- INFO: Beginning work on ATF3... {November 17, 2007 1:34:54 PM PST}
- SEARCH REDIRECT: Control Box Found: ATF3 {November 17, 2007 1:35:15 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 1:35:18 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 1:35:18 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 1:35:18 PM PST}
- UPDATED: Updated protein page: ATF3 {November 17, 2007 1:35:24 PM PST}
- INFO: Beginning work on CEL... {November 17, 2007 1:36:39 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:37:34 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| 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_CEL_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1f6w.
| PDB = {{PDB2|1f6w}}, {{PDB2|1jmy}}
| Name = Carboxyl ester lipase (bile salt-stimulated lipase)
| HGNCid = 1848
| Symbol = CEL
| AltSymbols =; FAP; BAL; BSDL; BSSL; CELL; CEase; FAPP; LIPA; MODY8
| OMIM = 114840
| ECnumber =
| Homologene = 37529
| MGIid = 88374
| GeneAtlas_image1 = PBB_GE_CEL_205910_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CEL_207412_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004759 |text = carboxylesterase activity}} {{GNF_GO|id=GO:0004771 |text = sterol esterase activity}} {{GNF_GO|id=GO:0004806 |text = triacylglycerol lipase activity}} {{GNF_GO|id=GO:0008201 |text = heparin binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006641 |text = triacylglycerol metabolic process}} {{GNF_GO|id=GO:0006707 |text = cholesterol catabolic process}} {{GNF_GO|id=GO:0009062 |text = fatty acid catabolic process}} {{GNF_GO|id=GO:0016042 |text = lipid catabolic process}} {{GNF_GO|id=GO:0018350 |text = protein amino acid esterification}} {{GNF_GO|id=GO:0030157 |text = pancreatic juice secretion}} {{GNF_GO|id=GO:0030299 |text = cholesterol absorption}} {{GNF_GO|id=GO:0044258 |text = intestinal lipid catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1056
| Hs_Ensembl = ENSG00000170835
| Hs_RefseqProtein = NP_001798
| Hs_RefseqmRNA = NM_001807
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 134927186
| Hs_GenLoc_end = 134937069
| Hs_Uniprot = P19835
| Mm_EntrezGene = 12613
| Mm_Ensembl = ENSMUSG00000026818
| Mm_RefseqmRNA = NM_009885
| Mm_RefseqProtein = NP_034015
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 28377831
| Mm_GenLoc_end = 28385375
| Mm_Uniprot = Q3V2H7
}}
}}
'''Carboxyl ester lipase (bile salt-stimulated lipase)''', also known as '''CEL''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CEL carboxyl ester lipase (bile salt-stimulated lipase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1056| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a glycoprotein secreted from the pancreas into the digestive tract and from the lactating mammary gland into human milk. The physiological role of this protein is in cholesterol and lipid-soluble vitamin ester hydrolysis and absorption. This encoded protein promotes large chylomicron production in the intestine. Also its presence in plasma suggests its interactions with cholesterol and oxidized lipoproteins to modulate the progression of atherosclerosis. In pancreatic tumoral cells, this encoded protein is thought to be sequestrated within the Golgi compartment and is probably not secreted. This gene contains a variable number of tandem repeat (VNTR) polymorphism in the coding region that may influence the function of the encoded protein.<ref name="entrez">{{cite web | title = Entrez Gene: CEL carboxyl ester lipase (bile salt-stimulated lipase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1056| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kumar BV, Aleman-Gomez JA, Colwell N, ''et al.'' |title=Structure of the human pancreatic cholesterol esterase gene. |journal=Biochemistry |volume=31 |issue= 26 |pages= 6077-81 |year= 1992 |pmid= 1627550 |doi= }}
*{{cite journal | author=Lidberg U, Nilsson J, Strömberg K, ''et al.'' |title=Genomic organization, sequence analysis, and chromosomal localization of the human carboxyl ester lipase (CEL) gene and a CEL-like (CELL) gene. |journal=Genomics |volume=13 |issue= 3 |pages= 630-40 |year= 1992 |pmid= 1639390 |doi= }}
*{{cite journal | author=Taylor AK, Zambaux JL, Klisak I, ''et al.'' |title=Carboxyl ester lipase: a highly polymorphic locus on human chromosome 9qter. |journal=Genomics |volume=10 |issue= 2 |pages= 425-31 |year= 1991 |pmid= 1676983 |doi= }}
*{{cite journal | author=Nilsson J, Bläckberg L, Carlsson P, ''et al.'' |title=cDNA cloning of human-milk bile-salt-stimulated lipase and evidence for its identity to pancreatic carboxylic ester hydrolase. |journal=Eur. J. Biochem. |volume=192 |issue= 2 |pages= 543-50 |year= 1990 |pmid= 1698625 |doi= }}
*{{cite journal | author=Lindström MB, Persson J, Thurn L, Borgström B |title=Effect of pancreatic phospholipase A2 and gastric lipase on the action of pancreatic carboxyl ester lipase against lipid substrates in vitro. |journal=Biochim. Biophys. Acta |volume=1084 |issue= 2 |pages= 194-7 |year= 1991 |pmid= 1854805 |doi= }}
*{{cite journal | author=Baba T, Downs D, Jackson KW, ''et al.'' |title=Structure of human milk bile salt activated lipase. |journal=Biochemistry |volume=30 |issue= 2 |pages= 500-10 |year= 1991 |pmid= 1988041 |doi= }}
*{{cite journal | author=Christie DL, Cleverly DR, O'Connor CJ |title=Human milk bile-salt stimulated lipase. Sequence similarity with rat lysophospholipase and homology with the active site region of cholinesterases. |journal=FEBS Lett. |volume=278 |issue= 2 |pages= 190-4 |year= 1991 |pmid= 1991511 |doi= }}
*{{cite journal | author=Reue K, Zambaux J, Wong H, ''et al.'' |title=cDNA cloning of carboxyl ester lipase from human pancreas reveals a unique proline-rich repeat unit. |journal=J. Lipid Res. |volume=32 |issue= 2 |pages= 267-76 |year= 1991 |pmid= 2066663 |doi= }}
*{{cite journal | author=Hui DY, Kissel JA |title=Sequence identity between human pancreatic cholesterol esterase and bile salt-stimulated milk lipase. |journal=FEBS Lett. |volume=276 |issue= 1-2 |pages= 131-4 |year= 1991 |pmid= 2265692 |doi= }}
*{{cite journal | author=Escribano MJ, Imperial S |title=Purification and molecular characterization of FAP, a feto-acinar protein associated with the differentiation of human pancreas. |journal=J. Biol. Chem. |volume=264 |issue= 36 |pages= 21865-71 |year= 1990 |pmid= 2600091 |doi= }}
*{{cite journal | author=Erlanson-Albertsson C, Sternby B, Johannesson U |title=The interaction between human pancreatic carboxylester hydrolase (bile-salt-stimulated lipase of human milk) and lactoferrin. |journal=Biochim. Biophys. Acta |volume=829 |issue= 2 |pages= 282-7 |year= 1985 |pmid= 3995055 |doi= }}
*{{cite journal | author=Chekhranova MK, Il'ina EN, Shuvalova ER, ''et al.'' |title=[Cloning, determination of primary structure, and expression of the C-terminal segment of human cholesterol-esterase/lipase, containing the antigenic determinant of the protein, in Escherichia coli] |journal=Mol. Biol. (Mosk.) |volume=28 |issue= 2 |pages= 464-7 |year= 1994 |pmid= 7514266 |doi= }}
*{{cite journal | author=Roudani S, Miralles F, Margotat A, ''et al.'' |title=Bile salt-dependent lipase transcripts in human fetal tissues. |journal=Biochim. Biophys. Acta |volume=1264 |issue= 1 |pages= 141-50 |year= 1995 |pmid= 7578248 |doi= }}
*{{cite journal | author=Bruneau N, de la Porte PL, Sbarra V, Lombardo D |title=Association of bile-salt-dependent lipase with membranes of human pancreatic microsomes. |journal=Eur. J. Biochem. |volume=233 |issue= 1 |pages= 209-18 |year= 1995 |pmid= 7588748 |doi= }}
*{{cite journal | author=Wang CS, Dashti A, Jackson KW, ''et al.'' |title=Isolation and characterization of human milk bile salt-activated lipase C-tail fragment. |journal=Biochemistry |volume=34 |issue= 33 |pages= 10639-44 |year= 1995 |pmid= 7654718 |doi= }}
*{{cite journal | author=Nilsson J, Hellquist M, Bjursell G |title=The human carboxyl ester lipase-like (CELL) gene is ubiquitously expressed and contains a hypervariable region. |journal=Genomics |volume=17 |issue= 2 |pages= 416-22 |year= 1993 |pmid= 7691717 |doi= 10.1006/geno.1993.1341 }}
*{{cite journal | author=Bruneau N, Lombardo D |title=Chaperone function of a Grp 94-related protein for folding and transport of the pancreatic bile salt-dependent lipase. |journal=J. Biol. Chem. |volume=270 |issue= 22 |pages= 13524-33 |year= 1995 |pmid= 7768954 |doi= }}
*{{cite journal | author=Mas E, Abouakil N, Roudani S, ''et al.'' |title=Human fetoacinar pancreatic protein: an oncofetal glycoform of the normally secreted pancreatic bile-salt-dependent lipase. |journal=Biochem. J. |volume=289 ( Pt 2) |issue= |pages= 609-15 |year= 1993 |pmid= 8424803 |doi= }}
*{{cite journal | author=Shamir R, Johnson WJ, Morlock-Fitzpatrick K, ''et al.'' |title=Pancreatic carboxyl ester lipase: a circulating enzyme that modifies normal and oxidized lipoproteins in vitro. |journal=J. Clin. Invest. |volume=97 |issue= 7 |pages= 1696-704 |year= 1996 |pmid= 8601635 |doi= }}
*{{cite journal | author=Landberg E, Påhlsson P, Krotkiewski H, ''et al.'' |title=Glycosylation of bile-salt-stimulated lipase from human milk: comparison of native and recombinant forms. |journal=Arch. Biochem. Biophys. |volume=344 |issue= 1 |pages= 94-102 |year= 1997 |pmid= 9244386 |doi= 10.1006/abbi.1997.0188 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CLCN1... {November 17, 2007 1:37:34 PM PST}
- SEARCH REDIRECT: Control Box Found: CLCN1 {November 17, 2007 1:38:06 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 1:38:09 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 1:38:09 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 1:38:09 PM PST}
- UPDATED: Updated protein page: CLCN1 {November 17, 2007 1:38:15 PM PST}
- INFO: Beginning work on CTSA... {November 17, 2007 1:44:21 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:44:58 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CTSA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ivy.
| PDB = {{PDB2|1ivy}}
| Name = Cathepsin A
| HGNCid = 9251
| Symbol = CTSA
| AltSymbols =; GLB2; GSL; NGBE; PPCA; PPGB
| OMIM = 256540
| ECnumber =
| Homologene = 80163
| MGIid = 97748
| GeneAtlas_image1 = PBB_GE_CTSA_200661_at_tn.png
| Function = {{GNF_GO|id=GO:0004185 |text = serine carboxypeptidase activity}} {{GNF_GO|id=GO:0004186 |text = carboxypeptidase C activity}} {{GNF_GO|id=GO:0005478 |text = transporter activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008047 |text = enzyme activator activity}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006886 |text = intracellular protein transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5476
| Hs_Ensembl = ENSG00000064601
| Hs_RefseqProtein = NP_000299
| Hs_RefseqmRNA = NM_000308
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 43952190
| Hs_GenLoc_end = 43960866
| Hs_Uniprot = P10619
| Mm_EntrezGene = 19025
| Mm_Ensembl = ENSMUSG00000017760
| Mm_RefseqmRNA = NM_001038492
| Mm_RefseqProtein = NP_001033581
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 164524078
| Mm_GenLoc_end = 164532237
| Mm_Uniprot = Q544R6
}}
}}
'''Cathepsin A''', also known as '''CTSA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CTSA cathepsin A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5476| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a glycoprotein which associates with lysosomal enzymes beta-galactosidase and neuraminidase to form a complex of high molecular weight multimers. The formation of this complex provides a protective role for stability and activity. Deficiencies in this gene are linked to multiple forms of galactosialidosis.<ref name="entrez">{{cite web | title = Entrez Gene: CTSA cathepsin A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5476| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Morreau H, Galjart NJ, Willemsen R, ''et al.'' |title=Human lysosomal protective protein. Glycosylation, intracellular transport, and association with beta-galactosidase in the endoplasmic reticulum. |journal=J. Biol. Chem. |volume=267 |issue= 25 |pages= 17949-56 |year= 1992 |pmid= 1387645 |doi= }}
*{{cite journal | author=Halal F, Chitayat D, Parikh H, ''et al.'' |title=Ring chromosome 20 and possible assignment of the structural gene encoding human carboxypeptidase-L to the distal segment of the long arm of chromosome 20. |journal=Am. J. Med. Genet. |volume=43 |issue= 3 |pages= 576-9 |year= 1992 |pmid= 1605251 |doi= 10.1002/ajmg.1320430314 }}
*{{cite journal | author=Jackman HL, Tan FL, Tamei H, ''et al.'' |title=A peptidase in human platelets that deamidates tachykinins. Probable identity with the lysosomal "protective protein". |journal=J. Biol. Chem. |volume=265 |issue= 19 |pages= 11265-72 |year= 1990 |pmid= 1694176 |doi= }}
*{{cite journal | author=Zhou XY, Galjart NJ, Willemsen R, ''et al.'' |title=A mutation in a mild form of galactosialidosis impairs dimerization of the protective protein and renders it unstable. |journal=EMBO J. |volume=10 |issue= 13 |pages= 4041-8 |year= 1992 |pmid= 1756715 |doi= }}
*{{cite journal | author=Galjart NJ, Morreau H, Willemsen R, ''et al.'' |title=Human lysosomal protective protein has cathepsin A-like activity distinct from its protective function. |journal=J. Biol. Chem. |volume=266 |issue= 22 |pages= 14754-62 |year= 1991 |pmid= 1907282 |doi= }}
*{{cite journal | author=Yoshida K, Oshima A, Shimmoto M, ''et al.'' |title=Human beta-galactosidase gene mutations in GM1-gangliosidosis: a common mutation among Japanese adult/chronic cases. |journal=Am. J. Hum. Genet. |volume=49 |issue= 2 |pages= 435-42 |year= 1991 |pmid= 1907800 |doi= }}
*{{cite journal | author=Wiegant J, Galjart NJ, Raap AK, d'Azzo A |title=The gene encoding human protective protein (PPGB) is on chromosome 20. |journal=Genomics |volume=10 |issue= 2 |pages= 345-9 |year= 1991 |pmid= 2071143 |doi= }}
*{{cite journal | author=Strisciuglio P, Sly WS, Dodson WE, ''et al.'' |title=Combined deficiency of beta-galactosidase and neuraminidase: natural history of the disease in the first 18 years of an American patient with late infantile onset form. |journal=Am. J. Med. Genet. |volume=37 |issue= 4 |pages= 573-7 |year= 1991 |pmid= 2148053 |doi= 10.1002/ajmg.1320370431 }}
*{{cite journal | author=Kase R, Itoh K, Takiyama N, ''et al.'' |title=Galactosialidosis: simultaneous deficiency of esterase, carboxy-terminal deamidase and acid carboxypeptidase activities. |journal=Biochem. Biophys. Res. Commun. |volume=172 |issue= 3 |pages= 1175-9 |year= 1990 |pmid= 2244901 |doi= }}
*{{cite journal | author=Willemsen R, Hoogeveen AT, Sips HJ, ''et al.'' |title=Immunoelectron microscopical localization of lysosomal beta-galactosidase and its precursor forms in normal and mutant human fibroblasts. |journal=Eur. J. Cell Biol. |volume=40 |issue= 1 |pages= 9-15 |year= 1986 |pmid= 3084261 |doi= }}
*{{cite journal | author=Verheijen FW, Palmeri S, Galjaard H |title=Purification and partial characterization of lysosomal neuraminidase from human placenta. |journal=Eur. J. Biochem. |volume=162 |issue= 1 |pages= 63-7 |year= 1987 |pmid= 3102233 |doi= }}
*{{cite journal | author=Nanba E, Tsuji A, Omura K, Suzuki Y |title=Galactosialidosis: a direct evidence that a 46-kilodalton protein restores deficient enzyme activities in fibroblasts. |journal=Biochem. Biophys. Res. Commun. |volume=144 |issue= 1 |pages= 138-42 |year= 1987 |pmid= 3107551 |doi= }}
*{{cite journal | author=Galjart NJ, Gillemans N, Harris A, ''et al.'' |title=Expression of cDNA encoding the human "protective protein" associated with lysosomal beta-galactosidase and neuraminidase: homology to yeast proteases. |journal=Cell |volume=54 |issue= 6 |pages= 755-64 |year= 1988 |pmid= 3136930 |doi= }}
*{{cite journal | author=Chitayat D, Applegarth DA, Lewis J, ''et al.'' |title=Juvenile galactosialidosis in a white male: a new variant. |journal=Am. J. Med. Genet. |volume=31 |issue= 4 |pages= 887-901 |year= 1989 |pmid= 3149149 |doi= 10.1002/ajmg.1320310423 }}
*{{cite journal | author=Verheijen FW, Palmeri S, Hoogeveen AT, Galjaard H |title=Human placental neuraminidase. Activation, stabilization and association with beta-galactosidase and its protective protein. |journal=Eur. J. Biochem. |volume=149 |issue= 2 |pages= 315-21 |year= 1985 |pmid= 3922758 |doi= }}
*{{cite journal | author=van der Horst GT, Kleijer WJ, Hoogeveen AT, ''et al.'' |title=Morquio B syndrome: a primary defect in beta-galactosidase. |journal=Am. J. Med. Genet. |volume=16 |issue= 2 |pages= 261-75 |year= 1984 |pmid= 6418007 |doi= 10.1002/ajmg.1320160215 }}
