- INFO: Beginning work on ADRB1... {November 15, 2007 5:37:13 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 5:38:00 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 = Adrenergic, beta-1-, receptor
| HGNCid = 285
| Symbol = ADRB1
| AltSymbols =; ADRB1R; B1AR; BETA1AR; RHR
| OMIM = 109630
| ECnumber =
| Homologene = 20171
| MGIid = 87937
| GeneAtlas_image1 = PBB_GE_ADRB1_208214_at_tn.png
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004935 |text = adrenoceptor activity}} {{GNF_GO|id=GO:0004940 |text = beta1-adrenergic receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0001996 |text = positive regulation of heart contraction rate by epinephrine-norepinephrine}} {{GNF_GO|id=GO:0001997 |text = increased strength of heart contraction by epinephrine-norepinephrine}} {{GNF_GO|id=GO:0002024 |text = diet induced thermogenesis}} {{GNF_GO|id=GO:0002025 |text = norepinephrine-epinephrine vasodilation during regulation of blood pressure}} {{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:0007190 |text = adenylate cyclase activation}} {{GNF_GO|id=GO:0009409 |text = response to cold}} {{GNF_GO|id=GO:0031649 |text = heat generation}} {{GNF_GO|id=GO:0040015 |text = negative regulation of body size}} {{GNF_GO|id=GO:0042596 |text = fear response}} {{GNF_GO|id=GO:0050873 |text = brown fat cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 153
| Hs_Ensembl = ENSG00000043591
| Hs_RefseqProtein = NP_000675
| Hs_RefseqmRNA = NM_000684
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 115793796
| Hs_GenLoc_end = 115796657
| Hs_Uniprot = P08588
| Mm_EntrezGene = 11554
| Mm_Ensembl = ENSMUSG00000035283
| Mm_RefseqmRNA = NM_007419
| Mm_RefseqProtein = NP_031445
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 56775622
| Mm_GenLoc_end = 56777022
| Mm_Uniprot = Q9CRR2
}}
}}
'''Adrenergic, beta-1-, receptor''', also known as '''ADRB1''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: ADRB1 adrenergic, beta-1-, receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=153| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The adrenergic receptors (subtypes alpha 1, alpha 2, beta 1, and beta 2) are a prototypic family of guanine nucleotide binding regulatory protein-coupled receptors that mediate the physiological effects of the hormone epinephrine and the neurotransmitter norepinephrine. Specific polymorphisms in this gene have been shown to affect the resting heart rate and can be involved in heart failure.<ref>{{cite web | title = Entrez Gene: ADRB1 adrenergic, beta-1-, receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=153| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Frielle T, Kobilka B, Lefkowitz RJ, Caron MG |title=Human beta 1- and beta 2-adrenergic receptors: structurally and functionally related receptors derived from distinct genes. |journal=Trends Neurosci. |volume=11 |issue= 7 |pages= 321-4 |year= 1989 |pmid= 2465637 |doi= }}
*{{cite journal | author=Muszkat M |title=Interethnic differences in drug response: the contribution of genetic variability in beta adrenergic receptor and cytochrome P4502C9. |journal=Clin. Pharmacol. Ther. |volume=82 |issue= 2 |pages= 215-8 |year= 2007 |pmid= 17329986 |doi= 10.1038/sj.clpt.6100142 }}
*{{cite journal | author=Yang-Feng TL, Xue FY, Zhong WW, ''et al.'' |title=Chromosomal organization of adrenergic receptor genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 4 |pages= 1516-20 |year= 1990 |pmid= 2154750 |doi= }}
*{{cite journal | author=Forse RA, Leibel R, Gagner M |title=The effect of Escherichia coli endotoxin on the adrenergic control of lipolysis in the human adipocyte. |journal=J. Surg. Res. |volume=46 |issue= 1 |pages= 41-8 |year= 1989 |pmid= 2536864 |doi= }}
*{{cite journal | author=Frielle T, Collins S, Daniel KW, ''et al.'' |title=Cloning of the cDNA for the human beta 1-adrenergic receptor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 22 |pages= 7920-4 |year= 1987 |pmid= 2825170 |doi= }}
*{{cite journal | author=Stiles GL, Strasser RH, Lavin TN, ''et al.'' |title=The cardiac beta-adrenergic receptor. Structural similarities of beta 1 and beta 2 receptor subtypes demonstrated by photoaffinity labeling. |journal=J. Biol. Chem. |volume=258 |issue= 13 |pages= 8443-9 |year= 1983 |pmid= 6305985 |doi= }}
*{{cite journal | author=Hoehe MR, Otterud B, Hsieh WT, ''et al.'' |title=Genetic mapping of adrenergic receptor genes in humans. |journal=J. Mol. Med. |volume=73 |issue= 6 |pages= 299-306 |year= 1995 |pmid= 7583452 |doi= }}
*{{cite journal | author=Elies R, Ferrari I, Wallukat G, ''et al.'' |title=Structural and functional analysis of the B cell epitopes recognized by anti-receptor autoantibodies in patients with Chagas' disease. |journal=J. Immunol. |volume=157 |issue= 9 |pages= 4203-11 |year= 1996 |pmid= 8892658 |doi= }}
