Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 01:38, 15 November 2007 (UTC)[edit]
Proteins without matches (6)[edit]
Proteins with a High Potential Match (11)[edit]
Redirected Proteins (8)[edit]
Manual Inspection (Page not found) (17)[edit]
Updated (8)[edit]
Protein Status Grid - Date: 01:38, 15 November 2007 (UTC)[edit]
Vebose Log - Date: 01:38, 15 November 2007 (UTC)[edit]
- INFO: Beginning work on ABCC8... {November 14, 2007 5:25:50 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:27:04 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 =
| image_source =
| PDB =
| Name = ATP-binding cassette, sub-family C (CFTR/MRP), member 8
| HGNCid = 59
| Symbol = ABCC8
| AltSymbols =; PHHI; MRP8; ABC36; HHF1; HI; HRINS; SUR; SUR1; TNDM2
| OMIM = 600509
| ECnumber =
| Homologene = 68048
| MGIid = 1352629
| GeneAtlas_image1 = PBB_GE_ABCC8_210246_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008281 |text = sulfonylurea receptor activity}} {{GNF_GO|id=GO:0015079 |text = potassium ion transmembrane transporter activity}} {{GNF_GO|id=GO:0016887 |text = ATPase activity}} {{GNF_GO|id=GO:0042626 |text = ATPase activity, coupled to transmembrane movement of substances}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006813 |text = potassium ion transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6833
| Hs_Ensembl = ENSG00000006071
| Hs_RefseqProtein = NP_000343
| Hs_RefseqmRNA = NM_000352
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 17371009
| Hs_GenLoc_end = 17455025
| Hs_Uniprot = Q09428
| Mm_EntrezGene = 20927
| Mm_Ensembl = ENSMUSG00000040136
| Mm_RefseqmRNA = NM_011510
| Mm_RefseqProtein = NP_035640
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 45972565
| Mm_GenLoc_end = 46048075
| Mm_Uniprot =
}}
}}
'''ATP-binding cassette, sub-family C (CFTR/MRP), member 8''', also known as '''ABCC8''', 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 superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the MRP subfamily which is involved in multi-drug resistance. This protein functions as a modulator of ATP-sensitive potassium channels and insulin release. Mutations and deficiencies in this protein have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type II, an autosomal dominant disease of defective insulin secretion. Alternative splicing of this gene has been observed; however, the transcript variants have not been fully described.<ref>{{cite web | title = Entrez Gene: ABCC8 ATP-binding cassette, sub-family C (CFTR/MRP), member 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6833| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Aguilar-Bryan L, Bryan J |title=Molecular biology of adenosine triphosphate-sensitive potassium channels. |journal=Endocr. Rev. |volume=20 |issue= 2 |pages= 101-35 |year= 1999 |pmid= 10204114 |doi= }}
*{{cite journal | author=Meissner T, Beinbrech B, Mayatepek E |title=Congenital hyperinsulinism: molecular basis of a heterogeneous disease. |journal=Hum. Mutat. |volume=13 |issue= 5 |pages= 351-61 |year= 1999 |pmid= 10338089 |doi= 10.1002/(SICI)1098-1004(1999)13:5<351::AID-HUMU3>3.0.CO;2-R }}
*{{cite journal | author=Gloyn AL, Siddiqui J, Ellard S |title=Mutations in the genes encoding the pancreatic beta-cell KATP channel subunits Kir6.2 (KCNJ11) and SUR1 (ABCC8) in diabetes mellitus and hyperinsulinism. |journal=Hum. Mutat. |volume=27 |issue= 3 |pages= 220-31 |year= 2006 |pmid= 16416420 |doi= 10.1002/humu.20292 }}
*{{cite journal | author=Bryan J, Muñoz A, Zhang X, ''et al.'' |title=ABCC8 and ABCC9: ABC transporters that regulate K+ channels. |journal=Pflugers Arch. |volume=453 |issue= 5 |pages= 703-18 |year= 2007 |pmid= 16897043 |doi= 10.1007/s00424-006-0116-z }}
*{{cite journal | author=Inagaki N, Gonoi T, Clement JP, ''et al.'' |title=Reconstitution of IKATP: an inward rectifier subunit plus the sulfonylurea receptor. |journal=Science |volume=270 |issue= 5239 |pages= 1166-70 |year= 1996 |pmid= 7502040 |doi= }}
*{{cite journal | author=Aguilar-Bryan L, Nichols CG, Wechsler SW, ''et al.'' |title=Cloning of the beta cell high-affinity sulfonylurea receptor: a regulator of insulin secretion. |journal=Science |volume=268 |issue= 5209 |pages= 423-6 |year= 1995 |pmid= 7716547 |doi= }}
*{{cite journal | author=Thomas PM, Cote GJ, Wohllk N, ''et al.'' |title=Mutations in the sulfonylurea receptor gene in familial persistent hyperinsulinemic hypoglycemia of infancy. |journal=Science |volume=268 |issue= 5209 |pages= 426-9 |year= 1995 |pmid= 7716548 |doi= }}
*{{cite journal | author=Thomas PM, Cote GJ, Hallman DM, Mathew PM |title=Homozygosity mapping, to chromosome 11p, of the gene for familial persistent hyperinsulinemic hypoglycemia of infancy. |journal=Am. J. Hum. Genet. |volume=56 |issue= 2 |pages= 416-21 |year= 1995 |pmid= 7847376 |doi= }}
*{{cite journal | author=Glaser B, Chiu KC, Anker R, ''et al.'' |title=Familial hyperinsulinism maps to chromosome 11p14-15.1, 30 cM centromeric to the insulin gene. |journal=Nat. Genet. |volume=7 |issue= 2 |pages= 185-8 |year= 1994 |pmid= 7920639 |doi= 10.1038/ng0694-185 }}
*{{cite journal | author=Inagaki N, Gonoi T, Clement JP, ''et al.'' |title=A family of sulfonylurea receptors determines the pharmacological properties of ATP-sensitive K+ channels. |journal=Neuron |volume=16 |issue= 5 |pages= 1011-7 |year= 1996 |pmid= 8630239 |doi= }}
*{{cite journal | author=Inoue H, Ferrer J, Welling CM, ''et al.'' |title=Sequence variants in the sulfonylurea receptor (SUR) gene are associated with NIDDM in Caucasians. |journal=Diabetes |volume=45 |issue= 6 |pages= 825-31 |year= 1996 |pmid= 8635661 |doi= }}
*{{cite journal | author=Nichols CG, Shyng SL, Nestorowicz A, ''et al.'' |title=Adenosine diphosphate as an intracellular regulator of insulin secretion. |journal=Science |volume=272 |issue= 5269 |pages= 1785-7 |year= 1996 |pmid= 8650576 |doi= }}
*{{cite journal | author=Thomas PM, Wohllk N, Huang E, ''et al.'' |title=Inactivation of the first nucleotide-binding fold of the sulfonylurea receptor, and familial persistent hyperinsulinemic hypoglycemia of infancy. |journal=Am. J. Hum. Genet. |volume=59 |issue= 3 |pages= 510-8 |year= 1996 |pmid= 8751851 |doi= }}
*{{cite journal | author=Nestorowicz A, Wilson BA, Schoor KP, ''et al.'' |title=Mutations in the sulonylurea receptor gene are associated with familial hyperinsulinism in Ashkenazi Jews. |journal=Hum. Mol. Genet. |volume=5 |issue= 11 |pages= 1813-22 |year= 1997 |pmid= 8923011 |doi= }}
*{{cite journal | author=Dunne MJ, Kane C, Shepherd RM, ''et al.'' |title=Familial persistent hyperinsulinemic hypoglycemia of infancy and mutations in the sulfonylurea receptor. |journal=N. Engl. J. Med. |volume=336 |issue= 10 |pages= 703-6 |year= 1997 |pmid= 9041101 |doi= }}
*{{cite journal | author=Gribble FM, Tucker SJ, Ashcroft FM |title=The essential role of the Walker A motifs of SUR1 in K-ATP channel activation by Mg-ADP and diazoxide. |journal=EMBO J. |volume=16 |issue= 6 |pages= 1145-52 |year= 1997 |pmid= 9135131 |doi= 10.1093/emboj/16.6.1145 }}
*{{cite journal | author=Ohta Y, Tanizawa Y, Inoue H, ''et al.'' |title=Identification and functional analysis of sulfonylurea receptor 1 variants in Japanese patients with NIDDM. |journal=Diabetes |volume=47 |issue= 3 |pages= 476-81 |year= 1998 |pmid= 9519757 |doi= }}
*{{cite journal | author=Hansen T, Echwald SM, Hansen L, ''et al.'' |title=Decreased tolbutamide-stimulated insulin secretion in healthy subjects with sequence variants in the high-affinity sulfonylurea receptor gene. |journal=Diabetes |volume=47 |issue= 4 |pages= 598-605 |year= 1998 |pmid= 9568693 |doi= }}
*{{cite journal | author=Nestorowicz A, Glaser B, Wilson BA, ''et al.'' |title=Genetic heterogeneity in familial hyperinsulinism. |journal=Hum. Mol. Genet. |volume=7 |issue= 7 |pages= 1119-28 |year= 1999 |pmid= 9618169 |doi= }}
*{{cite journal | author=Shyng SL, Ferrigni T, Shepard JB, ''et al.'' |title=Functional analyses of novel mutations in the sulfonylurea receptor 1 associated with persistent hyperinsulinemic hypoglycemia of infancy. |journal=Diabetes |volume=47 |issue= 7 |pages= 1145-51 |year= 1998 |pmid= 9648840 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on AQP1... {November 14, 2007 5:11:57 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:12:35 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_AQP1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1fqy.
| PDB = {{PDB2|1fqy}}, {{PDB2|1h6i}}, {{PDB2|1ih5}}, {{PDB2|1j4n}}
| Name = Aquaporin 1 (Colton blood group)
| HGNCid = 633
| Symbol = AQP1
| AltSymbols =; AQP-CHIP; CHIP28; CO; MGC26324
| OMIM = 107776
| ECnumber =
| Homologene = 68051
| MGIid = 103201
| GeneAtlas_image1 = PBB_GE_AQP1_209047_at_tn.png
| GeneAtlas_image2 = PBB_GE_AQP1_207542_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005372 |text = water transporter activity}} {{GNF_GO|id=GO:0015288 |text = porin activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0019867 |text = outer membrane}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006833 |text = water transport}} {{GNF_GO|id=GO:0007588 |text = excretion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 358
| Hs_Ensembl = ENSG00000106125
| Hs_RefseqProtein = NP_932766
| Hs_RefseqmRNA = NM_198098
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 30917993
| Hs_GenLoc_end = 30931656
| Hs_Uniprot = P29972
| Mm_EntrezGene = 11826
| Mm_Ensembl = ENSMUSG00000004655
| Mm_RefseqmRNA = NM_007472
| Mm_RefseqProtein = NP_031498
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 55266010
| Mm_GenLoc_end = 55278133
| Mm_Uniprot = Q3TLW5
}}
}}
'''Aquaporin 1 (Colton blood group)''', also known as '''AQP1''', 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 = Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). This gene encodes an aquaporin which functions as a molecular water channel protein. It is a homotetramer with 6 bilayer spanning domains and N-glycosylation sites. The protein physically resembles channel proteins and is abundant in erythrocytes and renal tubes. The gene encoding this aquaporin is a possible candidate for disorders involving imbalance in ocular fluid movement.<ref>{{cite web | title = Entrez Gene: AQP1 aquaporin 1 (Colton blood group)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=358| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Knepper MA |title=The aquaporin family of molecular water channels. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 14 |pages= 6255-8 |year= 1994 |pmid= 7517546 |doi= }}
*{{cite journal | author=Borgnia M, Nielsen S, Engel A, Agre P |title=Cellular and molecular biology of the aquaporin water channels. |journal=Annu. Rev. Biochem. |volume=68 |issue= |pages= 425-58 |year= 2000 |pmid= 10872456 |doi= 10.1146/annurev.biochem.68.1.425 }}
*{{cite journal | author=Horster M |title=Embryonic epithelial membrane transporters. |journal=Am. J. Physiol. Renal Physiol. |volume=279 |issue= 6 |pages= F982-96 |year= 2001 |pmid= 11097616 |doi= }}
*{{cite journal | author=Yool AJ, Weinstein AM |title=New roles for old holes: ion channel function in aquaporin-1. |journal=News Physiol. Sci. |volume=17 |issue= |pages= 68-72 |year= 2002 |pmid= 11909995 |doi= }}
*{{cite journal | author=Mitra AK, Ren G, Reddy VS, ''et al.'' |title=The architecture of a water-selective pore in the lipid bilayer visualized by electron crystallography in vitreous ice. |journal=Novartis Found. Symp. |volume=245 |issue= |pages= 33-46; discussion 46-50; 165-8 |year= 2002 |pmid= 12027013 |doi= }}
*{{cite journal | author=Ripoche P, Goossens D, Devuyst O, ''et al.'' |title=Role of RhAG and AQP1 in NH3 and CO2 gas transport in red cell ghosts: a stopped-flow analysis. |journal=Transfusion clinique et biologique : journal de la Société française de transfusion sanguine |volume=13 |issue= 1-2 |pages= 117-22 |year= 2006 |pmid= 16574458 |doi= 10.1016/j.tracli.2006.03.004 }}
*{{cite journal | author=Preston GM, Carroll TP, Guggino WB, Agre P |title=Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. |journal=Science |volume=256 |issue= 5055 |pages= 385-7 |year= 1992 |pmid= 1373524 |doi= }}
*{{cite journal | author=Preston GM, Agre P |title=Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 24 |pages= 11110-4 |year= 1992 |pmid= 1722319 |doi= }}
*{{cite journal | author=Smith BL, Agre P |title=Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins. |journal=J. Biol. Chem. |volume=266 |issue= 10 |pages= 6407-15 |year= 1991 |pmid= 2007592 |doi= }}
*{{cite journal | author=Denker BM, Smith BL, Kuhajda FP, Agre P |title=Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules. |journal=J. Biol. Chem. |volume=263 |issue= 30 |pages= 15634-42 |year= 1988 |pmid= 3049610 |doi= }}
*{{cite journal | author=Zelinski T, Kaita H, Lewis M, ''et al.'' |title=The Colton blood group locus. A linkage analysis. |journal=Transfusion |volume=28 |issue= 5 |pages= 435-8 |year= 1988 |pmid= 3166547 |doi= }}
*{{cite journal | author=Preston GM, Jung JS, Guggino WB, Agre P |title=Membrane topology of aquaporin CHIP. Analysis of functional epitope-scanning mutants by vectorial proteolysis. |journal=J. Biol. Chem. |volume=269 |issue= 3 |pages= 1668-73 |year= 1994 |pmid= 7507481 |doi= }}
*{{cite journal | author=Skach WR, Shi LB, Calayag MC, ''et al.'' |title=Biogenesis and transmembrane topology of the CHIP28 water channel at the endoplasmic reticulum. |journal=J. Cell Biol. |volume=125 |issue= 4 |pages= 803-15 |year= 1994 |pmid= 7514605 |doi= }}
*{{cite journal | author=Li X, Yu H, Koide SS |title=The water channel gene in human uterus. |journal=Biochem. Mol. Biol. Int. |volume=32 |issue= 2 |pages= 371-7 |year= 1994 |pmid= 7517253 |doi= }}
*{{cite journal | author=Walz T, Smith BL, Agre P, Engel A |title=The three-dimensional structure of human erythrocyte aquaporin CHIP. |journal=EMBO J. |volume=13 |issue= 13 |pages= 2985-93 |year= 1994 |pmid= 7518771 |doi= }}
*{{cite journal | author=Preston GM, Smith BL, Zeidel ML, ''et al.'' |title=Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels. |journal=Science |volume=265 |issue= 5178 |pages= 1585-7 |year= 1994 |pmid= 7521540 |doi= }}
*{{cite journal | author=Smith BL, Preston GM, Spring FA, ''et al.'' |title=Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens. |journal=J. Clin. Invest. |volume=94 |issue= 3 |pages= 1043-9 |year= 1994 |pmid= 7521882 |doi= }}
*{{cite journal | author=van Hoek AN, Wiener MC, Verbavatz JM, ''et al.'' |title=Purification and structure-function analysis of native, PNGase F-treated, and endo-beta-galactosidase-treated CHIP28 water channels. |journal=Biochemistry |volume=34 |issue= 7 |pages= 2212-9 |year= 1995 |pmid= 7532004 |doi= }}
*{{cite journal | author=Keen TJ, Inglehearn CF, Patel RJ, ''et al.'' |title=Localization of the aquaporin 1 (AQP1) gene within a YAC contig containing the polymorphic markers D7S632 and D7S526. |journal=Genomics |volume=25 |issue= 2 |pages= 599-600 |year= 1995 |pmid= 7540589 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on AXIN1... {November 14, 2007 5:29:03 PM PST}
- SEARCH REDIRECT: Control Box Found: AXIN1 {November 14, 2007 5:29:37 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 5:29:38 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 5:29:38 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 5:29:38 PM PST}
- UPDATED: Updated protein page: AXIN1 {November 14, 2007 5:29:45 PM PST}
- INFO: Beginning work on BCHE... {November 14, 2007 5:12:35 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:13:03 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_BCHE_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1p0i.
