- INFO: Beginning work on ACTG1... {November 12, 2007 7:24:54 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:26:20 PM PST}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ACTG1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1atn.
| PDB = {{PDB2|1atn}}, {{PDB2|1c0f}}, {{PDB2|1c0g}}, {{PDB2|1d4x}}, {{PDB2|1dej}}, {{PDB2|1eqy}}, {{PDB2|1esv}}, {{PDB2|1h1v}}, {{PDB2|1hlu}}, {{PDB2|1ijj}}, {{PDB2|1j6z}}, {{PDB2|1kxp}}, {{PDB2|1lcu}}, {{PDB2|1lot}}, {{PDB2|1m8q}}, {{PDB2|1ma9}}, {{PDB2|1mdu}}, {{PDB2|1mvw}}, {{PDB2|1nlv}}, {{PDB2|1nm1}}, {{PDB2|1nmd}}, {{PDB2|1nwk}}, {{PDB2|1o18}}, {{PDB2|1o19}}, {{PDB2|1o1a}}, {{PDB2|1o1b}}, {{PDB2|1o1c}}, {{PDB2|1o1d}}, {{PDB2|1o1e}}, {{PDB2|1o1f}}, {{PDB2|1o1g}}, {{PDB2|1p8z}}, {{PDB2|1qz5}}, {{PDB2|1qz6}}, {{PDB2|1rdw}}, {{PDB2|1rfq}}, {{PDB2|1rgi}}, {{PDB2|1s22}}, {{PDB2|1sqk}}, {{PDB2|1t44}}, {{PDB2|1wua}}, {{PDB2|1y64}}, {{PDB2|1yxq}}, {{PDB2|2a3z}}, {{PDB2|2a40}}, {{PDB2|2a41}}, {{PDB2|2a42}}, {{PDB2|2a5x}}, {{PDB2|2asm}}, {{PDB2|2aso}}, {{PDB2|2asp}}, {{PDB2|2btf}}, {{PDB2|2d1k}}, {{PDB2|2ff3}}, {{PDB2|2ff6}}, {{PDB2|2fxu}}, {{PDB2|2gwj}}, {{PDB2|2gwk}}, {{PDB2|2hf3}}, {{PDB2|2hf4}}, {{PDB2|2hmp}}, {{PDB2|2oan}}, {{PDB2|2q1n}}, {{PDB2|2q31}}, {{PDB2|2q36}}
| Name = Actin, gamma 1
| HGNCid = 144
| Symbol = ACTG1
| AltSymbols =; ACT; ACTG; DFNA20; DFNA26
| OMIM = 102560
| ECnumber =
| Homologene = 74402
| MGIid = 87906
| GeneAtlas_image1 = PBB_GE_ACTG1_211983_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_ACTG1_201550_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_ACTG1_211970_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}}
| Component = {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}} {{GNF_GO|id=GO:0030016 |text = myofibril}}
| Process = {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0045214 |text = sarcomere organization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 71
| Hs_Ensembl = ENSG00000184009
| Hs_RefseqProtein = NP_001605
| Hs_RefseqmRNA = NM_001614
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 77091594
| Hs_GenLoc_end = 77094422
| Hs_Uniprot = P63261
| Mm_EntrezGene = 11465
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_001052054
| Mm_RefseqProtein = XP_001052054
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Actin, gamma 1''', also known as '''ACTG1''', 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 = Actins are highly conserved proteins that are involved in various types of cell motility, and maintenance of the cytoskeleton. In vertebrates, three main groups of actin isoforms, alpha, beta and gamma have been identified. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins co-exist in most cell types as components of the cytoskeleton, and as mediators of internal cell motility. Actin, gamma 1, encoded by this gene, is a cytoplasmic actin found in nonmuscle cells.<ref>{{cite web | title = Entrez Gene: ACTG1 actin, gamma 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=71| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Snásel J, Pichová I |title=The cleavage of host cell proteins by HIV-1 protease. |journal=Folia Biol. (Praha) |volume=42 |issue= 5 |pages= 227-30 |year= 1997 |pmid= 8997639 |doi= }}
*{{cite journal | author=Rodríguez Del Castillo A, Vitale ML, Trifaró JM |title=Ca2+ and pH determine the interaction of chromaffin cell scinderin with phosphatidylserine and phosphatidylinositol 4,5,-biphosphate and its cellular distribution during nicotinic-receptor stimulation and protein kinase C activation. |journal=J. Cell Biol. |volume=119 |issue= 4 |pages= 797-810 |year= 1992 |pmid= 1331119 |doi= }}
*{{cite journal | author=Adams LD, Tomasselli AG, Robbins P, ''et al.'' |title=HIV-1 protease cleaves actin during acute infection of human T-lymphocytes. |journal=AIDS Res. Hum. Retroviruses |volume=8 |issue= 2 |pages= 291-5 |year= 1992 |pmid= 1540415 |doi= }}
*{{cite journal | author=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=Tomasselli AG, Hui JO, Adams L, ''et al.'' |title=Actin, troponin C, Alzheimer amyloid precursor protein and pro-interleukin 1 beta as substrates of the protease from human immunodeficiency virus. |journal=J. Biol. Chem. |volume=266 |issue= 22 |pages= 14548-53 |year= 1991 |pmid= 1907279 |doi= }}
*{{cite journal | author=Shoeman RL, Kesselmier C, Mothes E, ''et al.'' |title=Non-viral cellular substrates for human immunodeficiency virus type 1 protease. |journal=FEBS Lett. |volume=278 |issue= 2 |pages= 199-203 |year= 1991 |pmid= 1991513 |doi= }}
*{{cite journal | author=Erba HP, Eddy R, Shows T, ''et al.'' |title=Structure, chromosome location, and expression of the human gamma-actin gene: differential evolution, location, and expression of the cytoskeletal beta- and gamma-actin genes. |journal=Mol. Cell. Biol. |volume=8 |issue= 4 |pages= 1775-89 |year= 1988 |pmid= 2837653 |doi= }}
*{{cite journal | author=Vandekerckhove J, Schering B, Bärmann M, Aktories K |title=Botulinum C2 toxin ADP-ribosylates cytoplasmic beta/gamma-actin in arginine 177. |journal=J. Biol. Chem. |volume=263 |issue= 2 |pages= 696-700 |year= 1988 |pmid= 3335520 |doi= }}
*{{cite journal | author=Chou CC, Davis RC, Fuller ML, ''et al.'' |title=Gamma-actin: unusual mRNA 3'-untranslated sequence conservation and amino acid substitutions that may be cancer related. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 9 |pages= 2575-9 |year= 1987 |pmid= 3472224 |doi= }}
*{{cite journal | author=Hesterberg LK, Weber K |title=Isolation of a domain of villin retaining calcium-dependent interaction with G-actin, but devoid of F-actin fragmenting activity. |journal=Eur. J. Biochem. |volume=154 |issue= 1 |pages= 135-40 |year= 1986 |pmid= 3510866 |doi= }}
*{{cite journal | author=Erba HP, Gunning P, Kedes L |title=Nucleotide sequence of the human gamma cytoskeletal actin mRNA: anomalous evolution of vertebrate non-muscle actin genes. |journal=Nucleic Acids Res. |volume=14 |issue= 13 |pages= 5275-94 |year= 1986 |pmid= 3737401 |doi= }}
*{{cite journal | author=Fuchs E, Kim KH, Hanukoglu I, Tanese N |title=The evolution and complexity of the genes encoding the cytoskeletal proteins of human epidermal cells. |journal=Curr. Probl. Dermatol. |volume=11 |issue= |pages= 27-44 |year= 1984 |pmid= 6686106 |doi= }}
*{{cite journal | author=Gunning P, Ponte P, Okayama H, ''et al.'' |title=Isolation and characterization of full-length cDNA clones for human alpha-, beta-, and gamma-actin mRNAs: skeletal but not cytoplasmic actins have an amino-terminal cysteine that is subsequently removed. |journal=Mol. Cell. Biol. |volume=3 |issue= 5 |pages= 787-95 |year= 1983 |pmid= 6865942 |doi= }}
*{{cite journal | author=Bretscher A, Weber K |title=Villin is a major protein of the microvillus cytoskeleton which binds both G and F actin in a calcium-dependent manner. |journal=Cell |volume=20 |issue= 3 |pages= 839-47 |year= 1980 |pmid= 6893424 |doi= }}
*{{cite journal | author=Pedrotti B, Colombo R, Islam K |title=Microtubule associated protein MAP1A is an actin-binding and crosslinking protein. |journal=Cell Motil. Cytoskeleton |volume=29 |issue= 2 |pages= 110-6 |year= 1995 |pmid= 7820861 |doi= 10.1002/cm.970290203 }}
*{{cite journal | author=Pope B, Maciver S, Weeds A |title=Localization of the calcium-sensitive actin monomer binding site in gelsolin to segment 4 and identification of calcium binding sites. |journal=Biochemistry |volume=34 |issue= 5 |pages= 1583-8 |year= 1995 |pmid= 7849017 |doi= }}
*{{cite journal | author=Jesaitis AJ, Erickson RW, Klotz KN, ''et al.'' |title=Functional molecular complexes of human N-formyl chemoattractant receptors and actin. |journal=J. Immunol. |volume=151 |issue= 10 |pages= 5653-65 |year= 1993 |pmid= 8228254 |doi= }}
*{{cite journal | author=Hawkins M, Pope B, Maciver SK, Weeds AG |title=Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments. |journal=Biochemistry |volume=32 |issue= 38 |pages= 9985-93 |year= 1993 |pmid= 8399167 |doi= }}
*{{cite journal | author=Yu FX, Lin SC, Morrison-Bogorad M, ''et al.'' |title=Thymosin beta 10 and thymosin beta 4 are both actin monomer sequestering proteins. |journal=J. Biol. Chem. |volume=268 |issue= 1 |pages= 502-9 |year= 1993 |pmid= 8416954 |doi= }}
*{{cite journal | author=Jalaguier S, Mornet D, Mesnier D, ''et al.'' |title=Human mineralocorticoid receptor interacts with actin under mineralocorticoid ligand modulation. |journal=FEBS Lett. |volume=384 |issue= 2 |pages= 112-6 |year= 1996 |pmid= 8612804 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ADRBK1... {November 12, 2007 7:26:21 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:26:56 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_ADRBK1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bak.
| PDB = {{PDB2|1bak}}, {{PDB2|1omw}}, {{PDB2|1ym7}}, {{PDB2|2bcj}}
| Name = Adrenergic, beta, receptor kinase 1
| HGNCid = 289
| Symbol = ADRBK1
| AltSymbols =; BARK1; BETA-ARK1; GRK2
| OMIM = 109635
| ECnumber =
| Homologene = 1223
| MGIid = 87940
| GeneAtlas_image1 = PBB_GE_ADRBK1_38447_at_tn.png
| GeneAtlas_image2 = PBB_GE_ADRBK1_201401_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_ADRBK1_201402_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:0004703 |text = G-protein coupled receptor kinase activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0004872 |text = receptor 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:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0002026 |text = cardiac inotropy}} {{GNF_GO|id=GO:0002029 |text = desensitization of G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{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:0007507 |text = heart development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 156
| Hs_Ensembl = ENSG00000173020
| Hs_RefseqProtein = NP_001610
| Hs_RefseqmRNA = NM_001619
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 66790507
| Hs_GenLoc_end = 66810602
| Hs_Uniprot = P25098
| Mm_EntrezGene = 110355
| Mm_Ensembl = ENSMUSG00000024858
| Mm_RefseqmRNA = NM_130863
| Mm_RefseqProtein = NP_570933
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 4286001
| Mm_GenLoc_end = 4306014
| Mm_Uniprot = Q3U5J8
}}
}}
'''Adrenergic, beta, receptor kinase 1''', also known as '''ADRBK1''', 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 product of this gene phosphorylates the beta-2-adrenergic receptor and appears to mediate agonist-specific desensitization observed at high agonist concentrations. This protein is an ubiquitous cytosolic enzyme that specifically phosphorylates the activated form of the beta-adrenergic and related G-protein-coupled receptors. Abnormal coupling of beta-adrenergic receptor to G protein is involved in the pathogenesis of the failing heart.<ref>{{cite web | title = Entrez Gene: ADRBK1 adrenergic, beta, receptor kinase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=156| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Chuang TT, Sallese M, Ambrosini G, ''et al.'' |title=High expression of beta-adrenergic receptor kinase in human peripheral blood leukocytes. Isoproterenol and platelet activating factor can induce kinase translocation. |journal=J. Biol. Chem. |volume=267 |issue= 10 |pages= 6886-92 |year= 1992 |pmid= 1339451 |doi= }}
*{{cite journal | author=Benovic JL, Stone WC, Huebner K, ''et al.'' |title=cDNA cloning and chromosomal localization of the human beta-adrenergic receptor kinase. |journal=FEBS Lett. |volume=283 |issue= 1 |pages= 122-6 |year= 1991 |pmid= 2037065 |doi= }}
*{{cite journal | author=Prossnitz ER, Kim CM, Benovic JL, Ye RD |title=Phosphorylation of the N-formyl peptide receptor carboxyl terminus by the G protein-coupled receptor kinase, GRK2. |journal=J. Biol. Chem. |volume=270 |issue= 3 |pages= 1130-7 |year= 1995 |pmid= 7836371 |doi= }}
*{{cite journal | author=Eason MG, Moreira SP, Liggett SB |title=Four consecutive serines in the third intracellular loop are the sites for beta-adrenergic receptor kinase-mediated phosphorylation and desensitization of the alpha 2A-adrenergic receptor. |journal=J. Biol. Chem. |volume=270 |issue= 9 |pages= 4681-8 |year= 1995 |pmid= 7876239 |doi= }}
*{{cite journal | author=Penn RB, Benovic JL |title=Structure of the human gene encoding the beta-adrenergic receptor kinase. |journal=J. Biol. Chem. |volume=269 |issue= 21 |pages= 14924-30 |year= 1994 |pmid= 8195124 |doi= }}
*{{cite journal | author=Oppermann M, Freedman NJ, Alexander RW, Lefkowitz RJ |title=Phosphorylation of the type 1A angiotensin II receptor by G protein-coupled receptor kinases and protein kinase C. |journal=J. Biol. Chem. |volume=271 |issue= 22 |pages= 13266-72 |year= 1996 |pmid= 8662816 |doi= }}
*{{cite journal | author=Iacovelli L, Franchetti R, Masini M, De Blasi A |title=GRK2 and beta-arrestin 1 as negative regulators of thyrotropin receptor-stimulated response. |journal=Mol. Endocrinol. |volume=10 |issue= 9 |pages= 1138-46 |year= 1997 |pmid= 8885248 |doi= }}
*{{cite journal | author=Fushman D, Najmabadi-Haske T, Cahill S, ''et al.'' |title=The solution structure and dynamics of the pleckstrin homology domain of G protein-coupled receptor kinase 2 (beta-adrenergic receptor kinase 1). A binding partner of Gbetagamma subunits. |journal=J. Biol. Chem. |volume=273 |issue= 5 |pages= 2835-43 |year= 1998 |pmid= 9446593 |doi= }}
*{{cite journal | author=Aragay AM, Mellado M, Frade JM, ''et al.'' |title=Monocyte chemoattractant protein-1-induced CCR2B receptor desensitization mediated by the G protein-coupled receptor kinase 2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 6 |pages= 2985-90 |year= 1998 |pmid= 9501202 |doi= }}
*{{cite journal | author=Rockman HA, Chien KR, Choi DJ, ''et al.'' |title=Expression of a beta-adrenergic receptor kinase 1 inhibitor prevents the development of myocardial failure in gene-targeted mice. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 12 |pages= 7000-5 |year= 1998 |pmid= 9618528 |doi= }}
*{{cite journal | author=Premont RT, Claing A, Vitale N, ''et al.'' |title=beta2-Adrenergic receptor regulation by GIT1, a G protein-coupled receptor kinase-associated ADP ribosylation factor GTPase-activating protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 24 |pages= 14082-7 |year= 1998 |pmid= 9826657 |doi= }}
*{{cite journal | author=Carman CV, Lisanti MP, Benovic JL |title=Regulation of G protein-coupled receptor kinases by caveolin. |journal=J. Biol. Chem. |volume=274 |issue= 13 |pages= 8858-64 |year= 1999 |pmid= 10085129 |doi= }}
*{{cite journal | author=Oppermann M, Mack M, Proudfoot AE, Olbrich H |title=Differential effects of CC chemokines on CC chemokine receptor 5 (CCR5) phosphorylation and identification of phosphorylation sites on the CCR5 carboxyl terminus. |journal=J. Biol. Chem. |volume=274 |issue= 13 |pages= 8875-85 |year= 1999 |pmid= 10085131 |doi= }}
*{{cite journal | author=Ito K, Haga T, Lameh J, Sadée W |title=Sequestration of dopamine D2 receptors depends on coexpression of G-protein-coupled receptor kinases 2 or 5. |journal=Eur. J. Biochem. |volume=260 |issue= 1 |pages= 112-9 |year= 1999 |pmid= 10091590 |doi= }}
*{{cite journal | author=Lazari MF, Liu X, Nakamura K, ''et al.'' |title=Role of G protein-coupled receptor kinases on the agonist-induced phosphorylation and internalization of the follitropin receptor. |journal=Mol. Endocrinol. |volume=13 |issue= 6 |pages= 866-78 |year= 1999 |pmid= 10379886 |doi= }}
*{{cite journal | author=Brenninkmeijer CB, Price SA, López Bernal A, Phaneuf S |title=Expression of G-protein-coupled receptor kinases in pregnant term and non-pregnant human myometrium. |journal=J. Endocrinol. |volume=162 |issue= 3 |pages= 401-8 |year= 1999 |pmid= 10467231 |doi= }}
*{{cite journal | author=Pitcher JA, Tesmer JJ, Freeman JL, ''et al.'' |title=Feedback inhibition of G protein-coupled receptor kinase 2 (GRK2) activity by extracellular signal-regulated kinases. |journal=J. Biol. Chem. |volume=274 |issue= 49 |pages= 34531-4 |year= 2000 |pmid= 10574913 |doi= }}
*{{cite journal | author=Okochi M, Walter J, Koyama A, ''et al.'' |title=Constitutive phosphorylation of the Parkinson's disease associated alpha-synuclein. |journal=J. Biol. Chem. |volume=275 |issue= 1 |pages= 390-7 |year= 2000 |pmid= 10617630 |doi= }}
*{{cite journal | author=Gan XQ, Wang JY, Yang QH, ''et al.'' |title=Interaction between the conserved region in the C-terminal domain of GRK2 and rhodopsin is necessary for GRK2 to catalyze receptor phosphorylation. |journal=J. Biol. Chem. |volume=275 |issue= 12 |pages= 8469-74 |year= 2000 |pmid= 10722682 |doi= }}
*{{cite journal | author=Elorza A, Sarnago S, Mayor F |title=Agonist-dependent modulation of G protein-coupled receptor kinase 2 by mitogen-activated protein kinases. |journal=Mol. Pharmacol. |volume=57 |issue= 4 |pages= 778-83 |year= 2000 |pmid= 10727525 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ANGPT1... {November 12, 2007 7:26:56 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:27:36 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
| 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 = Angiopoietin 1
| HGNCid = 484
| Symbol = ANGPT1
| AltSymbols =; AGP1; AGPT; ANG1
| OMIM = 601667
| ECnumber =
| Homologene = 37447
| MGIid = 108448
| GeneAtlas_image1 = PBB_GE_ANGPT1_205608_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ANGPT1_205609_at_tn.png
| Function = {{GNF_GO|id=GO:0005102 |text = receptor binding}}
| Component =
| Process = {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 284
| Hs_Ensembl = ENSG00000154188
| Hs_RefseqProtein = NP_001137
| Hs_RefseqmRNA = NM_001146
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 108330899
| Hs_GenLoc_end = 108579459
| Hs_Uniprot = Q15389
| Mm_EntrezGene = 11600
| Mm_Ensembl = ENSMUSG00000022309
| Mm_RefseqmRNA = NM_009640
| Mm_RefseqProtein = NP_033770
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 42254801
| Mm_GenLoc_end = 42507051
| Mm_Uniprot = Q6A0F0
}}
}}
'''Angiopoietin 1''', also known as '''ANGPT1''', 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 = Angiopoietins are proteins with important roles in vascular development and angiogenesis. All angiopoietins bind with similar affinity to an endothelial cell-specific tyrosine-protein kinase receptor. The protein encoded by this gene is a secreted glycoprotein that activates the receptor by inducing its tyrosine phosphorylation. It plays a critical role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme. The protein also contributes to blood vessel maturation and stability, and may be involved in early development of the heart.<ref>{{cite web | title = Entrez Gene: ANGPT1 angiopoietin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=284| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nakajima D, Okazaki N, Yamakawa H, ''et al.'' |title=Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. |journal=DNA Res. |volume=9 |issue= 3 |pages= 99-106 |year= 2003 |pmid= 12168954 |doi= }}
*{{cite journal | author=Metheny-Barlow LJ, Li LY |title=The enigmatic role of angiopoietin-1 in tumor angiogenesis. |journal=Cell Res. |volume=13 |issue= 5 |pages= 309-17 |year= 2004 |pmid= 14672554 |doi= 10.1038/sj.cr.7290176 }}
*{{cite journal | author=Makinde T, Murphy RF, Agrawal DK |title=Immunomodulatory role of vascular endothelial growth factor and angiopoietin-1 in airway remodeling. |journal=Curr. Mol. Med. |volume=6 |issue= 8 |pages= 831-41 |year= 2007 |pmid= 17168735 |doi= }}
*{{cite journal | author=Nomura N, Miyajima N, Sazuka T, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. |journal=DNA Res. |volume=1 |issue= 1 |pages= 27-35 |year= 1995 |pmid= 7584026 |doi= }}
*{{cite journal | author=Nomura N, Miyajima N, Sazuka T, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1 (supplement). |journal=DNA Res. |volume=1 |issue= 1 |pages= 47-56 |year= 1995 |pmid= 7584028 |doi= }}
*{{cite journal | author=Rüegg C, Pytela R |title=Sequence of a human transcript expressed in T-lymphocytes and encoding a fibrinogen-like protein. |journal=Gene |volume=160 |issue= 2 |pages= 257-62 |year= 1995 |pmid= 7642106 |doi= }}
*{{cite journal | author=Davis S, Aldrich TH, Jones PF, ''et al.'' |title=Isolation of angiopoietin-1, a ligand for the TIE2 receptor, by secretion-trap expression cloning. |journal=Cell |volume=87 |issue= 7 |pages= 1161-9 |year= 1997 |pmid= 8980223 |doi= }}
*{{cite journal | author=Suri C, Jones PF, Patan S, ''et al.'' |title=Requisite role of angiopoietin-1, a ligand for the TIE2 receptor, during embryonic angiogenesis. |journal=Cell |volume=87 |issue= 7 |pages= 1171-80 |year= 1997 |pmid= 8980224 |doi= }}
*{{cite journal | author=Maisonpierre PC, Suri C, Jones PF, ''et al.'' |title=Angiopoietin-2, a natural antagonist for Tie2 that disrupts in vivo angiogenesis. |journal=Science |volume=277 |issue= 5322 |pages= 55-60 |year= 1997 |pmid= 9204896 |doi= }}
*{{cite journal | author=Ristimäki A, Narko K, Enholm B, ''et al.'' |title=Proinflammatory cytokines regulate expression of the lymphatic endothelial mitogen vascular endothelial growth factor-C. |journal=J. Biol. Chem. |volume=273 |issue= 14 |pages= 8413-8 |year= 1998 |pmid= 9525952 |doi= }}
*{{cite journal | author=Cheung AH, Stewart RJ, Marsden PA |title=Endothelial Tie2/Tek ligands angiopoietin-1 (ANGPT1) and angiopoietin-2 (ANGPT2): regional localization of the human genes to 8q22.3-q23 and 8p23. |journal=Genomics |volume=48 |issue= 3 |pages= 389-91 |year= 1998 |pmid= 9545648 |doi= 10.1006/geno.1997.5207 }}
*{{cite journal | author=Witzenbichler B, Maisonpierre PC, Jones P, ''et al.'' |title=Chemotactic properties of angiopoietin-1 and -2, ligands for the endothelial-specific receptor tyrosine kinase Tie2. |journal=J. Biol. Chem. |volume=273 |issue= 29 |pages= 18514-21 |year= 1998 |pmid= 9660821 |doi= }}
*{{cite journal | author=Sato A, Iwama A, Takakura N, ''et al.'' |title=Characterization of TEK receptor tyrosine kinase and its ligands, Angiopoietins, in human hematopoietic progenitor cells. |journal=Int. Immunol. |volume=10 |issue= 8 |pages= 1217-27 |year= 1998 |pmid= 9723709 |doi= }}
*{{cite journal | author=Valenzuela DM, Griffiths JA, Rojas J, ''et al.'' |title=Angiopoietins 3 and 4: diverging gene counterparts in mice and humans. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 5 |pages= 1904-9 |year= 1999 |pmid= 10051567 |doi= }}
*{{cite journal | author=Grosios K, Leek JP, Markham AF, ''et al.'' |title=Assignment of ANGPT4, ANGPT1, and ANGPT2 encoding angiopoietins 4, 1 and 2 to human chromosome bands 20p13, 8q22.3-->q23 and 8p23.1, respectively, by in situ hybridization and radiation hybrid mapping. |journal=Cytogenet. Cell Genet. |volume=84 |issue= 1-2 |pages= 118-20 |year= 1999 |pmid= 10343124 |doi= }}
*{{cite journal | author=Procopio WN, Pelavin PI, Lee WM, Yeilding NM |title=Angiopoietin-1 and -2 coiled coil domains mediate distinct homo-oligomerization patterns, but fibrinogen-like domains mediate ligand activity. |journal=J. Biol. Chem. |volume=274 |issue= 42 |pages= 30196-201 |year= 1999 |pmid= 10514510 |doi= }}
*{{cite journal | author=Huang YQ, Li JJ, Karpatkin S |title=Identification of a family of alternatively spliced mRNA species of angiopoietin-1. |journal=Blood |volume=95 |issue= 6 |pages= 1993-9 |year= 2000 |pmid= 10706866 |doi= }}
*{{cite journal | author=Kim I, Kim JH, Ryu YS, ''et al.'' |title=Characterization and expression of a novel alternatively spliced human angiopoietin-2. |journal=J. Biol. Chem. |volume=275 |issue= 24 |pages= 18550-6 |year= 2000 |pmid= 10766762 |doi= 10.1074/jbc.M910084199 }}
*{{cite journal | author=Dunk C, Shams M, Nijjar S, ''et al.'' |title=Angiopoietin-1 and angiopoietin-2 activate trophoblast Tie-2 to promote growth and migration during placental development. |journal=Am. J. Pathol. |volume=156 |issue= 6 |pages= 2185-99 |year= 2000 |pmid= 10854239 |doi= }}
*{{cite journal | author=Krikun G, Schatz F, Finlay T, ''et al.'' |title=Expression of angiopoietin-2 by human endometrial endothelial cells: regulation by hypoxia and inflammation. |journal=Biochem. Biophys. Res. Commun. |volume=275 |issue= 1 |pages= 159-63 |year= 2000 |pmid= 10944458 |doi= 10.1006/bbrc.2000.3277 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on BCAR1... {November 12, 2007 7:42:47 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:43:30 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_BCAR1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1wyx.