*{{cite journal | author=Maire I, Nivelon-Chevallier AR |title=Combined deficiency of beta-galactosidase and neuraminidase: three affected siblings in a French family. |journal=J. Inherit. Metab. Dis. |volume=4 |issue= 4 |pages= 221-3 |year= 1982 |pmid= 6796775 |doi= }}
*{{cite journal | author=Pshezhetsky AV, Potier M |title=Direct affinity purification and supramolecular organization of human lysosomal cathepsin A. |journal=Arch. Biochem. Biophys. |volume=313 |issue= 1 |pages= 64-70 |year= 1994 |pmid= 8053688 |doi= 10.1006/abbi.1994.1359 }}
*{{cite journal | author=Ishii N, Oshima A, Sakuraba H, ''et al.'' |title=Normal serum beta-galactosidase in juvenile GM1 gangliosidosis. |journal=Pediatr. Neurol. |volume=10 |issue= 4 |pages= 317-9 |year= 1994 |pmid= 8068159 |doi= }}
*{{cite journal | author=Chakraborty S, Rafi MA, Wenger DA |title=Mutations in the lysosomal beta-galactosidase gene that cause the adult form of GM1 gangliosidosis. |journal=Am. J. Hum. Genet. |volume=54 |issue= 6 |pages= 1004-13 |year= 1994 |pmid= 8198123 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DDR1... {November 17, 2007 1:35:24 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:36:19 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_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Discoidin domain receptor family, member 1
| HGNCid = 2730
| Symbol = DDR1
| AltSymbols =; CAK; CD167; DDR; EDDR1; MCK10; NEP; NTRK4; PTK3; PTK3A; RTK6; TRKE
| OMIM = 600408
| ECnumber =
| Homologene = 68212
| MGIid = 99216
| GeneAtlas_image1 = PBB_GE_DDR1_1007_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_DDR1_207169_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_DDR1_208779_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine kinase activity}} {{GNF_GO|id=GO:0004714 |text = transmembrane receptor protein tyrosine kinase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 780
| Hs_Ensembl = ENSG00000137332
| Hs_RefseqProtein = NP_001945
| Hs_RefseqmRNA = NM_001954
| Hs_GenLoc_db =
| Hs_GenLoc_chr = c6_COX
| Hs_GenLoc_start = 30989009
| Hs_GenLoc_end = 31005081
| Hs_Uniprot = Q08345
| Mm_EntrezGene = 12305
| Mm_Ensembl = ENSMUSG00000003534
| Mm_RefseqmRNA = NM_007584
| Mm_RefseqProtein = NP_031610
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 35289621
| Mm_GenLoc_end = 35312652
| Mm_Uniprot = O35407
}}
}}
'''Discoidin domain receptor family, member 1''', also known as '''DDR1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DDR1 discoidin domain receptor family, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=780| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Receptor tyrosine kinases (RTKs) play a key role in the communication of cells with their microenvironment. These molecules are involved in the regulation of cell growth, differentiation and metabolism. The protein encoded by this gene is a RTK that is widely expressed in normal and transformed epithelial cells and is activated by various types of collagen. This protein belongs to a subfamily of tyrosine kinase receptors with a homology region to the Dictyostelium discoideum protein discoidin I in their extracellular domain. Its autophosphorylation is achieved by all collagens so far tested (type I to type VI). In situ studies and Northern-blot analysis showed that expression of this encoded protein is restricted to epithelial cells, particularly in the kidney, lung, gastrointestinal tract, and brain. In addition, this protein is significantly over-expressed in several human tumors from breast, ovarian, esophageal, and pediatric brain. This gene is located on chromosome 6p21.3 in proximity to several HLA class I genes. Alternative splicing of this gene results in multiple transcript variants.<ref name="entrez">{{cite web | title = Entrez Gene: DDR1 discoidin domain receptor family, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=780| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Edelhoff S, Sweetser DA, Disteche CM |title=Mapping of the NEP receptor tyrosine kinase gene to human chromosome 6p21.3 and mouse chromosome 17C. |journal=Genomics |volume=25 |issue= 1 |pages= 309-11 |year= 1995 |pmid= 7774938 |doi= }}
*{{cite journal | author=Shelling AN, Butler R, Jones T, ''et al.'' |title=Localization of an epithelial-specific receptor kinase (EDDR1) to chromosome 6q16. |journal=Genomics |volume=25 |issue= 2 |pages= 584-7 |year= 1995 |pmid= 7789998 |doi= }}
*{{cite journal | author=Weiner TM, Liu ET, Craven RJ, Cance WG |title=Expression of growth factor receptors, the focal adhesion kinase, and other tyrosine kinases in human soft tissue tumors. |journal=Ann. Surg. Oncol. |volume=1 |issue= 1 |pages= 18-27 |year= 1995 |pmid= 7834423 |doi= }}
*{{cite journal | author=Laval S, Butler R, Shelling AN, ''et al.'' |title=Isolation and characterization of an epithelial-specific receptor tyrosine kinase from an ovarian cancer cell line. |journal=Cell Growth Differ. |volume=5 |issue= 11 |pages= 1173-83 |year= 1995 |pmid= 7848919 |doi= }}
*{{cite journal | author=Kato JY, Matsuoka M, Strom DK, Sherr CJ |title=Regulation of cyclin D-dependent kinase 4 (cdk4) by cdk4-activating kinase. |journal=Mol. Cell. Biol. |volume=14 |issue= 4 |pages= 2713-21 |year= 1994 |pmid= 8139570 |doi= }}
*{{cite journal | author=Di Marco E, Cutuli N, Guerra L, ''et al.'' |title=Molecular cloning of trkE, a novel trk-related putative tyrosine kinase receptor isolated from normal human keratinocytes and widely expressed by normal human tissues. |journal=J. Biol. Chem. |volume=268 |issue= 32 |pages= 24290-5 |year= 1993 |pmid= 8226977 |doi= }}
*{{cite journal | author=Perez JL, Shen X, Finkernagel S, ''et al.'' |title=Identification and chromosomal mapping of a receptor tyrosine kinase with a putative phospholipid binding sequence in its ectodomain. |journal=Oncogene |volume=9 |issue= 1 |pages= 211-9 |year= 1994 |pmid= 8302582 |doi= }}
*{{cite journal | author=Johnson JD, Edman JC, Rutter WJ |title=A receptor tyrosine kinase found in breast carcinoma cells has an extracellular discoidin I-like domain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 12 |pages= 5677-81 |year= 1993 |pmid= 8390675 |doi= }}
*{{cite journal | author=Perez JL, Jing SQ, Wong TW |title=Identification of two isoforms of the Cak receptor kinase that are coexpressed in breast tumor cell lines. |journal=Oncogene |volume=12 |issue= 7 |pages= 1469-77 |year= 1996 |pmid= 8622863 |doi= }}
*{{cite journal | author=Valent A, Meddeb M, Danglot G, ''et al.'' |title=Assignment of the NTRK4 (trkE) gene to chromosome 6p21. |journal=Hum. Genet. |volume=98 |issue= 1 |pages= 12-5 |year= 1996 |pmid= 8682498 |doi= }}
*{{cite journal | author=Playford MP, Butler RJ, Wang XC, ''et al.'' |title=The genomic structure of discoidin receptor tyrosine kinase. |journal=Genome Res. |volume=6 |issue= 7 |pages= 620-7 |year= 1996 |pmid= 8796349 |doi= }}
*{{cite journal | author=Sakuma S, Saya H, Tada M, ''et al.'' |title=Receptor protein tyrosine kinase DDR is up-regulated by p53 protein. |journal=FEBS Lett. |volume=398 |issue= 2-3 |pages= 165-9 |year= 1997 |pmid= 8977099 |doi= }}
*{{cite journal | author=Nemoto T, Ohashi K, Akashi T, ''et al.'' |title=Overexpression of protein tyrosine kinases in human esophageal cancer. |journal=Pathobiology |volume=65 |issue= 4 |pages= 195-203 |year= 1998 |pmid= 9396043 |doi= }}
*{{cite journal | author=Tanaka K, Nagayama Y, Nakano T, ''et al.'' |title=Expression profile of receptor-type protein tyrosine kinase genes in the human thyroid. |journal=Endocrinology |volume=139 |issue= 3 |pages= 852-8 |year= 1998 |pmid= 9492013 |doi= }}
*{{cite journal | author=Vogel W, Gish GD, Alves F, Pawson T |title=The discoidin domain receptor tyrosine kinases are activated by collagen. |journal=Mol. Cell |volume=1 |issue= 1 |pages= 13-23 |year= 1998 |pmid= 9659899 |doi= }}
*{{cite journal | author=Shrivastava A, Radziejewski C, Campbell E, ''et al.'' |title=An orphan receptor tyrosine kinase family whose members serve as nonintegrin collagen receptors. |journal=Mol. Cell |volume=1 |issue= 1 |pages= 25-34 |year= 1998 |pmid= 9659900 |doi= }}
*{{cite journal | author=Vogel W, Brakebusch C, Fässler R, ''et al.'' |title=Discoidin domain receptor 1 is activated independently of beta(1) integrin. |journal=J. Biol. Chem. |volume=275 |issue= 8 |pages= 5779-84 |year= 2000 |pmid= 10681566 |doi= }}
*{{cite journal | author=Foehr ED, Tatavos A, Tanabe E, ''et al.'' |title=Discoidin domain receptor 1 (DDR1) signaling in PC12 cells: activation of juxtamembrane domains in PDGFR/DDR/TrkA chimeric receptors. |journal=FASEB J. |volume=14 |issue= 7 |pages= 973-81 |year= 2000 |pmid= 10783152 |doi= }}
*{{cite journal | author=Weiner HL, Huang H, Zagzag D, ''et al.'' |title=Consistent and selective expression of the discoidin domain receptor-1 tyrosine kinase in human brain tumors. |journal=Neurosurgery |volume=47 |issue= 6 |pages= 1400-9 |year= 2001 |pmid= 11126911 |doi= }}
*{{cite journal | author=Mohan RR, Mohan RR, Wilson SE |title=Discoidin domain receptor (DDR) 1 and 2: collagen-activated tyrosine kinase receptors in the cornea. |journal=Exp. Eye Res. |volume=72 |issue= 1 |pages= 87-92 |year= 2001 |pmid= 11133186 |doi= 10.1006/exer.2000.0932 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GLUD1... {November 17, 2007 1:38:15 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:38:46 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_GLUD1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hwx.
| PDB = {{PDB2|1hwx}}, {{PDB2|1hwy}}, {{PDB2|1hwz}}, {{PDB2|1l1f}}, {{PDB2|1nqt}}, {{PDB2|1nr1}}, {{PDB2|1nr7}}
| Name = Glutamate dehydrogenase 1
| HGNCid = 4335
| Symbol = GLUD1
| AltSymbols =; GDH; GLUD; MGC132003
| OMIM = 138130
| ECnumber =
| Homologene = 55885
| MGIid = 95753
| GeneAtlas_image1 = PBB_GE_GLUD1_200947_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_GLUD1_200946_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004352 |text = glutamate dehydrogenase activity}} {{GNF_GO|id=GO:0004353 |text = glutamate dehydrogenase [NAD(P)+] activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}}
| Process = {{GNF_GO|id=GO:0006520 |text = amino acid metabolic process}} {{GNF_GO|id=GO:0006538 |text = glutamate catabolic process}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2746
| Hs_Ensembl = ENSG00000148672
| Hs_RefseqProtein = NP_005262
| Hs_RefseqmRNA = NM_005271
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 88800223
| Hs_GenLoc_end = 88844603
| Hs_Uniprot = P00367
| Mm_EntrezGene = 14661
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_987719
| Mm_RefseqProtein = XP_992813
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Glutamate dehydrogenase 1''', also known as '''GLUD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GLUD1 glutamate dehydrogenase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2746| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = L-glutamate dehydrogenase (EC 1.4.1.3) has a central role in nitrogen metabolism in plants and animals. Glutamate dehydrogenase is found in all organisms and catalyzes the oxidative deamination of 1-glutamate to 2-oxoglutarate (Smith et al., 2001). Glutamate, the main substrate of GLUD, is present in brain in concentrations higher than in other organs. In nervous tissue, GLUD appears to function in both the synthesis and the catabolism of glutamate and perhaps in ammonia detoxification (Mavrothalassitis et al., 1988).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: GLUD1 glutamate dehydrogenase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2746| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{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=Julliard JH, Smith EL |title=Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme. |journal=J. Biol. Chem. |volume=254 |issue= 9 |pages= 3427-38 |year= 1979 |pmid= 429360 |doi= }}
*{{cite journal | author=Hochstrasser DF, Frutiger S, Paquet N, ''et al.'' |title=Human liver protein map: a reference database established by microsequencing and gel comparison. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 992-1001 |year= 1993 |pmid= 1286669 |doi= }}
*{{cite journal | author=Jung KY, Warter S, Rumpler Y |title=Assignment of the GDH loci to human chromosomes 10q23 and Xq24 by in situ hybridization. |journal=Ann. Genet. |volume=32 |issue= 2 |pages= 109-10 |year= 1989 |pmid= 2757358 |doi= }}
*{{cite journal | author=Mavrothalassitis G, Tzimagiorgis G, Mitsialis A, ''et al.'' |title=Isolation and characterization of cDNA clones encoding human liver glutamate dehydrogenase: evidence for a small gene family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 10 |pages= 3494-8 |year= 1988 |pmid= 3368458 |doi= }}
*{{cite journal | author=Amuro N, Yamaura M, Goto Y, Okazaki T |title=Molecular cloning and nucleotide sequence of the cDNA for human liver glutamate dehydrogenase precursor. |journal=Biochem. Biophys. Res. Commun. |volume=152 |issue= 3 |pages= 1395-400 |year= 1988 |pmid= 3377777 |doi= }}
*{{cite journal | author=Nakatani Y, Schneider M, Banner C, Freese E |title=Complete nucleotide sequence of human glutamate dehydrogenase cDNA. |journal=Nucleic Acids Res. |volume=16 |issue= 13 |pages= 6237 |year= 1988 |pmid= 3399399 |doi= }}
*{{cite journal | author=Nakatani Y, Banner C, von Herrath M, ''et al.'' |title=Comparison of human brain and liver glutamate dehydrogenase cDNAS. |journal=Biochem. Biophys. Res. Commun. |volume=149 |issue= 2 |pages= 405-10 |year= 1988 |pmid= 3426581 |doi= }}
*{{cite journal | author=Banner C, Silverman S, Thomas JW, ''et al.'' |title=Isolation of a human brain cDNA for glutamate dehydrogenase. |journal=J. Neurochem. |volume=49 |issue= 1 |pages= 246-52 |year= 1987 |pmid= 3585334 |doi= }}
*{{cite journal | author=Fahien LA, Kmiotek EH, Woldegiorgis G, ''et al.'' |title=Regulation of aminotransferase-glutamate dehydrogenase interactions by carbamyl phosphate synthase-I, Mg2+ plus leucine versus citrate and malate. |journal=J. Biol. Chem. |volume=260 |issue= 10 |pages= 6069-79 |year= 1985 |pmid= 3997814 |doi= }}
*{{cite journal | author=Plaitakis A, Berl S, Yahr MD |title=Abnormal glutamate metabolism in an adult-onset degenerative neurological disorder. |journal=Science |volume=216 |issue= 4542 |pages= 193-6 |year= 1982 |pmid= 6121377 |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=Deloukas P, Dauwerse JG, Moschonas NK, ''et al.'' |title=Three human glutamate dehydrogenase genes (GLUD1, GLUDP2, and GLUDP3) are located on chromosome 10q, but are not closely physically linked. |journal=Genomics |volume=17 |issue= 3 |pages= 676-81 |year= 1993 |pmid= 8244384 |doi= 10.1006/geno.1993.1389 }}
*{{cite journal | author=Tzimagiorgis G, Leversha MA, Chroniary K, ''et al.'' |title=Structure and expression analysis of a member of the human glutamate dehydrogenase (GLUD) gene family mapped to chromosome 10p11.2. |journal=Hum. Genet. |volume=91 |issue= 5 |pages= 433-8 |year= 1993 |pmid= 8314555 |doi= }}
*{{cite journal | author=Michaelidis TM, Tzimagiorgis G, Moschonas NK, Papamatheakis J |title=The human glutamate dehydrogenase gene family: gene organization and structural characterization. |journal=Genomics |volume=16 |issue= 1 |pages= 150-60 |year= 1993 |pmid= 8486350 |doi= 10.1006/geno.1993.1152 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Stanley CA, Lieu YK, Hsu BY, ''et al.'' |title=Hyperinsulinism and hyperammonemia in infants with regulatory mutations of the glutamate dehydrogenase gene. |journal=N. Engl. J. Med. |volume=338 |issue= 19 |pages= 1352-7 |year= 1998 |pmid= 9571255 |doi= }}
*{{cite journal | author=Miki Y, Taki T, Ohura T, ''et al.'' |title=Novel missense mutations in the glutamate dehydrogenase gene in the congenital hyperinsulinism-hyperammonemia syndrome. |journal=J. Pediatr. |volume=136 |issue= 1 |pages= 69-72 |year= 2000 |pmid= 10636977 |doi= }}
*{{cite journal | author=Santer R, Kinner M, Passarge M, ''et al.'' |title=Novel missense mutations outside the allosteric domain of glutamate dehydrogenase are prevalent in European patients with the congenital hyperinsulinism-hyperammonemia syndrome. |journal=Hum. Genet. |volume=108 |issue= 1 |pages= 66-71 |year= 2001 |pmid= 11214910 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IL1R1... {November 17, 2007 1:38:47 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:39:22 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
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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_IL1R1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1g0y.
