Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 02:53, 16 November 2007 (UTC)[edit]
Proteins without matches (7)[edit]
Proteins with a High Potential Match (11)[edit]
Redirected Proteins (7)[edit]
Manual Inspection (Page not found) (18)[edit]
Updated (7)[edit]
Protein Status Grid - Date: 02:53, 16 November 2007 (UTC)[edit]
Vebose Log - Date: 02:53, 16 November 2007 (UTC)[edit]
- INFO: Beginning work on ACTC1... {November 15, 2007 6:34:36 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:34:59 PM PST}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ACTC1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1atn.
| PDB = {{PDB2|1atn}}, {{PDB2|1c0g}}, {{PDB2|1d4x}}, {{PDB2|1dej}}, {{PDB2|1eqy}}, {{PDB2|1esv}}, {{PDB2|1h1v}}, {{PDB2|1hlu}}, {{PDB2|1ijj}}, {{PDB2|1j6z}}, {{PDB2|1kxp}}, {{PDB2|1lcu}}, {{PDB2|1lot}}, {{PDB2|1m8q}}, {{PDB2|1ma9}}, {{PDB2|1mdu}}, {{PDB2|1mvw}}, {{PDB2|1nlv}}, {{PDB2|1nm1}}, {{PDB2|1nmd}}, {{PDB2|1nwk}}, {{PDB2|1o18}}, {{PDB2|1o19}}, {{PDB2|1o1a}}, {{PDB2|1o1b}}, {{PDB2|1o1c}}, {{PDB2|1o1d}}, {{PDB2|1o1e}}, {{PDB2|1o1f}}, {{PDB2|1o1g}}, {{PDB2|1p8z}}, {{PDB2|1qz5}}, {{PDB2|1qz6}}, {{PDB2|1rdw}}, {{PDB2|1rfq}}, {{PDB2|1rgi}}, {{PDB2|1s22}}, {{PDB2|1sqk}}, {{PDB2|1t44}}, {{PDB2|1wua}}, {{PDB2|1y64}}, {{PDB2|1yxq}}, {{PDB2|2a3z}}, {{PDB2|2a40}}, {{PDB2|2a41}}, {{PDB2|2a42}}, {{PDB2|2a5x}}, {{PDB2|2asm}}, {{PDB2|2aso}}, {{PDB2|2asp}}, {{PDB2|2btf}}, {{PDB2|2d1k}}, {{PDB2|2ff3}}, {{PDB2|2ff6}}, {{PDB2|2fxu}}, {{PDB2|2gwj}}, {{PDB2|2gwk}}, {{PDB2|2hf3}}, {{PDB2|2hf4}}, {{PDB2|2hmp}}, {{PDB2|2oan}}, {{PDB2|2q1n}}, {{PDB2|2q31}}, {{PDB2|2q36}}
| Name = Actin, alpha, cardiac muscle 1
| HGNCid = 143
| Symbol = ACTC1
| AltSymbols =; ACTC; CMD1R
| OMIM = 102540
| ECnumber =
| Homologene = 68446
| MGIid = 87905
| GeneAtlas_image1 = PBB_GE_ACTC1_205132_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008307 |text = structural constituent of muscle}}
| Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005884 |text = actin filament}}
| Process = {{GNF_GO|id=GO:0006936 |text = muscle contraction}} {{GNF_GO|id=GO:0008016 |text = regulation of heart contraction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 70
| Hs_Ensembl = ENSG00000159251
| Hs_RefseqProtein = NP_005150
| Hs_RefseqmRNA = NM_005159
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 32869724
| Hs_GenLoc_end = 32875181
| Hs_Uniprot = P68032
| Mm_EntrezGene = 11464
| Mm_Ensembl = ENSMUSG00000068614
| Mm_RefseqmRNA = XM_001002645
| Mm_RefseqProtein = XP_001002645
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 113738727
| Mm_GenLoc_end = 113744252
| Mm_Uniprot = Q3TG92
}}
}}
'''Actin, alpha, cardiac muscle 1''', also known as '''ACTC1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACTC1 actin, alpha, cardiac muscle 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=70| 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 = Actins are highly conserved proteins that are involved in various types of cell motility. Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to four others. The protein encoded by this gene belongs to the actin family which is comprised of three main groups of actin isoforms, alpha, beta, and gamma. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. Defects in this gene have been associated with idiopathic dilated cardiomyopathy (IDC) and familial hypertrophic cardiomyopathy (FHC).<ref name="entrez">{{cite web | title = Entrez Gene: ACTC1 actin, alpha, cardiac muscle 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=70| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Snásel J, Pichová I |title=The cleavage of host cell proteins by HIV-1 protease. |journal=Folia Biol. (Praha) |volume=42 |issue= 5 |pages= 227-30 |year= 1997 |pmid= 8997639 |doi= }}
*{{cite journal | author=Bearer EL, Prakash JM, Li Z |title=Actin dynamics in platelets. |journal=Int. Rev. Cytol. |volume=217 |issue= |pages= 137-82 |year= 2002 |pmid= 12019562 |doi= }}
*{{cite journal | author=Elzinga M, Maron BJ, Adelstein RS |title=Human heart and platelet actins are products of different genes. |journal=Science |volume=191 |issue= 4222 |pages= 94-5 |year= 1976 |pmid= 1246600 |doi= }}
*{{cite journal | author=Adams LD, Tomasselli AG, Robbins P, ''et al.'' |title=HIV-1 protease cleaves actin during acute infection of human T-lymphocytes. |journal=AIDS Res. Hum. Retroviruses |volume=8 |issue= 2 |pages= 291-5 |year= 1992 |pmid= 1540415 |doi= }}
*{{cite journal | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi= }}
*{{cite journal | author=Kramer PL, Luty JA, Litt M |title=Regional localization of the gene for cardiac muscle actin (ACTC) on chromosome 15q. |journal=Genomics |volume=13 |issue= 3 |pages= 904-5 |year= 1992 |pmid= 1639426 |doi= }}
*{{cite journal | author=Watkins C, Bodfish P, Warne D, ''et al.'' |title=Dinucleotide repeat polymorphism in the human alpha-cardiac actin gene, intron IV (ACTC), detected using the polymerase chain reaction. |journal=Nucleic Acids Res. |volume=19 |issue= 24 |pages= 6980 |year= 1992 |pmid= 1762945 |doi= }}
*{{cite journal | author=Tomasselli AG, Hui JO, Adams L, ''et al.'' |title=Actin, troponin C, Alzheimer amyloid precursor protein and pro-interleukin 1 beta as substrates of the protease from human immunodeficiency virus. |journal=J. Biol. Chem. |volume=266 |issue= 22 |pages= 14548-53 |year= 1991 |pmid= 1907279 |doi= }}
*{{cite journal | author=Shoeman RL, Kesselmier C, Mothes E, ''et al.'' |title=Non-viral cellular substrates for human immunodeficiency virus type 1 protease. |journal=FEBS Lett. |volume=278 |issue= 2 |pages= 199-203 |year= 1991 |pmid= 1991513 |doi= }}
*{{cite journal | author=Buckingham M, Alonso S, Barton P, ''et al.'' |title=Actin and myosin multigene families: their expression during the formation and maturation of striated muscle. |journal=Am. J. Med. Genet. |volume=25 |issue= 4 |pages= 623-34 |year= 1987 |pmid= 3789022 |doi= 10.1002/ajmg.1320250405 }}
*{{cite journal | author=Engel JN, Gunning PW, Kedes L |title=Isolation and characterization of human actin genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=78 |issue= 8 |pages= 4674-8 |year= 1982 |pmid= 6272269 |doi= }}
*{{cite journal | author=Humphries SE, Whittall R, Minty A, ''et al.'' |title=There are approximately 20 actin gene in the human genome. |journal=Nucleic Acids Res. |volume=9 |issue= 19 |pages= 4895-908 |year= 1982 |pmid= 6273789 |doi= }}
*{{cite journal | author=Hamada H, Petrino MG, Kakunaga T |title=Molecular structure and evolutionary origin of human cardiac muscle actin gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=79 |issue= 19 |pages= 5901-5 |year= 1983 |pmid= 6310553 |doi= }}
*{{cite journal | author=Gunning P, Ponte P, Kedes L, ''et al.'' |title=Chromosomal location of the co-expressed human skeletal and cardiac actin genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=81 |issue= 6 |pages= 1813-7 |year= 1984 |pmid= 6584914 |doi= }}
*{{cite journal | author=Gunning P, Ponte P, Blau H, Kedes L |title=alpha-skeletal and alpha-cardiac actin genes are coexpressed in adult human skeletal muscle and heart. |journal=Mol. Cell. Biol. |volume=3 |issue= 11 |pages= 1985-95 |year= 1984 |pmid= 6689196 |doi= }}
*{{cite journal | author=Ueyama H, Inazawa J, Ariyama T, ''et al.'' |title=Reexamination of chromosomal loci of human muscle actin genes by fluorescence in situ hybridization. |journal=Jpn. J. Hum. Genet. |volume=40 |issue= 1 |pages= 145-8 |year= 1995 |pmid= 7780165 |doi= }}
*{{cite journal | author=Moroianu J, Riordan JF |title=Nuclear translocation of angiogenin in proliferating endothelial cells is essential to its angiogenic activity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 5 |pages= 1677-81 |year= 1994 |pmid= 8127865 |doi= }}
*{{cite journal | author=Dunwoodie SL, Joya JE, Arkell RM, Hardeman EC |title=Multiple regions of the human cardiac actin gene are necessary for maturation-based expression in striated muscle. |journal=J. Biol. Chem. |volume=269 |issue= 16 |pages= 12212-9 |year= 1994 |pmid= 8163527 |doi= }}
*{{cite journal | author=Shuster CB, Lin AY, Nayak R, Herman IM |title=Beta cap73: a novel beta actin-specific binding protein. |journal=Cell Motil. Cytoskeleton |volume=35 |issue= 3 |pages= 175-87 |year= 1997 |pmid= 8913639 |doi= 10.1002/(SICI)1097-0169(1996)35:3<175::AID-CM1>3.0.CO;2-8 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on AQP2... {November 15, 2007 6:34:59 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:35:45 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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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 = Aquaporin 2 (collecting duct)
| HGNCid = 634
| Symbol = AQP2
| AltSymbols =; AQP-CD; MGC34501; WCH-CD
| OMIM = 107777
| ECnumber =
| Homologene = 20137
| MGIid = 1096865
| GeneAtlas_image1 = PBB_GE_AQP2_206672_at_tn.png
| Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0015250 |text = water channel activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0016324 |text = apical plasma membrane}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006833 |text = water transport}} {{GNF_GO|id=GO:0007588 |text = excretion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 359
| Hs_Ensembl = ENSG00000167580
| Hs_RefseqProtein = NP_000477
| Hs_RefseqmRNA = NM_000486
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 48630796
| Hs_GenLoc_end = 48638926
| Hs_Uniprot = P41181
| Mm_EntrezGene = 11827
| Mm_Ensembl = ENSMUSG00000023013
| Mm_RefseqmRNA = NM_009699
| Mm_RefseqProtein = NP_033829
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 99407090
| Mm_GenLoc_end = 99412579
| Mm_Uniprot = Q3UQD4
}}
}}
'''Aquaporin 2 (collecting duct)''', also known as '''AQP2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AQP2 aquaporin 2 (collecting duct)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=359| 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 water channel protein located in the kidney collecting tubule. It belongs to the MIP/aquaporin family, some members of which are clustered together on chromosome 12q13. Mutations in this gene have been linked to autosomal dominant, and recessive forms of nephrogenic diabetes insipidus.<ref name="entrez">{{cite web | title = Entrez Gene: AQP2 aquaporin 2 (collecting duct)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=359| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bichet DG |title=Nephrogenic diabetes insipidus. |journal=Advances in chronic kidney disease |volume=13 |issue= 2 |pages= 96-104 |year= 2006 |pmid= 16580609 |doi= 10.1053/j.ackd.2006.01.006 }}
*{{cite journal | author=Robben JH, Knoers NV, Deen PM |title=Cell biological aspects of the vasopressin type-2 receptor and aquaporin 2 water channel in nephrogenic diabetes insipidus. |journal=Am. J. Physiol. Renal Physiol. |volume=291 |issue= 2 |pages= F257-70 |year= 2006 |pmid= 16825342 |doi= 10.1152/ajprenal.00491.2005 }}
*{{cite journal | author=Sasaki S, Fushimi K, Saito H, ''et al.'' |title=Cloning, characterization, and chromosomal mapping of human aquaporin of collecting duct. |journal=J. Clin. Invest. |volume=93 |issue= 3 |pages= 1250-6 |year= 1994 |pmid= 7510718 |doi= }}
*{{cite journal | author=Deen PM, Weghuis DO, Sinke RJ, ''et al.'' |title=Assignment of the human gene for the water channel of renal collecting duct Aquaporin 2 (AQP2) to chromosome 12 region q12-->q13. |journal=Cytogenet. Cell Genet. |volume=66 |issue= 4 |pages= 260-2 |year= 1994 |pmid= 7512890 |doi= }}
*{{cite journal | author=Uchida S, Sasaki S, Fushimi K, Marumo F |title=Isolation of human aquaporin-CD gene. |journal=J. Biol. Chem. |volume=269 |issue= 38 |pages= 23451-5 |year= 1994 |pmid= 7522228 |doi= }}
*{{cite journal | author=van Lieburg AF, Verdijk MA, Knoers VV, ''et al.'' |title=Patients with autosomal nephrogenic diabetes insipidus homozygous for mutations in the aquaporin 2 water-channel gene. |journal=Am. J. Hum. Genet. |volume=55 |issue= 4 |pages= 648-52 |year= 1994 |pmid= 7524315 |doi= }}
*{{cite journal | author=Saito F, Sasaki S, Chepelinsky AB, ''et al.'' |title=Human AQP2 and MIP genes, two members of the MIP family, map within chromosome band 12q13 on the basis of two-color FISH. |journal=Cytogenet. Cell Genet. |volume=68 |issue= 1-2 |pages= 45-8 |year= 1994 |pmid= 7525161 |doi= }}
*{{cite journal | author=Nielsen S, Chou CL, Marples D, ''et al.'' |title=Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 4 |pages= 1013-7 |year= 1995 |pmid= 7532304 |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=Deen PM, Verdijk MA, Knoers NV, ''et al.'' |title=Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine. |journal=Science |volume=264 |issue= 5155 |pages= 92-5 |year= 1994 |pmid= 8140421 |doi= }}
*{{cite journal | author=Oksche A, Möller A, Dickson J, ''et al.'' |title=Two novel mutations in the aquaporin-2 and the vasopressin V2 receptor genes in patients with congenital nephrogenic diabetes insipidus. |journal=Hum. Genet. |volume=98 |issue= 5 |pages= 587-9 |year= 1996 |pmid= 8882880 |doi= }}
*{{cite journal | author=Mulders SM, Knoers NV, Van Lieburg AF, ''et al.'' |title=New mutations in the AQP2 gene in nephrogenic diabetes insipidus resulting in functional but misrouted water channels. |journal=J. Am. Soc. Nephrol. |volume=8 |issue= 2 |pages= 242-8 |year= 1997 |pmid= 9048343 |doi= }}
*{{cite journal | author=Ma T, Yang B, Umenishi F, Verkman AS |title=Closely spaced tandem arrangement of AQP2, AQP5, and AQP6 genes in a 27-kilobase segment at chromosome locus 12q13. |journal=Genomics |volume=43 |issue= 3 |pages= 387-9 |year= 1997 |pmid= 9268644 |doi= 10.1006/geno.1997.4836 }}
*{{cite journal | author=Canfield MC, Tamarappoo BK, Moses AM, ''et al.'' |title=Identification and characterization of aquaporin-2 water channel mutations causing nephrogenic diabetes insipidus with partial vasopressin response. |journal=Hum. Mol. Genet. |volume=6 |issue= 11 |pages= 1865-71 |year= 1998 |pmid= 9302264 |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=Vargas-Poussou R, Forestier L, Dautzenberg MD, ''et al.'' |title=Mutations in the vasopressin V2 receptor and aquaporin-2 genes in 12 families with congenital nephrogenic diabetes insipidus. |journal=J. Am. Soc. Nephrol. |volume=8 |issue= 12 |pages= 1855-62 |year= 1998 |pmid= 9402087 |doi= }}
*{{cite journal | author=Kuwahara M |title=Aquaporin-2, a vasopressin-sensitive water channel, and nephrogenic diabetes insipidus. |journal=Intern. Med. |volume=37 |issue= 2 |pages= 215-7 |year= 1998 |pmid= 9550615 |doi= }}
*{{cite journal | author=Mulders SM, Bichet DG, Rijss JP, ''et al.'' |title=An aquaporin-2 water channel mutant which causes autosomal dominant nephrogenic diabetes insipidus is retained in the Golgi complex. |journal=J. Clin. Invest. |volume=102 |issue= 1 |pages= 57-66 |year= 1998 |pmid= 9649557 |doi= }}
*{{cite journal | author=Goji K, Kuwahara M, Gu Y, ''et al.'' |title=Novel mutations in aquaporin-2 gene in female siblings with nephrogenic diabetes insipidus: evidence of disrupted water channel function. |journal=J. Clin. Endocrinol. Metab. |volume=83 |issue= 9 |pages= 3205-9 |year= 1998 |pmid= 9745427 |doi= }}
*{{cite journal | author=Saito T, Ishikawa S, Ito T, ''et al.'' |title=Urinary excretion of aquaporin-2 water channel differentiates psychogenic polydipsia from central diabetes insipidus. |journal=J. Clin. Endocrinol. Metab. |volume=84 |issue= 6 |pages= 2235-7 |year= 1999 |pmid= 10372737 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CACNA1C... {November 15, 2007 6:35:46 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:36:18 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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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_CACNA1C_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2be6.