*{{cite journal | author=Oldenhof J, Vickery R, Anafi M, ''et al.'' |title=SH3 binding domains in the dopamine D4 receptor. |journal=Biochemistry |volume=37 |issue= 45 |pages= 15726-36 |year= 1998 |pmid= 9843378 |doi= 10.1021/bi981634+ }}
*{{cite journal | author=Mason DA, Moore JD, Green SA, Liggett SB |title=A gain-of-function polymorphism in a G-protein coupling domain of the human beta1-adrenergic receptor. |journal=J. Biol. Chem. |volume=274 |issue= 18 |pages= 12670-4 |year= 1999 |pmid= 10212248 |doi= }}
*{{cite journal | author=Moore JD, Mason DA, Green SA, ''et al.'' |title=Racial differences in the frequencies of cardiac beta(1)-adrenergic receptor polymorphisms: analysis of c145A>G and c1165G>C. |journal=Hum. Mutat. |volume=14 |issue= 3 |pages= 271 |year= 1999 |pmid= 10477438 |doi= 10.1002/(SICI)1098-1004(1999)14:3<271::AID-HUMU14>3.0.CO;2-Q }}
*{{cite journal | author=Tang Y, Hu LA, Miller WE, ''et al.'' |title=Identification of the endophilins (SH3p4/p8/p13) as novel binding partners for the beta1-adrenergic receptor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 22 |pages= 12559-64 |year= 1999 |pmid= 10535961 |doi= }}
*{{cite journal | author=Podlowski S, Wenzel K, Luther HP, ''et al.'' |title=Beta1-adrenoceptor gene variations: a role in idiopathic dilated cardiomyopathy? |journal=J. Mol. Med. |volume=78 |issue= 2 |pages= 87-93 |year= 2000 |pmid= 10794544 |doi= }}
*{{cite journal | author=Shiina T, Kawasaki A, Nagao T, Kurose H |title=Interaction with beta-arrestin determines the difference in internalization behavor between beta1- and beta2-adrenergic receptors. |journal=J. Biol. Chem. |volume=275 |issue= 37 |pages= 29082-90 |year= 2000 |pmid= 10862778 |doi= 10.1074/jbc.M909757199 }}
*{{cite journal | author=Hu LA, Tang Y, Miller WE, ''et al.'' |title=beta 1-adrenergic receptor association with PSD-95. Inhibition of receptor internalization and facilitation of beta 1-adrenergic receptor interaction with N-methyl-D-aspartate receptors. |journal=J. Biol. Chem. |volume=275 |issue= 49 |pages= 38659-66 |year= 2001 |pmid= 10995758 |doi= 10.1074/jbc.M005938200 }}
*{{cite journal | author=Börjesson M, Magnusson Y, Hjalmarson A, Andersson B |title=A novel polymorphism in the gene coding for the beta(1)-adrenergic receptor associated with survival in patients with heart failure. |journal=Eur. Heart J. |volume=21 |issue= 22 |pages= 1853-8 |year= 2001 |pmid= 11052857 |doi= 10.1053/euhj.1999.1994 }}
*{{cite journal | author=Xu J, Paquet M, Lau AG, ''et al.'' |title=beta 1-adrenergic receptor association with the synaptic scaffolding protein membrane-associated guanylate kinase inverted-2 (MAGI-2). Differential regulation of receptor internalization by MAGI-2 and PSD-95. |journal=J. Biol. Chem. |volume=276 |issue= 44 |pages= 41310-7 |year= 2001 |pmid= 11526121 |doi= 10.1074/jbc.M107480200 }}
*{{cite journal | author=Hu LA, Chen W, Premont RT, ''et al.'' |title=G protein-coupled receptor kinase 5 regulates beta 1-adrenergic receptor association with PSD-95. |journal=J. Biol. Chem. |volume=277 |issue= 2 |pages= 1607-13 |year= 2002 |pmid= 11700307 |doi= 10.1074/jbc.M107297200 }}
*{{cite journal | author=Ranade K, Jorgenson E, Sheu WH, ''et al.'' |title=A polymorphism in the beta1 adrenergic receptor is associated with resting heart rate. |journal=Am. J. Hum. Genet. |volume=70 |issue= 4 |pages= 935-42 |year= 2002 |pmid= 11854867 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ADRB2... {November 15, 2007 5:38:00 PM PST}
- SEARCH REDIRECT: Control Box Found: ADRB2 {November 15, 2007 5:38:26 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 5:38:27 PM PST}
- SKIP SUMMARY: SKIPPING Summary, No Errors. {November 15, 2007 5:38:27 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 5:38:27 PM PST}
- UPDATED: Updated protein page: ADRB2 {November 15, 2007 5:38:34 PM PST}
- INFO: Beginning work on ADRB3... {November 15, 2007 5:38:34 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 5:38:56 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
}}
<!-- 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 = Adrenergic, beta-3-, receptor
| HGNCid = 288
| Symbol = ADRB3
| AltSymbols =; BETA3AR
| OMIM = 109691
| ECnumber =
| Homologene = 37250
| MGIid = 87939
| GeneAtlas_image1 = PBB_GE_ADRB3_206812_at_tn.png
| GeneAtlas_image2 = PBB_GE_ADRB3_217303_s_at_tn.png
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0015052 |text = beta3-adrenergic receptor activity}} {{GNF_GO|id=GO:0031699 |text = beta-3 adrenergic receptor binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0051380 |text = norepinephrine binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0043235 |text = receptor complex}}