| PDB = {{PDB2|1g0y}}, {{PDB2|1ira}}, {{PDB2|1itb}}
| Name = Interleukin 1 receptor, type I
| HGNCid = 5993
| Symbol = IL1R1
| AltSymbols =; CD121A; D2S1473; IL-1R-alpha; IL1R; IL1RA; P80
| OMIM = 147810
| ECnumber =
| Homologene = 677
| MGIid = 96545
| GeneAtlas_image1 = PBB_GE_IL1R1_215561_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004888 |text = transmembrane receptor activity}} {{GNF_GO|id=GO:0004909 |text = interleukin-1, Type I, activating receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0019221 |text = cytokine and chemokine mediated signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3554
| Hs_Ensembl = ENSG00000115594
| Hs_RefseqProtein = NP_000868
| Hs_RefseqmRNA = NM_000877
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 102125678
| Hs_GenLoc_end = 102159788
| Hs_Uniprot = P14778
| Mm_EntrezGene = 16177
| Mm_Ensembl = ENSMUSG00000026072
| Mm_RefseqmRNA = XM_979865
| Mm_RefseqProtein = XP_984959
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 40169626
| Mm_GenLoc_end = 40260723
| Mm_Uniprot = Q32MH0
}}
}}
'''Interleukin 1 receptor, type I''', also known as '''IL1R1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IL1R1 interleukin 1 receptor, type I| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3554| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a cytokine receptor that belongs to the interleukin 1 receptor family. This protein is a receptor for interleukin alpha (IL1A), interleukin beta (IL1B), and interleukin 1 receptor, type I(IL1R1/IL1RA). It is an important mediator involved in many cytokine induced immune and inflammatory responses. This gene along with interleukin 1 receptor, type II (IL1R2), interleukin 1 receptor-like 2 (IL1RL2), and interleukin 1 receptor-like 1 (IL1RL1) form a cytokine receptor gene cluster in a region mapped to chromosome 2q12.<ref name="entrez">{{cite web | title = Entrez Gene: IL1R1 interleukin 1 receptor, type I| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3554| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Copeland NG, Silan CM, Kingsley DM, ''et al.'' |title=Chromosomal location of murine and human IL-1 receptor genes. |journal=Genomics |volume=9 |issue= 1 |pages= 44-50 |year= 1991 |pmid= 1672292 |doi= }}
*{{cite journal | author=McMahan CJ, Slack JL, Mosley B, ''et al.'' |title=A novel IL-1 receptor, cloned from B cells by mammalian expression, is expressed in many cell types. |journal=EMBO J. |volume=10 |issue= 10 |pages= 2821-32 |year= 1991 |pmid= 1833184 |doi= }}
*{{cite journal | author=Uhl J, Newton RC, Giri JG, ''et al.'' |title=Identification of IL-1 receptors on human monocytes. |journal=J. Immunol. |volume=142 |issue= 5 |pages= 1576-81 |year= 1989 |pmid= 2521881 |doi= }}
*{{cite journal | author=Sims JE, Acres RB, Grubin CE, ''et al.'' |title=Cloning the interleukin 1 receptor from human T cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 22 |pages= 8946-50 |year= 1989 |pmid= 2530587 |doi= }}
*{{cite journal | author=Chua AO, Gubler U |title=Sequence of the cDNA for the human fibroblast type interleukin-1 receptor. |journal=Nucleic Acids Res. |volume=17 |issue= 23 |pages= 10114 |year= 1990 |pmid= 2532321 |doi= }}
*{{cite journal | author=Dower SK, Kronheim SR, Hopp TP, ''et al.'' |title=The cell surface receptors for interleukin-1 alpha and interleukin-1 beta are identical. |journal=Nature |volume=324 |issue= 6094 |pages= 266-8 |year= 1987 |pmid= 2946959 |doi= 10.1038/324266a0 }}
*{{cite journal | author=Rautonen N, Rautonen J, Martin NL, Wara DW |title=HIV-1 Tat induces cytokine synthesis by uninfected mononuclear cells. |journal=AIDS |volume=8 |issue= 10 |pages= 1504-6 |year= 1995 |pmid= 7818827 |doi= }}
*{{cite journal | author=Vigers GP, Anderson LJ, Caffes P, Brandhuber BJ |title=Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1beta. |journal=Nature |volume=386 |issue= 6621 |pages= 190-4 |year= 1997 |pmid= 9062193 |doi= 10.1038/386190a0 }}
*{{cite journal | author=Schreuder H, Tardif C, Trump-Kallmeyer S, ''et al.'' |title=A new cytokine-receptor binding mode revealed by the crystal structure of the IL-1 receptor with an antagonist. |journal=Nature |volume=386 |issue= 6621 |pages= 194-200 |year= 1997 |pmid= 9062194 |doi= 10.1038/386194a0 }}
*{{cite journal | author=Rameshwar P, Poddar A, Zhu G, Gascón P |title=Receptor induction regulates the synergistic effects of substance P with IL-1 and platelet-derived growth factor on the proliferation of bone marrow fibroblasts. |journal=J. Immunol. |volume=158 |issue= 7 |pages= 3417-24 |year= 1997 |pmid= 9120302 |doi= }}
*{{cite journal | author=Reddy SA, Huang JH, Liao WS |title=Phosphatidylinositol 3-kinase in interleukin 1 signaling. Physical interaction with the interleukin 1 receptor and requirement in NFkappaB and AP-1 activation. |journal=J. Biol. Chem. |volume=272 |issue= 46 |pages= 29167-73 |year= 1997 |pmid= 9360994 |doi= }}
*{{cite journal | author=Huang J, Gao X, Li S, Cao Z |title=Recruitment of IRAK to the interleukin 1 receptor complex requires interleukin 1 receptor accessory protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 24 |pages= 12829-32 |year= 1998 |pmid= 9371760 |doi= }}
*{{cite journal | author=Muzio M, Ni J, Feng P, Dixit VM |title=IRAK (Pelle) family member IRAK-2 and MyD88 as proximal mediators of IL-1 signaling. |journal=Science |volume=278 |issue= 5343 |pages= 1612-5 |year= 1997 |pmid= 9374458 |doi= }}
*{{cite journal | author=Dale M, Nicklin MJ |title=Interleukin-1 receptor cluster: gene organization of IL1R2, IL1R1, IL1RL2 (IL-1Rrp2), IL1RL1 (T1/ST2), and IL18R1 (IL-1Rrp) on human chromosome 2q. |journal=Genomics |volume=57 |issue= 1 |pages= 177-9 |year= 1999 |pmid= 10191101 |doi= 10.1006/geno.1999.5767 }}
*{{cite journal | author=Sizemore N, Leung S, Stark GR |title=Activation of phosphatidylinositol 3-kinase in response to interleukin-1 leads to phosphorylation and activation of the NF-kappaB p65/RelA subunit. |journal=Mol. Cell. Biol. |volume=19 |issue= 7 |pages= 4798-805 |year= 1999 |pmid= 10373529 |doi= }}
*{{cite journal | author=Burns K, Clatworthy J, Martin L, ''et al.'' |title=Tollip, a new component of the IL-1RI pathway, links IRAK to the IL-1 receptor. |journal=Nat. Cell Biol. |volume=2 |issue= 6 |pages= 346-51 |year= 2000 |pmid= 10854325 |doi= 10.1038/35014038 }}
*{{cite journal | author=Vigers GP, Dripps DJ, Edwards CK, Brandhuber BJ |title=X-ray crystal structure of a small antagonist peptide bound to interleukin-1 receptor type 1. |journal=J. Biol. Chem. |volume=275 |issue= 47 |pages= 36927-33 |year= 2001 |pmid= 10903327 |doi= 10.1074/jbc.M006071200 }}
*{{cite journal | author=Lin H, Ho AS, Haley-Vicente D, ''et al.'' |title=Cloning and characterization of IL-1HY2, a novel interleukin-1 family member. |journal=J. Biol. Chem. |volume=276 |issue= 23 |pages= 20597-602 |year= 2001 |pmid= 11278614 |doi= 10.1074/jbc.M010095200 }}
*{{cite journal | author=Joos L, McIntyre L, Ruan J, ''et al.'' |title=Association of IL-1beta and IL-1 receptor antagonist haplotypes with rate of decline in lung function in smokers. |journal=Thorax |volume=56 |issue= 11 |pages= 863-6 |year= 2001 |pmid= 11641511 |doi= }}
*{{cite journal | author=Köller M, Kutscha-Lissberg F, Brom J, ''et al.'' |title=Influence of low molecular weight heparin (certoparin) and unfractionated heparin on the release of cytokines from human leukocytes. |journal=Inflammation |volume=25 |issue= 5 |pages= 331-7 |year= 2003 |pmid= 11820460 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KCNA5... {November 17, 2007 1:39:22 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:40:02 PM PST}
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{{PBB_Controls
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| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Potassium voltage-gated channel, shaker-related subfamily, member 5
| HGNCid = 6224
| Symbol = KCNA5
| AltSymbols =; HK2; HCK1; HPCN1; KV1.5; MGC117058; MGC117059; PCN1
| OMIM = 176267
| ECnumber =
| Homologene = 1683
| MGIid = 96662
| GeneAtlas_image1 = PBB_GE_KCNA5_206762_at_tn.png
| Function = {{GNF_GO|id=GO:0005251 |text = delayed rectifier potassium channel activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0030955 |text = potassium ion binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0008076 |text = voltage-gated potassium channel complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006813 |text = potassium ion transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3741
| Hs_Ensembl = ENSG00000130037
| Hs_RefseqProtein = NP_002225
| Hs_RefseqmRNA = NM_002234
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 5023346
| Hs_GenLoc_end = 5026210
| Hs_Uniprot = P22460
| Mm_EntrezGene = 16493
| Mm_Ensembl = ENSMUSG00000045534
| Mm_RefseqmRNA = NM_145983
| Mm_RefseqProtein = NP_666095
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 126498974
| Mm_GenLoc_end = 126500782
| Mm_Uniprot = Q9Z1R6
}}
}}
'''Potassium voltage-gated channel, shaker-related subfamily, member 5''', also known as '''KCNA5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KCNA5 potassium voltage-gated channel, shaker-related subfamily, member 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3741| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Potassium channels represent the most complex class of voltage-gated ino channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. Four sequence-related potassium channel genes - shaker, shaw, shab, and shal - have been identified in Drosophila, and each has been shown to have human homolog(s). This gene encodes a member of the potassium channel, voltage-gated, shaker-related subfamily. This member contains six membrane-spanning domains with a shaker-type repeat in the fourth segment. It belongs to the delayed rectifier class, the function of which could restore the resting membrane potential of beta cells after depolarization and thereby contribute to the regulation of insulin secretion. This gene is intronless, and the gene is clustered with genes KCNA1 and KCNA6 on chromosome 12.<ref name="entrez">{{cite web | title = Entrez Gene: KCNA5 potassium voltage-gated channel, shaker-related subfamily, member 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3741| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Gutman GA, Chandy KG, Grissmer S, ''et al.'' |title=International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels. |journal=Pharmacol. Rev. |volume=57 |issue= 4 |pages= 473-508 |year= 2006 |pmid= 16382104 |doi= 10.1124/pr.57.4.10 }}
*{{cite journal | author=Curran ME, Landes GM, Keating MT |title=Molecular cloning, characterization, and genomic localization of a human potassium channel gene. |journal=Genomics |volume=12 |issue= 4 |pages= 729-37 |year= 1992 |pmid= 1349297 |doi= }}
*{{cite journal | author=Philipson LH, Hice RE, Schaefer K, ''et al.'' |title=Sequence and functional expression in Xenopus oocytes of a human insulinoma and islet potassium channel. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 1 |pages= 53-7 |year= 1991 |pmid= 1986382 |doi= }}
*{{cite journal | author=Tamkun MM, Knoth KM, Walbridge JA, ''et al.'' |title=Molecular cloning and characterization of two voltage-gated K+ channel cDNAs from human ventricle. |journal=FASEB J. |volume=5 |issue= 3 |pages= 331-7 |year= 1991 |pmid= 2001794 |doi= }}
*{{cite journal | author=Mays DJ, Foose JM, Philipson LH, Tamkun MM |title=Localization of the Kv1.5 K+ channel protein in explanted cardiac tissue. |journal=J. Clin. Invest. |volume=96 |issue= 1 |pages= 282-92 |year= 1995 |pmid= 7615797 |doi= }}
*{{cite journal | author=Crumb WJ, Wible B, Arnold DJ, ''et al.'' |title=Blockade of multiple human cardiac potassium currents by the antihistamine terfenadine: possible mechanism for terfenadine-associated cardiotoxicity. |journal=Mol. Pharmacol. |volume=47 |issue= 1 |pages= 181-90 |year= 1995 |pmid= 7838127 |doi= }}
*{{cite journal | author=Phromchotikul T, Browne DL, Curran ME, ''et al.'' |title=Dinucleotide repeat polymorphism at the KCNA5 locus. |journal=Hum. Mol. Genet. |volume=2 |issue= 9 |pages= 1512 |year= 1993 |pmid= 8242092 |doi= }}
*{{cite journal | author=Albrecht B, Weber K, Pongs O |title=Characterization of a voltage-activated K-channel gene cluster on human chromosome 12p13. |journal=Recept. Channels |volume=3 |issue= 3 |pages= 213-20 |year= 1996 |pmid= 8821794 |doi= }}
*{{cite journal | author=Holmes TC, Fadool DA, Ren R, Levitan IB |title=Association of Src tyrosine kinase with a human potassium channel mediated by SH3 domain. |journal=Science |volume=274 |issue= 5295 |pages= 2089-91 |year= 1997 |pmid= 8953041 |doi= }}
*{{cite journal | author=Lacerda AE, Roy ML, Lewis EW, Rampe D |title=Interactions of the nonsedating antihistamine loratadine with a Kv1.5-type potassium channel cloned from human heart. |journal=Mol. Pharmacol. |volume=52 |issue= 2 |pages= 314-22 |year= 1997 |pmid= 9271355 |doi= }}
*{{cite journal | author=Kääb S, Dixon J, Duc J, ''et al.'' |title=Molecular basis of transient outward potassium current downregulation in human heart failure: a decrease in Kv4.3 mRNA correlates with a reduction in current density. |journal=Circulation |volume=98 |issue= 14 |pages= 1383-93 |year= 1998 |pmid= 9760292 |doi= }}
*{{cite journal | author=Maruoka ND, Steele DF, Au BP, ''et al.'' |title=alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells. |journal=FEBS Lett. |volume=473 |issue= 2 |pages= 188-94 |year= 2000 |pmid= 10812072 |doi= }}
*{{cite journal | author=Peretz A, Gil-Henn H, Sobko A, ''et al.'' |title=Hypomyelination and increased activity of voltage-gated K(+) channels in mice lacking protein tyrosine phosphatase epsilon. |journal=EMBO J. |volume=19 |issue= 15 |pages= 4036-45 |year= 2000 |pmid= 10921884 |doi= 10.1093/emboj/19.15.4036 }}
*{{cite journal | author=Nitabach MN, Llamas DA, Araneda RC, ''et al.'' |title=A mechanism for combinatorial regulation of electrical activity: Potassium channel subunits capable of functioning as Src homology 3-dependent adaptors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 2 |pages= 705-10 |year= 2001 |pmid= 11149959 |doi= 10.1073/pnas.031446198 }}
*{{cite journal | author=Cukovic D, Lu GW, Wible B, ''et al.'' |title=A discrete amino terminal domain of Kv1.5 and Kv1.4 potassium channels interacts with the spectrin repeats of alpha-actinin-2. |journal=FEBS Lett. |volume=498 |issue= 1 |pages= 87-92 |year= 2001 |pmid= 11389904 |doi= }}
*{{cite journal | author=Kurata HT, Soon GS, Eldstrom JR, ''et al.'' |title=Amino-terminal determinants of U-type inactivation of voltage-gated K+ channels. |journal=J. Biol. Chem. |volume=277 |issue= 32 |pages= 29045-53 |year= 2002 |pmid= 12021261 |doi= 10.1074/jbc.M111470200 }}
*{{cite journal | author=Williams CP, Hu N, Shen W, ''et al.'' |title=Modulation of the human Kv1.5 channel by protein kinase C activation: role of the Kvbeta1.2 subunit. |journal=J. Pharmacol. Exp. Ther. |volume=302 |issue= 2 |pages= 545-50 |year= 2002 |pmid= 12130714 |doi= 10.1124/jpet.102.033357 }}
