Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 00:34, 15 November 2007 (UTC)[edit]
Proteins without matches (12)[edit]
Proteins with a High Potential Match (8)[edit]
Redirected Proteins (5)[edit]
Manual Inspection (Page not found) (20)[edit]
Updated (5)[edit]
Protein Status Grid - Date: 00:34, 15 November 2007 (UTC)[edit]
Vebose Log - Date: 00:34, 15 November 2007 (UTC)[edit]
- INFO: Beginning work on ADRB3... {November 14, 2007 4:10:33 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:11:01 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 =
| 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]].
<!-- 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 ALPL... {November 14, 2007 4:11:51 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:12:29 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Alkaline phosphatase, liver/bone/kidney
| HGNCid = 438
| Symbol = ALPL
| AltSymbols =; AP-TNAP; FLJ40094; HOPS; MGC161443; TNAP; TNSALP
| OMIM = 171760
| ECnumber =
| Homologene = 37314
| MGIid = 87983
| GeneAtlas_image1 = PBB_GE_ALPL_215783_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004035 |text = alkaline phosphatase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0048503 |text = GPI anchor binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0001503 |text = ossification}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 249
| Hs_Ensembl = ENSG00000162551
| Hs_RefseqProtein = NP_000469
| Hs_RefseqmRNA = NM_000478
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 21708452
| Hs_GenLoc_end = 21777492
| Hs_Uniprot = P05186
| Mm_EntrezGene = 11647
| Mm_Ensembl = ENSMUSG00000028766
| Mm_RefseqmRNA = NM_007431
| Mm_RefseqProtein = NP_031457
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 137013809
| Mm_GenLoc_end = 137068395
| Mm_Uniprot = Q3TJD3
}}
}}
'''Alkaline phosphatase, liver/bone/kidney''', also known as '''ALPL''', 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 = There are at least four distinct but related alkaline phosphatases: intestinal, placental, placental-like, and liver/bone/kidney (tissue non-specific). The first three are located together on chromosome 2 while the tissue non-specific form is located on chromosome 1. The product of this gene is a membrane bound glycosylated enzyme that is not expressed in any particular tissue and is, therefore, referred to as the tissue-nonspecific form of the enzyme. The exact physiological function of the alkaline phosphatases is not known. A proposed function of this form of the enzyme is matrix mineralization, however, mice that lack a functional form of this enzyme show normal skeletal development. This enzyme has been linked directly to a disorder known as hypophosphatasia, a disorder that is characterized by hypercalcemia and includes skeletal defects. The character of this disorder can vary, however, depending on the specific mutation since this determines age of onset and severity of symptoms.<ref>{{cite web | title = Entrez Gene: ALPL alkaline phosphatase, liver/bone/kidney| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=249| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Mornet E |title=Hypophosphatasia: the mutations in the tissue-nonspecific alkaline phosphatase gene. |journal=Hum. Mutat. |volume=15 |issue= 4 |pages= 309-15 |year= 2000 |pmid= 10737975 |doi= 10.1002/(SICI)1098-1004(200004)15:4<309::AID-HUMU2>3.0.CO;2-C }}
*{{cite journal | author=Khandwala HM, Mumm S, Whyte MP |title=Low serum alkaline phosphatase activity and pathologic fracture: case report and brief review of hypophosphatasia diagnosed in adulthood. |journal=Endocrine practice : official journal of the American College of Endocrinology and the American Association of Clinical Endocrinologists |volume=12 |issue= 6 |pages= 676-81 |year= 2007 |pmid= 17229666 |doi= }}
*{{cite journal | author=Nye KE, Riley GA, Pinching AJ |title=The defect seen in the phosphatidylinositol hydrolysis pathway in HIV-infected lymphocytes and lymphoblastoid cells is due to inhibition of the inositol 1,4,5-trisphosphate 1,3,4,5-tetrakisphosphate 5-phosphomonoesterase. |journal=Clin. Exp. Immunol. |volume=89 |issue= 1 |pages= 89-93 |year= 1992 |pmid= 1321014 |doi= }}
*{{cite journal | author=Henthorn PS, Raducha M, Fedde KN, ''et al.'' |title=Different missense mutations at the tissue-nonspecific alkaline phosphatase gene locus in autosomal recessively inherited forms of mild and severe hypophosphatasia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 20 |pages= 9924-8 |year= 1992 |pmid= 1409720 |doi= }}
*{{cite journal | author=Nishihara Y, Hayashi Y, Adachi T, ''et al.'' |title=Chemical nature of intestinal-type alkaline phosphatase in human kidney. |journal=Clin. Chem. |volume=38 |issue= 12 |pages= 2539-42 |year= 1993 |pmid= 1458595 |doi= }}
*{{cite journal | author=Fedde KN, Whyte MP |title=Alkaline phosphatase (tissue-nonspecific isoenzyme) is a phosphoethanolamine and pyridoxal-5'-phosphate ectophosphatase: normal and hypophosphatasia fibroblast study. |journal=Am. J. Hum. Genet. |volume=47 |issue= 5 |pages= 767-75 |year= 1990 |pmid= 2220817 |doi= }}
*{{cite journal | author=Kishi F, Matsuura S, Kajii T |title=Nucleotide sequence of the human liver-type alkaline phosphatase cDNA. |journal=Nucleic Acids Res. |volume=17 |issue= 5 |pages= 2129 |year= 1989 |pmid= 2928120 |doi= }}
*{{cite journal | author=Weiss MJ, Ray K, Henthorn PS, ''et al.'' |title=Structure of the human liver/bone/kidney alkaline phosphatase gene. |journal=J. Biol. Chem. |volume=263 |issue= 24 |pages= 12002-10 |year= 1988 |pmid= 3165380 |doi= }}
*{{cite journal | author=Weiss MJ, Cole DE, Ray K, ''et al.'' |title=A missense mutation in the human liver/bone/kidney alkaline phosphatase gene causing a lethal form of hypophosphatasia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 20 |pages= 7666-9 |year= 1988 |pmid= 3174660 |doi= }}
*{{cite journal | author=Smith M, Weiss MJ, Griffin CA, ''et al.'' |title=Regional assignment of the gene for human liver/bone/kidney alkaline phosphatase to chromosome 1p36.1-p34. |journal=Genomics |volume=2 |issue= 2 |pages= 139-43 |year= 1988 |pmid= 3410475 |doi= }}
*{{cite journal | author=Swallow DM, Povey S, Parkar M, ''et al.'' |title=Mapping of the gene coding for the human liver/bone/kidney isozyme of alkaline phosphatase to chromosome 1. |journal=Ann. Hum. Genet. |volume=50 |issue= Pt 3 |pages= 229-35 |year= 1988 |pmid= 3446011 |doi= }}
*{{cite journal | author=Weiss MJ, Henthorn PS, Lafferty MA, ''et al.'' |title=Isolation and characterization of a cDNA encoding a human liver/bone/kidney-type alkaline phosphatase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 19 |pages= 7182-6 |year= 1986 |pmid= 3532105 |doi= }}
*{{cite journal | author=Garattini E, Hua JC, Pan YC, Udenfriend S |title=Human liver alkaline phosphatase, purification and partial sequencing: homology with the placental isozyme. |journal=Arch. Biochem. Biophys. |volume=245 |issue= 2 |pages= 331-7 |year= 1986 |pmid= 3954357 |doi= }}
*{{cite journal | author=Goldstein DJ, Blasco L, Harris H |title=Placental alkaline phosphatase in nonmalignant human cervix. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=77 |issue= 7 |pages= 4226-8 |year= 1981 |pmid= 6933471 |doi= }}
*{{cite journal | author=Sato N, Takahashi Y, Asano S |title=Preferential usage of the bone-type leader sequence for the transcripts of liver/bone/kidney-type alkaline phosphatase gene in neutrophilic granulocytes. |journal=Blood |volume=83 |issue= 4 |pages= 1093-101 |year= 1994 |pmid= 7509208 |doi= }}
*{{cite journal | author=Orimo H, Hayashi Z, Watanabe A, ''et al.'' |title=Novel missense and frameshift mutations in the tissue-nonspecific alkaline phosphatase gene in a Japanese patient with hypophosphatasia. |journal=Hum. Mol. Genet. |volume=3 |issue= 9 |pages= 1683-4 |year= 1995 |pmid= 7833929 |doi= }}
*{{cite journal | author=Greenberg CR, Taylor CL, Haworth JC, ''et al.'' |title=A homoallelic Gly317-->Asp mutation in ALPL causes the perinatal (lethal) form of hypophosphatasia in Canadian mennonites. |journal=Genomics |volume=17 |issue= 1 |pages= 215-7 |year= 1993 |pmid= 8406453 |doi= 10.1006/geno.1993.1305 }}
*{{cite journal | author=Ozono K, Yamagata M, Michigami T, ''et al.'' |title=Identification of novel missense mutations (Phe310Leu and Gly439Arg) in a neonatal case of hypophosphatasia. |journal=J. Clin. Endocrinol. Metab. |volume=81 |issue= 12 |pages= 4458-61 |year= 1997 |pmid= 8954059 |doi= }}
*{{cite journal | author=Orimo H, Goseki-Sone M, Sato S, Shimada T |title=Detection of deletion 1154-1156 hypophosphatasia mutation using TNSALP exon amplification. |journal=Genomics |volume=42 |issue= 2 |pages= 364-6 |year= 1997 |pmid= 9192863 |doi= 10.1006/geno.1997.4733 }}
*{{cite journal | author=Sugimoto N, Iwamoto S, Hoshino Y, Kajii E |title=A novel missense mutation of the tissue-nonspecific alkaline phosphatase gene detected in a patient with hypophosphatasia. |journal=J. Hum. Genet. |volume=43 |issue= 3 |pages= 160-4 |year= 1998 |pmid= 9747027 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CD34... {November 14, 2007 4:13:04 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:13:33 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- 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 = CD34 molecule
| HGNCid = 1662
| Symbol = CD34
| AltSymbols =;
| OMIM = 142230
| ECnumber =
| Homologene = 1343
| MGIid = 88329
| GeneAtlas_image1 = PBB_GE_CD34_209543_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0030246 |text = carbohydrate binding}}
| Component = {{GNF_GO|id=GO:0009897 |text = external side of 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:0016337 |text = cell-cell adhesion}} {{GNF_GO|id=GO:0050900 |text = leukocyte migration}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 947
| Hs_Ensembl = ENSG00000174059
| Hs_RefseqProtein = NP_001020280
| Hs_RefseqmRNA = NM_001025109
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 206116942
| Hs_GenLoc_end = 206151370
| Hs_Uniprot = P28906
| Mm_EntrezGene = 12490
| Mm_Ensembl = ENSMUSG00000016494
| Mm_RefseqmRNA = NM_133654
| Mm_RefseqProtein = NP_598415
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 196639610
| Mm_GenLoc_end = 196662005
| Mm_Uniprot = Q3TJP6
}}
}}
'''CD34 molecule''', also known as '''CD34''', 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 = CD34 is a monomeric cell surface antigen with a molecular mass of approximately 110 kD that is selectively expressed on human hematopoietic progenitor cells.[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: CD34 CD34 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=947| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Simmons DL, Satterthwaite AB, Tenen DG, Seed B |title=Molecular cloning of a cDNA encoding CD34, a sialomucin of human hematopoietic stem cells. |journal=J. Immunol. |volume=148 |issue= 1 |pages= 267-71 |year= 1992 |pmid= 1370171 |doi= }}
*{{cite journal | author=Satterthwaite AB, Burn TC, Le Beau MM, Tenen DG |title=Structure of the gene encoding CD34, a human hematopoietic stem cell antigen. |journal=Genomics |volume=12 |issue= 4 |pages= 788-94 |year= 1992 |pmid= 1374051 |doi= }}
*{{cite journal | author=Fina L, Molgaard HV, Robertson D, ''et al.'' |title=Expression of the CD34 gene in vascular endothelial cells. |journal=Blood |volume=75 |issue= 12 |pages= 2417-26 |year= 1990 |pmid= 1693532 |doi= }}
*{{cite journal | author=Fackler MJ, Civin CI, Sutherland DR, ''et al.'' |title=Activated protein kinase C directly phosphorylates the CD34 antigen on hematopoietic cells. |journal=J. Biol. Chem. |volume=265 |issue= 19 |pages= 11056-61 |year= 1990 |pmid= 1694174 |doi= }}
*{{cite journal | author=Sutherland DR, Watt SM, Dowden G, ''et al.'' |title=Structural and partial amino acid sequence analysis of the human hemopoietic progenitor cell antigen CD34. |journal=Leukemia |volume=2 |issue= 12 |pages= 793-803 |year= 1989 |pmid= 2462139 |doi= }}
*{{cite journal | author=Nakamura Y, Komano H, Nakauchi H |title=Two alternative forms of cDNA encoding CD34. |journal=Exp. Hematol. |volume=21 |issue= 2 |pages= 236-42 |year= 1993 |pmid= 7678811 |doi= }}
*{{cite journal | author=Huyhn A, Dommergues M, Izac B, ''et al.'' |title=Characterization of hematopoietic progenitors from human yolk sacs and embryos. |journal=Blood |volume=86 |issue= 12 |pages= 4474-85 |year= 1996 |pmid= 8541536 |doi= }}
*{{cite journal | author=Tavian M, Coulombel L, Luton D, ''et al.'' |title=Aorta-associated CD34+ hematopoietic cells in the early human embryo. |journal=Blood |volume=87 |issue= 1 |pages= 67-72 |year= 1996 |pmid= 8547678 |doi= }}
*{{cite journal | author=Hillier LD, Lennon G, Becker M, ''et al.'' |title=Generation and analysis of 280,000 human expressed sequence tags. |journal=Genome Res. |volume=6 |issue= 9 |pages= 807-28 |year= 1997 |pmid= 8889549 |doi= }}
*{{cite journal | author=Uchida N, Yang Z, Combs J, ''et al.'' |title=The characterization, molecular cloning, and expression of a novel hematopoietic cell antigen from CD34+ human bone marrow cells. |journal=Blood |volume=89 |issue= 8 |pages= 2706-16 |year= 1997 |pmid= 9108388 |doi= }}
*{{cite journal | author=Ruiz ME, Cicala C, Arthos J, ''et al.'' |title=Peripheral blood-derived CD34+ progenitor cells: CXC chemokine receptor 4 and CC chemokine receptor 5 expression and infection by HIV. |journal=J. Immunol. |volume=161 |issue= 8 |pages= 4169-76 |year= 1998 |pmid= 9780190 |doi= }}
*{{cite journal | author=Kees UR, Ford J |title=Synergistic action of stem-cell factor and interleukin-7 in a human immature T-cell line. |journal=Immunology |volume=96 |issue= 2 |pages= 202-6 |year= 1999 |pmid= 10233696 |doi= }}
*{{cite journal | author=Bistrup A, Bhakta S, Lee JK, ''et al.'' |title=Sulfotransferases of two specificities function in the reconstitution of high endothelial cell ligands for L-selectin. |journal=J. Cell Biol. |volume=145 |issue= 4 |pages= 899-910 |year= 1999 |pmid= 10330415 |doi= }}
*{{cite journal | author=Lataillade JJ, Clay D, Dupuy C, ''et al.'' |title=Chemokine SDF-1 enhances circulating CD34(+) cell proliferation in synergy with cytokines: possible role in progenitor survival. |journal=Blood |volume=95 |issue= 3 |pages= 756-68 |year= 2000 |pmid= 10648383 |doi= }}
*{{cite journal | author=Felschow DM, McVeigh ML, Hoehn GT, ''et al.'' |title=The adapter protein CrkL associates with CD34. |journal=Blood |volume=97 |issue= 12 |pages= 3768-75 |year= 2001 |pmid= 11389015 |doi= }}
*{{cite journal | author=Dobo I, Robillard N, Pineau D, ''et al.'' |title=Use of pathology-specific peripheral blood CD34 thresholds to predict leukapheresis CD34 content with optimal accuracy: a bicentric analysis of 299 leukaphereses. |journal=Ann. Hematol. |volume=80 |issue= 11 |pages= 639-46 |year= 2001 |pmid= 11757722 |doi= }}
*{{cite journal | author=Hogan CJ, Shpall EJ, Keller G |title=Differential long-term and multilineage engraftment potential from subfractions of human CD34+ cord blood cells transplanted into NOD/SCID mice. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 1 |pages= 413-8 |year= 2002 |pmid= 11782553 |doi= 10.1073/pnas.012336799 }}
*{{cite journal | author=Krauter J, Hartl M, Hambach L, ''et al.'' |title=Receptor-mediated endocytosis of CD34 on hematopoietic cells after stimulation with the monoclonal antibody anti-HPCA-1. |journal=J. Hematother. Stem Cell Res. |volume=10 |issue= 6 |pages= 863-71 |year= 2003 |pmid= 11798512 |doi= 10.1089/152581601317210953 }}
*{{cite journal | author=Okuno Y, Iwasaki H, Huettner CS, ''et al.'' |title=Differential regulation of the human and murine CD34 genes in hematopoietic stem cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 9 |pages= 6246-51 |year= 2002 |pmid= 11983914 |doi= 10.1073/pnas.092027799 }}
*{{cite journal | author=Hotfilder M, Röttgers S, Rosemann A, ''et al.'' |title=Immature CD34+CD19- progenitor/stem cells in TEL/AML1-positive acute lymphoblastic leukemia are genetically and functionally normal. |journal=Blood |volume=100 |issue= 2 |pages= 640-6 |year= 2002 |pmid= 12091359 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ECGF1... {November 14, 2007 4:13:33 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:14:15 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_ECGF1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1uou.