| Process = {{GNF_GO|id=GO:0002024 |text = diet induced thermogenesis}} {{GNF_GO|id=GO:0002025 |text = norepinephrine-epinephrine vasodilation during regulation of blood pressure}} {{GNF_GO|id=GO:0002032 |text = arrestin mediated desensitization of G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006091 |text = generation of precursor metabolites and energy}} {{GNF_GO|id=GO:0006112 |text = energy reserve metabolic process}} {{GNF_GO|id=GO:0006898 |text = receptor-mediated endocytosis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007190 |text = adenylate cyclase activation}} {{GNF_GO|id=GO:0009409 |text = response to cold}} {{GNF_GO|id=GO:0031649 |text = heat generation}} {{GNF_GO|id=GO:0040015 |text = negative regulation of body size}} {{GNF_GO|id=GO:0043410 |text = positive regulation of MAPKKK cascade}} {{GNF_GO|id=GO:0050873 |text = brown fat cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 155
| Hs_Ensembl = ENSG00000188778
| Hs_RefseqProtein = NP_000016
| Hs_RefseqmRNA = NM_000025
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 37939673
| Hs_GenLoc_end = 37943341
| Hs_Uniprot = P13945
| Mm_EntrezGene = 11556
| Mm_Ensembl = ENSMUSG00000031489
| Mm_RefseqmRNA = NM_013462
| Mm_RefseqProtein = NP_038490
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 28691712
| Mm_GenLoc_end = 28695524
| Mm_Uniprot = Q3UP63
}}
}}
'''Adrenergic, beta-3-, receptor''', also known as '''ADRB3''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: ADRB3 adrenergic, beta-3-, receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=155| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The ADRB3 gene product, beta-3-adrenergic receptor, is located mainly in adipose tissue and is involved in the regulation of lipolysis and thermogenesis. Beta adrenergic receptors are involved in the epenephrine and norepinephrine-induced activation of adenylate cyclase through the action of G proteins.<ref>{{cite web | title = Entrez Gene: ADRB3 adrenergic, beta-3-, receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=155| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Granneman JG, Lahners KN, Rao DD |title=Rodent and human beta 3-adrenergic receptor genes contain an intron within the protein-coding block. |journal=Mol. Pharmacol. |volume=42 |issue= 6 |pages= 964-70 |year= 1993 |pmid= 1336117 |doi= }}
*{{cite journal | author=Nahmias C, Blin N, Elalouf JM, ''et al.'' |title=Molecular characterization of the mouse beta 3-adrenergic receptor: relationship with the atypical receptor of adipocytes. |journal=EMBO J. |volume=10 |issue= 12 |pages= 3721-7 |year= 1991 |pmid= 1718744 |doi= }}
*{{cite journal | author=Emorine LJ, Marullo S, Briend-Sutren MM, ''et al.'' |title=Molecular characterization of the human beta 3-adrenergic receptor. |journal=Science |volume=245 |issue= 4922 |pages= 1118-21 |year= 1989 |pmid= 2570461 |doi= }}
*{{cite journal | author=Guan XM, Amend A, Strader CD |title=Determination of structural domains for G protein coupling and ligand binding in beta 3-adrenergic receptor. |journal=Mol. Pharmacol. |volume=48 |issue= 3 |pages= 492-8 |year= 1995 |pmid= 7565630 |doi= }}
*{{cite journal | author=Rodriguez M, Carillon C, Coquerel A, ''et al.'' |title=Evidence for the presence of beta 3-adrenergic receptor mRNA in the human brain. |journal=Brain Res. Mol. Brain Res. |volume=29 |issue= 2 |pages= 369-75 |year= 1995 |pmid= 7609625 |doi= }}
*{{cite journal | author=Clément K, Vaisse C, Manning BS, ''et al.'' |title=Genetic variation in the beta 3-adrenergic receptor and an increased capacity to gain weight in patients with morbid obesity. |journal=N. Engl. J. Med. |volume=333 |issue= 6 |pages= 352-4 |year= 1995 |pmid= 7609752 |doi= }}
*{{cite journal | author=Dib A, Adélaïde J, Chaffanet M, ''et al.'' |title=Characterization of the region of the short arm of chromosome 8 amplified in breast carcinoma. |journal=Oncogene |volume=10 |issue= 5 |pages= 995-1001 |year= 1995 |pmid= 7898940 |doi= }}
*{{cite journal | author=Mahmoudian M |title=The complex of human Gs protein with the beta 3 adrenergic receptor: a computer-aided molecular modeling study. |journal=Journal of molecular graphics |volume=12 |issue= 1 |pages= 22-8, 34 |year= 1994 |pmid= 8011597 |doi= }}
*{{cite journal | author=Wilkie TM, Chen Y, Gilbert DJ, ''et al.'' |title=Identification, chromosomal location, and genome organization of mammalian G-protein-coupled receptors. |journal=Genomics |volume=18 |issue= 2 |pages= 175-84 |year= 1994 |pmid= 8288218 |doi= 10.1006/geno.1993.1452 }}
*{{cite journal | author=Krief S, Lönnqvist F, Raimbault S, ''et al.'' |title=Tissue distribution of beta 3-adrenergic receptor mRNA in man. |journal=J. Clin. Invest. |volume=91 |issue= 1 |pages= 344-9 |year= 1993 |pmid= 8380813 |doi= }}
*{{cite journal | author=van Spronsen A, Nahmias C, Krief S, ''et al.'' |title=The promoter and intron/exon structure of the human and mouse beta 3-adrenergic-receptor genes. |journal=Eur. J. Biochem. |volume=213 |issue= 3 |pages= 1117-24 |year= 1993 |pmid= 8389293 |doi= }}