*{{cite journal | author=Eldstrom J, Doerksen KW, Steele DF, Fedida D |title=N-terminal PDZ-binding domain in Kv1 potassium channels. |journal=FEBS Lett. |volume=531 |issue= 3 |pages= 529-37 |year= 2002 |pmid= 12435606 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Zhang S, Kurata HT, Kehl SJ, Fedida D |title=Rapid induction of P/C-type inactivation is the mechanism for acid-induced K+ current inhibition. |journal=J. Gen. Physiol. |volume=121 |issue= 3 |pages= 215-25 |year= 2003 |pmid= 12601085 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MEF2C... {November 17, 2007 1:40:02 PM PST}
- SEARCH REDIRECT: Control Box Found: MEF2C {November 17, 2007 1:40:35 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 1:40:36 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 1:40:36 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 1:40:36 PM PST}
- UPDATED: Updated protein page: MEF2C {November 17, 2007 1:40:42 PM PST}
- INFO: Beginning work on NEFL... {November 17, 2007 1:40:42 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:41:24 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 =
| image_source =
| PDB =
| Name = Neurofilament, light polypeptide 68kDa
| HGNCid = 7739
| Symbol = NEFL
| AltSymbols =; CMT1F; CMT2E; NF-L; NF68; NFL
| OMIM = 162280
| ECnumber =
| Homologene = 4487
| MGIid = 97313
| GeneAtlas_image1 = PBB_GE_NEFL_221805_at_tn.png
| GeneAtlas_image2 = PBB_GE_NEFL_221801_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_NEFL_221916_at_tn.png
| Function = {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005882 |text = intermediate filament}} {{GNF_GO|id=GO:0005883 |text = neurofilament}} {{GNF_GO|id=GO:0030424 |text = axon}}
| Process = {{GNF_GO|id=GO:0045104 |text = intermediate filament cytoskeleton organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4747
| Hs_Ensembl = ENSG00000104725
| Hs_RefseqProtein = NP_006149
| Hs_RefseqmRNA = NM_006158
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 24866240
| Hs_GenLoc_end = 24869946
| Hs_Uniprot = P07196
| Mm_EntrezGene = 18039
| Mm_Ensembl = ENSMUSG00000022055
| Mm_RefseqmRNA = NM_010910
| Mm_RefseqProtein = NP_035040
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 67037214
| Mm_GenLoc_end = 67041075
| Mm_Uniprot = Q05DD2
}}
}}
'''Neurofilament, light polypeptide 68kDa''', also known as '''NEFL''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NEFL neurofilament, light polypeptide 68kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4747| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hirokawa N, Takeda S |title=Gene targeting studies begin to reveal the function of neurofilament proteins. |journal=J. Cell Biol. |volume=143 |issue= 1 |pages= 1-4 |year= 1998 |pmid= 9763415 |doi= }}
*{{cite journal | author=Beaudet L, Charron G, Julien JP |title=Origin of the two mRNA species for the human neurofilament light gene. |journal=Biochem. Cell Biol. |volume=70 |issue= 5 |pages= 279-84 |year= 1992 |pmid= 1497855 |doi= }}
*{{cite journal | author=Frappier T, Stetzkowski-Marden F, Pradel LA |title=Interaction domains of neurofilament light chain and brain spectrin. |journal=Biochem. J. |volume=275 ( Pt 2) |issue= |pages= 521-7 |year= 1991 |pmid= 1902666 |doi= }}
*{{cite journal | author=Chin SS, Liem RK |title=Expression of rat neurofilament proteins NF-L and NF-M in transfected non-neuronal cells. |journal=Eur. J. Cell Biol. |volume=50 |issue= 2 |pages= 475-90 |year= 1990 |pmid= 2516804 |doi= }}
*{{cite journal | author=Julien JP, Grosveld F, Yazdanbaksh K, ''et al.'' |title=The structure of a human neurofilament gene (NF-L): a unique exon-intron organization in the intermediate filament gene family. |journal=Biochim. Biophys. Acta |volume=909 |issue= 1 |pages= 10-20 |year= 1987 |pmid= 3034332 |doi= }}
*{{cite journal | author=Hurst J, Flavell D, Julien JP, ''et al.'' |title=The human neurofilament gene (NEFL) is located on the short arm of chromosome 8. |journal=Cytogenet. Cell Genet. |volume=45 |issue= 1 |pages= 30-2 |year= 1987 |pmid= 3036423 |doi= }}
*{{cite journal | author=Frappier T, Regnouf F, Pradel LA |title=Binding of brain spectrin to the 70-kDa neurofilament subunit protein. |journal=Eur. J. Biochem. |volume=169 |issue= 3 |pages= 651-7 |year= 1988 |pmid= 3121319 |doi= }}
*{{cite journal | author=Nomata Y, Watanabe T, Wada H |title=Highly acidic proteins from human brain: purification and properties of Glu-50 protein. |journal=J. Biochem. |volume=93 |issue= 3 |pages= 825-31 |year= 1983 |pmid= 6135695 |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=Pospelov VA, Pospelova TV, Julien JP |title=AP-1 and Krox-24 transcription factors activate the neurofilament light gene promoter in P19 embryonal carcinoma cells. |journal=Cell Growth Differ. |volume=5 |issue= 2 |pages= 187-96 |year= 1994 |pmid= 8180132 |doi= }}
*{{cite journal | author=Dong DL, Xu ZS, Chevrier MR, ''et al.'' |title=Glycosylation of mammalian neurofilaments. Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. |journal=J. Biol. Chem. |volume=268 |issue= 22 |pages= 16679-87 |year= 1993 |pmid= 8344946 |doi= }}
*{{cite journal | author=Charron G, Guy LG, Bazinet M, Julien JP |title=Multiple neuron-specific enhancers in the gene coding for the human neurofilament light chain. |journal=J. Biol. Chem. |volume=270 |issue= 51 |pages= 30604-10 |year= 1996 |pmid= 8530496 |doi= }}
*{{cite journal | author=Mukai H, Toshimori M, Shibata H, ''et al.'' |title=PKN associates and phosphorylates the head-rod domain of neurofilament protein. |journal=J. Biol. Chem. |volume=271 |issue= 16 |pages= 9816-22 |year= 1996 |pmid= 8621664 |doi= }}
*{{cite journal | author=Rosengren LE, Karlsson JE, Karlsson JO, ''et al.'' |title=Patients with amyotrophic lateral sclerosis and other neurodegenerative diseases have increased levels of neurofilament protein in CSF. |journal=J. Neurochem. |volume=67 |issue= 5 |pages= 2013-8 |year= 1996 |pmid= 8863508 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Athlan ES, Mushynski WE |title=Heterodimeric associations between neuronal intermediate filament proteins. |journal=J. Biol. Chem. |volume=272 |issue= 49 |pages= 31073-8 |year= 1998 |pmid= 9388258 |doi= }}
*{{cite journal | author=Ehlers MD, Fung ET, O'Brien RJ, Huganir RL |title=Splice variant-specific interaction of the NMDA receptor subunit NR1 with neuronal intermediate filaments. |journal=J. Neurosci. |volume=18 |issue= 2 |pages= 720-30 |year= 1998 |pmid= 9425014 |doi= }}
*{{cite journal | author=Mersiyanova IV, Perepelov AV, Polyakov AV, ''et al.'' |title=A new variant of Charcot-Marie-Tooth disease type 2 is probably the result of a mutation in the neurofilament-light gene. |journal=Am. J. Hum. Genet. |volume=67 |issue= 1 |pages= 37-46 |year= 2000 |pmid= 10841809 |doi= }}
*{{cite journal | author=De Jonghe P, Mersivanova I, Nelis E, ''et al.'' |title=Further evidence that neurofilament light chain gene mutations can cause Charcot-Marie-Tooth disease type 2E. |journal=Ann. Neurol. |volume=49 |issue= 2 |pages= 245-9 |year= 2001 |pmid= 11220745 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on OPTN... {November 17, 2007 1:50:31 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:51:14 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Optineurin
| HGNCid = 17142
| Symbol = OPTN
| AltSymbols =; NRP; FIP2; GLC1E; HIP7; HYPL; TFIIIA-INTP
| OMIM = 602432
| ECnumber =
| Homologene = 11085
| MGIid = 1918898
| GeneAtlas_image1 = PBB_GE_OPTN_202073_at_tn.png
| GeneAtlas_image2 = PBB_GE_OPTN_202074_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008022 |text = protein C-terminus binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}}
| Process = {{GNF_GO|id=GO:0000042 |text = protein targeting to Golgi}} {{GNF_GO|id=GO:0007030 |text = Golgi organization and biogenesis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0008219 |text = cell death}} {{GNF_GO|id=GO:0043001 |text = Golgi to plasma membrane protein transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10133
| Hs_Ensembl = ENSG00000123240
| Hs_RefseqProtein = NP_001008212
| Hs_RefseqmRNA = NM_001008211
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 13181455
| Hs_GenLoc_end = 13220297
| Hs_Uniprot = Q96CV9
| Mm_EntrezGene = 71648
| Mm_Ensembl = ENSMUSG00000026672
| Mm_RefseqmRNA = NM_181848
| Mm_RefseqProtein = NP_862896
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 4937914
| Mm_GenLoc_end = 4981210
| Mm_Uniprot = Q8K3K8
}}
}}
'''Optineurin''', also known as '''OPTN''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: OPTN optineurin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10133| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes the coiled-coil containing protein optineurin. Optineurin may play a role in normal-tension glaucoma and adult-onset primary open angle glaucoma. Optineurin interacts with adenovirus E3-14.7K protein and may utilize tumor necrosis factor-alpha or Fas-ligand pathways to mediate apoptosis, inflammation or vasoconstriction. Optineurin may also function in cellular morphogenesis and membrane trafficking, vesicle trafficking, and transcription activation through its interactions with the RAB8, huntingtin, and transcription factor IIIA proteins. Alternative splicing results in multiple transcript variants encoding the same protein.<ref name="entrez">{{cite web | title = Entrez Gene: OPTN optineurin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10133| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Sarfarazi M, Rezaie T |title=Optineurin in primary open angle glaucoma. |journal=Ophthalmology clinics of North America |volume=16 |issue= 4 |pages= 529-41 |year= 2004 |pmid= 14740994 |doi= }}
*{{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=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi= }}
*{{cite journal | author=Li Y, Kang J, Horwitz MS |title=Interaction of an adenovirus E3 14.7-kilodalton protein with a novel tumor necrosis factor alpha-inducible cellular protein containing leucine zipper domains. |journal=Mol. Cell. Biol. |volume=18 |issue= 3 |pages= 1601-10 |year= 1998 |pmid= 9488477 |doi= }}
*{{cite journal | author=Sarfarazi M, Child A, Stoilova D, ''et al.'' |title=Localization of the fourth locus (GLC1E) for adult-onset primary open-angle glaucoma to the 10p15-p14 region. |journal=Am. J. Hum. Genet. |volume=62 |issue= 3 |pages= 641-52 |year= 1998 |pmid= 9497264 |doi= }}
*{{cite journal | author=Faber PW, Barnes GT, Srinidhi J, ''et al.'' |title=Huntingtin interacts with a family of WW domain proteins. |journal=Hum. Mol. Genet. |volume=7 |issue= 9 |pages= 1463-74 |year= 1998 |pmid= 9700202 |doi= }}
*{{cite journal | author=Fong KS, de Couet HG |title=Novel proteins interacting with the leucine-rich repeat domain of human flightless-I identified by the yeast two-hybrid system. |journal=Genomics |volume=58 |issue= 2 |pages= 146-57 |year= 1999 |pmid= 10366446 |doi= 10.1006/geno.1999.5817 }}
*{{cite journal | author=Moreland RJ, Dresser ME, Rodgers JS, ''et al.'' |title=Identification of a transcription factor IIIA-interacting protein. |journal=Nucleic Acids Res. |volume=28 |issue= 9 |pages= 1986-93 |year= 2000 |pmid= 10756201 |doi= }}
*{{cite journal | author=Schwamborn K, Weil R, Courtois G, ''et al.'' |title=Phorbol esters and cytokines regulate the expression of the NEMO-related protein, a molecule involved in a NF-kappa B-independent pathway. |journal=J. Biol. Chem. |volume=275 |issue= 30 |pages= 22780-9 |year= 2000 |pmid= 10807909 |doi= 10.1074/jbc.M001500200 }}
*{{cite journal | author=Hattula K, Peränen J |title=FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis. |journal=Curr. Biol. |volume=10 |issue= 24 |pages= 1603-6 |year= 2001 |pmid= 11137014 |doi= }}
*{{cite journal | author=Hales CM, Griner R, Hobdy-Henderson KC, ''et al.'' |title=Identification and characterization of a family of Rab11-interacting proteins. |journal=J. Biol. Chem. |volume=276 |issue= 42 |pages= 39067-75 |year= 2001 |pmid= 11495908 |doi= 10.1074/jbc.M104831200 }}
*{{cite journal | author=Rezaie T, Child A, Hitchings R, ''et al.'' |title=Adult-onset primary open-angle glaucoma caused by mutations in optineurin. |journal=Science |volume=295 |issue= 5557 |pages= 1077-9 |year= 2002 |pmid= 11834836 |doi= 10.1126/science.1066901 }}
*{{cite journal | author=Vittitow J, Borrás T |title=Expression of optineurin, a glaucoma-linked gene, is influenced by elevated intraocular pressure. |journal=Biochem. Biophys. Res. Commun. |volume=298 |issue= 1 |pages= 67-74 |year= 2002 |pmid= 12379221 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Kamphuis W, Schneemann A |title=Optineurin gene expression level in human trabecular meshwork does not change in response to pressure elevation. |journal=Ophthalmic Res. |volume=35 |issue= 2 |pages= 93-6 |year= 2003 |pmid= 12646749 |doi= 10.1159/000069133 }}
*{{cite journal | author=Tang S, Toda Y, Kashiwagi K, ''et al.'' |title=The association between Japanese primary open-angle glaucoma and normal tension glaucoma patients and the optineurin gene. |journal=Hum. Genet. |volume=113 |issue= 3 |pages= 276-9 |year= 2003 |pmid= 12811537 |doi= 10.1007/s00439-003-0964-y }}
*{{cite journal | author=Wiggs JL, Auguste J, Allingham RR, ''et al.'' |title=Lack of association of mutations in optineurin with disease in patients with adult-onset primary open-angle glaucoma. |journal=Arch. Ophthalmol. |volume=121 |issue= 8 |pages= 1181-3 |year= 2003 |pmid= 12912697 |doi= 10.1001/archopht.121.8.1181 }}
*{{cite journal | author=Aung T, Ebenezer ND, Brice G, ''et al.'' |title=Prevalence of optineurin sequence variants in adult primary open angle glaucoma: implications for diagnostic testing. |journal=J. Med. Genet. |volume=40 |issue= 8 |pages= e101 |year= 2003 |pmid= 12920093 |doi= }}
*{{cite journal | author=Leung YF, Fan BJ, Lam DS, ''et al.'' |title=Different optineurin mutation pattern in primary open-angle glaucoma. |journal=Invest. Ophthalmol. Vis. Sci. |volume=44 |issue= 9 |pages= 3880-4 |year= 2003 |pmid= 12939304 |doi= }}
*{{cite journal | author=Alward WL, Kwon YH, Kawase K, ''et al.'' |title=Evaluation of optineurin sequence variations in 1,048 patients with open-angle glaucoma. |journal=Am. J. Ophthalmol. |volume=136 |issue= 5 |pages= 904-10 |year= 2003 |pmid= 14597044 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PGK1... {November 17, 2007 1:41:24 PM PST}
- SEARCH REDIRECT: Control Box Found: PGK1 {November 17, 2007 1:42:05 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 1:42:06 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 1:42:06 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 1:42:06 PM PST}
- UPDATED: Updated protein page: PGK1 {November 17, 2007 1:43:29 PM PST}
- INFO: Beginning work on PITX2... {November 17, 2007 1:43:29 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:44:21 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PITX2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1yz8.