| PDB = {{PDB2|1p0i}}, {{PDB2|1p0m}}, {{PDB2|1p0p}}, {{PDB2|1p0q}}, {{PDB2|1xlu}}, {{PDB2|1xlv}}, {{PDB2|1xlw}}, {{PDB2|2j4c}}
| Name = Butyrylcholinesterase
| HGNCid = 983
| Symbol = BCHE
| AltSymbols =; CHE1; E1
| OMIM = 177400
| ECnumber =
| Homologene = 20065
| MGIid = 894278
| GeneAtlas_image1 = PBB_GE_BCHE_205433_at_tn.png
| Function = {{GNF_GO|id=GO:0001540 |text = beta-amyloid binding}} {{GNF_GO|id=GO:0004104 |text = cholinesterase activity}} {{GNF_GO|id=GO:0004759 |text = carboxylesterase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0019899 |text = enzyme binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005641 |text = nuclear envelope lumen}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}}
| Process = {{GNF_GO|id=GO:0050783 |text = cocaine metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 590
| Hs_Ensembl = ENSG00000114200
| Hs_RefseqProtein = NP_000046
| Hs_RefseqmRNA = NM_000055
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 166973387
| Hs_GenLoc_end = 167037944
| Hs_Uniprot = P06276
| Mm_EntrezGene = 12038
| Mm_Ensembl = ENSMUSG00000027792
| Mm_RefseqmRNA = NM_009738
| Mm_RefseqProtein = NP_033868
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 73721734
| Mm_GenLoc_end = 73794168
| Mm_Uniprot = Q499C7
}}
}}
'''Butyrylcholinesterase''', also known as '''BCHE''', 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 = Mutant alleles at the BCHE locus are responsible for suxamethonium sensitivity. Homozygous persons sustain prolonged apnea after administration of the muscle relaxant suxamethonium in connection with surgical anesthesia. The activity of pseudocholinesterase in the serum is low and its substrate behavior is atypical. In the absence of the relaxant, the homozygote is at no known disadvantage.<ref>{{cite web | title = Entrez Gene: BCHE butyrylcholinesterase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=590| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lockridge O |title=Structure of human serum cholinesterase. |journal=Bioessays |volume=9 |issue= 4 |pages= 125-8 |year= 1989 |pmid= 3067729 |doi= 10.1002/bies.950090406 }}
*{{cite journal | author=Allderdice PW, Gardner HA, Galutira D, ''et al.'' |title=The cloned butyrylcholinesterase (BCHE) gene maps to a single chromosome site, 3q26. |journal=Genomics |volume=11 |issue= 2 |pages= 452-4 |year= 1992 |pmid= 1769657 |doi= }}
*{{cite journal | author=Gaughan G, Park H, Priddle J, ''et al.'' |title=Refinement of the localization of human butyrylcholinesterase to chromosome 3q26.1-q26.2 using a PCR-derived probe. |journal=Genomics |volume=11 |issue= 2 |pages= 455-8 |year= 1992 |pmid= 1769658 |doi= }}
*{{cite journal | author=Arpagaus M, Kott M, Vatsis KP, ''et al.'' |title=Structure of the gene for human butyrylcholinesterase. Evidence for a single copy. |journal=Biochemistry |volume=29 |issue= 1 |pages= 124-31 |year= 1990 |pmid= 2322535 |doi= }}
*{{cite journal | author=Nogueira CP, McGuire MC, Graeser C, ''et al.'' |title=Identification of a frameshift mutation responsible for the silent phenotype of human serum cholinesterase, Gly 117 (GGT----GGAG). |journal=Am. J. Hum. Genet. |volume=46 |issue= 5 |pages= 934-42 |year= 1990 |pmid= 2339692 |doi= }}
*{{cite journal | author=McGuire MC, Nogueira CP, Bartels CF, ''et al.'' |title=Identification of the structural mutation responsible for the dibucaine-resistant (atypical) variant form of human serum cholinesterase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 3 |pages= 953-7 |year= 1989 |pmid= 2915989 |doi= }}
*{{cite journal | author=Prody CA, Zevin-Sonkin D, Gnatt A, ''et al.'' |title=Isolation and characterization of full-length cDNA clones coding for cholinesterase from fetal human tissues. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 11 |pages= 3555-9 |year= 1987 |pmid= 3035536 |doi= }}
*{{cite journal | author=Lockridge O, Adkins S, La Du BN |title=Location of disulfide bonds within the sequence of human serum cholinesterase. |journal=J. Biol. Chem. |volume=262 |issue= 27 |pages= 12945-52 |year= 1987 |pmid= 3115973 |doi= }}
*{{cite journal | author=McTiernan C, Adkins S, Chatonnet A, ''et al.'' |title=Brain cDNA clone for human cholinesterase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 19 |pages= 6682-6 |year= 1987 |pmid= 3477799 |doi= }}
*{{cite journal | author=Lockridge O, Bartels CF, Vaughan TA, ''et al.'' |title=Complete amino acid sequence of human serum cholinesterase. |journal=J. Biol. Chem. |volume=262 |issue= 2 |pages= 549-57 |year= 1987 |pmid= 3542989 |doi= }}
*{{cite journal | author=Jbilo O, Toutant JP, Vatsis KP, ''et al.'' |title=Promoter and transcription start site of human and rabbit butyrylcholinesterase genes. |journal=J. Biol. Chem. |volume=269 |issue= 33 |pages= 20829-37 |year= 1994 |pmid= 8063698 |doi= }}
*{{cite journal | author=Mattes C, Bradley R, Slaughter E, Browne S |title=Cocaine and butyrylcholinesterase (BChE): determination of enzymatic parameters. |journal=Life Sci. |volume=58 |issue= 13 |pages= PL257-61 |year= 1996 |pmid= 8622553 |doi= }}
*{{cite journal | author=Iida S, Kinoshita M, Fujii H, ''et al.'' |title=Mutations of human butyrylcholinesterase gene in a family with hypocholinesterasemia. |journal=Hum. Mutat. |volume=6 |issue= 4 |pages= 349-51 |year= 1996 |pmid= 8680411 |doi= 10.1002/humu.1380060411 }}
*{{cite journal | author=Kamendulis LM, Brzezinski MR, Pindel EV, ''et al.'' |title=Metabolism of cocaine and heroin is catalyzed by the same human liver carboxylesterases. |journal=J. Pharmacol. Exp. Ther. |volume=279 |issue= 2 |pages= 713-7 |year= 1996 |pmid= 8930175 |doi= }}
*{{cite journal | author=Hidaka K, Iuchi I, Tomita M, ''et al.'' |title=Genetic analysis of a Japanese patient with butyrylcholinesterase deficiency. |journal=Ann. Hum. Genet. |volume=61 |issue= Pt 6 |pages= 491-6 |year= 1998 |pmid= 9543549 |doi= 10.1046/j.1469-1809.1997.6160491.x }}
*{{cite journal | author=Browne SP, Slaughter EA, Couch RA, ''et al.'' |title=The influence of plasma butyrylcholinesterase concentration on the in vitro hydrolysis of cocaine in human plasma. |journal=Biopharmaceutics & drug disposition |volume=19 |issue= 5 |pages= 309-14 |year= 1998 |pmid= 9673783 |doi= }}
*{{cite journal | author=Altamirano CV, Lockridge O |title=Conserved aromatic residues of the C-terminus of human butyrylcholinesterase mediate the association of tetramers. |journal=Biochemistry |volume=38 |issue= 40 |pages= 13414-22 |year= 1999 |pmid= 10529218 |doi= }}
*{{cite journal | author=Darvesh S, Kumar R, Roberts S, ''et al.'' |title=Butyrylcholinesterase-Mediated enhancement of the enzymatic activity of trypsin. |journal=Cell. Mol. Neurobiol. |volume=21 |issue= 3 |pages= 285-96 |year= 2002 |pmid= 11569538 |doi= }}
*{{cite journal | author=Barta C, Sasvari-Szekely M, Devai A, ''et al.'' |title=Analysis of mutations in the plasma cholinesterase gene of patients with a history of prolonged neuromuscular block during anesthesia. |journal=Mol. Genet. Metab. |volume=74 |issue= 4 |pages= 484-8 |year= 2002 |pmid= 11749053 |doi= 10.1006/mgme.2001.3251 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CAMK2G... {November 14, 2007 5:13:03 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:14:12 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_CAMK2G_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2ux0.
| PDB = {{PDB2|2ux0}}
| Name = Calcium/calmodulin-dependent protein kinase (CaM kinase) II gamma
| HGNCid = 1463
| Symbol = CAMK2G
| AltSymbols =; CAMK; CAMK-II; CAMKG; FLJ16043; MGC26678
| OMIM = 602123
| ECnumber =
| Homologene = 15596
| MGIid = 88259
| GeneAtlas_image1 = PBB_GE_CAMK2G_212669_at_tn.png
| GeneAtlas_image2 = PBB_GE_CAMK2G_212757_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004685 |text = calmodulin-dependent protein kinase activity}} {{GNF_GO|id=GO:0004723 |text = calcium-dependent protein serine/threonine phosphatase activity}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005954 |text = calcium- and calmodulin-dependent protein kinase complex}}
| Process = {{GNF_GO|id=GO:0000082 |text = G1/S transition of mitotic cell cycle}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006816 |text = calcium ion transport}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0030073 |text = insulin secretion}} {{GNF_GO|id=GO:0046777 |text = protein amino acid autophosphorylation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 818
| Hs_Ensembl = ENSG00000148660
| Hs_RefseqProtein = NP_001213
| Hs_RefseqmRNA = NM_001222
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 75242265
| Hs_GenLoc_end = 75304349
| Hs_Uniprot = Q13555
| Mm_EntrezGene = 12325
| Mm_Ensembl = ENSMUSG00000021820
| Mm_RefseqmRNA = XM_980738
| Mm_RefseqProtein = XP_985832
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 19523427
| Mm_GenLoc_end = 19582640
| Mm_Uniprot = Q923T9
}}
}}
'''Calcium/calmodulin-dependent protein kinase (CaM kinase) II gamma''', also known as '''CAMK2G''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The product of this gene belongs to the Serine/Threonine protein kinase family, and to the Ca(2+)/calmodulin-dependent protein kinase subfamily. Calcium signaling is crucial for several aspects of plasticity at glutamatergic synapses. In mammalian cells the enzyme is composed of four different chains: alpha, beta, gamma, and delta. The product of this gene is a gamma chain. Six alternatively spliced variants that encode six different isoforms have been characterized to date. Additional alternative splice variants that encode different isoforms have been described, but their full-length nature has not been determined.<ref>{{cite web | title = Entrez Gene: CAMK2G calcium/calmodulin-dependent protein kinase (CaM kinase) II gamma| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=818| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hook SS, Means AR |title=Ca(2+)/CaM-dependent kinases: from activation to function. |journal=Annu. Rev. Pharmacol. Toxicol. |volume=41 |issue= |pages= 471-505 |year= 2001 |pmid= 11264466 |doi= 10.1146/annurev.pharmtox.41.1.471 }}
*{{cite journal | author=Yamamoto H |title=[Molecular mechanisms of the intracellular localizations of Ca2+/calmodulin-dependent protein kinase II isoforms, and their physiological functions] |journal=Tanpakushitsu Kakusan Koso |volume=47 |issue= 3 |pages= 241-7 |year= 2002 |pmid= 11889801 |doi= }}
*{{cite journal | author=Countaway JL, Nairn AC, Davis RJ |title=Mechanism of desensitization of the epidermal growth factor receptor protein-tyrosine kinase. |journal=J. Biol. Chem. |volume=267 |issue= 2 |pages= 1129-40 |year= 1992 |pmid= 1309762 |doi= }}
*{{cite journal | author=Ikebe M, Reardon S |title=Phosphorylation of smooth myosin light chain kinase by smooth muscle Ca2+/calmodulin-dependent multifunctional protein kinase. |journal=J. Biol. Chem. |volume=265 |issue= 16 |pages= 8975-8 |year= 1990 |pmid= 2160950 |doi= }}
*{{cite journal | author=Czernik AJ, Pang DT, Greengard P |title=Amino acid sequences surrounding the cAMP-dependent and calcium/calmodulin-dependent phosphorylation sites in rat and bovine synapsin I. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 21 |pages= 7518-22 |year= 1987 |pmid= 3118371 |doi= }}
*{{cite journal | author=Vulliet PR, Woodgett JR, Cohen P |title=Phosphorylation of tyrosine hydroxylase by calmodulin-dependent multiprotein kinase. |journal=J. Biol. Chem. |volume=259 |issue= 22 |pages= 13680-3 |year= 1984 |pmid= 6150037 |doi= }}
*{{cite journal | author=Wen Z, Zhong Z, Darnell JE |title=Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation. |journal=Cell |volume=82 |issue= 2 |pages= 241-50 |year= 1995 |pmid= 7543024 |doi= }}
*{{cite journal | author=Kwiatkowski AP, McGill JM |title=Human biliary epithelial cell line Mz-ChA-1 expresses new isoforms of calmodulin-dependent protein kinase II. |journal=Gastroenterology |volume=109 |issue= 4 |pages= 1316-23 |year= 1995 |pmid= 7557101 |doi= }}
*{{cite journal | author=Shuai K, Stark GR, Kerr IM, Darnell JE |title=A single phosphotyrosine residue of Stat91 required for gene activation by interferon-gamma. |journal=Science |volume=261 |issue= 5129 |pages= 1744-6 |year= 1993 |pmid= 7690989 |doi= }}
*{{cite journal | author=Zhu J, Reynet C, Caldwell JS, Kahn CR |title=Characterization of Rad, a new member of Ras/GTPase superfamily, and its regulation by a unique GTPase-activating protein (GAP)-like activity. |journal=J. Biol. Chem. |volume=270 |issue= 9 |pages= 4805-12 |year= 1995 |pmid= 7876254 |doi= }}
*{{cite journal | author=Yakel JL, Vissavajjhala P, Derkach VA, ''et al.'' |title=Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate glutamate receptors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 5 |pages= 1376-80 |year= 1995 |pmid= 7877986 |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 X, Nghiem P, Schulman H, Francke U |title=Localization of the CAMKG gene encoding gamma isoforms of multifunctional calcium/calmodulin-dependent protein kinase (CaM kinase) to human chromosome 10 band q22 and mouse chromosome 14. |journal=Cytogenet. Cell Genet. |volume=66 |issue= 2 |pages= 113-6 |year= 1994 |pmid= 8287681 |doi= }}
*{{cite journal | author=Suko J, Maurer-Fogy I, Plank B, ''et al.'' |title=Phosphorylation of serine 2843 in ryanodine receptor-calcium release channel of skeletal muscle by cAMP-, cGMP- and CaM-dependent protein kinase. |journal=Biochim. Biophys. Acta |volume=1175 |issue= 2 |pages= 193-206 |year= 1993 |pmid= 8380342 |doi= }}
*{{cite journal | author=de Groot RP, den Hertog J, Vandenheede JR, ''et al.'' |title=Multiple and cooperative phosphorylation events regulate the CREM activator function. |journal=EMBO J. |volume=12 |issue= 10 |pages= 3903-11 |year= 1993 |pmid= 8404858 |doi= }}
*{{cite journal | author=Nghiem P, Saati SM, Martens CL, ''et al.'' |title=Cloning and analysis of two new isoforms of multifunctional Ca2+/calmodulin-dependent protein kinase. Expression in multiple human tissues. |journal=J. Biol. Chem. |volume=268 |issue= 8 |pages= 5471-9 |year= 1993 |pmid= 8449910 |doi= }}
*{{cite journal | author=Shimomura A, Ogawa Y, Kitani T, ''et al.'' |title=Calmodulin-dependent protein kinase II potentiates transcriptional activation through activating transcription factor 1 but not cAMP response element-binding protein. |journal=J. Biol. Chem. |volume=271 |issue= 30 |pages= 17957-60 |year= 1996 |pmid= 8663317 |doi= }}
*{{cite journal | author=Wei J, Wayman G, Storm DR |title=Phosphorylation and inhibition of type III adenylyl cyclase by calmodulin-dependent protein kinase II in vivo. |journal=J. Biol. Chem. |volume=271 |issue= 39 |pages= 24231-5 |year= 1996 |pmid= 8798667 |doi= }}
*{{cite journal | author=Tombes RM, Krystal GW |title=Identification of novel human tumor cell-specific CaMK-II variants. |journal=Biochim. Biophys. Acta |volume=1355 |issue= 3 |pages= 281-92 |year= 1997 |pmid= 9060999 |doi= }}
*{{cite journal | author=Moyers JS, Bilan PJ, Zhu J, Kahn CR |title=Rad and Rad-related GTPases interact with calmodulin and calmodulin-dependent protein kinase II. |journal=J. Biol. Chem. |volume=272 |issue= 18 |pages= 11832-9 |year= 1997 |pmid= 9115241 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CASP2... {November 14, 2007 5:14:12 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:15:09 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CASP2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1pyo.