*{{cite journal | author=Lelias JM, Kaghad M, Rodriguez M, ''et al.'' |title=Molecular cloning of a human beta 3-adrenergic receptor cDNA. |journal=FEBS Lett. |volume=324 |issue= 2 |pages= 127-30 |year= 1993 |pmid= 8389717 |doi= }}
*{{cite journal | author=Candelore MR, Deng L, Tota LM, ''et al.'' |title=Pharmacological characterization of a recently described human beta 3-adrenergic receptor mutant. |journal=Endocrinology |volume=137 |issue= 6 |pages= 2638-41 |year= 1996 |pmid= 8641219 |doi= }}
*{{cite journal | author=Fujisawa T, Ikegami H, Yamato E, ''et al.'' |title=Association of Trp64Arg mutation of the beta3-adrenergic-receptor with NIDDM and body weight gain. |journal=Diabetologia |volume=39 |issue= 3 |pages= 349-52 |year= 1996 |pmid= 8721782 |doi= }}
*{{cite journal | author=Higashi K, Ishikawa T, Ito T, ''et al.'' |title=Association of a genetic variation in the beta 3-adrenergic receptor gene with coronary heart disease among Japanese. |journal=Biochem. Biophys. Res. Commun. |volume=232 |issue= 3 |pages= 728-30 |year= 1997 |pmid= 9126344 |doi= 10.1006/bbrc.1997.6339 }}
*{{cite journal | author=Hoffstedt J, Poirier O, Thörne A, ''et al.'' |title=Polymorphism of the human beta3-adrenoceptor gene forms a well-conserved haplotype that is associated with moderate obesity and altered receptor function. |journal=Diabetes |volume=48 |issue= 1 |pages= 203-5 |year= 1999 |pmid= 9892244 |doi= }}
*{{cite journal | author=Halushka MK, Fan JB, Bentley K, ''et al.'' |title=Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. |journal=Nat. Genet. |volume=22 |issue= 3 |pages= 239-47 |year= 1999 |pmid= 10391210 |doi= 10.1038/10297 }}
*{{cite journal | author=Kimura K, Sasaki N, Asano A, ''et al.'' |title=Mutated human beta3-adrenergic receptor (Trp64Arg) lowers the response to beta3-adrenergic agonists in transfected 3T3-L1 preadipocytes. |journal=Horm. Metab. Res. |volume=32 |issue= 3 |pages= 91-6 |year= 2000 |pmid= 10786926 |doi= }}
*{{cite journal | author=Cao W, Luttrell LM, Medvedev AV, ''et al.'' |title=Direct binding of activated c-Src to the beta 3-adrenergic receptor is required for MAP kinase activation. |journal=J. Biol. Chem. |volume=275 |issue= 49 |pages= 38131-4 |year= 2001 |pmid= 11013230 |doi= 10.1074/jbc.C000592200 }}
*{{cite journal | author=Russell ST, Hirai K, Tisdale MJ |title=Role of beta3-adrenergic receptors in the action of a tumour lipid mobilizing factor. |journal=Br. J. Cancer |volume=86 |issue= 3 |pages= 424-8 |year= 2002 |pmid= 11875710 |doi= 10.1038/sj.bjc.6600086 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ADRBK1... {November 15, 2007 5:38:56 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 5:39:27 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_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]].<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>
<!-- 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 ADRBK2... {November 15, 2007 5:39:27 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 5:40:32 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 = Adrenergic, beta, receptor kinase 2
| HGNCid = 290
| Symbol = ADRBK2
| AltSymbols =; BARK2; GRK3
| OMIM = 109636
| ECnumber =
| Homologene = 21072
| MGIid = 87941
| GeneAtlas_image1 = PBB_GE_ADRBK2_204184_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ADRBK2_204183_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{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:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 157
| Hs_Ensembl = ENSG00000100077
| Hs_RefseqProtein = NP_005151
| Hs_RefseqmRNA = NM_005160
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 24290946
| Hs_GenLoc_end = 24449916
| Hs_Uniprot = P35626
| Mm_EntrezGene = 320129
| Mm_Ensembl = ENSMUSG00000042249
| Mm_RefseqmRNA = NM_001035531
| Mm_RefseqProtein = NP_001030608
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 113150781
| Mm_GenLoc_end = 113255817
| Mm_Uniprot = Q8BVT9
}}
}}
'''Adrenergic, beta, receptor kinase 2''', also known as '''ADRBK2''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: ADRBK2 adrenergic, beta, receptor kinase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=157| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The beta-adrenergic receptor kinase specifically phosphorylates the agonist-occupied form of the beta-adrenergic and related G protein-coupled receptors. Overall, the beta adrenergic receptor kinase 2 has 85% amino acid similarity with beta adrenergic receptor kinase 1, with the protein kinase catalytic domain having 95% similarity. These data suggest the existence of a family of receptor kinases which may serve broadly to regulate receptor function.<ref>{{cite web | title = Entrez Gene: ADRBK2 adrenergic, beta, receptor kinase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=157| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Benovic JL, Onorato JJ, Arriza JL, ''et al.'' |title=Cloning, expression, and chromosomal localization of beta-adrenergic receptor kinase 2. A new member of the receptor kinase family. |journal=J. Biol. Chem. |volume=266 |issue= 23 |pages= 14939-46 |year= 1991 |pmid= 1869533 |doi= }}