| PDB = {{PDB2|1uou}}, {{PDB2|2j0f}}
| Name = Endothelial cell growth factor 1 (platelet-derived)
| HGNCid = 3148
| Symbol = ECGF1
| AltSymbols =; MNGIE; PDECGF; TP; hPD-ECGF
| OMIM = 131222
| ECnumber =
| Homologene = 1474
| MGIid = 1920212
| GeneAtlas_image1 = PBB_GE_ECGF1_204858_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ECGF1_205241_at_tn.png
| Function = {{GNF_GO|id=GO:0005161 |text = platelet-derived growth factor receptor binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}} {{GNF_GO|id=GO:0009032 |text = thymidine phosphorylase activity}} {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}}
| Process = {{GNF_GO|id=GO:0000002 |text = mitochondrial genome maintenance}} {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0006206 |text = pyrimidine base metabolic process}} {{GNF_GO|id=GO:0006220 |text = pyrimidine nucleotide metabolic process}} {{GNF_GO|id=GO:0006260 |text = DNA replication}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1890
| Hs_Ensembl = ENSG00000025708
| Hs_RefseqProtein = NP_001944
| Hs_RefseqmRNA = NM_001953
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 49311047
| Hs_GenLoc_end = 49315321
| Hs_Uniprot = P19971
| Mm_EntrezGene = 72962
| Mm_Ensembl = ENSMUSG00000022615
| Mm_RefseqmRNA = NM_138302
| Mm_RefseqProtein = NP_612175
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 89199698
| Mm_GenLoc_end = 89204806
| Mm_Uniprot = Q99N42
}}
}}
'''Endothelial cell growth factor 1 (platelet-derived)''', also known as '''ECGF1''', 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 = Platelet-derived endothelial cell growth factor (ECGF1) is an angiogenic factor which promotes angiogenesis in vivo and stimulates the in vitro growth of a variety of endothelial cells. ECGF1 has a highly restricted target cell specificity acting only on endothelial cells. Because it limits glial cell proliferation, ECGF1 is also known as thymidine phosphorylase and as gliostatin. The ECGF1 gene contains 10 exons spanning more than 4.3 kb. Thymidine phosphorylase activity of ECGF1 in leukocytes from mitochondrial neurogastrointestinal encephalomyopathy (MNGIE) patients was less than 5 percent of controls, indicating that loss-of-function mutations in thymidine phosphorylase cause MNGIE.<ref>{{cite web | title = Entrez Gene: ECGF1 endothelial cell growth factor 1 (platelet-derived)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1890| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Yang Q, Yoshimura G, Mori I, ''et al.'' |title=Thymidine phosphorylase and breast carcinoma. |journal=Anticancer Res. |volume=22 |issue= 4 |pages= 2355-60 |year= 2002 |pmid= 12174926 |doi= }}
*{{cite journal | author=Asai K, Nakanishi K, Isobe I, ''et al.'' |title=Neurotrophic action of gliostatin on cortical neurons. Identity of gliostatin and platelet-derived endothelial cell growth factor. |journal=J. Biol. Chem. |volume=267 |issue= 28 |pages= 20311-6 |year= 1992 |pmid= 1400349 |doi= }}
*{{cite journal | author=Furukawa T, Yoshimura A, Sumizawa T, ''et al.'' |title=Angiogenic factor. |journal=Nature |volume=356 |issue= 6371 |pages= 668 |year= 1992 |pmid= 1570012 |doi= 10.1038/356668a0 }}
*{{cite journal | author=Usuki K, Saras J, Waltenberger J, ''et al.'' |title=Platelet-derived endothelial cell growth factor has thymidine phosphorylase activity. |journal=Biochem. Biophys. Res. Commun. |volume=184 |issue= 3 |pages= 1311-6 |year= 1992 |pmid= 1590793 |doi= }}
*{{cite journal | author=Stenman G, Sahlin P, Dumanski JP, ''et al.'' |title=Regional localization of the human platelet-derived endothelial cell growth factor (ECGF1) gene to chromosome 22q13. |journal=Cytogenet. Cell Genet. |volume=59 |issue= 1 |pages= 22-3 |year= 1992 |pmid= 1733667 |doi= }}
*{{cite journal | author=Hagiwara K, Stenman G, Honda H, ''et al.'' |title=Organization and chromosomal localization of the human platelet-derived endothelial cell growth factor gene. |journal=Mol. Cell. Biol. |volume=11 |issue= 4 |pages= 2125-32 |year= 1991 |pmid= 2005900 |doi= }}
*{{cite journal | author=Ishikawa F, Miyazono K, Hellman U, ''et al.'' |title=Identification of angiogenic activity and the cloning and expression of platelet-derived endothelial cell growth factor. |journal=Nature |volume=338 |issue= 6216 |pages= 557-62 |year= 1989 |pmid= 2467210 |doi= 10.1038/338557a0 }}
*{{cite journal | author=Bardosi A, Creutzfeldt W, DiMauro S, ''et al.'' |title=Myo-, neuro-, gastrointestinal encephalopathy (MNGIE syndrome) due to partial deficiency of cytochrome-c-oxidase. A new mitochondrial multisystem disorder. |journal=Acta Neuropathol. |volume=74 |issue= 3 |pages= 248-58 |year= 1987 |pmid= 2823522 |doi= }}
*{{cite journal | author=Miyazono K, Okabe T, Urabe A, ''et al.'' |title=Purification and properties of an endothelial cell growth factor from human platelets. |journal=J. Biol. Chem. |volume=262 |issue= 9 |pages= 4098-103 |year= 1987 |pmid= 3549724 |doi= }}
*{{cite journal | author=Usuki K, Gonez LJ, Wernstedt C, ''et al.'' |title=Structural properties of 3.0 kb and 3.2 kb transcripts encoding platelet-derived endothelial cell growth factor/thymidine phosphorylase in A431 cells. |journal=Biochim. Biophys. Acta |volume=1222 |issue= 3 |pages= 411-4 |year= 1994 |pmid= 8038210 |doi= }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Hirano M, Silvestri G, Blake DM, ''et al.'' |title=Mitochondrial neurogastrointestinal encephalomyopathy (MNGIE): clinical, biochemical, and genetic features of an autosomal recessive mitochondrial disorder. |journal=Neurology |volume=44 |issue= 4 |pages= 721-7 |year= 1994 |pmid= 8164833 |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=Stevenson DP, Milligan SR, Collins WP |title=Effects of platelet-derived endothelial cell growth factor/thymidine phosphorylase, substrate, and products in a three-dimensional model of angiogenesis. |journal=Am. J. Pathol. |volume=152 |issue= 6 |pages= 1641-6 |year= 1998 |pmid= 9626068 |doi= }}
*{{cite journal | author=Nishino I, Spinazzola A, Hirano M |title=Thymidine phosphorylase gene mutations in MNGIE, a human mitochondrial disorder. |journal=Science |volume=283 |issue= 5402 |pages= 689-92 |year= 1999 |pmid= 9924029 |doi= }}
*{{cite journal | author=Asgari MM, Haggerty JG, McNiff JM, ''et al.'' |title=Expression and localization of thymidine phosphorylase/platelet-derived endothelial cell growth factor in skin and cutaneous tumors. |journal=J. Cutan. Pathol. |volume=26 |issue= 6 |pages= 287-94 |year= 1999 |pmid= 10472757 |doi= }}
*{{cite journal | author=Loftus BJ, Kim UJ, Sneddon VP, ''et al.'' |title=Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q. |journal=Genomics |volume=60 |issue= 3 |pages= 295-308 |year= 1999 |pmid= 10493829 |doi= 10.1006/geno.1999.5927 }}
*{{cite journal | author=Sivridis E, Giatromanolaki A, Koukourakis MI, ''et al.'' |title=Thymidine phosphorylase expression in normal and hyperplastic endometrium. |journal=J. Clin. Pathol. |volume=53 |issue= 9 |pages= 704-8 |year= 2000 |pmid= 11041061 |doi= }}
*{{cite journal | author=Komatsu T, Yamazaki H, Shimada N, ''et al.'' |title=Involvement of microsomal cytochrome P450 and cytosolic thymidine phosphorylase in 5-fluorouracil formation from tegafur in human liver. |journal=Clin. Cancer Res. |volume=7 |issue= 3 |pages= 675-81 |year= 2001 |pmid= 11297264 |doi= }}
*{{cite journal | author=Kojima H, Shijubo N, Abe S |title=Thymidine phosphorylase and vascular endothelial growth factor in patients with Stage I lung adenocarcinoma. |journal=Cancer |volume=94 |issue= 4 |pages= 1083-93 |year= 2002 |pmid= 11920479 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on EIF4G1... {November 14, 2007 4:14:16 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:14:55 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 = PBB_Protein_EIF4G1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ug3.
| PDB = {{PDB2|1ug3}}
| Name = Eukaryotic translation initiation factor 4 gamma, 1
| HGNCid = 3296
| Symbol = EIF4G1
| AltSymbols =; EIF4F; DKFZp686A1451; EIF4G; p220
| OMIM = 600495
| ECnumber =
| Homologene = 28096
| MGIid = 2384784
| GeneAtlas_image1 = PBB_GE_EIF4G1_208624_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_EIF4G1_208625_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0003743 |text = translation initiation factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0016281 |text = eukaryotic translation initiation factor 4F complex}}
| Process = {{GNF_GO|id=GO:0006446 |text = regulation of translational initiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1981
| Hs_Ensembl = ENSG00000114867
| Hs_RefseqProtein = NP_004944
| Hs_RefseqmRNA = NM_004953
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 185515033
| Hs_GenLoc_end = 185535839
| Hs_Uniprot = Q04637
| Mm_EntrezGene = 208643
| Mm_Ensembl = ENSMUSG00000045983
| Mm_RefseqmRNA = NM_001005331
| Mm_RefseqProtein = NP_001005331
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 20586292
| Mm_GenLoc_end = 20606426
| Mm_Uniprot = Q3UTK0
}}
}}
'''Eukaryotic translation initiation factor 4 gamma, 1''', also known as '''EIF4G1''', 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 component of the protein complex EIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure, and recruitment of mRNA to the ribosome. Alternative splicing results in five transcript variants encoding four distinct isoforms.<ref>{{cite web | title = Entrez Gene: EIF4G1 eukaryotic translation initiation factor 4 gamma, 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1981| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Gingras AC, Raught B, Sonenberg N |title=eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. |journal=Annu. Rev. Biochem. |volume=68 |issue= |pages= 913-63 |year= 2000 |pmid= 10872469 |doi= 10.1146/annurev.biochem.68.1.913 }}
*{{cite journal | author=Yan R, Rychlik W, Etchison D, Rhoads RE |title=Amino acid sequence of the human protein synthesis initiation factor eIF-4 gamma. |journal=J. Biol. Chem. |volume=267 |issue= 32 |pages= 23226-31 |year= 1992 |pmid= 1429670 |doi= }}
*{{cite journal | author=Yan R, Rhoads RE |title=Human protein synthesis initiation factor eIF-4 gamma is encoded by a single gene (EIF4G) that maps to chromosome 3q27-qter. |journal=Genomics |volume=26 |issue= 2 |pages= 394-8 |year= 1995 |pmid= 7601469 |doi= }}
*{{cite journal | author=Mader S, Lee H, Pause A, Sonenberg N |title=The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins. |journal=Mol. Cell. Biol. |volume=15 |issue= 9 |pages= 4990-7 |year= 1995 |pmid= 7651417 |doi= }}
*{{cite journal | author=Pause A, Belsham GJ, Gingras AC, ''et al.'' |title=Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function. |journal=Nature |volume=371 |issue= 6500 |pages= 762-7 |year= 1994 |pmid= 7935836 |doi= 10.1038/371762a0 }}
*{{cite journal | author=Lamphear BJ, Yan R, Yang F, ''et al.'' |title=Mapping the cleavage site in protein synthesis initiation factor eIF-4 gamma of the 2A proteases from human Coxsackievirus and rhinovirus. |journal=J. Biol. Chem. |volume=268 |issue= 26 |pages= 19200-3 |year= 1993 |pmid= 8396129 |doi= }}
*{{cite journal | author=Haghighat A, Mader S, Pause A, Sonenberg N |title=Repression of cap-dependent translation by 4E-binding protein 1: competition with p220 for binding to eukaryotic initiation factor-4E. |journal=EMBO J. |volume=14 |issue= 22 |pages= 5701-9 |year= 1996 |pmid= 8521827 |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=Lamphear BJ, Rhoads RE |title=A single amino acid change in protein synthesis initiation factor 4G renders cap-dependent translation resistant to picornaviral 2A proteases. |journal=Biochemistry |volume=35 |issue= 49 |pages= 15726-33 |year= 1997 |pmid= 8961935 |doi= 10.1021/bi961864t }}
*{{cite journal | author=Brass N, Heckel D, Sahin U, ''et al.'' |title=Translation initiation factor eIF-4gamma is encoded by an amplified gene and induces an immune response in squamous cell lung carcinoma. |journal=Hum. Mol. Genet. |volume=6 |issue= 1 |pages= 33-9 |year= 1997 |pmid= 9002667 |doi= }}
*{{cite journal | author=Eberle J, Krasagakis K, Orfanos CE |title=Translation initiation factor eIF-4A1 mRNA is consistently overexpressed in human melanoma cells in vitro. |journal=Int. J. Cancer |volume=71 |issue= 3 |pages= 396-401 |year= 1997 |pmid= 9139875 |doi= }}
*{{cite journal | author=Imataka H, Sonenberg N |title=Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A. |journal=Mol. Cell. Biol. |volume=17 |issue= 12 |pages= 6940-7 |year= 1997 |pmid= 9372926 |doi= }}
*{{cite journal | author=Gradi A, Imataka H, Svitkin YV, ''et al.'' |title=A novel functional human eukaryotic translation initiation factor 4G. |journal=Mol. Cell. Biol. |volume=18 |issue= 1 |pages= 334-42 |year= 1998 |pmid= 9418880 |doi= }}
*{{cite journal | author=Piron M, Vende P, Cohen J, Poncet D |title=Rotavirus RNA-binding protein NSP3 interacts with eIF4GI and evicts the poly(A) binding protein from eIF4F. |journal=EMBO J. |volume=17 |issue= 19 |pages= 5811-21 |year= 1998 |pmid= 9755181 |doi= 10.1093/emboj/17.19.5811 }}
*{{cite journal | author=Imataka H, Gradi A, Sonenberg N |title=A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation. |journal=EMBO J. |volume=17 |issue= 24 |pages= 7480-9 |year= 1999 |pmid= 9857202 |doi= 10.1093/emboj/17.24.7480 }}
*{{cite journal | author=Pyronnet S, Imataka H, Gingras AC, ''et al.'' |title=Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E. |journal=EMBO J. |volume=18 |issue= 1 |pages= 270-9 |year= 1999 |pmid= 9878069 |doi= 10.1093/emboj/18.1.270 }}
*{{cite journal | author=Laroia G, Cuesta R, Brewer G, Schneider RJ |title=Control of mRNA decay by heat shock-ubiquitin-proteasome pathway. |journal=Science |volume=284 |issue= 5413 |pages= 499-502 |year= 1999 |pmid= 10205060 |doi= }}
*{{cite journal | author=Vary TC, Jefferson LS, Kimball SR |title=Amino acid-induced stimulation of translation initiation in rat skeletal muscle. |journal=Am. J. Physiol. |volume=277 |issue= 6 Pt 1 |pages= E1077-86 |year= 2000 |pmid= 10600798 |doi= }}
*{{cite journal | author=Cuesta R, Laroia G, Schneider RJ |title=Chaperone hsp27 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes. |journal=Genes Dev. |volume=14 |issue= 12 |pages= 1460-70 |year= 2000 |pmid= 10859165 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on EPB41... {November 14, 2007 4:14:55 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:15:39 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
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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_EPB41_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1gg3.
| PDB = {{PDB2|1gg3}}
| Name = Erythrocyte membrane protein band 4.1 (elliptocytosis 1, RH-linked)
| HGNCid = 3377
| Symbol = EPB41
| AltSymbols =; 4.1R; EL1; HE
| OMIM = 130500
| ECnumber =
| Homologene = 44324
| MGIid = 95401
| GeneAtlas_image1 = PBB_GE_EPB41_207793_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_EPB41_214530_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_EPB41_gnf1h06881_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005488 |text = binding}} {{GNF_GO|id=GO:0005545 |text = phosphatidylinositol binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0008091 |text = spectrin}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0030863 |text = cortical cytoskeleton}} {{GNF_GO|id=GO:0043234 |text = protein complex}}
| Process = {{GNF_GO|id=GO:0008015 |text = circulation}} {{GNF_GO|id=GO:0030866 |text = cortical actin cytoskeleton organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2035
| Hs_Ensembl = ENSG00000159023
| Hs_RefseqProtein = NP_004428
| Hs_RefseqmRNA = NM_004437
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 29086215
| Hs_GenLoc_end = 29319545
| Hs_Uniprot = P11171
| Mm_EntrezGene = 269587
| Mm_Ensembl = ENSMUSG00000028906
| Mm_RefseqmRNA = NM_183428
| Mm_RefseqProtein = NP_906273
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 131195505
| Mm_GenLoc_end = 131347350
| Mm_Uniprot = Q3U0G7
}}
}}
'''Erythrocyte membrane protein band 4.1 (elliptocytosis 1, RH-linked)''', also known as '''EPB41''', 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 = Elliptocytosis is a hematologic disorder characterized by elliptically shaped erythrocytes and a variable degree of hemolytic anemia. Inherited as an autosomal dominant, elliptocytosis results from mutation in any one of several genes encoding proteins of the red cell membrane skeleton. The form discussed here is the one found in the 1950s to be linked to Rh blood group and more recently shown to be caused by a defect in protein 4.1. 'Rh-unlinked' forms of elliptocytosis are caused by mutation in the alpha-spectrin gene (MIM 182860), the beta-spectrin gene (MIM 182870), or the band 3 gene (MIM 109270).[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: EPB41 erythrocyte membrane protein band 4.1 (elliptocytosis 1, RH-linked)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2035| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Conboy JG |title=Structure, function, and molecular genetics of erythroid membrane skeletal protein 4.1 in normal and abnormal red blood cells. |journal=Semin. Hematol. |volume=30 |issue= 1 |pages= 58-73 |year= 1993 |pmid= 8434260 |doi= }}
*{{cite journal | author=Calinisan V, Gravem D, Chen RP, ''et al.'' |title=New insights into potential functions for the protein 4.1 superfamily of proteins in kidney epithelium. |journal=Front. Biosci. |volume=11 |issue= |pages= 1646-66 |year= 2006 |pmid= 16368544 |doi= }}
*{{cite journal | author=Dalla Venezia N, Gilsanz F, Alloisio N, ''et al.'' |title=Homozygous 4.1(-) hereditary elliptocytosis associated with a point mutation in the downstream initiation codon of protein 4.1 gene. |journal=J. Clin. Invest. |volume=90 |issue= 5 |pages= 1713-7 |year= 1992 |pmid= 1430200 |doi= }}
*{{cite journal | author=Jöns T, Drenckhahn D |title=Identification of the binding interface involved in linkage of cytoskeletal protein 4.1 to the erythrocyte anion exchanger. |journal=EMBO J. |volume=11 |issue= 8 |pages= 2863-7 |year= 1992 |pmid= 1639060 |doi= }}
*{{cite journal | author=Subrahmanyam G, Bertics PJ, Anderson RA |title=Phosphorylation of protein 4.1 on tyrosine-418 modulates its function in vitro. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 12 |pages= 5222-6 |year= 1991 |pmid= 1647028 |doi= }}
*{{cite journal | author=Conboy JG, Chan JY, Chasis JA, ''et al.'' |title=Tissue- and development-specific alternative RNA splicing regulates expression of multiple isoforms of erythroid membrane protein 4.1. |journal=J. Biol. Chem. |volume=266 |issue= 13 |pages= 8273-80 |year= 1991 |pmid= 2022644 |doi= }}
*{{cite journal | author=Horne WC, Prinz WC, Tang EK |title=Identification of two cAMP-dependent phosphorylation sites on erythrocyte protein 4.1. |journal=Biochim. Biophys. Acta |volume=1055 |issue= 1 |pages= 87-92 |year= 1990 |pmid= 2171679 |doi= }}