| PDB = {{PDB2|1wyx}}
| Name = Breast cancer anti-estrogen resistance 1
| HGNCid = 971
| Symbol = BCAR1
| AltSymbols =; CAS; CRKAS; P130Cas
| OMIM = 602941
| ECnumber =
| Homologene = 7674
| MGIid = 108091
| GeneAtlas_image1 = PBB_GE_BCAR1_gnf1h00170_at_tn.png
| Function = {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0019901 |text = protein kinase binding}} {{GNF_GO|id=GO:0019903 |text = protein phosphatase binding}}
| Component = {{GNF_GO|id=GO:0001726 |text = ruffle}} {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005925 |text = focal adhesion}}
| Process = {{GNF_GO|id=GO:0001558 |text = regulation of cell growth}} {{GNF_GO|id=GO:0007015 |text = actin filament organization}} {{GNF_GO|id=GO:0007173 |text = epidermal growth factor receptor signaling pathway}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008286 |text = insulin receptor signaling pathway}} {{GNF_GO|id=GO:0016477 |text = cell migration}} {{GNF_GO|id=GO:0030335 |text = positive regulation of cell migration}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}} {{GNF_GO|id=GO:0048008 |text = platelet-derived growth factor receptor signaling pathway}} {{GNF_GO|id=GO:0048011 |text = nerve growth factor receptor signaling pathway}} {{GNF_GO|id=GO:0050852 |text = T cell receptor signaling pathway}} {{GNF_GO|id=GO:0050853 |text = B cell receptor signaling pathway}} {{GNF_GO|id=GO:0051301 |text = cell division}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 9564
| Hs_Ensembl = ENSG00000050820
| Hs_RefseqProtein = NP_055382
| Hs_RefseqmRNA = NM_014567
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 73820430
| Hs_GenLoc_end = 73843004
| Hs_Uniprot = P56945
| Mm_EntrezGene = 12927
| Mm_Ensembl = ENSMUSG00000031955
| Mm_RefseqmRNA = NM_009954
| Mm_RefseqProtein = NP_034084
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 114597147
| Mm_GenLoc_end = 114608054
| Mm_Uniprot = Q3TIT7
}}
}}
'''Breast cancer anti-estrogen resistance 1''', also known as '''BCAR1''', 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=Rozengurt E |title=Signal transduction pathways in the mitogenic response to G protein-coupled neuropeptide receptor agonists. |journal=J. Cell. Physiol. |volume=177 |issue= 4 |pages= 507-17 |year= 1999 |pmid= 10092204 |doi= 10.1002/(SICI)1097-4652(199812)177:4<507::AID-JCP2>3.0.CO;2-K }}
*{{cite journal | author=O'Neill GM, Fashena SJ, Golemis EA |title=Integrin signalling: a new Cas(t) of characters enters the stage. |journal=Trends Cell Biol. |volume=10 |issue= 3 |pages= 111-9 |year= 2000 |pmid= 10675905 |doi= }}
*{{cite journal | author=Bouton AH, Riggins RB, Bruce-Staskal PJ |title=Functions of the adapter protein Cas: signal convergence and the determination of cellular responses. |journal=Oncogene |volume=20 |issue= 44 |pages= 6448-58 |year= 2001 |pmid= 11607844 |doi= 10.1038/sj.onc.1204785 }}
*{{cite journal | author=Panetti TS |title=Tyrosine phosphorylation of paxillin, FAK, and p130CAS: effects on cell spreading and migration. |journal=Front. Biosci. |volume=7 |issue= |pages= d143-50 |year= 2002 |pmid= 11779709 |doi= }}
*{{cite journal | author=Mayer BJ, Hirai H, Sakai R |title=Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases. |journal=Curr. Biol. |volume=5 |issue= 3 |pages= 296-305 |year= 1995 |pmid= 7780740 |doi= }}
*{{cite journal | author=Sakai R, Iwamatsu A, Hirano N, ''et al.'' |title=A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner. |journal=EMBO J. |volume=13 |issue= 16 |pages= 3748-56 |year= 1994 |pmid= 8070403 |doi= }}
*{{cite journal | author=Dorssers LC, van Agthoven T, Dekker A, ''et al.'' |title=Induction of antiestrogen resistance in human breast cancer cells by random insertional mutagenesis using defective retroviruses: identification of bcar-1, a common integration site. |journal=Mol. Endocrinol. |volume=7 |issue= 7 |pages= 870-8 |year= 1993 |pmid= 8413311 |doi= }}
*{{cite journal | author=Vuori K, Hirai H, Aizawa S, Ruoslahti E |title=Introduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: a role for Src family kinases. |journal=Mol. Cell. Biol. |volume=16 |issue= 6 |pages= 2606-13 |year= 1996 |pmid= 8649368 |doi= }}
*{{cite journal | author=Law SF, Estojak J, Wang B, ''et al.'' |title=Human enhancer of filamentation 1, a novel p130cas-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae. |journal=Mol. Cell. Biol. |volume=16 |issue= 7 |pages= 3327-37 |year= 1996 |pmid= 8668148 |doi= }}
*{{cite journal | author=Khwaja A, Hallberg B, Warne PH, Downward J |title=Networks of interaction of p120cbl and p130cas with Crk and Grb2 adaptor proteins. |journal=Oncogene |volume=12 |issue= 12 |pages= 2491-8 |year= 1996 |pmid= 8700507 |doi= }}
*{{cite journal | author=Salgia R, Pisick E, Sattler M, ''et al.'' |title=p130CAS forms a signaling complex with the adapter protein CRKL in hematopoietic cells transformed by the BCR/ABL oncogene. |journal=J. Biol. Chem. |volume=271 |issue= 41 |pages= 25198-203 |year= 1996 |pmid= 8810278 |doi= }}
*{{cite journal | author=Garton AJ, Flint AJ, Tonks NK |title=Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST. |journal=Mol. Cell. Biol. |volume=16 |issue= 11 |pages= 6408-18 |year= 1996 |pmid= 8887669 |doi= }}
*{{cite journal | author=Liu F, Hill DE, Chernoff J |title=Direct binding of the proline-rich region of protein tyrosine phosphatase 1B to the Src homology 3 domain of p130(Cas). |journal=J. Biol. Chem. |volume=271 |issue= 49 |pages= 31290-5 |year= 1997 |pmid= 8940134 |doi= }}
*{{cite journal | author=Astier A, Avraham H, Manie SN, ''et al.'' |title=The related adhesion focal tyrosine kinase is tyrosine-phosphorylated after beta1-integrin stimulation in B cells and binds to p130cas. |journal=J. Biol. Chem. |volume=272 |issue= 1 |pages= 228-32 |year= 1997 |pmid= 8995252 |doi= }}
*{{cite journal | author=Jücker M, McKenna K, da Silva AJ, ''et al.'' |title=The Fes protein-tyrosine kinase phosphorylates a subset of macrophage proteins that are involved in cell adhesion and cell-cell signaling. |journal=J. Biol. Chem. |volume=272 |issue= 4 |pages= 2104-9 |year= 1997 |pmid= 8999909 |doi= }}
*{{cite journal | author=Manié SN, Beck AR, Astier A, ''et al.'' |title=Involvement of p130(Cas) and p105(HEF1), a novel Cas-like docking protein, in a cytoskeleton-dependent signaling pathway initiated by ligation of integrin or antigen receptor on human B cells. |journal=J. Biol. Chem. |volume=272 |issue= 7 |pages= 4230-6 |year= 1997 |pmid= 9020138 |doi= }}
*{{cite journal | author=Schlaepfer DD, Hunter T |title=Focal adhesion kinase overexpression enhances ras-dependent integrin signaling to ERK2/mitogen-activated protein kinase through interactions with and activation of c-Src. |journal=J. Biol. Chem. |volume=272 |issue= 20 |pages= 13189-95 |year= 1997 |pmid= 9148935 |doi= }}
*{{cite journal | author=Manié SN, Astier A, Haghayeghi N, ''et al.'' |title=Regulation of integrin-mediated p130(Cas) tyrosine phosphorylation in human B cells. A role for p59(Fyn) and SHP2. |journal=J. Biol. Chem. |volume=272 |issue= 25 |pages= 15636-41 |year= 1997 |pmid= 9188452 |doi= }}
*{{cite journal | author=Garton AJ, Burnham MR, Bouton AH, Tonks NK |title=Association of PTP-PEST with the SH3 domain of p130cas; a novel mechanism of protein tyrosine phosphatase substrate recognition. |journal=Oncogene |volume=15 |issue= 8 |pages= 877-85 |year= 1997 |pmid= 9285683 |doi= 10.1038/sj.onc.1201279 }}
*{{cite journal | author=Kanda H, Mimura T, Morino N, ''et al.'' |title=Ligation of the T cell antigen receptor induces tyrosine phosphorylation of p105CasL, a member of the p130Cas-related docking protein family, and its subsequent binding to the Src homology 2 domain of c-Crk. |journal=Eur. J. Immunol. |volume=27 |issue= 8 |pages= 2113-7 |year= 1997 |pmid= 9295052 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on BCL2L11... {November 12, 2007 7:43:30 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:44:39 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 = BCL2-like 11 (apoptosis facilitator)
| HGNCid = 994
| Symbol = BCL2L11
| AltSymbols =; BAM; BIM; BIM-alpha6; BIM-beta6; BIM-beta7; BOD; BimEL; BimL
| OMIM = 603827
| ECnumber =
| Homologene = 7643
| MGIid = 1197519
| GeneAtlas_image1 = PBB_GE_BCL2L11_208536_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_BCL2L11_222343_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0043065 |text = positive regulation of apoptosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10018
| Hs_Ensembl = ENSG00000153094
| Hs_RefseqProtein = NP_619528
| Hs_RefseqmRNA = NM_138622
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 111597781
| Hs_GenLoc_end = 111641054
| Hs_Uniprot = O43521
| Mm_EntrezGene = 12125
| Mm_Ensembl = ENSMUSG00000027381
| Mm_RefseqmRNA = NM_009754
| Mm_RefseqProtein = NP_033884
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 127817479
| Mm_GenLoc_end = 127853613
| Mm_Uniprot = Q542N5
}}
}}
'''BCL2-like 11 (apoptosis facilitator)''', also known as '''BCL2L11''', 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 belongs to the BCL-2 protein family. BCL-2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. The protein encoded by this gene contains a Bcl-2 homology domain 3 (BH3). It has been shown to interact with other members of the BCL-2 protein family, including BCL2, BCL2L1/BCL-X(L), and MCL1, and to act as an apoptotic activator. The expression of this gene can be induced by nerve growth factor (NGF), as well as by the forkhead transcription factor FKHR-L1, which suggests a role of this gene in neuronal and lymphocyte apoptosis. Transgenic studies of the mouse counterpart suggested that this gene functions as an essential initiator of apoptosis in thymocyte-negative selection. Several alternatively spliced transcript variants of this gene have been identified.<ref>{{cite web | title = Entrez Gene: BCL2L11 BCL2-like 11 (apoptosis facilitator)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10018| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wang K, Yin XM, Chao DT, ''et al.'' |title=BID: a novel BH3 domain-only death agonist. |journal=Genes Dev. |volume=10 |issue= 22 |pages= 2859-69 |year= 1996 |pmid= 8918887 |doi= }}
*{{cite journal | author=Zha J, Harada H, Yang E, ''et al.'' |title=Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L) |journal=Cell |volume=87 |issue= 4 |pages= 619-28 |year= 1997 |pmid= 8929531 |doi= }}
*{{cite journal | author=O'Connor L, Strasser A, O'Reilly LA, ''et al.'' |title=Bim: a novel member of the Bcl-2 family that promotes apoptosis. |journal=EMBO J. |volume=17 |issue= 2 |pages= 384-95 |year= 1998 |pmid= 9430630 |doi= 10.1093/emboj/17.2.384 }}
*{{cite journal | author=Huang DC, Adams JM, Cory S |title=The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4. |journal=EMBO J. |volume=17 |issue= 4 |pages= 1029-39 |year= 1998 |pmid= 9463381 |doi= 10.1093/emboj/17.4.1029 }}
*{{cite journal | author=Hsu SY, Lin P, Hsueh AJ |title=BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing proapoptotic Bcl-2 protein capable of dimerization with diverse antiapoptotic Bcl-2 members. |journal=Mol. Endocrinol. |volume=12 |issue= 9 |pages= 1432-40 |year= 1998 |pmid= 9731710 |doi= }}
*{{cite journal | author=Puthalakath H, Huang DC, O'Reilly LA, ''et al.'' |title=The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex. |journal=Mol. Cell |volume=3 |issue= 3 |pages= 287-96 |year= 1999 |pmid= 10198631 |doi= }}
*{{cite journal | author=Ohi N, Tokunaga A, Tsunoda H, ''et al.'' |title=A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis induced by Nip3 by forming a heterodimer through the C-terminal hydrophobic region. |journal=Cell Death Differ. |volume=6 |issue= 4 |pages= 314-25 |year= 1999 |pmid= 10381623 |doi= 10.1038/sj.cdd.4400493 }}
*{{cite journal | author=Bouillet P, Metcalf D, Huang DC, ''et al.'' |title=Proapoptotic Bcl-2 relative Bim required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity. |journal=Science |volume=286 |issue= 5445 |pages= 1735-8 |year= 1999 |pmid= 10576740 |doi= }}
*{{cite journal | author=Bae J, Leo CP, Hsu SY, Hsueh AJ |title=MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain. |journal=J. Biol. Chem. |volume=275 |issue= 33 |pages= 25255-61 |year= 2000 |pmid= 10837489 |doi= 10.1074/jbc.M909826199 }}
*{{cite journal | author=Dijkers PF, Medema RH, Lammers JW, ''et al.'' |title=Expression of the pro-apoptotic Bcl-2 family member Bim is regulated by the forkhead transcription factor FKHR-L1. |journal=Curr. Biol. |volume=10 |issue= 19 |pages= 1201-4 |year= 2000 |pmid= 11050388 |doi= }}
*{{cite journal | author=Bouillet P, Zhang LC, Huang DC, ''et al.'' |title=Gene structure alternative splicing, and chromosomal localization of pro-apoptotic Bcl-2 relative Bim. |journal=Mamm. Genome |volume=12 |issue= 2 |pages= 163-8 |year= 2001 |pmid= 11210187 |doi= }}
*{{cite journal | author=Putcha GV, Moulder KL, Golden JP, ''et al.'' |title=Induction of BIM, a proapoptotic BH3-only BCL-2 family member, is critical for neuronal apoptosis. |journal=Neuron |volume=29 |issue= 3 |pages= 615-28 |year= 2001 |pmid= 11301022 |doi= }}
*{{cite journal | author=Murray S, Halford S, Ebenezer ND, ''et al.'' |title=Assignment of BCL2L11 to human chromosome band 2p13 with somatic cell and radiation hybrids. |journal=Cytogenet. Cell Genet. |volume=92 |issue= 3-4 |pages= 353 |year= 2001 |pmid= 11435715 |doi= }}
*{{cite journal | author=Cheng EH, Wei MC, Weiler S, ''et al.'' |title=BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. |journal=Mol. Cell |volume=8 |issue= 3 |pages= 705-11 |year= 2001 |pmid= 11583631 |doi= }}
*{{cite journal | author=U M, Miyashita T, Shikama Y, ''et al.'' |title=Molecular cloning and characterization of six novel isoforms of human Bim, a member of the proapoptotic Bcl-2 family. |journal=FEBS Lett. |volume=509 |issue= 1 |pages= 135-41 |year= 2002 |pmid= 11734221 |doi= }}
*{{cite journal | author=Bouillet P, Purton JF, Godfrey DI, ''et al.'' |title=BH3-only Bcl-2 family member Bim is required for apoptosis of autoreactive thymocytes. |journal=Nature |volume=415 |issue= 6874 |pages= 922-6 |year= 2002 |pmid= 11859372 |doi= 10.1038/415922a }}
*{{cite journal | author=Marani M, Tenev T, Hancock D, ''et al.'' |title=Identification of novel isoforms of the BH3 domain protein Bim which directly activate Bax to trigger apoptosis. |journal=Mol. Cell. Biol. |volume=22 |issue= 11 |pages= 3577-89 |year= 2002 |pmid= 11997495 |doi= }}
*{{cite journal | author=Liu JW, Chandra D, Tang SH, ''et al.'' |title=Identification and characterization of Bimgamma, a novel proapoptotic BH3-only splice variant of Bim. |journal=Cancer Res. |volume=62 |issue= 10 |pages= 2976-81 |year= 2002 |pmid= 12019181 |doi= }}
*{{cite journal | author=Terradillos O, Montessuit S, Huang DC, Martinou JC |title=Direct addition of BimL to mitochondria does not lead to cytochrome c release. |journal=FEBS Lett. |volume=522 |issue= 1-3 |pages= 29-34 |year= 2002 |pmid= 12095614 |doi= }}
*{{cite journal | author=Sugiyama T, Shimizu S, Matsuoka Y, ''et al.'' |title=Activation of mitochondrial voltage-dependent anion channel by apro-apoptotic BH3-only protein Bim. |journal=Oncogene |volume=21 |issue= 32 |pages= 4944-56 |year= 2002 |pmid= 12118373 |doi= 10.1038/sj.onc.1205621 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CSF1... {November 12, 2007 7:27:36 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:28:24 PM PST}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CSF1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hmc.