| PDB = {{PDB2|1pyo}}, {{PDB2|2p2c}}
| Name = Caspase 2, apoptosis-related cysteine peptidase (neural precursor cell expressed, developmentally down-regulated 2)
| HGNCid = 1503
| Symbol = CASP2
| AltSymbols =; CASP-2; ICH-1L; ICH-1L/1S; ICH1; NEDD2
| OMIM = 600639
| ECnumber =
| Homologene = 7254
| MGIid = 97295
| GeneAtlas_image1 = PBB_GE_CASP2_34449_at_tn.png
| GeneAtlas_image2 = PBB_GE_CASP2_208050_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_CASP2_209811_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008234 |text = cysteine-type peptidase activity}} {{GNF_GO|id=GO:0019899 |text = enzyme binding}} {{GNF_GO|id=GO:0030693 |text = caspase activity}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0008632 |text = apoptotic program}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 835
| Hs_Ensembl = ENSG00000106144
| Hs_RefseqProtein = NP_116764
| Hs_RefseqmRNA = NM_032982
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 142695524
| Hs_GenLoc_end = 142714906
| Hs_Uniprot = P42575
| Mm_EntrezGene = 12366
| Mm_Ensembl = ENSMUSG00000029863
| Mm_RefseqmRNA = NM_007610
| Mm_RefseqProtein = NP_031636
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 42194648
| Mm_GenLoc_end = 42212114
| Mm_Uniprot = P29594
}}
}}
'''Caspase 2, apoptosis-related cysteine peptidase (neural precursor cell expressed, developmentally down-regulated 2)''', also known as '''CASP2''', 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 which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. The proteolytic cleavage of this protein is induced by a variety of apoptotic stimuli. Alternative splicing of this gene results in multiple transcript variants that encode different isoforms.<ref>{{cite web | title = Entrez Gene: CASP2 caspase 2, apoptosis-related cysteine peptidase (neural precursor cell expressed, developmentally down-regulated 2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=835| accessdate = }}</ref>
}}
==References==
{{reflist}}
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CD38... {November 14, 2007 5:15:09 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:15:44 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_CD38_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1yh3.
| PDB = {{PDB2|1yh3}}, {{PDB2|1zvm}}, {{PDB2|2ef1}}, {{PDB2|2hct}}, {{PDB2|2i65}}, {{PDB2|2i66}}, {{PDB2|2i67}}, {{PDB2|2o3q}}, {{PDB2|2o3r}}, {{PDB2|2o3s}}, {{PDB2|2o3t}}, {{PDB2|2o3u}}, {{PDB2|2pgj}}, {{PDB2|2pgl}}
| Name = CD38 molecule
| HGNCid = 1667
| Symbol = CD38
| AltSymbols =; T10
| OMIM = 107270
| ECnumber =
| Homologene = 1345
| MGIid = 107474
| GeneAtlas_image1 = PBB_GE_CD38_205692_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003953 |text = NAD+ nucleosidase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0016798 |text = hydrolase activity, acting on glycosyl bonds}} {{GNF_GO|id=GO:0016849 |text = phosphorus-oxygen lyase activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006091 |text = generation of precursor metabolites and energy}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0008624 |text = induction of apoptosis by extracellular signals}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 952
| Hs_Ensembl = ENSG00000004468
| Hs_RefseqProtein = NP_001766
| Hs_RefseqmRNA = NM_001775
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 15388999
| Hs_GenLoc_end = 15460167
| Hs_Uniprot = P28907
| Mm_EntrezGene = 12494
| Mm_Ensembl = ENSMUSG00000029084
| Mm_RefseqmRNA = NM_007646
| Mm_RefseqProtein = NP_031672
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 44157098
| Mm_GenLoc_end = 44200622
| Mm_Uniprot = Q3UCS6
}}
}}
'''CD38 molecule''', also known as '''CD38''', 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 = CD38 is a novel multifunctional ectoenzyme widely expressed in cells and tissues especially in leukocytes. CD38 also functions in cell adhesion,signal transduction and calcium signaling.<ref>{{cite web | title = Entrez Gene: CD38 CD38 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=952| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=States DJ, Walseth TF, Lee HC |title=Similarities in amino acid sequences of Aplysia ADP-ribosyl cyclase and human lymphocyte antigen CD38. |journal=Trends Biochem. Sci. |volume=17 |issue= 12 |pages= 495 |year= 1993 |pmid= 1471258 |doi= }}
*{{cite journal | author=Malavasi F, Funaro A, Roggero S, ''et al.'' |title=Human CD38: a glycoprotein in search of a function. |journal=Immunol. Today |volume=15 |issue= 3 |pages= 95-7 |year= 1994 |pmid= 8172650 |doi= }}
*{{cite journal | author=Guse AH |title=Cyclic ADP-ribose: a novel Ca2+-mobilising second messenger. |journal=Cell. Signal. |volume=11 |issue= 5 |pages= 309-16 |year= 1999 |pmid= 10376802 |doi= }}
*{{cite journal | author=Funaro A, Malavasi F |title=Human CD38, a surface receptor, an enzyme, an adhesion molecule and not a simple marker. |journal=J. Biol. Regul. Homeost. Agents |volume=13 |issue= 1 |pages= 54-61 |year= 1999 |pmid= 10432444 |doi= }}
*{{cite journal | author=Mallone R, Perin PC |title=Anti-CD38 autoantibodies in type? diabetes. |journal=Diabetes Metab. Res. Rev. |volume=22 |issue= 4 |pages= 284-94 |year= 2006 |pmid= 16544364 |doi= 10.1002/dmrr.626 }}
*{{cite journal | author=Partidá-Sánchez S, Rivero-Nava L, Shi G, Lund FE |title=CD38: an ecto-enzyme at the crossroads of innate and adaptive immune responses. |journal=Adv. Exp. Med. Biol. |volume=590 |issue= |pages= 171-83 |year= 2007 |pmid= 17191385 |doi= }}
*{{cite journal | author=Jackson DG, Bell JI |title=Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell surface glycoprotein with an unusual discontinuous pattern of expression during lymphocyte differentiation. |journal=J. Immunol. |volume=144 |issue= 7 |pages= 2811-5 |year= 1990 |pmid= 2319135 |doi= }}
*{{cite journal | author=Dianzani U, Bragardo M, Buonfiglio D, ''et al.'' |title=Modulation of CD4 lateral interaction with lymphocyte surface molecules induced by HIV-1 gp120. |journal=Eur. J. Immunol. |volume=25 |issue= 5 |pages= 1306-11 |year= 1995 |pmid= 7539755 |doi= }}
*{{cite journal | author=Nakagawara K, Mori M, Takasawa S, ''et al.'' |title=Assignment of CD38, the gene encoding human leukocyte antigen CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase), to chromosome 4p15. |journal=Cytogenet. Cell Genet. |volume=69 |issue= 1-2 |pages= 38-9 |year= 1995 |pmid= 7835083 |doi= }}
*{{cite journal | author=Tohgo A, Takasawa S, Noguchi N, ''et al.'' |title=Essential cysteine residues for cyclic ADP-ribose synthesis and hydrolysis by CD38. |journal=J. Biol. Chem. |volume=269 |issue= 46 |pages= 28555-7 |year= 1994 |pmid= 7961800 |doi= }}
*{{cite journal | author=Takasawa S, Tohgo A, Noguchi N, ''et al.'' |title=Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte antigen CD38 and inhibition of the hydrolysis by ATP. |journal=J. Biol. Chem. |volume=268 |issue= 35 |pages= 26052-4 |year= 1994 |pmid= 8253715 |doi= }}
*{{cite journal | author=Nata K, Takamura T, Karasawa T, ''et al.'' |title=Human gene encoding CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase): organization, nucleotide sequence and alternative splicing. |journal=Gene |volume=186 |issue= 2 |pages= 285-92 |year= 1997 |pmid= 9074508 |doi= }}
*{{cite journal | author=Feito MJ, Bragardo M, Buonfiglio D, ''et al.'' |title=gp 120s derived from four syncytium-inducing HIV-1 strains induce different patterns of CD4 association with lymphocyte surface molecules. |journal=Int. Immunol. |volume=9 |issue= 8 |pages= 1141-7 |year= 1997 |pmid= 9263011 |doi= }}
*{{cite journal | author=Ferrero E, Malavasi F |title=Human CD38, a leukocyte receptor and ectoenzyme, is a member of a novel eukaryotic gene family of nicotinamide adenine dinucleotide+-converting enzymes: extensive structural homology with the genes for murine bone marrow stromal cell antigen 1 and aplysian ADP-ribosyl cyclase. |journal=J. Immunol. |volume=159 |issue= 8 |pages= 3858-65 |year= 1997 |pmid= 9378973 |doi= }}
*{{cite journal | author=Deaglio S, Morra M, Mallone R, ''et al.'' |title=Human CD38 (ADP-ribosyl cyclase) is a counter-receptor of CD31, an Ig superfamily member. |journal=J. Immunol. |volume=160 |issue= 1 |pages= 395-402 |year= 1998 |pmid= 9551996 |doi= }}
*{{cite journal | author=Yagui K, Shimada F, Mimura M, ''et al.'' |title=A missense mutation in the CD38 gene, a novel factor for insulin secretion: association with Type II diabetes mellitus in Japanese subjects and evidence of abnormal function when expressed in vitro. |journal=Diabetologia |volume=41 |issue= 9 |pages= 1024-8 |year= 1998 |pmid= 9754820 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CGA... {November 14, 2007 5:15:44 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:16:39 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CGA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dz7.
| PDB = {{PDB2|1dz7}}, {{PDB2|1e9j}}, {{PDB2|1fl7}}, {{PDB2|1hcn}}, {{PDB2|1hd4}}, {{PDB2|1hrp}}, {{PDB2|1qfw}}, {{PDB2|1xwd}}
| Name = Glycoprotein hormones, alpha polypeptide
| HGNCid = 1885
| Symbol = CGA
| AltSymbols =; CG-ALPHA; FSHA; GPHA1; GPHa; HCG; LHA; TSHA
| OMIM = 118850
| ECnumber =
| Homologene = 587
| MGIid = 88390
| GeneAtlas_image1 = PBB_GE_CGA_204637_at_tn.png
| Function = {{GNF_GO|id=GO:0005179 |text = hormone activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1081
| Hs_Ensembl = ENSG00000135346
| Hs_RefseqProtein = NP_000726
| Hs_RefseqmRNA = NM_000735
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 87851935
| Hs_GenLoc_end = 87861569
| Hs_Uniprot = P01215
| Mm_EntrezGene = 12640
| Mm_Ensembl = ENSMUSG00000028298
| Mm_RefseqmRNA = NM_009889
| Mm_RefseqProtein = NP_034019
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 35082666
| Mm_GenLoc_end = 35096261
| Mm_Uniprot = P01216
}}
}}
'''Glycoprotein hormones, alpha polypeptide''', also known as '''CGA''', 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 four human glycoprotein hormones chorionic gonadotropin (CG), luteinizing hormone (LH), follicle stimulating hormone (FSH), and thyroid stimulating hormone (TSH) are dimers consisting of alpha and beta subunits that are associated noncovalently. The alpha subunits of these hormones are identical, however, their beta chains are unique and confer biological specificity. The protein encoded by this gene is the alpha subunit and belongs to the glycoprotein hormones alpha chain family.<ref>{{cite web | title = Entrez Gene: CGA glycoprotein hormones, alpha polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1081| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Roger M, Lahlou N, Couzinet B, ''et al.'' |title=[Free alpha-subunit glycoprotein hormones: physiological and pathological data] |journal=J. Steroid Biochem. |volume=33 |issue= 4B |pages= 763-9 |year= 1990 |pmid= 2481154 |doi= }}
*{{cite journal | author=Pierce JG |title=Eli Lilly lecture. The subunits of pituitary thyrotropin--their relationship to other glycoprotein hormones. |journal=Endocrinology |volume=89 |issue= 6 |pages= 1331-44 |year= 1972 |pmid= 5002675 |doi= }}
*{{cite journal | author=Kourides IA, Gurr JA, Wolf O |title=The regulation and organization of thyroid stimulating hormone genes. |journal=Recent Prog. Horm. Res. |volume=40 |issue= |pages= 79-120 |year= 1984 |pmid= 6207569 |doi= }}
*{{cite journal | author=Miyoshi I, Kasai N, Hayashizaki Y |title=[Structure and regulation of human thyroid-stimulating hormone (TSH) gene] |journal=Nippon Rinsho |volume=52 |issue= 4 |pages= 940-7 |year= 1994 |pmid= 8196184 |doi= }}
*{{cite journal | author=Barrios-De-Tomasi J, Timossi C, Merchant H, ''et al.'' |title=Assessment of the in vitro and in vivo biological activities of the human follicle-stimulating isohormones. |journal=Mol. Cell. Endocrinol. |volume=186 |issue= 2 |pages= 189-98 |year= 2002 |pmid= 11900895 |doi= }}
*{{cite journal | author=Moyle WR, Bahl OP, März L |title=Role of carbohydrate of human chorionic gonadotropin in the mechanism of hormone action. |journal=J. Biol. Chem. |volume=250 |issue= 23 |pages= 9163-9 |year= 1976 |pmid= 172504 |doi= }}
*{{cite journal | author=Fiddes JC, Goodman HM |title=Isolation, cloning and sequence analysis of the cDNA for the alpha-subunit of human chorionic gonadotropin. |journal=Nature |volume=281 |issue= 5730 |pages= 351-6 |year= 1979 |pmid= 481597 |doi= }}
*{{cite journal | author=Sairam MR, Li CH |title=Human pituitary thyrotropin. The primary structure of the alpha and beta subunits. |journal=Can. J. Biochem. |volume=55 |issue= 7 |pages= 755-60 |year= 1977 |pmid= 890569 |doi= }}
*{{cite journal | author=Morgan FJ, Birken S, Canfield RE |title=The amino acid sequence of human chorionic gonadotropin. The alpha subunit and beta subunit. |journal=J. Biol. Chem. |volume=250 |issue= 13 |pages= 5247-58 |year= 1975 |pmid= 1150658 |doi= }}
*{{cite journal | author=Rathnam P, Saxena BB |title=Primary amino acid sequence of follicle-stimulating hormone from human pituitary glands. I. alpha subunit. |journal=J. Biol. Chem. |volume=250 |issue= 17 |pages= 6735-46 |year= 1975 |pmid= 1158880 |doi= }}
*{{cite journal | author=Weisshaar G, Hiyama J, Renwick AG, Nimtz M |title=NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin. |journal=Eur. J. Biochem. |volume=195 |issue= 1 |pages= 257-68 |year= 1991 |pmid= 1991473 |doi= }}
*{{cite journal | author=Sakakibara R, Yokoo Y, Yoshikoshi K, ''et al.'' |title=Subcellular localization of intracellular forms of human chorionic gonadotropin in first trimester placenta. |journal=J. Biochem. |volume=102 |issue= 5 |pages= 993-1001 |year= 1988 |pmid= 2449427 |doi= }}
*{{cite journal | author=Matzuk MM, Keene JL, Boime I |title=Site specificity of the chorionic gonadotropin N-linked oligosaccharides in signal transduction. |journal=J. Biol. Chem. |volume=264 |issue= 5 |pages= 2409-14 |year= 1989 |pmid= 2536708 |doi= }}
*{{cite journal | author=Lustbader JW, Birken S, Pileggi NF, ''et al.'' |title=Crystallization and characterization of human chorionic gonadotropin in chemically deglycosylated and enzymatically desialylated states. |journal=Biochemistry |volume=28 |issue= 24 |pages= 9239-43 |year= 1990 |pmid= 2611225 |doi= }}
*{{cite journal | author=Harris DC, Machin KJ, Evin GM, ''et al.'' |title=Preliminary X-ray diffraction analysis of human chorionic gonadotropin. |journal=J. Biol. Chem. |volume=264 |issue= 12 |pages= 6705-6 |year= 1989 |pmid= 2708337 |doi= }}
*{{cite journal | author=Hayashizaki Y, Miyai K, Kato K, Matsubara K |title=Molecular cloning of the human thyrotropin-beta subunit gene. |journal=FEBS Lett. |volume=188 |issue= 2 |pages= 394-400 |year= 1985 |pmid= 3839756 |doi= }}
*{{cite journal | author=Bellisario R, Carlsen RB, Bahl OP |title=Human chorionic gonadotropin. Linear amino acid sequence of the alpha subunit. |journal=J. Biol. Chem. |volume=248 |issue= 19 |pages= 6796-809 |year= 1973 |pmid= 4745444 |doi= }}
*{{cite journal | author=Shome B, Parlow AF |title=Human follicle stimulating hormone (hFSH): first proposal for the amino acid sequence of the alpha-subunit (hFSHa) and first demonstration of its identity with the alpha-subunit of human luteinizing hormone (hLHa). |journal=J. Clin. Endocrinol. Metab. |volume=39 |issue= 1 |pages= 199-202 |year= 1974 |pmid= 4835135 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CLTC... {November 14, 2007 5:16:39 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:17:24 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_CLTC_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1b89.