*{{cite journal | author=Conboy J, Marchesi S, Kim R, ''et al.'' |title=Molecular analysis of insertion/deletion mutations in protein 4.1 in elliptocytosis. II. Determination of molecular genetic origins of rearrangements. |journal=J. Clin. Invest. |volume=86 |issue= 2 |pages= 524-30 |year= 1990 |pmid= 2384598 |doi= }}
*{{cite journal | author=Inaba M, Maede Y |title=O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms regulated by alternative pathways. |journal=J. Biol. Chem. |volume=264 |issue= 30 |pages= 18149-55 |year= 1989 |pmid= 2808371 |doi= }}
*{{cite journal | author=Korsgren C, Cohen CM |title=Associations of human erythrocyte band 4.2. Binding to ankyrin and to the cytoplasmic domain of band 3. |journal=J. Biol. Chem. |volume=263 |issue= 21 |pages= 10212-8 |year= 1988 |pmid= 2968981 |doi= }}
*{{cite journal | author=Conboy JG, Chan J, Mohandas N, Kan YW |title=Multiple protein 4.1 isoforms produced by alternative splicing in human erythroid cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 23 |pages= 9062-5 |year= 1988 |pmid= 3194408 |doi= }}
*{{cite journal | author=Tang TK, Leto TL, Marchesi VT, Benz EJ |title=Expression of specific isoforms of protein 4.1 in erythroid and non-erythroid tissues. |journal=Adv. Exp. Med. Biol. |volume=241 |issue= |pages= 81-95 |year= 1989 |pmid= 3223413 |doi= }}
*{{cite journal | author=Tang TK, Leto TL, Correas I, ''et al.'' |title=Selective expression of an erythroid-specific isoform of protein 4.1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 11 |pages= 3713-7 |year= 1988 |pmid= 3375238 |doi= }}
*{{cite journal | author=Conboy J, Kan YW, Shohet SB, Mohandas N |title=Molecular cloning of protein 4.1, a major structural element of the human erythrocyte membrane skeleton. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 24 |pages= 9512-6 |year= 1987 |pmid= 3467321 |doi= }}
*{{cite journal | author=Correas I, Speicher DW, Marchesi VT |title=Structure of the spectrin-actin binding site of erythrocyte protein 4.1. |journal=J. Biol. Chem. |volume=261 |issue= 28 |pages= 13362-6 |year= 1986 |pmid= 3531202 |doi= }}
*{{cite journal | author=Tchernia G, Mohandas N, Shohet SB |title=Deficiency of skeletal membrane protein band 4.1 in homozygous hereditary elliptocytosis. Implications for erythrocyte membrane stability. |journal=J. Clin. Invest. |volume=68 |issue= 2 |pages= 454-60 |year= 1981 |pmid= 6894932 |doi= }}
*{{cite journal | author=Schischmanoff PO, Winardi R, Discher DE, ''et al.'' |title=Defining of the minimal domain of protein 4.1 involved in spectrin-actin binding. |journal=J. Biol. Chem. |volume=270 |issue= 36 |pages= 21243-50 |year= 1995 |pmid= 7673158 |doi= }}
*{{cite journal | author=Lue RA, Marfatia SM, Branton D, Chishti AH |title=Cloning and characterization of hdlg: the human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 21 |pages= 9818-22 |year= 1994 |pmid= 7937897 |doi= }}
*{{cite journal | author=Conboy JG, Chasis JA, Winardi R, ''et al.'' |title=An isoform-specific mutation in the protein 4.1 gene results in hereditary elliptocytosis and complete deficiency of protein 4.1 in erythrocytes but not in nonerythroid cells. |journal=J. Clin. Invest. |volume=91 |issue= 1 |pages= 77-82 |year= 1993 |pmid= 8423235 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IRAK1... {November 14, 2007 4:15:39 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:16:13 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 =
| image_source =
| PDB =
| Name = Interleukin-1 receptor-associated kinase 1
| HGNCid = 6112
| Symbol = IRAK1
| AltSymbols =; IRAK; pelle
| OMIM = 300283
| ECnumber =
| Homologene = 37496
| MGIid = 107420
| GeneAtlas_image1 = PBB_GE_IRAK1_201587_s_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:0004672 |text = protein kinase activity}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004704 |text = NF-kappaB-inducing kinase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005149 |text = interleukin-1 receptor binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016563 |text = transcription activator activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0019901 |text = protein kinase binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}}
| Component = {{GNF_GO|id=GO:0045323 |text = interleukin-1 receptor complex}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007178 |text = transmembrane receptor protein serine/threonine kinase signaling pathway}} {{GNF_GO|id=GO:0007250 |text = activation of NF-kappaB-inducing kinase}} {{GNF_GO|id=GO:0019221 |text = cytokine and chemokine mediated signaling pathway}} {{GNF_GO|id=GO:0045941 |text = positive regulation of transcription}} {{GNF_GO|id=GO:0046777 |text = protein amino acid autophosphorylation}} {{GNF_GO|id=GO:0051259 |text = protein oligomerization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3654
| Hs_Ensembl = ENSG00000184216
| Hs_RefseqProtein = NP_001020413
| Hs_RefseqmRNA = NM_001025242
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 152929145
| Hs_GenLoc_end = 152938625
| Hs_Uniprot = P51617
| Mm_EntrezGene = 16179
| Mm_Ensembl = ENSMUSG00000031392
| Mm_RefseqmRNA = NM_008363
| Mm_RefseqProtein = NP_032389
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 70266646
| Mm_GenLoc_end = 70276641
| Mm_Uniprot = Q8K4N7
}}
}}
'''Interleukin-1 receptor-associated kinase 1''', also known as '''IRAK1''', 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 interleukin-1 receptor-associated kinase 1, one of two putative serine/threonine kinases that become associated with the interleukin-1 receptor (IL1R) upon stimulation. This gene is partially responsible for IL1-induced upregulation of the transcription factor NF-kappa B. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.<ref>{{cite web | title = Entrez Gene: IRAK1 interleukin-1 receptor-associated kinase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3654| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Auron PE |title=The interleukin 1 receptor: ligand interactions and signal transduction. |journal=Cytokine Growth Factor Rev. |volume=9 |issue= 3-4 |pages= 221-37 |year= 1999 |pmid= 9918122 |doi= }}
*{{cite journal | author=Cao Z, Henzel WJ, Gao X |title=IRAK: a kinase associated with the interleukin-1 receptor. |journal=Science |volume=271 |issue= 5252 |pages= 1128-31 |year= 1996 |pmid= 8599092 |doi= }}
*{{cite journal | author=Cao Z, Xiong J, Takeuchi M, ''et al.'' |title=TRAF6 is a signal transducer for interleukin-1. |journal=Nature |volume=383 |issue= 6599 |pages= 443-6 |year= 1996 |pmid= 8837778 |doi= 10.1038/383443a0 }}
*{{cite journal | author=Brenner V, Nyakatura G, Rosenthal A, Platzer M |title=Genomic organization of two novel genes on human Xq28: compact head to head arrangement of IDH gamma and TRAP delta is conserved in rat and mouse. |journal=Genomics |volume=44 |issue= 1 |pages= 8-14 |year= 1997 |pmid= 9286695 |doi= 10.1006/geno.1997.4822 }}
*{{cite journal | author=Huang J, Gao X, Li S, Cao Z |title=Recruitment of IRAK to the interleukin 1 receptor complex requires interleukin 1 receptor accessory protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 24 |pages= 12829-32 |year= 1998 |pmid= 9371760 |doi= }}
*{{cite journal | author=Muzio M, Ni J, Feng P, Dixit VM |title=IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling. |journal=Science |volume=278 |issue= 5343 |pages= 1612-5 |year= 1997 |pmid= 9374458 |doi= }}
*{{cite journal | author=Muzio M, Natoli G, Saccani S, ''et al.'' |title=The human toll signaling pathway: divergence of nuclear factor kappaB and JNK/SAPK activation upstream of tumor necrosis factor receptor-associated factor 6 (TRAF6). |journal=J. Exp. Med. |volume=187 |issue= 12 |pages= 2097-101 |year= 1998 |pmid= 9625770 |doi= }}
*{{cite journal | author=Maschera B, Ray K, Burns K, Volpe F |title=Overexpression of an enzymically inactive interleukin-1-receptor-associated kinase activates nuclear factor-kappaB. |journal=Biochem. J. |volume=339 ( Pt 2) |issue= |pages= 227-31 |year= 1999 |pmid= 10191251 |doi= }}
*{{cite journal | author=Wesche H, Gao X, Li X, ''et al.'' |title=IRAK-M is a novel member of the Pelle/interleukin-1 receptor-associated kinase (IRAK) family. |journal=J. Biol. Chem. |volume=274 |issue= 27 |pages= 19403-10 |year= 1999 |pmid= 10383454 |doi= }}
*{{cite journal | author=Yang RB, Mark MR, Gurney AL, Godowski PJ |title=Signaling events induced by lipopolysaccharide-activated toll-like receptor 2. |journal=J. Immunol. |volume=163 |issue= 2 |pages= 639-43 |year= 1999 |pmid= 10395652 |doi= }}
*{{cite journal | author=Thomas JA, Allen JL, Tsen M, ''et al.'' |title=Impaired cytokine signaling in mice lacking the IL-1 receptor-associated kinase. |journal=J. Immunol. |volume=163 |issue= 2 |pages= 978-84 |year= 1999 |pmid= 10395695 |doi= }}
*{{cite journal | author=Reichwald K, Thiesen J, Wiehe T, ''et al.'' |title=Comparative sequence analysis of the MECP2-locus in human and mouse reveals new transcribed regions. |journal=Mamm. Genome |volume=11 |issue= 3 |pages= 182-90 |year= 2000 |pmid= 10723722 |doi= }}
*{{cite journal | author=Burns K, Clatworthy J, Martin L, ''et al.'' |title=Tollip, a new component of the IL-1RI pathway, links IRAK to the IL-1 receptor. |journal=Nat. Cell Biol. |volume=2 |issue= 6 |pages= 346-51 |year= 2000 |pmid= 10854325 |doi= 10.1038/35014038 }}
*{{cite journal | author=Böl G, Kreuzer OJ, Brigelius-Flohé R |title=Translocation of the interleukin-1 receptor-associated kinase-1 (IRAK-1) into the nucleus. |journal=FEBS Lett. |volume=477 |issue= 1-2 |pages= 73-8 |year= 2000 |pmid= 10899313 |doi= }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
*{{cite journal | author=Vig E, Green M, Liu Y, ''et al.'' |title=SIMPL is a tumor necrosis factor-specific regulator of nuclear factor-kappaB activity. |journal=J. Biol. Chem. |volume=276 |issue= 11 |pages= 7859-66 |year= 2001 |pmid= 11096118 |doi= 10.1074/jbc.M010399200 }}
*{{cite journal | author=Li X, Commane M, Jiang Z, Stark GR |title=IL-1-induced NFkappa B and c-Jun N-terminal kinase (JNK) activation diverge at IL-1 receptor-associated kinase (IRAK). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 8 |pages= 4461-5 |year= 2001 |pmid= 11287640 |doi= 10.1073/pnas.071054198 }}
*{{cite journal | author=Jensen LE, Whitehead AS |title=IRAK1b, a novel alternative splice variant of interleukin-1 receptor-associated kinase (IRAK), mediates interleukin-1 signaling and has prolonged stability. |journal=J. Biol. Chem. |volume=276 |issue= 31 |pages= 29037-44 |year= 2001 |pmid= 11397809 |doi= 10.1074/jbc.M103815200 }}
*{{cite journal | author=Qian Y, Commane M, Ninomiya-Tsuji J, ''et al.'' |title=IRAK-mediated translocation of TRAF6 and TAB2 in the interleukin-1-induced activation of NFkappa B. |journal=J. Biol. Chem. |volume=276 |issue= 45 |pages= 41661-7 |year= 2001 |pmid= 11518704 |doi= 10.1074/jbc.M102262200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on JAK3... {November 14, 2007 4:16:13 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:16:51 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_JAK3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1yvj.
| PDB = {{PDB2|1yvj}}
| Name = Janus kinase 3 (a protein tyrosine kinase, leukocyte)
| HGNCid = 6193
| Symbol = JAK3
| AltSymbols =; JAK-3; JAK3_HUMAN; JAKL; L-JAK; LJAK
| OMIM = 600173
| ECnumber =
| Homologene = 181
| MGIid = 99928
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine kinase activity}} {{GNF_GO|id=GO:0004718 |text = Janus kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0007498 |text = mesoderm development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3718
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000206
| Hs_RefseqmRNA = NM_000215
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 16453
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_010589
| Mm_RefseqProtein = NP_034719
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Janus kinase 3 (a protein tyrosine kinase, leukocyte)''', also known as '''JAK3''', 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 = JAK3 encodes Janus kinase 3, a tyrosine kinase that belongs to the Janus family. JAK3 functions in signal transduction and interacts with members of the STAT (signal transduction and activators of transcription) family. JAK3 is predominantly expressed in immune cells and transduces a signal in response to its activation via tyrosine phosphorylation by interleukin receptors. Mutations that abrogate Janus kinase 3 function cause an autosomal SCID (severe combined immunodeficiency disease).<ref>{{cite web | title = Entrez Gene: JAK3 Janus kinase 3 (a protein tyrosine kinase, leukocyte)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3718| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Notarangelo LD, Mella P, Jones A, ''et al.'' |title=Mutations in severe combined immune deficiency (SCID) due to JAK3 deficiency. |journal=Hum. Mutat. |volume=18 |issue= 4 |pages= 255-63 |year= 2002 |pmid= 11668610 |doi= 10.1002/humu.1188 }}
*{{cite journal | author=Russell SM, Tayebi N, Nakajima H, ''et al.'' |title=Mutation of Jak3 in a patient with SCID: essential role of Jak3 in lymphoid development. |journal=Science |volume=270 |issue= 5237 |pages= 797-800 |year= 1995 |pmid= 7481768 |doi= }}
*{{cite journal | author=Johnston JA, Wang LM, Hanson EP, ''et al.'' |title=Interleukins 2, 4, 7, and 15 stimulate tyrosine phosphorylation of insulin receptor substrates 1 and 2 in T cells. Potential role of JAK kinases. |journal=J. Biol. Chem. |volume=270 |issue= 48 |pages= 28527-30 |year= 1996 |pmid= 7499365 |doi= }}
*{{cite journal | author=Musso T, Johnston JA, Linnekin D, ''et al.'' |title=Regulation of JAK3 expression in human monocytes: phosphorylation in response to interleukins 2, 4, and 7. |journal=J. Exp. Med. |volume=181 |issue= 4 |pages= 1425-31 |year= 1995 |pmid= 7535338 |doi= }}
*{{cite journal | author=Rolling C, Treton D, Beckmann P, ''et al.'' |title=JAK3 associates with the human interleukin 4 receptor and is tyrosine phosphorylated following receptor triggering. |journal=Oncogene |volume=10 |issue= 9 |pages= 1757-61 |year= 1995 |pmid= 7538655 |doi= }}
*{{cite journal | author=Lai KS, Jin Y, Graham DK, ''et al.'' |title=A kinase-deficient splice variant of the human JAK3 is expressed in hematopoietic and epithelial cancer cells. |journal=J. Biol. Chem. |volume=270 |issue= 42 |pages= 25028-36 |year= 1995 |pmid= 7559633 |doi= }}
*{{cite journal | author=Macchi P, Villa A, Giliani S, ''et al.'' |title=Mutations of Jak-3 gene in patients with autosomal severe combined immune deficiency (SCID). |journal=Nature |volume=377 |issue= 6544 |pages= 65-8 |year= 1995 |pmid= 7659163 |doi= 10.1038/377065a0 }}
*{{cite journal | author=Russell SM, Johnston JA, Noguchi M, ''et al.'' |title=Interaction of IL-2R beta and gamma c chains with Jak1 and Jak3: implications for XSCID and XCID. |journal=Science |volume=266 |issue= 5187 |pages= 1042-5 |year= 1994 |pmid= 7973658 |doi= }}
*{{cite journal | author=Miyazaki T, Kawahara A, Fujii H, ''et al.'' |title=Functional activation of Jak1 and Jak3 by selective association with IL-2 receptor subunits. |journal=Science |volume=266 |issue= 5187 |pages= 1045-7 |year= 1994 |pmid= 7973659 |doi= }}
*{{cite journal | author=Johnston JA, Kawamura M, Kirken RA, ''et al.'' |title=Phosphorylation and activation of the Jak-3 Janus kinase in response to interleukin-2. |journal=Nature |volume=370 |issue= 6485 |pages= 151-3 |year= 1994 |pmid= 8022485 |doi= 10.1038/370151a0 }}
*{{cite journal | author=Witthuhn BA, Silvennoinen O, Miura O, ''et al.'' |title=Involvement of the Jak-3 Janus kinase in signalling by interleukins 2 and 4 in lymphoid and myeloid cells. |journal=Nature |volume=370 |issue= 6485 |pages= 153-7 |year= 1994 |pmid= 8022486 |doi= 10.1038/370153a0 }}
*{{cite journal | author=Kawamura M, McVicar DW, Johnston JA, ''et al.'' |title=Molecular cloning of L-JAK, a Janus family protein-tyrosine kinase expressed in natural killer cells and activated leukocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 14 |pages= 6374-8 |year= 1994 |pmid= 8022790 |doi= }}
*{{cite journal | author=Verbsky JW, Bach EA, Fang YF, ''et al.'' |title=Expression of Janus kinase 3 in human endothelial and other non-lymphoid and non-myeloid cells. |journal=J. Biol. Chem. |volume=271 |issue= 24 |pages= 13976-80 |year= 1996 |pmid= 8662778 |doi= }}
*{{cite journal | author=Riedy MC, Dutra AS, Blake TB, ''et al.'' |title=Genomic sequence, organization, and chromosomal localization of human JAK3. |journal=Genomics |volume=37 |issue= 1 |pages= 57-61 |year= 1997 |pmid= 8921370 |doi= 10.1006/geno.1996.0520 }}
*{{cite journal | author=Fusaki N, Iwamatsu A, Iwashima M, Fujisawa J |title=Interaction between Sam68 and Src family tyrosine kinases, Fyn and Lck, in T cell receptor signaling. |journal=J. Biol. Chem. |volume=272 |issue= 10 |pages= 6214-9 |year= 1997 |pmid= 9045636 |doi= }}
*{{cite journal | author=Fujitani Y, Hibi M, Fukada T, ''et al.'' |title=An alternative pathway for STAT activation that is mediated by the direct interaction between JAK and STAT. |journal=Oncogene |volume=14 |issue= 7 |pages= 751-61 |year= 1997 |pmid= 9047382 |doi= 10.1038/sj.onc.1200907 }}
*{{cite journal | author=Safford MG, Levenstein M, Tsifrina E, ''et al.'' |title=JAK3: expression and mapping to chromosome 19p12-13.1. |journal=Exp. Hematol. |volume=25 |issue= 5 |pages= 374-86 |year= 1997 |pmid= 9168059 |doi= }}
*{{cite journal | author=Sharfe N, Dadi HK, O'Shea JJ, Roifman CM |title=Jak3 activation in human lymphocyte precursor cells. |journal=Clin. Exp. Immunol. |volume=108 |issue= 3 |pages= 552-6 |year= 1997 |pmid= 9182906 |doi= }}
*{{cite journal | author=Hoffman SM, Lai KS, Tomfohrde J, ''et al.'' |title=JAK3 maps to human chromosome 19p12 within a cluster of proto-oncogenes and transcription factors. |journal=Genomics |volume=43 |issue= 1 |pages= 109-11 |year= 1997 |pmid= 9226382 |doi= 10.1006/geno.1997.4792 }}
*{{cite journal | author=Candotti F, Oakes SA, Johnston JA, ''et al.'' |title=Structural and functional basis for JAK3-deficient severe combined immunodeficiency. |journal=Blood |volume=90 |issue= 10 |pages= 3996-4003 |year= 1997 |pmid= 9354668 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MC4R... {November 14, 2007 4:16:51 PM PST}
- SEARCH REDIRECT: Control Box Found: MC4R {November 14, 2007 4:17:29 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 4:17:31 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 4:17:31 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 4:17:31 PM PST}
- UPDATED: Updated protein page: MC4R {November 14, 2007 4:17:37 PM PST}
- INFO: Beginning work on NFE2L2... {November 14, 2007 4:17:37 PM PST}