| PDB = {{PDB2|2be6}}
| Name = Calcium channel, voltage-dependent, L type, alpha 1C subunit
| HGNCid = 1390
| Symbol = CACNA1C
| AltSymbols =; CACH2; CACN2; CACNL1A1; CCHL1A1; CaV1.2; MGC120730; TS
| OMIM = 114205
| ECnumber =
| Homologene = 55484
| MGIid = 103013
| Function = {{GNF_GO|id=GO:0005216 |text = ion channel activity}} {{GNF_GO|id=GO:0005245 |text = voltage-gated calcium channel activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}}
| Component = {{GNF_GO|id=GO:0005891 |text = voltage-gated calcium channel complex}} {{GNF_GO|id=GO:0014069 |text = postsynaptic density}} {{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:0006816 |text = calcium ion transport}} {{GNF_GO|id=GO:0008016 |text = regulation of heart contraction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 775
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000710
| Hs_RefseqmRNA = NM_000719
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 12288
| Mm_Ensembl = ENSMUSG00000051331
| Mm_RefseqmRNA = NM_009781
| Mm_RefseqProtein = NP_033911
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 118557938
| Mm_GenLoc_end = 119023135
| Mm_Uniprot = Q0PCR4
}}
}}
'''Calcium channel, voltage-dependent, L type, alpha 1C subunit''', also known as '''CACNA1C''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CACNA1C calcium channel, voltage-dependent, L type, alpha 1C subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=775| 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-1 subunit of a voltage-dependent calcium channel. Calcium channels mediate the influx of calcium ions into the cell upon membrane polarization. The alpha-1 subunit consists of 24 transmembrane segments and forms the pore through which ions pass into the cell. The calcium channel consists of a complex of alpha-1, alpha-2/delta, beta, and gamma subunits in a 1:1:1:1 ratio. There are multiple isoforms of each of these proteins, either encoded by different genes or the result of alternative splicing of transcripts. The protein encoded by this gene binds to and is inhibited by dihydropyridine. Many alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.<ref name="entrez">{{cite web | title = Entrez Gene: CACNA1C calcium channel, voltage-dependent, L type, alpha 1C subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=775| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Catterall WA, Perez-Reyes E, Snutch TP, Striessnig J |title=International Union of Pharmacology. XLVIII. Nomenclature and structure-function relationships of voltage-gated calcium channels. |journal=Pharmacol. Rev. |volume=57 |issue= 4 |pages= 411-25 |year= 2006 |pmid= 16382099 |doi= 10.1124/pr.57.4.5 }}
*{{cite journal | author=Soldatov NM |title=Molecular diversity of L-type Ca2+ channel transcripts in human fibroblasts. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 10 |pages= 4628-32 |year= 1992 |pmid= 1316612 |doi= }}
*{{cite journal | author=Powers PA, Gregg RG, Hogan K |title=Linkage mapping of the human gene for the alpha 1 subunit of the cardiac DHP-sensitive Ca2+ channel (CACNL1A1) to chromosome 12p13.2-pter using a dinucleotide repeat. |journal=Genomics |volume=14 |issue= 1 |pages= 206-7 |year= 1992 |pmid= 1330882 |doi= }}
*{{cite journal | author=Sun W, McPherson JD, Hoang DQ, ''et al.'' |title=Mapping of a human brain voltage-gated calcium channel to human chromosome 12p13-pter. |journal=Genomics |volume=14 |issue= 4 |pages= 1092-4 |year= 1993 |pmid= 1335957 |doi= }}
*{{cite journal | author=Lacerda AE, Kim HS, Ruth P, ''et al.'' |title=Normalization of current kinetics by interaction between the alpha 1 and beta subunits of the skeletal muscle dihydropyridine-sensitive Ca2+ channel. |journal=Nature |volume=352 |issue= 6335 |pages= 527-30 |year= 1991 |pmid= 1650913 |doi= 10.1038/352527a0 }}
*{{cite journal | author=Powers PA, Gregg RG, Lalley PA, ''et al.'' |title=Assignment of the human gene for the alpha 1 subunit of the cardiac DHP-sensitive Ca2+ channel (CCHL1A1) to chromosome 12p12-pter. |journal=Genomics |volume=10 |issue= 3 |pages= 835-9 |year= 1991 |pmid= 1653763 |doi= }}
*{{cite journal | author=Perez-Reyes E, Wei XY, Castellano A, Birnbaumer L |title=Molecular diversity of L-type calcium channels. Evidence for alternative splicing of the transcripts of three non-allelic genes. |journal=J. Biol. Chem. |volume=265 |issue= 33 |pages= 20430-6 |year= 1990 |pmid= 2173707 |doi= }}
*{{cite journal | author=Soldatov NM, Bouron A, Reuter H |title=Different voltage-dependent inhibition by dihydropyridines of human Ca2+ channel splice variants. |journal=J. Biol. Chem. |volume=270 |issue= 18 |pages= 10540-3 |year= 1995 |pmid= 7737988 |doi= }}
*{{cite journal | author=Soldatov NM |title=Genomic structure of human L-type Ca2+ channel. |journal=Genomics |volume=22 |issue= 1 |pages= 77-87 |year= 1994 |pmid= 7959794 |doi= 10.1006/geno.1994.1347 }}
*{{cite journal | author=Tang S, Mikala G, Bahinski A, ''et al.'' |title=Molecular localization of ion selectivity sites within the pore of a human L-type cardiac calcium channel. |journal=J. Biol. Chem. |volume=268 |issue= 18 |pages= 13026-9 |year= 1993 |pmid= 8099908 |doi= }}
*{{cite journal | author=Schultz D, Mikala G, Yatani A, ''et al.'' |title=Cloning, chromosomal localization, and functional expression of the alpha 1 subunit of the L-type voltage-dependent calcium channel from normal human heart. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 13 |pages= 6228-32 |year= 1993 |pmid= 8392192 |doi= }}
*{{cite journal | author=Perets T, Blumenstein Y, Shistik E, ''et al.'' |title=A potential site of functional modulation by protein kinase A in the cardiac Ca2+ channel alpha 1C subunit. |journal=FEBS Lett. |volume=384 |issue= 2 |pages= 189-92 |year= 1996 |pmid= 8612821 |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=Soldatov NM, Zühlke RD, Bouron A, Reuter H |title=Molecular structures involved in L-type calcium channel inactivation. Role of the carboxyl-terminal region encoded by exons 40-42 in alpha1C subunit in the kinetics and Ca2+ dependence of inactivation. |journal=J. Biol. Chem. |volume=272 |issue= 6 |pages= 3560-6 |year= 1997 |pmid= 9013606 |doi= }}
*{{cite journal | author=Klöckner U, Mikala G, Eisfeld J, ''et al.'' |title=Properties of three COOH-terminal splice variants of a human cardiac L-type Ca2+-channel alpha1-subunit. |journal=Am. J. Physiol. |volume=272 |issue= 3 Pt 2 |pages= H1372-81 |year= 1997 |pmid= 9087614 |doi= }}
*{{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=Gao T, Yatani A, Dell'Acqua ML, ''et al.'' |title=cAMP-dependent regulation of cardiac L-type Ca2+ channels requires membrane targeting of PKA and phosphorylation of channel subunits. |journal=Neuron |volume=19 |issue= 1 |pages= 185-96 |year= 1997 |pmid= 9247274 |doi= }}
*{{cite journal | author=Zühlke RD, Bouron A, Soldatov NM, Reuter H |title=Ca2+ channel sensitivity towards the blocker isradipine is affected by alternative splicing of the human alpha1C subunit gene. |journal=FEBS Lett. |volume=427 |issue= 2 |pages= 220-4 |year= 1998 |pmid= 9607315 |doi= }}
*{{cite journal | author=Meyers MB, Puri TS, Chien AJ, ''et al.'' |title=Sorcin associates with the pore-forming subunit of voltage-dependent L-type Ca2+ channels. |journal=J. Biol. Chem. |volume=273 |issue= 30 |pages= 18930-5 |year= 1998 |pmid= 9668070 |doi= }}
*{{cite journal | author=Liu WS, Soldatov NM, Gustavsson I, Chowdhary BP |title=Fiber-FISH analysis of the 3'-terminal region of the human L-type Ca2+ channel alpha 1C subunit gene. |journal=Hereditas |volume=129 |issue= 2 |pages= 169-75 |year= 1999 |pmid= 10022083 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CCR7... {November 15, 2007 6:37:08 PM PST}
- SEARCH REDIRECT: Control Box Found: CCR7 {November 15, 2007 6:37:42 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 6:37:44 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 6:37:44 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 6:37:44 PM PST}
- UPDATED: Updated protein page: CCR7 {November 15, 2007 6:37:50 PM PST}
- INFO: Beginning work on CHGA... {November 15, 2007 6:36:45 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:37:08 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| 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 = Chromogranin A (parathyroid secretory protein 1)
| HGNCid = 1929
| Symbol = CHGA
| AltSymbols =; CGA
| OMIM = 118910
| ECnumber =
| Homologene = 976
| MGIid = 88394
| GeneAtlas_image1 = PBB_GE_CHGA_204697_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0008021 |text = synaptic vesicle}}
| Process = {{GNF_GO|id=GO:0008217 |text = blood pressure regulation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1113
| Hs_Ensembl = ENSG00000100604
| Hs_RefseqProtein = NP_001266
| Hs_RefseqmRNA = NM_001275
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 92459245
| Hs_GenLoc_end = 92471389
| Hs_Uniprot = P10645
| Mm_EntrezGene = 12652
| Mm_Ensembl = ENSMUSG00000021194
| Mm_RefseqmRNA = NM_007693
| Mm_RefseqProtein = NP_031719
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 102956019
| Mm_GenLoc_end = 102966077
| Mm_Uniprot = Q3UN28
}}
}}
'''Chromogranin A (parathyroid secretory protein 1)''', also known as '''CHGA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CHGA chromogranin A (parathyroid secretory protein 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1113| 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 chromogranin/secretogranin family of neuroendocrine secretory proteins. It is found in secretory vesicles of neurons and endocrine cells. This gene product is a precursor to three biologically active peptides; vasostatin, pancreastatin, and parastatin. These peptides act as autocrine or paracrine negative modulators of the neuroendocrine system. Other peptides, including chromostatin, beta-granin, WE-14 and GE-25, are also derived from the full-length protein. However, biological activities for these molecules have not been shown.<ref name="entrez">{{cite web | title = Entrez Gene: CHGA chromogranin A (parathyroid secretory protein 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1113| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hendy GN, Bevan S, Mattei MG, Mouland AJ |title=Chromogranin A. |journal=Clinical and investigative medicine. Médecine clinique et experimentale |volume=18 |issue= 1 |pages= 47-65 |year= 1995 |pmid= 7768066 |doi= }}
*{{cite journal | author=Iacangelo AL, Eiden LE |title=Chromogranin A: current status as a precursor for bioactive peptides and a granulogenic/sorting factor in the regulated secretory pathway. |journal=Regul. Pept. |volume=58 |issue= 3 |pages= 65-88 |year= 1996 |pmid= 8577930 |doi= }}
*{{cite journal | author=Curry WJ, Barkatullah SC, Johansson AN, ''et al.'' |title=WE-14, a chromogranin a-derived neuropeptide. |journal=Ann. N. Y. Acad. Sci. |volume=971 |issue= |pages= 311-6 |year= 2002 |pmid= 12438141 |doi= }}
*{{cite journal | author=Curry WJ, Shaw C, Johnston CF, ''et al.'' |title=Isolation and primary structure of a novel chromogranin A-derived peptide, WE-14, from a human midgut carcinoid tumour. |journal=FEBS Lett. |volume=301 |issue= 3 |pages= 319-21 |year= 1992 |pmid= 1577173 |doi= }}
*{{cite journal | author=Tamamura H, Ohta M, Yoshizawa K, ''et al.'' |title=Isolation and characterization of a tumor-derived human protein related to chromogranin A and its in vitro conversion to human pancreastatin-48. |journal=Eur. J. Biochem. |volume=191 |issue= 1 |pages= 33-9 |year= 1990 |pmid= 2165909 |doi= }}
*{{cite journal | author=Konecki DS, Benedum UM, Gerdes HH, Huttner WB |title=The primary structure of human chromogranin A and pancreastatin. |journal=J. Biol. Chem. |volume=262 |issue= 35 |pages= 17026-30 |year= 1988 |pmid= 2445752 |doi= }}
*{{cite journal | author=Sekiya K, Ghatei MA, Minamino N, ''et al.'' |title=Isolation of human pancreastatin fragment containing the active sequence from a glucagonoma. |journal=FEBS Lett. |volume=228 |issue= 1 |pages= 153-6 |year= 1988 |pmid= 2830133 |doi= }}
*{{cite journal | author=Helman LJ, Ahn TG, Levine MA, ''et al.'' |title=Molecular cloning and primary structure of human chromogranin A (secretory protein I) cDNA. |journal=J. Biol. Chem. |volume=263 |issue= 23 |pages= 11559-63 |year= 1988 |pmid= 3403545 |doi= }}
*{{cite journal | author=Wilson BS, Phan SH, Lloyd RV |title=Chromogranin from normal human adrenal glands: purification by monoclonal antibody affinity chromatography and partial N-terminal amino acid sequence. |journal=Regul. Pept. |volume=13 |issue= 3-4 |pages= 207-23 |year= 1986 |pmid= 3704195 |doi= }}