| PDB = {{PDB2|1b89}}, {{PDB2|1bpo}}, {{PDB2|1c9i}}, {{PDB2|1c9l}}, {{PDB2|1utc}}, {{PDB2|1xi4}}, {{PDB2|1xi5}}
| Name = Clathrin, heavy chain (Hc)
| HGNCid = 2092
| Symbol = CLTC
| AltSymbols =; CHC17; CLH-17; CLTCL2; Hc; KIAA0034
| OMIM = 118955
| ECnumber =
| Homologene = 3572
| MGIid = 2388633
| GeneAtlas_image1 = PBB_GE_CLTC_200614_at_tn.png
| Function = {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005905 |text = coated pit}} {{GNF_GO|id=GO:0030125 |text = clathrin vesicle coat}}
| Process = {{GNF_GO|id=GO:0006886 |text = intracellular protein transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1213
| Hs_Ensembl = ENSG00000141367
| Hs_RefseqProtein = NP_004850
| Hs_RefseqmRNA = NM_004859
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 55052038
| Hs_GenLoc_end = 55127254
| Hs_Uniprot = Q00610
| Mm_EntrezGene = 67300
| Mm_Ensembl = ENSMUSG00000047126
| Mm_RefseqmRNA = NM_001003908
| Mm_RefseqProtein = NP_001003908
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 86510546
| Mm_GenLoc_end = 86573760
| Mm_Uniprot = Q3TJ98
}}
}}
'''Clathrin, heavy chain (Hc)''', also known as '''CLTC''', 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 = Clathrin is a major protein component of the cytoplasmic face of intracellular organelles, called coated vesicles and coated pits. These specialized organelles are involved in the intracellular trafficking of receptors and endocytosis of a variety of macromolecules. The basic subunit of the clathrin coat is composed of three heavy chains and three light chains.<ref>{{cite web | title = Entrez Gene: CLTC clathrin, heavy chain (Hc)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1213| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Murphy JE, Keen JH |title=Recognition sites for clathrin-associated proteins AP-2 and AP-3 on clathrin triskelia. |journal=J. Biol. Chem. |volume=267 |issue= 15 |pages= 10850-5 |year= 1992 |pmid= 1587861 |doi= }}
*{{cite journal | author=Dodge GR, Kovalszky I, McBride OW, ''et al.'' |title=Human clathrin heavy chain (CLTC): partial molecular cloning, expression, and mapping of the gene to human chromosome 17q11-qter. |journal=Genomics |volume=11 |issue= 1 |pages= 174-8 |year= 1992 |pmid= 1765375 |doi= }}
*{{cite journal | author=Corvera S |title=Insulin stimulates the assembly of cytosolic clathrin onto adipocyte plasma membranes. |journal=J. Biol. Chem. |volume=265 |issue= 5 |pages= 2413-6 |year= 1990 |pmid= 2154445 |doi= }}
*{{cite journal | author=Scarmato P, Kirchhausen T |title=Analysis of clathrin light chain-heavy chain interactions using truncated mutants of rat liver light chain LCB3. |journal=J. Biol. Chem. |volume=265 |issue= 7 |pages= 3661-8 |year= 1990 |pmid= 2406259 |doi= }}
*{{cite journal | author=Hanspal M, Luna E, Branton D |title=The association of clathrin fragments with coated vesicle membranes. |journal=J. Biol. Chem. |volume=259 |issue= 17 |pages= 11075-82 |year= 1984 |pmid= 6147350 |doi= }}
*{{cite journal | author=Nomura N, Miyajima N, Sazuka T, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. |journal=DNA Res. |volume=1 |issue= 1 |pages= 27-35 |year= 1995 |pmid= 7584026 |doi= }}
*{{cite journal | author=Nomura N, Miyajima N, Sazuka T, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1 (supplement). |journal=DNA Res. |volume=1 |issue= 1 |pages= 47-56 |year= 1995 |pmid= 7584028 |doi= }}
*{{cite journal | author=Fausser JL, Ungewickell E, Ruch JV, Lesot H |title=Interaction of vinculin with the clathrin heavy chain. |journal=J. Biochem. |volume=114 |issue= 4 |pages= 498-503 |year= 1994 |pmid= 8276759 |doi= }}
*{{cite journal | author=Kedra D, Peyrard M, Fransson I, ''et al.'' |title=Characterization of a second human clathrin heavy chain polypeptide gene (CLH-22) from chromosome 22q11. |journal=Hum. Mol. Genet. |volume=5 |issue= 5 |pages= 625-31 |year= 1997 |pmid= 8733129 |doi= }}
*{{cite journal | author=Goodman OB, Krupnick JG, Gurevich VV, ''et al.'' |title=Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain. |journal=J. Biol. Chem. |volume=272 |issue= 23 |pages= 15017-22 |year= 1997 |pmid= 9169477 |doi= }}
*{{cite journal | author=Ramjaun AR, Micheva KD, Bouchelet I, McPherson PS |title=Identification and characterization of a nerve terminal-enriched amphiphysin isoform. |journal=J. Biol. Chem. |volume=272 |issue= 26 |pages= 16700-6 |year= 1997 |pmid= 9195986 |doi= }}
*{{cite journal | author=McMahon HT, Wigge P, Smith C |title=Clathrin interacts specifically with amphiphysin and is displaced by dynamin. |journal=FEBS Lett. |volume=413 |issue= 2 |pages= 319-22 |year= 1997 |pmid= 9280305 |doi= }}
*{{cite journal | author=Foti M, Mangasarian A, Piguet V, ''et al.'' |title=Nef-mediated clathrin-coated pit formation. |journal=J. Cell Biol. |volume=139 |issue= 1 |pages= 37-47 |year= 1998 |pmid= 9314527 |doi= }}
*{{cite journal | author=Dell'Angelica EC, Klumperman J, Stoorvogel W, Bonifacino JS |title=Association of the AP-3 adaptor complex with clathrin. |journal=Science |volume=280 |issue= 5362 |pages= 431-4 |year= 1998 |pmid= 9545220 |doi= }}
*{{cite journal | author=Ramjaun AR, McPherson PS |title=Multiple amphiphysin II splice variants display differential clathrin binding: identification of two distinct clathrin-binding sites. |journal=J. Neurochem. |volume=70 |issue= 6 |pages= 2369-76 |year= 1998 |pmid= 9603201 |doi= }}
*{{cite journal | author=ter Haar E, Musacchio A, Harrison SC, Kirchhausen T |title=Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker. |journal=Cell |volume=95 |issue= 4 |pages= 563-73 |year= 1998 |pmid= 9827808 |doi= }}
*{{cite journal | author=Laporte SA, Oakley RH, Zhang J, ''et al.'' |title=The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 7 |pages= 3712-7 |year= 1999 |pmid= 10097102 |doi= }}
*{{cite journal | author=Turner CE, Brown MC, Perrotta JA, ''et al.'' |title=Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling. |journal=J. Cell Biol. |volume=145 |issue= 4 |pages= 851-63 |year= 1999 |pmid= 10330411 |doi= }}
*{{cite journal | author=Hussain NK, Yamabhai M, Ramjaun AR, ''et al.'' |title=Splice variants of intersectin are components of the endocytic machinery in neurons and nonneuronal cells. |journal=J. Biol. Chem. |volume=274 |issue= 22 |pages= 15671-7 |year= 1999 |pmid= 10336464 |doi= }}
*{{cite journal | author=Ybe JA, Brodsky FM, Hofmann K, ''et al.'' |title=Clathrin self-assembly is mediated by a tandemly repeated superhelix. |journal=Nature |volume=399 |issue= 6734 |pages= 371-5 |year= 1999 |pmid= 10360576 |doi= 10.1038/20708 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on COL18A1... {November 14, 2007 5:31:12 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:31:49 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_COL18A1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bnl.
| PDB = {{PDB2|1bnl}}
| Name = Collagen, type XVIII, alpha 1
| HGNCid = 2195
| Symbol = COL18A1
| AltSymbols =; FLJ27325; KNO; MGC74745
| OMIM = 120328
| ECnumber =
| Homologene = 7673
| MGIid = 88451
| GeneAtlas_image1 = PBB_GE_COL18A1_209082_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_COL18A1_209081_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005201 |text = extracellular matrix structural constituent}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005581 |text = collagen}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006817 |text = phosphate transport}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007601 |text = visual perception}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 80781
| Hs_Ensembl = ENSG00000182871
| Hs_RefseqProtein = NP_085059
| Hs_RefseqmRNA = NM_030582
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 21
| Hs_GenLoc_start = 45649516
| Hs_GenLoc_end = 45758061
| Hs_Uniprot = P39060
| Mm_EntrezGene = 12822
| Mm_Ensembl = ENSMUSG00000001435
| Mm_RefseqmRNA = NM_009929
| Mm_RefseqProtein = NP_034059
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 76495895
| Mm_GenLoc_end = 76610217
| Mm_Uniprot = Q61434
}}
}}
'''Collagen, type XVIII, alpha 1''', also known as '''COL18A1''', 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 alpha chain of type XVIII collagen. This collagen is one of the multiplexins, extracellular matrix proteins that contain multiple triple-helix domains (collagenous domains) interrupted by non-collagenous domains. The proteolytically produced C-terminal fragment of type XVIII collagen is endostatin, a potent antiangiogenic protein. Mutations in this gene are associated with Knobloch syndrome. The main features of this syndrome involve retinal abnormalities so type XVIII collagen may play an important role in retinal structure and in neural tube closure. Two transcript variants encoding different isoforms have been found for this gene.<ref>{{cite web | title = Entrez Gene: COL18A1 collagen, type XVIII, alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=80781| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Pufe T, Kurz B, Petersen W, ''et al.'' |title=The influence of biomechanical parameters on the expression of VEGF and endostatin in the bone and joint system. |journal=Ann. Anat. |volume=187 |issue= 5-6 |pages= 461-72 |year= 2006 |pmid= 16320826 |doi= }}
*{{cite journal | author=Oh SP, Kamagata Y, Muragaki Y, ''et al.'' |title=Isolation and sequencing of cDNAs for proteins with multiple domains of Gly-Xaa-Yaa repeats identify a distinct family of collagenous proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 10 |pages= 4229-33 |year= 1994 |pmid= 8183893 |doi= }}
*{{cite journal | author=Oh SP, Warman ML, Seldin MF, ''et al.'' |title=Cloning of cDNA and genomic DNA encoding human type XVIII collagen and localization of the alpha 1(XVIII) collagen gene to mouse chromosome 10 and human chromosome 21. |journal=Genomics |volume=19 |issue= 3 |pages= 494-9 |year= 1994 |pmid= 8188291 |doi= 10.1006/geno.1994.1098 }}
*{{cite journal | author=Sertié AL, Quimby M, Moreira ES, ''et al.'' |title=A gene which causes severe ocular alterations and occipital encephalocele (Knobloch syndrome) is mapped to 21q22.3. |journal=Hum. Mol. Genet. |volume=5 |issue= 6 |pages= 843-7 |year= 1996 |pmid= 8776601 |doi= }}
*{{cite journal | author=O'Reilly MS, Boehm T, Shing Y, ''et al.'' |title=Endostatin: an endogenous inhibitor of angiogenesis and tumor growth. |journal=Cell |volume=88 |issue= 2 |pages= 277-85 |year= 1997 |pmid= 9008168 |doi= }}
*{{cite journal | author=Saarela J, Ylikärppä R, Rehn M, ''et al.'' |title=Complete primary structure of two variant forms of human type XVIII collagen and tissue-specific differences in the expression of the corresponding transcripts. |journal=Matrix Biol. |volume=16 |issue= 6 |pages= 319-28 |year= 1998 |pmid= 9503365 |doi= }}
*{{cite journal | author=Ding YH, Javaherian K, Lo KM, ''et al.'' |title=Zinc-dependent dimers observed in crystals of human endostatin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 18 |pages= 10443-8 |year= 1998 |pmid= 9724722 |doi= }}
*{{cite journal | author=Sasaki T, Göhring W, Miosge N, ''et al.'' |title=Tropoelastin binding to fibulins, nidogen-2 and other extracellular matrix proteins. |journal=FEBS Lett. |volume=460 |issue= 2 |pages= 280-4 |year= 1999 |pmid= 10544250 |doi= }}
*{{cite journal | author=Felbor U, Dreier L, Bryant RA, ''et al.'' |title=Secreted cathepsin L generates endostatin from collagen XVIII. |journal=EMBO J. |volume=19 |issue= 6 |pages= 1187-94 |year= 2000 |pmid= 10716919 |doi= 10.1093/emboj/19.6.1187 }}
*{{cite journal | author=Hattori M, Fujiyama A, Taylor TD, ''et al.'' |title=The DNA sequence of human chromosome 21. |journal=Nature |volume=405 |issue= 6784 |pages= 311-9 |year= 2000 |pmid= 10830953 |doi= 10.1038/35012518 }}
*{{cite journal | author=Sertié AL, Sossi V, Camargo AA, ''et al.'' |title=Collagen XVIII, containing an endogenous inhibitor of angiogenesis and tumor growth, plays a critical role in the maintenance of retinal structure and in neural tube closure (Knobloch syndrome). |journal=Hum. Mol. Genet. |volume=9 |issue= 13 |pages= 2051-8 |year= 2000 |pmid= 10942434 |doi= }}
*{{cite journal | author=Rehn M, Veikkola T, Kukk-Valdre E, ''et al.'' |title=Interaction of endostatin with integrins implicated in angiogenesis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 3 |pages= 1024-9 |year= 2001 |pmid= 11158588 |doi= 10.1073/pnas.031564998 }}
*{{cite journal | author=Karumanchi SA, Jha V, Ramchandran R, ''et al.'' |title=Cell surface glypicans are low-affinity endostatin receptors. |journal=Mol. Cell |volume=7 |issue= 4 |pages= 811-22 |year= 2001 |pmid= 11336704 |doi= }}
*{{cite journal | author=Feng Y, Cui LB, Liu CX, Ma QJ |title=[Inhibition effect in vitro of purified endostatin expressed in Pichia pastoris] |journal=Sheng Wu Gong Cheng Xue Bao |volume=17 |issue= 3 |pages= 278-82 |year= 2001 |pmid= 11517600 |doi= }}
*{{cite journal | author=Iughetti P, Suzuki O, Godoi PH, ''et al.'' |title=A polymorphism in endostatin, an angiogenesis inhibitor, predisposes for the development of prostatic adenocarcinoma. |journal=Cancer Res. |volume=61 |issue= 20 |pages= 7375-8 |year= 2001 |pmid= 11606364 |doi= }}
*{{cite journal | author=Wu P, Yonekura H, Li H, ''et al.'' |title=Hypoxia down-regulates endostatin production by human microvascular endothelial cells and pericytes. |journal=Biochem. Biophys. Res. Commun. |volume=288 |issue= 5 |pages= 1149-54 |year= 2001 |pmid= 11700031 |doi= 10.1006/bbrc.2001.5903 }}
*{{cite journal | author=Zorick TS, Mustacchi Z, Bando SY, ''et al.'' |title=High serum endostatin levels in Down syndrome: implications for improved treatment and prevention of solid tumours. |journal=Eur. J. Hum. Genet. |volume=9 |issue= 11 |pages= 811-4 |year= 2002 |pmid= 11781696 |doi= 10.1038/sj.ejhg.5200721 }}
*{{cite journal | author=Hanai J, Dhanabal M, Karumanchi SA, ''et al.'' |title=Endostatin causes G1 arrest of endothelial cells through inhibition of cyclin D1. |journal=J. Biol. Chem. |volume=277 |issue= 19 |pages= 16464-9 |year= 2002 |pmid= 11815623 |doi= 10.1074/jbc.M112274200 }}
*{{cite journal | author=Ergün S, Kilic N, Wurmbach JH, ''et al.'' |title=Endostatin inhibits angiogenesis by stabilization of newly formed endothelial tubes. |journal=Angiogenesis |volume=4 |issue= 3 |pages= 193-206 |year= 2002 |pmid= 11911017 |doi= }}
*{{cite journal | author=Tomono Y, Naito I, Ando K, ''et al.'' |title=Epitope-defined monoclonal antibodies against multiplexin collagens demonstrate that type XV and XVIII collagens are expressed in specialized basement membranes. |journal=Cell Struct. Funct. |volume=27 |issue= 1 |pages= 9-20 |year= 2002 |pmid= 11937714 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CTSG... {November 14, 2007 5:17:24 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:19:19 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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| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CTSG_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1au8.