| PDB = {{PDB2|1hmc}}
| Name = Colony stimulating factor 1 (macrophage)
| HGNCid = 2432
| Symbol = CSF1
| AltSymbols =; MCSF; MGC31930
| OMIM = 120420
| ECnumber =
| Homologene = 7282
| MGIid = 1339753
| GeneAtlas_image1 = PBB_GE_CSF1_211839_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CSF1_207082_at_tn.png
| Function = {{GNF_GO|id=GO:0005157 |text = macrophage colony stimulating factor receptor binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0030097 |text = hemopoiesis}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0030225 |text = macrophage differentiation}} {{GNF_GO|id=GO:0030278 |text = regulation of ossification}} {{GNF_GO|id=GO:0040018 |text = positive regulation of body size}} {{GNF_GO|id=GO:0042488 |text = positive regulation of odontogenesis (sensu Vertebrata)}} {{GNF_GO|id=GO:0045672 |text = positive regulation of osteoclast differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1435
| Hs_Ensembl = ENSG00000184371
| Hs_RefseqProtein = NP_000748
| Hs_RefseqmRNA = NM_000757
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 110254778
| Hs_GenLoc_end = 110275144
| Hs_Uniprot = P09603
| Mm_EntrezGene = 12977
| Mm_Ensembl = ENSMUSG00000014599
| Mm_RefseqmRNA = NM_007778
| Mm_RefseqProtein = NP_031804
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 107869116
| Mm_GenLoc_end = 107888525
| Mm_Uniprot = Q3TDK0
}}
}}
'''Colony stimulating factor 1 (macrophage)''', also known as '''CSF1''', 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 cytokine that controls the production, differentiation, and function of macrophages. The active form of the protein is found extracellularly as a disulfide-linked homodimer, and is thought to be produced by proteolytic cleavage of membrane-bound precursors. The encoded protein may be involved in development of the placenta. Four transcript variants encoding three different isoforms have been found for this gene.<ref>{{cite web | title = Entrez Gene: CSF1 colony stimulating factor 1 (macrophage)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1435| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Stanley ER, Berg KL, Einstein DB, ''et al.'' |title=The biology and action of colony stimulating factor-1. |journal=Stem Cells |volume=12 Suppl 1 |issue= |pages= 15-24; discussion 25 |year= 1995 |pmid= 7696959 |doi= }}
*{{cite journal | author=Alterman RL, Stanley ER |title=Colony stimulating factor-1 expression in human glioma. |journal=Mol. Chem. Neuropathol. |volume=21 |issue= 2-3 |pages= 177-88 |year= 1994 |pmid= 8086034 |doi= }}
*{{cite journal | author=Stanley ER, Berg KL, Einstein DB, ''et al.'' |title=Biology and action of colony--stimulating factor-1. |journal=Mol. Reprod. Dev. |volume=46 |issue= 1 |pages= 4-10 |year= 1997 |pmid= 8981357 |doi= 10.1002/(SICI)1098-2795(199701)46:1<4::AID-MRD2>3.0.CO;2-V }}
*{{cite journal | author=Sweet MJ, Hume DA |title=CSF-1 as a regulator of macrophage activation and immune responses. |journal=Arch. Immunol. Ther. Exp. (Warsz.) |volume=51 |issue= 3 |pages= 169-77 |year= 2004 |pmid= 12894871 |doi= }}
*{{cite journal | author=Mroczko B, Szmitkowski M |title=Hematopoietic cytokines as tumor markers. |journal=Clin. Chem. Lab. Med. |volume=42 |issue= 12 |pages= 1347-54 |year= 2005 |pmid= 15576295 |doi= 10.1515/CCLM.2004.253 }}
*{{cite journal | author=Pandit J, Bohm A, Jancarik J, ''et al.'' |title=Three-dimensional structure of dimeric human recombinant macrophage colony-stimulating factor. |journal=Science |volume=258 |issue= 5086 |pages= 1358-62 |year= 1993 |pmid= 1455231 |doi= }}
*{{cite journal | author=Suzu S, Ohtsuki T, Yanai N, ''et al.'' |title=Identification of a high molecular weight macrophage colony-stimulating factor as a glycosaminoglycan-containing species. |journal=J. Biol. Chem. |volume=267 |issue= 7 |pages= 4345-8 |year= 1992 |pmid= 1531650 |doi= }}
*{{cite journal | author=Saltman DL, Dolganov GM, Hinton LM, Lovett M |title=Reassignment of the human macrophage colony stimulating factor gene to chromosome 1p13-21. |journal=Biochem. Biophys. Res. Commun. |volume=182 |issue= 3 |pages= 1139-43 |year= 1992 |pmid= 1540160 |doi= }}
*{{cite journal | author=Praloran V, Chevalier S, Gascan H |title=Macrophage colony-stimulating factor is produced by activated T lymphocytes in vitro and is detected in vivo in T cells from reactive lymph nodes. |journal=Blood |volume=79 |issue= 9 |pages= 2500-1 |year= 1992 |pmid= 1571567 |doi= }}
*{{cite journal | author=Price LK, Choi HU, Rosenberg L, Stanley ER |title=The predominant form of secreted colony stimulating factor-1 is a proteoglycan. |journal=J. Biol. Chem. |volume=267 |issue= 4 |pages= 2190-9 |year= 1992 |pmid= 1733926 |doi= }}
*{{cite journal | author=Pampfer S, Tabibzadeh S, Chuan FC, Pollard JW |title=Expression of colony-stimulating factor-1 (CSF-1) messenger RNA in human endometrial glands during the menstrual cycle: molecular cloning of a novel transcript that predicts a cell surface form of CSF-1. |journal=Mol. Endocrinol. |volume=5 |issue= 12 |pages= 1931-8 |year= 1992 |pmid= 1791839 |doi= }}
*{{cite journal | author=Stein J, Borzillo GV, Rettenmier CW |title=Direct stimulation of cells expressing receptors for macrophage colony-stimulating factor (CSF-1) by a plasma membrane-bound precursor of human CSF-1. |journal=Blood |volume=76 |issue= 7 |pages= 1308-14 |year= 1990 |pmid= 2145044 |doi= }}
*{{cite journal | author=Sherr CJ, Rettenmier CW, Sacca R, ''et al.'' |title=The c-fms proto-oncogene product is related to the receptor for the mononuclear phagocyte growth factor, CSF-1. |journal=Cell |volume=41 |issue= 3 |pages= 665-76 |year= 1985 |pmid= 2408759 |doi= }}
*{{cite journal | author=Cerretti DP, Wignall J, Anderson D, ''et al.'' |title=Human macrophage-colony stimulating factor: alternative RNA and protein processing from a single gene. |journal=Mol. Immunol. |volume=25 |issue= 8 |pages= 761-70 |year= 1988 |pmid= 2460758 |doi= }}
*{{cite journal | author=Takahashi M, Hirato T, Takano M, ''et al.'' |title=Amino-terminal region of human macrophage colony-stimulating factor (M-CSF) is sufficient for its in vitro biological activity: molecular cloning and expression of carboxyl-terminal deletion mutants of human M-CSF. |journal=Biochem. Biophys. Res. Commun. |volume=161 |issue= 2 |pages= 892-901 |year= 1989 |pmid= 2660794 |doi= }}
*{{cite journal | author=Kawasaki ES, Ladner MB, Wang AM, ''et al.'' |title=Molecular cloning of a complementary DNA encoding human macrophage-specific colony-stimulating factor (CSF-1). |journal=Science |volume=230 |issue= 4723 |pages= 291-6 |year= 1985 |pmid= 2996129 |doi= }}
*{{cite journal | author=Rettenmier CW, Roussel MF, Ashmun RA, ''et al.'' |title=Synthesis of membrane-bound colony-stimulating factor 1 (CSF-1) and downmodulation of CSF-1 receptors in NIH 3T3 cells transformed by cotransfection of the human CSF-1 and c-fms (CSF-1 receptor) genes. |journal=Mol. Cell. Biol. |volume=7 |issue= 7 |pages= 2378-87 |year= 1987 |pmid= 3039346 |doi= }}
*{{cite journal | author=Takahashi M, Hong YM, Yasuda S, ''et al.'' |title=Macrophage colony-stimulating factor is produced by human T lymphoblastoid cell line, CEM-ON: identification by amino-terminal amino acid sequence analysis. |journal=Biochem. Biophys. Res. Commun. |volume=152 |issue= 3 |pages= 1401-9 |year= 1988 |pmid= 3259875 |doi= }}
*{{cite journal | author=Rettenmier CW, Roussel MF |title=Differential processing of colony-stimulating factor 1 precursors encoded by two human cDNAs. |journal=Mol. Cell. Biol. |volume=8 |issue= 11 |pages= 5026-34 |year= 1989 |pmid= 3264877 |doi= }}
*{{cite journal | author=Wong GG, Temple PA, Leary AC, ''et al.'' |title=Human CSF-1: molecular cloning and expression of 4-kb cDNA encoding the human urinary protein. |journal=Science |volume=235 |issue= 4795 |pages= 1504-8 |year= 1987 |pmid= 3493529 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DNMT1... {November 12, 2007 7:28:24 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:29:23 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 = DNA (cytosine-5-)-methyltransferase 1
| HGNCid = 2976
| Symbol = DNMT1
| AltSymbols =; CXXC9; DNMT; FLJ16293; MCMT; MGC104992
| OMIM = 126375
| ECnumber =
| Homologene = 1055
| MGIid = 94912
| GeneAtlas_image1 = PBB_GE_DNMT1_201697_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003886 |text = DNA (cytosine-5-)-methyltransferase activity}} {{GNF_GO|id=GO:0008134 |text = transcription factor binding}} {{GNF_GO|id=GO:0008168 |text = methyltransferase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006306 |text = DNA methylation}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1786
| Hs_Ensembl = ENSG00000130816
| Hs_RefseqProtein = NP_001370
| Hs_RefseqmRNA = NM_001379
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 10105023
| Hs_GenLoc_end = 10166811
| Hs_Uniprot = P26358
| Mm_EntrezGene = 13433
| Mm_Ensembl = ENSMUSG00000004099
| Mm_RefseqmRNA = NM_010066
| Mm_RefseqProtein = NP_034196
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 20657611
| Mm_GenLoc_end = 20703267
| Mm_Uniprot = Q0VDW2
}}
}}
'''DNA (cytosine-5-)-methyltransferase 1''', also known as '''DNMT1''', 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 = DNA (cytosine-5-)-methyltransferase 1 has a role in the establishment and regulation of tissue-specific patterns of methylated cytosine residues. Aberrant methylation patterns are associated with certain human tumors and developmental abnormalities.<ref>{{cite web | title = Entrez Gene: DNMT1 DNA (cytosine-5-)-methyltransferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1786| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Yen RW, Vertino PM, Nelkin BD, ''et al.'' |title=Isolation and characterization of the cDNA encoding human DNA methyltransferase. |journal=Nucleic Acids Res. |volume=20 |issue= 9 |pages= 2287-91 |year= 1992 |pmid= 1594447 |doi= }}
*{{cite journal | author=Bestor T, Laudano A, Mattaliano R, Ingram V |title=Cloning and sequencing of a cDNA encoding DNA methyltransferase of mouse cells. The carboxyl-terminal domain of the mammalian enzymes is related to bacterial restriction methyltransferases. |journal=J. Mol. Biol. |volume=203 |issue= 4 |pages= 971-83 |year= 1989 |pmid= 3210246 |doi= }}
*{{cite journal | author=Hijmans EM, Voorhoeve PM, Beijersbergen RL, ''et al.'' |title=E2F-5, a new E2F family member that interacts with p130 in vivo. |journal=Mol. Cell. Biol. |volume=15 |issue= 6 |pages= 3082-9 |year= 1995 |pmid= 7760804 |doi= }}
*{{cite journal | author=Yoder JA, Yen RW, Vertino PM, ''et al.'' |title=New 5' regions of the murine and human genes for DNA (cytosine-5)-methyltransferase. |journal=J. Biol. Chem. |volume=271 |issue= 49 |pages= 31092-7 |year= 1997 |pmid= 8940105 |doi= }}
*{{cite journal | author=Chuang LS, Ian HI, Koh TW, ''et al.'' |title=Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for p21WAF1. |journal=Science |volume=277 |issue= 5334 |pages= 1996-2000 |year= 1997 |pmid= 9302295 |doi= }}
*{{cite journal | author=Baylin SB |title=Tying it all together: epigenetics, genetics, cell cycle, and cancer. |journal=Science |volume=277 |issue= 5334 |pages= 1948-9 |year= 1997 |pmid= 9333948 |doi= }}
*{{cite journal | author=Robertson KD, Uzvolgyi E, Liang G, ''et al.'' |title=The human DNA methyltransferases (DNMTs) 1, 3a and 3b: coordinate mRNA expression in normal tissues and overexpression in tumors. |journal=Nucleic Acids Res. |volume=27 |issue= 11 |pages= 2291-8 |year= 1999 |pmid= 10325416 |doi= }}
*{{cite journal | author=Michaelson JS, Bader D, Kuo F, ''et al.'' |title=Loss of Daxx, a promiscuously interacting protein, results in extensive apoptosis in early mouse development. |journal=Genes Dev. |volume=13 |issue= 15 |pages= 1918-23 |year= 1999 |pmid= 10444590 |doi= }}
*{{cite journal | author=Hsu DW, Lin MJ, Lee TL, ''et al.'' |title=Two major forms of DNA (cytosine-5) methyltransferase in human somatic tissues. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 17 |pages= 9751-6 |year= 1999 |pmid= 10449766 |doi= }}
*{{cite journal | author=Fuks F, Burgers WA, Brehm A, ''et al.'' |title=DNA methyltransferase Dnmt1 associates with histone deacetylase activity. |journal=Nat. Genet. |volume=24 |issue= 1 |pages= 88-91 |year= 2000 |pmid= 10615135 |doi= 10.1038/71750 }}
*{{cite journal | author=Bonfils C, Beaulieu N, Chan E, ''et al.'' |title=Characterization of the human DNA methyltransferase splice variant Dnmt1b. |journal=J. Biol. Chem. |volume=275 |issue= 15 |pages= 10754-60 |year= 2000 |pmid= 10753866 |doi= }}
*{{cite journal | author=Rountree MR, Bachman KE, Baylin SB |title=DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci. |journal=Nat. Genet. |volume=25 |issue= 3 |pages= 269-77 |year= 2000 |pmid= 10888872 |doi= 10.1038/77023 }}
*{{cite journal | author=Robertson KD, Ait-Si-Ali S, Yokochi T, ''et al.'' |title=DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters. |journal=Nat. Genet. |volume=25 |issue= 3 |pages= 338-42 |year= 2000 |pmid= 10888886 |doi= 10.1038/77124 }}
*{{cite journal | author=Tatematsu KI, Yamazaki T, Ishikawa F |title=MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex containing DNMT1 at the replication foci in late S phase. |journal=Genes Cells |volume=5 |issue= 8 |pages= 677-88 |year= 2000 |pmid= 10947852 |doi= }}
*{{cite journal | author=Mizuno S, Chijiwa T, Okamura T, ''et al.'' |title=Expression of DNA methyltransferases DNMT1, 3A, and 3B in normal hematopoiesis and in acute and chronic myelogenous leukemia. |journal=Blood |volume=97 |issue= 5 |pages= 1172-9 |year= 2001 |pmid= 11222358 |doi= }}
*{{cite journal | author=Fatemi M, Hermann A, Pradhan S, Jeltsch A |title=The activity of the murine DNA methyltransferase Dnmt1 is controlled by interaction of the catalytic domain with the N-terminal part of the enzyme leading to an allosteric activation of the enzyme after binding to methylated DNA. |journal=J. Mol. Biol. |volume=309 |issue= 5 |pages= 1189-99 |year= 2001 |pmid= 11399088 |doi= 10.1006/jmbi.2001.4709 }}
*{{cite journal | author=Dintilhac A, Bernués J |title=HMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid sequences. |journal=J. Biol. Chem. |volume=277 |issue= 9 |pages= 7021-8 |year= 2002 |pmid= 11748221 |doi= 10.1074/jbc.M108417200 }}
*{{cite journal | author=Di Croce L, Raker VA, Corsaro M, ''et al.'' |title=Methyltransferase recruitment and DNA hypermethylation of target promoters by an oncogenic transcription factor. |journal=Science |volume=295 |issue= 5557 |pages= 1079-82 |year= 2002 |pmid= 11834837 |doi= 10.1126/science.1065173 }}
*{{cite journal | author=Pradhan S, Kim GD |title=The retinoblastoma gene product interacts with maintenance human DNA (cytosine-5) methyltransferase and modulates its activity. |journal=EMBO J. |volume=21 |issue= 4 |pages= 779-88 |year= 2002 |pmid= 11847125 |doi= 10.1093/emboj/21.4.779 }}
*{{cite journal | author=Rhee I, Bachman KE, Park BH, ''et al.'' |title=DNMT1 and DNMT3b cooperate to silence genes in human cancer cells. |journal=Nature |volume=416 |issue= 6880 |pages= 552-6 |year= 2002 |pmid= 11932749 |doi= 10.1038/416552a }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FGB... {November 12, 2007 7:29:23 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:30:15 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_FGB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1fza.
| PDB = {{PDB2|1fza}}, {{PDB2|1fzb}}, {{PDB2|1fzc}}, {{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 beta chain
| HGNCid = 3662
| Symbol = FGB
| AltSymbols =; MGC104327; MGC120405
| OMIM = 134830
| ECnumber =
| Homologene = 3772
| MGIid = 99501
| GeneAtlas_image1 = PBB_GE_FGB_216238_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_FGB_204988_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 = 2244
| Hs_Ensembl = ENSG00000171564
| Hs_RefseqProtein = NP_005132
| Hs_RefseqmRNA = NM_005141
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 155703596
| Hs_GenLoc_end = 155711683
| Hs_Uniprot = P02675
| Mm_EntrezGene = 110135
| Mm_Ensembl = ENSMUSG00000033831
| Mm_RefseqmRNA = NM_181849
| Mm_RefseqProtein = NP_862897
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 83128174
| Mm_GenLoc_end = 83135736
| Mm_Uniprot = Q3TGR2
}}
}}
'''Fibrinogen beta chain''', also known as '''FGB''', 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 beta 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 afibrinogenemia, dysfibrinogenemia, hypodysfibrinogenemia and thrombotic tendency.<ref>{{cite web | title = Entrez Gene: FGB fibrinogen beta chain| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2244| 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=Vasse M, Paysant J, Soria J, ''et al.'' |title=Regulation of fibrinogen biosynthesis by cytokines, consequences on the vascular risk. |journal=Haemostasis |volume=26 Suppl 4 |issue= |pages= 331-9 |year= 1997 |pmid= 8979138 |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=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=Brennan SO, Fellowes AP, George PM |title=Molecular mechanisms of hypo- and afibrinogenemia. |journal=Ann. N. Y. Acad. Sci. |volume=936 |issue= |pages= 91-100 |year= 2001 |pmid= 11460528 |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=Chen XC, Xu MT, Zhou W, ''et al.'' |title=A meta-analysis of relationship between beta-fibrinogen gene -148C/T polymorphism and susceptibility to cerebral infarction in Han Chinese. |journal=Chin. Med. J. |volume=120 |issue= 13 |pages= 1198-202 |year= 2007 |pmid= 17637253 |doi= }}
*{{cite journal | author=Tarakhovskiĭ IuS, Galushchenko IV, Boroviagin VL, ''et al.'' |title=[Temperature-dependent changes in the profile of the sarcoplasmic reticulum membrane hydrophobic zones] |journal=Biokhimiia |volume=44 |issue= 5 |pages= 897-902 |year= 1979 |pmid= 156564 |doi= }}
*{{cite journal | author=Watt KW, Takagi T, Doolittle RF |title=Amino acid sequence of the beta chain of human fibrinogen. |journal=Biochemistry |volume=18 |issue= 1 |pages= 68-76 |year= 1979 |pmid= 420779 |doi= }}
*{{cite journal | author=Gårdlund B, Hessel B, Marguerie G, ''et al.'' |title=Primary structure of human fibrinogen. Characterization of disulfide-containing cyanogen-bromide fragments. |journal=Eur. J. Biochem. |volume=77 |issue= 3 |pages= 595-610 |year= 1977 |pmid= 891553 |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=Abnormal fibrinogens IJmuiden (B beta Arg14----Cys) and Nijmegen (B beta Arg44----Cys) form disulfide-linked fibrinogen-albumin complexes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 8 |pages= 3478-82 |year= 1992 |pmid= 1565641 |doi= }}
*{{cite journal | author=Koopman J, Haverkate F, Lord ST, ''et al.'' |title=Molecular basis of fibrinogen Naples associated with defective thrombin binding and thrombophilia. Homozygous substitution of B beta 68 Ala----Thr. |journal=J. Clin. Invest. |volume=90 |issue= 1 |pages= 238-44 |year= 1992 |pmid= 1634610 |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= }}
*{{cite journal | author=Yoshida N, Wada H, Morita K, ''et al.'' |title=A new congenital abnormal fibrinogen Ise characterized by the replacement of B beta glycine-15 by cysteine. |journal=Blood |volume=77 |issue= 9 |pages= 1958-63 |year= 1991 |pmid= 2018836 |doi= }}
*{{cite journal | author=Chung DW, Harris JE, Davie EW |title=Nucleotide sequences of the three genes coding for human fibrinogen. |journal=Adv. Exp. Med. Biol. |volume=281 |issue= |pages= 39-48 |year= 1991 |pmid= 2102623 |doi= }}
*{{cite journal | author=Danishefsky K, Hartwig R, Banerjee D, Redman C |title=Intracellular fate of fibrinogen B beta chain expressed in COS cells. |journal=Biochim. Biophys. Acta |volume=1048 |issue= 2-3 |pages= 202-8 |year= 1990 |pmid= 2322576 |doi= }}
*{{cite journal | author=Berg K, Kierulf P |title=DNA polymorphisms at fibrinogen loci and plasma fibrinogen concentration. |journal=Clin. Genet. |volume=36 |issue= 4 |pages= 229-35 |year= 1989 |pmid= 2572363 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FGF1... {November 12, 2007 7:30:15 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:31:08 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_FGF1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1afc.