*{{cite journal | author=Deftos LJ, Murray SS, Burton DW, ''et al.'' |title=A cloned chromogranin A (CgA) cDNA detects a 2.3Kb mRNA in diverse neuroendocrine tissues. |journal=Biochem. Biophys. Res. Commun. |volume=137 |issue= 1 |pages= 418-23 |year= 1986 |pmid= 3718511 |doi= }}
*{{cite journal | author=Hagn C, Schmid KW, Fischer-Colbrie R, Winkler H |title=Chromogranin A, B, and C in human adrenal medulla and endocrine tissues. |journal=Lab. Invest. |volume=55 |issue= 4 |pages= 405-11 |year= 1986 |pmid= 3762065 |doi= }}
*{{cite journal | author=Murray SS, Deaven LL, Burton DW, ''et al.'' |title=The gene for human chromogranin A (CgA) is located on chromosome 14. |journal=Biochem. Biophys. Res. Commun. |volume=142 |issue= 1 |pages= 141-6 |year= 1987 |pmid= 3814131 |doi= }}
*{{cite journal | author=Cetin Y, Aunis D, Bader MF, ''et al.'' |title=Chromostatin, a chromogranin A-derived bioactive peptide, is present in human pancreatic insulin (beta) cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 6 |pages= 2360-4 |year= 1993 |pmid= 8096340 |doi= }}
*{{cite journal | author=Mouland AJ, Bevan S, White JH, Hendy GN |title=Human chromogranin A gene. Molecular cloning, structural analysis, and neuroendocrine cell-specific expression. |journal=J. Biol. Chem. |volume=269 |issue= 9 |pages= 6918-26 |year= 1994 |pmid= 8120054 |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=Simon-Chazottes D, Wu H, Parmer RJ, ''et al.'' |title=Assignment of the chromogranin A (Chga) locus to homologous regions on mouse chromosome 12 and rat chromosome 6. |journal=Genomics |volume=17 |issue= 1 |pages= 252-5 |year= 1993 |pmid= 8406464 |doi= 10.1006/geno.1993.1316 }}
*{{cite journal | author=Mahata SK, Kozak CA, Szpirer J, ''et al.'' |title=Dispersion of chromogranin/secretogranin secretory protein family loci in mammalian genomes. |journal=Genomics |volume=33 |issue= 1 |pages= 135-9 |year= 1996 |pmid= 8617499 |doi= 10.1006/geno.1996.0171 }}
*{{cite journal | author=Strub JM, Goumon Y, Lugardon K, ''et al.'' |title=Antibacterial activity of glycosylated and phosphorylated chromogranin A-derived peptide 173-194 from bovine adrenal medullary chromaffin granules. |journal=J. Biol. Chem. |volume=271 |issue= 45 |pages= 28533-40 |year= 1996 |pmid= 8910482 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on COPS5... {November 15, 2007 6:46:51 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:47:20 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 = COP9 constitutive photomorphogenic homolog subunit 5 (Arabidopsis)
| HGNCid = 2240
| Symbol = COPS5
| AltSymbols =; CSN5; JAB1; MGC3149; MOV-34; SGN5
| OMIM = 604850
| ECnumber =
| Homologene = 55992
| MGIid = 1349415
| GeneAtlas_image1 = PBB_GE_COPS5_201652_at_tn.png
| GeneAtlas_image2 = PBB_GE_COPS5_gnf1h08492_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0003743 |text = translation initiation factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008237 |text = metallopeptidase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005852 |text = eukaryotic translation initiation factor 3 complex}} {{GNF_GO|id=GO:0008180 |text = signalosome}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006412 |text = translation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10987
| Hs_Ensembl = ENSG00000121022
| Hs_RefseqProtein = NP_006828
| Hs_RefseqmRNA = NM_006837
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 68117871
| Hs_GenLoc_end = 68136785
| Hs_Uniprot = Q92905
| Mm_EntrezGene = 26754
| Mm_Ensembl = ENSMUSG00000025917
| Mm_RefseqmRNA = NM_013715
| Mm_RefseqProtein = NP_038743
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 10009816
| Mm_GenLoc_end = 10023160
| Mm_Uniprot = Q3V0K7
}}
}}
'''COP9 constitutive photomorphogenic homolog subunit 5 (Arabidopsis)''', also known as '''COPS5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: COPS5 COP9 constitutive photomorphogenic homolog subunit 5 (Arabidopsis)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10987| 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 the eight subunits of COP9 signalosome, a highly conserved protein complex that functions as an important regulator in multiple signaling pathways. The structure and function of COP9 signalosome is similar to that of the 19S regulatory particle of 26S proteasome. COP9 signalosome has been shown to interact with SCF-type E3 ubiquitin ligases and act as a positive regulator of E3 ubiquitin ligases. This protein is reported to be involved in the degradation of cyclin-dependent kinase inhibitor CDKN1B/p27Kip1. It is also known to be an coactivator that increases the specificity of JUN/AP1 transcription factors.<ref name="entrez">{{cite web | title = Entrez Gene: COPS5 COP9 constitutive photomorphogenic homolog subunit 5 (Arabidopsis)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10987| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wolf DA, Zhou C, Wee S |title=The COP9 signalosome: an assembly and maintenance platform for cullin ubiquitin ligases? |journal=Nat. Cell Biol. |volume=5 |issue= 12 |pages= 1029-33 |year= 2004 |pmid= 14647295 |doi= 10.1038/ncb1203-1029 }}
*{{cite journal | author=Claret FX, Hibi M, Dhut S, ''et al.'' |title=A new group of conserved coactivators that increase the specificity of AP-1 transcription factors. |journal=Nature |volume=383 |issue= 6599 |pages= 453-7 |year= 1996 |pmid= 8837781 |doi= 10.1038/383453a0 }}
*{{cite journal | author=Asano K, Vornlocher HP, Richter-Cook NJ, ''et al.'' |title=Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits. Possible roles in RNA binding and macromolecular assembly. |journal=J. Biol. Chem. |volume=272 |issue= 43 |pages= 27042-52 |year= 1997 |pmid= 9341143 |doi= }}
*{{cite journal | author=Seeger M, Kraft R, Ferrell K, ''et al.'' |title=A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits. |journal=FASEB J. |volume=12 |issue= 6 |pages= 469-78 |year= 1998 |pmid= 9535219 |doi= }}
*{{cite journal | author=Wei N, Tsuge T, Serino G, ''et al.'' |title=The COP9 complex is conserved between plants and mammals and is related to the 26S proteasome regulatory complex. |journal=Curr. Biol. |volume=8 |issue= 16 |pages= 919-22 |year= 1998 |pmid= 9707402 |doi= }}
*{{cite journal | author=Tomoda K, Kubota Y, Kato J |title=Degradation of the cyclin-dependent-kinase inhibitor p27Kip1 is instigated by Jab1. |journal=Nature |volume=398 |issue= 6723 |pages= 160-5 |year= 1999 |pmid= 10086358 |doi= 10.1038/18230 }}
*{{cite journal | author=Dechend R, Hirano F, Lehmann K, ''et al.'' |title=The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators. |journal=Oncogene |volume=18 |issue= 22 |pages= 3316-23 |year= 1999 |pmid= 10362352 |doi= 10.1038/sj.onc.1202717 }}
*{{cite journal | author=Chauchereau A, Georgiakaki M, Perrin-Wolff M, ''et al.'' |title=JAB1 interacts with both the progesterone receptor and SRC-1. |journal=J. Biol. Chem. |volume=275 |issue= 12 |pages= 8540-8 |year= 2000 |pmid= 10722692 |doi= }}
*{{cite journal | author=Bianchi E, Denti S, Granata A, ''et al.'' |title=Integrin LFA-1 interacts with the transcriptional co-activator JAB1 to modulate AP-1 activity. |journal=Nature |volume=404 |issue= 6778 |pages= 617-21 |year= 2000 |pmid= 10766246 |doi= 10.1038/35007098 }}
*{{cite journal | author=Kleemann R, Hausser A, Geiger G, ''et al.'' |title=Intracellular action of the cytokine MIF to modulate AP-1 activity and the cell cycle through Jab1. |journal=Nature |volume=408 |issue= 6809 |pages= 211-6 |year= 2000 |pmid= 11089976 |doi= 10.1038/35041591 }}
*{{cite journal | author=Bech-Otschir D, Kraft R, Huang X, ''et al.'' |title=COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system. |journal=EMBO J. |volume=20 |issue= 7 |pages= 1630-9 |year= 2001 |pmid= 11285227 |doi= 10.1093/emboj/20.7.1630 }}
*{{cite journal | author=Lyapina S, Cope G, Shevchenko A, ''et al.'' |title=Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome. |journal=Science |volume=292 |issue= 5520 |pages= 1382-5 |year= 2001 |pmid= 11337588 |doi= 10.1126/science.1059780 }}
*{{cite journal | author=Tomoda K, Kubota Y, Arata Y, ''et al.'' |title=The cytoplasmic shuttling and subsequent degradation of p27Kip1 mediated by Jab1/CSN5 and the COP9 signalosome complex. |journal=J. Biol. Chem. |volume=277 |issue= 3 |pages= 2302-10 |year= 2002 |pmid= 11704659 |doi= 10.1074/jbc.M104431200 }}
*{{cite journal | author=Bae MK, Ahn MY, Jeong JW, ''et al.'' |title=Jab1 interacts directly with HIF-1alpha and regulates its stability. |journal=J. Biol. Chem. |volume=277 |issue= 1 |pages= 9-12 |year= 2002 |pmid= 11707426 |doi= 10.1074/jbc.C100442200 }}
*{{cite journal | author=Lu C, Li Y, Zhao Y, ''et al.'' |title=Intracrine hepatopoietin potentiates AP-1 activity through JAB1 independent of MAPK pathway. |journal=FASEB J. |volume=16 |issue= 1 |pages= 90-2 |year= 2002 |pmid= 11709497 |doi= 10.1096/fj.01-0506fje }}
*{{cite journal | author=Dai YS, Cserjesi P |title=The basic helix-loop-helix factor, HAND2, functions as a transcriptional activator by binding to E-boxes as a heterodimer. |journal=J. Biol. Chem. |volume=277 |issue= 15 |pages= 12604-12 |year= 2002 |pmid= 11812799 |doi= 10.1074/jbc.M200283200 }}
*{{cite journal | author=Wan M, Cao X, Wu Y, ''et al.'' |title=Jab1 antagonizes TGF-beta signaling by inducing Smad4 degradation. |journal=EMBO Rep. |volume=3 |issue= 2 |pages= 171-6 |year= 2002 |pmid= 11818334 |doi= 10.1093/embo-reports/kvf024 }}
*{{cite journal | author=Gemmill RM, Bemis LT, Lee JP, ''et al.'' |title=The TRC8 hereditary kidney cancer gene suppresses growth and functions with VHL in a common pathway. |journal=Oncogene |volume=21 |issue= 22 |pages= 3507-16 |year= 2002 |pmid= 12032852 |doi= 10.1038/sj.onc.1205437 }}
*{{cite journal | author=Caballero OL, Resto V, Patturajan M, ''et al.'' |title=Interaction and colocalization of PGP9.5 with JAB1 and p27(Kip1). |journal=Oncogene |volume=21 |issue= 19 |pages= 3003-10 |year= 2002 |pmid= 12082530 |doi= 10.1038/sj.onc.1205390 }}
*{{cite journal | author=Chopra S, Fernandez De Mattos S, Lam EW, Mann DJ |title=Jab1 co-activation of c-Jun is abrogated by the serine 10-phosphorylated form of p27Kip1. |journal=J. Biol. Chem. |volume=277 |issue= 36 |pages= 32413-6 |year= 2002 |pmid= 12119282 |doi= 10.1074/jbc.C200311200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CSF1R... {November 15, 2007 6:37:50 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:38:21 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Colony stimulating factor 1 receptor, formerly McDonough feline sarcoma viral (v-fms) oncogene homolog
| HGNCid = 2433
| Symbol = CSF1R
| AltSymbols =; C-FMS; CD115; CSFR; FIM2; FMS
| OMIM = 164770
| ECnumber =
| Homologene = 3817
| MGIid = 1339758
| GeneAtlas_image1 = PBB_GE_CSF1R_203104_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005011 |text = macrophage colony stimulating factor receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0019735 |text = antimicrobial humoral response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1436
| Hs_Ensembl = ENSG00000182578
| Hs_RefseqProtein = NP_005202
| Hs_RefseqmRNA = NM_005211
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 149413051
| Hs_GenLoc_end = 149473128
| Hs_Uniprot = P07333
| Mm_EntrezGene = 12978
| Mm_Ensembl = ENSMUSG00000024621
| Mm_RefseqmRNA = NM_001037859
| Mm_RefseqProtein = NP_001032948
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 18
| Mm_GenLoc_start = 61230941
| Mm_GenLoc_end = 61256506
| Mm_Uniprot = Q0P635
}}
}}
'''Colony stimulating factor 1 receptor, formerly McDonough feline sarcoma viral (v-fms) oncogene homolog''', also known as '''CSF1R''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CSF1R colony stimulating factor 1 receptor, formerly McDonough feline sarcoma viral (v-fms) oncogene homolog| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1436| 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 the receptor for colony stimulating factor 1, a cytokine which controls the production, differentiation, and function of macrophages. This receptor mediates most if not all of the biological effects of this cytokine. Ligand binding activates the receptor kinase through a process of oligomerization and transphosphorylation. The encoded protein is a tyrosine kinase transmembrane receptor and member of the CSF1/PDGF receptor family of tyrosine-protein kinases. Mutations in this gene have been associated with a predisposition to myeloid malignancy. The first intron of this gene contains a transcriptionally inactive ribosomal protein L7 processed pseudogene oriented in the opposite direction.<ref name="entrez">{{cite web | title = Entrez Gene: CSF1R colony stimulating factor 1 receptor, formerly McDonough feline sarcoma viral (v-fms) oncogene homolog| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1436| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Rettenmier CW, Roussel MF, Sherr CJ |title=The colony-stimulating factor 1 (CSF-1) receptor (c-fms proto-oncogene product) and its ligand. |journal=J. Cell Sci. Suppl. |volume=9 |issue= |pages= 27-44 |year= 1989 |pmid= 2978516 |doi= }}