- SEARCH REDIRECT: Control Box Found: NFE2L2 {November 14, 2007 4:18:18 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 4:18:20 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 4:18:20 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 4:18:20 PM PST}
- UPDATED: Updated protein page: NFE2L2 {November 14, 2007 4:18:26 PM PST}
- INFO: Beginning work on NR0B1... {November 14, 2007 4:11:01 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:11:51 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 = Nuclear receptor subfamily 0, group B, member 1
| HGNCid = 7960
| Symbol = NR0B1
| AltSymbols =; AHC; AHCH; AHX; DAX-1; DAX1; DSS; GTD; HHG; NROB1
| OMIM = 300473
| ECnumber =
| Homologene = 403
| MGIid = 1352460
| GeneAtlas_image1 = PBB_GE_NR0B1_206644_at_tn.png
| GeneAtlas_image2 = PBB_GE_NR0B1_206645_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003706 |text = ligand-regulated transcription factor activity}} {{GNF_GO|id=GO:0003707 |text = steroid hormone receptor activity}} {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016564 |text = transcription repressor activity}} {{GNF_GO|id=GO:0017163 |text = negative regulator of basal transcription activity}} {{GNF_GO|id=GO:0032448 |text = DNA hairpin binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0042788 |text = polysomal ribosome}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006694 |text = steroid biosynthetic process}} {{GNF_GO|id=GO:0008406 |text = gonad development}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0030238 |text = male sex determination}} {{GNF_GO|id=GO:0030325 |text = adrenal gland development}} {{GNF_GO|id=GO:0045892 |text = negative regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 190
| Hs_Ensembl = ENSG00000169297
| Hs_RefseqProtein = NP_000466
| Hs_RefseqmRNA = NM_000475
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 30232244
| Hs_GenLoc_end = 30237636
| Hs_Uniprot = P51843
| Mm_EntrezGene = 11614
| Mm_Ensembl = ENSMUSG00000025056
| Mm_RefseqmRNA = NM_007430
| Mm_RefseqProtein = NP_031456
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 82444494
| Mm_GenLoc_end = 82448663
| Mm_Uniprot = Q53ZY9
}}
}}
'''Nuclear receptor subfamily 0, group B, member 1''', also known as '''NR0B1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a protein that contains a DNA-binding domain. The encoded protein acts as a dominant-negative regulator of transcription which is mediated by the retinoic acid receptor. This protein also functions as an anti-testis gene by acting antagonistically to Sry. Mutations in this gene result in both X-linked congenital adrenal hypoplasia and hypogonadotropic hypogonadism.<ref>{{cite web | title = Entrez Gene: NR0B1 nuclear receptor subfamily 0, group B, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=190| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Goodfellow PN, Camerino G |title=DAX-1, an 'antitestis' gene. |journal=Cell. Mol. Life Sci. |volume=55 |issue= 6-7 |pages= 857-63 |year= 1999 |pmid= 10412368 |doi= }}
*{{cite journal | author=Achermann JC, Meeks JJ, Jameson JL |title=Phenotypic spectrum of mutations in DAX-1 and SF-1. |journal=Mol. Cell. Endocrinol. |volume=185 |issue= 1-2 |pages= 17-25 |year= 2003 |pmid= 11738790 |doi= }}
*{{cite journal | author=Franzese A, Brunetti-Pierri N, Spagnuolo MI, ''et al.'' |title=Inappropriate tall stature and renal ectopy in a male patient with X-linked congenital adrenal hypoplasia due to a novel missense mutation in the DAX-1 gene. |journal=Am. J. Med. Genet. A |volume=135 |issue= 1 |pages= 72-4 |year= 2005 |pmid= 15800903 |doi= 10.1002/ajmg.a.30670 }}
*{{cite journal | author=Achermann JC |title=The role of SF1/DAX1 in adrenal and reproductive function. |journal=Ann. Endocrinol. (Paris) |volume=66 |issue= 3 |pages= 233-9 |year= 2005 |pmid= 15988384 |doi= }}
*{{cite journal | author=Niakan KK, McCabe ER |title=DAX1 origin, function, and novel role. |journal=Mol. Genet. Metab. |volume=86 |issue= 1-2 |pages= 70-83 |year= 2006 |pmid= 16146703 |doi= 10.1016/j.ymgme.2005.07.019 }}
*{{cite journal | author=Walker AP, Chelly J, Love DR, ''et al.'' |title=A YAC contig in Xp21 containing the adrenal hypoplasia congenita and glycerol kinase deficiency genes. |journal=Hum. Mol. Genet. |volume=1 |issue= 8 |pages= 579-85 |year= 1993 |pmid= 1301166 |doi= }}
*{{cite journal | author=Worley KC, Towbin JA, Zhu XM, ''et al.'' |title=Identification of new markers in Xp21 between DXS28 (C7) and DMD. |journal=Genomics |volume=13 |issue= 4 |pages= 957-61 |year= 1992 |pmid= 1505987 |doi= }}
*{{cite journal | author=Petersen KE, Bille T, Jacobsen BB, Iversen T |title=X-linked congenital adrenal hypoplasia. A study of five generations of a Greenlandic Family. |journal=Acta paediatrica Scandinavica |volume=71 |issue= 6 |pages= 947-51 |year= 1983 |pmid= 6891556 |doi= }}
*{{cite journal | author=Burris TP, Guo W, Le T, McCabe ER |title=Identification of a putative steroidogenic factor-1 response element in the DAX-1 promoter. |journal=Biochem. Biophys. Res. Commun. |volume=214 |issue= 2 |pages= 576-81 |year= 1995 |pmid= 7677767 |doi= }}
*{{cite journal | author=Bardoni B, Zanaria E, Guioli S, ''et al.'' |title=A dosage sensitive locus at chromosome Xp21 is involved in male to female sex reversal. |journal=Nat. Genet. |volume=7 |issue= 4 |pages= 497-501 |year= 1994 |pmid= 7951319 |doi= 10.1038/ng0894-497 }}
*{{cite journal | author=Zanaria E, Muscatelli F, Bardoni B, ''et al.'' |title=An unusual member of the nuclear hormone receptor superfamily responsible for X-linked adrenal hypoplasia congenita. |journal=Nature |volume=372 |issue= 6507 |pages= 635-41 |year= 1995 |pmid= 7990953 |doi= 10.1038/372635a0 }}
*{{cite journal | author=Muscatelli F, Strom TM, Walker AP, ''et al.'' |title=Mutations in the DAX-1 gene give rise to both X-linked adrenal hypoplasia congenita and hypogonadotropic hypogonadism. |journal=Nature |volume=372 |issue= 6507 |pages= 672-6 |year= 1995 |pmid= 7990958 |doi= 10.1038/372672a0 }}
*{{cite journal | author=Guo W, Burris TP, McCabe ER |title=Expression of DAX-1, the gene responsible for X-linked adrenal hypoplasia congenita and hypogonadotropic hypogonadism, in the hypothalamic-pituitary-adrenal/gonadal axis. |journal=Biochem. Mol. Med. |volume=56 |issue= 1 |pages= 8-13 |year= 1996 |pmid= 8593542 |doi= }}
*{{cite journal | author=Yanase T, Takayanagi R, Oba K, ''et al.'' |title=New mutations of DAX-1 genes in two Japanese patients with X-linked congenital adrenal hypoplasia and hypogonadotropic hypogonadism. |journal=J. Clin. Endocrinol. Metab. |volume=81 |issue= 2 |pages= 530-5 |year= 1996 |pmid= 8636263 |doi= }}
*{{cite journal | author=Guo W, Burris TP, Zhang YH, ''et al.'' |title=Genomic sequence of the DAX1 gene: an orphan nuclear receptor responsible for X-linked adrenal hypoplasia congenita and hypogonadotropic hypogonadism. |journal=J. Clin. Endocrinol. Metab. |volume=81 |issue= 7 |pages= 2481-6 |year= 1996 |pmid= 8675564 |doi= }}
*{{cite journal | author=Nakae J, Tajima T, Kusuda S, ''et al.'' |title=Truncation at the C-terminus of the DAX-1 protein impairs its biological actions in patients with X-linked adrenal hypoplasia congenita. |journal=J. Clin. Endocrinol. Metab. |volume=81 |issue= 10 |pages= 3680-5 |year= 1996 |pmid= 8855822 |doi= }}
*{{cite journal | author=Schwartz M, Blichfeldt S, Müller J |title=X-linked adrenal hypoplasia in a large Greenlandic family. Detection of a missense mutation (N4401) in the DAX-1 gene; implication for genetic counselling and carrier diagnosis. |journal=Hum. Genet. |volume=99 |issue= 1 |pages= 83-7 |year= 1997 |pmid= 9003500 |doi= }}
*{{cite journal | author=Takahashi T, Shoji Y, Shoji Y, ''et al.'' |title=Active hypothalamic-pituitary-gonadal axis in an infant with X-linked adrenal hypoplasia congenita. |journal=J. Pediatr. |volume=130 |issue= 3 |pages= 485-8 |year= 1997 |pmid= 9063431 |doi= }}
*{{cite journal | author=Nakae J, Abe S, Tajima T, ''et al.'' |title=Three novel mutations and a de novo deletion mutation of the DAX-1 gene in patients with X-linked adrenal hypoplasia congenita. |journal=J. Clin. Endocrinol. Metab. |volume=82 |issue= 11 |pages= 3835-41 |year= 1997 |pmid= 9360549 |doi= }}
*{{cite journal | author=Zazopoulos E, Lalli E, Stocco DM, Sassone-Corsi P |title=DNA binding and transcriptional repression by DAX-1 blocks steroidogenesis. |journal=Nature |volume=390 |issue= 6657 |pages= 311-5 |year= 1997 |pmid= 9384387 |doi= 10.1038/36899 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on POLR2G... {November 14, 2007 4:19:54 PM PST}
- SEARCH REDIRECT: Control Box Found: POLR2G {November 14, 2007 4:20:33 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 4:20:34 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 4:20:34 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 4:20:34 PM PST}
- UPDATED: Updated protein page: POLR2G {November 14, 2007 4:20:42 PM PST}
- INFO: Beginning work on POLR2H... {November 14, 2007 4:20:42 PM PST}
- SEARCH REDIRECT: Control Box Found: POLR2H {November 14, 2007 4:21:18 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 4:21:19 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 4:21:19 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 4:21:19 PM PST}
- UPDATED: Updated protein page: POLR2H {November 14, 2007 4:21:26 PM PST}
- INFO: Beginning work on PPARD... {November 14, 2007 4:21:26 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:22:15 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_PPARD_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1gwx.
| PDB = {{PDB2|1gwx}}, {{PDB2|1y0s}}, {{PDB2|2awh}}, {{PDB2|2b50}}, {{PDB2|2baw}}, {{PDB2|2gwx}}, {{PDB2|2j14}}, {{PDB2|3gwx}}
| Name = Peroxisome proliferator-activated receptor delta
| HGNCid = 9235
| Symbol = PPARD
| AltSymbols =; FAAR; MGC3931; NR1C2; NUC1; NUCI; NUCII; PPAR-beta; PPARB
| OMIM = 600409
| ECnumber =
| Homologene = 4544
| MGIid = 101884
| GeneAtlas_image1 = PBB_GE_PPARD_37152_at_tn.png
| GeneAtlas_image2 = PBB_GE_PPARD_208044_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_PPARD_210636_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003707 |text = steroid hormone receptor activity}} {{GNF_GO|id=GO:0005504 |text = fatty acid binding}} {{GNF_GO|id=GO:0008047 |text = enzyme activator activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016501 |text = prostacyclin receptor activity}} {{GNF_GO|id=GO:0016564 |text = transcription repressor activity}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0046965 |text = retinoid X receptor binding}} {{GNF_GO|id=GO:0046982 |text = protein heterodimerization activity}}
| 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:0006006 |text = glucose metabolic process}} {{GNF_GO|id=GO:0006091 |text = generation of precursor metabolites and energy}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006635 |text = fatty acid beta-oxidation}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0007566 |text = embryo implantation}} {{GNF_GO|id=GO:0008203 |text = cholesterol metabolic process}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008366 |text = axon ensheathment}} {{GNF_GO|id=GO:0008544 |text = epidermis development}} {{GNF_GO|id=GO:0009062 |text = fatty acid catabolic process}} {{GNF_GO|id=GO:0014068 |text = positive regulation of phosphoinositide 3-kinase cascade}} {{GNF_GO|id=GO:0015758 |text = glucose transport}} {{GNF_GO|id=GO:0015908 |text = fatty acid transport}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0042640 |text = anagen}} {{GNF_GO|id=GO:0045600 |text = positive regulation of fat cell differentiation}} {{GNF_GO|id=GO:0046697 |text = decidualization}} {{GNF_GO|id=GO:0050796 |text = regulation of insulin secretion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5467
| Hs_Ensembl = ENSG00000112033
| Hs_RefseqProtein = NP_006229
| Hs_RefseqmRNA = NM_006238
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 35418320
| Hs_GenLoc_end = 35503933
| Hs_Uniprot = Q03181
| Mm_EntrezGene = 19015
| Mm_Ensembl = ENSMUSG00000002250
| Mm_RefseqmRNA = XM_990965
| Mm_RefseqProtein = XP_996059
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 27960392
| Mm_GenLoc_end = 28029058
| Mm_Uniprot = Q546I3
}}
}}
'''Peroxisome proliferator-activated receptor delta''', also known as '''PPARD''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the peroxisome proliferator-activated receptor (PPAR) family. PPARs are nuclear hormone receptors that bind peroxisome proliferators and control the size and number of peroxisomes produced by cells. PPARs mediate a variety of biological processes, and may be involved in the development of several chronic diseases, including diabetes, obesity, atherosclerosis, and cancer. This protein is a potent inhibitor of ligand-induced transcription activity of PPAR alpha and PPAR gamma. It may function as an integrator of transcription repression and nuclear receptor signaling. The expression of this gene is found to be elevated in colorectal cancer cells. The elevated expression can be repressed by adenomatosis polyposis coli (APC), a tumor suppressor protein related to APC/beta-catenin signaling pathway. Knockout studies in mice suggested the role of this protein in myelination of the corpus callosum, lipid metabolism, and epidermal cell proliferation.<ref>{{cite web | title = Entrez Gene: PPARD peroxisome proliferator-activated receptor delta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5467| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kersten S, Desvergne B, Wahli W |title=Roles of PPARs in health and disease. |journal=Nature |volume=405 |issue= 6785 |pages= 421-4 |year= 2000 |pmid= 10839530 |doi= 10.1038/35013000 }}
*{{cite journal | author=Bastie C |title=[PPARdelta and PPARgamma: roles in fatty acids signalling, implication in tumorigenesis] |journal=Bulletin du cancer |volume=89 |issue= 1 |pages= 23-8 |year= 2002 |pmid= 11847022 |doi= }}
*{{cite journal | author=Fredenrich A, Grimaldi PA |title=Roles of peroxisome proliferator-activated receptor delta in skeletal muscle function and adaptation. |journal=Current opinion in clinical nutrition and metabolic care |volume=7 |issue= 4 |pages= 377-81 |year= 2004 |pmid= 15192438 |doi= }}
*{{cite journal | author=Fredenrich A, Grimaldi PA |title=PPAR delta: an uncompletely known nuclear receptor. |journal=Diabetes Metab. |volume=31 |issue= 1 |pages= 23-7 |year= 2005 |pmid= 15803109 |doi= }}
*{{cite journal | author=Barish GD, Narkar VA, Evans RM |title=PPAR delta: a dagger in the heart of the metabolic syndrome. |journal=J. Clin. Invest. |volume=116 |issue= 3 |pages= 590-7 |year= 2006 |pmid= 16511591 |doi= 10.1172/JCI27955 }}
*{{cite journal | author=Fürnsinn C, Willson TM, Brunmair B |title=Peroxisome proliferator-activated receptor-delta, a regulator of oxidative capacity, fuel switching and cholesterol transport. |journal=Diabetologia |volume=50 |issue= 1 |pages= 8-17 |year= 2007 |pmid= 17119917 |doi= 10.1007/s00125-006-0492-0 }}
*{{cite journal | author=Takahashi S, Tanaka T, Sakai J |title=New therapeutic target for metabolic syndrome: PPARdelta. |journal=Endocr. J. |volume=54 |issue= 3 |pages= 347-57 |year= 2007 |pmid= 17409576 |doi= }}
*{{cite journal | author=Schmidt A, Endo N, Rutledge SJ, ''et al.'' |title=Identification of a new member of the steroid hormone receptor superfamily that is activated by a peroxisome proliferator and fatty acids. |journal=Mol. Endocrinol. |volume=6 |issue= 10 |pages= 1634-41 |year= 1992 |pmid= 1333051 |doi= }}
*{{cite journal | author=Jow L, Mukherjee R |title=The human peroxisome proliferator-activated receptor (PPAR) subtype NUC1 represses the activation of hPPAR alpha and thyroid hormone receptors. |journal=J. Biol. Chem. |volume=270 |issue= 8 |pages= 3836-40 |year= 1995 |pmid= 7876127 |doi= }}
*{{cite journal | author=Yoshikawa T, Brkanac Z, Dupont BR, ''et al.'' |title=Assignment of the human nuclear hormone receptor, NUC1 (PPARD), to chromosome 6p21.1-p21.2. |journal=Genomics |volume=35 |issue= 3 |pages= 637-8 |year= 1996 |pmid= 8812511 |doi= 10.1006/geno.1996.0417 }}
*{{cite journal | author=Chu R, Lin Y, Rao MS, Reddy JK |title=Cloning and identification of rat deoxyuridine triphosphatase as an inhibitor of peroxisome proliferator-activated receptor alpha. |journal=J. Biol. Chem. |volume=271 |issue= 44 |pages= 27670-6 |year= 1996 |pmid= 8910358 |doi= }}
*{{cite journal | author=Tripodis N, Mason R, Humphray SJ, ''et al.'' |title=Physical map of human 6p21.2-6p21.3: region flanking the centromeric end of the major histocompatibility complex. |journal=Genome Res. |volume=8 |issue= 6 |pages= 631-43 |year= 1999 |pmid= 9647638 |doi= }}
*{{cite journal | author=Xu HE, Lambert MH, Montana VG, ''et al.'' |title=Molecular recognition of fatty acids by peroxisome proliferator-activated receptors. |journal=Mol. Cell |volume=3 |issue= 3 |pages= 397-403 |year= 1999 |pmid= 10198642 |doi= }}
*{{cite journal | author=He TC, Chan TA, Vogelstein B, Kinzler KW |title=PPARdelta is an APC-regulated target of nonsteroidal anti-inflammatory drugs. |journal=Cell |volume=99 |issue= 3 |pages= 335-45 |year= 1999 |pmid= 10555149 |doi= }}
*{{cite journal | author=Kraus WL, Manning ET, Kadonaga JT |title=Biochemical analysis of distinct activation functions in p300 that enhance transcription initiation with chromatin templates. |journal=Mol. Cell. Biol. |volume=19 |issue= 12 |pages= 8123-35 |year= 2000 |pmid= 10567538 |doi= }}
*{{cite journal | author=Skogsberg J, Kannisto K, Roshani L, ''et al.'' |title=Characterization of the human peroxisome proliferator activated receptor delta gene and its expression. |journal=Int. J. Mol. Med. |volume=6 |issue= 1 |pages= 73-81 |year= 2000 |pmid= 10851270 |doi= }}
*{{cite journal | author=Peters JM, Lee SS, Li W, ''et al.'' |title=Growth, adipose, brain, and skin alterations resulting from targeted disruption of the mouse peroxisome proliferator-activated receptor beta(delta). |journal=Mol. Cell. Biol. |volume=20 |issue= 14 |pages= 5119-28 |year= 2000 |pmid= 10866668 |doi= }}
*{{cite journal | author=Yi YW, Kim D, Jung N, ''et al.'' |title=Gadd45 family proteins are coactivators of nuclear hormone receptors. |journal=Biochem. Biophys. Res. Commun. |volume=272 |issue= 1 |pages= 193-8 |year= 2000 |pmid= 10872826 |doi= }}
*{{cite journal | author=Bastie C, Luquet S, Holst D, ''et al.'' |title=Alterations of peroxisome proliferator-activated receptor delta activity affect fatty acid-controlled adipose differentiation. |journal=J. Biol. Chem. |volume=275 |issue= 49 |pages= 38768-73 |year= 2001 |pmid= 10991946 |doi= 10.1074/jbc.M006450200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on REN... {November 14, 2007 4:22:15 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:22:45 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_REN_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bbs.