| PDB = {{PDB2|1afc}}, {{PDB2|1axm}}, {{PDB2|1bar}}, {{PDB2|1djs}}, {{PDB2|1dzc}}, {{PDB2|1dzd}}, {{PDB2|1e0o}}, {{PDB2|1evt}}, {{PDB2|1hkn}}, {{PDB2|1jqz}}, {{PDB2|1jt3}}, {{PDB2|1jt4}}, {{PDB2|1jt5}}, {{PDB2|1jt7}}, {{PDB2|1jtc}}, {{PDB2|1jy0}}, {{PDB2|1k5u}}, {{PDB2|1k5v}}, {{PDB2|1m16}}, {{PDB2|1nzk}}, {{PDB2|1p63}}, {{PDB2|1pzz}}, {{PDB2|1q03}}, {{PDB2|1q04}}, {{PDB2|1rg8}}, {{PDB2|1rml}}, {{PDB2|1ry7}}, {{PDB2|1yto}}, {{PDB2|1z2v}}, {{PDB2|1z4s}}, {{PDB2|2afg}}, {{PDB2|2aqz}}, {{PDB2|2axm}}, {{PDB2|2erm}}, {{PDB2|2j3p}}
| Name = Fibroblast growth factor 1 (acidic)
| HGNCid = 3665
| Symbol = FGF1
| AltSymbols =; AFGF; ECGF; ECGF-beta; ECGFA; ECGFB; FGF-alpha; FGFA; GLIO703; HBGF1
| OMIM = 131220
| ECnumber =
| Homologene = 625
| MGIid = 95515
| GeneAtlas_image1 = PBB_GE_FGF1_205117_at_tn.png
| GeneAtlas_image2 = PBB_GE_FGF1_208240_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}} {{GNF_GO|id=GO:0008201 |text = heparin binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0001759 |text = induction of an organ}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0009653 |text = anatomical structure morphogenesis}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0030324 |text = lung development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2246
| Hs_Ensembl = ENSG00000113578
| Hs_RefseqProtein = NP_000791
| Hs_RefseqmRNA = NM_000800
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 141951927
| Hs_GenLoc_end = 142046134
| Hs_Uniprot = P05230
| Mm_EntrezGene = 14164
| Mm_Ensembl = ENSMUSG00000036585
| Mm_RefseqmRNA = NM_010197
| Mm_RefseqProtein = NP_034327
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 18
| Mm_GenLoc_start = 38965154
| Mm_GenLoc_end = 39044673
| Mm_Uniprot = Q6ZWS1
}}
}}
'''Fibroblast growth factor 1 (acidic)''', also known as '''FGF1''', 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 fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described.<ref>{{cite web | title = Entrez Gene: FGF1 fibroblast growth factor 1 (acidic)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2246| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Yu YL, Kha H, Golden JA, ''et al.'' |title=An acidic fibroblast growth factor protein generated by alternate splicing acts like an antagonist. |journal=J. Exp. Med. |volume=175 |issue= 4 |pages= 1073-80 |year= 1992 |pmid= 1372643 |doi= }}
*{{cite journal | author=Chiu IM, Wang WP, Lehtoma K |title=Alternative splicing generates two forms of mRNA coding for human heparin-binding growth factor 1. |journal=Oncogene |volume=5 |issue= 5 |pages= 755-62 |year= 1990 |pmid= 1693186 |doi= }}
*{{cite journal | author=Zhu X, Komiya H, Chirino A, ''et al.'' |title=Three-dimensional structures of acidic and basic fibroblast growth factors. |journal=Science |volume=251 |issue= 4989 |pages= 90-3 |year= 1991 |pmid= 1702556 |doi= }}
*{{cite journal | author=Wang WP, Quick D, Balcerzak SP, ''et al.'' |title=Cloning and sequence analysis of the human acidic fibroblast growth factor gene and its preservation in leukemia patients. |journal=Oncogene |volume=6 |issue= 9 |pages= 1521-9 |year= 1991 |pmid= 1717925 |doi= }}
*{{cite journal | author=Wu DQ, Kan MK, Sato GH, ''et al.'' |title=Characterization and molecular cloning of a putative binding protein for heparin-binding growth factors. |journal=J. Biol. Chem. |volume=266 |issue= 25 |pages= 16778-85 |year= 1991 |pmid= 1885605 |doi= }}
*{{cite journal | author=Crumley G, Dionne CA, Jaye M |title=The gene for human acidic fibroblast growth factor encodes two upstream exons alternatively spliced to the first coding exon. |journal=Biochem. Biophys. Res. Commun. |volume=171 |issue= 1 |pages= 7-13 |year= 1990 |pmid= 2393407 |doi= }}
*{{cite journal | author=Harper JW, Strydom DJ, Lobb RR |title=Human class 1 heparin-binding growth factor: structure and homology to bovine acidic brain fibroblast growth factor. |journal=Biochemistry |volume=25 |issue= 14 |pages= 4097-103 |year= 1986 |pmid= 2427112 |doi= }}
*{{cite journal | author=Winkles JA, Friesel R, Burgess WH, ''et al.'' |title=Human vascular smooth muscle cells both express and respond to heparin-binding growth factor I (endothelial cell growth factor). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 20 |pages= 7124-8 |year= 1987 |pmid= 2444975 |doi= }}
*{{cite journal | author=Wang WP, Lehtoma K, Varban ML, ''et al.'' |title=Cloning of the gene coding for human class 1 heparin-binding growth factor and its expression in fetal tissues. |journal=Mol. Cell. Biol. |volume=9 |issue= 6 |pages= 2387-95 |year= 1989 |pmid= 2474753 |doi= }}
*{{cite journal | author=Mergia A, Tischer E, Graves D, ''et al.'' |title=Structural analysis of the gene for human acidic fibroblast growth factor. |journal=Biochem. Biophys. Res. Commun. |volume=164 |issue= 3 |pages= 1121-9 |year= 1989 |pmid= 2590193 |doi= }}
*{{cite journal | author=Jaye M, Howk R, Burgess W, ''et al.'' |title=Human endothelial cell growth factor: cloning, nucleotide sequence, and chromosome localization. |journal=Science |volume=233 |issue= 4763 |pages= 541-5 |year= 1986 |pmid= 3523756 |doi= }}
*{{cite journal | author=Gimenez-Gallego G, Conn G, Hatcher VB, Thomas KA |title=The complete amino acid sequence of human brain-derived acidic fibroblast growth factor. |journal=Biochem. Biophys. Res. Commun. |volume=138 |issue= 2 |pages= 611-7 |year= 1986 |pmid= 3527167 |doi= }}
*{{cite journal | author=Gautschi P, Fràter-Schröder M, Böhlen P |title=Partial molecular characterization of endothelial cell mitogens from human brain: acidic and basic fibroblast growth factors. |journal=FEBS Lett. |volume=204 |issue= 2 |pages= 203-7 |year= 1986 |pmid= 3732516 |doi= }}
*{{cite journal | author=Gautschi-Sova P, Müller T, Böhlen P |title=Amino acid sequence of human acidic fibroblast growth factor. |journal=Biochem. Biophys. Res. Commun. |volume=140 |issue= 3 |pages= 874-80 |year= 1986 |pmid= 3778488 |doi= }}
*{{cite journal | author=Gimenez-Gallego G, Conn G, Hatcher VB, Thomas KA |title=Human brain-derived acidic and basic fibroblast growth factors: amino terminal sequences and specific mitogenic activities. |journal=Biochem. Biophys. Res. Commun. |volume=135 |issue= 2 |pages= 541-8 |year= 1986 |pmid= 3964259 |doi= }}
*{{cite journal | author=Zhao XM, Yeoh TK, Hiebert M, ''et al.'' |title=The expression of acidic fibroblast growth factor (heparin-binding growth factor-1) and cytokine genes in human cardiac allografts and T cells. |journal=Transplantation |volume=56 |issue= 5 |pages= 1177-82 |year= 1993 |pmid= 7504343 |doi= }}
*{{cite journal | author=Pineda-Lucena A, Jiménez MA, Nieto JL, ''et al.'' |title=1H-NMR assignment and solution structure of human acidic fibroblast growth factor activated by inositol hexasulfate. |journal=J. Mol. Biol. |volume=242 |issue= 1 |pages= 81-98 |year= 1994 |pmid= 7521397 |doi= 10.1006/jmbi.1994.1558 }}
*{{cite journal | author=Chotani MA, Payson RA, Winkles JA, Chiu IM |title=Human fibroblast growth factor 1 gene expression in vascular smooth muscle cells is modulated via an alternate promoter in response to serum and phorbol ester. |journal=Nucleic Acids Res. |volume=23 |issue= 3 |pages= 434-41 |year= 1995 |pmid= 7533902 |doi= }}
*{{cite journal | author=Opalenik SR, Shin JT, Wehby JN, ''et al.'' |title=The HIV-1 TAT protein induces the expression and extracellular appearance of acidic fibroblast growth factor. |journal=J. Biol. Chem. |volume=270 |issue= 29 |pages= 17457-67 |year= 1995 |pmid= 7542239 |doi= }}
*{{cite journal | author=Myers RL, Payson RA, Chotani MA, ''et al.'' |title=Gene structure and differential expression of acidic fibroblast growth factor mRNA: identification and distribution of four different transcripts. |journal=Oncogene |volume=8 |issue= 2 |pages= 341-9 |year= 1993 |pmid= 7678925 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GRIN2B... {November 12, 2007 7:31:08 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:31:55 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Glutamate receptor, ionotropic, N-methyl D-aspartate 2B
| HGNCid = 4586
| Symbol = GRIN2B
| AltSymbols =; MGC142178; MGC142180; NMDAR2B; NR2B; hNR3
| OMIM = 138252
| ECnumber =
| Homologene = 646
| MGIid = 95821
| GeneAtlas_image1 = PBB_GE_GRIN2B_210412_at_tn.png
| GeneAtlas_image2 = PBB_GE_GRIN2B_210411_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004972 |text = N-methyl-D-aspartate selective glutamate receptor activity}} {{GNF_GO|id=GO:0005216 |text = ion channel activity}} {{GNF_GO|id=GO:0005234 |text = extracellular-glutamate-gated ion channel activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0008021 |text = synaptic vesicle}} {{GNF_GO|id=GO:0042734 |text = presynaptic membrane}} {{GNF_GO|id=GO:0045211 |text = postsynaptic membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0007215 |text = glutamate signaling pathway}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007611 |text = learning and/or memory}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2904
| Hs_Ensembl = ENSG00000150086
| Hs_RefseqProtein = NP_000825
| Hs_RefseqmRNA = NM_000834
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 13605411
| Hs_GenLoc_end = 14024319
| Hs_Uniprot = Q13224
| Mm_EntrezGene = 14812
| Mm_Ensembl = ENSMUSG00000030209
| Mm_RefseqmRNA = NM_008171
| Mm_RefseqProtein = NP_032197
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 135697791
| Mm_GenLoc_end = 136009994
| Mm_Uniprot = Q8CG69
}}
}}
'''Glutamate receptor, ionotropic, N-methyl D-aspartate 2B''', also known as '''GRIN2B''', 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 = N-methyl-D-aspartate (NMDA) receptors are a class of ionotropic glutamate receptors. NMDA receptor channel has been shown to be involved in long-term potentiation, an activity-dependent increase in the efficiency of synaptic transmission thought to underlie certain kinds of memory and learning. NMDA receptor channels are heteromers composed of the key receptor subunit NMDAR1 (GRIN1) and 1 or more of the 4 NMDAR2 subunits: NMDAR2A (GRIN2A), NMDAR2B (GRIN2B), NMDAR2C (GRIN2C), and NMDAR2D (GRIN2D). GRIN2B may be a candidate gene for the neurodegenerative disorder dentato-rubro-pallidoluysian atrophy (DRPLA)<ref>{{cite web | title = Entrez Gene: GRIN2B glutamate receptor, ionotropic, N-methyl D-aspartate 2B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2904| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schröder HC, Perovic S, Kavsan V, ''et al.'' |title=Mechanisms of prionSc- and HIV-1 gp120 induced neuronal cell death. |journal=Neurotoxicology |volume=19 |issue= 4-5 |pages= 683-8 |year= 1998 |pmid= 9745929 |doi= }}
*{{cite journal | author=Nagy J |title=The NR2B subtype of NMDA receptor: a potential target for the treatment of alcohol dependence. |journal=Current drug targets. CNS and neurological disorders |volume=3 |issue= 3 |pages= 169-79 |year= 2004 |pmid= 15180478 |doi= }}
*{{cite journal | author=King JE, Eugenin EA, Buckner CM, Berman JW |title=HIV tat and neurotoxicity. |journal=Microbes Infect. |volume=8 |issue= 5 |pages= 1347-57 |year= 2006 |pmid= 16697675 |doi= 10.1016/j.micinf.2005.11.014 }}
*{{cite journal | author=Monyer H, Sprengel R, Schoepfer R, ''et al.'' |title=Heteromeric NMDA receptors: molecular and functional distinction of subtypes. |journal=Science |volume=256 |issue= 5060 |pages= 1217-21 |year= 1992 |pmid= 1350383 |doi= }}
*{{cite journal | author=Kornau HC, Schenker LT, Kennedy MB, Seeburg PH |title=Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. |journal=Science |volume=269 |issue= 5231 |pages= 1737-40 |year= 1995 |pmid= 7569905 |doi= }}
*{{cite journal | author=Magnuson DS, Knudsen BE, Geiger JD, ''et al.'' |title=Human immunodeficiency virus type 1 tat activates non-N-methyl-D-aspartate excitatory amino acid receptors and causes neurotoxicity. |journal=Ann. Neurol. |volume=37 |issue= 3 |pages= 373-80 |year= 1995 |pmid= 7695237 |doi= 10.1002/ana.410370314 }}
*{{cite journal | author=Mandich P, Schito AM, Bellone E, ''et al.'' |title=Mapping of the human NMDAR2B receptor subunit gene (GRIN2B) to chromosome 12p12. |journal=Genomics |volume=22 |issue= 1 |pages= 216-8 |year= 1994 |pmid= 7959773 |doi= 10.1006/geno.1994.1366 }}
*{{cite journal | author=Adams SL, Foldes RL, Kamboj RK |title=Human N-methyl-D-aspartate receptor modulatory subunit hNR3: cloning and sequencing of the cDNA and primary structure of the protein. |journal=Biochim. Biophys. Acta |volume=1260 |issue= 1 |pages= 105-8 |year= 1995 |pmid= 7999784 |doi= }}
*{{cite journal | author=Sheng M, Cummings J, Roldan LA, ''et al.'' |title=Changing subunit composition of heteromeric NMDA receptors during development of rat cortex. |journal=Nature |volume=368 |issue= 6467 |pages= 144-7 |year= 1994 |pmid= 8139656 |doi= 10.1038/368144a0 }}
*{{cite journal | author=Roche KW, Raymond LA, Blackstone C, Huganir RL |title=Transmembrane topology of the glutamate receptor subunit GluR6. |journal=J. Biol. Chem. |volume=269 |issue= 16 |pages= 11679-82 |year= 1994 |pmid= 8163463 |doi= }}
*{{cite journal | author=Lannuzel A, Lledo PM, Lamghitnia HO, ''et al.'' |title=HIV-1 envelope proteins gp120 and gp160 potentiate NMDA-induced [Ca2+]i increase, alter [Ca2+]i homeostasis and induce neurotoxicity in human embryonic neurons. |journal=Eur. J. Neurosci. |volume=7 |issue= 11 |pages= 2285-93 |year= 1996 |pmid= 8563977 |doi= }}
*{{cite journal | author=Corasaniti MT, Melino G, Navarra M, ''et al.'' |title=Death of cultured human neuroblastoma cells induced by HIV-1 gp120 is prevented by NMDA receptor antagonists and inhibitors of nitric oxide and cyclooxygenase. |journal=Neurodegeneration : a journal for neurodegenerative disorders, neuroprotection, and neuroregeneration |volume=4 |issue= 3 |pages= 315-21 |year= 1996 |pmid= 8581564 |doi= }}
*{{cite journal | author=Niethammer M, Kim E, Sheng M |title=Interaction between the C terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases. |journal=J. Neurosci. |volume=16 |issue= 7 |pages= 2157-63 |year= 1996 |pmid= 8601796 |doi= }}
*{{cite journal | author=Pittaluga A, Pattarini R, Severi P, Raiteri M |title=Human brain N-methyl-D-aspartate receptors regulating noradrenaline release are positively modulated by HIV-1 coat protein gp120. |journal=AIDS |volume=10 |issue= 5 |pages= 463-8 |year= 1996 |pmid= 8724036 |doi= }}
*{{cite journal | author=Hess SD, Daggett LP, Crona J, ''et al.'' |title=Cloning and functional characterization of human heteromeric N-methyl-D-aspartate receptors. |journal=J. Pharmacol. Exp. Ther. |volume=278 |issue= 2 |pages= 808-16 |year= 1996 |pmid= 8768735 |doi= }}
*{{cite journal | author=Müller BM, Kistner U, Kindler S, ''et al.'' |title=SAP102, a novel postsynaptic protein that interacts with NMDA receptor complexes in vivo. |journal=Neuron |volume=17 |issue= 2 |pages= 255-65 |year= 1996 |pmid= 8780649 |doi= }}
*{{cite journal | author=Wu P, Price P, Du B, ''et al.'' |title=Direct cytotoxicity of HIV-1 envelope protein gp120 on human NT neurons. |journal=Neuroreport |volume=7 |issue= 5 |pages= 1045-9 |year= 1996 |pmid= 8804048 |doi= }}
*{{cite journal | author=Bennett BA, Rusyniak DE, Hollingsworth CK |title=HIV-1 gp120-induced neurotoxicity to midbrain dopamine cultures. |journal=Brain Res. |volume=705 |issue= 1-2 |pages= 168-76 |year= 1996 |pmid= 8821747 |doi= }}
*{{cite journal | author=Toggas SM, Masliah E, Mucke L |title=Prevention of HIV-1 gp120-induced neuronal damage in the central nervous system of transgenic mice by the NMDA receptor antagonist memantine. |journal=Brain Res. |volume=706 |issue= 2 |pages= 303-7 |year= 1996 |pmid= 8822372 |doi= }}
*{{cite journal | author=Dreyer EB, Lipton SA |title=The coat protein gp120 of HIV-1 inhibits astrocyte uptake of excitatory amino acids via macrophage arachidonic acid. |journal=Eur. J. Neurosci. |volume=7 |issue= 12 |pages= 2502-7 |year= 1996 |pmid= 8845955 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GSN... {November 12, 2007 7:31:55 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:32:30 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_GSN_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1c0f.