*{{cite journal | author=Stanley ER, Berg KL, Einstein DB, ''et al.'' |title=Biology and action of colony--stimulating factor-1. |journal=Mol. Reprod. Dev. |volume=46 |issue= 1 |pages= 4-10 |year= 1997 |pmid= 8981357 |doi= 10.1002/(SICI)1098-2795(199701)46:1<4::AID-MRD2>3.0.CO;2-V }}
*{{cite journal | author=Gout I, Dhand R, Panayotou G, ''et al.'' |title=Expression and characterization of the p85 subunit of the phosphatidylinositol 3-kinase complex and a related p85 beta protein by using the baculovirus expression system. |journal=Biochem. J. |volume=288 ( Pt 2) |issue= |pages= 395-405 |year= 1993 |pmid= 1334406 |doi= }}
*{{cite journal | author=Galland F, Stefanova M, Lafage M, Birnbaum D |title=Localization of the 5' end of the MCF2 oncogene to human chromosome 15q15----q23. |journal=Cytogenet. Cell Genet. |volume=60 |issue= 2 |pages= 114-6 |year= 1992 |pmid= 1611909 |doi= }}
*{{cite journal | author=Boultwood J, Rack K, Kelly S, ''et al.'' |title=Loss of both CSF1R (FMS) alleles in patients with myelodysplasia and a chromosome 5 deletion. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 14 |pages= 6176-80 |year= 1991 |pmid= 1829836 |doi= }}
*{{cite journal | author=Roussel MF, Cleveland JL, Shurtleff SA, Sherr CJ |title=Myc rescue of a mutant CSF-1 receptor impaired in mitogenic signalling. |journal=Nature |volume=353 |issue= 6342 |pages= 361-3 |year= 1991 |pmid= 1833648 |doi= 10.1038/353361a0 }}
*{{cite journal | author=Reedijk M, Liu XQ, Pawson T |title=Interactions of phosphatidylinositol kinase, GTPase-activating protein (GAP), and GAP-associated proteins with the colony-stimulating factor 1 receptor. |journal=Mol. Cell. Biol. |volume=10 |issue= 11 |pages= 5601-8 |year= 1990 |pmid= 2172781 |doi= }}
*{{cite journal | author=Ridge SA, Worwood M, Oscier D, ''et al.'' |title=FMS mutations in myelodysplastic, leukemic, and normal subjects. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 4 |pages= 1377-80 |year= 1990 |pmid= 2406720 |doi= }}
*{{cite journal | author=Sherr CJ, Rettenmier CW, Sacca R, ''et al.'' |title=The c-fms proto-oncogene product is related to the receptor for the mononuclear phagocyte growth factor, CSF-1. |journal=Cell |volume=41 |issue= 3 |pages= 665-76 |year= 1985 |pmid= 2408759 |doi= }}
*{{cite journal | author=Coussens L, Van Beveren C, Smith D, ''et al.'' |title=Structural alteration of viral homologue of receptor proto-oncogene fms at carboxyl terminus. |journal=Nature |volume=320 |issue= 6059 |pages= 277-80 |year= 1986 |pmid= 2421165 |doi= 10.1038/320277a0 }}
*{{cite journal | author=Hampe A, Shamoon BM, Gobet M, ''et al.'' |title=Nucleotide sequence and structural organization of the human FMS proto-oncogene. |journal=Oncogene Res. |volume=4 |issue= 1 |pages= 9-17 |year= 1989 |pmid= 2524025 |doi= }}
*{{cite journal | author=Visvader J, Verma IM |title=Differential transcription of exon 1 of the human c-fms gene in placental trophoblasts and monocytes. |journal=Mol. Cell. Biol. |volume=9 |issue= 3 |pages= 1336-41 |year= 1989 |pmid= 2524648 |doi= }}
*{{cite journal | author=Roberts WM, Look AT, Roussel MF, Sherr CJ |title=Tandem linkage of human CSF-1 receptor (c-fms) and PDGF receptor genes. |journal=Cell |volume=55 |issue= 4 |pages= 655-61 |year= 1988 |pmid= 2846185 |doi= }}
*{{cite journal | author=Xu DQ, Guilhot S, Galibert F |title=Restriction fragment length polymorphism of the human c-fms gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 9 |pages= 2862-5 |year= 1985 |pmid= 2986142 |doi= }}
*{{cite journal | author=Sherr CJ, Rettenmier CW |title=The fms gene and the CSF-1 receptor. |journal=Cancer Surv. |volume=5 |issue= 2 |pages= 221-32 |year= 1987 |pmid= 3022923 |doi= }}
*{{cite journal | author=Le Beau MM, Westbrook CA, Diaz MO, ''et al.'' |title=Evidence for the involvement of GM-CSF and FMS in the deletion (5q) in myeloid disorders. |journal=Science |volume=231 |issue= 4741 |pages= 984-7 |year= 1986 |pmid= 3484837 |doi= }}
*{{cite journal | author=Wheeler EF, Roussel MF, Hampe A, ''et al.'' |title=The amino-terminal domain of the v-fms oncogene product includes a functional signal peptide that directs synthesis of a transforming glycoprotein in the absence of feline leukemia virus gag sequences. |journal=J. Virol. |volume=59 |issue= 2 |pages= 224-33 |year= 1986 |pmid= 3525854 |doi= }}
*{{cite journal | author=Browning PJ, Bunn HF, Cline A, ''et al.'' |title="Replacement" of COOH-terminal truncation of v-fms with c-fms sequences markedly reduces transformation potential. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 20 |pages= 7800-4 |year= 1986 |pmid= 3532121 |doi= }}
*{{cite journal | author=Verbeek JS, Roebroek AJ, van den Ouweland AM, ''et al.'' |title=Human c-fms proto-oncogene: comparative analysis with an abnormal allele. |journal=Mol. Cell. Biol. |volume=5 |issue= 2 |pages= 422-6 |year= 1985 |pmid= 3974576 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on EWSR1... {November 15, 2007 6:38:21 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:38:42 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_EWSR1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2cpe.
| PDB = {{PDB2|2cpe}}
| Name = Ewing sarcoma breakpoint region 1
| HGNCid = 3508
| Symbol = EWSR1
| AltSymbols =; EWS
| OMIM = 133450
| ECnumber =
| Homologene = 22438
| MGIid = 99960
| GeneAtlas_image1 = PBB_GE_EWSR1_210012_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003676 |text = nucleic acid binding}} {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2130
| Hs_Ensembl = ENSG00000182944
| Hs_RefseqProtein = NP_005234
| Hs_RefseqmRNA = NM_005243
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 27994283
| Hs_GenLoc_end = 28026504
| Hs_Uniprot = Q01844
| Mm_EntrezGene = 14030
| Mm_Ensembl = ENSMUSG00000009079
| Mm_RefseqmRNA = XM_988357
| Mm_RefseqProtein = XP_993451
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 4969692
| Mm_GenLoc_end = 4999269
| Mm_Uniprot = Q9CRS5
}}
}}
'''Ewing sarcoma breakpoint region 1''', also known as '''EWSR1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EWSR1 Ewing sarcoma breakpoint region 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2130| 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 putative RNA binding protein. Mutations in this gene, specifically a t(11;22)(q24;q12) translocation, are known to cause Ewing sarcoma as well as neuroectodermal and various other tumors. Alternative splicing of this gene results in two products.<ref name="entrez">{{cite web | title = Entrez Gene: EWSR1 Ewing sarcoma breakpoint region 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2130| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ban J, Siligan C, Kreppel M, ''et al.'' |title=EWS-FLI1 in Ewing's sarcoma: real targets and collateral damage. |journal=Adv. Exp. Med. Biol. |volume=587 |issue= |pages= 41-52 |year= 2007 |pmid= 17163154 |doi= }}
*{{cite journal | author=Meister HP |title=[Morphological findings of chronic constipation in childhood] |journal=Monatsschrift für Kinderheilkunde |volume=124 |issue= 5 |pages= 354-6 |year= 1976 |pmid= 934118 |doi= }}
*{{cite journal | author=Guthrie GM, Verstraete A, Deines MM, Stern RM |title=Symptoms of stress in four societies. |journal=The Journal of social psychology |volume=95 |issue= Second half |pages= 165-72 |year= 1975 |pmid= 1127890 |doi= }}
*{{cite journal | author=Delattre O, Zucman J, Plougastel B, ''et al.'' |title=Gene fusion with an ETS DNA-binding domain caused by chromosome translocation in human tumours. |journal=Nature |volume=359 |issue= 6391 |pages= 162-5 |year= 1992 |pmid= 1522903 |doi= 10.1038/359162a0 }}
*{{cite journal | author=Bhagirath T, Abe S, Nojima T, Yoshida MC |title=Molecular analysis of a t(11;22) translocation junction in a case of Ewing's sarcoma. |journal=Genes Chromosomes Cancer |volume=13 |issue= 2 |pages= 126-32 |year= 1995 |pmid= 7542907 |doi= }}
*{{cite journal | author=Ohno T, Ouchida M, Lee L, ''et al.'' |title=The EWS gene, involved in Ewing family of tumors, malignant melanoma of soft parts and desmoplastic small round cell tumors, codes for an RNA binding protein with novel regulatory domains. |journal=Oncogene |volume=9 |issue= 10 |pages= 3087-97 |year= 1994 |pmid= 8084618 |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=Plougastel B, Zucman J, Peter M, ''et al.'' |title=Genomic structure of the EWS gene and its relationship to EWSR1, a site of tumor-associated chromosome translocation. |journal=Genomics |volume=18 |issue= 3 |pages= 609-15 |year= 1994 |pmid= 8307570 |doi= }}
*{{cite journal | author=Zucman J, Delattre O, Desmaze C, ''et al.'' |title=EWS and ATF-1 gene fusion induced by t(12;22) translocation in malignant melanoma of soft parts. |journal=Nat. Genet. |volume=4 |issue= 4 |pages= 341-5 |year= 1993 |pmid= 8401579 |doi= 10.1038/ng0893-341 }}
*{{cite journal | author=Brodie SG, Stocker SJ, Wardlaw JC, ''et al.'' |title=EWS and WT-1 gene fusion in desmoplastic small round cell tumor of the abdomen. |journal=Hum. Pathol. |volume=26 |issue= 12 |pages= 1370-4 |year= 1996 |pmid= 8522311 |doi= }}
*{{cite journal | author=Fujimura Y, Ohno T, Siddique H, ''et al.'' |title=The EWS-ATF-1 gene involved in malignant melanoma of soft parts with t(12;22) chromosome translocation, encodes a constitutive transcriptional activator. |journal=Oncogene |volume=12 |issue= 1 |pages= 159-67 |year= 1996 |pmid= 8552387 |doi= }}
*{{cite journal | author=Clark J, Benjamin H, Gill S, ''et al.'' |title=Fusion of the EWS gene to CHN, a member of the steroid/thyroid receptor gene superfamily, in a human myxoid chondrosarcoma. |journal=Oncogene |volume=12 |issue= 2 |pages= 229-35 |year= 1996 |pmid= 8570200 |doi= }}
*{{cite journal | author=Magnaghi-Jaulin L, Masutani H, Robin P, ''et al.'' |title=SRE elements are binding sites for the fusion protein EWS-FLI-1. |journal=Nucleic Acids Res. |volume=24 |issue= 6 |pages= 1052-8 |year= 1996 |pmid= 8604338 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Aman P, Panagopoulos I, Lassen C, ''et al.'' |title=Expression patterns of the human sarcoma-associated genes FUS and EWS and the genomic structure of FUS. |journal=Genomics |volume=37 |issue= 1 |pages= 1-8 |year= 1997 |pmid= 8921363 |doi= 10.1006/geno.1996.0513 }}
*{{cite journal | author=Morohoshi F, Arai K, Takahashi EI, ''et al.'' |title=Cloning and mapping of a human RBP56 gene encoding a putative RNA binding protein similar to FUS/TLS and EWS proteins. |journal=Genomics |volume=38 |issue= 1 |pages= 51-7 |year= 1997 |pmid= 8954779 |doi= 10.1006/geno.1996.0591 }}
*{{cite journal | author=Zucman-Rossi J, Legoix P, Thomas G |title=Identification of new members of the Gas2 and Ras families in the 22q12 chromosome region. |journal=Genomics |volume=38 |issue= 3 |pages= 247-54 |year= 1997 |pmid= 8975699 |doi= 10.1006/geno.1996.0625 }}
*{{cite journal | author=Guinamard R, Fougereau M, Seckinger P |title=The SH3 domain of Bruton's tyrosine kinase interacts with Vav, Sam68 and EWS. |journal=Scand. J. Immunol. |volume=45 |issue= 6 |pages= 587-95 |year= 1997 |pmid= 9201297 |doi= }}
*{{cite journal | author=Deloulme JC, Prichard L, Delattre O, Storm DR |title=The prooncoprotein EWS binds calmodulin and is phosphorylated by protein kinase C through an IQ domain. |journal=J. Biol. Chem. |volume=272 |issue= 43 |pages= 27369-77 |year= 1997 |pmid= 9341188 |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 GDNF... {November 15, 2007 6:38:42 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:39:10 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
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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_GDNF_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1agq.