| PDB = {{PDB2|1au8}}, {{PDB2|1cgh}}, {{PDB2|1kyn}}, {{PDB2|1t32}}
| Name = Cathepsin G
| HGNCid = 2532
| Symbol = CTSG
| AltSymbols =; CG; MGC23078
| OMIM = 116830
| ECnumber =
| Homologene = 20450
| MGIid = 88563
| GeneAtlas_image1 = PBB_GE_CTSG_205653_at_tn.png
| Function = {{GNF_GO|id=GO:0004261 |text = cathepsin G activity}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}}
| Component = {{GNF_GO|id=GO:0005626 |text = insoluble fraction}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006955 |text = immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1511
| Hs_Ensembl = ENSG00000100448
| Hs_RefseqProtein = NP_001902
| Hs_RefseqmRNA = NM_001911
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 24112564
| Hs_GenLoc_end = 24115306
| Hs_Uniprot = P08311
| Mm_EntrezGene = 13035
| Mm_Ensembl = ENSMUSG00000040314
| Mm_RefseqmRNA = NM_007800
| Mm_RefseqProtein = NP_031826
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 55053952
| Mm_GenLoc_end = 55056645
| Mm_Uniprot = Q059V7
}}
}}
'''Cathepsin G''', also known as '''CTSG''', 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, a member of the peptidase S1 protein family, is found in azurophil granules of neutrophilic polymorphonuclear leukocytes. The encoded protease has a specificity similar to that of chymotrypsin C, and may participate in the killing and digestion of engulfed pathogens, and in connective tissue remodeling at sites of inflammation. Transcript variants utilizing alternative polyadenylation signals exist for this gene.<ref>{{cite web | title = Entrez Gene: CTSG cathepsin G| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1511| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Shafer WM, Katzif S, Bowers S, ''et al.'' |title=Tailoring an antibacterial peptide of human lysosomal cathepsin G to enhance its broad-spectrum action against antibiotic-resistant bacterial pathogens. |journal=Curr. Pharm. Des. |volume=8 |issue= 9 |pages= 695-702 |year= 2002 |pmid= 11945165 |doi= }}
*{{cite journal | author=Cohen AB, Stevens MD, Miller EJ, ''et al.'' |title=Generation of the neutrophil-activating peptide-2 by cathepsin G and cathepsin G-treated human platelets. |journal=Am. J. Physiol. |volume=263 |issue= 2 Pt 1 |pages= L249-56 |year= 1992 |pmid= 1387511 |doi= }}
*{{cite journal | author=Sasaki T, Ueno-Matsuda E |title=Immunocytochemical localization of cathepsins B and G in odontoclasts of human deciduous teeth. |journal=J. Dent. Res. |volume=71 |issue= 12 |pages= 1881-4 |year= 1993 |pmid= 1452887 |doi= }}
*{{cite journal | author=Maison CM, Villiers CL, Colomb MG |title=Proteolysis of C3 on U937 cell plasma membranes. Purification of cathepsin G. |journal=J. Immunol. |volume=147 |issue= 3 |pages= 921-6 |year= 1991 |pmid= 1861080 |doi= }}
*{{cite journal | author=Brandt E, Van Damme J, Flad HD |title=Neutrophils can generate their activator neutrophil-activating peptide 2 by proteolytic cleavage of platelet-derived connective tissue-activating peptide III. |journal=Cytokine |volume=3 |issue= 4 |pages= 311-21 |year= 1991 |pmid= 1873479 |doi= }}
*{{cite journal | author=Kargi HA, Campbell EJ, Kuhn C |title=Elastase and cathepsin G of human monocytes: heterogeneity and subcellular localization to peroxidase-positive granules. |journal=J. Histochem. Cytochem. |volume=38 |issue= 8 |pages= 1179-86 |year= 1990 |pmid= 2164060 |doi= }}
*{{cite journal | author=Pratt CW, Tobin RB, Church FC |title=Interaction of heparin cofactor II with neutrophil elastase and cathepsin G. |journal=J. Biol. Chem. |volume=265 |issue= 11 |pages= 6092-7 |year= 1990 |pmid= 2318847 |doi= }}
*{{cite journal | author=Gabay JE, Scott RW, Campanelli D, ''et al.'' |title=Antibiotic proteins of human polymorphonuclear leukocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 14 |pages= 5610-4 |year= 1989 |pmid= 2501794 |doi= }}
*{{cite journal | author=Hohn PA, Popescu NC, Hanson RD, ''et al.'' |title=Genomic organization and chromosomal localization of the human cathepsin G gene. |journal=J. Biol. Chem. |volume=264 |issue= 23 |pages= 13412-9 |year= 1989 |pmid= 2569462 |doi= }}
*{{cite journal | author=Livesey SA, Buescher ES, Krannig GL, ''et al.'' |title=Human neutrophil granule heterogeneity: immunolocalization studies using cryofixed, dried and embedded specimens. |journal=Scanning Microsc. Suppl. |volume=3 |issue= |pages= 231-9; discussion 239-40 |year= 1990 |pmid= 2616953 |doi= }}
*{{cite journal | author=Campbell EJ, Silverman EK, Campbell MA |title=Elastase and cathepsin G of human monocytes. Quantification of cellular content, release in response to stimuli, and heterogeneity in elastase-mediated proteolytic activity. |journal=J. Immunol. |volume=143 |issue= 9 |pages= 2961-8 |year= 1989 |pmid= 2681419 |doi= }}
*{{cite journal | author=Salvesen G, Farley D, Shuman J, ''et al.'' |title=Molecular cloning of human cathepsin G: structural similarity to mast cell and cytotoxic T lymphocyte proteinases. |journal=Biochemistry |volume=26 |issue= 8 |pages= 2289-93 |year= 1987 |pmid= 3304423 |doi= }}
*{{cite journal | author=Heck LW, Rostand KS, Hunter FA, Bhown A |title=Isolation, characterization, and amino-terminal amino acid sequence analysis of human neutrophil cathepsin G from normal donors. |journal=Anal. Biochem. |volume=158 |issue= 1 |pages= 217-27 |year= 1987 |pmid= 3799965 |doi= }}
*{{cite journal | author=Crocker J, Jenkins R, Burnett D |title=Immunohistochemical localization of cathepsin G in human tissues. |journal=Am. J. Surg. Pathol. |volume=9 |issue= 5 |pages= 338-43 |year= 1986 |pmid= 3911778 |doi= }}
*{{cite journal | author=Klickstein LB, Kaempfer CE, Wintroub BU |title=The granulocyte-angiotensin system. Angiotensin I-converting activity of cathepsin G. |journal=J. Biol. Chem. |volume=257 |issue= 24 |pages= 15042-6 |year= 1983 |pmid= 6294088 |doi= }}
*{{cite journal | author=LaRosa CA, Rohrer MJ, Benoit SE, ''et al.'' |title=Neutrophil cathepsin G modulates the platelet surface expression of the glycoprotein (GP) Ib-IX complex by proteolysis of the von Willebrand factor binding site on GPIb alpha and by a cytoskeletal-mediated redistribution of the remainder of the complex. |journal=Blood |volume=84 |issue= 1 |pages= 158-68 |year= 1994 |pmid= 7517206 |doi= }}
*{{cite journal | author=Owen CA, Campbell MA, Sannes PL, ''et al.'' |title=Cell surface-bound elastase and cathepsin G on human neutrophils: a novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases. |journal=J. Cell Biol. |volume=131 |issue= 3 |pages= 775-89 |year= 1995 |pmid= 7593196 |doi= }}
*{{cite journal | author=Savage MJ, Iqbal M, Loh T, ''et al.'' |title=Cathepsin G: localization in human cerebral cortex and generation of amyloidogenic fragments from the beta-amyloid precursor protein. |journal=Neuroscience |volume=60 |issue= 3 |pages= 607-19 |year= 1994 |pmid= 7936190 |doi= }}
*{{cite journal | author=Grisolano JL, Sclar GM, Ley TJ |title=Early myeloid cell-specific expression of the human cathepsin G gene in transgenic mice. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 19 |pages= 8989-93 |year= 1994 |pmid= 8090757 |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= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HIST3H3... {November 14, 2007 5:28:17 PM PST}
- SEARCH REDIRECT: Control Box Found: HIST3H3 {November 14, 2007 5:28:56 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 5:28:57 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 5:28:57 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 5:28:57 PM PST}
- UPDATED: Updated protein page: HIST3H3 {November 14, 2007 5:29:03 PM PST}
- INFO: Beginning work on HP... {November 14, 2007 5:19:19 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:19:52 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 =
| image_source =
| PDB =
| Name = Haptoglobin
| HGNCid = 5141
| Symbol = HP
| AltSymbols =; MGC111141; hp2-alpha
| OMIM = 140100
| ECnumber =
| Homologene =
| MGIid =
| GeneAtlas_image1 = PBB_GE_HP_206697_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_HP_208470_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004252 |text = serine-type endopeptidase activity}} {{GNF_GO|id=GO:0030492 |text = hemoglobin binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006879 |text = cellular iron ion homeostasis}} {{GNF_GO|id=GO:0006952 |text = defense response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3240
| Hs_Ensembl = ENSG00000197711
| Hs_RefseqProtein = NP_005134
| Hs_RefseqmRNA = NM_005143
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 70646009
| Hs_GenLoc_end = 70652441
| Hs_Uniprot = P00738
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Haptoglobin''', also known as '''HP''', 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=Graversen JH, Madsen M, Moestrup SK |title=CD163: a signal receptor scavenging haptoglobin-hemoglobin complexes from plasma. |journal=Int. J. Biochem. Cell Biol. |volume=34 |issue= 4 |pages= 309-14 |year= 2002 |pmid= 11854028 |doi= }}
*{{cite journal | author=Madsen M, Graversen JH, Moestrup SK |title=Haptoglobin and CD163: captor and receptor gating hemoglobin to macrophage lysosomes. |journal=Redox Rep. |volume=6 |issue= 6 |pages= 386-8 |year= 2002 |pmid= 11865982 |doi= }}
*{{cite journal | author=Erickson LM, Kim HS, Maeda N |title=Junctions between genes in the haptoglobin gene cluster of primates. |journal=Genomics |volume=14 |issue= 4 |pages= 948-58 |year= 1993 |pmid= 1478675 |doi= }}
*{{cite journal | author=Maeda N |title=Nucleotide sequence of the haptoglobin and haptoglobin-related gene pair. The haptoglobin-related gene contains a retrovirus-like element. |journal=J. Biol. Chem. |volume=260 |issue= 11 |pages= 6698-709 |year= 1985 |pmid= 2987228 |doi= }}
*{{cite journal | author=Simmers RN, Stupans I, Sutherland GR |title=Localization of the human haptoglobin genes distal to the fragile site at 16q22 using in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=41 |issue= 1 |pages= 38-41 |year= 1986 |pmid= 3455911 |doi= }}
*{{cite journal | author=van der Straten A, Falque JC, Loriau R, ''et al.'' |title=Expression of cloned human haptoglobin and alpha 1-antitrypsin complementary DNAs in Saccharomyces cerevisiae. |journal=DNA |volume=5 |issue= 2 |pages= 129-36 |year= 1986 |pmid= 3519135 |doi= }}
*{{cite journal | author=Bensi G, Raugei G, Klefenz H, Cortese R |title=Structure and expression of the human haptoglobin locus. |journal=EMBO J. |volume=4 |issue= 1 |pages= 119-26 |year= 1985 |pmid= 4018023 |doi= }}
*{{cite journal | author=Malchy B, Dixon GH |title=Studies on the interchain disulfides of human haptoglobins. |journal=Can. J. Biochem. |volume=51 |issue= 3 |pages= 249-64 |year= 1973 |pmid= 4573324 |doi= }}
*{{cite journal | author=Raugei G, Bensi G, Colantuoni V, ''et al.'' |title=Sequence of human haptoglobin cDNA: evidence that the alpha and beta subunits are coded by the same mRNA. |journal=Nucleic Acids Res. |volume=11 |issue= 17 |pages= 5811-9 |year= 1983 |pmid= 6310515 |doi= }}
*{{cite journal | author=Yang F, Brune JL, Baldwin WD, ''et al.'' |title=Identification and characterization of human haptoglobin cDNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=80 |issue= 19 |pages= 5875-9 |year= 1983 |pmid= 6310599 |doi= }}
*{{cite journal | author=Maeda N, Yang F, Barnett DR, ''et al.'' |title=Duplication within the haptoglobin Hp2 gene. |journal=Nature |volume=309 |issue= 5964 |pages= 131-5 |year= 1984 |pmid= 6325933 |doi= }}
*{{cite journal | author=Brune JL, Yang F, Barnett DR, Bowman BH |title=Evolution of haptoglobin: comparison of complementary DNA encoding Hp alpha 1S and Hp alpha 2FS. |journal=Nucleic Acids Res. |volume=12 |issue= 11 |pages= 4531-8 |year= 1984 |pmid= 6330675 |doi= }}
*{{cite journal | author=van der Straten A, Herzog A, Cabezón T, Bollen A |title=Characterization of human haptoglobin cDNAs coding for alpha 2FS beta and alpha 1S beta variants. |journal=FEBS Lett. |volume=168 |issue= 1 |pages= 103-7 |year= 1984 |pmid= 6546723 |doi= }}
*{{cite journal | author=vander Straten A, Herzog A, Jacobs P, ''et al.'' |title=Molecular cloning of human haptoglobin cDNA: evidence for a single mRNA coding for alpha 2 and beta chains. |journal=EMBO J. |volume=2 |issue= 6 |pages= 1003-7 |year= 1984 |pmid= 6688992 |doi= }}
*{{cite journal | author=Kurosky A, Barnett DR, Lee TH, ''et al.'' |title=Covalent structure of human haptoglobin: a serine protease homolog. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=77 |issue= 6 |pages= 3388-92 |year= 1980 |pmid= 6997877 |doi= }}
*{{cite journal | author=Eaton JW, Brandt P, Mahoney JR, Lee JT |title=Haptoglobin: a natural bacteriostat. |journal=Science |volume=215 |issue= 4533 |pages= 691-3 |year= 1982 |pmid= 7036344 |doi= }}
*{{cite journal | author=Kazim AL, Atassi MZ |title=Haemoglobin binding with haptoglobin. Unequivocal demonstration that the beta-chains of human haemoglobin bind to haptoglobin. |journal=Biochem. J. |volume=185 |issue= 1 |pages= 285-7 |year= 1980 |pmid= 7378053 |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=Tabak S, Lev A, Valansi C, ''et al.'' |title=Transcriptionally active haptoglobin-related (Hpr) gene in hepatoma G2 and leukemia molt-4 cells. |journal=DNA Cell Biol. |volume=15 |issue= 11 |pages= 1001-7 |year= 1997 |pmid= 8945641 |doi= }}
*{{cite journal | author=Koda Y, Soejima M, Yoshioka N, Kimura H |title=The haptoglobin-gene deletion responsible for anhaptoglobinemia. |journal=Am. J. Hum. Genet. |volume=62 |issue= 2 |pages= 245-52 |year= 1998 |pmid= 9463309 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IGFBP5... {November 14, 2007 5:19:52 PM PST}
- SEARCH REDIRECT: Control Box Found: IGFBP5 {November 14, 2007 5:20:44 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 5:20:45 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 5:20:45 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 5:20:45 PM PST}
- UPDATED: Updated protein page: IGFBP5 {November 14, 2007 5:20:51 PM PST}
- INFO: Beginning work on JUP... {November 14, 2007 5:20:51 PM PST}
- SEARCH REDIRECT: Control Box Found: JUP {November 14, 2007 5:21:30 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 5:21:33 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 5:21:33 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 5:21:33 PM PST}