| PDB = {{PDB2|1yz8}}
| Name = Paired-like homeodomain transcription factor 2
| HGNCid = 9005
| Symbol = PITX2
| AltSymbols =; PTX2; ARP1; Brx1; IDG2; IGDS; IGDS2; IHG2; IRID2; MGC111022; MGC20144; Otlx2; RGS; RIEG; RIEG1; RS
| OMIM = 601542
| ECnumber =
| Homologene = 55454
| MGIid = 109340
| GeneAtlas_image1 = PBB_GE_PITX2_207558_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0008134 |text = transcription factor binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005667 |text = transcription factor complex}}
| Process = {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007368 |text = determination of left/right symmetry}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5308
| Hs_Ensembl = ENSG00000164093
| Hs_RefseqProtein = NP_000316
| Hs_RefseqmRNA = NM_000325
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 111758031
| Hs_GenLoc_end = 111782566
| Hs_Uniprot = Q99697
| Mm_EntrezGene = 18741
| Mm_Ensembl = ENSMUSG00000028023
| Mm_RefseqmRNA = NM_001042502
| Mm_RefseqProtein = NP_001035967
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 129191965
| Mm_GenLoc_end = 129211613
| Mm_Uniprot = P97474
}}
}}
'''Paired-like homeodomain transcription factor 2''', also known as '''PITX2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PITX2 paired-like homeodomain transcription factor 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5308| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the RIEG/PITX homeobox family, which is in the bicoid class of homeodomain proteins. This protein acts as a transcription factor and regulates procollagen lysyl hydroxylase gene expression. Mutations in this gene are associated with Axenfeld-Rieger syndrome (ARS), iridogoniodysgenesis syndrome (IGDS), and sporadic cases of Peters anomaly. This protein plays a role in the terminal differentiation of somatotroph and lactotroph cell phenotypes. This protein is involved in the development of the eye, tooth and abdominal organs. This protein acts as a transcriptional regulator involved in basal and hormone-regulated activity of prolactin. A similar protein in other vertebrates is involved in the determination of left-right asymmetry during development. Three transcript variants encoding distinct isoforms have been identified for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: PITX2 paired-like homeodomain transcription factor 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5308| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Franco D, Campione M |title=The role of Pitx2 during cardiac development. Linking left-right signaling and congenital heart diseases. |journal=Trends Cardiovasc. Med. |volume=13 |issue= 4 |pages= 157-63 |year= 2003 |pmid= 12732450 |doi= }}
*{{cite journal | author=Hjalt TA, Semina EV |title=Current molecular understanding of Axenfeld-Rieger syndrome. |journal=Expert reviews in molecular medicine |volume=7 |issue= 25 |pages= 1-17 |year= 2007 |pmid= 16274491 |doi= 10.1017/S1462399405010082 }}
*{{cite journal | author=Murray JC, Bennett SR, Kwitek AE, ''et al.'' |title=Linkage of Rieger syndrome to the region of the epidermal growth factor gene on chromosome 4. |journal=Nat. Genet. |volume=2 |issue= 1 |pages= 46-9 |year= 1993 |pmid= 1303248 |doi= 10.1038/ng0992-46 }}
*{{cite journal | author=Héon E, Sheth BP, Kalenak JW, ''et al.'' |title=Linkage of autosomal dominant iris hypoplasia to the region of the Rieger syndrome locus (4q25). |journal=Hum. Mol. Genet. |volume=4 |issue= 8 |pages= 1435-9 |year= 1995 |pmid= 7581385 |doi= }}
*{{cite journal | author=Walter MA, Mirzayans F, Mears AJ, ''et al.'' |title=Autosomal-dominant iridogoniodysgenesis and Axenfeld-Rieger syndrome are genetically distinct. |journal=Ophthalmology |volume=103 |issue= 11 |pages= 1907-15 |year= 1996 |pmid= 8942889 |doi= }}
*{{cite journal | author=Semina EV, Reiter R, Leysens NJ, ''et al.'' |title=Cloning and characterization of a novel bicoid-related homeobox transcription factor gene, RIEG, involved in Rieger syndrome. |journal=Nat. Genet. |volume=14 |issue= 4 |pages= 392-9 |year= 1997 |pmid= 8944018 |doi= 10.1038/ng1296-392 }}
*{{cite journal | author=Alward WL, Semina EV, Kalenak JW, ''et al.'' |title=Autosomal dominant iris hypoplasia is caused by a mutation in the Rieger syndrome (RIEG/PITX2) gene. |journal=Am. J. Ophthalmol. |volume=125 |issue= 1 |pages= 98-100 |year= 1998 |pmid= 9437321 |doi= }}
*{{cite journal | author=Arakawa H, Nakamura T, Zhadanov AB, ''et al.'' |title=Identification and characterization of the ARP1 gene, a target for the human acute leukemia ALL1 gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 8 |pages= 4573-8 |year= 1998 |pmid= 9539779 |doi= }}
*{{cite journal | author=Kulak SC, Kozlowski K, Semina EV, ''et al.'' |title=Mutation in the RIEG1 gene in patients with iridogoniodysgenesis syndrome. |journal=Hum. Mol. Genet. |volume=7 |issue= 7 |pages= 1113-7 |year= 1999 |pmid= 9618168 |doi= }}
*{{cite journal | author=Amendt BA, Sutherland LB, Semina EV, Russo AF |title=The molecular basis of Rieger syndrome. Analysis of Pitx2 homeodomain protein activities. |journal=J. Biol. Chem. |volume=273 |issue= 32 |pages= 20066-72 |year= 1998 |pmid= 9685346 |doi= }}
*{{cite journal | author=Yoshioka H, Meno C, Koshiba K, ''et al.'' |title=Pitx2, a bicoid-type homeobox gene, is involved in a lefty-signaling pathway in determination of left-right asymmetry. |journal=Cell |volume=94 |issue= 3 |pages= 299-305 |year= 1998 |pmid= 9708732 |doi= }}
*{{cite journal | author=Doward W, Perveen R, Lloyd IC, ''et al.'' |title=A mutation in the RIEG1 gene associated with Peters' anomaly. |journal=J. Med. Genet. |volume=36 |issue= 2 |pages= 152-5 |year= 1999 |pmid= 10051017 |doi= }}
*{{cite journal | author=Pellegrini-Bouiller I, Manrique C, Gunz G, ''et al.'' |title=Expression of the members of the Ptx family of transcription factors in human pituitary adenomas. |journal=J. Clin. Endocrinol. Metab. |volume=84 |issue= 6 |pages= 2212-20 |year= 1999 |pmid= 10372733 |doi= }}
*{{cite journal | author=Hjalt TA, Amendt BA, Murray JC |title=PITX2 regulates procollagen lysyl hydroxylase (PLOD) gene expression: implications for the pathology of Rieger syndrome. |journal=J. Cell Biol. |volume=152 |issue= 3 |pages= 545-52 |year= 2001 |pmid= 11157981 |doi= }}
*{{cite journal | author=Priston M, Kozlowski K, Gill D, ''et al.'' |title=Functional analyses of two newly identified PITX2 mutants reveal a novel molecular mechanism for Axenfeld-Rieger syndrome. |journal=Hum. Mol. Genet. |volume=10 |issue= 16 |pages= 1631-8 |year= 2001 |pmid= 11487566 |doi= }}
*{{cite journal | author=Green PD, Hjalt TA, Kirk DE, ''et al.'' |title=Antagonistic regulation of Dlx2 expression by PITX2 and Msx2: implications for tooth development. |journal=Gene Expr. |volume=9 |issue= 6 |pages= 265-81 |year= 2002 |pmid= 11763998 |doi= }}
*{{cite journal | author=Vincent AL, Billingsley G, Buys Y, ''et al.'' |title=Digenic inheritance of early-onset glaucoma: CYP1B1, a potential modifier gene. |journal=Am. J. Hum. Genet. |volume=70 |issue= 2 |pages= 448-60 |year= 2002 |pmid= 11774072 |doi= }}
*{{cite journal | author=Borges AS, Susanna R, Carani JC, ''et al.'' |title=Genetic analysis of PITX2 and FOXC1 in Rieger Syndrome patients from Brazil. |journal=J. Glaucoma |volume=11 |issue= 1 |pages= 51-6 |year= 2002 |pmid= 11821690 |doi= }}
*{{cite journal | author=Cox CJ, Espinoza HM, McWilliams B, ''et al.'' |title=Differential regulation of gene expression by PITX2 isoforms. |journal=J. Biol. Chem. |volume=277 |issue= 28 |pages= 25001-10 |year= 2002 |pmid= 11948188 |doi= 10.1074/jbc.M201737200 }}
*{{cite journal | author=Quentien MH, Pitoia F, Gunz G, ''et al.'' |title=Regulation of prolactin, GH, and Pit-1 gene expression in anterior pituitary by Pitx2: An approach using Pitx2 mutants. |journal=Endocrinology |volume=143 |issue= 8 |pages= 2839-51 |year= 2002 |pmid= 12130547 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on POLI... {November 17, 2007 1:51:14 PM PST}
- SEARCH REDIRECT: Control Box Found: POLI {November 17, 2007 1:51:36 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 1:51:37 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 1:51:37 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 1:51:37 PM PST}
- UPDATED: Updated protein page: POLI {November 17, 2007 1:51:43 PM PST}
- INFO: Beginning work on PSMA2... {November 17, 2007 1:44:58 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:45:28 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PSMA2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1iru.
| PDB = {{PDB2|1iru}}
| Name = Proteasome (prosome, macropain) subunit, alpha type, 2
| HGNCid = 9531
| Symbol = PSMA2
| AltSymbols =; MU; HC3; PMSA2; PSC2
| OMIM = 176842
| ECnumber =
| Homologene = 2081
| MGIid = 104885
| GeneAtlas_image1 = PBB_GE_PSMA2_201317_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PSMA2_201316_at_tn.png
| Function = {{GNF_GO|id=GO:0004298 |text = threonine endopeptidase activity}}
| Component = {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005839 |text = proteasome core complex (sensu Eukaryota)}}
| Process = {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5683
| Hs_Ensembl = ENSG00000106588
| Hs_RefseqProtein = NP_002778
| Hs_RefseqmRNA = NM_002787
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 42922989
| Hs_GenLoc_end = 42938330
| Hs_Uniprot = P25787
| Mm_EntrezGene = 19166
| Mm_Ensembl = ENSMUSG00000015671
| Mm_RefseqmRNA = NM_008944
| Mm_RefseqProtein = NP_032970
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 14405380
| Mm_GenLoc_end = 14419533
| Mm_Uniprot = Q3UWT6
}}
}}
'''Proteasome (prosome, macropain) subunit, alpha type, 2''', also known as '''PSMA2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMA2 proteasome (prosome, macropain) subunit, alpha type, 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5683| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the peptidase T1A family, that is a 20S core alpha subunit.<ref name="entrez">{{cite web | title = Entrez Gene: PSMA2 proteasome (prosome, macropain) subunit, alpha type, 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5683| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Coux O, Tanaka K, Goldberg AL |title=Structure and functions of the 20S and 26S proteasomes. |journal=Annu. Rev. Biochem. |volume=65 |issue= |pages= 801-47 |year= 1996 |pmid= 8811196 |doi= 10.1146/annurev.bi.65.070196.004101 }}
*{{cite journal | author=Goff SP |title=Death by deamination: a novel host restriction system for HIV-1. |journal=Cell |volume=114 |issue= 3 |pages= 281-3 |year= 2003 |pmid= 12914693 |doi= }}
*{{cite journal | author=DeMartino GN, Orth K, McCullough ML, ''et al.'' |title=The primary structures of four subunits of the human, high-molecular-weight proteinase, macropain (proteasome), are distinct but homologous. |journal=Biochim. Biophys. Acta |volume=1079 |issue= 1 |pages= 29-38 |year= 1991 |pmid= 1888762 |doi= }}
*{{cite journal | author=Tamura T, Lee DH, Osaka F, ''et al.'' |title=Molecular cloning and sequence analysis of cDNAs for five major subunits of human proteasomes (multi-catalytic proteinase complexes). |journal=Biochim. Biophys. Acta |volume=1089 |issue= 1 |pages= 95-102 |year= 1991 |pmid= 2025653 |doi= }}
*{{cite journal | author=Okumura K, Nogami M, Taguchi H, ''et al.'' |title=The genes for the alpha-type HC3 (PMSA2) and beta-type HC5 (PMSB1) subunits of human proteasomes map to chromosomes 6q27 and 7p12-p13 by fluorescence in situ hybridization. |journal=Genomics |volume=27 |issue= 2 |pages= 377-9 |year= 1995 |pmid= 7558012 |doi= 10.1006/geno.1995.1062 }}
*{{cite journal | author=Kristensen P, Johnsen AH, Uerkvitz W, ''et al.'' |title=Human proteasome subunits from 2-dimensional gels identified by partial sequencing. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 3 |pages= 1785-9 |year= 1995 |pmid= 7811265 |doi= }}
*{{cite journal | author=Tamura T, Osaka F, Kawamura Y, ''et al.'' |title=Isolation and characterization of alpha-type HC3 and beta-type HC5 subunit genes of human proteasomes. |journal=J. Mol. Biol. |volume=244 |issue= 1 |pages= 117-24 |year= 1994 |pmid= 7966316 |doi= 10.1006/jmbi.1994.1710 }}
*{{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=Knuehl C, Seelig A, Brecht B, ''et al.'' |title=Functional analysis of eukaryotic 20S proteasome nuclear localization signal. |journal=Exp. Cell Res. |volume=225 |issue= 1 |pages= 67-74 |year= 1996 |pmid= 8635518 |doi= 10.1006/excr.1996.0157 }}
*{{cite journal | author=Seeger M, Ferrell K, Frank R, Dubiel W |title=HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8145-8 |year= 1997 |pmid= 9079628 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Madani N, Kabat D |title=An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. |journal=J. Virol. |volume=72 |issue= 12 |pages= 10251-5 |year= 1998 |pmid= 9811770 |doi= }}
*{{cite journal | author=Simon JH, Gaddis NC, Fouchier RA, Malim MH |title=Evidence for a newly discovered cellular anti-HIV-1 phenotype. |journal=Nat. Med. |volume=4 |issue= 12 |pages= 1397-400 |year= 1998 |pmid= 9846577 |doi= 10.1038/3987 }}
*{{cite journal | author=Elenich LA, Nandi D, Kent AE, ''et al.'' |title=The complete primary structure of mouse 20S proteasomes. |journal=Immunogenetics |volume=49 |issue= 10 |pages= 835-42 |year= 1999 |pmid= 10436176 |doi= }}
*{{cite journal | author=Mulder LC, Muesing MA |title=Degradation of HIV-1 integrase by the N-end rule pathway. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29749-53 |year= 2000 |pmid= 10893419 |doi= 10.1074/jbc.M004670200 }}
*{{cite journal | author=Kleijnen MF, Shih AH, Zhou P, ''et al.'' |title=The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome. |journal=Mol. Cell |volume=6 |issue= 2 |pages= 409-19 |year= 2000 |pmid= 10983987 |doi= }}
*{{cite journal | author=Sheehy AM, Gaddis NC, Choi JD, Malim MH |title=Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. |journal=Nature |volume=418 |issue= 6898 |pages= 646-50 |year= 2002 |pmid= 12167863 |doi= 10.1038/nature00939 }}
*{{cite journal | author=Huang X, Seifert U, Salzmann U, ''et al.'' |title=The RTP site shared by the HIV-1 Tat protein and the 11S regulator subunit alpha is crucial for their effects on proteasome function including antigen processing. |journal=J. Mol. Biol. |volume=323 |issue= 4 |pages= 771-82 |year= 2002 |pmid= 12419264 |doi= }}
*{{cite journal | author=Bommel H, Xie G, Rossoll W, ''et al.'' |title=Missense mutation in the tubulin-specific chaperone E (Tbce) gene in the mouse mutant progressive motor neuronopathy, a model of human motoneuron disease. |journal=J. Cell Biol. |volume=159 |issue= 4 |pages= 563-9 |year= 2003 |pmid= 12446740 |doi= 10.1083/jcb.200208001 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PTPRF... {November 17, 2007 1:45:28 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:46:01 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_PTPRF_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1lar.
| PDB = {{PDB2|1lar}}, {{PDB2|2dju}}, {{PDB2|2dn7}}
| Name = Protein tyrosine phosphatase, receptor type, F
| HGNCid = 9670
| Symbol = PTPRF
| AltSymbols =; FLJ43335; FLJ45062; FLJ45567; LAR
| OMIM = 179590
| ECnumber =
| Homologene = 20623
| MGIid = 102695
| GeneAtlas_image1 = PBB_GE_PTPRF_200636_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PTPRF_200635_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_PTPRF_200637_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004725 |text = protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005001 |text = transmembrane receptor protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006470 |text = protein amino acid dephosphorylation}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007185 |text = transmembrane receptor protein tyrosine phosphatase signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5792
| Hs_Ensembl = ENSG00000142949
| Hs_RefseqProtein = NP_002831
| Hs_RefseqmRNA = NM_002840
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 43769134
| Hs_GenLoc_end = 43861924
| Hs_Uniprot = P10586
| Mm_EntrezGene = 19268
| Mm_Ensembl = ENSMUSG00000033295
| Mm_RefseqmRNA = NM_011213
| Mm_RefseqProtein = NP_035343
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 117707733
| Mm_GenLoc_end = 117775378
| Mm_Uniprot =
}}
}}
'''Protein tyrosine phosphatase, receptor type, F''', also known as '''PTPRF''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTPRF protein tyrosine phosphatase, receptor type, F| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5792| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains three Ig-like domains, and nine non-Ig like domains similar to that of neural-cell adhesion molecule. This PTP was shown to function in the regulation of epithelial cell-cell contacts at adherents junctions, as well as in the control of beta-catenin signaling. An increased expression level of this protein was found in the insulin-responsive tissue of obese, insulin-resistant individuals, and may contribute to the pathogenesis of insulin resistance. Two alternatively spliced transcript variants of this gene, which encode distinct proteins, have been reported.<ref name="entrez">{{cite web | title = Entrez Gene: PTPRF protein tyrosine phosphatase, receptor type, F| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5792| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Chernoff J |title=Protein tyrosine phosphatases as negative regulators of mitogenic signaling. |journal=J. Cell. Physiol. |volume=180 |issue= 2 |pages= 173-81 |year= 1999 |pmid= 10395287 |doi= 10.1002/(SICI)1097-4652(199908)180:2<173::AID-JCP5>3.0.CO;2-Y }}
*{{cite journal | author=Hashimoto N, Feener EP, Zhang WR, Goldstein BJ |title=Insulin receptor protein-tyrosine phosphatases. Leukocyte common antigen-related phosphatase rapidly deactivates the insulin receptor kinase by preferential dephosphorylation of the receptor regulatory domain. |journal=J. Biol. Chem. |volume=267 |issue= 20 |pages= 13811-4 |year= 1992 |pmid= 1321126 |doi= }}
*{{cite journal | author=Jirik FR, Harder KW, Melhado IG, ''et al.'' |title=The gene for leukocyte antigen-related tyrosine phosphatase (LAR) is localized to human chromosome 1p32, a region frequently deleted in tumors of neuroectodermal origin. |journal=Cytogenet. Cell Genet. |volume=61 |issue= 4 |pages= 266-8 |year= 1993 |pmid= 1486801 |doi= }}
*{{cite journal | author=Streuli M, Krueger NX, Thai T, ''et al.'' |title=Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR. |journal=EMBO J. |volume=9 |issue= 8 |pages= 2399-407 |year= 1990 |pmid= 1695146 |doi= }}
*{{cite journal | author=Streuli M, Krueger NX, Tsai AY, Saito H |title=A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 22 |pages= 8698-702 |year= 1989 |pmid= 2554325 |doi= }}
*{{cite journal | author=Streuli M, Krueger NX, Hall LR, ''et al.'' |title=A new member of the immunoglobulin superfamily that has a cytoplasmic region homologous to the leukocyte common antigen. |journal=J. Exp. Med. |volume=168 |issue= 5 |pages= 1523-30 |year= 1988 |pmid= 2972792 |doi= }}
*{{cite journal | author=Harder KW, Saw J, Miki N, Jirik F |title=Coexisting amplifications of the chromosome 1p32 genes (PTPRF and MYCL1) encoding protein tyrosine phosphatase LAR and L-myc in a small cell lung cancer line. |journal=Genomics |volume=27 |issue= 3 |pages= 552-3 |year= 1995 |pmid= 7558042 |doi= 10.1006/geno.1995.1092 }}
*{{cite journal | author=Schaapveld RQ, van den Maagdenberg AM, Schepens JT, ''et al.'' |title=The mouse gene Ptprf encoding the leukocyte common antigen-related molecule LAR: cloning, characterization, and chromosomal localization. |journal=Genomics |volume=27 |issue= 1 |pages= 124-30 |year= 1995 |pmid= 7665159 |doi= }}
*{{cite journal | author=Serra-Pagès C, Kedersha NL, Fazikas L, ''et al.'' |title=The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions. |journal=EMBO J. |volume=14 |issue= 12 |pages= 2827-38 |year= 1995 |pmid= 7796809 |doi= }}
*{{cite journal | author=O'Grady P, Krueger NX, Streuli M, Saito H |title=Genomic organization of the human LAR protein tyrosine phosphatase gene and alternative splicing in the extracellular fibronectin type-III domains. |journal=J. Biol. Chem. |volume=269 |issue= 40 |pages= 25193-9 |year= 1994 |pmid= 7929208 |doi= }}
*{{cite journal | author=Pulido R, Serra-Pagès C, Tang M, Streuli M |title=The LAR/PTP delta/PTP sigma subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 25 |pages= 11686-90 |year= 1996 |pmid= 8524829 |doi= }}
*{{cite journal | author=Liu X, Vega QC, Decker RA, ''et al.'' |title=Oncogenic RET receptors display different autophosphorylation sites and substrate binding specificities. |journal=J. Biol. Chem. |volume=271 |issue= 10 |pages= 5309-12 |year= 1996 |pmid= 8621380 |doi= }}
*{{cite journal | author=Debant A, Serra-Pagès C, Seipel K, ''et al.'' |title=The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 11 |pages= 5466-71 |year= 1996 |pmid= 8643598 |doi= }}
*{{cite journal | author=Zhang WR, Li PM, Oswald MA, Goldstein BJ |title=Modulation of insulin signal transduction by eutopic overexpression of the receptor-type protein-tyrosine phosphatase LAR. |journal=Mol. Endocrinol. |volume=10 |issue= 5 |pages= 575-84 |year= 1996 |pmid= 8732688 |doi= }}
*{{cite journal | author=Tabiti K, Cui L, Chhatwal VJ, ''et al.'' |title=Novel alternative splicing predicts a secreted extracellular isoform of the human receptor-like protein tyrosine phosphatase LAR. |journal=Gene |volume=175 |issue= 1-2 |pages= 7-13 |year= 1996 |pmid= 8917069 |doi= }}
*{{cite journal | author=Ahmad F, Goldstein BJ |title=Functional association between the insulin receptor and the transmembrane protein-tyrosine phosphatase LAR in intact cells. |journal=J. Biol. Chem. |volume=272 |issue= 1 |pages= 448-57 |year= 1997 |pmid= 8995282 |doi= }}
*{{cite journal | author=Aicher B, Lerch MM, Müller T, ''et al.'' |title=Cellular redistribution of protein tyrosine phosphatases LAR and PTPsigma by inducible proteolytic processing. |journal=J. Cell Biol. |volume=138 |issue= 3 |pages= 681-96 |year= 1997 |pmid= 9245795 |doi= }}
*{{cite journal | author=Serra-Pagès C, Medley QG, Tang M, ''et al.'' |title=Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins. |journal=J. Biol. Chem. |volume=273 |issue= 25 |pages= 15611-20 |year= 1998 |pmid= 9624153 |doi= }}
*{{cite journal | author=O'Grady P, Thai TC, Saito H |title=The laminin-nidogen complex is a ligand for a specific splice isoform of the transmembrane protein tyrosine phosphatase LAR. |journal=J. Cell Biol. |volume=141 |issue= 7 |pages= 1675-84 |year= 1998 |pmid= 9647658 |doi= }}
*{{cite journal | author=Chiplunkar S, Chamblis K, Chwa M, ''et al.'' |title=Enhanced expression of a transmembrane phosphotyrosine phosphatase (LAR) in keratoconus cultures and corneas. |journal=Exp. Eye Res. |volume=68 |issue= 3 |pages= 283-93 |year= 1999 |pmid= 10079136 |doi= 10.1006/exer.1998.0604 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PYCARD... {November 17, 2007 1:51:43 PM PST}
- UPLOAD: Added new Image to wiki: File:PBB Protein PYCARD image.jpg {November 17, 2007 1:52:01 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:52:19 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_PYCARD_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ucp.