| PDB = {{PDB2|1agq}}
| Name = Glial cell derived neurotrophic factor
| HGNCid = 4232
| Symbol = GDNF
| AltSymbols =; ATF1; ATF2; HFB1-GDNF
| OMIM = 600837
| ECnumber =
| Homologene = 433
| MGIid = 107430
| GeneAtlas_image1 = PBB_GE_GDNF_221359_at_tn.png
| Function = {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}}
| Process = {{GNF_GO|id=GO:0001657 |text = ureteric bud development}} {{GNF_GO|id=GO:0001755 |text = neural crest cell migration}} {{GNF_GO|id=GO:0001759 |text = induction of an organ}} {{GNF_GO|id=GO:0001941 |text = postsynaptic membrane organization}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007422 |text = peripheral nervous system development}} {{GNF_GO|id=GO:0008150 |text = biological_process}} {{GNF_GO|id=GO:0030432 |text = peristalsis}} {{GNF_GO|id=GO:0031175 |text = neurite development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2668
| Hs_Ensembl = ENSG00000168621
| Hs_RefseqProtein = NP_000505
| Hs_RefseqmRNA = NM_000514
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 37848536
| Hs_GenLoc_end = 37875539
| Hs_Uniprot = P39905
| Mm_EntrezGene = 14573
| Mm_Ensembl = ENSMUSG00000022144
| Mm_RefseqmRNA = NM_010275
| Mm_RefseqProtein = NP_034405
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 7758226
| Mm_GenLoc_end = 7784790
| Mm_Uniprot = Q6LEL9
}}
}}
'''Glial cell derived neurotrophic factor''', also known as '''GDNF''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GDNF glial cell derived neurotrophic factor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2668| 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 highly conserved neurotrophic factor. The recombinant form of this protein was shown to promote the survival and differentiation of dopaminergic neurons in culture, and was able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.<ref name="entrez">{{cite web | title = Entrez Gene: GDNF glial cell derived neurotrophic factor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2668| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hofstra RM, Osinga J, Buys CH |title=Mutations in Hirschsprung disease: when does a mutation contribute to the phenotype. |journal=Eur. J. Hum. Genet. |volume=5 |issue= 4 |pages= 180-5 |year= 1998 |pmid= 9359036 |doi= }}
*{{cite journal | author=Martucciello G, Ceccherini I, Lerone M, Jasonni V |title=Pathogenesis of Hirschsprung's disease. |journal=J. Pediatr. Surg. |volume=35 |issue= 7 |pages= 1017-25 |year= 2000 |pmid= 10917288 |doi= }}
*{{cite journal | author=Schindelhauer D, Schuffenhauer S, Gasser T, ''et al.'' |title=The gene coding for glial cell line derived neurotrophic factor (GDNF) maps to chromosome 5p12-p13.1. |journal=Genomics |volume=28 |issue= 3 |pages= 605-7 |year= 1996 |pmid= 7490108 |doi= 10.1006/geno.1995.1202 }}
*{{cite journal | author=Tomac A, Lindqvist E, Lin LF, ''et al.'' |title=Protection and repair of the nigrostriatal dopaminergic system by GDNF in vivo. |journal=Nature |volume=373 |issue= 6512 |pages= 335-9 |year= 1995 |pmid= 7830766 |doi= 10.1038/373335a0 }}
*{{cite journal | author=Oppenheim RW, Houenou LJ, Johnson JE, ''et al.'' |title=Developing motor neurons rescued from programmed and axotomy-induced cell death by GDNF. |journal=Nature |volume=373 |issue= 6512 |pages= 344-6 |year= 1995 |pmid= 7830769 |doi= 10.1038/373344a0 }}
*{{cite journal | author=Schaar DG, Sieber BA, Sherwood AC, ''et al.'' |title=Multiple astrocyte transcripts encode nigral trophic factors in rat and human. |journal=Exp. Neurol. |volume=130 |issue= 2 |pages= 387-93 |year= 1995 |pmid= 7867768 |doi= 10.1006/exnr.1994.1218 }}
*{{cite journal | author=Lin LF, Doherty DH, Lile JD, ''et al.'' |title=GDNF: a glial cell line-derived neurotrophic factor for midbrain dopaminergic neurons. |journal=Science |volume=260 |issue= 5111 |pages= 1130-2 |year= 1993 |pmid= 8493557 |doi= }}
*{{cite journal | author=Bermingham N, Hillermann R, Gilmour F, ''et al.'' |title=Human glial cell line-derived neurotrophic factor (GDNF) maps to chromosome 5. |journal=Hum. Genet. |volume=96 |issue= 6 |pages= 671-3 |year= 1996 |pmid= 8522325 |doi= }}
*{{cite journal | author=Gash DM, Zhang Z, Ovadia A, ''et al.'' |title=Functional recovery in parkinsonian monkeys treated with GDNF. |journal=Nature |volume=380 |issue= 6571 |pages= 252-5 |year= 1996 |pmid= 8637574 |doi= 10.1038/380252a0 }}
*{{cite journal | author=Jing S, Wen D, Yu Y, ''et al.'' |title=GDNF-induced activation of the ret protein tyrosine kinase is mediated by GDNFR-alpha, a novel receptor for GDNF. |journal=Cell |volume=85 |issue= 7 |pages= 1113-24 |year= 1996 |pmid= 8674117 |doi= }}
*{{cite journal | author=Angrist M, Bolk S, Halushka M, ''et al.'' |title=Germline mutations in glial cell line-derived neurotrophic factor (GDNF) and RET in a Hirschsprung disease patient. |journal=Nat. Genet. |volume=14 |issue= 3 |pages= 341-4 |year= 1996 |pmid= 8896568 |doi= 10.1038/ng1196-341 }}
*{{cite journal | author=Salomon R, Attié T, Pelet A, ''et al.'' |title=Germline mutations of the RET ligand GDNF are not sufficient to cause Hirschsprung disease. |journal=Nat. Genet. |volume=14 |issue= 3 |pages= 345-7 |year= 1996 |pmid= 8896569 |doi= 10.1038/ng1196-345 }}
*{{cite journal | author=Ivanchuk SM, Myers SM, Eng C, Mulligan LM |title=De novo mutation of GDNF, ligand for the RET/GDNFR-alpha receptor complex, in Hirschsprung disease. |journal=Hum. Mol. Genet. |volume=5 |issue= 12 |pages= 2023-6 |year= 1997 |pmid= 8968758 |doi= }}
*{{cite journal | author=Haniu M, Hui J, Young Y, ''et al.'' |title=Glial cell line-derived neurotrophic factor: selective reduction of the intermolecular disulfide linkage and characterization of its disulfide structure. |journal=Biochemistry |volume=35 |issue= 51 |pages= 16799-805 |year= 1997 |pmid= 8988018 |doi= 10.1021/bi9605550 }}
*{{cite journal | author=Bär KJ, Facer P, Williams NS, ''et al.'' |title=Glial-derived neurotrophic factor in human adult and fetal intestine and in Hirschsprung's disease. |journal=Gastroenterology |volume=112 |issue= 4 |pages= 1381-5 |year= 1997 |pmid= 9098026 |doi= }}
*{{cite journal | author=Jing S, Yu Y, Fang M, ''et al.'' |title=GFRalpha-2 and GFRalpha-3 are two new receptors for ligands of the GDNF family. |journal=J. Biol. Chem. |volume=272 |issue= 52 |pages= 33111-7 |year= 1998 |pmid= 9407096 |doi= }}
*{{cite journal | author=Eng C, Myers SM, Kogon MD, ''et al.'' |title=Genomic structure and chromosomal localization of the human GDNFR-alpha gene. |journal=Oncogene |volume=16 |issue= 5 |pages= 597-601 |year= 1998 |pmid= 9482105 |doi= 10.1038/sj.onc.1201573 }}
*{{cite journal | author=Amiel J, Salomon R, Attié T, ''et al.'' |title=Mutations of the RET-GDNF signaling pathway in Ondine's curse. |journal=Am. J. Hum. Genet. |volume=62 |issue= 3 |pages= 715-7 |year= 1998 |pmid= 9497256 |doi= }}
*{{cite journal | author=Yamaguchi Y, Wada T, Suzuki F, ''et al.'' |title=Casein kinase II interacts with the bZIP domains of several transcription factors. |journal=Nucleic Acids Res. |volume=26 |issue= 16 |pages= 3854-61 |year= 1998 |pmid= 9685505 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IFNGR1... {November 15, 2007 6:39:10 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:39:36 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_IFNGR1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1fg9.
| PDB = {{PDB2|1fg9}}, {{PDB2|1fyh}}, {{PDB2|1jrh}}
| Name = Interferon gamma receptor 1
| HGNCid = 5439
| Symbol = IFNGR1
| AltSymbols =; CD119; FLJ45734; IFNGR
| OMIM = 107470
| ECnumber =
| Homologene = 359
| MGIid = 107655
| GeneAtlas_image1 = PBB_GE_IFNGR1_202727_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_IFNGR1_211676_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004906 |text = interferon-gamma receptor activity}} {{GNF_GO|id=GO:0019955 |text = cytokine binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0009615 |text = response to virus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3459
| Hs_Ensembl = ENSG00000027697
| Hs_RefseqProtein = NP_000407
| Hs_RefseqmRNA = NM_000416
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 137560314
| Hs_GenLoc_end = 137582279
| Hs_Uniprot = P15260
| Mm_EntrezGene = 15979
| Mm_Ensembl = ENSMUSG00000020009
| Mm_RefseqmRNA = NM_010511
| Mm_RefseqProtein = NP_034641
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 19281386
| Mm_GenLoc_end = 19299641
| Mm_Uniprot = Q3TW49
}}
}}
'''Interferon gamma receptor 1''', also known as '''IFNGR1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IFNGR1 interferon gamma receptor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3459| 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 = IFNGR1 encodes the ligand-binding chain (alpha) of the heterodimeric gamma interferon receptor. IFNGR2 encodes the non-ligand-binding partner of the heterodimeric receptor.<ref name="entrez">{{cite web | title = Entrez Gene: IFNGR1 interferon gamma receptor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3459| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Samuel CE |title=Antiviral actions of interferons. |journal=Clin. Microbiol. Rev. |volume=14 |issue= 4 |pages= 778-809, table of contents |year= 2002 |pmid= 11585785 |doi= 10.1128/CMR.14.4.778-809.2001 }}
*{{cite journal | author=van Loon AP, Ozmen L, Fountoulakis M, ''et al.'' |title=High-affinity receptor for interferon-gamma (IFN-gamma), a ubiquitous protein occurring in different molecular forms on human cells: blood monocytes and eleven different cell lines have the same IFN-gamma receptor protein. |journal=J. Leukoc. Biol. |volume=49 |issue= 5 |pages= 462-73 |year= 1991 |pmid= 1826725 |doi= }}
*{{cite journal | author=Le Coniat M, Alcaide-Loridan C, Fellous M, Berger R |title=Human interferon gamma receptor 1 (IFNGR1) gene maps to chromosome region 6q23-6q24. |journal=Hum. Genet. |volume=84 |issue= 1 |pages= 92-4 |year= 1990 |pmid= 2532616 |doi= }}
*{{cite journal | author=Novick D, Orchansky P, Revel M, Rubinstein M |title=The human interferon-gamma receptor. Purification, characterization, and preparation of antibodies. |journal=J. Biol. Chem. |volume=262 |issue= 18 |pages= 8483-7 |year= 1987 |pmid= 2954953 |doi= }}
*{{cite journal | author=Aguet M, Dembić Z, Merlin G |title=Molecular cloning and expression of the human interferon-gamma receptor. |journal=Cell |volume=55 |issue= 2 |pages= 273-80 |year= 1988 |pmid= 2971451 |doi= }}
*{{cite journal | author=Szente BE, Subramaniam PS, Johnson HM |title=Identification of IFN-gamma receptor binding sites for JAK2 and enhancement of binding by IFN-gamma and its C-terminal peptide IFN-gamma(95-133). |journal=J. Immunol. |volume=155 |issue= 12 |pages= 5617-22 |year= 1996 |pmid= 7499845 |doi= }}
*{{cite journal | author=Igarashi K, Garotta G, Ozmen L, ''et al.'' |title=Interferon-gamma induces tyrosine phosphorylation of interferon-gamma receptor and regulated association of protein tyrosine kinases, Jak1 and Jak2, with its receptor. |journal=J. Biol. Chem. |volume=269 |issue= 20 |pages= 14333-6 |year= 1994 |pmid= 7514165 |doi= }}
*{{cite journal | author=Walter MR, Windsor WT, Nagabhushan TL, ''et al.'' |title=Crystal structure of a complex between interferon-gamma and its soluble high-affinity receptor. |journal=Nature |volume=376 |issue= 6537 |pages= 230-5 |year= 1995 |pmid= 7617032 |doi= 10.1038/376230a0 }}
*{{cite journal | author=Kotenko SV, Izotova LS, Pollack BP, ''et al.'' |title=Interaction between the components of the interferon gamma receptor complex. |journal=J. Biol. Chem. |volume=270 |issue= 36 |pages= 20915-21 |year= 1995 |pmid= 7673114 |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=Tjoelker LW, Seyfried CE, Eddy RL, ''et al.'' |title=Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5. |journal=Biochemistry |volume=33 |issue= 11 |pages= 3229-36 |year= 1994 |pmid= 8136357 |doi= }}
*{{cite journal | author=Greenlund AC, Farrar MA, Viviano BL, Schreiber RD |title=Ligand-induced IFN gamma receptor tyrosine phosphorylation couples the receptor to its signal transduction system (p91). |journal=EMBO J. |volume=13 |issue= 7 |pages= 1591-600 |year= 1994 |pmid= 8156998 |doi= }}
*{{cite journal | author=Stüber D, Friedlein A, Fountoulakis M, ''et al.'' |title=Alignment of disulfide bonds of the extracellular domain of the interferon gamma receptor and investigation of their role in biological activity. |journal=Biochemistry |volume=32 |issue= 9 |pages= 2423-30 |year= 1993 |pmid= 8443182 |doi= }}
*{{cite journal | author=Dalton DK, Pitts-Meek S, Keshav S, ''et al.'' |title=Multiple defects of immune cell function in mice with disrupted interferon-gamma genes. |journal=Science |volume=259 |issue= 5102 |pages= 1739-42 |year= 1993 |pmid= 8456300 |doi= }}
*{{cite journal | author=Novelli F, Giovarelli M, Gentz R, ''et al.'' |title=Modulation of interferon-gamma receptor during human T lymphocyte alloactivation. |journal=Eur. J. Immunol. |volume=23 |issue= 6 |pages= 1226-31 |year= 1993 |pmid= 8500521 |doi= }}
*{{cite journal | author=Newport MJ, Huxley CM, Huston S, ''et al.'' |title=A mutation in the interferon-gamma-receptor gene and susceptibility to mycobacterial infection. |journal=N. Engl. J. Med. |volume=335 |issue= 26 |pages= 1941-9 |year= 1997 |pmid= 8960473 |doi= }}
*{{cite journal | author=Jouanguy E, Altare F, Lamhamedi S, ''et al.'' |title=Interferon-gamma-receptor deficiency in an infant with fatal bacille Calmette-Guérin infection. |journal=N. Engl. J. Med. |volume=335 |issue= 26 |pages= 1956-61 |year= 1997 |pmid= 8960475 |doi= }}
*{{cite journal | author=Gerritsma JS, Gerritsen AF, De Ley M, ''et al.'' |title=Interferon-gamma induces biosynthesis of complement components C2, C4 and factor H by human proximal tubular epithelial cells. |journal=Cytokine |volume=9 |issue= 4 |pages= 276-83 |year= 1997 |pmid= 9112336 |doi= 10.1006/cyto.1996.0164 }}
*{{cite journal | author=Sogabe S, Stuart F, Henke C, ''et al.'' |title=Neutralizing epitopes on the extracellular interferon gamma receptor (IFNgammaR) alpha-chain characterized by homolog scanning mutagenesis and X-ray crystal structure of the A6 fab-IFNgammaR1-108 complex. |journal=J. Mol. Biol. |volume=273 |issue= 4 |pages= 882-97 |year= 1998 |pmid= 9367779 |doi= 10.1006/jmbi.1997.1336 }}
*{{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 LCAT... {November 15, 2007 6:40:16 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:40:31 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 = Lecithin-cholesterol acyltransferase
| HGNCid = 6522
| Symbol = LCAT
| AltSymbols =;
| OMIM = 606967
| ECnumber =
| Homologene = 68042
| MGIid = 96755
| Function = {{GNF_GO|id=GO:0004607 |text = phosphatidylcholine-sterol O-acyltransferase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008415 |text = acyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0008202 |text = steroid metabolic process}} {{GNF_GO|id=GO:0008203 |text = cholesterol metabolic process}} {{GNF_GO|id=GO:0018350 |text = protein amino acid esterification}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3931
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000220
| Hs_RefseqmRNA = NM_000229
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 16816
| Mm_Ensembl = ENSMUSG00000035237
| Mm_RefseqmRNA = NM_008490
| Mm_RefseqProtein = NP_032516
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 108828681
| Mm_GenLoc_end = 108832511
| Mm_Uniprot = Q791M3
}}
}}