| PDB = {{PDB2|1bbs}}, {{PDB2|1bil}}, {{PDB2|1bim}}, {{PDB2|1hrn}}, {{PDB2|1rne}}, {{PDB2|2bks}}, {{PDB2|2bkt}}, {{PDB2|2fs4}}, {{PDB2|2g1n}}, {{PDB2|2g1o}}, {{PDB2|2g1r}}, {{PDB2|2g1s}}, {{PDB2|2g1y}}, {{PDB2|2g20}}, {{PDB2|2g21}}, {{PDB2|2g22}}, {{PDB2|2g24}}, {{PDB2|2g26}}, {{PDB2|2g27}}, {{PDB2|2i4q}}, {{PDB2|2iko}}, {{PDB2|2iku}}, {{PDB2|2il2}}, {{PDB2|2ren}}
| Name = Renin
| HGNCid = 9958
| Symbol = REN
| AltSymbols =; FLJ10761
| OMIM = 179820
| ECnumber =
| Homologene = 20151
| MGIid = 97898
| GeneAtlas_image1 = PBB_GE_REN_206367_at_tn.png
| Function = {{GNF_GO|id=GO:0004194 |text = pepsin A activity}} {{GNF_GO|id=GO:0004195 |text = renin activity}} {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0002003 |text = angiotensin maturation}} {{GNF_GO|id=GO:0002016 |text = renin-angiotensin regulation of body fluid levels}} {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0008217 |text = blood pressure regulation}} {{GNF_GO|id=GO:0009755 |text = hormone-mediated signaling}} {{GNF_GO|id=GO:0042756 |text = drinking behavior}} {{GNF_GO|id=GO:0043408 |text = regulation of MAPKKK cascade}} {{GNF_GO|id=GO:0048469 |text = cell maturation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5972
| Hs_Ensembl = ENSG00000143839
| Hs_RefseqProtein = NP_000528
| Hs_RefseqmRNA = NM_000537
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 202390570
| Hs_GenLoc_end = 202402088
| Hs_Uniprot = P00797
| Mm_EntrezGene = 19701
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_031192
| Mm_RefseqProtein = NP_112469
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Renin''', also known as '''REN''', 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 = Renin catalyzes the first step in the activation pathway of angiotensinogen--a cascade that can result in aldosterone release,vasoconstriction, and increase in blood pressure. Renin, an aspartyl protease, cleaves angiotensinogen to form angiotensin I, which is converted to angiotensin II by angiotensin I converting enzyme, an important regulator of blood pressure and electrolyte balance. Transcript variants that encode different protein isoforms and that arise from alternative splicing and the use of alternative promoters have been described, but their full-length nature has not been determined. Mutations in this gene have been shown to cause familial hyperproreninemia.<ref>{{cite web | title = Entrez Gene: REN renin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5972| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Morris BJ |title=New possibilities for intracellular renin and inactive renin now that the structure of the human renin gene has been elucidated. |journal=Clin. Sci. |volume=71 |issue= 4 |pages= 345-55 |year= 1986 |pmid= 3530608 |doi= }}
*{{cite journal | author=Tamura K, Umemura S, Fukamizu A, ''et al.'' |title=Recent advances in the study of renin and angiotensinogen genes: from molecules to the whole body. |journal=Hypertens. Res. |volume=18 |issue= 1 |pages= 7-18 |year= 1995 |pmid= 7584914 |doi= }}
*{{cite journal | author=Padmanabhan N, Padmanabhan S, Connell JM |title=Genetic basis of cardiovascular disease--the renin-angiotensin-aldosterone system as a paradigm. |journal=Journal of the renin-angiotensin-aldosterone system : JRAAS |volume=1 |issue= 4 |pages= 316-24 |year= 2002 |pmid= 11967817 |doi= 10.3317/jraas.2000.060 }}
*{{cite journal | author=Varagic J, Frohlich ED |title=Local cardiac renin-angiotensin system: hypertension and cardiac failure. |journal=J. Mol. Cell. Cardiol. |volume=34 |issue= 11 |pages= 1435-42 |year= 2003 |pmid= 12431442 |doi= }}
*{{cite journal | author=Jan Danser AH, Saris JJ |title=Prorenin uptake in the heart: a prerequisite for local angiotensin generation? |journal=J. Mol. Cell. Cardiol. |volume=34 |issue= 11 |pages= 1463-72 |year= 2003 |pmid= 12431445 |doi= }}
*{{cite journal | author=Benjannet S, Reudelhuber T, Mercure C, ''et al.'' |title=Proprotein conversion is determined by a multiplicity of factors including convertase processing, substrate specificity, and intracellular environment. Cell type-specific processing of human prorenin by the convertase PC1. |journal=J. Biol. Chem. |volume=267 |issue= 16 |pages= 11417-23 |year= 1992 |pmid= 1597471 |doi= }}
*{{cite journal | author=Dhanaraj V, Dealwis CG, Frazao C, ''et al.'' |title=X-ray analyses of peptide-inhibitor complexes define the structural basis of specificity for human and mouse renins. |journal=Nature |volume=357 |issue= 6378 |pages= 466-72 |year= 1992 |pmid= 1608447 |doi= 10.1038/357466a0 }}
*{{cite journal | author=Ishizuka Y, Shoda A, Yoshida S, ''et al.'' |title=Isolation and characterization of recombinant human prorenin in Chinese hamster ovary cells. |journal=J. Biochem. |volume=109 |issue= 1 |pages= 30-5 |year= 1991 |pmid= 2016271 |doi= }}
*{{cite journal | author=van Hooft IM, Grobbee DE, Derkx FH, ''et al.'' |title=Renal hemodynamics and the renin-angiotensin-aldosterone system in normotensive subjects with hypertensive and normotensive parents. |journal=N. Engl. J. Med. |volume=324 |issue= 19 |pages= 1305-11 |year= 1991 |pmid= 2017226 |doi= }}
*{{cite journal | author=Wang PH, Do YS, Macaulay L, ''et al.'' |title=Identification of renal cathepsin B as a human prorenin-processing enzyme. |journal=J. Biol. Chem. |volume=266 |issue= 19 |pages= 12633-8 |year= 1991 |pmid= 2061332 |doi= }}
*{{cite journal | author=Green DW, Aykent S, Gierse JK, Zupec ME |title=Substrate specificity of recombinant human renal renin: effect of histidine in the P2 subsite on pH dependence. |journal=Biochemistry |volume=29 |issue= 12 |pages= 3126-33 |year= 1990 |pmid= 2186807 |doi= }}
*{{cite journal | author=Vlahos CJ, Walls JD, Berg DT, Grinnell BW |title=The purification and characterization of recombinant human renin expressed in the human kidney cell line 293. |journal=Biochem. Biophys. Res. Commun. |volume=171 |issue= 1 |pages= 375-83 |year= 1990 |pmid= 2203348 |doi= }}
*{{cite journal | author=Evin G, Galen FX, Carlson WD, ''et al.'' |title=Characterization of five epitopes of human renin from a computer model. |journal=Biochemistry |volume=27 |issue= 1 |pages= 156-64 |year= 1988 |pmid= 2450565 |doi= }}
*{{cite journal | author=Sielecki AR, Hayakawa K, Fujinaga M, ''et al.'' |title=Structure of recombinant human renin, a target for cardiovascular-active drugs, at 2.5 A resolution. |journal=Science |volume=243 |issue= 4896 |pages= 1346-51 |year= 1989 |pmid= 2493678 |doi= }}
*{{cite journal | author=Burt DW, Nakamura N, Kelley P, Dzau VJ |title=Identification of negative and positive regulatory elements in the human renin gene. |journal=J. Biol. Chem. |volume=264 |issue= 13 |pages= 7357-62 |year= 1989 |pmid= 2540188 |doi= }}
*{{cite journal | author=Faust PL, Chirgwin JM, Kornfeld S |title=Renin, a secretory glycoprotein, acquires phosphomannosyl residues. |journal=J. Cell Biol. |volume=105 |issue= 5 |pages= 1947-55 |year= 1988 |pmid= 2960682 |doi= }}
*{{cite journal | author=Fukamizu A, Nishi K, Nishimatsu S, ''et al.'' |title=Human renin gene of renin-secreting tumor. |journal=Gene |volume=49 |issue= 1 |pages= 139-45 |year= 1987 |pmid= 3032746 |doi= }}
*{{cite journal | author=Hori H, Yoshino T, Ishizuka Y, ''et al.'' |title=Characterization of N-linked oligosaccharides attached to human renin expressed in COS cells. |journal=Clinical and experimental hypertension. Part A, Theory and practice |volume=10 |issue= 6 |pages= 1147-55 |year= 1989 |pmid= 3066525 |doi= }}
*{{cite journal | author=Hori H, Yoshino T, Ishizuka Y, ''et al.'' |title=Role of N-linked oligosaccharides attached to human renin expressed in COS cells. |journal=FEBS Lett. |volume=232 |issue= 2 |pages= 391-4 |year= 1988 |pmid= 3288503 |doi= }}
*{{cite journal | author=McGill JR, Chirgwin JM, Moore CM, McCombs JL |title=Chromosome localization of the human renin gene (REN) by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=45 |issue= 1 |pages= 55-7 |year= 1987 |pmid= 3297510 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SAA1... {November 14, 2007 4:22:45 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:23:18 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 = Serum amyloid A1
| HGNCid = 10513
| Symbol = SAA1
| AltSymbols =; SAA; MGC111216; PIG4; TP53I4
| OMIM = 104750
| ECnumber =
| Homologene = 69088
| MGIid = 98221
| GeneAtlas_image1 = PBB_GE_SAA1_208607_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SAA1_214456_x_at_tn.png
| Function = {{GNF_GO|id=GO:0001664 |text = G-protein-coupled receptor binding}} {{GNF_GO|id=GO:0005319 |text = lipid transporter activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006953 |text = acute-phase response}} {{GNF_GO|id=GO:0007204 |text = elevation of cytosolic calcium ion concentration}} {{GNF_GO|id=GO:0030168 |text = platelet activation}} {{GNF_GO|id=GO:0030593 |text = neutrophil chemotaxis}} {{GNF_GO|id=GO:0045785 |text = positive regulation of cell adhesion}} {{GNF_GO|id=GO:0048246 |text = macrophage chemotaxis}} {{GNF_GO|id=GO:0048247 |text = lymphocyte chemotaxis}} {{GNF_GO|id=GO:0050708 |text = regulation of protein secretion}} {{GNF_GO|id=GO:0050716 |text = positive regulation of interleukin-1 secretion}} {{GNF_GO|id=GO:0050728 |text = negative regulation of inflammatory response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6288
| Hs_Ensembl = ENSG00000173432
| Hs_RefseqProtein = NP_000322
| Hs_RefseqmRNA = NM_000331
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 18244346
| Hs_GenLoc_end = 18248088
| Hs_Uniprot = P02735
| Mm_EntrezGene = 20208
| Mm_Ensembl = ENSMUSG00000074115
| Mm_RefseqmRNA = NM_009117
| Mm_RefseqProtein = NP_033143
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 46608540
| Mm_GenLoc_end = 46611022
| Mm_Uniprot = Q64454
}}
}}
'''Serum amyloid A1''', also known as '''SAA1''', 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=Kisilevsky R, Tam SP |title=Acute phase serum amyloid A, cholesterol metabolism, and cardiovascular disease. |journal=Pediatric pathology & molecular medicine |volume=21 |issue= 3 |pages= 291-305 |year= 2002 |pmid= 12056504 |doi= 10.1080/02770930290056523 }}
*{{cite journal | author=Sletten K, Husby G, Natvig JB |title=The complete amino acid sequence of an amyloid fibril protein AA1 of unusual size (64 residues). |journal=Biochem. Biophys. Res. Commun. |volume=69 |issue= 1 |pages= 19-25 |year= 1976 |pmid= 1259755 |doi= }}
*{{cite journal | author=Beach CM, De Beer MC, Sipe JD, ''et al.'' |title=Human serum amyloid A protein. Complete amino acid sequence of a new variant. |journal=Biochem. J. |volume=282 ( Pt 2) |issue= |pages= 615-20 |year= 1992 |pmid= 1546977 |doi= }}
*{{cite journal | author=Betts JC, Edbrooke MR, Thakker RV, Woo P |title=The human acute-phase serum amyloid A gene family: structure, evolution and expression in hepatoma cells. |journal=Scand. J. Immunol. |volume=34 |issue= 4 |pages= 471-82 |year= 1991 |pmid= 1656519 |doi= }}
*{{cite journal | author=Zimlichman S, Danon A, Nathan I, ''et al.'' |title=Serum amyloid A, an acute phase protein, inhibits platelet activation. |journal=J. Lab. Clin. Med. |volume=116 |issue= 2 |pages= 180-6 |year= 1990 |pmid= 1697614 |doi= }}
*{{cite journal | author=Steinkasserer A, Weiss EH, Schwaeble W, Linke RP |title=Heterogeneity of human serum amyloid A protein. Five different variants from one individual demonstrated by cDNA sequence analysis. |journal=Biochem. J. |volume=268 |issue= 1 |pages= 187-93 |year= 1990 |pmid= 1971508 |doi= }}
*{{cite journal | author=Sack GH, Talbot CC |title=Highly polymorphic domains of the human serum amyloid A (SAA) gene GSAA1. |journal=Scand. J. Immunol. |volume=33 |issue= 4 |pages= 485-8 |year= 1991 |pmid= 2017667 |doi= }}
*{{cite journal | author=Glaser T, Housman D, Lewis WH, ''et al.'' |title=A fine-structure deletion map of human chromosome 11p: analysis of J1 series hybrids. |journal=Somat. Cell Mol. Genet. |volume=15 |issue= 6 |pages= 477-501 |year= 1990 |pmid= 2595451 |doi= }}
*{{cite journal | author=Woo P, Sipe J, Dinarello CA, Colten HR |title=Structure of a human serum amyloid A gene and modulation of its expression in transfected L cells. |journal=J. Biol. Chem. |volume=262 |issue= 32 |pages= 15790-5 |year= 1987 |pmid= 2890635 |doi= }}
*{{cite journal | author=Kluve-Beckerman B, Dwulet FE, Benson MD |title=Human serum amyloid A. Three hepatic mRNAs and the corresponding proteins in one person. |journal=J. Clin. Invest. |volume=82 |issue= 5 |pages= 1670-5 |year= 1988 |pmid= 3183061 |doi= }}
*{{cite journal | author=Prelli F, Pras M, Frangione B |title=Degradation and deposition of amyloid AA fibrils are tissue specific. |journal=Biochemistry |volume=26 |issue= 25 |pages= 8251-6 |year= 1988 |pmid= 3442653 |doi= }}
*{{cite journal | author=Kluve-Beckerman B, Long GL, Benson MD |title=DNA sequence evidence for polymorphic forms of human serum amyloid A (SAA). |journal=Biochem. Genet. |volume=24 |issue= 11-12 |pages= 795-803 |year= 1987 |pmid= 3800865 |doi= }}
*{{cite journal | author=Sipe JD, Colten HR, Goldberger G, ''et al.'' |title=Human serum amyloid A (SAA): biosynthesis and postsynthetic processing of preSAA and structural variants defined by complementary DNA. |journal=Biochemistry |volume=24 |issue= 12 |pages= 2931-6 |year= 1985 |pmid= 3839415 |doi= }}
*{{cite journal | author=Sletten K, Husby G |title=The complete amino-acid sequence of non-immunoglobulin amyloid fibril protein AS in rheumatoid arthritis. |journal=Eur. J. Biochem. |volume=41 |issue= 1 |pages= 117-25 |year= 1974 |pmid= 4816450 |doi= }}
*{{cite journal | author=Ein D, Kimura S, Terry WD, ''et al.'' |title=Amino acid sequence of an amyloid fibril protein of unknown origin. |journal=J. Biol. Chem. |volume=247 |issue= 17 |pages= 5653-5 |year= 1972 |pmid= 5055786 |doi= }}
*{{cite journal | author=Levin M, Franklin EC, Frangione B, Pras M |title=The amino acid sequence of a major nonimmunoglobulin component of some amyloid fibrils. |journal=J. Clin. Invest. |volume=51 |issue= 10 |pages= 2773-6 |year= 1972 |pmid= 5056669 |doi= }}
*{{cite journal | author=Møyner K, Sletten K, Husby G, Natvig JB |title=An unusually large (83 amino acid residues) amyloid fibril protein AA from a patient with Waldenström's macroglobulinaemia and amyloidosis. |journal=Scand. J. Immunol. |volume=11 |issue= 5 |pages= 549-54 |year= 1980 |pmid= 6155694 |doi= }}
*{{cite journal | author=Parmelee DC, Titani K, Ericsson LH, ''et al.'' |title=Amino acid sequence of amyloid-related apoprotein (apoSAA1) from human high-density lipoprotein. |journal=Biochemistry |volume=21 |issue= 14 |pages= 3298-303 |year= 1982 |pmid= 7115671 |doi= }}
*{{cite journal | author=Badolato R, Wang JM, Murphy WJ, ''et al.'' |title=Serum amyloid A is a chemoattractant: induction of migration, adhesion, and tissue infiltration of monocytes and polymorphonuclear leukocytes. |journal=J. Exp. Med. |volume=180 |issue= 1 |pages= 203-9 |year= 1994 |pmid= 7516407 |doi= }}
*{{cite journal | author=Badolato R, Johnston JA, Wang JM, ''et al.'' |title=Serum amyloid A induces calcium mobilization and chemotaxis of human monocytes by activating a pertussis toxin-sensitive signaling pathway. |journal=J. Immunol. |volume=155 |issue= 8 |pages= 4004-10 |year= 1995 |pmid= 7561109 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SELPLG... {November 14, 2007 4:23:18 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:23:57 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 = Selectin P ligand
| HGNCid = 10722
| Symbol = SELPLG
| AltSymbols =; CD162; CLA; PSGL-1; PSGL1
| OMIM = 600738
| ECnumber =
| Homologene = 2261
| MGIid = 106689
| GeneAtlas_image1 = PBB_GE_SELPLG_209879_at_tn.png
| GeneAtlas_image2 = PBB_GE_SELPLG_209880_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005529 |text = sugar binding}} {{GNF_GO|id=GO:0008367 |text = bacterial binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6404
| Hs_Ensembl = ENSG00000110876
| Hs_RefseqProtein = NP_002997
| Hs_RefseqmRNA = NM_003006
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 107540974
| Hs_GenLoc_end = 107542212
| Hs_Uniprot = Q14242
| Mm_EntrezGene = 20345
| Mm_Ensembl = ENSMUSG00000048163
| Mm_RefseqmRNA = NM_009151
| Mm_RefseqProtein = NP_033177
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 114079535
| Mm_GenLoc_end = 114091474
| Mm_Uniprot = Q99L34
}}
}}
'''Selectin P ligand''', also known as '''SELPLG''', 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 = SELPLG is the high affinity counter-receptor for P-selectin on myeloid cells and stimulated T lymphocytes. As such, it plays a critical role in the tethering of these cells to activated platelets or endothelia expressing P-selectin. The organization of the SELPG gene closely resembles that of CD43 and the human platelet glycoprotein GpIb-alpha both of which have an intron in the 5-prime-noncoding region, a long second exon containing the complete coding region, and TATA-less promoters.<ref>{{cite web | title = Entrez Gene: SELPLG selectin P ligand| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6404| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Furie B, Furie BC |title=Role of platelet P-selectin and microparticle PSGL-1 in thrombus formation. |journal=Trends in molecular medicine |volume=10 |issue= 4 |pages= 171-8 |year= 2004 |pmid= 15059608 |doi= 10.1016/j.molmed.2004.02.008 }}
*{{cite journal | author=Sako D, Chang XJ, Barone KM, ''et al.'' |title=Expression cloning of a functional glycoprotein ligand for P-selectin. |journal=Cell |volume=75 |issue= 6 |pages= 1179-86 |year= 1994 |pmid= 7505206 |doi= }}
*{{cite journal | author=Moore KL, Eaton SF, Lyons DE, ''et al.'' |title=The P-selectin glycoprotein ligand from human neutrophils displays sialylated, fucosylated, O-linked poly-N-acetyllactosamine. |journal=J. Biol. Chem. |volume=269 |issue= 37 |pages= 23318-27 |year= 1994 |pmid= 7521878 |doi= }}
*{{cite journal | author=Veldman GM, Bean KM, Cumming DA, ''et al.'' |title=Genomic organization and chromosomal localization of the gene encoding human P-selectin glycoprotein ligand. |journal=J. Biol. Chem. |volume=270 |issue= 27 |pages= 16470-5 |year= 1995 |pmid= 7541799 |doi= }}
*{{cite journal | author=Wilkins PP, Moore KL, McEver RP, Cummings RD |title=Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required for high affinity binding to P-selectin. |journal=J. Biol. Chem. |volume=270 |issue= 39 |pages= 22677-80 |year= 1995 |pmid= 7559387 |doi= }}
*{{cite journal | author=Sako D, Comess KM, Barone KM, ''et al.'' |title=A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding. |journal=Cell |volume=83 |issue= 2 |pages= 323-31 |year= 1995 |pmid= 7585949 |doi= }}
*{{cite journal | author=Pouyani T, Seed B |title=PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus. |journal=Cell |volume=83 |issue= 2 |pages= 333-43 |year= 1995 |pmid= 7585950 |doi= }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Li F, Wilkins PP, Crawley S, ''et al.'' |title=Post-translational modifications of recombinant P-selectin glycoprotein ligand-1 required for binding to P- and E-selectin. |journal=J. Biol. Chem. |volume=271 |issue= 6 |pages= 3255-64 |year= 1996 |pmid= 8621728 |doi= }}
*{{cite journal | author=Guyer DA, Moore KL, Lynam EB, ''et al.'' |title=P-selectin glycoprotein ligand-1 (PSGL-1) is a ligand for L-selectin in neutrophil aggregation. |journal=Blood |volume=88 |issue= 7 |pages= 2415-21 |year= 1996 |pmid= 8839831 |doi= }}
*{{cite journal | author=Goetz DJ, Greif DM, Ding H, ''et al.'' |title=Isolated P-selectin glycoprotein ligand-1 dynamic adhesion to P- and E-selectin. |journal=J. Cell Biol. |volume=137 |issue= 2 |pages= 509-19 |year= 1997 |pmid= 9128259 |doi= }}
*{{cite journal | author=Fuhlbrigge RC, Kieffer JD, Armerding D, Kupper TS |title=Cutaneous lymphocyte antigen is a specialized form of PSGL-1 expressed on skin-homing T cells. |journal=Nature |volume=389 |issue= 6654 |pages= 978-81 |year= 1997 |pmid= 9353122 |doi= 10.1038/40166 }}
*{{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=Snapp KR, Ding H, Atkins K, ''et al.'' |title=A novel P-selectin glycoprotein ligand-1 monoclonal antibody recognizes an epitope within the tyrosine sulfate motif of human PSGL-1 and blocks recognition of both P- and L-selectin. |journal=Blood |volume=91 |issue= 1 |pages= 154-64 |year= 1998 |pmid= 9414280 |doi= }}
*{{cite journal | author=Bennett EP, Hassan H, Mandel U, ''et al.'' |title=Cloning of a human UDP-N-acetyl-alpha-D-Galactosamine:polypeptide N-acetylgalactosaminyltransferase that complements other GalNAc-transferases in complete O-glycosylation of the MUC1 tandem repeat. |journal=J. Biol. Chem. |volume=273 |issue= 46 |pages= 30472-81 |year= 1998 |pmid= 9804815 |doi= }}
*{{cite journal | author=Wimazal F, Ghannadan M, Müller MR, ''et al.'' |title=Expression of homing receptors and related molecules on human mast cells and basophils: a comparative analysis using multi-color flow cytometry and toluidine blue/immunofluorescence staining techniques. |journal=Tissue Antigens |volume=54 |issue= 5 |pages= 499-507 |year= 2000 |pmid= 10599889 |doi= }}
*{{cite journal | author=Epperson TK, Patel KD, McEver RP, Cummings RD |title=Noncovalent association of P-selectin glycoprotein ligand-1 and minimal determinants for binding to P-selectin. |journal=J. Biol. Chem. |volume=275 |issue= 11 |pages= 7839-53 |year= 2000 |pmid= 10713099 |doi= }}
*{{cite journal | author=André P, Spertini O, Guia S, ''et al.'' |title=Modification of P-selectin glycoprotein ligand-1 with a natural killer cell-restricted sulfated lactosamine creates an alternate ligand for L-selectin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3400-5 |year= 2000 |pmid= 10725346 |doi= 10.1073/pnas.040569797 }}
*{{cite journal | author=Frenette PS, Denis CV, Weiss L, ''et al.'' |title=P-Selectin glycoprotein ligand 1 (PSGL-1) is expressed on platelets and can mediate platelet-endothelial interactions in vivo. |journal=J. Exp. Med. |volume=191 |issue= 8 |pages= 1413-22 |year= 2000 |pmid= 10770806 |doi= }}
*{{cite journal | author=Woltmann G, McNulty CA, Dewson G, ''et al.'' |title=Interleukin-13 induces PSGL-1/P-selectin-dependent adhesion of eosinophils, but not neutrophils, to human umbilical vein endothelial cells under flow. |journal=Blood |volume=95 |issue= 10 |pages= 3146-52 |year= 2000 |pmid= 10807781 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SERPINB5... {November 14, 2007 4:19:18 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:19:54 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_SERPINB5_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1wz9.