- UPDATED: Updated protein page: JUP {November 14, 2007 5:21:40 PM PST}
- INFO: Beginning work on MUC2... {November 14, 2007 5:21:40 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:22:07 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Mucin 2, oligomeric mucus/gel-forming
| HGNCid = 7512
| Symbol = MUC2
| AltSymbols =; MLP; SMUC
| OMIM = 158370
| ECnumber =
| Homologene = 80094
| MGIid =
| Function = {{GNF_GO|id=GO:0005201 |text = extracellular matrix structural constituent}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0030197 |text = extracellular matrix constituent, lubricant activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0008150 |text = biological_process}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0030277 |text = maintenance of gastrointestinal epithelium}} {{GNF_GO|id=GO:0030336 |text = negative regulation of cell migration}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4583
| Hs_Ensembl =
| Hs_RefseqProtein = NP_002448
| Hs_RefseqmRNA = NM_002457
| 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 =
}}
}}
'''Mucin 2, oligomeric mucus/gel-forming''', also known as '''MUC2''', 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 mucin protein family. Mucins are high molecular weight glycoproteins produced by many epithelial tissues. The protein encoded by this gene is secreted and forms an insoluble mucous barrier that protects the gut lumen. The protein polymerizes into a gel of which 80% is composed of oligosaccharide side chains by weight. The protein features a central domain containing tandem repeats rich in threonine and proline that varies between 50 and 115 copies in different individuals. Alternatively spliced transcript variants of this gene have been described, but their full-length nature is not known.<ref>{{cite web | title = Entrez Gene: MUC2 mucin 2, oligomeric mucus/gel-forming| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4583| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Allen A, Hutton DA, Pearson JP |title=The MUC2 gene product: a human intestinal mucin. |journal=Int. J. Biochem. Cell Biol. |volume=30 |issue= 7 |pages= 797-801 |year= 1998 |pmid= 9722984 |doi= }}
*{{cite journal | author=Byrd JC, Bresalier RS |title=Mucins and mucin binding proteins in colorectal cancer. |journal=Cancer Metastasis Rev. |volume=23 |issue= 1-2 |pages= 77-99 |year= 2004 |pmid= 15000151 |doi= }}
*{{cite journal | author=Gum JR, Hicks JW, Toribara NW, ''et al.'' |title=The human MUC2 intestinal mucin has cysteine-rich subdomains located both upstream and downstream of its central repetitive region. |journal=J. Biol. Chem. |volume=267 |issue= 30 |pages= 21375-83 |year= 1992 |pmid= 1400449 |doi= }}
*{{cite journal | author=Xu G, Huan L, Khatri I, ''et al.'' |title=Human intestinal mucin-like protein (MLP) is homologous with rat MLP in the C-terminal region, and is encoded by a gene on chromosome 11 p 15.5. |journal=Biochem. Biophys. Res. Commun. |volume=183 |issue= 2 |pages= 821-8 |year= 1992 |pmid= 1550588 |doi= }}
*{{cite journal | author=Toribara NW, Gum JR, Culhane PJ, ''et al.'' |title=MUC-2 human small intestinal mucin gene structure. Repeated arrays and polymorphism. |journal=J. Clin. Invest. |volume=88 |issue= 3 |pages= 1005-13 |year= 1991 |pmid= 1885763 |doi= }}
*{{cite journal | author=Griffiths B, Matthews DJ, West L, ''et al.'' |title=Assignment of the polymorphic intestinal mucin gene (MUC2) to chromosome 11p15. |journal=Ann. Hum. Genet. |volume=54 |issue= Pt 4 |pages= 277-85 |year= 1991 |pmid= 1980995 |doi= }}
*{{cite journal | author=Jany BH, Gallup MW, Yan PS, ''et al.'' |title=Human bronchus and intestine express the same mucin gene. |journal=J. Clin. Invest. |volume=87 |issue= 1 |pages= 77-82 |year= 1991 |pmid= 1985113 |doi= }}
*{{cite journal | author=Gerard C, Eddy RL, Shows TB |title=The core polypeptide of cystic fibrosis tracheal mucin contains a tandem repeat structure. Evidence for a common mucin in airway and gastrointestinal tissue. |journal=J. Clin. Invest. |volume=86 |issue= 6 |pages= 1921-7 |year= 1991 |pmid= 2254452 |doi= }}
*{{cite journal | author=Nguyen VC, Aubert JP, Gross MS, ''et al.'' |title=Assignment of human tracheobronchial mucin gene(s) to 11p15 and a tracheobronchial mucin-related sequence to chromosome 13. |journal=Hum. Genet. |volume=86 |issue= 2 |pages= 167-72 |year= 1991 |pmid= 2265829 |doi= }}
*{{cite journal | author=Gum JR, Byrd JC, Hicks JW, ''et al.'' |title=Molecular cloning of human intestinal mucin cDNAs. Sequence analysis and evidence for genetic polymorphism. |journal=J. Biol. Chem. |volume=264 |issue= 11 |pages= 6480-7 |year= 1989 |pmid= 2703501 |doi= }}
*{{cite journal | author=Shankar V, Gilmore MS, Sachdev GP |title=Further evidence that the human MUC2 gene transcripts in the intestine and trachea are identical. |journal=Biochem. J. |volume=306 ( Pt 1) |issue= |pages= 311-2 |year= 1995 |pmid= 7864825 |doi= }}
*{{cite journal | author=Tytgat KM, Büller HA, Opdam FJ, ''et al.'' |title=Biosynthesis of human colonic mucin: Muc2 is the prominent secretory mucin. |journal=Gastroenterology |volume=107 |issue= 5 |pages= 1352-63 |year= 1994 |pmid= 7926500 |doi= }}
*{{cite journal | author=Gum JR, Hicks JW, Toribara NW, ''et al.'' |title=Molecular cloning of human intestinal mucin (MUC2) cDNA. Identification of the amino terminus and overall sequence similarity to prepro-von Willebrand factor. |journal=J. Biol. Chem. |volume=269 |issue= 4 |pages= 2440-6 |year= 1994 |pmid= 8300571 |doi= }}
*{{cite journal | author=Pigny P, Guyonnet-Duperat V, Hill AS, ''et al.'' |title=Human mucin genes assigned to 11p15.5: identification and organization of a cluster of genes. |journal=Genomics |volume=38 |issue= 3 |pages= 340-52 |year= 1997 |pmid= 8975711 |doi= 10.1006/geno.1996.0637 }}
*{{cite journal | author=Velcich A, Palumbo L, Selleri L, ''et al.'' |title=Organization and regulatory aspects of the human intestinal mucin gene (MUC2) locus. |journal=J. Biol. Chem. |volume=272 |issue= 12 |pages= 7968-76 |year= 1997 |pmid= 9065467 |doi= }}
*{{cite journal | author=Gum JR, Hicks JW, Kim YS |title=Identification and characterization of the MUC2 (human intestinal mucin) gene 5'-flanking region: promoter activity in cultured cells. |journal=Biochem. J. |volume=325 ( Pt 1) |issue= |pages= 259-67 |year= 1997 |pmid= 9224654 |doi= }}
*{{cite journal | author=Eckhardt AE, Timpte CS, DeLuca AW, Hill RL |title=The complete cDNA sequence and structural polymorphism of the polypeptide chain of porcine submaxillary mucin. |journal=J. Biol. Chem. |volume=272 |issue= 52 |pages= 33204-10 |year= 1998 |pmid= 9407109 |doi= }}
*{{cite journal | author=Asker N, Axelsson MA, Olofsson SO, Hansson GC |title=Dimerization of the human MUC2 mucin in the endoplasmic reticulum is followed by a N-glycosylation-dependent transfer of the mono- and dimers to the Golgi apparatus. |journal=J. Biol. Chem. |volume=273 |issue= 30 |pages= 18857-63 |year= 1998 |pmid= 9668061 |doi= }}
*{{cite journal | author=Retz M, Lehmann J, Röder C, ''et al.'' |title=Differential mucin MUC7 gene expression in invasive bladder carcinoma in contrast to uniform MUC1 and MUC2 gene expression in both normal urothelium and bladder carcinoma. |journal=Cancer Res. |volume=58 |issue= 24 |pages= 5662-6 |year= 1999 |pmid= 9865718 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NCOA2... {November 14, 2007 5:29:45 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:30:25 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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| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Nuclear receptor coactivator 2
| HGNCid = 7669
| Symbol = NCOA2
| AltSymbols =; GRIP1; MGC138808; NCoA-2; TIF2
| OMIM = 601993
| ECnumber =
| Homologene = 4768
| MGIid = 1276533
| GeneAtlas_image1 = PBB_GE_NCOA2_gnf1h04995_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0016564 |text = transcription repressor activity}} {{GNF_GO|id=GO:0030375 |text = thyroid hormone receptor coactivator activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10499
| Hs_Ensembl = ENSG00000140396
| Hs_RefseqProtein = NP_006531
| Hs_RefseqmRNA = NM_006540
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 71196006
| Hs_GenLoc_end = 71478574
| Hs_Uniprot = Q15596
| Mm_EntrezGene = 17978
| Mm_Ensembl = ENSMUSG00000005886
| Mm_RefseqmRNA = NM_001077695
| Mm_RefseqProtein = NP_001071163
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 13127689
| Mm_GenLoc_end = 13359278
| Mm_Uniprot = Q61026
}}
}}
'''Nuclear receptor coactivator 2''', also known as '''NCOA2''', 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=Voegel JJ, Heine MJ, Zechel C, ''et al.'' |title=TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors. |journal=EMBO J. |volume=15 |issue= 14 |pages= 3667-75 |year= 1996 |pmid= 8670870 |doi= }}
*{{cite journal | author=Hong H, Kohli K, Garabedian MJ, Stallcup MR |title=GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors. |journal=Mol. Cell. Biol. |volume=17 |issue= 5 |pages= 2735-44 |year= 1997 |pmid= 9111344 |doi= }}
*{{cite journal | author=Voegel JJ, Heine MJ, Tini M, ''et al.'' |title=The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways. |journal=EMBO J. |volume=17 |issue= 2 |pages= 507-19 |year= 1998 |pmid= 9430642 |doi= 10.1093/emboj/17.2.507 }}
*{{cite journal | author=Carapeti M, Aguiar RC, Goldman JM, Cross NC |title=A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in acute myeloid leukemia. |journal=Blood |volume=91 |issue= 9 |pages= 3127-33 |year= 1998 |pmid= 9558366 |doi= }}
*{{cite journal | author=Fryer CJ, Archer TK |title=Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex. |journal=Nature |volume=393 |issue= 6680 |pages= 88-91 |year= 1998 |pmid= 9590696 |doi= 10.1038/30032 }}
*{{cite journal | author=Berrevoets CA, Doesburg P, Steketee K, ''et al.'' |title=Functional interactions of the AF-2 activation domain core region of the human androgen receptor with the amino-terminal domain and with the transcriptional coactivator TIF2 (transcriptional intermediary factor2). |journal=Mol. Endocrinol. |volume=12 |issue= 8 |pages= 1172-83 |year= 1998 |pmid= 9717843 |doi= }}
*{{cite journal | author=Wang JC, Stafford JM, Granner DK |title=SRC-1 and GRIP1 coactivate transcription with hepatocyte nuclear factor 4. |journal=J. Biol. Chem. |volume=273 |issue= 47 |pages= 30847-50 |year= 1998 |pmid= 9812974 |doi= }}
*{{cite journal | author=Hong H, Darimont BD, Ma H, ''et al.'' |title=An additional region of coactivator GRIP1 required for interaction with the hormone-binding domains of a subset of nuclear receptors. |journal=J. Biol. Chem. |volume=274 |issue= 6 |pages= 3496-502 |year= 1999 |pmid= 9920895 |doi= }}
*{{cite journal | author=Chen D, Ma H, Hong H, ''et al.'' |title=Regulation of transcription by a protein methyltransferase. |journal=Science |volume=284 |issue= 5423 |pages= 2174-7 |year= 1999 |pmid= 10381882 |doi= }}
*{{cite journal | author=Ma H, Hong H, Huang SM, ''et al.'' |title=Multiple signal input and output domains of the 160-kilodalton nuclear receptor coactivator proteins. |journal=Mol. Cell. Biol. |volume=19 |issue= 9 |pages= 6164-73 |year= 1999 |pmid= 10454563 |doi= }}
*{{cite journal | author=Atkins GB, Hu X, Guenther MG, ''et al.'' |title=Coactivators for the orphan nuclear receptor RORalpha. |journal=Mol. Endocrinol. |volume=13 |issue= 9 |pages= 1550-7 |year= 1999 |pmid= 10478845 |doi= }}
*{{cite journal | author=Carrero P, Okamoto K, Coumailleau P, ''et al.'' |title=Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha. |journal=Mol. Cell. Biol. |volume=20 |issue= 1 |pages= 402-15 |year= 2000 |pmid= 10594042 |doi= }}
*{{cite journal | author=Xie W, Hong H, Yang NN, ''et al.'' |title=Constitutive activation of transcription and binding of coactivator by estrogen-related receptors 1 and 2. |journal=Mol. Endocrinol. |volume=13 |issue= 12 |pages= 2151-62 |year= 2000 |pmid= 10598588 |doi= }}
*{{cite journal | author=Naltner A, Ghaffari M, Whitsett JA, Yan C |title=Retinoic acid stimulation of the human surfactant protein B promoter is thyroid transcription factor 1 site-dependent. |journal=J. Biol. Chem. |volume=275 |issue= 1 |pages= 56-62 |year= 2000 |pmid= 10617585 |doi= }}
*{{cite journal | author=Jimenez-Lara AM, Heine MJ, Gronemeyer H |title=Cloning of a mouse glucocorticoid modulatory element binding protein, a new member of the KDWK family. |journal=FEBS Lett. |volume=468 |issue= 2-3 |pages= 203-10 |year= 2000 |pmid= 10692587 |doi= }}
*{{cite journal | author=Poelzl G, Kasai Y, Mochizuki N, ''et al.'' |title=Specific association of estrogen receptor beta with the cell cycle spindle assembly checkpoint protein, MAD2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 6 |pages= 2836-9 |year= 2000 |pmid= 10706629 |doi= 10.1073/pnas.050580997 }}
*{{cite journal | author=Herdick M, Steinmeyer A, Carlberg C |title=Antagonistic action of a 25-carboxylic ester analogue of 1alpha, 25-dihydroxyvitamin D3 is mediated by a lack of ligand-induced vitamin D receptor interaction with coactivators. |journal=J. Biol. Chem. |volume=275 |issue= 22 |pages= 16506-12 |year= 2000 |pmid= 10748178 |doi= 10.1074/jbc.M910000199 }}
*{{cite journal | author=Kodera Y, Takeyama K, Murayama A, ''et al.'' |title=Ligand type-specific interactions of peroxisome proliferator-activated receptor gamma with transcriptional coactivators. |journal=J. Biol. Chem. |volume=275 |issue= 43 |pages= 33201-4 |year= 2000 |pmid= 10944516 |doi= 10.1074/jbc.C000517200 }}
*{{cite journal | author=Koh SS, Chen D, Lee YH, Stallcup MR |title=Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities. |journal=J. Biol. Chem. |volume=276 |issue= 2 |pages= 1089-98 |year= 2001 |pmid= 11050077 |doi= 10.1074/jbc.M004228200 }}
*{{cite journal | author=Park JJ, Irvine RA, Buchanan G, ''et al.'' |title=Breast cancer susceptibility gene 1 (BRCAI) is a coactivator of the androgen receptor. |journal=Cancer Res. |volume=60 |issue= 21 |pages= 5946-9 |year= 2000 |pmid= 11085509 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PF4... {November 14, 2007 5:22:07 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:22:36 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PF4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1f9q.