| PDB = {{PDB2|1ucp}}
| Name = PYD and CARD domain containing
| HGNCid = 16608
| Symbol = PYCARD
| AltSymbols =; ASC; CARD5; MGC10332; TMS1
| OMIM = 606838
| ECnumber =
| Homologene = 8307
| MGIid = 1931465
| GeneAtlas_image1 = PBB_GE_PYCARD_221666_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008656 |text = caspase activator activity}} {{GNF_GO|id=GO:0030693 |text = caspase activity}} {{GNF_GO|id=GO:0032090 |text = Pyrin domain binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0006919 |text = caspase activation}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}} {{GNF_GO|id=GO:0050718 |text = positive regulation of interleukin-1 beta secretion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 29108
| Hs_Ensembl = ENSG00000103490
| Hs_RefseqProtein = NP_037390
| Hs_RefseqmRNA = NM_013258
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 31120310
| Hs_GenLoc_end = 31121512
| Hs_Uniprot = Q9ULZ3
| Mm_EntrezGene = 66824
| Mm_Ensembl = ENSMUSG00000030793
| Mm_RefseqmRNA = NM_023258
| Mm_RefseqProtein = NP_075747
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 127783251
| Mm_GenLoc_end = 127784895
| Mm_Uniprot = Q54AA2
}}
}}
'''PYD and CARD domain containing''', also known as '''PYCARD''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PYCARD PYD and CARD domain containing| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29108| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes an adaptor protein that is composed of two protein-protein interaction domains: a N-terminal PYRIN-PAAD-DAPIN domain (PYD) and a C-terminal caspase-recruitment domain (CARD). The PYD and CARD domains are members of the six-helix bundle death domain-fold superfamily that mediates assembly of large signaling complexes in the inflammatory and apoptotic signaling pathways via the activation of caspase. In normal cells, this protein is localized to the cytoplasm; however, in cells undergoing apoptosis, it forms ball-like aggregates near the nuclear periphery. Two transcript variants encoding different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: PYCARD PYD and CARD domain containing| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29108| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Masumoto J, Taniguchi S, Ayukawa K, ''et al.'' |title=ASC, a novel 22-kDa protein, aggregates during apoptosis of human promyelocytic leukemia HL-60 cells. |journal=J. Biol. Chem. |volume=274 |issue= 48 |pages= 33835-8 |year= 1999 |pmid= 10567338 |doi= }}
*{{cite journal | author=Lee SK, Na SY, Jung SY, ''et al.'' |title=Activating protein-1, nuclear factor-kappaB, and serum response factor as novel target molecules of the cancer-amplified transcription coactivator ASC-2. |journal=Mol. Endocrinol. |volume=14 |issue= 6 |pages= 915-25 |year= 2000 |pmid= 10847592 |doi= }}
*{{cite journal | author=Conway KE, McConnell BB, Bowring CE, ''et al.'' |title=TMS1, a novel proapoptotic caspase recruitment domain protein, is a target of methylation-induced gene silencing in human breast cancers. |journal=Cancer Res. |volume=60 |issue= 22 |pages= 6236-42 |year= 2000 |pmid= 11103776 |doi= }}
*{{cite journal | author=McConnell BB, Vertino PM |title=Activation of a caspase-9-mediated apoptotic pathway by subcellular redistribution of the novel caspase recruitment domain protein TMS1. |journal=Cancer Res. |volume=60 |issue= 22 |pages= 6243-7 |year= 2000 |pmid= 11103777 |doi= }}
*{{cite journal | author=Martinon F, Hofmann K, Tschopp J |title=The pyrin domain: a possible member of the death domain-fold family implicated in apoptosis and inflammation. |journal=Curr. Biol. |volume=11 |issue= 4 |pages= R118-20 |year= 2001 |pmid= 11250163 |doi= }}
*{{cite journal | author=Geddes BJ, Wang L, Huang WJ, ''et al.'' |title=Human CARD12 is a novel CED4/Apaf-1 family member that induces apoptosis. |journal=Biochem. Biophys. Res. Commun. |volume=284 |issue= 1 |pages= 77-82 |year= 2001 |pmid= 11374873 |doi= 10.1006/bbrc.2001.4928 }}
*{{cite journal | author=Richards N, Schaner P, Diaz A, ''et al.'' |title=Interaction between pyrin and the apoptotic speck protein (ASC) modulates ASC-induced apoptosis. |journal=J. Biol. Chem. |volume=276 |issue= 42 |pages= 39320-9 |year= 2001 |pmid= 11498534 |doi= 10.1074/jbc.M104730200 }}
*{{cite journal | author=Stimson KM, Vertino PM |title=Methylation-mediated silencing of TMS1/ASC is accompanied by histone hypoacetylation and CpG island-localized changes in chromatin architecture. |journal=J. Biol. Chem. |volume=277 |issue= 7 |pages= 4951-8 |year= 2002 |pmid= 11733524 |doi= 10.1074/jbc.M109809200 }}
*{{cite journal | author=Manji GA, Wang L, Geddes BJ, ''et al.'' |title=PYPAF1, a PYRIN-containing Apaf1-like protein that assembles with ASC and regulates activation of NF-kappa B. |journal=J. Biol. Chem. |volume=277 |issue= 13 |pages= 11570-5 |year= 2002 |pmid= 11786556 |doi= 10.1074/jbc.M112208200 }}
*{{cite journal | author=Srinivasula SM, Poyet JL, Razmara M, ''et al.'' |title=The PYRIN-CARD protein ASC is an activating adaptor for caspase-1. |journal=J. Biol. Chem. |volume=277 |issue= 24 |pages= 21119-22 |year= 2002 |pmid= 11967258 |doi= 10.1074/jbc.C200179200 }}
*{{cite journal | author=Wang L, Manji GA, Grenier JM, ''et al.'' |title=PYPAF7, a novel PYRIN-containing Apaf1-like protein that regulates activation of NF-kappa B and caspase-1-dependent cytokine processing. |journal=J. Biol. Chem. |volume=277 |issue= 33 |pages= 29874-80 |year= 2002 |pmid= 12019269 |doi= 10.1074/jbc.M203915200 }}
*{{cite journal | author=Shiohara M, Taniguchi S, Masumoto J, ''et al.'' |title=ASC, which is composed of a PYD and a CARD, is up-regulated by inflammation and apoptosis in human neutrophils. |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue= 5 |pages= 1314-8 |year= 2002 |pmid= 12054656 |doi= 10.1016/S0006-291X(02)00384-4 }}
*{{cite journal | author=Martinon F, Burns K, Tschopp J |title=The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta. |journal=Mol. Cell |volume=10 |issue= 2 |pages= 417-26 |year= 2002 |pmid= 12191486 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Stehlik C, Fiorentino L, Dorfleutner A, ''et al.'' |title=The PAAD/PYRIN-family protein ASC is a dual regulator of a conserved step in nuclear factor kappaB activation pathways. |journal=J. Exp. Med. |volume=196 |issue= 12 |pages= 1605-15 |year= 2003 |pmid= 12486103 |doi= }}
*{{cite journal | author=Moriai R, Tsuji N, Kobayashi D, ''et al.'' |title=A proapoptotic caspase recruitment domain protein gene, TMS1, is hypermethylated in human breast and gastric cancers. |journal=Anticancer Res. |volume=22 |issue= 6C |pages= 4163-8 |year= 2003 |pmid= 12553049 |doi= }}
*{{cite journal | author=Dowds TA, Masumoto J, Chen FF, ''et al.'' |title=Regulation of cryopyrin/Pypaf1 signaling by pyrin, the familial Mediterranean fever gene product. |journal=Biochem. Biophys. Res. Commun. |volume=302 |issue= 3 |pages= 575-80 |year= 2003 |pmid= 12615073 |doi= }}
*{{cite journal | author=Masumoto J, Dowds TA, Schaner P, ''et al.'' |title=ASC is an activating adaptor for NF-kappa B and caspase-8-dependent apoptosis. |journal=Biochem. Biophys. Res. Commun. |volume=303 |issue= 1 |pages= 69-73 |year= 2003 |pmid= 12646168 |doi= }}
*{{cite journal | author=Stehlik C, Krajewska M, Welsh K, ''et al.'' |title=The PAAD/PYRIN-only protein POP1/ASC2 is a modulator of ASC-mediated nuclear-factor-kappa B and pro-caspase-1 regulation. |journal=Biochem. J. |volume=373 |issue= Pt 1 |pages= 101-13 |year= 2003 |pmid= 12656673 |doi= 10.1042/BJ20030304 }}
*{{cite journal | author=Levine JJ, Stimson-Crider KM, Vertino PM |title=Effects of methylation on expression of TMS1/ASC in human breast cancer cells. |journal=Oncogene |volume=22 |issue= 22 |pages= 3475-88 |year= 2003 |pmid= 12776200 |doi= 10.1038/sj.onc.1206430 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RAC2... {November 17, 2007 1:46:01 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:46:31 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_RAC2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ds6.
| PDB = {{PDB2|1ds6}}, {{PDB2|1e96}}, {{PDB2|1foe}}, {{PDB2|1g4u}}, {{PDB2|1he1}}, {{PDB2|1hh4}}, {{PDB2|1i4d}}, {{PDB2|1i4l}}, {{PDB2|1i4t}}, {{PDB2|1mh1}}, {{PDB2|2fju}}, {{PDB2|2g0n}}, {{PDB2|2h7v}}, {{PDB2|2ic5}}, {{PDB2|2nz8}}, {{PDB2|2ov2}}, {{PDB2|2p2l}}
| Name = Ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2)
| HGNCid = 9802
| Symbol = RAC2
| AltSymbols =; EN-7; Gx; HSPC022
| OMIM = 602049
| ECnumber =
| Homologene = 55699
| MGIid = 97846
| GeneAtlas_image1 = PBB_GE_RAC2_213603_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005635 |text = nuclear envelope}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}} {{GNF_GO|id=GO:0030031 |text = cell projection biogenesis}} {{GNF_GO|id=GO:0030036 |text = actin cytoskeleton organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5880
| Hs_Ensembl = ENSG00000128340
| Hs_RefseqProtein = NP_002863
| Hs_RefseqmRNA = NM_002872
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 35951238
| Hs_GenLoc_end = 35970241
| Hs_Uniprot = P15153
| Mm_EntrezGene = 19354
| Mm_Ensembl = ENSMUSG00000033220
| Mm_RefseqmRNA = XM_001000836
| Mm_RefseqProtein = XP_001000836
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 78386424
| Mm_GenLoc_end = 78400038
| Mm_Uniprot = Q8CEV8
}}
}}
'''Ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2)''', also known as '''RAC2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RAC2 ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5880| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a GTPase which belongs to the RAS superfamily of small GTP-binding proteins. Members of this superfamily appear to regulate a diverse array of cellular events, including the control of cell growth, cytoskeletal reorganization, and the activation of protein kinases.<ref name="entrez">{{cite web | title = Entrez Gene: RAC2 ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5880| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Mizuno T, Kaibuchi K, Ando S, ''et al.'' |title=Regulation of the superoxide-generating NADPH oxidase by a small GTP-binding protein and its stimulatory and inhibitory GDP/GTP exchange proteins. |journal=J. Biol. Chem. |volume=267 |issue= 15 |pages= 10215-8 |year= 1992 |pmid= 1316893 |doi= }}
*{{cite journal | author=Reibel L, Dorseuil O, Stancou R, ''et al.'' |title=A hemopoietic specific gene encoding a small GTP binding protein is overexpressed during T cell activation. |journal=Biochem. Biophys. Res. Commun. |volume=175 |issue= 2 |pages= 451-8 |year= 1991 |pmid= 1902092 |doi= }}
*{{cite journal | author=Kinsella BT, Erdman RA, Maltese WA |title=Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins encoded by rac1, rac2, and ralA. |journal=J. Biol. Chem. |volume=266 |issue= 15 |pages= 9786-94 |year= 1991 |pmid= 1903399 |doi= }}
*{{cite journal | author=Didsbury J, Weber RF, Bokoch GM, ''et al.'' |title=rac, a novel ras-related family of proteins that are botulinum toxin substrates. |journal=J. Biol. Chem. |volume=264 |issue= 28 |pages= 16378-82 |year= 1989 |pmid= 2674130 |doi= }}
*{{cite journal | author=Kwong CH, Malech HL, Rotrosen D, Leto TL |title=Regulation of the human neutrophil NADPH oxidase by rho-related G-proteins. |journal=Biochemistry |volume=32 |issue= 21 |pages= 5711-7 |year= 1993 |pmid= 8504089 |doi= }}
*{{cite journal | author=Courjal F, Chuchana P, Theillet C, Fort P |title=Structure and chromosomal assignment to 22q12 and 17qter of the ras-related Rac2 and Rac3 human genes. |journal=Genomics |volume=44 |issue= 2 |pages= 242-6 |year= 1997 |pmid= 9299243 |doi= 10.1006/geno.1997.4871 }}
*{{cite journal | author=Gorvel JP, Chang TC, Boretto J, ''et al.'' |title=Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity. |journal=FEBS Lett. |volume=422 |issue= 2 |pages= 269-73 |year= 1998 |pmid= 9490022 |doi= }}
*{{cite journal | author=Dai Q, Choy E, Chiu V, ''et al.'' |title=Mammalian prenylcysteine carboxyl methyltransferase is in the endoplasmic reticulum. |journal=J. Biol. Chem. |volume=273 |issue= 24 |pages= 15030-4 |year= 1998 |pmid= 9614111 |doi= }}
*{{cite journal | author=Ahmed S, Prigmore E, Govind S, ''et al.'' |title=Cryptic Rac-binding and p21(Cdc42Hs/Rac)-activated kinase phosphorylation sites of NADPH oxidase component p67(phox). |journal=J. Biol. Chem. |volume=273 |issue= 25 |pages= 15693-701 |year= 1998 |pmid= 9624165 |doi= }}
*{{cite journal | author=Faris SL, Rinckel LA, Huang J, ''et al.'' |title=Phagocyte NADPH oxidase p67-phox possesses a novel carboxylterminal binding site for the GTPases Rac2 and Cdc42. |journal=Biochem. Biophys. Res. Commun. |volume=247 |issue= 2 |pages= 271-6 |year= 1998 |pmid= 9642115 |doi= 10.1006/bbrc.1998.8775 }}
*{{cite journal | author=Zhang B, Zheng Y |title=Negative regulation of Rho family GTPases Cdc42 and Rac2 by homodimer formation. |journal=J. Biol. Chem. |volume=273 |issue= 40 |pages= 25728-33 |year= 1998 |pmid= 9748241 |doi= }}
*{{cite journal | author=Nishihara H, Kobayashi S, Hashimoto Y, ''et al.'' |title=Non-adherent cell-specific expression of DOCK2, a member of the human CDM-family proteins. |journal=Biochim. Biophys. Acta |volume=1452 |issue= 2 |pages= 179-87 |year= 1999 |pmid= 10559471 |doi= }}
*{{cite journal | author=Dunham I, Shimizu N, Roe BA, ''et al.'' |title=The DNA sequence of human chromosome 22. |journal=Nature |volume=402 |issue= 6761 |pages= 489-95 |year= 1999 |pmid= 10591208 |doi= 10.1038/990031 }}
*{{cite journal | author=Scheffzek K, Stephan I, Jensen ON, ''et al.'' |title=The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI. |journal=Nat. Struct. Biol. |volume=7 |issue= 2 |pages= 122-6 |year= 2000 |pmid= 10655614 |doi= 10.1038/72392 }}
*{{cite journal | author=Ambruso DR, Knall C, Abell AN, ''et al.'' |title=Human neutrophil immunodeficiency syndrome is associated with an inhibitory Rac2 mutation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 9 |pages= 4654-9 |year= 2000 |pmid= 10758162 |doi= 10.1073/pnas.080074897 }}
*{{cite journal | author=Williams DA, Tao W, Yang F, ''et al.'' |title=Dominant negative mutation of the hematopoietic-specific Rho GTPase, Rac2, is associated with a human phagocyte immunodeficiency. |journal=Blood |volume=96 |issue= 5 |pages= 1646-54 |year= 2000 |pmid= 10961859 |doi= }}
*{{cite journal | author=Tamura M, Kai T, Tsunawaki S, ''et al.'' |title=Direct interaction of actin with p47(phox) of neutrophil NADPH oxidase. |journal=Biochem. Biophys. Res. Commun. |volume=276 |issue= 3 |pages= 1186-90 |year= 2000 |pmid= 11027608 |doi= 10.1006/bbrc.2000.3598 }}
*{{cite journal | author=Zhang QH, Ye M, Wu XY, ''et al.'' |title=Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. |journal=Genome Res. |volume=10 |issue= 10 |pages= 1546-60 |year= 2001 |pmid= 11042152 |doi= }}
*{{cite journal | author=Lapouge K, Smith SJ, Walker PA, ''et al.'' |title=Structure of the TPR domain of p67phox in complex with Rac.GTP. |journal=Mol. Cell |volume=6 |issue= 4 |pages= 899-907 |year= 2000 |pmid= 11090627 |doi= }}
*{{cite journal | author=Tarricone C, Xiao B, Justin N, ''et al.'' |title=The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways. |journal=Nature |volume=411 |issue= 6834 |pages= 215-9 |year= 2001 |pmid= 11346801 |doi= 10.1038/35075620 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RXRB... {November 17, 2007 1:46:31 PM PST}
- SEARCH REDIRECT: Control Box Found: RXRB {November 17, 2007 1:47:11 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 1:47:12 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 1:47:12 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 1:47:12 PM PST}