| PDB = {{PDB2|1wz9}}, {{PDB2|1xqg}}, {{PDB2|1xqj}}, {{PDB2|1xu8}}
| Name = Serpin peptidase inhibitor, clade B (ovalbumin), member 5
| HGNCid = 8949
| Symbol = SERPINB5
| AltSymbols =; PI5; maspin
| OMIM = 154790
| ECnumber =
| Homologene = 20580
| MGIid = 109579
| GeneAtlas_image1 = PBB_GE_SERPINB5_204855_at_tn.png
| Function = {{GNF_GO|id=GO:0004867 |text = serine-type endopeptidase inhibitor activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006928 |text = cell motility}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5268
| Hs_Ensembl = ENSG00000206075
| Hs_RefseqProtein = NP_002630
| Hs_RefseqmRNA = NM_002639
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 18
| Hs_GenLoc_start = 59295199
| Hs_GenLoc_end = 59323297
| Hs_Uniprot = P36952
| Mm_EntrezGene = 20724
| Mm_Ensembl = ENSMUSG00000067006
| Mm_RefseqmRNA = NM_009257
| Mm_RefseqProtein = NP_033283
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 108688727
| Mm_GenLoc_end = 108710895
| Mm_Uniprot = Q3ULZ0
}}
}}
'''Serpin peptidase inhibitor, clade B (ovalbumin), member 5''', also known as '''SERPINB5''', 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=Sager R, Sheng S, Pemberton P, Hendrix MJ |title=Maspin. A tumor suppressing serpin. |journal=Adv. Exp. Med. Biol. |volume=425 |issue= |pages= 77-88 |year= 1998 |pmid= 9433491 |doi= }}
*{{cite journal | author=Sheng S |title=The promise and challenge toward the clinical application of maspin in cancer. |journal=Front. Biosci. |volume=9 |issue= |pages= 2733-45 |year= 2006 |pmid= 15353310 |doi= }}
*{{cite journal | author=Lockett J, Yin S, Li X, ''et al.'' |title=Tumor suppressive maspin and epithelial homeostasis. |journal=J. Cell. Biochem. |volume=97 |issue= 4 |pages= 651-60 |year= 2006 |pmid= 16329135 |doi= 10.1002/jcb.20721 }}
*{{cite journal | author=Chen EI, Yates JR |title=Maspin and tumor metastasis. |journal=IUBMB Life |volume=58 |issue= 1 |pages= 25-9 |year= 2006 |pmid= 16540429 |doi= 10.1080/15216540500531721 }}
*{{cite journal | author=Khalkhali-Ellis Z |title=Maspin: the new frontier. |journal=Clin. Cancer Res. |volume=12 |issue= 24 |pages= 7279-83 |year= 2007 |pmid= 17189399 |doi= 10.1158/1078-0432.CCR-06-1589 }}
*{{cite journal | author=Schneider SS, Schick C, Fish KE, ''et al.'' |title=A serine proteinase inhibitor locus at 18q21.3 contains a tandem duplication of the human squamous cell carcinoma antigen gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 8 |pages= 3147-51 |year= 1995 |pmid= 7724531 |doi= }}
*{{cite journal | author=Pemberton PA, Wong DT, Gibson HL, ''et al.'' |title=The tumor suppressor maspin does not undergo the stressed to relaxed transition or inhibit trypsin-like serine proteases. Evidence that maspin is not a protease inhibitory serpin. |journal=J. Biol. Chem. |volume=270 |issue= 26 |pages= 15832-7 |year= 1995 |pmid= 7797587 |doi= }}
*{{cite journal | author=Zou Z, Anisowicz A, Hendrix MJ, ''et al.'' |title=Maspin, a serpin with tumor-suppressing activity in human mammary epithelial cells. |journal=Science |volume=263 |issue= 5146 |pages= 526-9 |year= 1994 |pmid= 8290962 |doi= }}
*{{cite journal | author=Pemberton PA, Tipton AR, Pavloff N, ''et al.'' |title=Maspin is an intracellular serpin that partitions into secretory vesicles and is present at the cell surface. |journal=J. Histochem. Cytochem. |volume=45 |issue= 12 |pages= 1697-706 |year= 1998 |pmid= 9389773 |doi= }}
*{{cite journal | author=Xia W, Lau YK, Hu MC, ''et al.'' |title=High tumoral maspin expression is associated with improved survival of patients with oral squamous cell carcinoma. |journal=Oncogene |volume=19 |issue= 20 |pages= 2398-403 |year= 2000 |pmid= 10828881 |doi= 10.1038/sj.onc.1203535 }}
*{{cite journal | author=Biliran H, Sheng S |title=Pleiotrophic inhibition of pericellular urokinase-type plasminogen activator system by endogenous tumor suppressive maspin. |journal=Cancer Res. |volume=61 |issue= 24 |pages= 8676-82 |year= 2002 |pmid= 11751384 |doi= }}
*{{cite journal | author=Blacque OE, Worrall DM |title=Evidence for a direct interaction between the tumor suppressor serpin, maspin, and types I and III collagen. |journal=J. Biol. Chem. |volume=277 |issue= 13 |pages= 10783-8 |year= 2002 |pmid= 11788595 |doi= 10.1074/jbc.M110992200 }}
*{{cite journal | author=Dokras A, Gardner LM, Kirschmann DA, ''et al.'' |title=The tumour suppressor gene maspin is differentially regulated in cytotrophoblasts during human placental development. |journal=Placenta |volume=23 |issue= 4 |pages= 274-80 |year= 2002 |pmid= 11969337 |doi= 10.1053/plac.2001.0784 }}
*{{cite journal | author=Jiang N, Meng Y, Zhang S, ''et al.'' |title=Maspin sensitizes breast carcinoma cells to induced apoptosis. |journal=Oncogene |volume=21 |issue= 26 |pages= 4089-98 |year= 2002 |pmid= 12037665 |doi= 10.1038/sj.onc.1205507 }}
*{{cite journal | author=Odero-Marah VA, Khalkhali-Ellis Z, Schneider GB, ''et al.'' |title=Tyrosine phosphorylation of maspin in normal mammary epithelia and breast cancer cells. |journal=Biochem. Biophys. Res. Commun. |volume=295 |issue= 4 |pages= 800-5 |year= 2002 |pmid= 12127964 |doi= }}
*{{cite journal | author=Maass N, Biallek M, Rösel F, ''et al.'' |title=Hypermethylation and histone deacetylation lead to silencing of the maspin gene in human breast cancer. |journal=Biochem. Biophys. Res. Commun. |volume=297 |issue= 1 |pages= 125-8 |year= 2002 |pmid= 12220518 |doi= }}
*{{cite journal | author=Sood AK, Fletcher MS, Gruman LM, ''et al.'' |title=The paradoxical expression of maspin in ovarian carcinoma. |journal=Clin. Cancer Res. |volume=8 |issue= 9 |pages= 2924-32 |year= 2002 |pmid= 12231537 |doi= }}
*{{cite journal | author=Son HJ, Sohn TS, Song SY, ''et al.'' |title=Maspin expression in human gastric adenocarcinoma. |journal=Pathol. Int. |volume=52 |issue= 8 |pages= 508-13 |year= 2003 |pmid= 12366809 |doi= }}
*{{cite journal | author=Bass R, Fernández AM, Ellis V |title=Maspin inhibits cell migration in the absence of protease inhibitory activity. |journal=J. Biol. Chem. |volume=277 |issue= 49 |pages= 46845-8 |year= 2003 |pmid= 12384513 |doi= 10.1074/jbc.C200532200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SERPING1... {November 14, 2007 4:12:29 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:13:04 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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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_SERPING1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2oay.
| PDB = {{PDB2|2oay}}
| Name = Serpin peptidase inhibitor, clade G (C1 inhibitor), member 1, (angioedema, hereditary)
| HGNCid = 1228
| Symbol = SERPING1
| AltSymbols =; C1IN; C1INH; C1NH; HAE1; HAE2
| OMIM = 606860
| ECnumber =
| Homologene = 44
| MGIid = 894696
| GeneAtlas_image1 = PBB_GE_SERPING1_200986_at_tn.png
| Function = {{GNF_GO|id=GO:0004867 |text = serine-type endopeptidase inhibitor activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006958 |text = complement activation, classical pathway}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}} {{GNF_GO|id=GO:0008015 |text = circulation}} {{GNF_GO|id=GO:0045087 |text = innate immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 710
| Hs_Ensembl = ENSG00000149131
| Hs_RefseqProtein = NP_000053
| Hs_RefseqmRNA = NM_000062
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 57121603
| Hs_GenLoc_end = 57138902
| Hs_Uniprot = P05155
| Mm_EntrezGene = 12258
| Mm_Ensembl = ENSMUSG00000023224
| Mm_RefseqmRNA = NM_009776
| Mm_RefseqProtein = NP_033906
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 84566224
| Mm_GenLoc_end = 84576243
| Mm_Uniprot = P97290
}}
}}
'''Serpin peptidase inhibitor, clade G (C1 inhibitor), member 1, (angioedema, hereditary)''', also known as '''SERPING1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a highly glycosylated plasma protein involved in the regulation of the complement cascade. Its protein inhibits activated C1r and C1s of the first complement component and thus regulates complement activation. Deficiency of this protein is associated with hereditary angioneurotic oedema (HANE). Alternative splicing results in multiple transcript variants encoding the same isoform.<ref>{{cite web | title = Entrez Gene: SERPING1 serpin peptidase inhibitor, clade G (C1 inhibitor), member 1, (angioedema, hereditary)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=710| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lappin D, Whaley K |title=Regulation of C1-inhibitor synthesis by interferons and other agents. |journal=Behring Inst. Mitt. |volume= |issue= 84 |pages= 180-92 |year= 1989 |pmid= 2478116 |doi= }}
*{{cite journal | author=Stein PE, Carrell RW |title=What do dysfunctional serpins tell us about molecular mobility and disease? |journal=Nat. Struct. Biol. |volume=2 |issue= 2 |pages= 96-113 |year= 1995 |pmid= 7749926 |doi= }}
*{{cite journal | author=Davis AE, Bissler JJ, Cicardi M |title=Mutations in the C1 inhibitor gene that result in hereditary angioneurotic edema. |journal=Behring Inst. Mitt. |volume= |issue= 93 |pages= 313-20 |year= 1994 |pmid= 8172583 |doi= }}
*{{cite journal | author=Davis AE |title=The pathophysiology of hereditary angioedema. |journal=Clin. Immunol. |volume=114 |issue= 1 |pages= 3-9 |year= 2005 |pmid= 15596403 |doi= 10.1016/j.clim.2004.05.007 }}
*{{cite journal | author=Siddique Z, McPhaden AR, McCluskey D, Whaley K |title=A single base deletion from the C1-inhibitor gene causes type I hereditary angio-oedema. |journal=Hum. Hered. |volume=42 |issue= 4 |pages= 231-4 |year= 1992 |pmid= 1339401 |doi= }}
*{{cite journal | author=Davis AE, Aulak K, Parad RB, ''et al.'' |title=C1 inhibitor hinge region mutations produce dysfunction by different mechanisms. |journal=Nat. Genet. |volume=1 |issue= 5 |pages= 354-8 |year= 1993 |pmid= 1363816 |doi= 10.1038/ng0892-354 }}
*{{cite journal | author=Frangi D, Aulak KS, Cicardi M, ''et al.'' |title=A dysfunctional C1 inhibitor protein with a new reactive center mutation (Arg-444-->Leu). |journal=FEBS Lett. |volume=301 |issue= 1 |pages= 34-6 |year= 1992 |pmid= 1451784 |doi= }}
*{{cite journal | author=Lappin DF, Guc D, Hill A, ''et al.'' |title=Effect of interferon-gamma on complement gene expression in different cell types. |journal=Biochem. J. |volume=281 ( Pt 2) |issue= |pages= 437-42 |year= 1992 |pmid= 1531292 |doi= }}
*{{cite journal | author=Siddique Z, McPhaden AR, Lappin DF, Whaley K |title=An RNA splice site mutation in the C1-inhibitor gene causes type I hereditary angio-oedema. |journal=Hum. Genet. |volume=88 |issue= 2 |pages= 231-2 |year= 1992 |pmid= 1684567 |doi= }}
*{{cite journal | author=Frangi D, Cicardi M, Sica A, ''et al.'' |title=Nonsense mutations affect C1 inhibitor messenger RNA levels in patients with type I hereditary angioneurotic edema. |journal=J. Clin. Invest. |volume=88 |issue= 3 |pages= 755-9 |year= 1991 |pmid= 1885769 |doi= }}
*{{cite journal | author=Carter PE, Duponchel C, Tosi M, Fothergill JE |title=Complete nucleotide sequence of the gene for human C1 inhibitor with an unusually high density of Alu elements. |journal=Eur. J. Biochem. |volume=197 |issue= 2 |pages= 301-8 |year= 1991 |pmid= 2026152 |doi= }}
*{{cite journal | author=Parad RB, Kramer J, Strunk RC, ''et al.'' |title=Dysfunctional C1 inhibitor Ta: deletion of Lys-251 results in acquisition of an N-glycosylation site. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 17 |pages= 6786-90 |year= 1990 |pmid= 2118657 |doi= }}
*{{cite journal | author=Stoppa-Lyonnet D, Carter PE, Meo T, Tosi M |title=Clusters of intragenic Alu repeats predispose the human C1 inhibitor locus to deleterious rearrangements. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 4 |pages= 1551-5 |year= 1990 |pmid= 2154751 |doi= }}
*{{cite journal | author=Levy NJ, Ramesh N, Cicardi M, ''et al.'' |title=Type II hereditary angioneurotic edema that may result from a single nucleotide change in the codon for alanine-436 in the C1 inhibitor gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 1 |pages= 265-8 |year= 1990 |pmid= 2296585 |doi= }}
*{{cite journal | author=Theriault A, Whaley K, McPhaden AR, ''et al.'' |title=Regional assignment of the human C1-inhibitor gene to 11q11-q13.1. |journal=Hum. Genet. |volume=84 |issue= 5 |pages= 477-9 |year= 1990 |pmid= 2323781 |doi= }}
*{{cite journal | author=Aulak KS, Cicardi M, Harrison RA |title=Identification of a new P1 residue mutation (444Arg----Ser) in a dysfunctional C1 inhibitor protein contained in a type II hereditary angioedema plasma. |journal=FEBS Lett. |volume=266 |issue= 1-2 |pages= 13-6 |year= 1990 |pmid= 2365061 |doi= }}
*{{cite journal | author=Skriver K, Radziejewska E, Silbermann JA, ''et al.'' |title=CpG mutations in the reactive site of human C1 inhibitor. |journal=J. Biol. Chem. |volume=264 |issue= 6 |pages= 3066-71 |year= 1989 |pmid= 2563376 |doi= }}
*{{cite journal | author=Ariga T, Igarashi T, Ramesh N, ''et al.'' |title=Type I C1 inhibitor deficiency with a small messenger RNA resulting from deletion of one exon. |journal=J. Clin. Invest. |volume=83 |issue= 6 |pages= 1888-93 |year= 1989 |pmid= 2723063 |doi= }}
*{{cite journal | author=Tosi M, Duponchel C, Bourgarel P, ''et al.'' |title=Molecular cloning of human C1 inhibitor: sequence homologies with alpha 1-antitrypsin and other members of the serpins superfamily. |journal=Gene |volume=42 |issue= 3 |pages= 265-72 |year= 1986 |pmid= 3089875 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SNAP25... {November 14, 2007 4:23:57 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:24:43 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_SNAP25_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1jth.