'''Lecithin-cholesterol acyltransferase''', also known as '''LCAT''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LCAT lecithin-cholesterol acyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3931| 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 extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase. The esterification of cholesterol is required for cholesterol transport. Mutations in this gene have been found to cause fish-eye disease as well as LCAT deficiency.<ref name="entrez">{{cite web | title = Entrez Gene: LCAT lecithin-cholesterol acyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3931| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kuivenhoven JA, Pritchard H, Hill J, ''et al.'' |title=The molecular pathology of lecithin:cholesterol acyltransferase (LCAT) deficiency syndromes. |journal=J. Lipid Res. |volume=38 |issue= 2 |pages= 191-205 |year= 1997 |pmid= 9162740 |doi= }}
*{{cite journal | author=de Vries R, Borggreve SE, Dullaart RP |title=Role of lipases, lecithin:cholesterol acyltransferase and cholesteryl ester transfer protein in abnormal high density lipoprotein metabolism in insulin resistance and type 2 diabetes mellitus. |journal=Clin. Lab. |volume=49 |issue= 11-12 |pages= 601-13 |year= 2004 |pmid= 14651331 |doi= }}
*{{cite journal | author=Teisberg P, Gjone E, Olaisen B |title=Genetics of LCAT (lecithin: cholesterol acyltransferase) deficiency. |journal=Ann. Hum. Genet. |volume=38 |issue= 3 |pages= 327-31 |year= 1975 |pmid= 806250 |doi= }}
*{{cite journal | author=Cogan DG, Kruth HS, Datilis MB, Martin N |title=Corneal opacity in LCAT disease. |journal=Cornea |volume=11 |issue= 6 |pages= 595-9 |year= 1993 |pmid= 1468226 |doi= }}
*{{cite journal | author=Skretting G, Blomhoff JP, Solheim J, Prydz H |title=The genetic defect of the original Norwegian lecithin:cholesterol acyltransferase deficiency families. |journal=FEBS Lett. |volume=309 |issue= 3 |pages= 307-10 |year= 1992 |pmid= 1516702 |doi= }}
*{{cite journal | author=Skretting G, Prydz H |title=An amino acid exchange in exon I of the human lecithin: cholesterol acyltransferase (LCAT) gene is associated with fish eye disease. |journal=Biochem. Biophys. Res. Commun. |volume=182 |issue= 2 |pages= 583-7 |year= 1992 |pmid= 1571050 |doi= }}
*{{cite journal | author=Furukawa Y, Urano T, Hida Y, ''et al.'' |title=Interaction of rat lecithin-cholesterol acyltransferase with rat apolipoprotein A-I and with lecithin-cholesterol vesicles. |journal=J. Biochem. |volume=111 |issue= 3 |pages= 413-8 |year= 1992 |pmid= 1587806 |doi= }}
*{{cite journal | author=Minnich A, Collet X, Roghani A, ''et al.'' |title=Site-directed mutagenesis and structure-function analysis of the human apolipoprotein A-I. Relation between lecithin-cholesterol acyltransferase activation and lipid binding. |journal=J. Biol. Chem. |volume=267 |issue= 23 |pages= 16553-60 |year= 1992 |pmid= 1644835 |doi= }}
*{{cite journal | author=Bujo H, Kusunoki J, Ogasawara M, ''et al.'' |title=Molecular defect in familial lecithin:cholesterol acyltransferase (LCAT) deficiency: a single nucleotide insertion in LCAT gene causes a complete deficient type of the disease. |journal=Biochem. Biophys. Res. Commun. |volume=181 |issue= 3 |pages= 933-40 |year= 1992 |pmid= 1662503 |doi= }}
*{{cite journal | author=Gotoda T, Yamada N, Murase T, ''et al.'' |title=Differential phenotypic expression by three mutant alleles in familial lecithin:cholesterol acyltransferase deficiency. |journal=Lancet |volume=338 |issue= 8770 |pages= 778-81 |year= 1991 |pmid= 1681161 |doi= }}
*{{cite journal | author=Klein HG, Lohse P, Pritchard PH, ''et al.'' |title=Two different allelic mutations in the lecithin-cholesterol acyltransferase gene associated with the fish eye syndrome. Lecithin-cholesterol acyltransferase (Thr123----Ile) and lecithin-cholesterol acyltransferase (Thr347----Met). |journal=J. Clin. Invest. |volume=89 |issue= 2 |pages= 499-506 |year= 1992 |pmid= 1737840 |doi= }}
*{{cite journal | author=Maeda E, Naka Y, Matozaki T, ''et al.'' |title=Lecithin-cholesterol acyltransferase (LCAT) deficiency with a missense mutation in exon 6 of the LCAT gene. |journal=Biochem. Biophys. Res. Commun. |volume=178 |issue= 2 |pages= 460-6 |year= 1991 |pmid= 1859405 |doi= }}
*{{cite journal | author=Funke H, von Eckardstein A, Pritchard PH, ''et al.'' |title=A molecular defect causing fish eye disease: an amino acid exchange in lecithin-cholesterol acyltransferase (LCAT) leads to the selective loss of alpha-LCAT activity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 11 |pages= 4855-9 |year= 1991 |pmid= 2052566 |doi= }}
*{{cite journal | author=Taramelli R, Pontoglio M, Candiani G, ''et al.'' |title=Lecithin cholesterol acyl transferase deficiency: molecular analysis of a mutated allele. |journal=Hum. Genet. |volume=85 |issue= 2 |pages= 195-9 |year= 1990 |pmid= 2370048 |doi= }}
*{{cite journal | author=Rogne S, Skretting G, Larsen F, ''et al.'' |title=The isolation and characterisation of a cDNA clone for human lecithin:cholesterol acyl transferase and its use to analyse the genes in patients with LCAT deficiency and fish eye disease. |journal=Biochem. Biophys. Res. Commun. |volume=148 |issue= 1 |pages= 161-9 |year= 1987 |pmid= 2823801 |doi= }}
*{{cite journal | author=Tata F, Chaves ME, Markham AF, ''et al.'' |title=The isolation and characterisation of cDNA and genomic clones for human lecithin: cholesterol acyltransferase. |journal=Biochim. Biophys. Acta |volume=910 |issue= 2 |pages= 142-8 |year= 1987 |pmid= 2823898 |doi= }}
*{{cite journal | author=Yang CY, Manoogian D, Pao Q, ''et al.'' |title=Lecithin:cholesterol acyltransferase. Functional regions and a structural model of the enzyme. |journal=J. Biol. Chem. |volume=262 |issue= 7 |pages= 3086-91 |year= 1987 |pmid= 2880847 |doi= }}
*{{cite journal | author=McLean J, Fielding C, Drayna D, ''et al.'' |title=Cloning and expression of human lecithin-cholesterol acyltransferase cDNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 8 |pages= 2335-9 |year= 1986 |pmid= 3458198 |doi= }}
*{{cite journal | author=Azoulay M, Henry I, Tata F, ''et al.'' |title=The structural gene for lecithin:cholesterol acyl transferase (LCAT) maps to 16q22. |journal=Ann. Hum. Genet. |volume=51 |issue= Pt 2 |pages= 129-36 |year= 1987 |pmid= 3674753 |doi= }}
*{{cite journal | author=McLean J, Wion K, Drayna D, ''et al.'' |title=Human lecithin-cholesterol acyltransferase gene: complete gene sequence and sites of expression. |journal=Nucleic Acids Res. |volume=14 |issue= 23 |pages= 9397-406 |year= 1987 |pmid= 3797244 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PAPPA... {November 15, 2007 6:40:31 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:41:09 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Pregnancy-associated plasma protein A, pappalysin 1
| HGNCid = 8602
| Symbol = PAPPA
| AltSymbols =; PAPA; ASBABP2; DIPLA1; IGFBP-4ase; PAPP-A; PAPPA1
| OMIM = 176385
| ECnumber =
| Homologene = 31097
| MGIid = 97479
| GeneAtlas_image1 = PBB_GE_PAPPA_201981_at_tn.png
| GeneAtlas_image2 = PBB_GE_PAPPA_201982_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008237 |text = metallopeptidase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007565 |text = female pregnancy}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5069
| Hs_Ensembl = ENSG00000182752
| Hs_RefseqProtein = NP_002572
| Hs_RefseqmRNA = NM_002581
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 117955892
| Hs_GenLoc_end = 118204420
| Hs_Uniprot = Q13219
| Mm_EntrezGene = 18491
| Mm_Ensembl = ENSMUSG00000028370
| Mm_RefseqmRNA = NM_021362
| Mm_RefseqProtein = NP_067337
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 64610535
| Mm_GenLoc_end = 64843870
| Mm_Uniprot = Q8R4K8
}}
}}
'''Pregnancy-associated plasma protein A, pappalysin 1''', also known as '''PAPPA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PAPPA pregnancy-associated plasma protein A, pappalysin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5069| 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 secreted metalloproteinase which cleaves insulin-like growth factor binding proteins (IGFBPs). It is thought to be involved in local proliferative processes such as wound healing and bone remodeling. Low plasma level of this protein has been suggested as a biochemical marker for pregnancies with aneuploid fetuses.<ref name="entrez">{{cite web | title = Entrez Gene: PAPPA pregnancy-associated plasma protein A, pappalysin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5069| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Sinosich MJ, Zakher A |title=Pregnancy-associated plasma protein A interaction with heparin: a critical appraisal. |journal=Gynecol. Obstet. Invest. |volume=32 |issue= 2 |pages= 72-7 |year= 1992 |pmid= 1721035 |doi= }}
*{{cite journal | author=Bischof P, Tseng L |title=In vitro release of pregnancy-associated plasma protein-A (PAPP-A) by human endometrial cells. |journal=American journal of reproductive immunology and microbiology : AJRIM |volume=10 |issue= 4 |pages= 139-42 |year= 1986 |pmid= 2422961 |doi= }}
*{{cite journal | author=Bolton AE, Pinto-Furtado LG, Andrew CE, Chapman MG |title=Measurement of the pregnancy-associated proteins, placental protein 14 and pregnancy-associated plasma protein A in human seminal plasma. |journal=Clinical reproduction and fertility |volume=4 |issue= 3 |pages= 233-40 |year= 1986 |pmid= 2427179 |doi= }}
*{{cite journal | author=Sinosich MJ, Saunders DM |title=Potential role of pregnancy-associated plasma protein-A in human reproduction. |journal=J. Reprod. Immunol. |volume=10 |issue= 1 |pages= 55-65 |year= 1987 |pmid= 2438405 |doi= }}
*{{cite journal | author=Tornehave D, Chemnitz J, Teisner B, ''et al.'' |title=Immunohistochemical demonstration of pregnancy-associated plasma protein A (PAPP-A) in the syncytiotrophoblast of the normal placenta at different gestational ages. |journal=Placenta |volume=5 |issue= 5 |pages= 427-31 |year= 1985 |pmid= 6084247 |doi= }}
*{{cite journal | author=McIntyre JA, Hsi B, Faulk WP, ''et al.'' |title=Immunological studies of the human placenta: functional and morphological analysis of pregnancy-associated plasma protein A (PAPP-A). |journal=Immunology |volume=44 |issue= 3 |pages= 577-83 |year= 1982 |pmid= 6172371 |doi= }}
*{{cite journal | author=Bischof P, Geinoz A, Herrmann WL, Sizonenko PC |title=Pregnancy-associated plasma protein A (PAPP-A) specifically inhibits the third component of human complement (C3). |journal=Placenta |volume=5 |issue= 1 |pages= 1-7 |year= 1984 |pmid= 6203109 |doi= }}
*{{cite journal | author=Schindler AM, Bischof P |title=Histochemical localization of pregnancy-associated plasma protein A in fetal, infant, and adult organs and comparison between antisera. |journal=Gynecol. Obstet. Invest. |volume=18 |issue= 2 |pages= 88-94 |year= 1984 |pmid= 6207082 |doi= }}
*{{cite journal | author=Kristensen T, Oxvig C, Sand O, ''et al.'' |title=Amino acid sequence of human pregnancy-associated plasma protein-A derived from cloned cDNA. |journal=Biochemistry |volume=33 |issue= 6 |pages= 1592-8 |year= 1994 |pmid= 7508748 |doi= }}
*{{cite journal | author=Durham SK, Kiefer MC, Riggs BL, Conover CA |title=Regulation of insulin-like growth factor binding protein 4 by a specific insulin-like growth factor binding protein 4 proteinase in normal human osteoblast-like cells: implications in bone cell physiology. |journal=J. Bone Miner. Res. |volume=9 |issue= 1 |pages= 111-7 |year= 1994 |pmid= 7512304 |doi= }}
*{{cite journal | author=Bonno M, Oxvig C, Kephart GM, ''et al.'' |title=Localization of pregnancy-associated plasma protein-A and colocalization of pregnancy-associated plasma protein-A messenger ribonucleic acid and eosinophil granule major basic protein messenger ribonucleic acid in placenta. |journal=Lab. Invest. |volume=71 |issue= 4 |pages= 560-6 |year= 1994 |pmid= 7526035 |doi= }}
*{{cite journal | author=Oxvig C, Haaning J, Kristensen L, ''et al.'' |title=Identification of angiotensinogen and complement C3dg as novel proteins binding the proform of eosinophil major basic protein in human pregnancy serum and plasma. |journal=J. Biol. Chem. |volume=270 |issue= 23 |pages= 13645-51 |year= 1995 |pmid= 7539791 |doi= }}
*{{cite journal | author=Zorin NA, Zhabin SG, Semenkov NN |title=Interaction of human pregnancy-associated plasma protein-A with serine proteinases. |journal=Clin. Chim. Acta |volume=239 |issue= 1 |pages= 47-55 |year= 1995 |pmid= 7586586 |doi= }}
*{{cite journal | author=Silahtaroglu AN, Tümer Z, Kristensen T, ''et al.'' |title=Assignment of the human gene for pregnancy-associated plasma protein A (PAPPA) to 9q33.1 by fluorescence in situ hybridization to mitotic and meiotic chromosomes. |journal=Cytogenet. Cell Genet. |volume=62 |issue= 4 |pages= 214-6 |year= 1993 |pmid= 7679961 |doi= }}
*{{cite journal | author=Oxvig C, Sand O, Kristensen T, ''et al.'' |title=Circulating human pregnancy-associated plasma protein-A is disulfide-bridged to the proform of eosinophil major basic protein. |journal=J. Biol. Chem. |volume=268 |issue= 17 |pages= 12243-6 |year= 1993 |pmid= 7685339 |doi= }}
*{{cite journal | author=Haaning J, Oxvig C, Overgaard MT, ''et al.'' |title=Complete cDNA sequence of the preproform of human pregnancy-associated plasma protein-A. Evidence for expression in the brain and induction by cAMP. |journal=Eur. J. Biochem. |volume=237 |issue= 1 |pages= 159-63 |year= 1996 |pmid= 8620868 |doi= }}
*{{cite journal | author=Lawrence JB, Oxvig C, Overgaard MT, ''et al.'' |title=The insulin-like growth factor (IGF)-dependent IGF binding protein-4 protease secreted by human fibroblasts is pregnancy-associated plasma protein-A. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 6 |pages= 3149-53 |year= 1999 |pmid= 10077652 |doi= }}
*{{cite journal | author=Overgaard MT, Oxvig C, Christiansen M, ''et al.'' |title=Messenger ribonucleic acid levels of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein: expression in human reproductive and nonreproductive tissues. |journal=Biol. Reprod. |volume=61 |issue= 4 |pages= 1083-9 |year= 1999 |pmid= 10491647 |doi= }}
*{{cite journal | author=Overgaard MT, Haaning J, Boldt HB, ''et al.'' |title=Expression of recombinant human pregnancy-associated plasma protein-A and identification of the proform of eosinophil major basic protein as its physiological inhibitor. |journal=J. Biol. Chem. |volume=275 |issue= 40 |pages= 31128-33 |year= 2000 |pmid= 10913121 |doi= 10.1074/jbc.M001384200 }}
*{{cite journal | author=Hourvitz A, Widger AE, Filho FL, ''et al.'' |title=Pregnancy-associated plasma protein-A gene expression in human ovaries is restricted to healthy follicles and corpora lutea. |journal=J. Clin. Endocrinol. Metab. |volume=85 |issue= 12 |pages= 4916-20 |year= 2001 |pmid= 11134163 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PLD1... {November 15, 2007 6:41:09 PM PST}
- SEARCH REDIRECT: Control Box Found: PLD1 {November 15, 2007 6:41:42 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 6:41:45 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 6:41:45 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 6:41:45 PM PST}
- UPDATED: Updated protein page: PLD1 {November 15, 2007 6:41:51 PM PST}
- INFO: Beginning work on POLB... {November 15, 2007 6:41:51 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:42:09 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_POLB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bno.