| PDB = {{PDB2|1c0f}}, {{PDB2|1c0g}}, {{PDB2|1d0n}}, {{PDB2|1d4x}}, {{PDB2|1dej}}, {{PDB2|1eqy}}, {{PDB2|1esv}}, {{PDB2|1h1v}}, {{PDB2|1kcq}}, {{PDB2|1mdu}}, {{PDB2|1nlv}}, {{PDB2|1nm1}}, {{PDB2|1nmd}}, {{PDB2|1nph}}, {{PDB2|1p8x}}, {{PDB2|1p8z}}, {{PDB2|1rgi}}, {{PDB2|1t44}}, {{PDB2|1yag}}, {{PDB2|1yvn}}, {{PDB2|2ff3}}, {{PDB2|2ff6}}, {{PDB2|2fgh}}, {{PDB2|2fh1}}, {{PDB2|2fh2}}, {{PDB2|2fh3}}, {{PDB2|2fh4}}
| Name = Gelsolin (amyloidosis, Finnish type)
| HGNCid = 4620
| Symbol = GSN
| AltSymbols =; DKFZp313L0718
| OMIM = 137350
| ECnumber =
| Homologene = 147
| MGIid = 95851
| GeneAtlas_image1 = PBB_GE_GSN_200696_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_GSN_214040_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}} {{GNF_GO|id=GO:0030027 |text = lamellipodium}}
| Process = {{GNF_GO|id=GO:0016192 |text = vesicle-mediated transport}} {{GNF_GO|id=GO:0030041 |text = actin filament polymerization}} {{GNF_GO|id=GO:0051014 |text = actin filament severing}} {{GNF_GO|id=GO:0051016 |text = barbed-end actin filament capping}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2934
| Hs_Ensembl = ENSG00000148180
| Hs_RefseqProtein = NP_000168
| Hs_RefseqmRNA = NM_000177
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 123070228
| Hs_GenLoc_end = 123134941
| Hs_Uniprot = P06396
| Mm_EntrezGene = 227753
| Mm_Ensembl = ENSMUSG00000026879
| Mm_RefseqmRNA = NM_146120
| Mm_RefseqProtein = NP_666232
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 35104449
| Mm_GenLoc_end = 35129901
| Mm_Uniprot = Q3TGJ9
}}
}}
'''Gelsolin (amyloidosis, Finnish type)''', also known as '''GSN''', 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=Fujita H |title=[An actin-regulatory protein, gelsolin functions as a regulator of cell growth and apoptosis] |journal=Seikagaku |volume=74 |issue= 2 |pages= 135-9 |year= 2002 |pmid= 11925941 |doi= }}
*{{cite journal | author=Silacci P, Mazzolai L, Gauci C, ''et al.'' |title=Gelsolin superfamily proteins: key regulators of cellular functions. |journal=Cell. Mol. Life Sci. |volume=61 |issue= 19-20 |pages= 2614-23 |year= 2004 |pmid= 15526166 |doi= 10.1007/s00018-004-4225-6 }}
*{{cite journal | author=Haltia M, Levy E, Meretoja J, ''et al.'' |title=Gelsolin gene mutation--at codon 187--in familial amyloidosis, Finnish: DNA-diagnostic assay. |journal=Am. J. Med. Genet. |volume=42 |issue= 3 |pages= 357-9 |year= 1992 |pmid= 1311149 |doi= 10.1002/ajmg.1320420321 }}
*{{cite journal | author=Paunio T, Kiuru S, Hongell V, ''et al.'' |title=Solid-phase minisequencing test reveals Asp187----Asn (G654----A) mutation of gelsolin in all affected individuals with Finnish type of familial amyloidosis. |journal=Genomics |volume=13 |issue= 1 |pages= 237-9 |year= 1992 |pmid= 1315718 |doi= }}
*{{cite journal | author=Yu FX, Sun HQ, Janmey PA, Yin HL |title=Identification of a polyphosphoinositide-binding sequence in an actin monomer-binding domain of gelsolin. |journal=J. Biol. Chem. |volume=267 |issue= 21 |pages= 14616-21 |year= 1992 |pmid= 1321812 |doi= }}
*{{cite journal | author=de la Chapelle A, Kere J, Sack GH, ''et al.'' |title=Familial amyloidosis, Finnish type: G654----a mutation of the gelsolin gene in Finnish families and an unrelated American family. |journal=Genomics |volume=13 |issue= 3 |pages= 898-901 |year= 1992 |pmid= 1322359 |doi= }}
*{{cite journal | author=de la Chapelle A, Tolvanen R, Boysen G, ''et al.'' |title=Gelsolin-derived familial amyloidosis caused by asparagine or tyrosine substitution for aspartic acid at residue 187. |journal=Nat. Genet. |volume=2 |issue= 2 |pages= 157-60 |year= 1993 |pmid= 1338910 |doi= 10.1038/ng1092-157 }}
*{{cite journal | author=Hiltunen T, Kiuru S, Hongell V, ''et al.'' |title=Finnish type of familial amyloidosis: cosegregation of Asp187----Asn mutation of gelsolin with the disease in three large families. |journal=Am. J. Hum. Genet. |volume=49 |issue= 3 |pages= 522-8 |year= 1991 |pmid= 1652889 |doi= }}
*{{cite journal | author=Gorevic PD, Munoz PC, Gorgone G, ''et al.'' |title=Amyloidosis due to a mutation of the gelsolin gene in an American family with lattice corneal dystrophy type II. |journal=N. Engl. J. Med. |volume=325 |issue= 25 |pages= 1780-5 |year= 1991 |pmid= 1658654 |doi= }}
*{{cite journal | author=Maury CP, Alli K, Baumann M |title=Finnish hereditary amyloidosis. Amino acid sequence homology between the amyloid fibril protein and human plasma gelsoline. |journal=FEBS Lett. |volume=260 |issue= 1 |pages= 85-7 |year= 1990 |pmid= 2153578 |doi= }}
*{{cite journal | author=Haltia M, Prelli F, Ghiso J, ''et al.'' |title=Amyloid protein in familial amyloidosis (Finnish type) is homologous to gelsolin, an actin-binding protein. |journal=Biochem. Biophys. Res. Commun. |volume=167 |issue= 3 |pages= 927-32 |year= 1990 |pmid= 2157434 |doi= }}
*{{cite journal | author=Levy E, Haltia M, Fernandez-Madrid I, ''et al.'' |title=Mutation in gelsolin gene in Finnish hereditary amyloidosis. |journal=J. Exp. Med. |volume=172 |issue= 6 |pages= 1865-7 |year= 1991 |pmid= 2175344 |doi= }}
*{{cite journal | author=Ghiso J, Haltia M, Prelli F, ''et al.'' |title=Gelsolin variant (Asn-187) in familial amyloidosis, Finnish type. |journal=Biochem. J. |volume=272 |issue= 3 |pages= 827-30 |year= 1991 |pmid= 2176481 |doi= }}
*{{cite journal | author=Kwiatkowski DJ, Westbrook CA, Bruns GA, Morton CC |title=Localization of gelsolin proximal to ABL on chromosome 9. |journal=Am. J. Hum. Genet. |volume=42 |issue= 4 |pages= 565-72 |year= 1988 |pmid= 2831714 |doi= }}
*{{cite journal | author=Kwiatkowski DJ, Stossel TP, Orkin SH, ''et al.'' |title=Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain. |journal=Nature |volume=323 |issue= 6087 |pages= 455-8 |year= 1986 |pmid= 3020431 |doi= 10.1038/323455a0 }}
*{{cite journal | author=Lind SE, Janmey PA |title=Human plasma gelsolin binds to fibronectin. |journal=J. Biol. Chem. |volume=259 |issue= 21 |pages= 13262-6 |year= 1984 |pmid= 6092370 |doi= }}
*{{cite journal | author=Lind SE, Yin HL, Stossel TP |title=Human platelets contain gelsolin. A regulator of actin filament length. |journal=J. Clin. Invest. |volume=69 |issue= 6 |pages= 1384-7 |year= 1982 |pmid= 6282935 |doi= }}
*{{cite journal | author=Paunio T, Sunada Y, Kiuru S, ''et al.'' |title=Haplotype analysis in gelsolin-related amyloidosis reveals independent origin of identical mutation (G654A) of gelsolin in Finland and Japan. |journal=Hum. Mutat. |volume=6 |issue= 1 |pages= 60-5 |year= 1995 |pmid= 7550233 |doi= 10.1002/humu.1380060112 }}
*{{cite journal | author=Pope B, Maciver S, Weeds A |title=Localization of the calcium-sensitive actin monomer binding site in gelsolin to segment 4 and identification of calcium binding sites. |journal=Biochemistry |volume=34 |issue= 5 |pages= 1583-8 |year= 1995 |pmid= 7849017 |doi= }}
*{{cite journal | author=Steiner RD, Paunio T, Uemichi T, ''et al.'' |title=Asp187Asn mutation of gelsolin in an American kindred with familial amyloidosis, Finnish type (FAP IV). |journal=Hum. Genet. |volume=95 |issue= 3 |pages= 327-30 |year= 1995 |pmid= 7868127 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HLA-DPB1... {November 12, 2007 7:32:30 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:33:10 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 = Major histocompatibility complex, class II, DP beta 1
| HGNCid = 4940
| Symbol = HLA-DPB1
| AltSymbols =; DPB1; HLA-DP1B; MHC DPB1
| OMIM = 142858
| ECnumber =
| Homologene = 88656
| MGIid =
| GeneAtlas_image1 = PBB_GE_HLA-DPB1_201137_s_at_tn.png
| Function = {{GNF_GO|id=GO:0032395 |text = MHC class II receptor activity}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0042613 |text = MHC class II protein complex}}
| Process = {{GNF_GO|id=GO:0002504 |text = antigen processing and presentation of peptide or polysaccharide antigen via MHC class II}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0009405 |text = pathogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3115
| Hs_Ensembl = ENSG00000168383
| Hs_RefseqProtein = NP_002112
| Hs_RefseqmRNA = NM_002121
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 33151694
| Hs_GenLoc_end = 33162956
| Hs_Uniprot = P04232
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Major histocompatibility complex, class II, DP beta 1''', also known as '''HLA-DPB1''', 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 = HLA-DPB belongs to the HLA class II beta chain paralogues. This class II molecule is a heterodimer consisting of an alpha (DPA) and a beta chain (DPB), both anchored in the membrane. It plays a central role in the immune system by presenting peptides derived from extracellular proteins. Class II molecules are expressed in antigen presenting cells (APC: B lymphocytes, dendritic cells, macrophages). The beta chain is approximately 26-28 kDa and its gene contains 6 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, exon 4 encodes the transmembrane domain and exon 5 encodes the cytoplasmic tail. Within the DP molecule both the alpha chain and the beta chain contain the polymorphisms specifying the peptide binding specificities, resulting in up to 4 different molecules.<ref>{{cite web | title = Entrez Gene: HLA-DPB1 major histocompatibility complex, class II, DP beta 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3115| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Mitsunaga S, Kuwata S, Tokunaga K, ''et al.'' |title=Family study on HLA-DPB1 polymorphism: linkage analysis with HLA-DR/DQ and two "new" alleles. |journal=Hum. Immunol. |volume=34 |issue= 3 |pages= 203-11 |year= 1992 |pmid= 1358867 |doi= }}
*{{cite journal | author=Marsh SG, Bodmer JG |title=HLA class II nucleotide sequences, 1992. |journal=Tissue Antigens |volume=40 |issue= 5 |pages= 229-43 |year= 1993 |pmid= 1362295 |doi= }}
*{{cite journal | author=Eiermann TH, Uhl S, Fakler J, Goldmann SF |title=A novel HLA-DPB1 sequence, DPB1*2301. |journal=Tissue Antigens |volume=40 |issue= 2 |pages= 108-10 |year= 1992 |pmid= 1412416 |doi= }}
*{{cite journal | author=Korioth F, Hartung K, Deicher H, Frey J |title=A new HLA-DPB1 allele from a patient with systemic lupus erythematosus. |journal=Tissue Antigens |volume=39 |issue= 4 |pages= 216-9 |year= 1992 |pmid= 1529429 |doi= }}
*{{cite journal | author=de Koster HS, Kenter MJ, D'Amaro J, ''et al.'' |title=Positive correlation between oligonucleotide typing and T-cell recognition of HLA-DP molecules. |journal=Immunogenetics |volume=34 |issue= 1 |pages= 12-22 |year= 1991 |pmid= 1713190 |doi= }}
*{{cite journal | author=Vanderbeeken YE, Duchateau J, Colle H, ''et al.'' |title=Modulation of the HLA class II antigen at a molecular level by maternal serum among cord blood cells and unrelated lymphocytes. |journal=Arch. Gynecol. Obstet. |volume=248 |issue= 4 |pages= 199-209 |year= 1991 |pmid= 1832848 |doi= }}
*{{cite journal | author=Piatier-Tonneau D, Gastinel LN, Amblard F, ''et al.'' |title=Interaction of CD4 with HLA class II antigens and HIV gp120. |journal=Immunogenetics |volume=34 |issue= 2 |pages= 121-8 |year= 1991 |pmid= 1869305 |doi= }}
*{{cite journal | author=Rosenstein Y, Burakoff SJ, Herrmann SH |title=HIV-gp120 can block CD4-class II MHC-mediated adhesion. |journal=J. Immunol. |volume=144 |issue= 2 |pages= 526-31 |year= 1990 |pmid= 1967269 |doi= }}
*{{cite journal | author=Bowman MR, MacFerrin KD, Schreiber SL, Burakoff SJ |title=Identification and structural analysis of residues in the V1 region of CD4 involved in interaction with human immunodeficiency virus envelope glycoprotein gp120 and class II major histocompatibility complex molecules. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 22 |pages= 9052-6 |year= 1991 |pmid= 1978941 |doi= }}
*{{cite journal | author=Bugawan TL, Begovich AB, Erlich HA |title=Rapid HLA-DPB typing using enzymatically amplified DNA and nonradioactive sequence-specific oligonucleotide probes. |journal=Immunogenetics |volume=32 |issue= 4 |pages= 231-41 |year= 1990 |pmid= 2242906 |doi= }}
*{{cite journal | author=Lair B, Alber C, Yu WY, ''et al.'' |title=A newly characterized HLA-DP beta-chain allele. Evidence for DP beta heterogeneity within the DPw4 specificity. |journal=J. Immunol. |volume=141 |issue= 4 |pages= 1353-7 |year= 1988 |pmid= 2456351 |doi= }}
*{{cite journal | author=Bugawan TL, Horn GT, Long CM, ''et al.'' |title=Analysis of HLA-DP allelic sequence polymorphism using the in vitro enzymatic DNA amplification of DP-alpha and DP-beta loci. |journal=J. Immunol. |volume=141 |issue= 11 |pages= 4024-30 |year= 1988 |pmid= 2460556 |doi= }}
*{{cite journal | author=Begovich AB, Bugawan TL, Nepom BS, ''et al.'' |title=A specific HLA-DP beta allele is associated with pauciarticular juvenile rheumatoid arthritis but not adult rheumatoid arthritis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 23 |pages= 9489-93 |year= 1990 |pmid= 2512583 |doi= }}
*{{cite journal | author=Scholl P, Diez A, Mourad W, ''et al.'' |title=Toxic shock syndrome toxin 1 binds to major histocompatibility complex class II molecules. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 11 |pages= 4210-4 |year= 1989 |pmid= 2542966 |doi= }}
*{{cite journal | author=Clayton LK, Sieh M, Pious DA, Reinherz EL |title=Identification of human CD4 residues affecting class II MHC versus HIV-1 gp120 binding. |journal=Nature |volume=339 |issue= 6225 |pages= 548-51 |year= 1989 |pmid= 2543930 |doi= 10.1038/339548a0 }}
*{{cite journal | author=Lee JS, Sartoris S, Briata P, ''et al.'' |title=Sequence polymorphism of HLA-DP beta chains. |journal=Immunogenetics |volume=29 |issue= 5 |pages= 346-9 |year= 1989 |pmid= 2714855 |doi= }}
*{{cite journal | author=Compagnone-Post P, Turco E, Robinson C, Trucco M |title=The beta-chains of DP4 molecules from different haplotypes are encoded by the same gene. |journal=Genomics |volume=2 |issue= 1 |pages= 8-13 |year= 1988 |pmid= 2838415 |doi= }}
*{{cite journal | author=Diamond DC, Sleckman BP, Gregory T, ''et al.'' |title=Inhibition of CD4+ T cell function by the HIV envelope protein, gp120. |journal=J. Immunol. |volume=141 |issue= 11 |pages= 3715-7 |year= 1988 |pmid= 2846691 |doi= }}
*{{cite journal | author=Ando A, Inoko H, Kimura M, ''et al.'' |title=Isolation and allelic polymorphism of cDNA clones and genomic clones of HLA-DP heavy and light chains. |journal=Hum. Immunol. |volume=17 |issue= 3 |pages= 355-67 |year= 1987 |pmid= 2878910 |doi= }}
*{{cite journal | author=Kelly A, Trowsdale J |title=Complete nucleotide sequence of a functional HLA-DP beta gene and the region between the DP beta 1 and DP alpha 1 genes: comparison of the 5' ends of HLA class II genes. |journal=Nucleic Acids Res. |volume=13 |issue= 5 |pages= 1607-21 |year= 1985 |pmid= 2987832 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HPSE... {November 12, 2007 7:44:39 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:45:21 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 = Heparanase
| HGNCid = 5164
| Symbol = HPSE
| AltSymbols =; HPR1; HPA; HPSE1; HSE1
| OMIM = 604724
| ECnumber =
| Homologene = 68528
| MGIid = 1343124
| GeneAtlas_image1 = PBB_GE_HPSE_219403_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004566 |text = beta-glucuronidase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006029 |text = proteoglycan metabolic process}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10855
| Hs_Ensembl = ENSG00000173083
| Hs_RefseqProtein = NP_006656
| Hs_RefseqmRNA = NM_006665
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 84432639
| Hs_GenLoc_end = 84475329
| Hs_Uniprot = Q9Y251
| Mm_EntrezGene = 15442
| Mm_Ensembl = ENSMUSG00000035273
| Mm_RefseqmRNA = XM_982223
| Mm_RefseqProtein = XP_987317
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 100920698
| Mm_GenLoc_end = 100959985
| Mm_Uniprot = Q6YGZ1
}}
}}
'''Heparanase''', also known as '''HPSE''', 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=Zcharia E, Metzger S, Chajek-Shaul T, ''et al.'' |title=Molecular properties and involvement of heparanase in cancer progression and mammary gland morphogenesis. |journal=Journal of mammary gland biology and neoplasia |volume=6 |issue= 3 |pages= 311-22 |year= 2002 |pmid= 11547900 |doi= }}
*{{cite journal | author=Vlodavsky I, Goldshmidt O, Zcharia E, ''et al.'' |title=Mammalian heparanase: involvement in cancer metastasis, angiogenesis and normal development. |journal=Semin. Cancer Biol. |volume=12 |issue= 2 |pages= 121-9 |year= 2003 |pmid= 12027584 |doi= 10.1006/scbi.2001.0420 }}
*{{cite journal | author=Vlodavsky I, Abboud-Jarrous G, Elkin M, ''et al.'' |title=The impact of heparanese and heparin on cancer metastasis and angiogenesis. |journal=Pathophysiol. Haemost. Thromb. |volume=35 |issue= 1-2 |pages= 116-27 |year= 2006 |pmid= 16855356 |doi= 10.1159/000093553 }}
*{{cite journal | author=van den Hoven MJ, Rops AL, Vlodavsky I, ''et al.'' |title=Heparanase in glomerular diseases. |journal=Kidney Int. |volume=72 |issue= 5 |pages= 543-8 |year= 2007 |pmid= 17519955 |doi= 10.1038/sj.ki.5002337 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Pikas DS, Li JP, Vlodavsky I, Lindahl U |title=Substrate specificity of heparanases from human hepatoma and platelets. |journal=J. Biol. Chem. |volume=273 |issue= 30 |pages= 18770-7 |year= 1998 |pmid= 9668050 |doi= }}
*{{cite journal | author=Vlodavsky I, Friedmann Y, Elkin M, ''et al.'' |title=Mammalian heparanase: gene cloning, expression and function in tumor progression and metastasis. |journal=Nat. Med. |volume=5 |issue= 7 |pages= 793-802 |year= 1999 |pmid= 10395325 |doi= 10.1038/10518 }}
*{{cite journal | author=Hulett MD, Freeman C, Hamdorf BJ, ''et al.'' |title=Cloning of mammalian heparanase, an important enzyme in tumor invasion and metastasis. |journal=Nat. Med. |volume=5 |issue= 7 |pages= 803-9 |year= 1999 |pmid= 10395326 |doi= 10.1038/10525 }}
*{{cite journal | author=Kussie PH, Hulmes JD, Ludwig DL, ''et al.'' |title=Cloning and functional expression of a human heparanase gene. |journal=Biochem. Biophys. Res. Commun. |volume=261 |issue= 1 |pages= 183-7 |year= 1999 |pmid= 10405343 |doi= 10.1006/bbrc.1999.0962 }}
*{{cite journal | author=Toyoshima M, Nakajima M |title=Human heparanase. Purification, characterization, cloning, and expression. |journal=J. Biol. Chem. |volume=274 |issue= 34 |pages= 24153-60 |year= 1999 |pmid= 10446189 |doi= }}
*{{cite journal | author=Dempsey LA, Plummer TB, Coombes SL, Platt JL |title=Heparanase expression in invasive trophoblasts and acute vascular damage. |journal=Glycobiology |volume=10 |issue= 5 |pages= 467-75 |year= 2000 |pmid= 10764835 |doi= }}
*{{cite journal | author=Dong J, Kukula AK, Toyoshima M, Nakajima M |title=Genomic organization and chromosome localization of the newly identified human heparanase gene. |journal=Gene |volume=253 |issue= 2 |pages= 171-8 |year= 2000 |pmid= 10940554 |doi= }}
*{{cite journal | author=Hulett MD, Hornby JR, Ohms SJ, ''et al.'' |title=Identification of active-site residues of the pro-metastatic endoglycosidase heparanase. |journal=Biochemistry |volume=39 |issue= 51 |pages= 15659-67 |year= 2001 |pmid= 11123890 |doi= }}
*{{cite journal | author=Ginath S, Menczer J, Friedmann Y, ''et al.'' |title=Expression of heparanase, Mdm2, and erbB2 in ovarian cancer. |journal=Int. J. Oncol. |volume=18 |issue= 6 |pages= 1133-44 |year= 2001 |pmid= 11351242 |doi= }}
*{{cite journal | author=Koliopanos A, Friess H, Kleeff J, ''et al.'' |title=Heparanase expression in primary and metastatic pancreatic cancer. |journal=Cancer Res. |volume=61 |issue= 12 |pages= 4655-9 |year= 2001 |pmid= 11406531 |doi= }}
*{{cite journal | author=Sasaki M, Ito T, Kashima M, ''et al.'' |title=Erythromycin and clarithromycin modulation of growth factor-induced expression of heparanase mRNA on human lung cancer cells in vitro. |journal=Mediators Inflamm. |volume=10 |issue= 5 |pages= 259-67 |year= 2002 |pmid= 11759110 |doi= }}
*{{cite journal | author=Jiang P, Kumar A, Parrillo JE, ''et al.'' |title=Cloning and characterization of the human heparanase-1 (HPR1) gene promoter: role of GA-binding protein and Sp1 in regulating HPR1 basal promoter activity. |journal=J. Biol. Chem. |volume=277 |issue= 11 |pages= 8989-98 |year= 2002 |pmid= 11779847 |doi= 10.1074/jbc.M105682200 }}
*{{cite journal | author=Nadav L, Eldor A, Yacoby-Zeevi O, ''et al.'' |title=Activation, processing and trafficking of extracellular heparanase by primary human fibroblasts. |journal=J. Cell. Sci. |volume=115 |issue= Pt 10 |pages= 2179-87 |year= 2003 |pmid= 11973358 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IL8RB... {November 12, 2007 7:33:10 PM PST}
- SEARCH REDIRECT: Control Box Found: IL8RB {November 12, 2007 7:34:03 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 12, 2007 7:34:06 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 12, 2007 7:34:06 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 12, 2007 7:34:06 PM PST}
- UPDATED: Updated protein page: IL8RB {November 12, 2007 7:34:13 PM PST}
- INFO: Beginning work on ILK... {November 12, 2007 7:34:13 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:34:48 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Integrin-linked kinase
| HGNCid = 6040
| Symbol = ILK
| AltSymbols =; DKFZp686F1765; P59
| OMIM = 602366
| ECnumber =
| Homologene = 3318
| MGIid = 1195267
| GeneAtlas_image1 = PBB_GE_ILK_201234_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:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016301 |text = kinase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005925 |text = focal adhesion}}
| Process = {{GNF_GO|id=GO:0001658 |text = ureteric bud branching}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007160 |text = cell-matrix adhesion}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0045197 |text = establishment and/or maintenance of epithelial cell polarity}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3611
| Hs_Ensembl = ENSG00000166333
| Hs_RefseqProtein = NP_001014794
| Hs_RefseqmRNA = NM_001014794
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 6581540
| Hs_GenLoc_end = 6588673
| Hs_Uniprot = Q13418
| Mm_EntrezGene = 16202
| Mm_Ensembl = ENSMUSG00000030890
| Mm_RefseqmRNA = NM_010562
| Mm_RefseqProtein = NP_034692
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 105610473
| Mm_GenLoc_end = 105616745
| Mm_Uniprot = O55222
}}
}}
'''Integrin-linked kinase''', also known as '''ILK''', 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 = Transduction of extracellular matrix signals through integrins influences intracellular and extracellular functions, and appears to require interaction of integrin cytoplasmic domains with cellular proteins. Integrin-linked kinase (ILK), interacts with the cytoplasmic domain of beta-1 integrin. This gene encodes a serine/threonine protein kinase with 4 ankyrin-like repeats, which associates with the cytoplasmic domain of beta integrins and acts as a proximal receptor kinase regulating integrin-mediated signal transduction. Multiple alternatively spliced transcript variants encoding the same protein have been found for this gene.<ref>{{cite web | title = Entrez Gene: ILK integrin-linked kinase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3611| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Dedhar S |title=Cell-substrate interactions and signaling through ILK. |journal=Curr. Opin. Cell Biol. |volume=12 |issue= 2 |pages= 250-6 |year= 2000 |pmid= 10712922 |doi= }}
*{{cite journal | author=Persad S, Dedhar S |title=The role of integrin-linked kinase (ILK) in cancer progression. |journal=Cancer Metastasis Rev. |volume=22 |issue= 4 |pages= 375-84 |year= 2004 |pmid= 12884912 |doi= }}
*{{cite journal | author=Srivastava D, Yu S |title=Stretching to meet needs: integrin-linked kinase and the cardiac pump. |journal=Genes Dev. |volume=20 |issue= 17 |pages= 2327-31 |year= 2006 |pmid= 16951248 |doi= 10.1101/gad.1472506 }}
*{{cite journal | author=Hannigan GE, Leung-Hagesteijn C, Fitz-Gibbon L, ''et al.'' |title=Regulation of cell adhesion and anchorage-dependent growth by a new beta 1-integrin-linked protein kinase. |journal=Nature |volume=379 |issue= 6560 |pages= 91-6 |year= 1996 |pmid= 8538749 |doi= 10.1038/379091a0 }}
*{{cite journal | author=Hannigan GE, Bayani J, Weksberg R, ''et al.'' |title=Mapping of the gene encoding the integrin-linked kinase, ILK, to human chromosome 11p15.5-p15.4. |journal=Genomics |volume=42 |issue= 1 |pages= 177-9 |year= 1997 |pmid= 9177792 |doi= 10.1006/geno.1997.4719 }}
*{{cite journal | author=Li F, Liu J, Mayne R, Wu C |title=Identification and characterization of a mouse protein kinase that is highly homologous to human integrin-linked kinase. |journal=Biochim. Biophys. Acta |volume=1358 |issue= 3 |pages= 215-20 |year= 1997 |pmid= 9366252 |doi= }}
*{{cite journal | author=Delcommenne M, Tan C, Gray V, ''et al.'' |title=Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 19 |pages= 11211-6 |year= 1998 |pmid= 9736715 |doi= }}
*{{cite journal | author=Chung DH, Lee JI, Kook MC, ''et al.'' |title=ILK (beta1-integrin-linked protein kinase): a novel immunohistochemical marker for Ewing's sarcoma and primitive neuroectodermal tumour. |journal=Virchows Arch. |volume=433 |issue= 2 |pages= 113-7 |year= 1998 |pmid= 9737788 |doi= }}
*{{cite journal | author=Tu Y, Li F, Goicoechea S, Wu C |title=The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells. |journal=Mol. Cell. Biol. |volume=19 |issue= 3 |pages= 2425-34 |year= 1999 |pmid= 10022929 |doi= }}
*{{cite journal | author=Feng J, Ito M, Ichikawa K, ''et al.'' |title=Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase. |journal=J. Biol. Chem. |volume=274 |issue= 52 |pages= 37385-90 |year= 2000 |pmid= 10601309 |doi= }}
*{{cite journal | author=Janji B, Melchior C, Vallar L, Kieffer N |title=Cloning of an isoform of integrin-linked kinase (ILK) that is upregulated in HT-144 melanoma cells following TGF-beta1 stimulation. |journal=Oncogene |volume=19 |issue= 27 |pages= 3069-77 |year= 2000 |pmid= 10871859 |doi= 10.1038/sj.onc.1203640 }}
*{{cite journal | author=Velyvis A, Yang Y, Wu C, Qin J |title=Solution structure of the focal adhesion adaptor PINCH LIM1 domain and characterization of its interaction with the integrin-linked kinase ankyrin repeat domain. |journal=J. Biol. Chem. |volume=276 |issue= 7 |pages= 4932-9 |year= 2001 |pmid= 11078733 |doi= 10.1074/jbc.M007632200 }}
*{{cite journal | author=Matsumoto M, Ogawa W, Hino Y, ''et al.'' |title=Inhibition of insulin-induced activation of Akt by a kinase-deficient mutant of the epsilon isozyme of protein kinase C. |journal=J. Biol. Chem. |volume=276 |issue= 17 |pages= 14400-6 |year= 2001 |pmid= 11278835 |doi= 10.1074/jbc.M011093200 }}
*{{cite journal | author=Nikolopoulos SN, Turner CE |title=Integrin-linked kinase (ILK) binding to paxillin LD1 motif regulates ILK localization to focal adhesions. |journal=J. Biol. Chem. |volume=276 |issue= 26 |pages= 23499-505 |year= 2001 |pmid= 11304546 |doi= 10.1074/jbc.M102163200 }}
*{{cite journal | author=Persad S, Attwell S, Gray V, ''et al.'' |title=Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: critical roles for kinase activity and amino acids arginine 211 and serine 343. |journal=J. Biol. Chem. |volume=276 |issue= 29 |pages= 27462-9 |year= 2001 |pmid= 11313365 |doi= 10.1074/jbc.M102940200 }}
*{{cite journal | author=Tu Y, Huang Y, Zhang Y, ''et al.'' |title=A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading. |journal=J. Cell Biol. |volume=153 |issue= 3 |pages= 585-98 |year= 2001 |pmid= 11331308 |doi= }}
*{{cite journal | author=Leung-Hagesteijn C, Mahendra A, Naruszewicz I, Hannigan GE |title=Modulation of integrin signal transduction by ILKAP, a protein phosphatase 2C associating with the integrin-linked kinase, ILK1. |journal=EMBO J. |volume=20 |issue= 9 |pages= 2160-70 |year= 2001 |pmid= 11331582 |doi= 10.1093/emboj/20.9.2160 }}
*{{cite journal | author=Yamaji S, Suzuki A, Sugiyama Y, ''et al.'' |title=A novel integrin-linked kinase-binding protein, affixin, is involved in the early stage of cell-substrate interaction. |journal=J. Cell Biol. |volume=153 |issue= 6 |pages= 1251-64 |year= 2001 |pmid= 11402068 |doi= }}
*{{cite journal | author=Chen R, Kim O, Yang J, ''et al.'' |title=Regulation of Akt/PKB activation by tyrosine phosphorylation. |journal=J. Biol. Chem. |volume=276 |issue= 34 |pages= 31858-62 |year= 2001 |pmid= 11445557 |doi= 10.1074/jbc.C100271200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KITLG... {November 12, 2007 7:36:21 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:37:25 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
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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_KITLG_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1exz.
