 7522245 |doi= }}
*{{cite journal | author=Isakov N, Wange RL, Burgess WH, ''et al.'' |title=ZAP-70 binding specificity to T cell receptor tyrosine-based activation motifs: the tandem SH2 domains of ZAP-70 bind distinct tyrosine-based activation motifs with varying affinity. |journal=J. Exp. Med. |volume=181 |issue= 1 |pages= 375-80 |year= 1995 |pmid= 7528772 |doi= }}
*{{cite journal | author=Nel AE, Gupta S, Lee L, ''et al.'' |title=Ligation of the T-cell antigen receptor (TCR) induces association of hSos1, ZAP-70, phospholipase C-gamma 1, and other phosphoproteins with Grb2 and the zeta-chain of the TCR. |journal=J. Biol. Chem. |volume=270 |issue= 31 |pages= 18428-36 |year= 1995 |pmid= 7629168 |doi= }}
*{{cite journal | author=Negishi I, Motoyama N, Nakayama K, ''et al.'' |title=Essential role for ZAP-70 in both positive and negative selection of thymocytes. |journal=Nature |volume=376 |issue= 6539 |pages= 435-8 |year= 1995 |pmid= 7630421 |doi= 10.1038/376435a0 }}
*{{cite journal | author=Mustelin T, Williams S, Tailor P, ''et al.'' |title=Regulation of the p70zap tyrosine protein kinase in T cells by the CD45 phosphotyrosine phosphatase. |journal=Eur. J. Immunol. |volume=25 |issue= 4 |pages= 942-6 |year= 1995 |pmid= 7737297 |doi= }}
*{{cite journal | author=Neumeister EN, Zhu Y, Richard S, ''et al.'' |title=Binding of ZAP-70 to phosphorylated T-cell receptor zeta and eta enhances its autophosphorylation and generates specific binding sites for SH2 domain-containing proteins. |journal=Mol. Cell. Biol. |volume=15 |issue= 6 |pages= 3171-8 |year= 1995 |pmid= 7760813 |doi= }}
*{{cite journal | author=Katzav S, Sutherland M, Packham G, ''et al.'' |title=The protein tyrosine kinase ZAP-70 can associate with the SH2 domain of proto-Vav. |journal=J. Biol. Chem. |volume=269 |issue= 51 |pages= 32579-85 |year= 1995 |pmid= 7798261 |doi= }}
*{{cite journal | author=Schumann G, Dasgupta JD |title=Specificity of signal transduction through CD16, TCR-CD3 and BCR receptor chains containing the tyrosine-associated activation motif. |journal=Int. Immunol. |volume=6 |issue= 9 |pages= 1383-92 |year= 1995 |pmid= 7819147 |doi= }}
*{{cite journal | author=Watts JD, Affolter M, Krebs DL, ''et al.'' |title=Identification by electrospray ionization mass spectrometry of the sites of tyrosine phosphorylation induced in activated Jurkat T cells on the protein tyrosine kinase ZAP-70. |journal=J. Biol. Chem. |volume=269 |issue= 47 |pages= 29520-9 |year= 1994 |pmid= 7961936 |doi= }}
*{{cite journal | author=Ku G, Malissen B, Mattei MG |title=Chromosomal location of the Syk and ZAP-70 tyrosine kinase genes in mice and humans. |journal=Immunogenetics |volume=40 |issue= 4 |pages= 300-2 |year= 1994 |pmid= 8082894 |doi= }}
*{{cite journal | author=Chan AC, van Oers NS, Tran A, ''et al.'' |title=Differential expression of ZAP-70 and Syk protein tyrosine kinases, and the role of this family of protein tyrosine kinases in TCR signaling. |journal=J. Immunol. |volume=152 |issue= 10 |pages= 4758-66 |year= 1994 |pmid= 8176201 |doi= }}
*{{cite journal | author=Elder ME, Lin D, Clever J, ''et al.'' |title=Human severe combined immunodeficiency due to a defect in ZAP-70, a T cell tyrosine kinase. |journal=Science |volume=264 |issue= 5165 |pages= 1596-9 |year= 1994 |pmid= 8202712 |doi= }}
*{{cite journal | author=Chan AC, Kadlecek TA, Elder ME, ''et al.'' |title=ZAP-70 deficiency in an autosomal recessive form of severe combined immunodeficiency. |journal=Science |volume=264 |issue= 5165 |pages= 1599-601 |year= 1994 |pmid= 8202713 |doi= }}
*{{cite journal | author=Wange RL, Malek SN, Desiderio S, Samelson LE |title=Tandem SH2 domains of ZAP-70 bind to T cell antigen receptor zeta and CD3 epsilon from activated Jurkat T cells. |journal=J. Biol. Chem. |volume=268 |issue= 26 |pages= 19797-801 |year= 1993 |pmid= 8366117 |doi= }}
*{{cite journal | author=Huby RD, Carlile GW, Ley SC |title=Interactions between the protein-tyrosine kinase ZAP-70, the proto-oncoprotein Vav, and tubulin in Jurkat T cells. |journal=J. Biol. Chem. |volume=270 |issue= 51 |pages= 30241-4 |year= 1996 |pmid= 8530437 |doi= }}
*{{cite journal | author=Plas DR, Johnson R, Pingel JT, ''et al.'' |title=Direct regulation of ZAP-70 by SHP-1 in T cell antigen receptor signaling. |journal=Science |volume=272 |issue= 5265 |pages= 1173-6 |year= 1996 |pmid= 8638162 |doi= }}
*{{cite journal | author=Wardenburg JB, Fu C, Jackman JK, ''et al.'' |title=Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function. |journal=J. Biol. Chem. |volume=271 |issue= 33 |pages= 19641-4 |year= 1996 |pmid= 8702662 |doi= }}
}}
{{refend}}
{{protein-stub}}
end log.