*{{cite journal | author=Calabrese G, Sallese M, Stornaiuolo A, ''et al.'' |title=Chromosome mapping of the human arrestin (SAG), beta-arrestin 2 (ARRB2), and beta-adrenergic receptor kinase 2 (ADRBK2) genes. |journal=Genomics |volume=23 |issue= 1 |pages= 286-8 |year= 1995 |pmid= 7695743 |doi= 10.1006/geno.1994.1497 }}
*{{cite journal | author=Parruti G, Ambrosini G, Sallese M, De Blasi A |title=Molecular cloning, functional expression and mRNA analysis of human beta-adrenergic receptor kinase 2. |journal=Biochem. Biophys. Res. Commun. |volume=190 |issue= 2 |pages= 475-81 |year= 1993 |pmid= 8427589 |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=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=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=Dunham I, Shimizu N, Roe BA, ''et al.'' |title=The DNA sequence of human chromosome 22. |journal=Nature |volume=402 |issue= 6761 |pages= 489-95 |year= 1999 |pmid= 10591208 |doi= 10.1038/990031 }}
*{{cite journal | author=Inngjerdingen M, Damaj B, Maghazachi AA |title=Human NK cells express CC chemokine receptors 4 and 8 and respond to thymus and activation-regulated chemokine, macrophage-derived chemokine, and I-309. |journal=J. Immunol. |volume=164 |issue= 8 |pages= 4048-54 |year= 2000 |pmid= 10754297 |doi= }}
*{{cite journal | author=Celver JP, Lowe J, Kovoor A, ''et al.'' |title=Threonine 180 is required for G-protein-coupled receptor kinase 3- and beta-arrestin 2-mediated desensitization of the mu-opioid receptor in Xenopus oocytes. |journal=J. Biol. Chem. |volume=276 |issue= 7 |pages= 4894-900 |year= 2001 |pmid= 11060299 |doi= 10.1074/jbc.M007437200 }}
*{{cite journal | author=Blaukat A, Pizard A, Breit A, ''et al.'' |title=Determination of bradykinin B2 receptor in vivo phosphorylation sites and their role in receptor function. |journal=J. Biol. Chem. |volume=276 |issue= 44 |pages= 40431-40 |year= 2001 |pmid= 11517230 |doi= 10.1074/jbc.M107024200 }}
*{{cite journal | author=Wang J, Guan E, Roderiquez G, ''et al.'' |title=Role of tyrosine phosphorylation in ligand-independent sequestration of CXCR4 in human primary monocytes-macrophages. |journal=J. Biol. Chem. |volume=276 |issue= 52 |pages= 49236-43 |year= 2002 |pmid= 11668182 |doi= 10.1074/jbc.M108523200 }}
*{{cite journal | author=Obara K, Arai K, Tomita Y, ''et al.'' |title=G-protein coupled receptor kinase 2 and 3 expression in human detrusor cultured smooth muscle cells. |journal=Urol. Res. |volume=29 |issue= 5 |pages= 325-9 |year= 2002 |pmid= 11762794 |doi= }}
*{{cite journal | author=Mandyam CD, Thakker DR, Christensen JL, Standifer KM |title=Orphanin FQ/nociceptin-mediated desensitization of opioid receptor-like 1 receptor and mu opioid receptors involves protein kinase C: a molecular mechanism for heterologous cross-talk. |journal=J. Pharmacol. Exp. Ther. |volume=302 |issue= 2 |pages= 502-9 |year= 2002 |pmid= 12130708 |doi= 10.1124/jpet.102.033159 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Barrett TB, Hauger RL, Kennedy JL, ''et al.'' |title=Evidence that a single nucleotide polymorphism in the promoter of the G protein receptor kinase 3 gene is associated with bipolar disorder. |journal=Mol. Psychiatry |volume=8 |issue= 5 |pages= 546-57 |year= 2004 |pmid= 12808434 |doi= 10.1038/sj.mp.4001268 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Dzimiri N, Muiya P, Andres E, Al-Halees Z |title=Differential functional expression of human myocardial G protein receptor kinases in left ventricular cardiac diseases. |journal=Eur. J. Pharmacol. |volume=489 |issue= 3 |pages= 167-77 |year= 2005 |pmid= 15087239 |doi= 10.1016/j.ejphar.2004.03.015 }}
*{{cite journal | author=Teli T, Markovic D, Levine MA, ''et al.'' |title=Regulation of corticotropin-releasing hormone receptor type 1alpha signaling: structural determinants for G protein-coupled receptor kinase-mediated phosphorylation and agonist-mediated desensitization. |journal=Mol. Endocrinol. |volume=19 |issue= 2 |pages= 474-90 |year= 2005 |pmid= 15498832 |doi= 10.1210/me.2004-0275 }}
*{{cite journal | author=Feng YH, Wang L, Wang Q, ''et al.'' |title=ATP stimulates GRK-3 phosphorylation and beta-arrestin-2-dependent internalization of P2X7 receptor. |journal=Am. J. Physiol., Cell Physiol. |volume=288 |issue= 6 |pages= C1342-56 |year= 2005 |pmid= 15728711 |doi= 10.1152/ajpcell.00315.2004 }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CYP2C19... {November 15, 2007 5:40:32 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 5:41:01 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_CYP2C19_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1r9o.