| PDB = {{PDB2|1bno}}, {{PDB2|1bnp}}, {{PDB2|1bpb}}, {{PDB2|1bpd}}, {{PDB2|1bpe}}, {{PDB2|1bpx}}, {{PDB2|1bpy}}, {{PDB2|1bpz}}, {{PDB2|1dk2}}, {{PDB2|1dk3}}, {{PDB2|1huo}}, {{PDB2|1huz}}, {{PDB2|1jn3}}, {{PDB2|1mq2}}, {{PDB2|1mq3}}, {{PDB2|1nom}}, {{PDB2|1rpl}}, {{PDB2|1tv9}}, {{PDB2|1tva}}, {{PDB2|1zjm}}, {{PDB2|1zjn}}, {{PDB2|1zqa}}, {{PDB2|1zqb}}, {{PDB2|1zqc}}, {{PDB2|1zqd}}, {{PDB2|1zqe}}, {{PDB2|1zqf}}, {{PDB2|1zqg}}, {{PDB2|1zqh}}, {{PDB2|1zqi}}, {{PDB2|1zqj}}, {{PDB2|1zqk}}, {{PDB2|1zql}}, {{PDB2|1zqm}}, {{PDB2|1zqn}}, {{PDB2|1zqo}}, {{PDB2|1zqp}}, {{PDB2|1zqq}}, {{PDB2|1zqr}}, {{PDB2|1zqs}}, {{PDB2|1zqt}}, {{PDB2|1zqu}}, {{PDB2|1zqv}}, {{PDB2|1zqw}}, {{PDB2|1zqx}}, {{PDB2|1zqy}}, {{PDB2|1zqz}}, {{PDB2|2bpc}}, {{PDB2|2bpf}}, {{PDB2|2bpg}}, {{PDB2|2fmp}}, {{PDB2|2fmq}}, {{PDB2|2fms}}, {{PDB2|2i9g}}, {{PDB2|2iso}}, {{PDB2|2isp}}, {{PDB2|2p66}}, {{PDB2|7ice}}, {{PDB2|7icf}}, {{PDB2|7icg}}, {{PDB2|7ich}}, {{PDB2|7ici}}, {{PDB2|7icj}}, {{PDB2|7ick}}, {{PDB2|7icl}}, {{PDB2|7icm}}, {{PDB2|7icn}}, {{PDB2|7ico}}, {{PDB2|7icp}}, {{PDB2|7icq}}, {{PDB2|7icr}}, {{PDB2|7ics}}, {{PDB2|7ict}}, {{PDB2|7icu}}, {{PDB2|7icv}}, {{PDB2|8ica}}, {{PDB2|8icb}}, {{PDB2|8icc}}, {{PDB2|8ice}}, {{PDB2|8icf}}, {{PDB2|8icg}}, {{PDB2|8ich}}, {{PDB2|8ici}}, {{PDB2|8icj}}, {{PDB2|8ick}}, {{PDB2|8icl}}, {{PDB2|8icm}}, {{PDB2|8icn}}, {{PDB2|8ico}}, {{PDB2|8icp}}, {{PDB2|8icq}}, {{PDB2|8icr}}, {{PDB2|8ics}}, {{PDB2|8ict}}, {{PDB2|8icu}}, {{PDB2|8icv}}, {{PDB2|8icw}}, {{PDB2|8icx}}, {{PDB2|8icy}}, {{PDB2|8icz}}, {{PDB2|9ica}}, {{PDB2|9icb}}, {{PDB2|9icc}}, {{PDB2|9ice}}, {{PDB2|9icf}}, {{PDB2|9icg}}, {{PDB2|9ich}}, {{PDB2|9ici}}, {{PDB2|9icj}}, {{PDB2|9ick}}, {{PDB2|9icl}}, {{PDB2|9icm}}, {{PDB2|9icn}}, {{PDB2|9ico}}, {{PDB2|9icp}}, {{PDB2|9icq}}, {{PDB2|9icr}}, {{PDB2|9ics}}, {{PDB2|9ict}}, {{PDB2|9icu}}, {{PDB2|9icv}}, {{PDB2|9icw}}, {{PDB2|9icx}}, {{PDB2|9icy}}
| Name = Polymerase (DNA directed), beta
| HGNCid = 9174
| Symbol = POLB
| AltSymbols =; MGC125976
| OMIM = 174760
| ECnumber =
| Homologene = 2013
| MGIid = 97740
| GeneAtlas_image1 = PBB_GE_POLB_203616_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0003890 |text = beta DNA polymerase activity}} {{GNF_GO|id=GO:0008017 |text = microtubule binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0016829 |text = lyase activity}} {{GNF_GO|id=GO:0031402 |text = sodium ion binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005876 |text = spindle microtubule}}
| Process = {{GNF_GO|id=GO:0006261 |text = DNA-dependent DNA replication}} {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0008219 |text = cell death}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5423
| Hs_Ensembl = ENSG00000070501
| Hs_RefseqProtein = NP_002681
| Hs_RefseqmRNA = NM_002690
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 42315131
| Hs_GenLoc_end = 42348482
| Hs_Uniprot = P06746
| Mm_EntrezGene = 18970
| Mm_Ensembl = ENSMUSG00000031536
| Mm_RefseqmRNA = NM_011130
| Mm_RefseqProtein = NP_035260
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 24093675
| Mm_GenLoc_end = 24118966
| Mm_Uniprot = Q62085
}}
}}
'''Polymerase (DNA directed), beta''', also known as '''POLB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: POLB polymerase (DNA directed), beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5423| 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 = In eukaryotic cells, DNA polymerase beta (POLB) performs base excision repair (BER) required for DNA maintenance, replication, recombination, and drug resistance. Also see POLA (MIM 312040).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: POLB polymerase (DNA directed), beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5423| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Date T, Tanihara K, Yamamoto S, ''et al.'' |title=Two regions in human DNA polymerase beta mRNA suppress translation in Escherichia coli. |journal=Nucleic Acids Res. |volume=20 |issue= 18 |pages= 4859-64 |year= 1992 |pmid= 1408801 |doi= }}
*{{cite journal | author=Wang L, Patel U, Ghosh L, Banerjee S |title=DNA polymerase beta mutations in human colorectal cancer. |journal=Cancer Res. |volume=52 |issue= 17 |pages= 4824-7 |year= 1992 |pmid= 1511447 |doi= }}
*{{cite journal | author=Tokui T, Inagaki M, Nishizawa K, ''et al.'' |title=Inactivation of DNA polymerase beta by in vitro phosphorylation with protein kinase C. |journal=J. Biol. Chem. |volume=266 |issue= 17 |pages= 10820-4 |year= 1991 |pmid= 2040602 |doi= }}
*{{cite journal | author=SenGupta DN, Zmudzka BZ, Kumar P, ''et al.'' |title=Sequence of human DNA polymerase beta mRNA obtained through cDNA cloning. |journal=Biochem. Biophys. Res. Commun. |volume=136 |issue= 1 |pages= 341-7 |year= 1986 |pmid= 2423078 |doi= }}
*{{cite journal | author=Zmudzka BZ, Fornace A, Collins J, Wilson SH |title=Characterization of DNA polymerase beta mRNA: cell-cycle and growth response in cultured human cells. |journal=Nucleic Acids Res. |volume=16 |issue= 20 |pages= 9587-96 |year= 1988 |pmid= 2460824 |doi= }}
*{{cite journal | author=Widen SG, Kedar P, Wilson SH |title=Human beta-polymerase gene. Structure of the 5'-flanking region and active promoter. |journal=J. Biol. Chem. |volume=263 |issue= 32 |pages= 16992-8 |year= 1988 |pmid= 3182828 |doi= }}
*{{cite journal | author=Abbotts J, SenGupta DN, Zmudzka B, ''et al.'' |title=Expression of human DNA polymerase beta in Escherichia coli and characterization of the recombinant enzyme. |journal=Biochemistry |volume=27 |issue= 3 |pages= 901-9 |year= 1988 |pmid= 3284575 |doi= }}
*{{cite journal | author=Dobashi Y, Kubota Y, Shuin T, ''et al.'' |title=Polymorphisms in the human DNA polymerase beta gene. |journal=Hum. Genet. |volume=95 |issue= 4 |pages= 389-90 |year= 1995 |pmid= 7705833 |doi= }}
*{{cite journal | author=Chyan YJ, Ackerman S, Shepherd NS, ''et al.'' |title=The human DNA polymerase beta gene structure. Evidence of alternative splicing in gene expression. |journal=Nucleic Acids Res. |volume=22 |issue= 14 |pages= 2719-25 |year= 1994 |pmid= 7914364 |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=Chang M, Burmer GC, Sweasy J, ''et al.'' |title=Evidence against DNA polymerase beta as a candidate gene for Werner syndrome. |journal=Hum. Genet. |volume=93 |issue= 5 |pages= 507-12 |year= 1994 |pmid= 8168825 |doi= }}
*{{cite journal | author=Chyan YJ, Strauss PR, Wood TG, Wilson SH |title=Identification of novel mRNA isoforms for human DNA polymerase beta. |journal=DNA Cell Biol. |volume=15 |issue= 8 |pages= 653-9 |year= 1996 |pmid= 8769567 |doi= }}
*{{cite journal | author=Pelletier H, Sawaya MR, Wolfle W, ''et al.'' |title=Crystal structures of human DNA polymerase beta complexed with DNA: implications for catalytic mechanism, processivity, and fidelity. |journal=Biochemistry |volume=35 |issue= 39 |pages= 12742-61 |year= 1996 |pmid= 8841118 |doi= 10.1021/bi952955d }}
*{{cite journal | author=Pelletier H, Sawaya MR, Wolfle W, ''et al.'' |title=A structural basis for metal ion mutagenicity and nucleotide selectivity in human DNA polymerase beta. |journal=Biochemistry |volume=35 |issue= 39 |pages= 12762-77 |year= 1996 |pmid= 8841119 |doi= 10.1021/bi9529566 }}
*{{cite journal | author=Pelletier H, Sawaya MR |title=Characterization of the metal ion binding helix-hairpin-helix motifs in human DNA polymerase beta by X-ray structural analysis. |journal=Biochemistry |volume=35 |issue= 39 |pages= 12778-87 |year= 1996 |pmid= 8841120 |doi= 10.1021/bi960790i }}
*{{cite journal | author=Kubota Y, Nash RA, Klungland A, ''et al.'' |title=Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein. |journal=EMBO J. |volume=15 |issue= 23 |pages= 6662-70 |year= 1997 |pmid= 8978692 |doi= }}
*{{cite journal | author=Bennett RA, Wilson DM, Wong D, Demple B |title=Interaction of human apurinic endonuclease and DNA polymerase beta in the base excision repair pathway. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 14 |pages= 7166-9 |year= 1997 |pmid= 9207062 |doi= }}
*{{cite journal | author=Sawaya MR, Prasad R, Wilson SH, ''et al.'' |title=Crystal structures of human DNA polymerase beta complexed with gapped and nicked DNA: evidence for an induced fit mechanism. |journal=Biochemistry |volume=36 |issue= 37 |pages= 11205-15 |year= 1997 |pmid= 9287163 |doi= 10.1021/bi9703812 }}
*{{cite journal | author=Bhattacharyya N, Banerjee S |title=A variant of DNA polymerase beta acts as a dominant negative mutant. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 19 |pages= 10324-9 |year= 1997 |pmid= 9294209 |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 POLR2I... {November 15, 2007 6:42:09 PM PST}
- SEARCH REDIRECT: Control Box Found: POLR2I {November 15, 2007 6:42:34 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 6:42:36 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 6:42:36 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 6:42:36 PM PST}
- UPDATED: Updated protein page: POLR2I {November 15, 2007 6:42:43 PM PST}
- INFO: Beginning work on PRKCI... {November 15, 2007 6:42:43 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:43:16 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_PRKCI_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1vd2.