- UPDATED: Updated protein page: RXRB {November 17, 2007 1:47:18 PM PST}
- INFO: Beginning work on SERPINA6... {November 17, 2007 1:36:19 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:36:39 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 6
| HGNCid = 1540
| Symbol = SERPINA6
| AltSymbols =; CBG
| OMIM = 122500
| ECnumber =
| Homologene = 20417
| MGIid = 88278
| GeneAtlas_image1 = PBB_GE_SERPINA6_206325_at_tn.png
| Function = {{GNF_GO|id=GO:0004867 |text = serine-type endopeptidase inhibitor activity}} {{GNF_GO|id=GO:0005496 |text = steroid binding}} {{GNF_GO|id=GO:0008289 |text = lipid binding}}
| Component =
| Process = {{GNF_GO|id=GO:0006810 |text = transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 866
| Hs_Ensembl = ENSG00000170099
| Hs_RefseqProtein = NP_001747
| Hs_RefseqmRNA = NM_001756
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 93840339
| Hs_GenLoc_end = 93859441
| Hs_Uniprot = P08185
| Mm_EntrezGene = 12401
| Mm_Ensembl = ENSMUSG00000060807
| Mm_RefseqmRNA = NM_007618
| Mm_RefseqProtein = NP_031644
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 104047683
| Mm_GenLoc_end = 104058140
| Mm_Uniprot = Q3UKW1
}}
}}
'''Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 6''', also known as '''SERPINA6''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SERPINA6 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=866| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes an alpha-globulin protein with corticosteroid-binding properties. This is the major transport protein for glucorticoids and progestins in the blood of most vertebrates. The gene localizes to a chromosomal region containing several closely related serine protease inhibitors which may have evolved by duplication events.<ref name="entrez">{{cite web | title = Entrez Gene: SERPINA6 serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=866| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Rosner W, Beers PC, Awan T, Khan MS |title=Identification of corticosteroid-binding globulin in human milk: measurement with a filter disk assay. |journal=J. Clin. Endocrinol. Metab. |volume=42 |issue= 6 |pages= 1064-73 |year= 1976 |pmid= 932172 |doi= }}
*{{cite journal | author=Smith CL, Power SG, Hammond GL |title=A Leu----His substitution at residue 93 in human corticosteroid binding globulin results in reduced affinity for cortisol. |journal=J. Steroid Biochem. Mol. Biol. |volume=42 |issue= 7 |pages= 671-6 |year= 1992 |pmid= 1504007 |doi= }}
*{{cite journal | author=Brotherton J |title=Cortisol and transcortin in human seminal plasma and amniotic fluid as estimated by modern specific assays. |journal=Andrologia |volume=22 |issue= 3 |pages= 197-204 |year= 1990 |pmid= 2240617 |doi= }}
*{{cite journal | author=Seralini GE, Bérubé D, Gagné R, Hammond GL |title=The human corticosteroid binding globulin gene is located on chromosome 14q31-q32.1 near two other serine protease inhibitor genes. |journal=Hum. Genet. |volume=86 |issue= 1 |pages= 73-5 |year= 1991 |pmid= 2253941 |doi= }}
*{{cite journal | author=Underhill DA, Hammond GL |title=Organization of the human corticosteroid binding globulin gene and analysis of its 5'-flanking region. |journal=Mol. Endocrinol. |volume=3 |issue= 9 |pages= 1448-54 |year= 1990 |pmid= 2608068 |doi= }}
*{{cite journal | author=Loric S, Egloff M, Domingo M, ''et al.'' |title=Immunochemical characterization of corticosteroid-binding globulin in human bronchoalveolar fluid. |journal=Clin. Chim. Acta |volume=186 |issue= 1 |pages= 19-23 |year= 1990 |pmid= 2612005 |doi= }}
*{{cite journal | author=Heubner A, Belovsky O, Müller W, ''et al.'' |title=Application of liquid-liquid partition chromatography in the simultaneous purification of sex-hormone-binding globulin and corticosteroid-binding globulin. |journal=J. Chromatogr. |volume=397 |issue= |pages= 419-34 |year= 1987 |pmid= 2821037 |doi= }}
*{{cite journal | author=Hammond GL, Smith CL, Goping IS, ''et al.'' |title=Primary structure of human corticosteroid binding globulin, deduced from hepatic and pulmonary cDNAs, exhibits homology with serine protease inhibitors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 15 |pages= 5153-7 |year= 1987 |pmid= 3299377 |doi= }}
*{{cite journal | author=Kato EA, Hsu BR, Kuhn RW |title=Comparative structural analyses of corticosteroid binding globulin. |journal=J. Steroid Biochem. |volume=29 |issue= 2 |pages= 213-20 |year= 1988 |pmid= 3347061 |doi= }}
*{{cite journal | author=Bardin CW, Gunsalus GL, Musto NA, ''et al.'' |title=Corticosteroid binding globulin, testosterone-estradiol binding globulin, and androgen binding protein belong to protein families distinct from steroid receptors. |journal=J. Steroid Biochem. |volume=30 |issue= 1-6 |pages= 131-9 |year= 1988 |pmid= 3386241 |doi= }}
*{{cite journal | author=Hammond GL, Langley MS |title=Identification and measurement of sex hormone binding globulin (SHBG) and corticosteroid binding globulin (CBG) in human saliva. |journal=Acta Endocrinol. |volume=112 |issue= 4 |pages= 603-8 |year= 1986 |pmid= 3751467 |doi= }}
*{{cite journal | author=Agrimonti F, Frairia R, Fornaro D, ''et al.'' |title=Circadian and circaseptan rhythmicities in corticosteroid-binding globulin (CBG) binding activity of human milk. |journal=Chronobiologia |volume=9 |issue= 3 |pages= 281-90 |year= 1983 |pmid= 7172869 |doi= }}
*{{cite journal | author=Misao R, Hori M, Ichigo S, ''et al.'' |title=Levels of sex hormone-binding globulin (SHBG) and corticosteroid-binding globulin (CBG) messenger ribonucleic acid (mRNAs) in ovarian endometriosis. |journal=Reprod. Nutr. Dev. |volume=35 |issue= 2 |pages= 155-65 |year= 1995 |pmid= 7734053 |doi= }}
*{{cite journal | author=Misao R, Hori M, Ichigo S, ''et al.'' |title=Corticosteroid-binding globulin mRNA levels in human uterine endometrium. |journal=Steroids |volume=59 |issue= 10 |pages= 603-7 |year= 1995 |pmid= 7878688 |doi= }}
*{{cite journal | author=Byth BC, Billingsley GD, Cox DW |title=Physical and genetic mapping of the serpin gene cluster at 14q32.1: allelic association and a unique haplotype associated with alpha 1-antitrypsin deficiency. |journal=Am. J. Hum. Genet. |volume=55 |issue= 1 |pages= 126-33 |year= 1994 |pmid= 7912884 |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=Avvakumov GV, Hammond GL |title=Glycosylation of human corticosteroid-binding globulin. Differential processing and significance of carbohydrate chains at individual sites. |journal=Biochemistry |volume=33 |issue= 19 |pages= 5759-65 |year= 1994 |pmid= 8180202 |doi= }}
*{{cite journal | author=Van Baelen H, Power SG, Hammond GL |title=Decreased cortisol-binding affinity of transcortin Leuven is associated with an amino acid substitution at residue-93. |journal=Steroids |volume=58 |issue= 6 |pages= 275-7 |year= 1993 |pmid= 8212073 |doi= }}
*{{cite journal | author=Misao R, Nakanishi Y, Fujimoto J, ''et al.'' |title=Expression of corticosteroid-binding globulin mRNA in human uterine endometrial cancers. |journal=Steroids |volume=60 |issue= 10 |pages= 720-4 |year= 1996 |pmid= 8539782 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SLC1A2... {November 17, 2007 1:47:18 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:47:59 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Solute carrier family 1 (glial high affinity glutamate transporter), member 2
| HGNCid = 10940
| Symbol = SLC1A2
| AltSymbols =; EAAT2; GLT-1
| OMIM = 600300
| ECnumber =
| Homologene = 3075
| MGIid = 101931
| GeneAtlas_image1 = PBB_GE_SLC1A2_208389_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005313 |text = L-glutamate transmembrane transporter activity}} {{GNF_GO|id=GO:0015293 |text = symporter activity}} {{GNF_GO|id=GO:0017153 |text = sodium:dicarboxylate symporter activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006835 |text = dicarboxylic acid transport}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0015813 |text = glutamate transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6506
| Hs_Ensembl = ENSG00000110436
| Hs_RefseqProtein = NP_004162
| Hs_RefseqmRNA = NM_004171
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 35229329
| Hs_GenLoc_end = 35397372
| Hs_Uniprot = P43004
| Mm_EntrezGene = 20511
| Mm_Ensembl = ENSMUSG00000005089
| Mm_RefseqmRNA = NM_001077514
| Mm_RefseqProtein = NP_001070982
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 102459499
| Mm_GenLoc_end = 102582993
| Mm_Uniprot = Q3USU5
}}
}}
'''Solute carrier family 1 (glial high affinity glutamate transporter), member 2''', also known as '''SLC1A2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SLC1A2 solute carrier family 1 (glial high affinity glutamate transporter), member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6506| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of a family of solute transporter proteins. The membrane-bound protein is the principal transporter that clears the excitatory neurotransmitter glutamate from the extracellular space at synapses in the central nervous system. Glutamate clearance is necessary for proper synaptic activation and to prevent neuronal damage from excessive activation of glutamate receptors. Mutations in and decreased expression of this protein are associated with amyotrophic lateral sclerosis. Alternatively spliced transcript variants of this gene have been described, but their full-length nature is not known.<ref name="entrez">{{cite web | title = Entrez Gene: SLC1A2 solute carrier family 1 (glial high affinity glutamate transporter), member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6506| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wang Z, Trillo-Pazos G, Kim SY, ''et al.'' |title=Effects of human immunodeficiency virus type 1 on astrocyte gene expression and function: potential role in neuropathogenesis. |journal=J. Neurovirol. |volume=10 Suppl 1 |issue= |pages= 25-32 |year= 2004 |pmid= 14982736 |doi= }}
*{{cite journal | author=Arriza JL, Fairman WA, Wadiche JI, ''et al.'' |title=Functional comparisons of three glutamate transporter subtypes cloned from human motor cortex. |journal=J. Neurosci. |volume=14 |issue= 9 |pages= 5559-69 |year= 1994 |pmid= 7521911 |doi= }}
*{{cite journal | author=Manfras BJ, Rudert WA, Trucco M, Boehm BO |title=Cloning and characterization of a glutamate transporter cDNA from human brain and pancreas. |journal=Biochim. Biophys. Acta |volume=1195 |issue= 1 |pages= 185-8 |year= 1994 |pmid= 7522567 |doi= }}
*{{cite journal | author=Li X, Francke U |title=Assignment of the gene SLC1A2 coding for the human glutamate transporter EAAT2 to human chromosome 11 bands p13-p12. |journal=Cytogenet. Cell Genet. |volume=71 |issue= 3 |pages= 212-3 |year= 1995 |pmid= 7587378 |doi= }}
*{{cite journal | author=Shashidharan P, Wittenberg I, Plaitakis A |title=Molecular cloning of human brain glutamate/aspartate transporter II. |journal=Biochim. Biophys. Acta |volume=1191 |issue= 2 |pages= 393-6 |year= 1994 |pmid= 8172925 |doi= }}
*{{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=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi= }}
*{{cite journal | author=Milton ID, Banner SJ, Ince PG, ''et al.'' |title=Expression of the glial glutamate transporter EAAT2 in the human CNS: an immunohistochemical study. |journal=Brain Res. Mol. Brain Res. |volume=52 |issue= 1 |pages= 17-31 |year= 1998 |pmid= 9450673 |doi= }}
*{{cite journal | author=Shimamoto K, Lebrun B, Yasuda-Kamatani Y, ''et al.'' |title=DL-threo-beta-benzyloxyaspartate, a potent blocker of excitatory amino acid transporters. |journal=Mol. Pharmacol. |volume=53 |issue= 2 |pages= 195-201 |year= 1998 |pmid= 9463476 |doi= }}
*{{cite journal | author=Lin CL, Bristol LA, Jin L, ''et al.'' |title=Aberrant RNA processing in a neurodegenerative disease: the cause for absent EAAT2, a glutamate transporter, in amyotrophic lateral sclerosis. |journal=Neuron |volume=20 |issue= 3 |pages= 589-602 |year= 1998 |pmid= 9539131 |doi= }}
*{{cite journal | author=Aoki M, Lin CL, Rothstein JD, ''et al.'' |title=Mutations in the glutamate transporter EAAT2 gene do not cause abnormal EAAT2 transcripts in amyotrophic lateral sclerosis. |journal=Ann. Neurol. |volume=43 |issue= 5 |pages= 645-53 |year= 1998 |pmid= 9585360 |doi= 10.1002/ana.410430514 }}
*{{cite journal | author=Trotti D, Aoki M, Pasinelli P, ''et al.'' |title=Amyotrophic lateral sclerosis-linked glutamate transporter mutant has impaired glutamate clearance capacity. |journal=J. Biol. Chem. |volume=276 |issue= 1 |pages= 576-82 |year= 2001 |pmid= 11031254 |doi= 10.1074/jbc.M003779200 }}
*{{cite journal | author=Münch C, Schwalenstöcker B, Hermann C, ''et al.'' |title=Differential RNA cleavage and polyadenylation of the glutamate transporter EAAT2 in the human brain. |journal=Brain Res. Mol. Brain Res. |volume=80 |issue= 2 |pages= 244-51 |year= 2001 |pmid= 11038258 |doi= }}
*{{cite journal | author=Honig LS, Chambliss DD, Bigio EH, ''et al.'' |title=Glutamate transporter EAAT2 splice variants occur not only in ALS, but also in AD and controls. |journal=Neurology |volume=55 |issue= 8 |pages= 1082-8 |year= 2000 |pmid= 11071482 |doi= }}
*{{cite journal | author=Flowers JM, Powell JF, Leigh PN, ''et al.'' |title=Intron 7 retention and exon 9 skipping EAAT2 mRNA variants are not associated with amyotrophic lateral sclerosis. |journal=Ann. Neurol. |volume=49 |issue= 5 |pages= 643-9 |year= 2001 |pmid= 11357955 |doi= }}
*{{cite journal | author=Rimaniol AC, Mialocq P, Clayette P, ''et al.'' |title=Role of glutamate transporters in the regulation of glutathione levels in human macrophages. |journal=Am. J. Physiol., Cell Physiol. |volume=281 |issue= 6 |pages= C1964-70 |year= 2001 |pmid= 11698255 |doi= }}
*{{cite journal | author=Tozaki H, Kanno T, Nomura T, ''et al.'' |title=Role of glial glutamate transporters in the facilitatory action of FK960 on hippocampal neurotransmission. |journal=Brain Res. Mol. Brain Res. |volume=97 |issue= 1 |pages= 7-12 |year= 2002 |pmid= 11744157 |doi= }}
*{{cite journal | author=Palmada M, Kinne-Saffran E, Centelles JJ, Kinne RK |title=Benzodiazepines differently modulate EAAT1/GLAST and EAAT2/GLT1 glutamate transporters expressed in CHO cells. |journal=Neurochem. Int. |volume=40 |issue= 4 |pages= 321-6 |year= 2002 |pmid= 11792462 |doi= }}
*{{cite journal | author=Marie H, Billups D, Bedford FK, ''et al.'' |title=The amino terminus of the glial glutamate transporter GLT-1 interacts with the LIM protein Ajuba. |journal=Mol. Cell. Neurosci. |volume=19 |issue= 2 |pages= 152-64 |year= 2002 |pmid= 11860269 |doi= 10.1006/mcne.2001.1066 }}
*{{cite journal | author=Reye P, Sullivan R, Fletcher EL, Pow DV |title=Distribution of two splice variants of the glutamate transporter GLT1 in the retinas of humans, monkeys, rabbits, rats, cats, and chickens. |journal=J. Comp. Neurol. |volume=445 |issue= 1 |pages= 1-12 |year= 2002 |pmid= 11891650 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SMN1... {November 17, 2007 1:47:59 PM PST}
- SEARCH REDIRECT: Control Box Found: SMN1 {November 17, 2007 1:48:49 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 1:48:50 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 1:48:50 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 1:48:50 PM PST}
- UPDATED: Updated protein page: SMN1 {November 17, 2007 1:48:56 PM PST}
- INFO: Beginning work on SNRPB... {November 17, 2007 1:48:56 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:49:24 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_SNRPB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1d3b.