| PDB = {{PDB2|1r9o}}
| Name = Cytochrome P450, family 2, subfamily C, polypeptide 19
| HGNCid = 2621
| Symbol = CYP2C19
| AltSymbols =; CPCJ; CYP 2C; CYP2C; P450C2C; P450IIC19
| OMIM = 124020
| ECnumber =
| Homologene = 86659
| MGIid = 1306818
| GeneAtlas_image1 = PBB_GE_CYP2C19_216058_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004497 |text = monooxygenase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0016712 |text = oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen}} {{GNF_GO|id=GO:0018675 |text = (S)-limonene 6-monooxygenase activity}} {{GNF_GO|id=GO:0018676 |text = (S)-limonene 7-monooxygenase activity}} {{GNF_GO|id=GO:0019825 |text = oxygen binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1557
| Hs_Ensembl = ENSG00000165841
| Hs_RefseqProtein = NP_000760
| Hs_RefseqmRNA = NM_000769
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 96512371
| Hs_GenLoc_end = 96603007
| Hs_Uniprot = P33261
| Mm_EntrezGene = 13098
| Mm_Ensembl = ENSMUSG00000025003
| Mm_RefseqmRNA = NM_010003
| Mm_RefseqProtein = NP_034133
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 39564182
| Mm_GenLoc_end = 39621840
| Mm_Uniprot = Q6PER7
}}
}}
'''Cytochrome P450, family 2, subfamily C, polypeptide 19''', also known as '''CYP2C19''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: CYP2C19 cytochrome P450, family 2, subfamily C, polypeptide 19| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1557| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum and is known to metabolize many xenobiotics, including the anticonvulsive drug mephenytoin, omeprazole, diazepam and some barbiturates. Polymorphism within this gene is associated with variable ability to metabolize mephenytoin, known as the poor metabolizer and extensive metabolizer phenotypes. The gene is located within a cluster of cytochrome P450 genes on chromosome 10q24.<ref>{{cite web | title = Entrez Gene: CYP2C19 cytochrome P450, family 2, subfamily C, polypeptide 19| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1557| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Goldstein JA, de Morais SM |title=Biochemistry and molecular biology of the human CYP2C subfamily. |journal=Pharmacogenetics |volume=4 |issue= 6 |pages= 285-99 |year= 1995 |pmid= 7704034 |doi= }}
*{{cite journal | author=Smith G, Stubbins MJ, Harries LW, Wolf CR |title=Molecular genetics of the human cytochrome P450 monooxygenase superfamily. |journal=Xenobiotica |volume=28 |issue= 12 |pages= 1129-65 |year= 1999 |pmid= 9890157 |doi= }}
*{{cite journal | author=Ding X, Kaminsky LS |title=Human extrahepatic cytochromes P450: function in xenobiotic metabolism and tissue-selective chemical toxicity in the respiratory and gastrointestinal tracts. |journal=Annu. Rev. Pharmacol. Toxicol. |volume=43 |issue= |pages= 149-73 |year= 2003 |pmid= 12171978 |doi= 10.1146/annurev.pharmtox.43.100901.140251 }}
*{{cite journal | author=Romkes M, Faletto MB, Blaisdell JA, ''et al.'' |title=Cloning and expression of complementary DNAs for multiple members of the human cytochrome P450IIC subfamily. |journal=Biochemistry |volume=30 |issue= 13 |pages= 3247-55 |year= 1991 |pmid= 2009263 |doi= }}
*{{cite journal | author=Meier UT, Meyer UA |title=Genetic polymorphism of human cytochrome P-450 (S)-mephenytoin 4-hydroxylase. Studies with human autoantibodies suggest a functionally altered cytochrome P-450 isozyme as cause of the genetic deficiency. |journal=Biochemistry |volume=26 |issue= 25 |pages= 8466-74 |year= 1988 |pmid= 3442670 |doi= }}
*{{cite journal | author=De Morais SM, Wilkinson GR, Blaisdell J, ''et al.'' |title=Identification of a new genetic defect responsible for the polymorphism of (S)-mephenytoin metabolism in Japanese. |journal=Mol. Pharmacol. |volume=46 |issue= 4 |pages= 594-8 |year= 1994 |pmid= 7969038 |doi= }}
*{{cite journal | author=Romkes M, Faletto MB, Blaisdell JA, ''et al.'' |title=Cloning and expression of complementary DNAs for multiple members of the human cytochrome PH50IIC subfamily. |journal=Biochemistry |volume=32 |issue= 5 |pages= 1390 |year= 1993 |pmid= 8095407 |doi= }}
*{{cite journal | author=Goldstein JA, Faletto MB, Romkes-Sparks M, ''et al.'' |title=Evidence that CYP2C19 is the major (S)-mephenytoin 4'-hydroxylase in humans. |journal=Biochemistry |volume=33 |issue= 7 |pages= 1743-52 |year= 1994 |pmid= 8110777 |doi= }}
*{{cite journal | author=de Morais SM, Wilkinson GR, Blaisdell J, ''et al.'' |title=The major genetic defect responsible for the polymorphism of S-mephenytoin metabolism in humans. |journal=J. Biol. Chem. |volume=269 |issue= 22 |pages= 15419-22 |year= 1994 |pmid= 8195181 |doi= }}
*{{cite journal | author=Gray IC, Nobile C, Muresu R, ''et al.'' |title=A 2.4-megabase physical map spanning the CYP2C gene cluster on chromosome 10q24. |journal=Genomics |volume=28 |issue= 2 |pages= 328-32 |year= 1996 |pmid= 8530044 |doi= 10.1006/geno.1995.1149 }}
*{{cite journal | author=Karam WG, Goldstein JA, Lasker JM, Ghanayem BI |title=Human CYP2C19 is a major omeprazole 5-hydroxylase, as demonstrated with recombinant cytochrome P450 enzymes. |journal=Drug Metab. Dispos. |volume=24 |issue= 10 |pages= 1081-7 |year= 1997 |pmid= 8894508 |doi= }}