| PDB = {{PDB2|1jth}}, {{PDB2|1kil}}, {{PDB2|1n7s}}, {{PDB2|1sfc}}, {{PDB2|1urq}}, {{PDB2|1xtg}}
| Name = Synaptosomal-associated protein, 25kDa
| HGNCid = 11132
| Symbol = SNAP25
| AltSymbols =; FLJ23079; RIC-4; RIC4; SEC9; SNAP; SNAP-25; bA416N4.2; dJ1068F16.2
| OMIM = 600322
| ECnumber =
| Homologene = 13311
| MGIid = 98331
| GeneAtlas_image1 = PBB_GE_SNAP25_202508_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SNAP25_202507_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000149 |text = SNARE binding}}
| Component = {{GNF_GO|id=GO:0019717 |text = synaptosome}} {{GNF_GO|id=GO:0045202 |text = synapse}}
| Process = {{GNF_GO|id=GO:0001504 |text = neurotransmitter uptake}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007269 |text = neurotransmitter secretion}} {{GNF_GO|id=GO:0016081 |text = synaptic vesicle docking during exocytosis}} {{GNF_GO|id=GO:0050796 |text = regulation of insulin secretion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6616
| Hs_Ensembl = ENSG00000132639
| Hs_RefseqProtein = NP_003072
| Hs_RefseqmRNA = NM_003081
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 10147477
| Hs_GenLoc_end = 10236066
| Hs_Uniprot = P60880
| Mm_EntrezGene = 20614
| Mm_Ensembl = ENSMUSG00000027273
| Mm_RefseqmRNA = NM_011428
| Mm_RefseqProtein = NP_035558
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 136404894
| Mm_GenLoc_end = 136473860
| Mm_Uniprot = P60879
}}
}}
'''Synaptosomal-associated protein, 25kDa''', also known as '''SNAP25''', 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 = Synaptic vesicle membrane docking and fusion is mediated by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) located on the vesicle membrane (v-SNAREs) and the target membrane (t-SNAREs). The assembled v-SNARE/t-SNARE complex consists of a bundle of four helices, one of which is supplied by v-SNARE and the other three by t-SNARE. For t-SNAREs on the plasma membrane, the protein syntaxin supplies one helix and the protein encoded by this gene contributes the other two. Therefore, this gene product is a presynaptic plasma membrane protein involved in the regulation of neurotransmitter release. Two alternative transcript variants encoding different protein isoforms have been described for this gene.<ref>{{cite web | title = Entrez Gene: SNAP25 synaptosomal-associated protein, 25kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6616| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hanson PI, Otto H, Barton N, Jahn R |title=The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin. |journal=J. Biol. Chem. |volume=270 |issue= 28 |pages= 16955-61 |year= 1995 |pmid= 7622514 |doi= }}
*{{cite journal | author=Hata Y, Südhof TC |title=A novel ubiquitous form of Munc-18 interacts with multiple syntaxins. Use of the yeast two-hybrid system to study interactions between proteins involved in membrane traffic. |journal=J. Biol. Chem. |volume=270 |issue= 22 |pages= 13022-8 |year= 1995 |pmid= 7768895 |doi= }}
*{{cite journal | author=Chapman ER, An S, Barton N, Jahn R |title=SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils. |journal=J. Biol. Chem. |volume=269 |issue= 44 |pages= 27427-32 |year= 1994 |pmid= 7961655 |doi= }}
*{{cite journal | author=Zhao N, Hashida H, Takahashi N, Sakaki Y |title=Cloning and sequence analysis of the human SNAP25 cDNA. |journal=Gene |volume=145 |issue= 2 |pages= 313-4 |year= 1994 |pmid= 8056350 |doi= }}
*{{cite journal | author=Bark IC, Wilson MC |title=Human cDNA clones encoding two different isoforms of the nerve terminal protein SNAP-25. |journal=Gene |volume=139 |issue= 2 |pages= 291-2 |year= 1994 |pmid= 8112622 |doi= }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=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= }}
*{{cite journal | author=Ravichandran V, Chawla A, Roche PA |title=Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues. |journal=J. Biol. Chem. |volume=271 |issue= 23 |pages= 13300-3 |year= 1996 |pmid= 8663154 |doi= }}
*{{cite journal | author=Rettig J, Sheng ZH, Kim DK, ''et al.'' |title=Isoform-specific interaction of the alpha1A subunits of brain Ca2+ channels with the presynaptic proteins syntaxin and SNAP-25. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 14 |pages= 7363-8 |year= 1996 |pmid= 8692999 |doi= }}
*{{cite journal | author=Jagadish MN, Fernandez CS, Hewish DR, ''et al.'' |title=Insulin-responsive tissues contain the core complex protein SNAP-25 (synaptosomal-associated protein 25) A and B isoforms in addition to syntaxin 4 and synaptobrevins 1 and 2. |journal=Biochem. J. |volume=317 ( Pt 3) |issue= |pages= 945-54 |year= 1996 |pmid= 8760387 |doi= }}
*{{cite journal | author=Betz A, Okamoto M, Benseler F, Brose N |title=Direct interaction of the rat unc-13 homologue Munc13-1 with the N terminus of syntaxin. |journal=J. Biol. Chem. |volume=272 |issue= 4 |pages= 2520-6 |year= 1997 |pmid= 8999968 |doi= }}
*{{cite journal | author=Araki S, Tamori Y, Kawanishi M, ''et al.'' |title=Inhibition of the binding of SNAP-23 to syntaxin 4 by Munc18c. |journal=Biochem. Biophys. Res. Commun. |volume=234 |issue= 1 |pages= 257-62 |year= 1997 |pmid= 9168999 |doi= 10.1006/bbrc.1997.6560 }}
*{{cite journal | author=Lane SR, Liu Y |title=Characterization of the palmitoylation domain of SNAP-25. |journal=J. Neurochem. |volume=69 |issue= 5 |pages= 1864-9 |year= 1997 |pmid= 9349529 |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=Okamoto M, Südhof TC |title=Mints, Munc18-interacting proteins in synaptic vesicle exocytosis. |journal=J. Biol. Chem. |volume=272 |issue= 50 |pages= 31459-64 |year= 1998 |pmid= 9395480 |doi= }}
*{{cite journal | author=Low SH, Roche PA, Anderson HA, ''et al.'' |title=Targeting of SNAP-23 and SNAP-25 in polarized epithelial cells. |journal=J. Biol. Chem. |volume=273 |issue= 6 |pages= 3422-30 |year= 1998 |pmid= 9452464 |doi= }}
*{{cite journal | author=Poirier MA, Hao JC, Malkus PN, ''et al.'' |title=Protease resistance of syntaxin.SNAP-25.VAMP complexes. Implications for assembly and structure. |journal=J. Biol. Chem. |volume=273 |issue= 18 |pages= 11370-7 |year= 1998 |pmid= 9556632 |doi= }}
*{{cite journal | author=Prekeris R, Klumperman J, Chen YA, Scheller RH |title=Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes. |journal=J. Cell Biol. |volume=143 |issue= 4 |pages= 957-71 |year= 1998 |pmid= 9817754 |doi= }}
*{{cite journal | author=Gonelle-Gispert C, Halban PA, Niemann H, ''et al.'' |title=SNAP-25a and -25b isoforms are both expressed in insulin-secreting cells and can function in insulin secretion. |journal=Biochem. J. |volume=339 ( Pt 1) |issue= |pages= 159-65 |year= 1999 |pmid= 10085240 |doi= }}
*{{cite journal | author=Ilardi JM, Mochida S, Sheng ZH |title=Snapin: a SNARE-associated protein implicated in synaptic transmission. |journal=Nat. Neurosci. |volume=2 |issue= 2 |pages= 119-24 |year= 1999 |pmid= 10195194 |doi= 10.1038/5673 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SQSTM1... {November 14, 2007 4:26:58 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:27:40 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_SQSTM1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1q02.
| PDB = {{PDB2|1q02}}
| Name = Sequestosome 1
| HGNCid = 11280
| Symbol = SQSTM1
| AltSymbols =; p60; A170; OSIL; PDB3; ZIP3; p62; p62B
| OMIM = 601530
| ECnumber =
| Homologene = 31202
| MGIid = 107931
| GeneAtlas_image1 = PBB_GE_SQSTM1_201471_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SQSTM1_213112_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0019901 |text = protein kinase binding}} {{GNF_GO|id=GO:0030971 |text = receptor tyrosine kinase binding}} {{GNF_GO|id=GO:0042169 |text = SH2 domain binding}} {{GNF_GO|id=GO:0043130 |text = ubiquitin binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006950 |text = response to stress}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0008104 |text = protein localization}} {{GNF_GO|id=GO:0016197 |text = endosome transport}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0043122 |text = regulation of I-kappaB kinase/NF-kappaB cascade}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8878
| Hs_Ensembl = ENSG00000161011
| Hs_RefseqProtein = NP_003891
| Hs_RefseqmRNA = NM_003900
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 179180503
| Hs_GenLoc_end = 179196199
| Hs_Uniprot = Q13501
| Mm_EntrezGene = 18412
| Mm_Ensembl = ENSMUSG00000015837
| Mm_RefseqmRNA = NM_011018
| Mm_RefseqProtein = NP_035148
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 50043578
| Mm_GenLoc_end = 50054213
| Mm_Uniprot = Q64337
}}
}}
'''Sequestosome 1''', also known as '''SQSTM1''', 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=Geetha T, Wooten MW |title=Structure and functional properties of the ubiquitin binding protein p62. |journal=FEBS Lett. |volume=512 |issue= 1-3 |pages= 19-24 |year= 2002 |pmid= 11852044 |doi= }}
*{{cite journal | author=Layfield R, Ciani B, Ralston SH, ''et al.'' |title=Structural and functional studies of mutations affecting the UBA domain of SQSTM1 (p62) which cause Paget's disease of bone. |journal=Biochem. Soc. Trans. |volume=32 |issue= Pt 5 |pages= 728-30 |year= 2005 |pmid= 15493999 |doi= 10.1042/BST0320728 }}
*{{cite journal | author=Michou L, Collet C, Laplanche JL, ''et al.'' |title=Genetics of Paget's disease of bone. |journal=Joint Bone Spine |volume=73 |issue= 3 |pages= 243-8 |year= 2006 |pmid= 16574459 |doi= 10.1016/j.jbspin.2005.05.009 }}
*{{cite journal | author=Devergne O, Hummel M, Koeppen H, ''et al.'' |title=A novel interleukin-12 p40-related protein induced by latent Epstein-Barr virus infection in B lymphocytes. |journal=J. Virol. |volume=70 |issue= 2 |pages= 1143-53 |year= 1996 |pmid= 8551575 |doi= }}
*{{cite journal | author=Park I, Chung J, Walsh CT, ''et al.'' |title=Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56lck and its regulation by phosphorylation of Ser-59 in the lck unique N-terminal region. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 26 |pages= 12338-42 |year= 1996 |pmid= 8618896 |doi= }}
*{{cite journal | author=Joung I, Strominger JL, Shin J |title=Molecular cloning of a phosphotyrosine-independent ligand of the p56lck SH2 domain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 12 |pages= 5991-5 |year= 1996 |pmid= 8650207 |doi= }}
*{{cite journal | author=Iyer N, Reagan MS, Wu KJ, ''et al.'' |title=Interactions involving the human RNA polymerase II transcription/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein. |journal=Biochemistry |volume=35 |issue= 7 |pages= 2157-67 |year= 1996 |pmid= 8652557 |doi= 10.1021/bi9524124 }}
*{{cite journal | author=Vadlamudi RK, Joung I, Strominger JL, Shin J |title=p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins. |journal=J. Biol. Chem. |volume=271 |issue= 34 |pages= 20235-7 |year= 1996 |pmid= 8702753 |doi= }}
*{{cite journal | author=Marcus SL, Winrow CJ, Capone JP, Rachubinski RA |title=A p56(lck) ligand serves as a coactivator of an orphan nuclear hormone receptor. |journal=J. Biol. Chem. |volume=271 |issue= 44 |pages= 27197-200 |year= 1996 |pmid= 8910285 |doi= }}
*{{cite journal | author=Jallal B, Mossie K, Vasiloudis G, ''et al.'' |title=The receptor-like protein-tyrosine phosphatase DEP-1 is constitutively associated with a 64-kDa protein serine/threonine kinase. |journal=J. Biol. Chem. |volume=272 |issue= 18 |pages= 12158-63 |year= 1997 |pmid= 9115287 |doi= }}
*{{cite journal | author=Sanchez P, De Carcer G, Sandoval IV, ''et al.'' |title=Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62. |journal=Mol. Cell. Biol. |volume=18 |issue= 5 |pages= 3069-80 |year= 1998 |pmid= 9566925 |doi= }}
*{{cite journal | author=Vadlamudi RK, Shin J |title=Genomic structure and promoter analysis of the p62 gene encoding a non-proteasomal multiubiquitin chain binding protein. |journal=FEBS Lett. |volume=435 |issue= 2-3 |pages= 138-42 |year= 1998 |pmid= 9762895 |doi= }}
*{{cite journal | author=Sanz L, Sanchez P, Lallena MJ, ''et al.'' |title=The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation. |journal=EMBO J. |volume=18 |issue= 11 |pages= 3044-53 |year= 1999 |pmid= 10356400 |doi= 10.1093/emboj/18.11.3044 }}
*{{cite journal | author=Stumptner C, Heid H, Fuchsbichler A, ''et al.'' |title=Analysis of intracytoplasmic hyaline bodies in a hepatocellular carcinoma. Demonstration of p62 as major constituent. |journal=Am. J. Pathol. |volume=154 |issue= 6 |pages= 1701-10 |year= 1999 |pmid= 10362795 |doi= }}
*{{cite journal | author=Sudo T, Maruyama M, Osada H |title=p62 functions as a p38 MAP kinase regulator. |journal=Biochem. Biophys. Res. Commun. |volume=269 |issue= 2 |pages= 521-5 |year= 2000 |pmid= 10708586 |doi= 10.1006/bbrc.2000.2333 }}
*{{cite journal | author=Sanz L, Diaz-Meco MT, Nakano H, Moscat J |title=The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL-1-TRAF6 pathway. |journal=EMBO J. |volume=19 |issue= 7 |pages= 1576-86 |year= 2000 |pmid= 10747026 |doi= 10.1093/emboj/19.7.1576 }}
*{{cite journal | author=Wooten MW, Seibenhener ML, Mamidipudi V, ''et al.'' |title=The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor. |journal=J. Biol. Chem. |volume=276 |issue= 11 |pages= 7709-12 |year= 2001 |pmid= 11244088 |doi= 10.1074/jbc.C000869200 }}
*{{cite journal | author=Kuusisto E, Salminen A, Alafuzoff I |title=Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies. |journal=Neuroreport |volume=12 |issue= 10 |pages= 2085-90 |year= 2001 |pmid= 11447312 |doi= }}
*{{cite journal | author=Laurin N, Brown JP, Lemainque A, ''et al.'' |title=Paget disease of bone: mapping of two loci at 5q35-qter and 5q31. |journal=Am. J. Hum. Genet. |volume=69 |issue= 3 |pages= 528-43 |year= 2001 |pmid= 11473345 |doi= }}
*{{cite journal | author=Chang S, Kim JH, Shin J |title=p62 forms a ternary complex with PKCzeta and PAR-4 and antagonizes PAR-4-induced PKCzeta inhibition. |journal=FEBS Lett. |volume=510 |issue= 1-2 |pages= 57-61 |year= 2002 |pmid= 11755531 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TNNT2... {November 14, 2007 4:24:43 PM PST}
- SEARCH REDIRECT: Control Box Found: TNNT2 {November 14, 2007 4:25:15 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 4:25:16 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 4:25:16 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 4:25:16 PM PST}
- UPDATED: Updated protein page: TNNT2 {November 14, 2007 4:25:23 PM PST}
- INFO: Beginning work on TUBB2A... {November 14, 2007 4:25:23 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:26:21 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 = PBB_Protein_TUBB2A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ffx.