| PDB = {{PDB2|1d3b}}
| Name = Small nuclear ribonucleoprotein polypeptides B and B1
| HGNCid = 11153
| Symbol = SNRPB
| AltSymbols =; SNRPB1; COD; SmB/SmB'; snRNP-B
| OMIM = 182282
| ECnumber =
| Homologene = 21719
| MGIid = 98342
| GeneAtlas_image1 = PBB_GE_SNRPB_208821_at_tn.png
| GeneAtlas_image2 = PBB_GE_SNRPB_213175_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005681 |text = spliceosome}} {{GNF_GO|id=GO:0030529 |text = ribonucleoprotein complex}} {{GNF_GO|id=GO:0030532 |text = small nuclear ribonucleoprotein complex}}
| Process = {{GNF_GO|id=GO:0006397 |text = mRNA processing}} {{GNF_GO|id=GO:0008380 |text = RNA splicing}} {{GNF_GO|id=GO:0016071 |text = mRNA metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6628
| Hs_Ensembl = ENSG00000125835
| Hs_RefseqProtein = NP_003082
| Hs_RefseqmRNA = NM_003091
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 2390281
| Hs_GenLoc_end = 2399499
| Hs_Uniprot = P14678
| Mm_EntrezGene = 20638
| Mm_Ensembl = ENSMUSG00000027404
| Mm_RefseqmRNA = NM_009225
| Mm_RefseqProtein = NP_033251
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 129863076
| Mm_GenLoc_end = 129870844
| Mm_Uniprot = P27048
}}
}}
'''Small nuclear ribonucleoprotein polypeptides B and B1''', also known as '''SNRPB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SNRPB small nuclear ribonucleoprotein polypeptides B and B1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6628| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is one of several nuclear proteins that are found in common among U1, U2, U4/U6, and U5 small ribonucleoprotein particles (snRNPs). These snRNPs are involved in pre-mRNA splicing, and the encoded protein may also play a role in pre-mRNA splicing or snRNP structure. Autoantibodies from patients with systemic lupus erythematosus frequently recognize epitopes on the encoded protein. Two transcript variants encoding different isoforms (B and B') have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: SNRPB small nuclear ribonucleoprotein polypeptides B and B1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6628| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Will CL, Lührmann R |title=Spliceosomal UsnRNP biogenesis, structure and function. |journal=Curr. Opin. Cell Biol. |volume=13 |issue= 3 |pages= 290-301 |year= 2001 |pmid= 11343899 |doi= }}
*{{cite journal | author=Griffith AJ, Schmauss C, Craft J |title=The murine gene encoding the highly conserved Sm B protein contains a nonfunctional alternative 3' splice site. |journal=Gene |volume=114 |issue= 2 |pages= 195-201 |year= 1992 |pmid= 1376292 |doi= }}
*{{cite journal | author=Schmauss C, Lerner MR |title=The closely related small nuclear ribonucleoprotein polypeptides N and B/B' are distinguishable by antibodies as well as by differences in their mRNAs and gene structures. |journal=J. Biol. Chem. |volume=265 |issue= 18 |pages= 10733-9 |year= 1990 |pmid= 1693924 |doi= }}
*{{cite journal | author=Elkon KB, Hines JJ, Chu JL, Parnassa A |title=Epitope mapping of recombinant HeLa SmB and B' peptides obtained by the polymerase chain reaction. |journal=J. Immunol. |volume=145 |issue= 2 |pages= 636-43 |year= 1990 |pmid= 1694885 |doi= }}
*{{cite journal | author=Chu JL, Elkon KB |title=The small nuclear ribonucleoproteins, SmB and B', are products of a single gene. |journal=Gene |volume=97 |issue= 2 |pages= 311-2 |year= 1991 |pmid= 1825643 |doi= }}
*{{cite journal | author=Sharpe NG, Williams DG, Latchman DS |title=Regulated expression of the small nuclear ribonucleoprotein particle protein SmN in embryonic stem cell differentiation. |journal=Mol. Cell. Biol. |volume=10 |issue= 12 |pages= 6817-20 |year= 1991 |pmid= 2174118 |doi= }}
*{{cite journal | author=Schmauss C, McAllister G, Ohosone Y, ''et al.'' |title=A comparison of snRNP-associated Sm-autoantigens: human N, rat N and human B/B'. |journal=Nucleic Acids Res. |volume=17 |issue= 4 |pages= 1733-43 |year= 1989 |pmid= 2522186 |doi= }}
*{{cite journal | author=Feeney RJ, Sauterer RA, Feeney JL, Zieve GW |title=Cytoplasmic assembly and nuclear accumulation of mature small nuclear ribonucleoprotein particles. |journal=J. Biol. Chem. |volume=264 |issue= 10 |pages= 5776-83 |year= 1989 |pmid= 2522439 |doi= }}
*{{cite journal | author=Ohosone Y, Mimori T, Griffith A, ''et al.'' |title=Molecular cloning of cDNA encoding Sm autoantigen: derivation of a cDNA for a B polypeptide of the U series of small nuclear ribonucleoprotein particles. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 11 |pages= 4249-53 |year= 1989 |pmid= 2524838 |doi= }}
*{{cite journal | author=van Dam A, Winkel I, Zijlstra-Baalbergen J, ''et al.'' |title=Cloned human snRNP proteins B and B' differ only in their carboxy-terminal part. |journal=EMBO J. |volume=8 |issue= 12 |pages= 3853-60 |year= 1990 |pmid= 2531083 |doi= }}
*{{cite journal | author=Huntriss JD, Latchman DS, Williams DG |title=Lupus autoantibodies discriminate between the highly homologous Sm polypeptides B/B' and SmN by binding an epitope restricted to B/B'. |journal=Clin. Exp. Immunol. |volume=92 |issue= 2 |pages= 263-7 |year= 1993 |pmid= 7683587 |doi= }}
*{{cite journal | author=Gerrelli D, Grimaldi K, Horn D, ''et al.'' |title=The cardiac form of the tissue-specific SmN protein is identical to the brain and embryonic forms of the protein. |journal=J. Mol. Cell. Cardiol. |volume=25 |issue= 3 |pages= 321-9 |year= 1993 |pmid= 8510173 |doi= 10.1006/jmcc.1993.1038 }}
*{{cite journal | author=Simons A, Melamed-Bessudo C, Wolkowicz R, ''et al.'' |title=PACT: cloning and characterization of a cellular p53 binding protein that interacts with Rb. |journal=Oncogene |volume=14 |issue= 2 |pages= 145-55 |year= 1997 |pmid= 9010216 |doi= 10.1038/sj.onc.1200825 }}
*{{cite journal | author=Liu Q, Fischer U, Wang F, Dreyfuss G |title=The spinal muscular atrophy disease gene product, SMN, and its associated protein SIP1 are in a complex with spliceosomal snRNP proteins. |journal=Cell |volume=90 |issue= 6 |pages= 1013-21 |year= 1997 |pmid= 9323129 |doi= }}
*{{cite journal | author=Fury MG, Zhang W, Christodoulopoulos I, Zieve GW |title=Multiple protein: protein interactions between the snRNP common core proteins. |journal=Exp. Cell Res. |volume=237 |issue= 1 |pages= 63-9 |year= 1998 |pmid= 9417867 |doi= 10.1006/excr.1997.3750 }}
*{{cite journal | author=Bedford MT, Reed R, Leder P |title=WW domain-mediated interactions reveal a spliceosome-associated protein that binds a third class of proline-rich motif: the proline glycine and methionine-rich motif. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 18 |pages= 10602-7 |year= 1998 |pmid= 9724750 |doi= }}
*{{cite journal | author=Kambach C, Walke S, Young R, ''et al.'' |title=Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs. |journal=Cell |volume=96 |issue= 3 |pages= 375-87 |year= 1999 |pmid= 10025403 |doi= }}
*{{cite journal | author=Gray TA, Smithwick MJ, Schaldach MA, ''et al.'' |title=Concerted regulation and molecular evolution of the duplicated SNRPB'/B and SNRPN loci. |journal=Nucleic Acids Res. |volume=27 |issue= 23 |pages= 4577-84 |year= 2000 |pmid= 10556313 |doi= }}
*{{cite journal | author=Charroux B, Pellizzoni L, Perkinson RA, ''et al.'' |title=Gemin3: A novel DEAD box protein that interacts with SMN, the spinal muscular atrophy gene product, and is a component of gems. |journal=J. Cell Biol. |volume=147 |issue= 6 |pages= 1181-94 |year= 2000 |pmid= 10601333 |doi= }}
*{{cite journal | author=Charroux B, Pellizzoni L, Perkinson RA, ''et al.'' |title=Gemin4. A novel component of the SMN complex that is found in both gems and nucleoli. |journal=J. Cell Biol. |volume=148 |issue= 6 |pages= 1177-86 |year= 2000 |pmid= 10725331 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TRAF5... {November 17, 2007 1:49:24 PM PST}
- SEARCH REDIRECT: Control Box Found: TRAF5 {November 17, 2007 1:49:50 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 1:49:54 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 1:49:54 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 1:49:54 PM PST}
- UPDATED: Updated protein page: TRAF5 {November 17, 2007 1:50:00 PM PST}
- INFO: Beginning work on UMOD... {November 17, 2007 1:50:00 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:50:31 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Uromodulin (uromucoid, Tamm-Horsfall glycoprotein)
| HGNCid = 12559
| Symbol = UMOD
| AltSymbols =; FJHN; ADMCKD2; HNFJ; MCKD2; THGP
| OMIM = 191845
| ECnumber =
| Homologene = 2522
| MGIid = 102674
| GeneAtlas_image1 = PBB_GE_UMOD_206716_at_tn.png
| Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0048503 |text = GPI anchor binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0019898 |text = extrinsic to membrane}}
| Process = {{GNF_GO|id=GO:0006968 |text = cellular defense response}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7369
| Hs_Ensembl = ENSG00000169344
| Hs_RefseqProtein = NP_001008390
| Hs_RefseqmRNA = NM_001008389
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 20251875
| Hs_GenLoc_end = 20271533
| Hs_Uniprot = P07911
| Mm_EntrezGene = 22242
| Mm_Ensembl = ENSMUSG00000030963
| Mm_RefseqmRNA = NM_009470
| Mm_RefseqProtein = NP_033496
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 119254013
| Mm_GenLoc_end = 119270404
| Mm_Uniprot = Q8CJA0
}}
}}
'''Uromodulin (uromucoid, Tamm-Horsfall glycoprotein)''', also known as '''UMOD''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: UMOD uromodulin (uromucoid, Tamm-Horsfall glycoprotein)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7369| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes uromodulin, the most abundant protein in normal urine. Its excretion in urine follows proteolytic cleavage of the ectodomain of its glycosyl phosphatidylinosital-anchored counterpart that is situated on the luminal cell surface of the loop of Henle. Uromodulin may act as a constitutive inhibitor of calcium crystallization in renal fluids. Excretion of uromodulin in urine may provide defense against urinary tract infections caused by uropathogenic bacteria. Defects in this gene are associated with the autosomal dominant renal disorders medullary cystic kidney disease-2 (MCKD2) and familial juvenile hyperuricemic nephropathy (FJHN). These disorders are characterized by juvenile onset of hyperuricemia, gout, and progressive renal failure. While several transcript variants may exist for this gene, the full-length natures of only two have been described to date. These two represent the major variants of this gene and encode the same isoform.<ref name="entrez">{{cite web | title = Entrez Gene: UMOD uromodulin (uromucoid, Tamm-Horsfall glycoprotein)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7369| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Scolari F, Viola BF, Ghiggeri GM, ''et al.'' |title=Towards the identification of (a) gene(s) for autosomal dominant medullary cystic kidney disease. |journal=J. Nephrol. |volume=16 |issue= 3 |pages= 321-8 |year= 2003 |pmid= 12832729 |doi= }}
*{{cite journal | author=Rindler MJ, Naik SS, Li N, ''et al.'' |title=Uromodulin (Tamm-Horsfall glycoprotein/uromucoid) is a phosphatidylinositol-linked membrane protein. |journal=J. Biol. Chem. |volume=265 |issue= 34 |pages= 20784-9 |year= 1991 |pmid= 2249987 |doi= }}
*{{cite journal | author=Muchmore AV, Decker JM |title=Uromodulin: a unique 85-kilodalton immunosuppressive glycoprotein isolated from urine of pregnant women. |journal=Science |volume=229 |issue= 4712 |pages= 479-81 |year= 1985 |pmid= 2409603 |doi= }}
*{{cite journal | author=Pennica D, Kohr WJ, Kuang WJ, ''et al.'' |title=Identification of human uromodulin as the Tamm-Horsfall urinary glycoprotein. |journal=Science |volume=236 |issue= 4797 |pages= 83-8 |year= 1987 |pmid= 3453112 |doi= }}
*{{cite journal | author=Hession C, Decker JM, Sherblom AP, ''et al.'' |title=Uromodulin (Tamm-Horsfall glycoprotein): a renal ligand for lymphokines. |journal=Science |volume=237 |issue= 4821 |pages= 1479-84 |year= 1987 |pmid= 3498215 |doi= }}
*{{cite journal | author=Prasadan K, Bates J, Badgett A, ''et al.'' |title=Nucleotide sequence and peptide motifs of mouse uromodulin (Tamm-Horsfall protein)--the most abundant protein in mammalian urine. |journal=Biochim. Biophys. Acta |volume=1260 |issue= 3 |pages= 328-32 |year= 1995 |pmid= 7873609 |doi= }}
*{{cite journal | author=Huang ZQ, Kirk KA, Connelly KG, Sanders PW |title=Bence Jones proteins bind to a common peptide segment of Tamm-Horsfall glycoprotein to promote heterotypic aggregation. |journal=J. Clin. Invest. |volume=92 |issue= 6 |pages= 2975-83 |year= 1994 |pmid= 8254051 |doi= }}
*{{cite journal | author=Rhodes DC, Hinsman EJ, Rhodes JA |title=Tamm-Horsfall glycoprotein binds IgG with high affinity. |journal=Kidney Int. |volume=44 |issue= 5 |pages= 1014-21 |year= 1994 |pmid= 8264130 |doi= }}
*{{cite journal | author=Fukushima K, Watanabe H, Takeo K, ''et al.'' |title=N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity. |journal=Arch. Biochem. Biophys. |volume=304 |issue= 1 |pages= 144-53 |year= 1993 |pmid= 8323280 |doi= 10.1006/abbi.1993.1332 }}
*{{cite journal | author=Jeanpierre C, Whitmore SA, Austruy E, ''et al.'' |title=Chromosomal assignment of the uromodulin gene (UMOD) to 16p13.11. |journal=Cytogenet. Cell Genet. |volume=62 |issue= 4 |pages= 185-7 |year= 1993 |pmid= 8382593 |doi= }}
*{{cite journal | author=Thomas DB, Davies M, Peters JR, Williams JD |title=Tamm Horsfall protein binds to a single class of carbohydrate specific receptors on human neutrophils. |journal=Kidney Int. |volume=44 |issue= 2 |pages= 423-9 |year= 1993 |pmid= 8397318 |doi= }}
*{{cite journal | author=Badgett A, Kumar S |title=Phylogeny of Tamm-Horsfall protein. |journal=Urol. Int. |volume=61 |issue= 2 |pages= 72-5 |year= 1999 |pmid= 9873244 |doi= }}
*{{cite journal | author=van Rooijen JJ, Voskamp AF, Kamerling JP, Vliegenthart JF |title=Glycosylation sites and site-specific glycosylation in human Tamm-Horsfall glycoprotein. |journal=Glycobiology |volume=9 |issue= 1 |pages= 21-30 |year= 1999 |pmid= 9884403 |doi= }}
*{{cite journal | author=Scolari F, Puzzer D, Amoroso A, ''et al.'' |title=Identification of a new locus for medullary cystic disease, on chromosome 16p12. |journal=Am. J. Hum. Genet. |volume=64 |issue= 6 |pages= 1655-60 |year= 1999 |pmid= 10330352 |doi= }}
*{{cite journal | author=Kamatani N, Moritani M, Yamanaka H, ''et al.'' |title=Localization of a gene for familial juvenile hyperuricemic nephropathy causing underexcretion-type gout to 16p12 by genome-wide linkage analysis of a large family. |journal=Arthritis Rheum. |volume=43 |issue= 4 |pages= 925-9 |year= 2000 |pmid= 10765940 |doi= 10.1002/1529-0131(200004)43:4<925::AID-ANR26>3.0.CO;2-B }}
*{{cite journal | author=Pirulli D, Puzzer D, De Fusco M, ''et al.'' |title=Molecular analysis of uromodulin and SAH genes, positional candidates for autosomal dominant medullary cystic kidney disease linked to 16p12. |journal=J. Nephrol. |volume=14 |issue= 5 |pages= 392-6 |year= 2002 |pmid= 11730273 |doi= }}
*{{cite journal | author=Menozzi FD, Debrie AS, Tissier JP, ''et al.'' |title=Interaction of human Tamm-Horsfall glycoprotein with Bordetella pertussis toxin. |journal=Microbiology (Reading, Engl.) |volume=148 |issue= Pt 4 |pages= 1193-201 |year= 2002 |pmid= 11932463 |doi= }}
*{{cite journal | author=Zbikowska HM, Soukhareva N, Behnam R, ''et al.'' |title=Uromodulin promoter directs high-level expression of biologically active human alpha1-antitrypsin into mouse urine. |journal=Biochem. J. |volume=365 |issue= Pt 1 |pages= 7-11 |year= 2002 |pmid= 11982485 |doi= 10.1042/BJ20020643 }}
*{{cite journal | author=Hart TC, Gorry MC, Hart PS, ''et al.'' |title=Mutations of the UMOD gene are responsible for medullary cystic kidney disease 2 and familial juvenile hyperuricaemic nephropathy. |journal=J. Med. Genet. |volume=39 |issue= 12 |pages= 882-92 |year= 2003 |pmid= 12471200 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}
{{protein-stub}}
end log.