*{{cite journal | author=Xiao ZS, Goldstein JA, Xie HG, ''et al.'' |title=Differences in the incidence of the CYP2C19 polymorphism affecting the S-mephenytoin phenotype in Chinese Han and Bai populations and identification of a new rare CYP2C19 mutant allele. |journal=J. Pharmacol. Exp. Ther. |volume=281 |issue= 1 |pages= 604-9 |year= 1997 |pmid= 9103550 |doi= }}
*{{cite journal | author=Guengerich FP, Johnson WW |title=Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: rapid reduction in the absence of substrate and variations among cytochrome P450 systems. |journal=Biochemistry |volume=36 |issue= 48 |pages= 14741-50 |year= 1998 |pmid= 9398194 |doi= 10.1021/bi9719399 }}
*{{cite journal | author=Ferguson RJ, De Morais SM, Benhamou S, ''et al.'' |title=A new genetic defect in human CYP2C19: mutation of the initiation codon is responsible for poor metabolism of S-mephenytoin. |journal=J. Pharmacol. Exp. Ther. |volume=284 |issue= 1 |pages= 356-61 |year= 1998 |pmid= 9435198 |doi= }}
*{{cite journal | author=Ibeanu GC, Goldstein JA, Meyer U, ''et al.'' |title=Identification of new human CYP2C19 alleles (CYP2C19*6 and CYP2C19*2B) in a Caucasian poor metabolizer of mephenytoin. |journal=J. Pharmacol. Exp. Ther. |volume=286 |issue= 3 |pages= 1490-5 |year= 1998 |pmid= 9732415 |doi= }}
*{{cite journal | author=Ibeanu GC, Blaisdell J, Ghanayem BI, ''et al.'' |title=An additional defective allele, CYP2C19*5, contributes to the S-mephenytoin poor metabolizer phenotype in Caucasians. |journal=Pharmacogenetics |volume=8 |issue= 2 |pages= 129-35 |year= 1999 |pmid= 10022751 |doi= }}
*{{cite journal | author=Foster DJ, Somogyi AA, Bochner F |title=Methadone N-demethylation in human liver microsomes: lack of stereoselectivity and involvement of CYP3A4. |journal=British journal of clinical pharmacology |volume=47 |issue= 4 |pages= 403-12 |year= 1999 |pmid= 10233205 |doi= }}
*{{cite journal | author=Ibeanu GC, Blaisdell J, Ferguson RJ, ''et al.'' |title=A novel transversion in the intron 5 donor splice junction of CYP2C19 and a sequence polymorphism in exon 3 contribute to the poor metabolizer phenotype for the anticonvulsant drug S-mephenytoin. |journal=J. Pharmacol. Exp. Ther. |volume=290 |issue= 2 |pages= 635-40 |year= 1999 |pmid= 10411572 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DMPK... {November 15, 2007 5:41:01 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 5:41:36 PM PST}
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{{PBB_Controls
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| update_protein_box = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_DMPK_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1wt6.
| PDB = {{PDB2|1wt6}}
| Name = Dystrophia myotonica-protein kinase
| HGNCid = 2933
| Symbol = DMPK
| AltSymbols =; DM; DM1; DM1PK; DMK; MDPK; MT-PK
| OMIM = 605377
| ECnumber =
| Homologene = 3247
| MGIid = 94906
| GeneAtlas_image1 = PBB_GE_DMPK_37996_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_DMPK_217066_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_DMPK_217661_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component =
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006936 |text = muscle contraction}} {{GNF_GO|id=GO:0008016 |text = regulation of heart contraction}} {{GNF_GO|id=GO:0051056 |text = regulation of small GTPase mediated signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1760
| Hs_Ensembl = ENSG00000104936
| Hs_RefseqProtein = NP_001075029
| Hs_RefseqmRNA = NM_001081560
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 50965579
| Hs_GenLoc_end = 50977469
| Hs_Uniprot = Q09013
| Mm_EntrezGene = 13400
| Mm_Ensembl = ENSMUSG00000030409
| Mm_RefseqmRNA = XM_986224
| Mm_RefseqProtein = XP_991318
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 18242463
| Mm_GenLoc_end = 18252340
| Mm_Uniprot = Q05CL1
}}
}}
'''Dystrophia myotonica-protein kinase''', also known as '''DMPK''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: DMPK dystrophia myotonica-protein kinase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1760| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a serine-threonine kinase that is closely related to other kinases that interact with members of the Rho family of small GTPases. Substrates for this enzyme include myogenin, the beta-subunit of the L-type calcium channels, and phospholemman. The 3' untranslated region of this gene contains 5-37 copies of a CTG trinucleotide repeat. Expansion of this unstable motif to 50-5,000 copies causes myotonic dystrophy type I, which increases in severity with increasing repeat element copy number. Repeat expansion is associated with condensation of local chromatin structure that disrupts the expression of genes in this region. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined.<ref>{{cite web | title = Entrez Gene: DMPK dystrophia myotonica-protein kinase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1760| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Groenen P, Wieringa B |title=Expanding complexity in myotonic dystrophy. |journal=Bioessays |volume=20 |issue= 11 |pages= 901-12 |year= 1999 |pmid= 9872056 |doi= 10.1002/(SICI)1521-1878(199811)20:11<901::AID-BIES5>3.0.CO;2-0 }}