| PDB = {{PDB2|1ffx}}, {{PDB2|1ia0}}, {{PDB2|1jff}}, {{PDB2|1sa0}}, {{PDB2|1sa1}}, {{PDB2|1tub}}, {{PDB2|1tvk}}, {{PDB2|1z2b}}, {{PDB2|2hxf}}, {{PDB2|2hxh}}
| Name = Tubulin, beta 2A
| HGNCid = 12412
| Symbol = TUBB2A
| AltSymbols =; TUBB; TUBB2; dJ40E16.7
| OMIM =
| ECnumber =
| Homologene = 68156
| MGIid = 107861
| GeneAtlas_image1 = PBB_GE_TUBB2A_202154_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_TUBB2A_208977_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_TUBB2A_204141_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005874 |text = microtubule}} {{GNF_GO|id=GO:0043234 |text = protein complex}}
| Process = {{GNF_GO|id=GO:0007018 |text = microtubule-based movement}} {{GNF_GO|id=GO:0051258 |text = protein polymerization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7280
| Hs_Ensembl = ENSG00000137267
| Hs_RefseqProtein = NP_001060
| Hs_RefseqmRNA = NM_001069
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 3098918
| Hs_GenLoc_end = 3102808
| Hs_Uniprot = Q13885
| Mm_EntrezGene = 22151
| Mm_Ensembl = ENSMUSG00000058672
| Mm_RefseqmRNA = NM_009450
| Mm_RefseqProtein = NP_033476
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 34081743
| Mm_GenLoc_end = 34085453
| Mm_Uniprot = Q62363
}}
}}
'''Tubulin, beta 2A''', also known as '''TUBB2A''', 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=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=Horisberger MA |title=Interferon-induced human protein MxA is a GTPase which binds transiently to cellular proteins. |journal=J. Virol. |volume=66 |issue= 8 |pages= 4705-9 |year= 1992 |pmid= 1629950 |doi= }}
*{{cite journal | author=Wang D, Villasante A, Lewis SA, Cowan NJ |title=The mammalian beta-tubulin repertoire: hematopoietic expression of a novel, heterologous beta-tubulin isotype. |journal=J. Cell Biol. |volume=103 |issue= 5 |pages= 1903-10 |year= 1987 |pmid= 3782288 |doi= }}
*{{cite journal | author=Lee MG, Lewis SA, Wilde CD, Cowan NJ |title=Evolutionary history of a multigene family: an expressed human beta-tubulin gene and three processed pseudogenes. |journal=Cell |volume=33 |issue= 2 |pages= 477-87 |year= 1983 |pmid= 6688039 |doi= }}
*{{cite journal | author=Takahashi M, Tomizawa K, Sato K, ''et al.'' |title=A novel tau-tubulin kinase from bovine brain. |journal=FEBS Lett. |volume=372 |issue= 1 |pages= 59-64 |year= 1995 |pmid= 7556643 |doi= }}
*{{cite journal | author=Yamaguchi N, Fukuda MN |title=Golgi retention mechanism of beta-1,4-galactosyltransferase. Membrane-spanning domain-dependent homodimerization and association with alpha- and beta-tubulins. |journal=J. Biol. Chem. |volume=270 |issue= 20 |pages= 12170-6 |year= 1995 |pmid= 7744867 |doi= }}
*{{cite journal | author=Waterman-Storer CM, Karki S, Holzbaur EL |title=The p150Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 5 |pages= 1634-8 |year= 1995 |pmid= 7878030 |doi= }}
*{{cite journal | author=Carr D, Knull H |title=Aldolase-tubulin interactions: removal of tubulin C-terminals impairs interactions. |journal=Biochem. Biophys. Res. Commun. |volume=195 |issue= 1 |pages= 289-93 |year= 1993 |pmid= 8103323 |doi= 10.1006/bbrc.1993.2043 }}
*{{cite journal | author=Volz A, Weiss E, Trowsdale J, Ziegler A |title=Presence of an expressed beta-tubulin gene (TUBB) in the HLA class I region may provide the genetic basis for HLA-linked microtubule dysfunction. |journal=Hum. Genet. |volume=93 |issue= 1 |pages= 42-6 |year= 1994 |pmid= 8270253 |doi= }}
*{{cite journal | author=Paschal BM, Holzbaur EL, Pfister KK, ''et al.'' |title=Characterization of a 50-kDa polypeptide in cytoplasmic dynein preparations reveals a complex with p150GLUED and a novel actin. |journal=J. Biol. Chem. |volume=268 |issue= 20 |pages= 15318-23 |year= 1993 |pmid= 8325901 |doi= }}
*{{cite journal | author=Linhartová I, Dráberová E, Viklický V, Dráber P |title=Distribution of non-class-III beta-tubulin isoforms in neuronal and non-neuronal cells. |journal=FEBS Lett. |volume=320 |issue= 1 |pages= 79-82 |year= 1993 |pmid= 8462682 |doi= }}
*{{cite journal | author=Huby RD, Carlile GW, Ley SC |title=Interactions between the protein-tyrosine kinase ZAP-70, the proto-oncoprotein Vav, and tubulin in Jurkat T cells. |journal=J. Biol. Chem. |volume=270 |issue= 51 |pages= 30241-4 |year= 1996 |pmid= 8530437 |doi= }}
*{{cite journal | author=Bosc C, Cronk JD, Pirollet F, ''et al.'' |title=Cloning, expression, and properties of the microtubule-stabilizing protein STOP. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 5 |pages= 2125-30 |year= 1996 |pmid= 8700896 |doi= }}
*{{cite journal | author=Tian G, Huang Y, Rommelaere H, ''et al.'' |title=Pathway leading to correctly folded beta-tubulin. |journal=Cell |volume=86 |issue= 2 |pages= 287-96 |year= 1996 |pmid= 8706133 |doi= }}
*{{cite journal | author=Tokito MK, Howland DS, Lee VM, Holzbaur EL |title=Functionally distinct isoforms of dynactin are expressed in human neurons. |journal=Mol. Biol. Cell |volume=7 |issue= 8 |pages= 1167-80 |year= 1997 |pmid= 8856662 |doi= }}
*{{cite journal | author=Kinnunen T, Kaksonen M, Saarinen J, ''et al.'' |title=Cortactin-Src kinase signaling pathway is involved in N-syndecan-dependent neurite outgrowth. |journal=J. Biol. Chem. |volume=273 |issue= 17 |pages= 10702-8 |year= 1998 |pmid= 9553134 |doi= }}
*{{cite journal | author=Niethammer M, Valtschanoff JG, Kapoor TM, ''et al.'' |title=CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90. |journal=Neuron |volume=20 |issue= 4 |pages= 693-707 |year= 1998 |pmid= 9581762 |doi= }}
*{{cite journal | author=Rasmussen RK, Ji H, Eddes JS, ''et al.'' |title=Two-dimensional electrophoretic analysis of mixed lineage kinase 2 N-terminal domain binding proteins. |journal=Electrophoresis |volume=19 |issue= 5 |pages= 809-17 |year= 1998 |pmid= 9629920 |doi= 10.1002/elps.1150190535 }}
*{{cite journal | author=Ciruela F, Robbins MJ, Willis AC, McIlhinney RA |title=Interactions of the C terminus of metabotropic glutamate receptor type 1alpha with rat brain proteins: evidence for a direct interaction with tubulin. |journal=J. Neurochem. |volume=72 |issue= 1 |pages= 346-54 |year= 1999 |pmid= 9886087 |doi= }}
*{{cite journal | author=Chau MF, Radeke MJ, de Inés C, ''et al.'' |title=The microtubule-associated protein tau cross-links to two distinct sites on each alpha and beta tubulin monomer via separate domains. |journal=Biochemistry |volume=37 |issue= 51 |pages= 17692-703 |year= 1999 |pmid= 9922135 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on VEGFC... {November 14, 2007 4:26:21 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:26:58 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Vascular endothelial growth factor C
| HGNCid = 12682
| Symbol = VEGFC
| AltSymbols =; Flt4-L; VRP
| OMIM = 601528
| ECnumber =
| Homologene = 3962
| MGIid = 109124
| GeneAtlas_image1 = PBB_GE_VEGFC_209946_at_tn.png
| Function = {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0006929 |text = substrate-bound cell migration}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0016331 |text = morphogenesis of embryonic epithelium}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7424
| Hs_Ensembl = ENSG00000150630
| Hs_RefseqProtein = NP_005420
| Hs_RefseqmRNA = NM_005429
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 177841685
| Hs_GenLoc_end = 177950889
| Hs_Uniprot = P49767
| Mm_EntrezGene = 22341
| Mm_Ensembl = ENSMUSG00000031520
| Mm_RefseqmRNA = NM_009506
| Mm_RefseqProtein = NP_033532
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 55576304
| Mm_GenLoc_end = 55685794
| Mm_Uniprot = P97953
}}
}}
'''Vascular endothelial growth factor C''', also known as '''VEGFC''', 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 platelet-derived growth factor/vascular endothelial growth factor (PDGF/VEGF) family, is active in angiogenesis and endothelial cell growth, and can also affect the permeability of blood vessels. This secreted protein undergoes a complex proteolytic maturation, generating multiple processed forms which bind and activate VEGFR-3 receptors. Only the fully processed form can bind and activate VEGFR-2 receptors. This protein is structurally and functionally similar to vascular endothelial growth factor D.<ref>{{cite web | title = Entrez Gene: VEGFC vascular endothelial growth factor C| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7424| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Orpana A, Salven P |title=Angiogenic and lymphangiogenic molecules in hematological malignancies. |journal=Leuk. Lymphoma |volume=43 |issue= 2 |pages= 219-24 |year= 2003 |pmid= 11999550 |doi= }}
*{{cite journal | author=Joukov V, Pajusola K, Kaipainen A, ''et al.'' |title=A novel vascular endothelial growth factor, VEGF-C, is a ligand for the Flt4 (VEGFR-3) and KDR (VEGFR-2) receptor tyrosine kinases. |journal=EMBO J. |volume=15 |issue= 7 |pages= 1751 |year= 1996 |pmid= 8612600 |doi= }}
*{{cite journal | author=Joukov V, Pajusola K, Kaipainen A, ''et al.'' |title=A novel vascular endothelial growth factor, VEGF-C, is a ligand for the Flt4 (VEGFR-3) and KDR (VEGFR-2) receptor tyrosine kinases. |journal=EMBO J. |volume=15 |issue= 2 |pages= 290-98 |year= 1996 |pmid= 8617204 |doi= }}
*{{cite journal | author=Paavonen K, Horelli-Kuitunen N, Chilov D, ''et al.'' |title=Novel human vascular endothelial growth factor genes VEGF-B and VEGF-C localize to chromosomes 11q13 and 4q34, respectively. |journal=Circulation |volume=93 |issue= 6 |pages= 1079-82 |year= 1996 |pmid= 8653826 |doi= }}
*{{cite journal | author=Lee J, Gray A, Yuan J, ''et al.'' |title=Vascular endothelial growth factor-related protein: a ligand and specific activator of the tyrosine kinase receptor Flt4. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 5 |pages= 1988-92 |year= 1996 |pmid= 8700872 |doi= }}
*{{cite journal | author=Joukov V, Sorsa T, Kumar V, ''et al.'' |title=Proteolytic processing regulates receptor specificity and activity of VEGF-C. |journal=EMBO J. |volume=16 |issue= 13 |pages= 3898-911 |year= 1997 |pmid= 9233800 |doi= 10.1093/emboj/16.13.3898 }}
*{{cite journal | author=Fitz LJ, Morris JC, Towler P, ''et al.'' |title=Characterization of murine Flt4 ligand/VEGF-C. |journal=Oncogene |volume=15 |issue= 5 |pages= 613-8 |year= 1997 |pmid= 9247316 |doi= 10.1038/sj.onc.1201191 }}
*{{cite journal | author=Dunk C, Ahmed A |title=Expression of VEGF-C and activation of its receptors VEGFR-2 and VEGFR-3 in trophoblast. |journal=Histol. Histopathol. |volume=16 |issue= 2 |pages= 359-75 |year= 2001 |pmid= 11332691 |doi= }}
*{{cite journal | author=Dias S, Choy M, Alitalo K, Rafii S |title=Vascular endothelial growth factor (VEGF)-C signaling through FLT-4 (VEGFR-3) mediates leukemic cell proliferation, survival, and resistance to chemotherapy. |journal=Blood |volume=99 |issue= 6 |pages= 2179-84 |year= 2002 |pmid= 11877295 |doi= }}
*{{cite journal | author=Ueda M, Terai Y, Yamashita Y, ''et al.'' |title=Correlation between vascular endothelial growth factor-C expression and invasion phenotype in cervical carcinomas. |journal=Int. J. Cancer |volume=98 |issue= 3 |pages= 335-43 |year= 2002 |pmid= 11920583 |doi= }}
*{{cite journal | author=Witte D, Thomas A, Ali N, ''et al.'' |title=Expression of the vascular endothelial growth factor receptor-3 (VEGFR-3) and its ligand VEGF-C in human colorectal adenocarcinoma. |journal=Anticancer Res. |volume=22 |issue= 3 |pages= 1463-6 |year= 2002 |pmid= 12168824 |doi= }}
*{{cite journal | author=Schoppmann SF, Birner P, Stöckl J, ''et al.'' |title=Tumor-associated macrophages express lymphatic endothelial growth factors and are related to peritumoral lymphangiogenesis. |journal=Am. J. Pathol. |volume=161 |issue= 3 |pages= 947-56 |year= 2002 |pmid= 12213723 |doi= }}
*{{cite journal | author=Shin HY, Smith ML, Toy KJ, ''et al.'' |title=VEGF-C mediates cyclic pressure-induced endothelial cell proliferation. |journal=Physiol. Genomics |volume=11 |issue= 3 |pages= 245-51 |year= 2002 |pmid= 12388793 |doi= 10.1152/physiolgenomics.00068.2002 }}
*{{cite journal | author=Yu DH, Wen YM, Sun JD, ''et al.'' |title=[Relationship among expression of vascular endothelial growth factor-C(VEGF-C), angiogenesis, lymphangiogenesis, and lymphatic metastasis in oral cancer] |journal=Ai Zheng |volume=21 |issue= 3 |pages= 319-22 |year= 2003 |pmid= 12452004 |doi= }}
*{{cite journal | author=Nakashima T, Kondoh S, Kitoh H, ''et al.'' |title=Vascular endothelial growth factor-C expression in human gallbladder cancer and its relationship to lymph node metastasis. |journal=Int. J. Mol. Med. |volume=11 |issue= 1 |pages= 33-9 |year= 2003 |pmid= 12469214 |doi= }}
*{{cite journal | author=Tsai PW, Shiah SG, Lin MT, ''et al.'' |title=Up-regulation of vascular endothelial growth factor C in breast cancer cells by heregulin-beta 1. A critical role of p38/nuclear factor-kappa B signaling pathway. |journal=J. Biol. Chem. |volume=278 |issue= 8 |pages= 5750-9 |year= 2003 |pmid= 12471041 |doi= 10.1074/jbc.M204863200 }}
*{{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=Masood R, Kundra A, Zhu S, ''et al.'' |title=Malignant mesothelioma growth inhibition by agents that target the VEGF and VEGF-C autocrine loops. |journal=Int. J. Cancer |volume=104 |issue= 5 |pages= 603-10 |year= 2003 |pmid= 12594815 |doi= 10.1002/ijc.10996 }}
*{{cite journal | author=Ohno M, Nakamura T, Kunimoto Y, ''et al.'' |title=Lymphagenesis correlates with expression of vascular endothelial growth factor-C in colorectal cancer. |journal=Oncol. Rep. |volume=10 |issue= 4 |pages= 939-43 |year= 2004 |pmid= 12792749 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on YBX1... {November 14, 2007 4:18:26 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:19:18 PM PST}
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{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_YBX1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1h95.
| PDB = {{PDB2|1h95}}
| Name = Y box binding protein 1
| HGNCid = 8014
| Symbol = YBX1
| AltSymbols =; BP-8; CSDA2; CSDB; DBPB; MDR-NF1; MGC104858; MGC110976; MGC117250; NSEP-1; NSEP1; YB-1; YB1
| OMIM = 154030
| ECnumber =
| Homologene = 88707
| MGIid =
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003690 |text = double-stranded DNA binding}} {{GNF_GO|id=GO:0003697 |text = single-stranded DNA binding}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016564 |text = transcription repressor activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006397 |text = mRNA processing}} {{GNF_GO|id=GO:0008380 |text = RNA splicing}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4904
| Hs_Ensembl =
| Hs_RefseqProtein = NP_004550
| Hs_RefseqmRNA = NM_004559
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Y box binding protein 1''', also known as '''YBX1''', 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=Kolluri R, Torrey TA, Kinniburgh AJ |title=A CT promoter element binding protein: definition of a double-strand and a novel single-strand DNA binding motif. |journal=Nucleic Acids Res. |volume=20 |issue= 1 |pages= 111-6 |year= 1992 |pmid= 1738588 |doi= }}
*{{cite journal | author=Kolluri R, Kinniburgh AJ |title=Full length cDNA sequence encoding a nuclease-sensitive element DNA binding protein. |journal=Nucleic Acids Res. |volume=19 |issue= 17 |pages= 4771 |year= 1991 |pmid= 1891370 |doi= }}
*{{cite journal | author=Sakura H, Maekawa T, Imamoto F, ''et al.'' |title=Two human genes isolated by a novel method encode DNA-binding proteins containing a common region of homology. |journal=Gene |volume=73 |issue= 2 |pages= 499-507 |year= 1989 |pmid= 2977358 |doi= }}
*{{cite journal | author=Didier DK, Schiffenbauer J, Woulfe SL, ''et al.'' |title=Characterization of the cDNA encoding a protein binding to the major histocompatibility complex class II Y box. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 19 |pages= 7322-6 |year= 1988 |pmid= 3174636 |doi= }}
*{{cite journal | author=Kudo S, Mattei MG, Fukuda M |title=Characterization of the gene for dbpA, a family member of the nucleic-acid-binding proteins containing a cold-shock domain. |journal=Eur. J. Biochem. |volume=231 |issue= 1 |pages= 72-82 |year= 1995 |pmid= 7628487 |doi= }}
*{{cite journal | author=Lloberas J, Maki RA, Celada A |title=Repression of major histocompatibility complex I-A beta gene expression by dbpA and dbpB (mYB-1) proteins. |journal=Mol. Cell. Biol. |volume=15 |issue= 9 |pages= 5092-9 |year= 1995 |pmid= 7651426 |doi= }}
*{{cite journal | author=Chen NN, Chang CF, Gallia GL, ''et al.'' |title=Cooperative action of cellular proteins YB-1 and Pur alpha with the tumor antigen of the human JC polyomavirus determines their interaction with the viral lytic control element. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 4 |pages= 1087-91 |year= 1995 |pmid= 7862639 |doi= }}
*{{cite journal | author=Horwitz EM, Maloney KA, Ley TJ |title=A human protein containing a "cold shock" domain binds specifically to H-DNA upstream from the human gamma-globin genes. |journal=J. Biol. Chem. |volume=269 |issue= 19 |pages= 14130-9 |year= 1994 |pmid= 8188694 |doi= }}
*{{cite journal | author=Kashanchi F, Duvall JF, Dittmer J, ''et al.'' |title=Involvement of transcription factor YB-1 in human T-cell lymphotropic virus type I basal gene expression. |journal=J. Virol. |volume=68 |issue= 1 |pages= 561-5 |year= 1994 |pmid= 8254772 |doi= }}
*{{cite journal | author=Makino Y, Ohga T, Toh S, ''et al.'' |title=Structural and functional analysis of the human Y-box binding protein (YB-1) gene promoter. |journal=Nucleic Acids Res. |volume=24 |issue= 10 |pages= 1873-8 |year= 1996 |pmid= 8657568 |doi= }}
*{{cite journal | author=Funke B, Zuleger B, Benavente R, ''et al.'' |title=The mouse poly(C)-binding protein exists in multiple isoforms and interacts with several RNA-binding proteins. |journal=Nucleic Acids Res. |volume=24 |issue= 19 |pages= 3821-8 |year= 1996 |pmid= 8871564 |doi= }}
*{{cite journal | author=Koike K, Uchiumi T, Ohga T, ''et al.'' |title=Nuclear translocation of the Y-box binding protein by ultraviolet irradiation. |journal=FEBS Lett. |volume=417 |issue= 3 |pages= 390-4 |year= 1998 |pmid= 9409758 |doi= }}
*{{cite journal | author=Toh S, Nakamura T, Ohga T, ''et al.'' |title=Genomic organization of the human Y-box protein (YB-1) gene. |journal=Gene |volume=206 |issue= 1 |pages= 93-7 |year= 1998 |pmid= 9461420 |doi= }}
*{{cite journal | author=Sawaya BE, Khalili K, Amini S |title=Transcription of the human immunodeficiency virus type 1 (HIV-1) promoter in central nervous system cells: effect of YB-1 on expression of the HIV-1 long terminal repeat. |journal=J. Gen. Virol. |volume=79 ( Pt 2) |issue= |pages= 239-46 |year= 1998 |pmid= 9472608 |doi= }}
*{{cite journal | author=Mertens PR, Alfonso-Jaume MA, Steinmann K, Lovett DH |title=A synergistic interaction of transcription factors AP2 and YB-1 regulates gelatinase A enhancer-dependent transcription. |journal=J. Biol. Chem. |volume=273 |issue= 49 |pages= 32957-65 |year= 1999 |pmid= 9830047 |doi= }}
*{{cite journal | author=Ise T, Nagatani G, Imamura T, ''et al.'' |title=Transcription factor Y-box binding protein 1 binds preferentially to cisplatin-modified DNA and interacts with proliferating cell nuclear antigen. |journal=Cancer Res. |volume=59 |issue= 2 |pages= 342-6 |year= 1999 |pmid= 9927044 |doi= }}
*{{cite journal | author=Safak M, Gallia GL, Khalili K |title=Reciprocal interaction between two cellular proteins, Puralpha and YB-1, modulates transcriptional activity of JCVCY in glial cells. |journal=Mol. Cell. Biol. |volume=19 |issue= 4 |pages= 2712-23 |year= 1999 |pmid= 10082537 |doi= }}
*{{cite journal | author=Kelm RJ, Cogan JG, Elder PK, ''et al.'' |title=Molecular interactions between single-stranded DNA-binding proteins associated with an essential MCAT element in the mouse smooth muscle alpha-actin promoter. |journal=J. Biol. Chem. |volume=274 |issue= 20 |pages= 14238-45 |year= 1999 |pmid= 10318844 |doi= }}
*{{cite journal | author=Safak M, Gallia GL, Ansari SA, Khalili K |title=Physical and functional interaction between the Y-box binding protein YB-1 and human polyomavirus JC virus large T antigen. |journal=J. Virol. |volume=73 |issue= 12 |pages= 10146-57 |year= 1999 |pmid= 10559330 |doi= }}
*{{cite journal | author=Ansari SA, Safak M, Gallia GL, ''et al.'' |title=Interaction of YB-1 with human immunodeficiency virus type 1 Tat and TAR RNA modulates viral promoter activity. |journal=J. Gen. Virol. |volume=80 ( Pt 10) |issue= |pages= 2629-38 |year= 1999 |pmid= 10573156 |doi= }}
}}
{{refend}}
{{protein-stub}}
end log.