| PDB = {{PDB2|1exz}}, {{PDB2|1scf}}
| Name = KIT ligand
| HGNCid = 6343
| Symbol = KITLG
| AltSymbols =; SF; DKFZp686F2250; KL-1; Kitl; MGF; SCF
| OMIM = 184745
| ECnumber =
| Homologene = 692
| MGIid = 96974
| GeneAtlas_image1 = PBB_GE_KITLG_207029_at_tn.png
| GeneAtlas_image2 = PBB_GE_KITLG_211124_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005173 |text = stem cell factor receptor binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0030097 |text = hemopoiesis}} {{GNF_GO|id=GO:0050731 |text = positive regulation of peptidyl-tyrosine phosphorylation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4254
| Hs_Ensembl = ENSG00000049130
| Hs_RefseqProtein = NP_000890
| Hs_RefseqmRNA = NM_000899
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 87410697
| Hs_GenLoc_end = 87498369
| Hs_Uniprot = P21583
| Mm_EntrezGene = 17311
| Mm_Ensembl = ENSMUSG00000019966
| Mm_RefseqmRNA = NM_013598
| Mm_RefseqProtein = NP_038626
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 99445514
| Mm_GenLoc_end = 99518923
| Mm_Uniprot = Q61854
}}
}}
'''KIT ligand''', also known as '''KITLG''', 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 ligand of the tyrosine-kinase receptor encoded by the KIT locus. This ligand is a pleiotropic factor that acts in utero in germ cell and neural cell development, and hematopoiesis, all believed to reflect a role in cell migration. In adults, it functions pleiotropically, while mostly noted for its continued requirement in hematopoiesis. Two transcript variants encoding different isoforms have been found for this gene.<ref>{{cite web | title = Entrez Gene: KITLG KIT ligand| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4254| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Broudy VC |title=Stem cell factor and hematopoiesis. |journal=Blood |volume=90 |issue= 4 |pages= 1345-64 |year= 1997 |pmid= 9269751 |doi= }}
*{{cite journal | author=Andrews RG, Briddell RA, Appelbaum FR, McNiece IK |title=Stimulation of hematopoiesis in vivo by stem cell factor. |journal=Curr. Opin. Hematol. |volume=1 |issue= 3 |pages= 187-96 |year= 1999 |pmid= 9371281 |doi= }}
*{{cite journal | author=Wehrle-Haller B |title=The role of Kit-ligand in melanocyte development and epidermal homeostasis. |journal=Pigment Cell Res. |volume=16 |issue= 3 |pages= 287-96 |year= 2004 |pmid= 12753403 |doi= }}
*{{cite journal | author=Rönnstrand L |title=Signal transduction via the stem cell factor receptor/c-Kit. |journal=Cell. Mol. Life Sci. |volume=61 |issue= 19-20 |pages= 2535-48 |year= 2004 |pmid= 15526160 |doi= 10.1007/s00018-004-4189-6 }}
*{{cite journal | author=Mroczko B, Szmitkowski M |title=Hematopoietic cytokines as tumor markers. |journal=Clin. Chem. Lab. Med. |volume=42 |issue= 12 |pages= 1347-54 |year= 2005 |pmid= 15576295 |doi= 10.1515/CCLM.2004.253 }}
*{{cite journal | author=Lev S, Yarden Y, Givol D |title=A recombinant ectodomain of the receptor for the stem cell factor (SCF) retains ligand-induced receptor dimerization and antagonizes SCF-stimulated cellular responses. |journal=J. Biol. Chem. |volume=267 |issue= 15 |pages= 10866-73 |year= 1992 |pmid= 1375232 |doi= }}
*{{cite journal | author=Huang EJ, Nocka KH, Buck J, Besmer P |title=Differential expression and processing of two cell associated forms of the kit-ligand: KL-1 and KL-2. |journal=Mol. Biol. Cell |volume=3 |issue= 3 |pages= 349-62 |year= 1992 |pmid= 1378327 |doi= }}
*{{cite journal | author=Toyota M, Hinoda Y, Itoh F, ''et al.'' |title=Expression of two types of kit ligand mRNAs in human tumor cells. |journal=Int. J. Hematol. |volume=55 |issue= 3 |pages= 301-4 |year= 1992 |pmid= 1379846 |doi= }}
*{{cite journal | author=Lu HS, Clogston CL, Wypych J, ''et al.'' |title=Post-translational processing of membrane-associated recombinant human stem cell factor expressed in Chinese hamster ovary cells. |journal=Arch. Biochem. Biophys. |volume=298 |issue= 1 |pages= 150-8 |year= 1992 |pmid= 1381905 |doi= }}
*{{cite journal | author=Sharkey A, Jones DS, Brown KD, Smith SK |title=Expression of messenger RNA for kit-ligand in human placenta: localization by in situ hybridization and identification of alternatively spliced variants. |journal=Mol. Endocrinol. |volume=6 |issue= 8 |pages= 1235-41 |year= 1992 |pmid= 1383693 |doi= }}
*{{cite journal | author=Mathew S, Murty VV, Hunziker W, Chaganti RS |title=Subregional mapping of 13 single-copy genes on the long arm of chromosome 12 by fluorescence in situ hybridization. |journal=Genomics |volume=14 |issue= 3 |pages= 775-9 |year= 1992 |pmid= 1427906 |doi= }}
*{{cite journal | author=Geissler EN, Liao M, Brook JD, ''et al.'' |title=Stem cell factor (SCF), a novel hematopoietic growth factor and ligand for c-kit tyrosine kinase receptor, maps on human chromosome 12 between 12q14.3 and 12qter. |journal=Somat. Cell Mol. Genet. |volume=17 |issue= 2 |pages= 207-14 |year= 1991 |pmid= 1707188 |doi= }}
*{{cite journal | author=Anderson DM, Williams DE, Tushinski R, ''et al.'' |title=Alternate splicing of mRNAs encoding human mast cell growth factor and localization of the gene to chromosome 12q22-q24. |journal=Cell Growth Differ. |volume=2 |issue= 8 |pages= 373-8 |year= 1992 |pmid= 1724381 |doi= }}
*{{cite journal | author=Martin FH, Suggs SV, Langley KE, ''et al.'' |title=Primary structure and functional expression of rat and human stem cell factor DNAs. |journal=Cell |volume=63 |issue= 1 |pages= 203-11 |year= 1990 |pmid= 2208279 |doi= }}
*{{cite journal | author=Ramenghi U, Ruggieri L, Dianzani I, ''et al.'' |title=Human peripheral blood granulocytes and myeloid leukemic cell lines express both transcripts encoding for stem cell factor. |journal=Stem Cells |volume=12 |issue= 5 |pages= 521-6 |year= 1995 |pmid= 7528592 |doi= }}
*{{cite journal | author=Saito S, Enomoto M, Sakakura S, ''et al.'' |title=Localization of stem cell factor (SCF) and c-kit mRNA in human placental tissue and biological effects of SCF on DNA synthesis in primary cultured cytotrophoblasts. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 3 |pages= 1762-9 |year= 1995 |pmid= 7529021 |doi= 10.1006/bbrc.1994.2873 }}
*{{cite journal | author=Laitinen M, Rutanen EM, Ritvos O |title=Expression of c-kit ligand messenger ribonucleic acids in human ovaries and regulation of their steady state levels by gonadotropins in cultured granulosa-luteal cells. |journal=Endocrinology |volume=136 |issue= 10 |pages= 4407-14 |year= 1995 |pmid= 7545103 |doi= }}
*{{cite journal | author=Blechman JM, Lev S, Brizzi MF, ''et al.'' |title=Soluble c-kit proteins and antireceptor monoclonal antibodies confine the binding site of the stem cell factor. |journal=J. Biol. Chem. |volume=268 |issue= 6 |pages= 4399-406 |year= 1993 |pmid= 7680037 |doi= }}
*{{cite journal | author=Lu HS, Jones MD, Shieh JH, ''et al.'' |title=Isolation and characterization of a disulfide-linked human stem cell factor dimer. Biochemical, biophysical, and biological comparison to the noncovalently held dimer. |journal=J. Biol. Chem. |volume=271 |issue= 19 |pages= 11309-16 |year= 1996 |pmid= 8626683 |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= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KRT8... {November 12, 2007 7:34:48 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:35:36 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Keratin 8
| HGNCid = 6446
| Symbol = KRT8
| AltSymbols =; K8; CARD2; CK8; CYK8; K2C8; KO
| OMIM = 148060
| ECnumber =
| Homologene = 55643
| MGIid = 96705
| Function = {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005882 |text = intermediate filament}}
| Process = {{GNF_GO|id=GO:0007010 |text = cytoskeleton organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3856
| Hs_Ensembl =
| Hs_RefseqProtein = NP_002264
| Hs_RefseqmRNA = NM_002273
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 16691
| Mm_Ensembl = ENSMUSG00000049382
| Mm_RefseqmRNA = NM_031170
| Mm_RefseqProtein = NP_112447
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 101824745
| Mm_GenLoc_end = 101832348
| Mm_Uniprot = P11679
}}
}}
'''Keratin 8''', also known as '''KRT8''', 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=Moll R, Franke WW, Schiller DL, ''et al.'' |title=The catalog of human cytokeratins: patterns of expression in normal epithelia, tumors and cultured cells. |journal=Cell |volume=31 |issue= 1 |pages= 11-24 |year= 1983 |pmid= 6186379 |doi= }}
*{{cite journal | author=Ljubimov AV, Bartek J, Couchman JR, ''et al.'' |title=Distribution of individual components of basement membrane in human colon polyps and adenocarcinomas as revealed by monoclonal antibodies. |journal=Int. J. Cancer |volume=50 |issue= 4 |pages= 562-6 |year= 1992 |pmid= 1371500 |doi= }}
*{{cite journal | author=Smedts F, Ramaekers F, Robben H, ''et al.'' |title=Changing patterns of keratin expression during progression of cervical intraepithelial neoplasia. |journal=Am. J. Pathol. |volume=136 |issue= 3 |pages= 657-68 |year= 1990 |pmid= 1690513 |doi= }}
*{{cite journal | author=Krauss S, Franke WW |title=Organization and sequence of the human gene encoding cytokeratin 8. |journal=Gene |volume=86 |issue= 2 |pages= 241-9 |year= 1990 |pmid= 1691124 |doi= }}
*{{cite journal | author=Yamamoto R, Kao LC, McKnight CE, Strauss JF |title=Cloning and sequence of cDNA for human placental cytokeratin 8. Regulation of the mRNA in trophoblastic cells by cAMP. |journal=Mol. Endocrinol. |volume=4 |issue= 3 |pages= 370-4 |year= 1990 |pmid= 1692965 |doi= }}
*{{cite journal | author=Waseem A, Alexander CM, Steel JB, Lane EB |title=Embryonic simple epithelial keratins 8 and 18: chromosomal location emphasizes difference from other keratin pairs. |journal=New Biol. |volume=2 |issue= 5 |pages= 464-78 |year= 1991 |pmid= 1705144 |doi= }}
*{{cite journal | author=Tsubura A, Okada H, Sasaki M, ''et al.'' |title=Immunohistochemical demonstration of keratins 8 and 14 in benign tumours of the skin appendage. |journal=Virchows Archiv. A, Pathological anatomy and histopathology |volume=418 |issue= 6 |pages= 503-7 |year= 1991 |pmid= 1711732 |doi= }}
*{{cite journal | author=Leube RE, Bosch FX, Romano V, ''et al.'' |title=Cytokeratin expression in simple epithelia. III. Detection of mRNAs encoding human cytokeratins nos. 8 and 18 in normal and tumor cells by hybridization with cDNA sequences in vitro and in situ. |journal=Differentiation |volume=33 |issue= 1 |pages= 69-85 |year= 1987 |pmid= 2434381 |doi= }}
*{{cite journal | author=Guelstein VI, Tchypysheva TA, Ermilova VD, ''et al.'' |title=Monoclonal antibody mapping of keratins 8 and 17 and of vimentin in normal human mammary gland, benign tumors, dysplasias and breast cancer. |journal=Int. J. Cancer |volume=42 |issue= 2 |pages= 147-53 |year= 1988 |pmid= 2456993 |doi= }}
*{{cite journal | author=Osborn M, Mazzoleni G, Santini D, ''et al.'' |title=Villin, intestinal brush border hydrolases and keratin polypeptides in intestinal metaplasia and gastric cancer; an immunohistologic study emphasizing the different degrees of intestinal and gastric differentiation in signet ring cell carcinomas. |journal=Virchows Archiv. A, Pathological anatomy and histopathology |volume=413 |issue= 4 |pages= 303-12 |year= 1988 |pmid= 2459839 |doi= }}
*{{cite journal | author=Fisher HP, Doppl W, Osborn M, Altmannsberger M |title=Evidence for a hepatocellular lineage in a combined hepatocellular-cholangiocarcinoma of transitional type. |journal=Virchows Arch., B, Cell Pathol. |volume=56 |issue= 2 |pages= 71-6 |year= 1989 |pmid= 2467436 |doi= }}
*{{cite journal | author=Kulesh DA, Ceceña G, Darmon YM, ''et al.'' |title=Posttranslational regulation of keratins: degradation of mouse and human keratins 18 and 8. |journal=Mol. Cell. Biol. |volume=9 |issue= 4 |pages= 1553-65 |year= 1989 |pmid= 2471065 |doi= }}
*{{cite journal | author=Gel'shteĭn VI, Chipysheva TA, Ermilova VD, Bannikov GA |title=[The expression of keratins Nos. 8, 17 and vimentin in pleomorphic adenoma of the salivary glands] |journal=Arkh. Patol. |volume=51 |issue= 10 |pages= 28-35 |year= 1990 |pmid= 2482017 |doi= }}
*{{cite journal | author=Eichbaum QG, Beatty DW, Parker MI |title=Identification of cardiac autoantigens in human heart cDNA libraries using acute rheumatic fever sera. |journal=J. Autoimmun. |volume=7 |issue= 2 |pages= 243-61 |year= 1994 |pmid= 8037842 |doi= 10.1006/jaut.1994.1019 }}
*{{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=Ku NO, Omary MB |title=Phosphorylation of human keratin 8 in vivo at conserved head domain serine 23 and at epidermal growth factor-stimulated tail domain serine 431. |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 7556-64 |year= 1997 |pmid= 9054461 |doi= }}
*{{cite journal | author=Ji H, Reid GE, Moritz RL, ''et al.'' |title=A two-dimensional gel database of human colon carcinoma proteins. |journal=Electrophoresis |volume=18 |issue= 3-4 |pages= 605-13 |year= 1997 |pmid= 9150948 |doi= 10.1002/elps.1150180344 }}
*{{cite journal | author=Liao J, Ku NO, Omary MB |title=Stress, apoptosis, and mitosis induce phosphorylation of human keratin 8 at Ser-73 in tissues and cultured cells. |journal=J. Biol. Chem. |volume=272 |issue= 28 |pages= 17565-73 |year= 1997 |pmid= 9211903 |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= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LHCGR... {November 12, 2007 7:35:36 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:36:21 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Luteinizing hormone/choriogonadotropin receptor
| HGNCid = 6585
| Symbol = LHCGR
| AltSymbols =; LHR; LCGR; LGR2; hLHR
| OMIM = 152790
| ECnumber =
| Homologene = 37276
| MGIid = 96783
| GeneAtlas_image1 = PBB_GE_LHCGR_207240_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004964 |text = lutropin-choriogonadotropic hormone receptor activity}}
| Component = {{GNF_GO|id=GO:0005768 |text = endosome}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007187 |text = G-protein signaling, coupled to cyclic nucleotide second messenger}} {{GNF_GO|id=GO:0008584 |text = male gonad development}} {{GNF_GO|id=GO:0030539 |text = male genitalia development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3973
| Hs_Ensembl = ENSG00000138039
| Hs_RefseqProtein = NP_000224
| Hs_RefseqmRNA = NM_000233
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 48768340
| Hs_GenLoc_end = 48836314
| Hs_Uniprot = P22888
| Mm_EntrezGene = 16867
| Mm_Ensembl = ENSMUSG00000024107
| Mm_RefseqmRNA = NM_013582
| Mm_RefseqProtein = NP_038610
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 88649875
| Mm_GenLoc_end = 88700302
| Mm_Uniprot = P30730
}}
}}
'''Luteinizing hormone/choriogonadotropin receptor''', also known as '''LHCGR''', 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 = LHCGR encodes the receptor for both luteinizing hormone and choriogonadotropin. Mutations in this gonadotropin receptor result in disorders of male secondary sexual character development, such as familial male precocious puberty and male pseudohermaphtoditism.<ref>{{cite web | title = Entrez Gene: LHCGR luteinizing hormone/choriogonadotropin receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3973| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ji TH, Ryu KS, Gilchrist R, Ji I |title=Interaction, signal generation, signal divergence, and signal transduction of LH/CG and the receptor. |journal=Recent Prog. Horm. Res. |volume=52 |issue= |pages= 431-53; discussion 454 |year= 1997 |pmid= 9238862 |doi= }}
*{{cite journal | author=Dufau ML |title=The luteinizing hormone receptor. |journal=Annu. Rev. Physiol. |volume=60 |issue= |pages= 461-96 |year= 1998 |pmid= 9558473 |doi= 10.1146/annurev.physiol.60.1.461 }}
*{{cite journal | author=Ascoli M, Fanelli F, Segaloff DL |title=The lutropin/choriogonadotropin receptor, a 2002 perspective. |journal=Endocr. Rev. |volume=23 |issue= 2 |pages= 141-74 |year= 2002 |pmid= 11943741 |doi= }}
*{{cite journal | author=Amsterdam A, Hanoch T, Dantes A, ''et al.'' |title=Mechanisms of gonadotropin desensitization. |journal=Mol. Cell. Endocrinol. |volume=187 |issue= 1-2 |pages= 69-74 |year= 2003 |pmid= 11988313 |doi= }}
*{{cite journal | author=Fanelli F, Puett D |title=Structural aspects of luteinizing hormone receptor: information from molecular modeling and mutagenesis. |journal=Endocrine |volume=18 |issue= 3 |pages= 285-93 |year= 2003 |pmid= 12450321 |doi= }}
*{{cite journal | author=Latronico AC, Segaloff DL |title=Insights learned from L457(3.43)R, an activating mutant of the human lutropin receptor. |journal=Mol. Cell. Endocrinol. |volume=260-262 |issue= |pages= 287-93 |year= 2007 |pmid= 17055147 |doi= 10.1016/j.mce.2005.11.053 }}
*{{cite journal | author=Nagayama Y, Russo D, Wadsworth HL, ''et al.'' |title=Eleven amino acids (Lys-201 to Lys-211) and 9 amino acids (Gly-222 to Leu-230) in the human thyrotropin receptor are involved in ligand binding. |journal=J. Biol. Chem. |volume=266 |issue= 23 |pages= 14926-30 |year= 1991 |pmid= 1651314 |doi= }}
*{{cite journal | author=Jia XC, Oikawa M, Bo M, ''et al.'' |title=Expression of human luteinizing hormone (LH) receptor: interaction with LH and chorionic gonadotropin from human but not equine, rat, and ovine species. |journal=Mol. Endocrinol. |volume=5 |issue= 6 |pages= 759-68 |year= 1991 |pmid= 1922095 |doi= }}
*{{cite journal | author=Minegishi T, Nakamura K, Takakura Y, ''et al.'' |title=Cloning and sequencing of human LH/hCG receptor cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=172 |issue= 3 |pages= 1049-54 |year= 1990 |pmid= 2244890 |doi= }}
*{{cite journal | author=Rousseau-Merck MF, Misrahi M, Atger M, ''et al.'' |title=Localization of the human luteinizing hormone/choriogonadotropin receptor gene (LHCGR) to chromosome 2p21. |journal=Cytogenet. Cell Genet. |volume=54 |issue= 1-2 |pages= 77-9 |year= 1991 |pmid= 2249480 |doi= }}
*{{cite journal | author=Xie YB, Wang H, Segaloff DL |title=Extracellular domain of lutropin/choriogonadotropin receptor expressed in transfected cells binds choriogonadotropin with high affinity. |journal=J. Biol. Chem. |volume=265 |issue= 35 |pages= 21411-4 |year= 1991 |pmid= 2254302 |doi= }}
*{{cite journal | author=Frazier AL, Robbins LS, Stork PJ, ''et al.'' |title=Isolation of TSH and LH/CG receptor cDNAs from human thyroid: regulation by tissue specific splicing. |journal=Mol. Endocrinol. |volume=4 |issue= 8 |pages= 1264-76 |year= 1991 |pmid= 2293030 |doi= }}
*{{cite journal | author=Keutmann HT, Charlesworth MC, Mason KA, ''et al.'' |title=A receptor-binding region in human choriogonadotropin/lutropin beta subunit. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 7 |pages= 2038-42 |year= 1987 |pmid= 3470775 |doi= }}
*{{cite journal | author=Atger M, Misrahi M, Sar S, ''et al.'' |title=Structure of the human luteinizing hormone-choriogonadotropin receptor gene: unusual promoter and 5' non-coding regions. |journal=Mol. Cell. Endocrinol. |volume=111 |issue= 2 |pages= 113-23 |year= 1995 |pmid= 7556872 |doi= }}
*{{cite journal | author=Latronico AC, Anasti J, Arnhold IJ, ''et al.'' |title=A novel mutation of the luteinizing hormone receptor gene causing male gonadotropin-independent precocious puberty. |journal=J. Clin. Endocrinol. Metab. |volume=80 |issue= 8 |pages= 2490-4 |year= 1995 |pmid= 7629248 |doi= }}
*{{cite journal | author=Shenker A, Laue L, Kosugi S, ''et al.'' |title=A constitutively activating mutation of the luteinizing hormone receptor in familial male precocious puberty. |journal=Nature |volume=365 |issue= 6447 |pages= 652-4 |year= 1993 |pmid= 7692306 |doi= 10.1038/365652a0 }}
*{{cite journal | author=Yano K, Saji M, Hidaka A, ''et al.'' |title=A new constitutively activating point mutation in the luteinizing hormone/choriogonadotropin receptor gene in cases of male-limited precocious puberty. |journal=J. Clin. Endocrinol. Metab. |volume=80 |issue= 4 |pages= 1162-8 |year= 1995 |pmid= 7714085 |doi= }}
*{{cite journal | author=Kremer H, Kraaij R, Toledo SP, ''et al.'' |title=Male pseudohermaphroditism due to a homozygous missense mutation of the luteinizing hormone receptor gene. |journal=Nat. Genet. |volume=9 |issue= 2 |pages= 160-4 |year= 1995 |pmid= 7719343 |doi= 10.1038/ng0295-160 }}
*{{cite journal | author=Kosugi S, Van Dop C, Geffner ME, ''et al.'' |title=Characterization of heterogeneous mutations causing constitutive activation of the luteinizing hormone receptor in familial male precocious puberty. |journal=Hum. Mol. Genet. |volume=4 |issue= 2 |pages= 183-8 |year= 1995 |pmid= 7757065 |doi= }}
*{{cite journal | author=Kremer H, Mariman E, Otten BJ, ''et al.'' |title=Cosegregation of missense mutations of the luteinizing hormone receptor gene with familial male-limited precocious puberty. |journal=Hum. Mol. Genet. |volume=2 |issue= 11 |pages= 1779-83 |year= 1994 |pmid= 8281137 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NCOA3... {November 12, 2007 7:41:34 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:42:47 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
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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_NCOA3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1kbh.