*{{cite journal | author=Jansen G, Mahadevan M, Amemiya C, ''et al.'' |title=Characterization of the myotonic dystrophy region predicts multiple protein isoform-encoding mRNAs. |journal=Nat. Genet. |volume=1 |issue= 4 |pages= 261-6 |year= 1993 |pmid= 1302022 |doi= 10.1038/ng0792-261 }}
*{{cite journal | author=Tsilfidis C, MacKenzie AE, Mettler G, ''et al.'' |title=Correlation between CTG trinucleotide repeat length and frequency of severe congenital myotonic dystrophy. |journal=Nat. Genet. |volume=1 |issue= 3 |pages= 192-5 |year= 1993 |pmid= 1303233 |doi= 10.1038/ng0692-192 }}
*{{cite journal | author=Brook JD, McCurrach ME, Harley HG, ''et al.'' |title=Molecular basis of myotonic dystrophy: expansion of a trinucleotide (CTG) repeat at the 3' end of a transcript encoding a protein kinase family member. |journal=Cell |volume=68 |issue= 4 |pages= 799-808 |year= 1992 |pmid= 1310900 |doi= }}
*{{cite journal | author=Mahadevan M, Tsilfidis C, Sabourin L, ''et al.'' |title=Myotonic dystrophy mutation: an unstable CTG repeat in the 3' untranslated region of the gene. |journal=Science |volume=255 |issue= 5049 |pages= 1253-5 |year= 1992 |pmid= 1546325 |doi= }}
*{{cite journal | author=Fu YH, Pizzuti A, Fenwick RG, ''et al.'' |title=An unstable triplet repeat in a gene related to myotonic muscular dystrophy. |journal=Science |volume=255 |issue= 5049 |pages= 1256-8 |year= 1992 |pmid= 1546326 |doi= }}
*{{cite journal | author=Harley HG, Walsh KV, Rundle S, ''et al.'' |title=Localisation of the myotonic dystrophy locus to 19q13.2-19q13.3 and its relationship to twelve polymorphic loci on 19q. |journal=Hum. Genet. |volume=87 |issue= 1 |pages= 73-80 |year= 1991 |pmid= 2037285 |doi= }}
*{{cite journal | author=Gennarelli M, Lucarelli M, Zelano G, ''et al.'' |title=Different expression of the myotonin protein kinase gene in discrete areas of human brain. |journal=Biochem. Biophys. Res. Commun. |volume=216 |issue= 2 |pages= 489-94 |year= 1995 |pmid= 7488138 |doi= 10.1006/bbrc.1995.2649 }}
*{{cite journal | author=Shaw DJ, McCurrach M, Rundle SA, ''et al.'' |title=Genomic organization and transcriptional units at the myotonic dystrophy locus. |journal=Genomics |volume=18 |issue= 3 |pages= 673-9 |year= 1994 |pmid= 7905855 |doi= }}
*{{cite journal | author=Sasagawa N, Sorimachi H, Maruyama K, ''et al.'' |title=Expression of a novel human myotonin protein kinase (MtPK) cDNA clone which encodes a protein with a thymopoietin-like domain in COS cells. |journal=FEBS Lett. |volume=351 |issue= 1 |pages= 22-6 |year= 1994 |pmid= 8076686 |doi= }}
*{{cite journal | author=van der Ven PF, Jansen G, van Kuppevelt TH, ''et al.'' |title=Myotonic dystrophy kinase is a component of neuromuscular junctions. |journal=Hum. Mol. Genet. |volume=2 |issue= 11 |pages= 1889-94 |year= 1994 |pmid= 8281152 |doi= }}
*{{cite journal | author=Carango P, Noble JE, Marks HG, Funanage VL |title=Absence of myotonic dystrophy protein kinase (DMPK) mRNA as a result of a triplet repeat expansion in myotonic dystrophy. |journal=Genomics |volume=18 |issue= 2 |pages= 340-8 |year= 1994 |pmid= 8288237 |doi= 10.1006/geno.1993.1474 }}
*{{cite journal | author=Jansen G, Bartolomei M, Kalscheuer V, ''et al.'' |title=No imprinting involved in the expression of DM-kinase mRNAs in mouse and human tissues. |journal=Hum. Mol. Genet. |volume=2 |issue= 8 |pages= 1221-7 |year= 1993 |pmid= 8401505 |doi= }}
*{{cite journal | author=Fu YH, Friedman DL, Richards S, ''et al.'' |title=Decreased expression of myotonin-protein kinase messenger RNA and protein in adult form of myotonic dystrophy. |journal=Science |volume=260 |issue= 5105 |pages= 235-8 |year= 1993 |pmid= 8469976 |doi= }}
*{{cite journal | author=Mahadevan MS, Amemiya C, Jansen G, ''et al.'' |title=Structure and genomic sequence of the myotonic dystrophy (DM kinase) gene. |journal=Hum. Mol. Genet. |volume=2 |issue= 3 |pages= 299-304 |year= 1993 |pmid= 8499920 |doi= }}
*{{cite journal | author=Boucher CA, King SK, Carey N, ''et al.'' |title=A novel homeodomain-encoding gene is associated with a large CpG island interrupted by the myotonic dystrophy unstable (CTG)n repeat. |journal=Hum. Mol. Genet. |volume=4 |issue= 10 |pages= 1919-25 |year= 1996 |pmid= 8595416 |doi= }}
*{{cite journal | author=Roberts R, Timchenko NA, Miller JW, ''et al.'' |title=Altered phosphorylation and intracellular distribution of a (CUG)n triplet repeat RNA-binding protein in patients with myotonic dystrophy and in myotonin protein kinase knockout mice. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 24 |pages= 13221-6 |year= 1998 |pmid= 9371827 |doi= }}
*{{cite journal | author=Suzuki A, Sugiyama Y, Hayashi Y, ''et al.'' |title=MKBP, a novel member of the small heat shock protein family, binds and activates the myotonic dystrophy protein kinase. |journal=J. Cell Biol. |volume=140 |issue= 5 |pages= 1113-24 |year= 1998 |pmid= 9490724 |doi= }}
*{{cite journal | author=Pham YC, Man N, Lam LT, Morris GE |title=Localization of myotonic dystrophy protein kinase in human and rabbit tissues using a new panel of monoclonal antibodies. |journal=Hum. Mol. Genet. |volume=7 |issue= 12 |pages= 1957-65 |year= 1998 |pmid= 9811941 |doi= }}
}}
{{refend}}
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