| PDB = {{PDB2|1f9q}}, {{PDB2|1f9r}}, {{PDB2|1f9s}}, {{PDB2|1pfm}}, {{PDB2|1pfn}}, {{PDB2|1rhp}}
| Name = Platelet factor 4 (chemokine (C-X-C motif) ligand 4)
| HGNCid = 8861
| Symbol = PF4
| AltSymbols =; CXCL4; MGC138298; SCYB4
| OMIM = 173460
| ECnumber =
| Homologene = 87791
| MGIid = 1888711
| GeneAtlas_image1 = PBB_GE_PF4_206390_x_at_tn.png
| Function = {{GNF_GO|id=GO:0008009 |text = chemokine activity}} {{GNF_GO|id=GO:0008201 |text = heparin binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0016525 |text = negative regulation of angiogenesis}} {{GNF_GO|id=GO:0019221 |text = cytokine and chemokine mediated signaling pathway}} {{GNF_GO|id=GO:0030168 |text = platelet activation}} {{GNF_GO|id=GO:0030595 |text = leukocyte chemotaxis}} {{GNF_GO|id=GO:0045653 |text = negative regulation of megakaryocyte differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5196
| Hs_Ensembl = ENSG00000163737
| Hs_RefseqProtein = NP_002610
| Hs_RefseqmRNA = NM_002619
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 75065660
| Hs_GenLoc_end = 75066541
| Hs_Uniprot = P02776
| Mm_EntrezGene = 56744
| Mm_Ensembl = ENSMUSG00000029373
| Mm_RefseqmRNA = NM_019932
| Mm_RefseqProtein = NP_064316
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 91847703
| Mm_GenLoc_end = 91848577
| Mm_Uniprot = Q3TVN6
}}
}}
'''Platelet factor 4 (chemokine (C-X-C motif) ligand 4)''', also known as '''PF4''', 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 factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets and binds with high affinity to heparin. Its major physiologic role appears to be neutralization of heparin-like molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair (Eisman et al., 1990).[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: PF4 platelet factor 4 (chemokine (C-X-C motif) ligand 4)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5196| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bikfalvi A, Gimenez-Gallego G |title=The control of angiogenesis and tumor invasion by platelet factor-4 and platelet factor-4-derived molecules. |journal=Semin. Thromb. Hemost. |volume=30 |issue= 1 |pages= 137-44 |year= 2004 |pmid= 15034805 |doi= 10.1055/s-2004-822978 }}
*{{cite journal | author=Maurer AM, Zhou B, Han ZC |title=Roles of platelet factor 4 in hematopoiesis and angiogenesis. |journal=Growth Factors |volume=24 |issue= 4 |pages= 242-52 |year= 2007 |pmid= 17381065 |doi= }}
*{{cite journal | author=Deuel TF, Keim PS, Farmer M, Heinrikson RL |title=Amino acid sequence of human platelet factor 4. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=74 |issue= 6 |pages= 2256-8 |year= 1977 |pmid= 267922 |doi= }}
*{{cite journal | author=Walz DA, Wu VY, de Lamo R, ''et al.'' |title=Primary structure of human platelet factor 4. |journal=Thromb. Res. |volume=11 |issue= 6 |pages= 893-8 |year= 1978 |pmid= 601757 |doi= }}
*{{cite journal | author=Nath N, Lowery CT, Niewiarowski S |title=Antigenic and antiheparin properties of human platelet factor 4 (PF4). |journal=Blood |volume=45 |issue= 4 |pages= 537-50 |year= 1975 |pmid= 803847 |doi= }}
*{{cite journal | author=Hermodson M, Schmer G, Kurachi K |title=Isolation, crystallization, and primary amino acid sequence of human platelet factor 4. |journal=J. Biol. Chem. |volume=252 |issue= 18 |pages= 6276-9 |year= 1977 |pmid= 893407 |doi= }}
*{{cite journal | author=Maione TE, Gray GS, Petro J, ''et al.'' |title=Inhibition of angiogenesis by recombinant human platelet factor-4 and related peptides. |journal=Science |volume=247 |issue= 4938 |pages= 77-9 |year= 1990 |pmid= 1688470 |doi= }}
*{{cite journal | author=Eisman R, Surrey S, Ramachandran B, ''et al.'' |title=Structural and functional comparison of the genes for human platelet factor 4 and PF4alt. |journal=Blood |volume=76 |issue= 2 |pages= 336-44 |year= 1990 |pmid= 1695112 |doi= }}
*{{cite journal | author=Han ZC, Bellucci S, Tenza D, Caen JP |title=Negative regulation of human megakaryocytopoiesis by human platelet factor 4 and beta thromboglobulin: comparative analysis in bone marrow cultures from normal individuals and patients with essential thrombocythaemia and immune thrombocytopenic purpura. |journal=Br. J. Haematol. |volume=74 |issue= 4 |pages= 395-401 |year= 1990 |pmid= 2140694 |doi= }}
*{{cite journal | author=Poncz M, Surrey S, LaRocco P, ''et al.'' |title=Cloning and characterization of platelet factor 4 cDNA derived from a human erythroleukemic cell line. |journal=Blood |volume=69 |issue= 1 |pages= 219-23 |year= 1987 |pmid= 3098319 |doi= }}
*{{cite journal | author=Griffin CA, Emanuel BS, LaRocco P, ''et al.'' |title=Human platelet factor 4 gene is mapped to 4q12----q21. |journal=Cytogenet. Cell Genet. |volume=45 |issue= 2 |pages= 67-9 |year= 1987 |pmid= 3622011 |doi= }}
*{{cite journal | author=Senior RM, Griffin GL, Huang JS, ''et al.'' |title=Chemotactic activity of platelet alpha granule proteins for fibroblasts. |journal=J. Cell Biol. |volume=96 |issue= 2 |pages= 382-5 |year= 1983 |pmid= 6187750 |doi= }}
*{{cite journal | author=Morgan FJ, Begg GS, Chesterman CN |title=Complete covalent structure of human platelet factor 4. |journal=Thromb. Haemost. |volume=42 |issue= 5 |pages= 1652-60 |year= 1980 |pmid= 6445090 |doi= }}
*{{cite journal | author=Deuel TF, Senior RM, Chang D, ''et al.'' |title=Platelet factor 4 is chemotactic for neutrophils and monocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=78 |issue= 7 |pages= 4584-7 |year= 1981 |pmid= 6945600 |doi= }}
*{{cite journal | author=Brown KJ, Parish CR |title=Histidine-rich glycoprotein and platelet factor 4 mask heparan sulfate proteoglycans recognized by acidic and basic fibroblast growth factor. |journal=Biochemistry |volume=33 |issue= 46 |pages= 13918-27 |year= 1994 |pmid= 7524669 |doi= }}
*{{cite journal | author=Mayo KH, Roongta V, Ilyina E, ''et al.'' |title=NMR solution structure of the 32-kDa platelet factor 4 ELR-motif N-terminal chimera: a symmetric tetramer. |journal=Biochemistry |volume=34 |issue= 36 |pages= 11399-409 |year= 1995 |pmid= 7547867 |doi= }}
*{{cite journal | author=Barker S, Mayo KH |title=Quarternary structure amplification of protein folding differences observed in 'native' platelet factor-4. |journal=FEBS Lett. |volume=357 |issue= 3 |pages= 301-4 |year= 1995 |pmid= 7835432 |doi= }}
*{{cite journal | author=Zhang X, Chen L, Bancroft DP, ''et al.'' |title=Crystal structure of recombinant human platelet factor 4. |journal=Biochemistry |volume=33 |issue= 27 |pages= 8361-6 |year= 1994 |pmid= 8031770 |doi= }}
*{{cite journal | author=Horne MK |title=The effect of secreted heparin-binding proteins on heparin binding to platelets. |journal=Thromb. Res. |volume=70 |issue= 1 |pages= 91-8 |year= 1993 |pmid= 8511754 |doi= }}
*{{cite journal | author=Kolset SO, Mann DM, Uhlin-Hansen L, ''et al.'' |title=Serglycin-binding proteins in activated macrophages and platelets. |journal=J. Leukoc. Biol. |volume=59 |issue= 4 |pages= 545-54 |year= 1996 |pmid= 8613703 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on POLR2K... {November 14, 2007 5:22:36 PM PST}
- SEARCH REDIRECT: Control Box Found: POLR2K {November 14, 2007 5:23:18 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 5:23:21 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 5:23:21 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 5:23:21 PM PST}
- UPDATED: Updated protein page: POLR2K {November 14, 2007 5:23:27 PM PST}
- INFO: Beginning work on REL... {November 14, 2007 5:23:27 PM PST}
- SEARCH REDIRECT: Control Box Found: REL {November 14, 2007 5:24:03 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 5:24:05 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 5:24:05 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 5:24:05 PM PST}
- UPDATED: Updated protein page: REL {November 14, 2007 5:24:12 PM PST}
- INFO: Beginning work on SOS1... {November 14, 2007 5:24:12 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:25:00 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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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_SOS1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1awe.
| PDB = {{PDB2|1awe}}, {{PDB2|1bkd}}, {{PDB2|1dbh}}, {{PDB2|1nvu}}, {{PDB2|1nvv}}, {{PDB2|1nvw}}, {{PDB2|1nvx}}, {{PDB2|1pms}}, {{PDB2|1q9c}}, {{PDB2|1xd2}}, {{PDB2|1xd4}}, {{PDB2|1xdv}}, {{PDB2|2ii0}}
| Name = Son of sevenless homolog 1 (Drosophila)
| HGNCid = 11187
| Symbol = SOS1
| AltSymbols =; GF1; HGF; GGF1; GINGF; NS4
| OMIM = 182530
| ECnumber =
| Homologene = 4117
| MGIid = 98354
| GeneAtlas_image1 = PBB_GE_SOS1_212777_at_tn.png
| GeneAtlas_image2 = PBB_GE_SOS1_212780_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0005085 |text = guanyl-nucleotide exchange factor activity}} {{GNF_GO|id=GO:0005089 |text = Rho guanyl-nucleotide exchange factor activity}} {{GNF_GO|id=GO:0005100 |text = Rho GTPase activator activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0000786 |text = nucleosome}} {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005694 |text = chromosome}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007265 |text = Ras protein signal transduction}} {{GNF_GO|id=GO:0035023 |text = regulation of Rho protein signal transduction}} {{GNF_GO|id=GO:0051056 |text = regulation of small GTPase mediated signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6654
| Hs_Ensembl = ENSG00000115904
| Hs_RefseqProtein = NP_005624
| Hs_RefseqmRNA = NM_005633
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 39066469
| Hs_GenLoc_end = 39201067
| Hs_Uniprot = Q07889
| Mm_EntrezGene = 20662
| Mm_Ensembl = ENSMUSG00000024241
| Mm_RefseqmRNA = NM_009231
| Mm_RefseqProtein = NP_033257
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 80306507
| Mm_GenLoc_end = 80388261
| Mm_Uniprot = Q2M4G6
}}
}}
'''Son of sevenless homolog 1 (Drosophila)''', also known as '''SOS1''', 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 = RAS genes (e.g., MIM 190020) encode membrane-bound guanine nucleotide-binding proteins that function in the transduction of signals that control cell growth and differentiation. Binding of GTP activates RAS proteins, and subsequent hydrolysis of the bound GTP to GDP and phosphate inactivates signaling by these proteins. GTP binding can be catalyzed by guanine nucleotide exchange factors for RAS, and GTP hydrolysis can be accelerated by GTPase-activating proteins (GAPs). The first exchange factor to be identified for RAS was the S. cerevisiae CDC25 gene product. Genetic analysis indicated that CDC25 is essential for activation of RAS proteins. In Drosophila, the protein encoded by the 'son of sevenless' gene (Sos) contains a domain that shows sequence similarity with the catalytic domain of CDC25. Sos may act as a positive regulator of RAS by promoting guanine nucleotide exchange.[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: SOS1 son of sevenless homolog 1 (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6654| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lioubin MN, Myles GM, Carlberg K, ''et al.'' |title=Shc, Grb2, Sos1, and a 150-kilodalton tyrosine-phosphorylated protein form complexes with Fms in hematopoietic cells. |journal=Mol. Cell. Biol. |volume=14 |issue= 9 |pages= 5682-91 |year= 1994 |pmid= 7520523 |doi= }}
*{{cite journal | author=Nel AE, Gupta S, Lee L, ''et al.'' |title=Ligation of the T-cell antigen receptor (TCR) induces association of hSos1, ZAP-70, phospholipase C-gamma 1, and other phosphoproteins with Grb2 and the zeta-chain of the TCR. |journal=J. Biol. Chem. |volume=270 |issue= 31 |pages= 18428-36 |year= 1995 |pmid= 7629168 |doi= }}
*{{cite journal | author=Pandey P, Kharbanda S, Kufe D |title=Association of the DF3/MUC1 breast cancer antigen with Grb2 and the Sos/Ras exchange protein. |journal=Cancer Res. |volume=55 |issue= 18 |pages= 4000-3 |year= 1995 |pmid= 7664271 |doi= }}
*{{cite journal | author=Hu Q, Milfay D, Williams LT |title=Binding of NCK to SOS and activation of ras-dependent gene expression. |journal=Mol. Cell. Biol. |volume=15 |issue= 3 |pages= 1169-74 |year= 1995 |pmid= 7862111 |doi= }}
*{{cite journal | author=Puil L, Liu J, Gish G, ''et al.'' |title=Bcr-Abl oncoproteins bind directly to activators of the Ras signalling pathway. |journal=EMBO J. |volume=13 |issue= 4 |pages= 764-73 |year= 1994 |pmid= 8112292 |doi= }}
*{{cite journal | author=Webb GC, Jenkins NA, Largaespada DA, ''et al.'' |title=Mammalian homologues of the Drosophila Son of sevenless gene map to murine chromosomes 17 and 12 and to human chromosomes 2 and 14, respectively. |journal=Genomics |volume=18 |issue= 1 |pages= 14-9 |year= 1994 |pmid= 8276400 |doi= 10.1006/geno.1993.1421 }}
*{{cite journal | author=Li N, Batzer A, Daly R, ''et al.'' |title=Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling. |journal=Nature |volume=363 |issue= 6424 |pages= 85-8 |year= 1993 |pmid= 8479541 |doi= 10.1038/363085a0 }}
*{{cite journal | author=Chardin P, Camonis JH, Gale NW, ''et al.'' |title=Human Sos1: a guanine nucleotide exchange factor for Ras that binds to GRB2. |journal=Science |volume=260 |issue= 5112 |pages= 1338-43 |year= 1993 |pmid= 8493579 |doi= }}
*{{cite journal | author=Sadoshima J, Izumo S |title=The heterotrimeric G q protein-coupled angiotensin II receptor activates p21 ras via the tyrosine kinase-Shc-Grb2-Sos pathway in cardiac myocytes. |journal=EMBO J. |volume=15 |issue= 4 |pages= 775-87 |year= 1996 |pmid= 8631299 |doi= }}
*{{cite journal | author=Feng GS, Ouyang YB, Hu DP, ''et al.'' |title=Grap is a novel SH3-SH2-SH3 adaptor protein that couples tyrosine kinases to the Ras pathway. |journal=J. Biol. Chem. |volume=271 |issue= 21 |pages= 12129-32 |year= 1996 |pmid= 8647802 |doi= }}
*{{cite journal | author=Okada S, Pessin JE |title=Interactions between Src homology (SH) 2/SH3 adapter proteins and the guanylnucleotide exchange factor SOS are differentially regulated by insulin and epidermal growth factor. |journal=J. Biol. Chem. |volume=271 |issue= 41 |pages= 25533-8 |year= 1996 |pmid= 8810325 |doi= }}