| PDB = {{PDB2|1kbh}}
| Name = Nuclear receptor coactivator 3
| HGNCid = 7670
| Symbol = NCOA3
| AltSymbols =; RAC3; ACTR; AIB-1; AIB1; CAGH16; CTG26; MGC141848; SRC-1; SRC3; TNRC14; TNRC16; TRAM-1; pCIP
| OMIM = 601937
| ECnumber =
| Homologene = 4764
| MGIid = 1276535
| GeneAtlas_image1 = PBB_GE_NCOA3_207700_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_NCOA3_209060_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_NCOA3_209062_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0004402 |text = histone acetyltransferase activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008415 |text = acyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0030528 |text = transcription regulator activity}} {{GNF_GO|id=GO:0046966 |text = thyroid hormone receptor binding}} {{GNF_GO|id=GO:0050681 |text = androgen receptor binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0030521 |text = androgen receptor signaling pathway}} {{GNF_GO|id=GO:0045893 |text = positive regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8202
| Hs_Ensembl = ENSG00000124151
| Hs_RefseqProtein = NP_006525
| Hs_RefseqmRNA = NM_006534
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 45564053
| Hs_GenLoc_end = 45717938
| Hs_Uniprot = Q9Y6Q9
| Mm_EntrezGene = 17979
| Mm_Ensembl = ENSMUSG00000027678
| Mm_RefseqmRNA = NM_008679
| Mm_RefseqProtein = NP_032705
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 165683882
| Mm_GenLoc_end = 165762141
| Mm_Uniprot = O09000
}}
}}
'''Nuclear receptor coactivator 3''', also known as '''NCOA3''', 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 nuclear receptor coactivator that interacts with nuclear hormone receptors to enhance their transcriptional activator functions. The encoded protein has histone acetyltransferase activity and recruits p300/CBP-associated factor and CREB binding protein as part of a multisubunit coactivation complex. This protein is initially found in the cytoplasm but is translocated into the nucleus upon phosphorylation. Two transcript variants encoding different isoforms have been found for this gene. In addition, a polymorphic repeat region is found in the C-terminus of the encoded protein.<ref>{{cite web | title = Entrez Gene: NCOA3 nuclear receptor coactivator 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8202| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Liao L, Kuang SQ, Yuan Y, ''et al.'' |title=Molecular structure and biological function of the cancer-amplified nuclear receptor coactivator SRC-3/AIB1. |journal=J. Steroid Biochem. Mol. Biol. |volume=83 |issue= 1-5 |pages= 3-14 |year= 2003 |pmid= 12650696 |doi= }}
*{{cite journal | author=Liu F, Ventura F, Doody J, Massagué J |title=Human type II receptor for bone morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs. |journal=Mol. Cell. Biol. |volume=15 |issue= 7 |pages= 3479-86 |year= 1995 |pmid= 7791754 |doi= }}
*{{cite journal | author=Guan XY, Xu J, Anzick SL, ''et al.'' |title=Hybrid selection of transcribed sequences from microdissected DNA: isolation of genes within amplified region at 20q11-q13.2 in breast cancer. |journal=Cancer Res. |volume=56 |issue= 15 |pages= 3446-50 |year= 1996 |pmid= 8758910 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Margolis RL, Abraham MR, Gatchell SB, ''et al.'' |title=cDNAs with long CAG trinucleotide repeats from human brain. |journal=Hum. Genet. |volume=100 |issue= 1 |pages= 114-22 |year= 1997 |pmid= 9225980 |doi= }}
*{{cite journal | author=Li H, Gomes PJ, Chen JD |title=RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 16 |pages= 8479-84 |year= 1997 |pmid= 9238002 |doi= }}
*{{cite journal | author=Anzick SL, Kononen J, Walker RL, ''et al.'' |title=AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer. |journal=Science |volume=277 |issue= 5328 |pages= 965-8 |year= 1997 |pmid= 9252329 |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=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=Shirazi SK, Bober MA, Coetzee GA |title=Polymorphic exonic CAG microsatellites in the gene amplified in breast cancer (AIB1 gene). |journal=Clin. Genet. |volume=54 |issue= 1 |pages= 102-3 |year= 1998 |pmid= 9727751 |doi= }}
*{{cite journal | author=Wang JC, Stafford JM, Granner DK |title=SRC-1 and GRIP1 coactivate transcription with hepatocyte nuclear factor 4. |journal=J. Biol. Chem. |volume=273 |issue= 47 |pages= 30847-50 |year= 1998 |pmid= 9812974 |doi= }}
*{{cite journal | author=Zwijsen RM, Buckle RS, Hijmans EM, ''et al.'' |title=Ligand-independent recruitment of steroid receptor coactivators to estrogen receptor by cyclin D1. |journal=Genes Dev. |volume=12 |issue= 22 |pages= 3488-98 |year= 1999 |pmid= 9832502 |doi= }}
*{{cite journal | author=Chen H, Lin RJ, Xie W, ''et al.'' |title=Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase. |journal=Cell |volume=98 |issue= 5 |pages= 675-86 |year= 1999 |pmid= 10490106 |doi= }}
*{{cite journal | author=Ebisawa T, Tada K, Kitajima I, ''et al.'' |title=Characterization of bone morphogenetic protein-6 signaling pathways in osteoblast differentiation. |journal=J. Cell. Sci. |volume=112 ( Pt 20) |issue= |pages= 3519-27 |year= 2000 |pmid= 10504300 |doi= }}
*{{cite journal | author=Xie W, Hong H, Yang NN, ''et al.'' |title=Constitutive activation of transcription and binding of coactivator by estrogen-related receptors 1 and 2. |journal=Mol. Endocrinol. |volume=13 |issue= 12 |pages= 2151-62 |year= 2000 |pmid= 10598588 |doi= }}
*{{cite journal | author=Pao GM, Janknecht R, Ruffner H, ''et al.'' |title=CBP/p300 interact with and function as transcriptional coactivators of BRCA1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 3 |pages= 1020-5 |year= 2000 |pmid= 10655477 |doi= }}
*{{cite journal | author=Leo C, Li H, Chen JD |title=Differential mechanisms of nuclear receptor regulation by receptor-associated coactivator 3. |journal=J. Biol. Chem. |volume=275 |issue= 8 |pages= 5976-82 |year= 2000 |pmid= 10681591 |doi= }}
*{{cite journal | author=Font de Mora J, Brown M |title=AIB1 is a conduit for kinase-mediated growth factor signaling to the estrogen receptor. |journal=Mol. Cell. Biol. |volume=20 |issue= 14 |pages= 5041-7 |year= 2000 |pmid= 10866661 |doi= }}
*{{cite journal | author=Tan JA, Hall SH, Petrusz P, French FS |title=Thyroid receptor activator molecule, TRAM-1, is an androgen receptor coactivator. |journal=Endocrinology |volume=141 |issue= 9 |pages= 3440-50 |year= 2000 |pmid= 10965917 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PTGS1... {November 12, 2007 7:37:25 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:38:28 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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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_PTGS1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cqe.
| PDB = {{PDB2|1cqe}}, {{PDB2|1diy}}, {{PDB2|1ebv}}, {{PDB2|1eqg}}, {{PDB2|1eqh}}, {{PDB2|1fe2}}, {{PDB2|1ht5}}, {{PDB2|1ht8}}, {{PDB2|1igx}}, {{PDB2|1igz}}, {{PDB2|1pge}}, {{PDB2|1pgf}}, {{PDB2|1pgg}}, {{PDB2|1prh}}, {{PDB2|1pth}}, {{PDB2|1q4g}}, {{PDB2|1u67}}, {{PDB2|2ayl}}
| Name = Prostaglandin-endoperoxide synthase 1 (prostaglandin G/H synthase and cyclooxygenase)
| HGNCid = 9604
| Symbol = PTGS1
| AltSymbols =; COX1; COX3; PCOX1; PGG/HS; PGHS-1; PGHS1; PHS1; PTGHS
| OMIM = 176805
| ECnumber =
| Homologene = 743
| MGIid = 97797
| GeneAtlas_image1 = PBB_GE_PTGS1_215813_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PTGS1_205127_at_tn.png
| GeneAtlas_image3 = PBB_GE_PTGS1_205128_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004601 |text = peroxidase activity}} {{GNF_GO|id=GO:0004666 |text = prostaglandin-endoperoxide synthase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0016702 |text = oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0001516 |text = prostaglandin biosynthetic process}} {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006633 |text = fatty acid biosynthetic process}} {{GNF_GO|id=GO:0008217 |text = blood pressure regulation}} {{GNF_GO|id=GO:0030216 |text = keratinocyte differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5742
| Hs_Ensembl = ENSG00000095303
| Hs_RefseqProtein = NP_000953
| Hs_RefseqmRNA = NM_000962
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 124173050
| Hs_GenLoc_end = 124197802
| Hs_Uniprot = P23219
| Mm_EntrezGene = 19224
| Mm_Ensembl = ENSMUSG00000047250
| Mm_RefseqmRNA = NM_008969
| Mm_RefseqProtein = NP_032995
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 36052509
| Mm_GenLoc_end = 36074278
| Mm_Uniprot = Q3TJN9
}}
}}
'''Prostaglandin-endoperoxide synthase 1 (prostaglandin G/H synthase and cyclooxygenase)''', also known as '''PTGS1''', 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 = Prostaglandin-endoperoxide synthase (PTGS), also known as cyclooxygenase, is the key enzyme in prostaglandin biosynthesis, and acts both as a dioxygenase and as a peroxidase. There are two isozymes of PTGS: a constitutive PTGS1 and an inducible PTGS2, which differ in their regulation of expression and tissue distribution. This gene encodes PTGS1, which regulates angiogenesis in endothelial cells, and is inhibited by nonsteroidal anti-inflammatory drugs such as aspirin. PTGS1 is thought to be involved in cell-cell signaling and maintaining tissue homeostasis. Alternative splicing of this gene generates two transcript variants. The expression of these two transcripts is differentially regulated by relevant cytokines and growth factors.<ref>{{cite web | title = Entrez Gene: PTGS1 prostaglandin-endoperoxide synthase 1 (prostaglandin G/H synthase and cyclooxygenase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5742| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Richards JA, Petrel TA, Brueggemeier RW |title=Signaling pathways regulating aromatase and cyclooxygenases in normal and malignant breast cells. |journal=J. Steroid Biochem. Mol. Biol. |volume=80 |issue= 2 |pages= 203-12 |year= 2002 |pmid= 11897504 |doi= }}
*{{cite journal | author=Jain S, Khuri FR, Shin DM |title=Prevention of head and neck cancer: current status and future prospects. |journal=Current problems in cancer |volume=28 |issue= 5 |pages= 265-86 |year= 2004 |pmid= 15375804 |doi= }}
*{{cite journal | author=Bingham S, Beswick PJ, Blum DE, ''et al.'' |title=The role of the cylooxygenase pathway in nociception and pain. |journal=Semin. Cell Dev. Biol. |volume=17 |issue= 5 |pages= 544-54 |year= 2007 |pmid= 17071117 |doi= 10.1016/j.semcdb.2006.09.001 }}
*{{cite journal | author=Diaz A, Reginato AM, Jimenez SA |title=Alternative splicing of human prostaglandin G/H synthase mRNA and evidence of differential regulation of the resulting transcripts by transforming growth factor beta 1, interleukin 1 beta, and tumor necrosis factor alpha. |journal=J. Biol. Chem. |volume=267 |issue= 15 |pages= 10816-22 |year= 1992 |pmid= 1587858 |doi= }}
*{{cite journal | author=Takahashi Y, Ueda N, Yoshimoto T, ''et al.'' |title=Immunoaffinity purification and cDNA cloning of human platelet prostaglandin endoperoxide synthase (cyclooxygenase). |journal=Biochem. Biophys. Res. Commun. |volume=182 |issue= 2 |pages= 433-8 |year= 1992 |pmid= 1734857 |doi= }}
*{{cite journal | author=Funk CD, Funk LB, Kennedy ME, ''et al.'' |title=Human platelet/erythroleukemia cell prostaglandin G/H synthase: cDNA cloning, expression, and gene chromosomal assignment. |journal=FASEB J. |volume=5 |issue= 9 |pages= 2304-12 |year= 1991 |pmid= 1907252 |doi= }}
*{{cite journal | author=Yokoyama C, Tanabe T |title=Cloning of human gene encoding prostaglandin endoperoxide synthase and primary structure of the enzyme. |journal=Biochem. Biophys. Res. Commun. |volume=165 |issue= 2 |pages= 888-94 |year= 1990 |pmid= 2512924 |doi= }}
*{{cite journal | author=Vane JR, Mitchell JA, Appleton I, ''et al.'' |title=Inducible isoforms of cyclooxygenase and nitric-oxide synthase in inflammation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 6 |pages= 2046-50 |year= 1994 |pmid= 7510883 |doi= }}
*{{cite journal | author=Mollace V, Colasanti M, Rodino P, ''et al.'' |title=HIV coating gp 120 glycoprotein-dependent prostaglandin E2 release by human cultured astrocytoma cells is regulated by nitric oxide formation. |journal=Biochem. Biophys. Res. Commun. |volume=203 |issue= 1 |pages= 87-92 |year= 1994 |pmid= 7521167 |doi= 10.1006/bbrc.1994.2152 }}
*{{cite journal | author=Inoue H, Yokoyama C, Hara S, ''et al.'' |title=Transcriptional regulation of human prostaglandin-endoperoxide synthase-2 gene by lipopolysaccharide and phorbol ester in vascular endothelial cells. Involvement of both nuclear factor for interleukin-6 expression site and cAMP response element. |journal=J. Biol. Chem. |volume=270 |issue= 42 |pages= 24965-71 |year= 1995 |pmid= 7559624 |doi= }}
*{{cite journal | author=Ren Y, Loose-Mitchell DS, Kulmacz RJ |title=Prostaglandin H synthase-1: evaluation of C-terminus function. |journal=Arch. Biochem. Biophys. |volume=316 |issue= 2 |pages= 751-7 |year= 1995 |pmid= 7864630 |doi= }}
*{{cite journal | author=Picot D, Loll PJ, Garavito RM |title=The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1. |journal=Nature |volume=367 |issue= 6460 |pages= 243-9 |year= 1994 |pmid= 8121489 |doi= 10.1038/367243a0 }}
*{{cite journal | author=Kosaka T, Miyata A, Ihara H, ''et al.'' |title=Characterization of the human gene (PTGS2) encoding prostaglandin-endoperoxide synthase 2. |journal=Eur. J. Biochem. |volume=221 |issue= 3 |pages= 889-97 |year= 1994 |pmid= 8181472 |doi= }}
*{{cite journal | author=Otto JC, DeWitt DL, Smith WL |title=N-glycosylation of prostaglandin endoperoxide synthases-1 and -2 and their orientations in the endoplasmic reticulum. |journal=J. Biol. Chem. |volume=268 |issue= 24 |pages= 18234-42 |year= 1993 |pmid= 8349699 |doi= }}
*{{cite journal | author=O'Neill GP, Ford-Hutchinson AW |title=Expression of mRNA for cyclooxygenase-1 and cyclooxygenase-2 in human tissues. |journal=FEBS Lett. |volume=330 |issue= 2 |pages= 156-60 |year= 1993 |pmid= 8365485 |doi= }}
*{{cite journal | author=Corasaniti MT, Melino G, Navarra M, ''et al.'' |title=Death of cultured human neuroblastoma cells induced by HIV-1 gp120 is prevented by NMDA receptor antagonists and inhibitors of nitric oxide and cyclooxygenase. |journal=Neurodegeneration : a journal for neurodegenerative disorders, neuroprotection, and neuroregeneration |volume=4 |issue= 3 |pages= 315-21 |year= 1996 |pmid= 8581564 |doi= }}
*{{cite journal | author=Ballif BA, Mincek NV, Barratt JT, ''et al.'' |title=Interaction of cyclooxygenases with an apoptosis- and autoimmunity-associated protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 11 |pages= 5544-9 |year= 1996 |pmid= 8643612 |doi= }}
*{{cite journal | author=Hla T |title=Molecular characterization of the 5.2 KB isoform of the human cyclooxygenase-1 transcript. |journal=Prostaglandins |volume=51 |issue= 1 |pages= 81-5 |year= 1996 |pmid= 8900446 |doi= }}
*{{cite journal | author=Mahida YR, Beltinger J, Makh S, ''et al.'' |title=Adult human colonic subepithelial myofibroblasts express extracellular matrix proteins and cyclooxygenase-1 and -2. |journal=Am. J. Physiol. |volume=273 |issue= 6 Pt 1 |pages= G1341-8 |year= 1998 |pmid= 9435560 |doi= }}
*{{cite journal | author=Tsujii M, Kawano S, Tsuji S, ''et al.'' |title=Cyclooxygenase regulates angiogenesis induced by colon cancer cells. |journal=Cell |volume=93 |issue= 5 |pages= 705-16 |year= 1998 |pmid= 9630216 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SDC1... {November 12, 2007 7:38:28 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:39:09 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 = Syndecan 1
| HGNCid = 10658
| Symbol = SDC1
| AltSymbols =; CD138; SDC; SYND1; syndecan
| OMIM = 186355
| ECnumber =
| Homologene = 2252
| MGIid = 1349162
| GeneAtlas_image1 = PBB_GE_SDC1_201286_at_tn.png
| GeneAtlas_image2 = PBB_GE_SDC1_201287_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008092 |text = cytoskeletal protein binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6382
| Hs_Ensembl = ENSG00000115884
| Hs_RefseqProtein = NP_001006947
| Hs_RefseqmRNA = NM_001006946
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 20264039
| Hs_GenLoc_end = 20288675
| Hs_Uniprot = P18827
| Mm_EntrezGene = 20969
| Mm_Ensembl = ENSMUSG00000020592
| Mm_RefseqmRNA = NM_011519
| Mm_RefseqProtein = NP_035649
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 8797404
| Mm_GenLoc_end = 8819683
| Mm_Uniprot = Q3THY2
}}
}}
'''Syndecan 1''', also known as '''SDC1''', 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 transmembrane (type I) heparan sulfate proteoglycan and is a member of the syndecan proteoglycan family. The syndecans mediate cell binding, cell signaling, and cytoskeletal organization and syndecan receptors are required for internalization of the HIV-1 tat protein. The syndecan-1 protein functions as an integral membrane protein and participates in cell proliferation, cell migration and cell-matrix interactions via its receptor for extracellular matrix proteins. Altered syndecan-1 expression has been detected in several different tumor types. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. These two represent the major variants of this gene and encode the same protein.<ref>{{cite web | title = Entrez Gene: SDC1 syndecan 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6382| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=David G |title=Structural and functional diversity of the heparan sulfate proteoglycans. |journal=Adv. Exp. Med. Biol. |volume=313 |issue= |pages= 69-78 |year= 1992 |pmid= 1442271 |doi= }}
*{{cite journal | author=Jaakkola P, Jalkanen M |title=Transcriptional regulation of Syndecan-1 expression by growth factors. |journal=Prog. Nucleic Acid Res. Mol. Biol. |volume=63 |issue= |pages= 109-38 |year= 1999 |pmid= 10506830 |doi= }}
*{{cite journal | author=Wijdenes J, Dore JM, Clement C, Vermot-Desroches C |title=CD138. |journal=J. Biol. Regul. Homeost. Agents |volume=16 |issue= 2 |pages= 152-5 |year= 2003 |pmid= 12144130 |doi= }}
*{{cite journal | author=Lories V, Cassiman JJ, Van den Berghe H, David G |title=Differential expression of cell surface heparan sulfate proteoglycans in human mammary epithelial cells and lung fibroblasts. |journal=J. Biol. Chem. |volume=267 |issue= 2 |pages= 1116-22 |year= 1992 |pmid= 1339431 |doi= }}
*{{cite journal | author=Vainio S, Jalkanen M, Bernfield M, Saxén L |title=Transient expression of syndecan in mesenchymal cell aggregates of the embryonic kidney. |journal=Dev. Biol. |volume=152 |issue= 2 |pages= 221-32 |year= 1992 |pmid= 1644217 |doi= }}
*{{cite journal | author=Kiefer MC, Ishihara M, Swiedler SJ, ''et al.'' |title=The molecular biology of heparan sulfate fibroblast growth factor receptors. |journal=Ann. N. Y. Acad. Sci. |volume=638 |issue= |pages= 167-76 |year= 1992 |pmid= 1664683 |doi= }}
*{{cite journal | author=Ala-Kapee M, Nevanlinna H, Mali M, ''et al.'' |title=Localization of gene for human syndecan, an integral membrane proteoglycan and a matrix receptor, to chromosome 2. |journal=Somat. Cell Mol. Genet. |volume=16 |issue= 5 |pages= 501-5 |year= 1990 |pmid= 2173154 |doi= }}
*{{cite journal | author=Mali M, Jaakkola P, Arvilommi AM, Jalkanen M |title=Sequence of human syndecan indicates a novel gene family of integral membrane proteoglycans. |journal=J. Biol. Chem. |volume=265 |issue= 12 |pages= 6884-9 |year= 1990 |pmid= 2324102 |doi= }}
*{{cite journal | author=Sanderson RD, Lalor P, Bernfield M |title=B lymphocytes express and lose syndecan at specific stages of differentiation. |journal=Cell Regul. |volume=1 |issue= 1 |pages= 27-35 |year= 1992 |pmid= 2519615 |doi= }}
*{{cite journal | author=Asundi VK, Carey DJ |title=Self-association of N-syndecan (syndecan-3) core protein is mediated by a novel structural motif in the transmembrane domain and ectodomain flanking region. |journal=J. Biol. Chem. |volume=270 |issue= 44 |pages= 26404-10 |year= 1995 |pmid= 7592855 |doi= }}
*{{cite journal | author=Zhang L, David G, Esko JD |title=Repetitive Ser-Gly sequences enhance heparan sulfate assembly in proteoglycans. |journal=J. Biol. Chem. |volume=270 |issue= 45 |pages= 27127-35 |year= 1995 |pmid= 7592967 |doi= }}
*{{cite journal | author=Barillari G, Gendelman R, Gallo RC, Ensoli B |title=The Tat protein of human immunodeficiency virus type 1, a growth factor for AIDS Kaposi sarcoma and cytokine-activated vascular cells, induces adhesion of the same cell types by using integrin receptors recognizing the RGD amino acid sequence. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 17 |pages= 7941-5 |year= 1993 |pmid= 7690138 |doi= }}
*{{cite journal | author=Spring J, Goldberger OA, Jenkins NA, ''et al.'' |title=Mapping of the syndecan genes in the mouse: linkage with members of the myc gene family. |journal=Genomics |volume=21 |issue= 3 |pages= 597-601 |year= 1994 |pmid= 7959737 |doi= 10.1006/geno.1994.1319 }}
*{{cite journal | author=Sneed TB, Stanley DJ, Young LA, Sanderson RD |title=Interleukin-6 regulates expression of the syndecan-1 proteoglycan on B lymphoid cells. |journal=Cell. Immunol. |volume=153 |issue= 2 |pages= 456-67 |year= 1994 |pmid= 8118875 |doi= 10.1006/cimm.1994.1042 }}
*{{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=Kokenyesi R, Bernfield M |title=Core protein structure and sequence determine the site and presence of heparan sulfate and chondroitin sulfate on syndecan-1. |journal=J. Biol. Chem. |volume=269 |issue= 16 |pages= 12304-9 |year= 1994 |pmid= 8163535 |doi= }}
*{{cite journal | author=Albini A, Benelli R, Presta M, ''et al.'' |title=HIV-tat protein is a heparin-binding angiogenic growth factor. |journal=Oncogene |volume=12 |issue= 2 |pages= 289-97 |year= 1996 |pmid= 8570206 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Kaukonen J, Alanen-Kurki L, Jalkanen M, Palotie A |title=The mapping and visual ordering of the human syndecan-1 and N-myc genes near the telomeric region of chromosome 2p. |journal=Hum. Genet. |volume=99 |issue= 3 |pages= 295-7 |year= 1997 |pmid= 9050911 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on THBD... {November 12, 2007 7:39:09 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:40:10 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_THBD_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1adx.
| PDB = {{PDB2|1adx}}, {{PDB2|1dqb}}, {{PDB2|1dx5}}, {{PDB2|1zaq}}, {{PDB2|2adx}}
| Name = Thrombomodulin
| HGNCid = 11784
| Symbol = THBD
| AltSymbols =; TM; CD141; THRM
| OMIM = 188040
| ECnumber =
| Homologene = 308
| MGIid = 98736
| GeneAtlas_image1 = PBB_GE_THBD_203887_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_THBD_203888_at_tn.png
| Function = {{GNF_GO|id=GO:0004888 |text = transmembrane receptor activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005529 |text = sugar binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0007565 |text = female pregnancy}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}} {{GNF_GO|id=GO:0009790 |text = embryonic development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7056
| Hs_Ensembl = ENSG00000178726
| Hs_RefseqProtein = NP_000352
| Hs_RefseqmRNA = NM_000361
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 22974270
| Hs_GenLoc_end = 22978287
| Hs_Uniprot = P07204
| Mm_EntrezGene = 21824
| Mm_Ensembl = ENSMUSG00000074743
| Mm_RefseqmRNA = NM_009378
| Mm_RefseqProtein = NP_033404
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 148097654
| Mm_GenLoc_end = 148099387
| Mm_Uniprot = Q543W3
}}
}}
'''Thrombomodulin''', also known as '''THBD''', 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 intronless gene is an endothelial-specific type I membrane receptor that binds thrombin. This binding results in the activation of protein C, which degrades clotting factors Va and VIIIa and reduces the amount of thrombin generated. Mutations in this gene are a cause of thromboembolic disease, also known as inherited thrombophilia.<ref>{{cite web | title = Entrez Gene: THBD thrombomodulin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7056| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Esmon CT |title=Thrombomodulin as a model of molecular mechanisms that modulate protease specificity and function at the vessel surface. |journal=FASEB J. |volume=9 |issue= 10 |pages= 946-55 |year= 1995 |pmid= 7615164 |doi= }}
*{{cite journal | author=Ohlin AK, Norlund L, Marlar RA |title=Thrombomodulin gene variations and thromboembolic disease. |journal=Thromb. Haemost. |volume=78 |issue= 1 |pages= 396-400 |year= 1997 |pmid= 9198186 |doi= }}
*{{cite journal | author=Van de Wouwer M, Collen D, Conway EM |title=Thrombomodulin-protein C-EPCR system: integrated to regulate coagulation and inflammation. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=24 |issue= 8 |pages= 1374-83 |year= 2005 |pmid= 15178554 |doi= 10.1161/01.ATV.0000134298.25489.92 }}
*{{cite journal | author=Boffa MC, Jackman RW, Peyri N, ''et al.'' |title=Thrombomodulin in the central nervous system. |journal=Nouvelle revue française d'hématologie |volume=33 |issue= 6 |pages= 423-9 |year= 1992 |pmid= 1667949 |doi= }}
*{{cite journal | author=Jakubowski HV, Owen WG |title=Macromolecular specificity determinants on thrombin for fibrinogen and thrombomodulin. |journal=J. Biol. Chem. |volume=264 |issue= 19 |pages= 11117-21 |year= 1989 |pmid= 2544585 |doi= }}
*{{cite journal | author=Jackman RW, Beeler DL, Fritze L, ''et al.'' |title=Human thrombomodulin gene is intron depleted: nucleic acid sequences of the cDNA and gene predict protein structure and suggest sites of regulatory control. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 18 |pages= 6425-9 |year= 1987 |pmid= 2819876 |doi= }}
*{{cite journal | author=Suzuki K, Kusumoto H, Deyashiki Y, ''et al.'' |title=Structure and expression of human thrombomodulin, a thrombin receptor on endothelium acting as a cofactor for protein C activation. |journal=EMBO J. |volume=6 |issue= 7 |pages= 1891-7 |year= 1987 |pmid= 2820710 |doi= }}
*{{cite journal | author=Wen DZ, Dittman WA, Ye RD, ''et al.'' |title=Human thrombomodulin: complete cDNA sequence and chromosome localization of the gene. |journal=Biochemistry |volume=26 |issue= 14 |pages= 4350-7 |year= 1987 |pmid= 2822087 |doi= }}
*{{cite journal | author=Shirai T, Shiojiri S, Ito H, ''et al.'' |title=Gene structure of human thrombomodulin, a cofactor for thrombin-catalyzed activation of protein C. |journal=J. Biochem. |volume=103 |issue= 2 |pages= 281-5 |year= 1988 |pmid= 2836377 |doi= }}
*{{cite journal | author=Yonezawa S, Maruyama I, Tanaka S, ''et al.'' |title=Immunohistochemical localization of thrombomodulin in chorionic diseases of the uterus and choriocarcinoma of the stomach. A comparative study with the distribution of human chorionic gonadotropin. |journal=Cancer |volume=62 |issue= 3 |pages= 569-76 |year= 1988 |pmid= 2839283 |doi= }}
*{{cite journal | author=Ishii H, Majerus PW |title=Thrombomodulin is present in human plasma and urine. |journal=J. Clin. Invest. |volume=76 |issue= 6 |pages= 2178-81 |year= 1986 |pmid= 3001144 |doi= }}
*{{cite journal | author=Adler M, Seto MH, Nitecki DE, ''et al.'' |title=The structure of a 19-residue fragment from the C-loop of the fourth epidermal growth factor-like domain of thrombomodulin. |journal=J. Biol. Chem. |volume=270 |issue= 40 |pages= 23366-72 |year= 1995 |pmid= 7559494 |doi= }}
*{{cite journal | author=Ohlin AK, Marlar RA |title=The first mutation identified in the thrombomodulin gene in a 45-year-old man presenting with thromboembolic disease. |journal=Blood |volume=85 |issue= 2 |pages= 330-6 |year= 1995 |pmid= 7811989 |doi= }}
*{{cite journal | author=Srinivasan J, Hu S, Hrabal R, ''et al.'' |title=Thrombin-bound structure of an EGF subdomain from human thrombomodulin determined by transferred nuclear Overhauser effects. |journal=Biochemistry |volume=33 |issue= 46 |pages= 13553-60 |year= 1994 |pmid= 7947766 |doi= }}
*{{cite journal | author=Gerlitz B, Hassell T, Vlahos CJ, ''et al.'' |title=Identification of the predominant glycosaminoglycan-attachment site in soluble recombinant human thrombomodulin: potential regulation of functionality by glycosyltransferase competition for serine474. |journal=Biochem. J. |volume=295 ( Pt 1) |issue= |pages= 131-40 |year= 1993 |pmid= 8216207 |doi= }}
*{{cite journal | author=Yasuda K, Espinosa R, Davis EM, ''et al.'' |title=Human somatostatin receptor genes: localization of SSTR5 to human chromosome 20p11.2. |journal=Genomics |volume=17 |issue= 3 |pages= 785-6 |year= 1993 |pmid= 8244401 |doi= 10.1006/geno.1993.1410 }}
*{{cite journal | author=Yamamoto S, Mizoguchi T, Tamaki T, ''et al.'' |title=Urinary thrombomodulin, its isolation and characterization. |journal=J. Biochem. |volume=113 |issue= 4 |pages= 433-40 |year= 1993 |pmid= 8390446 |doi= }}
*{{cite journal | author=Meininger DP, Hunter MJ, Komives EA |title=Synthesis, activity, and preliminary structure of the fourth EGF-like domain of thrombomodulin. |journal=Protein Sci. |volume=4 |issue= 9 |pages= 1683-95 |year= 1996 |pmid= 8528067 |doi= }}
*{{cite journal | author=Maglott DR, Feldblyum TV, Durkin AS, Nierman WC |title=Radiation hybrid mapping of SNAP, PCSK2, and THBD (human chromosome 20p). |journal=Mamm. Genome |volume=7 |issue= 5 |pages= 400-1 |year= 1996 |pmid= 8661740 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TSG101... {November 12, 2007 7:40:10 PM PST}
- SEARCH REDIRECT: Control Box Found: TSG101 {November 12, 2007 7:40:46 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 12, 2007 7:40:47 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 12, 2007 7:40:47 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 12, 2007 7:40:47 PM PST}
- UPDATED: Updated protein page: TSG101 {November 12, 2007 7:40:54 PM PST}
- INFO: Beginning work on TYR... {November 12, 2007 7:40:54 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:41:34 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Tyrosinase (oculocutaneous albinism IA)
| HGNCid = 12442
| Symbol = TYR
| AltSymbols =; OCA1A; OCAIA
| OMIM = 606933
| ECnumber =
| Homologene = 30969
| MGIid = 98880
| GeneAtlas_image1 = PBB_GE_TYR_206630_at_tn.png
| Function = {{GNF_GO|id=GO:0004497 |text = monooxygenase activity}} {{GNF_GO|id=GO:0004503 |text = monophenol monooxygenase activity}} {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0046982 |text = protein heterodimerization activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0005798 |text = Golgi-associated vesicle}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0042470 |text = melanosome}} {{GNF_GO|id=GO:0048471 |text = perinuclear region of cytoplasm}}
| Process = {{GNF_GO|id=GO:0006583 |text = melanin biosynthetic process from tyrosine}} {{GNF_GO|id=GO:0006726 |text = eye pigment biosynthetic process}} {{GNF_GO|id=GO:0007601 |text = visual perception}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0043473 |text = pigmentation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7299
| Hs_Ensembl = ENSG00000077498
| Hs_RefseqProtein = NP_000363
| Hs_RefseqmRNA = NM_000372
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 88550268
| Hs_GenLoc_end = 88668474
| Hs_Uniprot = P14679
| Mm_EntrezGene = 22173
| Mm_Ensembl = ENSMUSG00000004651
| Mm_RefseqmRNA = NM_011661
| Mm_RefseqProtein = NP_035791
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 87303166
| Mm_GenLoc_end = 87369172
| Mm_Uniprot = Q3UFK9
}}
}}
'''Tyrosinase (oculocutaneous albinism IA)''', also known as '''TYR''', 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=Oetting WS, King RA |title=Molecular basis of albinism: mutations and polymorphisms of pigmentation genes associated with albinism. |journal=Hum. Mutat. |volume=13 |issue= 2 |pages= 99-115 |year= 1999 |pmid= 10094567 |doi= 10.1002/(SICI)1098-1004(1999)13:2<99::AID-HUMU2>3.0.CO;2-C }}
*{{cite journal | author=Bard LA |title=Heterogeneity in Waardenburg's syndrome. Report of a family with ocular albinism. |journal=Arch. Ophthalmol. |volume=96 |issue= 7 |pages= 1193-8 |year= 1978 |pmid= 666627 |doi= }}
*{{cite journal | author=Oetting WS, King RA |title=Molecular analysis of type I-A (tyrosinase negative) oculocutaneous albinism. |journal=Hum. Genet. |volume=90 |issue= 3 |pages= 258-62 |year= 1993 |pmid= 1487241 |doi= }}
*{{cite journal | author=Tripathi RK, Strunk KM, Giebel LB, ''et al.'' |title=Tyrosinase gene mutations in type I (tyrosinase-deficient) oculocutaneous albinism define two clusters of missense substitutions. |journal=Am. J. Med. Genet. |volume=43 |issue= 5 |pages= 865-71 |year= 1992 |pmid= 1642278 |doi= 10.1002/ajmg.1320430523 }}
*{{cite journal | author=Chintamaneni CD, Halaban R, Kobayashi Y, ''et al.'' |title=A single base insertion in the putative transmembrane domain of the tyrosinase gene as a cause for tyrosinase-negative oculocutaneous albinism. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 12 |pages= 5272-6 |year= 1991 |pmid= 1711223 |doi= }}
*{{cite journal | author=Giebel LB, Musarella MA, Spritz RA |title=A nonsense mutation in the tyrosinase gene of Afghan patients with tyrosinase negative (type IA) oculocutaneous albinism. |journal=J. Med. Genet. |volume=28 |issue= 7 |pages= 464-7 |year= 1991 |pmid= 1832718 |doi= }}
*{{cite journal | author=Spritz RA, Strunk KM, Hsieh CL, ''et al.'' |title=Homozygous tyrosinase gene mutation in an American black with tyrosinase-negative (type IA) oculocutaneous albinism. |journal=Am. J. Hum. Genet. |volume=48 |issue= 2 |pages= 318-24 |year= 1991 |pmid= 1899321 |doi= }}
*{{cite journal | author=King RA, Townsend D, Oetting W, ''et al.'' |title=Temperature-sensitive tyrosinase associated with peripheral pigmentation in oculocutaneous albinism. |journal=J. Clin. Invest. |volume=87 |issue= 3 |pages= 1046-53 |year= 1991 |pmid= 1900307 |doi= }}
*{{cite journal | author=Giebel LB, Tripathi RK, King RA, Spritz RA |title=A tyrosinase gene missense mutation in temperature-sensitive type I oculocutaneous albinism. A human homologue to the Siamese cat and the Himalayan mouse. |journal=J. Clin. Invest. |volume=87 |issue= 3 |pages= 1119-22 |year= 1991 |pmid= 1900309 |doi= }}
*{{cite journal | author=Giebel LB, Strunk KM, Spritz RA |title=Organization and nucleotide sequences of the human tyrosinase gene and a truncated tyrosinase-related segment. |journal=Genomics |volume=9 |issue= 3 |pages= 435-45 |year= 1991 |pmid= 1903356 |doi= }}
*{{cite journal | author=Giebel LB, Tripathi RK, Strunk KM, ''et al.'' |title=Tyrosinase gene mutations associated with type IB ("yellow") oculocutaneous albinism. |journal=Am. J. Hum. Genet. |volume=48 |issue= 6 |pages= 1159-67 |year= 1991 |pmid= 1903591 |doi= }}
*{{cite journal | author=Oetting WS, Mentink MM, Summers CG, ''et al.'' |title=Three different frameshift mutations of the tyrosinase gene in type IA oculocutaneous albinism. |journal=Am. J. Hum. Genet. |volume=49 |issue= 1 |pages= 199-206 |year= 1991 |pmid= 1905879 |doi= }}
*{{cite journal | author=King RA, Mentink MM, Oetting WS |title=Non-random distribution of missense mutations within the human tyrosinase gene in type I (tyrosinase-related) oculocutaneous albinism. |journal=Mol. Biol. Med. |volume=8 |issue= 1 |pages= 19-29 |year= 1991 |pmid= 1943686 |doi= }}
*{{cite journal | author=Giebel LB, Strunk KM, King RA, ''et al.'' |title=A frequent tyrosinase gene mutation in classic, tyrosinase-negative (type IA) oculocutaneous albinism. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 9 |pages= 3255-8 |year= 1990 |pmid= 1970634 |doi= }}
*{{cite journal | author=Kikuchi H, Hara S, Ishiguro S, ''et al.'' |title=Detection of point mutation in the tyrosinase gene of a Japanese albino patient by a direct sequencing of amplified DNA. |journal=Hum. Genet. |volume=85 |issue= 1 |pages= 123-4 |year= 1990 |pmid= 2113511 |doi= }}
*{{cite journal | author=Takeda A, Tomita Y, Matsunaga J, ''et al.'' |title=Molecular basis of tyrosinase-negative oculocutaneous albinism. A single base mutation in the tyrosinase gene causing arginine to glutamine substitution at position 59. |journal=J. Biol. Chem. |volume=265 |issue= 29 |pages= 17792-7 |year= 1990 |pmid= 2120217 |doi= }}
*{{cite journal | author=Spritz RA, Strunk KM, Giebel LB, King RA |title=Detection of mutations in the tyrosinase gene in a patient with type IA oculocutaneous albinism. |journal=N. Engl. J. Med. |volume=322 |issue= 24 |pages= 1724-8 |year= 1990 |pmid= 2342539 |doi= }}
*{{cite journal | author=Kikuchi H, Miura H, Yamamoto H, ''et al.'' |title=Characteristic sequences in the upstream region of the human tyrosinase gene. |journal=Biochim. Biophys. Acta |volume=1009 |issue= 3 |pages= 283-6 |year= 1990 |pmid= 2480811 |doi= }}
*{{cite journal | author=Bouchard B, Fuller BB, Vijayasaradhi S, Houghton AN |title=Induction of pigmentation in mouse fibroblasts by expression of human tyrosinase cDNA. |journal=J. Exp. Med. |volume=169 |issue= 6 |pages= 2029-42 |year= 1989 |pmid= 2499655 |doi= }}
*{{cite journal | author=Takeda A, Tomita Y, Okinaga S, ''et al.'' |title=Functional analysis of the cDNA encoding human tyrosinase precursor. |journal=Biochem. Biophys. Res. Commun. |volume=162 |issue= 3 |pages= 984-90 |year= 1989 |pmid= 2504160 |doi= }}
}}
{{refend}}
{{protein-stub}}
end log.