*{{cite journal | author=Corbalan-Garcia S, Yang SS, Degenhardt KR, Bar-Sagi D |title=Identification of the mitogen-activated protein kinase phosphorylation sites on human Sos1 that regulate interaction with Grb2. |journal=Mol. Cell. Biol. |volume=16 |issue= 10 |pages= 5674-82 |year= 1996 |pmid= 8816480 |doi= }}
*{{cite journal | author=Sattler M, Salgia R, Shrikhande G, ''et al.'' |title=Differential signaling after beta1 integrin ligation is mediated through binding of CRKL to p120(CBL) and p110(HEF1). |journal=J. Biol. Chem. |volume=272 |issue= 22 |pages= 14320-6 |year= 1997 |pmid= 9162067 |doi= }}
*{{cite journal | author=Leprince C, Romero F, Cussac D, ''et al.'' |title=A new member of the amphiphysin family connecting endocytosis and signal transduction pathways. |journal=J. Biol. Chem. |volume=272 |issue= 24 |pages= 15101-5 |year= 1997 |pmid= 9182529 |doi= }}
*{{cite journal | author=Kouhara H, Hadari YR, Spivak-Kroizman T, ''et al.'' |title=A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway. |journal=Cell |volume=89 |issue= 5 |pages= 693-702 |year= 1997 |pmid= 9182757 |doi= }}
*{{cite journal | author=Chin H, Saito T, Arai A, ''et al.'' |title=Erythropoietin and IL-3 induce tyrosine phosphorylation of CrkL and its association with Shc, SHP-2, and Cbl in hematopoietic cells. |journal=Biochem. Biophys. Res. Commun. |volume=239 |issue= 2 |pages= 412-7 |year= 1997 |pmid= 9344843 |doi= 10.1006/bbrc.1997.7480 }}
*{{cite journal | author=Zheng J, Chen RH, Corblan-Garcia S, ''et al.'' |title=The solution structure of the pleckstrin homology domain of human SOS1. A possible structural role for the sequential association of diffuse B cell lymphoma and pleckstrin homology domains. |journal=J. Biol. Chem. |volume=272 |issue= 48 |pages= 30340-4 |year= 1997 |pmid= 9374522 |doi= }}
*{{cite journal | author=Li S, Kim M, Hu YL, ''et al.'' |title=Fluid shear stress activation of focal adhesion kinase. Linking to mitogen-activated protein kinases. |journal=J. Biol. Chem. |volume=272 |issue= 48 |pages= 30455-62 |year= 1997 |pmid= 9374537 |doi= }}
*{{cite journal | author=Qian X, Vass WC, Papageorge AG, ''et al.'' |title=N terminus of Sos1 Ras exchange factor: critical roles for the Dbl and pleckstrin homology domains. |journal=Mol. Cell. Biol. |volume=18 |issue= 2 |pages= 771-8 |year= 1998 |pmid= 9447973 |doi= }}
*{{cite journal | author=Curto M, Frankel P, Carrero A, Foster DA |title=Novel recruitment of Shc, Grb2, and Sos by fibroblast growth factor receptor-1 in v-Src-transformed cells. |journal=Biochem. Biophys. Res. Commun. |volume=243 |issue= 2 |pages= 555-60 |year= 1998 |pmid= 9480847 |doi= 10.1006/bbrc.1997.7982 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SPAST... {November 14, 2007 5:25:00 PM PST}
- SEARCH REDIRECT: Control Box Found: SPAST {November 14, 2007 5:25:41 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 5:25:44 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 5:25:44 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 5:25:44 PM PST}
- UPDATED: Updated protein page: SPAST {November 14, 2007 5:25:50 PM PST}
- INFO: Beginning work on TUBA4A... {November 14, 2007 5:27:04 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:27:38 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_TUBA4A_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, alpha 4a
| HGNCid = 12407
| Symbol = TUBA4A
| AltSymbols =; FLJ30169; H2-ALPHA; TUBA1
| OMIM = 191110
| ECnumber =
| Homologene = 68496
| MGIid = 1095410
| GeneAtlas_image1 = PBB_GE_TUBA4A_212242_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{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 = 7277
| Hs_Ensembl = ENSG00000127824
| Hs_RefseqProtein = NP_005991
| Hs_RefseqmRNA = NM_006000
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 219822677
| Hs_GenLoc_end = 219826882
| Hs_Uniprot = P68366
| Mm_EntrezGene = 22145
| Mm_Ensembl = ENSMUSG00000026202
| Mm_RefseqmRNA = NM_009447
| Mm_RefseqProtein = NP_033473
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 75098770
| Mm_GenLoc_end = 75100582
| Mm_Uniprot = Q3TY31
}}
}}
'''Tubulin, alpha 4a''', also known as '''TUBA4A''', 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 = Microtubules of the eukaryotic cytoskeleton perform essential and diverse functions and are composed of a heterodimer of alpha and beta tubulin. The genes encoding these microtubule constituents are part of the tubulin superfamily, which is composed of six distinct families. Genes from the alpha, beta and gamma tubulin families are found in all eukaryotes. The alpha and beta tubulins represent the major components of microtubules, while gamma tubulin plays a critical role in the nucleation of microtubule assembly. There are multiple alpha and beta tubulin genes and they are highly conserved among and between species. This gene encodes an alpha tubulin that is a highly conserved homolog of a rat testis-specific alpha tubulin.<ref>{{cite web | title = Entrez Gene: TUBA4A tubulin, alpha 4a| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7277| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Desai A, Mitchison TJ |title=Tubulin and FtsZ structures: functional and therapeutic implications. |journal=Bioessays |volume=20 |issue= 7 |pages= 523-7 |year= 1998 |pmid= 9722999 |doi= 10.1002/(SICI)1521-1878(199807)20:7<523::AID-BIES1>3.0.CO;2-L }}
*{{cite journal | author=Oakley BR |title=An abundance of tubulins. |journal=Trends Cell Biol. |volume=10 |issue= 12 |pages= 537-42 |year= 2001 |pmid= 11121746 |doi= }}
*{{cite journal | author=Dutcher SK |title=The tubulin fraternity: alpha to eta. |journal=Curr. Opin. Cell Biol. |volume=13 |issue= 1 |pages= 49-54 |year= 2001 |pmid= 11163133 |doi= }}
*{{cite journal | author=Kirsch J, Langosch D, Prior P, ''et al.'' |title=The 93-kDa glycine receptor-associated protein binds to tubulin. |journal=J. Biol. Chem. |volume=266 |issue= 33 |pages= 22242-5 |year= 1991 |pmid= 1657993 |doi= }}
*{{cite journal | author=Dobner PR, Kislauskis E, Wentworth BM, Villa-Komaroff L |title=Alternative 5' exons either provide or deny an initiator methionine codon to the same alpha-tubulin coding region. |journal=Nucleic Acids Res. |volume=15 |issue= 1 |pages= 199-218 |year= 1987 |pmid= 3029670 |doi= }}
*{{cite journal | author=Villasante A, Wang D, Dobner P, ''et al.'' |title=Six mouse alpha-tubulin mRNAs encode five distinct isotypes: testis-specific expression of two sister genes. |journal=Mol. Cell. Biol. |volume=6 |issue= 7 |pages= 2409-19 |year= 1987 |pmid= 3785200 |doi= }}
*{{cite journal | author=Hall JL, Cowan NJ |title=Structural features and restricted expression of a human alpha-tubulin gene. |journal=Nucleic Acids Res. |volume=13 |issue= 1 |pages= 207-23 |year= 1985 |pmid= 3839072 |doi= }}
*{{cite journal | author=Alexandrova N, Niklinski J, Bliskovsky V, ''et al.'' |title=The N-terminal domain of c-Myc associates with alpha-tubulin and microtubules in vivo and in vitro. |journal=Mol. Cell. Biol. |volume=15 |issue= 9 |pages= 5188-95 |year= 1995 |pmid= 7651436 |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=Lu Q, Luduena RF |title=In vitro analysis of microtubule assembly of isotypically pure tubulin dimers. Intrinsic differences in the assembly properties of alpha beta II, alpha beta III, and alpha beta IV tubulin dimers in the absence of microtubule-associated proteins. |journal=J. Biol. Chem. |volume=269 |issue= 3 |pages= 2041-7 |year= 1994 |pmid= 8294455 |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=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=Marie-Cardine A, Kirchgessner H, Eckerskorn C, ''et al.'' |title=Human T lymphocyte activation induces tyrosine phosphorylation of alpha-tubulin and its association with the SH2 domain of the p59fyn protein tyrosine kinase. |journal=Eur. J. Immunol. |volume=25 |issue= 12 |pages= 3290-7 |year= 1996 |pmid= 8566014 |doi= }}
*{{cite journal | author=Peters JD, Furlong MT, Asai DJ, ''et al.'' |title=Syk, activated by cross-linking the B-cell antigen receptor, localizes to the cytosol where it interacts with and phosphorylates alpha-tubulin on tyrosine. |journal=J. Biol. Chem. |volume=271 |issue= 9 |pages= 4755-62 |year= 1996 |pmid= 8617742 |doi= }}
*{{cite journal | author=Best A, Ahmed S, Kozma R, Lim L |title=The Ras-related GTPase Rac1 binds tubulin. |journal=J. Biol. Chem. |volume=271 |issue= 7 |pages= 3756-62 |year= 1996 |pmid= 8631991 |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=Tian G, Lewis SA, Feierbach B, ''et al.'' |title=Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors. |journal=J. Cell Biol. |volume=138 |issue= 4 |pages= 821-32 |year= 1997 |pmid= 9265649 |doi= }}
*{{cite journal | author=Vaillant AR, Müller R, Langkopf A, Brown DL |title=Characterization of the microtubule-binding domain of microtubule-associated protein 1A and its effects on microtubule dynamics. |journal=J. Biol. Chem. |volume=273 |issue= 22 |pages= 13973-81 |year= 1998 |pmid= 9593747 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on YWHAH... {November 14, 2007 5:27:38 PM PST}
- SEARCH REDIRECT: Control Box Found: YWHAH {November 14, 2007 5:28:08 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 5:28:09 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 5:28:09 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 5:28:09 PM PST}
- UPDATED: Updated protein page: YWHAH {November 14, 2007 5:28:17 PM PST}
- INFO: Beginning work on YWHAQ... {November 14, 2007 5:30:25 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 5:31:12 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_YWHAQ_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2btp.
| PDB = {{PDB2|2btp}}
| Name = Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, theta polypeptide
| HGNCid = 12854
| Symbol = YWHAQ
| AltSymbols =; HS1; 14-3-3; 1C5
| OMIM = 609009
| ECnumber =
| Homologene = 48407
| MGIid = 891963
| GeneAtlas_image1 = PBB_GE_YWHAQ_212426_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_YWHAQ_200693_at_tn.png
| GeneAtlas_image3 = PBB_GE_YWHAQ_213699_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008426 |text = protein kinase C inhibitor activity}} {{GNF_GO|id=GO:0019904 |text = protein domain specific binding}}
| Component =
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006605 |text = protein targeting}} {{GNF_GO|id=GO:0006887 |text = exocytosis}} {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10971
| Hs_Ensembl = ENSG00000134308
| Hs_RefseqProtein = NP_006817
| Hs_RefseqmRNA = NM_006826
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 9641552
| Hs_GenLoc_end = 9688629
| Hs_Uniprot = P27348
| Mm_EntrezGene = 22630
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_011739
| Mm_RefseqProtein = NP_035869
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, theta polypeptide''', also known as '''YWHAQ''', 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 product belongs to the 14-3-3 family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins. This highly conserved protein family is found in both plants and mammals, and this protein is 99% identical to the mouse and rat orthologs. This gene is upregulated in patients with amyotrophic lateral sclerosis. It contains in its 5' UTR a 6 bp tandem repeat sequence which is polymorphic, however, there is no correlation between the repeat number and the disease.<ref>{{cite web | title = Entrez Gene: YWHAQ tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, theta polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10971| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kino T, Chrousos GP |title=Human immunodeficiency virus type-1 accessory protein Vpr: a causative agent of the AIDS-related insulin resistance/lipodystrophy syndrome? |journal=Ann. N. Y. Acad. Sci. |volume=1024 |issue= |pages= 153-67 |year= 2004 |pmid= 15265780 |doi= 10.1196/annals.1321.013 }}
*{{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=Nielsen PJ |title=Primary structure of a human protein kinase regulator protein. |journal=Biochim. Biophys. Acta |volume=1088 |issue= 3 |pages= 425-8 |year= 1991 |pmid= 2015305 |doi= }}
*{{cite journal | author=Bonnefoy-Bérard N, Liu YC, von Willebrand M, ''et al.'' |title=Inhibition of phosphatidylinositol 3-kinase activity by association with 14-3-3 proteins in T cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 22 |pages= 10142-6 |year= 1995 |pmid= 7479742 |doi= }}
*{{cite journal | author=Xiao B, Smerdon SJ, Jones DH, ''et al.'' |title=Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways. |journal=Nature |volume=376 |issue= 6536 |pages= 188-91 |year= 1995 |pmid= 7603573 |doi= 10.1038/376188a0 }}
*{{cite journal | author=Leffers H, Madsen P, Rasmussen HH, ''et al.'' |title=Molecular cloning and expression of the transformation sensitive epithelial marker stratifin. A member of a protein family that has been involved in the protein kinase C signalling pathway. |journal=J. Mol. Biol. |volume=231 |issue= 4 |pages= 982-98 |year= 1993 |pmid= 8515476 |doi= 10.1006/jmbi.1993.1346 }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal | author=Liu YC, Elly C, Yoshida H, ''et al.'' |title=Activation-modulated association of 14-3-3 proteins with Cbl in T cells. |journal=J. Biol. Chem. |volume=271 |issue= 24 |pages= 14591-5 |year= 1996 |pmid= 8663231 |doi= }}
*{{cite journal | author=Papin C, Denouel A, Calothy G, Eychène A |title=Identification of signalling proteins interacting with B-Raf in the yeast two-hybrid system. |journal=Oncogene |volume=12 |issue= 10 |pages= 2213-21 |year= 1996 |pmid= 8668348 |doi= }}
*{{cite journal | author=Zha J, Harada H, Yang E, ''et al.'' |title=Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L) |journal=Cell |volume=87 |issue= 4 |pages= 619-28 |year= 1997 |pmid= 8929531 |doi= }}
*{{cite journal | author=Suzuki Y, Demoliere C, Kitamura D, ''et al.'' |title=HAX-1, a novel intracellular protein, localized on mitochondria, directly associates with HS1, a substrate of Src family tyrosine kinases. |journal=J. Immunol. |volume=158 |issue= 6 |pages= 2736-44 |year= 1997 |pmid= 9058808 |doi= }}
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}}
{{refend}}
{{protein-stub}}
end log.