| PDB = {{PDB2|1vd2}}, {{PDB2|1wmh}}, {{PDB2|1zrz}}
| Name = Protein kinase C, iota
| HGNCid = 9404
| Symbol = PRKCI
| AltSymbols =; DXS1179E; MGC26534; PKCI; nPKC-iota
| OMIM = 600539
| ECnumber =
| Homologene = 37667
| MGIid = 99260
| GeneAtlas_image1 = PBB_GE_PRKCI_209678_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PRKCI_209677_at_tn.png
| GeneAtlas_image3 = PBB_GE_PRKCI_213518_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004700 |text = atypical protein kinase C activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0005543 |text = phospholipid binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0019992 |text = diacylglycerol binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0000133 |text = polarisome}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0045177 |text = apical part of cell}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006612 |text = protein targeting to membrane}} {{GNF_GO|id=GO:0007010 |text = cytoskeleton organization and biogenesis}} {{GNF_GO|id=GO:0007015 |text = actin filament organization}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0016044 |text = membrane organization and biogenesis}} {{GNF_GO|id=GO:0016192 |text = vesicle-mediated transport}} {{GNF_GO|id=GO:0035089 |text = establishment of apical/basal cell polarity}} {{GNF_GO|id=GO:0042462 |text = eye photoreceptor cell development}} {{GNF_GO|id=GO:0045197 |text = establishment and/or maintenance of epithelial cell polarity}} {{GNF_GO|id=GO:0045216 |text = intercellular junction assembly and maintenance}} {{GNF_GO|id=GO:0046903 |text = secretion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5584
| Hs_Ensembl = ENSG00000163558
| Hs_RefseqProtein = NP_002731
| Hs_RefseqmRNA = NM_002740
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 171422919
| Hs_GenLoc_end = 171506458
| Hs_Uniprot = P41743
| Mm_EntrezGene = 18759
| Mm_Ensembl = ENSMUSG00000037643
| Mm_RefseqmRNA = NM_008857
| Mm_RefseqProtein = NP_032883
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 31186625
| Mm_GenLoc_end = 31243615
| Mm_Uniprot = Q3TJJ5
}}
}}
'''Protein kinase C, iota''', also known as '''PRKCI''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRKCI protein kinase C, iota| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5584| 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 protein kinase C (PKC) family of serine/threonine protein kinases. The PKC family comprises at least eight members, which are differentially expressed and are involved in a wide variety of cellular processes. This protein kinase is calcium-independent and phospholipid-dependent. It is not activated by phorbolesters or diacylglycerol. This kinase can be recruited to vesicle tubular clusters (VTCs) by direct interaction with the small GTPase RAB2, where this kinase phosphorylates glyceraldehyde-3-phosphate dehydrogenase (GAPD/GAPDH) and plays a role in microtubule dynamics in the early secretory pathway. This kinase is found to be necessary for BCL-ABL-mediated resistance to drug-induced apoptosis and therefore protects leukemia cells against drug-induced apoptosis. There is a single exon pseudogene mapped on chromosome X.<ref name="entrez">{{cite web | title = Entrez Gene: PRKCI protein kinase C, iota| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5584| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Suzuki A, Akimoto K, Ohno S |title=Protein kinase C lambda/iota (PKClambda/iota): a PKC isotype essential for the development of multicellular organisms. |journal=J. Biochem. |volume=133 |issue= 1 |pages= 9-16 |year= 2003 |pmid= 12761193 |doi= }}
*{{cite journal | author=Fields AP, Regala RP |title=Protein kinase C iota: human oncogene, prognostic marker and therapeutic target. |journal=Pharmacol. Res. |volume=55 |issue= 6 |pages= 487-97 |year= 2007 |pmid= 17570678 |doi= 10.1016/j.phrs.2007.04.015 }}
*{{cite journal | author=Ruegg CL, Strand M |title=A synthetic peptide with sequence identity to the transmembrane protein GP41 of HIV-1 inhibits distinct lymphocyte activation pathways dependent on protein kinase C and intracellular calcium influx. |journal=Cell. Immunol. |volume=137 |issue= 1 |pages= 1-13 |year= 1991 |pmid= 1832084 |doi= }}
*{{cite journal | author=Chowdhury IH, Koyanagi Y, Kobayashi S, ''et al.'' |title=The phorbol ester TPA strongly inhibits HIV-1-induced syncytia formation but enhances virus production: possible involvement of protein kinase C pathway. |journal=Virology |volume=176 |issue= 1 |pages= 126-32 |year= 1990 |pmid= 1970444 |doi= }}
*{{cite journal | author=Ruegg CL, Strand M |title=Inhibition of protein kinase C and anti-CD3-induced Ca2+ influx in Jurkat T cells by a synthetic peptide with sequence identity to HIV-1 gp41. |journal=J. Immunol. |volume=144 |issue= 10 |pages= 3928-35 |year= 1990 |pmid= 2139676 |doi= }}
*{{cite journal | author=Jakobovits A, Rosenthal A, Capon DJ |title=Trans-activation of HIV-1 LTR-directed gene expression by tat requires protein kinase C. |journal=EMBO J. |volume=9 |issue= 4 |pages= 1165-70 |year= 1990 |pmid= 2182321 |doi= }}
*{{cite journal | author=Fields AP, Bednarik DP, Hess A, May WS |title=Human immunodeficiency virus induces phosphorylation of its cell surface receptor. |journal=Nature |volume=333 |issue= 6170 |pages= 278-80 |year= 1988 |pmid= 3259291 |doi= 10.1038/333278a0 }}
*{{cite journal | author=Mazzarella R, Ciccodicola A, Esposito T, ''et al.'' |title=Human protein kinase C Iota gene (PRKCI) is closely linked to the BTK gene in Xq21.3. |journal=Genomics |volume=26 |issue= 3 |pages= 629-31 |year= 1995 |pmid= 7607695 |doi= }}
*{{cite journal | author=Chirmule N, Goonewardena H, Pahwa S, ''et al.'' |title=HIV-1 envelope glycoproteins induce activation of activated protein-1 in CD4+ T cells. |journal=J. Biol. Chem. |volume=270 |issue= 33 |pages= 19364-9 |year= 1995 |pmid= 7642615 |doi= }}
*{{cite journal | author=Ward NE, Gravitt KR, O'Brian CA |title=Inhibition of protein kinase C by a synthetic peptide corresponding to cytoplasmic domain residues 828-848 of the human immunodeficiency virus type 1 envelope glycoprotein. |journal=Cancer Lett. |volume=88 |issue= 1 |pages= 37-40 |year= 1995 |pmid= 7850771 |doi= }}
*{{cite journal | author=Gupta S, Aggarwal S, Kim C, Gollapudi S |title=Human immunodeficiency virus-1 recombinant gp120 induces changes in protein kinase C isozymes--a preliminary report. |journal=Int. J. Immunopharmacol. |volume=16 |issue= 3 |pages= 197-204 |year= 1994 |pmid= 8206685 |doi= }}
*{{cite journal | author=Selbie LA, Schmitz-Peiffer C, Sheng Y, Biden TJ |title=Molecular cloning and characterization of PKC iota, an atypical isoform of protein kinase C derived from insulin-secreting cells. |journal=J. Biol. Chem. |volume=268 |issue= 32 |pages= 24296-302 |year= 1993 |pmid= 8226978 |doi= }}
*{{cite journal | author=Diaz-Meco MT, Municio MM, Sanchez P, ''et al.'' |title=Lambda-interacting protein, a novel protein that specifically interacts with the zinc finger domain of the atypical protein kinase C isotype lambda/iota and stimulates its kinase activity in vitro and in vivo. |journal=Mol. Cell. Biol. |volume=16 |issue= 1 |pages= 105-14 |year= 1996 |pmid= 8524286 |doi= }}
*{{cite journal | author=Parada NA, Cruikshank WW, Danis HL, ''et al.'' |title=IL-16- and other CD4 ligand-induced migration is dependent upon protein kinase C. |journal=Cell. Immunol. |volume=168 |issue= 1 |pages= 100-6 |year= 1996 |pmid= 8599832 |doi= 10.1006/cimm.1996.0054 }}
*{{cite journal | author=Conant K, Ma M, Nath A, Major EO |title=Extracellular human immunodeficiency virus type 1 Tat protein is associated with an increase in both NF-kappa B binding and protein kinase C activity in primary human astrocytes. |journal=J. Virol. |volume=70 |issue= 3 |pages= 1384-9 |year= 1996 |pmid= 8627654 |doi= }}
*{{cite journal | author=Díaz-Meco MT, Municio MM, Frutos S, ''et al.'' |title=The product of par-4, a gene induced during apoptosis, interacts selectively with the atypical isoforms of protein kinase C. |journal=Cell |volume=86 |issue= 5 |pages= 777-86 |year= 1996 |pmid= 8797824 |doi= }}
*{{cite journal | author=Holmes AM |title=In vitro phosphorylation of human immunodeficiency virus type 1 Tat protein by protein kinase C: evidence for the phosphorylation of amino acid residue serine-46. |journal=Arch. Biochem. Biophys. |volume=335 |issue= 1 |pages= 8-12 |year= 1996 |pmid= 8914829 |doi= 10.1006/abbi.1996.0476 }}
*{{cite journal | author=Murray NR, Fields AP |title=Atypical protein kinase C iota protects human leukemia cells against drug-induced apoptosis. |journal=J. Biol. Chem. |volume=272 |issue= 44 |pages= 27521-4 |year= 1997 |pmid= 9346882 |doi= }}
*{{cite journal | author=Borgatti P, Zauli G, Cantley LC, Capitani S |title=Extracellular HIV-1 Tat protein induces a rapid and selective activation of protein kinase C (PKC)-alpha, and -epsilon and -zeta isoforms in PC12 cells. |journal=Biochem. Biophys. Res. Commun. |volume=242 |issue= 2 |pages= 332-7 |year= 1998 |pmid= 9446795 |doi= }}
*{{cite journal | author=Sanchez P, De Carcer G, Sandoval IV, ''et al.'' |title=Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62. |journal=Mol. Cell. Biol. |volume=18 |issue= 5 |pages= 3069-80 |year= 1998 |pmid= 9566925 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PRKD1... {November 15, 2007 6:43:16 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:43:42 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 = Protein kinase D1
| HGNCid = 9407
| Symbol = PRKD1
| AltSymbols =; PKC-MU; PKCM; PKD; PRKCM
| OMIM = 605435
| ECnumber =
| Homologene = 55680
| MGIid = 99879
| GeneAtlas_image1 = PBB_GE_PRKD1_205880_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004700 |text = atypical protein kinase C activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0019992 |text = diacylglycerol binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5587
| Hs_Ensembl = ENSG00000184304
| Hs_RefseqProtein = NP_002733
| Hs_RefseqmRNA = NM_002742
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 29116195
| Hs_GenLoc_end = 29466469
| Hs_Uniprot = Q15139
| Mm_EntrezGene = 18760
| Mm_Ensembl = ENSMUSG00000002688
| Mm_RefseqmRNA = NM_008858
| Mm_RefseqProtein = NP_032884
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 51217854
| Mm_GenLoc_end = 51571105
| Mm_Uniprot = Q62101
}}
}}
'''Protein kinase D1''', also known as '''PRKD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRKD1 protein kinase D1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5587| 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 = Members of the protein kinase C (PKC) family function in many extracellular receptor-mediated signal transduction pathways. See PRKCA (MIM 176960) for further background information. The PRKCM gene encodes a cytosolic serine-threonine kinase that binds to the trans-Golgi network and regulates the fission of transport carriers specifically destined to the cell surface.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: PRKD1 protein kinase D1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5587| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Van Lint J, Rykx A, Maeda Y, ''et al.'' |title=Protein kinase D: an intracellular traffic regulator on the move. |journal=Trends Cell Biol. |volume=12 |issue= 4 |pages= 193-200 |year= 2002 |pmid= 11978539 |doi= }}
*{{cite journal | author=Busch H, Eisenhart-Rothe BV |title=[Old and new dangers of blood transfusion (author's transl)] |journal=MMW, Münchener medizinische Wochenschrift |volume=118 |issue= 22 |pages= 713-8 |year= 1976 |pmid= 5668 |doi= }}
*{{cite journal | author=Jakobovits A, Rosenthal A, Capon DJ |title=Trans-activation of HIV-1 LTR-directed gene expression by tat requires protein kinase C. |journal=EMBO J. |volume=9 |issue= 4 |pages= 1165-70 |year= 1990 |pmid= 2182321 |doi= }}
*{{cite journal | author=Davis RJ, Czech MP |title=Tumor-promoting phorbol diesters cause the phosphorylation of epidermal growth factor receptors in normal human fibroblasts at threonine-654. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 7 |pages= 1974-8 |year= 1985 |pmid= 2984676 |doi= }}
*{{cite journal | author=Davis RJ, Czech MP |title=Platelet-derived growth factor mimics phorbol diester action on epidermal growth factor receptor phosphorylation at threonine-654. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 12 |pages= 4080-4 |year= 1985 |pmid= 2987962 |doi= }}
*{{cite journal | author=Johannes FJ, Prestle J, Eis S, ''et al.'' |title=PKCu is a novel, atypical member of the protein kinase C family. |journal=J. Biol. Chem. |volume=269 |issue= 8 |pages= 6140-8 |year= 1994 |pmid= 8119958 |doi= }}
*{{cite journal | author=Conant K, Ma M, Nath A, Major EO |title=Extracellular human immunodeficiency virus type 1 Tat protein is associated with an increase in both NF-kappa B binding and protein kinase C activity in primary human astrocytes. |journal=J. Virol. |volume=70 |issue= 3 |pages= 1384-9 |year= 1996 |pmid= 8627654 |doi= }}
*{{cite journal | author=Sidorenko SP, Law CL, Klaus SJ, ''et al.'' |title=Protein kinase C mu (PKC mu) associates with the B cell antigen receptor complex and regulates lymphocyte signaling. |journal=Immunity |volume=5 |issue= 4 |pages= 353-63 |year= 1996 |pmid= 8885868 |doi= }}
*{{cite journal | author=Holmes AM |title=In vitro phosphorylation of human immunodeficiency virus type 1 Tat protein by protein kinase C: evidence for the phosphorylation of amino acid residue serine-46. |journal=Arch. Biochem. Biophys. |volume=335 |issue= 1 |pages= 8-12 |year= 1996 |pmid= 8914829 |doi= 10.1006/abbi.1996.0476 }}
*{{cite journal | author=Borgatti P, Zauli G, Cantley LC, Capitani S |title=Extracellular HIV-1 Tat protein induces a rapid and selective activation of protein kinase C (PKC)-alpha, and -epsilon and -zeta isoforms in PC12 cells. |journal=Biochem. Biophys. Res. Commun. |volume=242 |issue= 2 |pages= 332-7 |year= 1998 |pmid= 9446795 |doi= }}
*{{cite journal | author=Zidovetzki R, Wang JL, Chen P, ''et al.'' |title=Human immunodeficiency virus Tat protein induces interleukin 6 mRNA expression in human brain endothelial cells via protein kinase C- and cAMP-dependent protein kinase pathways. |journal=AIDS Res. Hum. Retroviruses |volume=14 |issue= 10 |pages= 825-33 |year= 1998 |pmid= 9671211 |doi= }}
*{{cite journal | author=Waldron RT, Iglesias T, Rozengurt E |title=The pleckstrin homology domain of protein kinase D interacts preferentially with the eta isoform of protein kinase C. |journal=J. Biol. Chem. |volume=274 |issue= 14 |pages= 9224-30 |year= 1999 |pmid= 10092595 |doi= }}
*{{cite journal | author=Hausser A, Storz P, Link G, ''et al.'' |title=Protein kinase C mu is negatively regulated by 14-3-3 signal transduction proteins. |journal=J. Biol. Chem. |volume=274 |issue= 14 |pages= 9258-64 |year= 1999 |pmid= 10092600 |doi= }}
*{{cite journal | author=Jamora C, Yamanouye N, Van Lint J, ''et al.'' |title=Gbetagamma-mediated regulation of Golgi organization is through the direct activation of protein kinase D. |journal=Cell |volume=98 |issue= 1 |pages= 59-68 |year= 1999 |pmid= 10412981 |doi= 10.1016/S0092-8674(00)80606-6 }}
*{{cite journal | author=Bagowski CP, Stein-Gerlach M, Choidas A, Ullrich A |title=Cell-type specific phosphorylation of threonines T654 and T669 by PKD defines the signal capacity of the EGF receptor. |journal=EMBO J. |volume=18 |issue= 20 |pages= 5567-76 |year= 1999 |pmid= 10523301 |doi= 10.1093/emboj/18.20.5567 }}
*{{cite journal | author=Johannes FJ, Hausser A, Storz P, ''et al.'' |title=Bruton's tyrosine kinase (Btk) associates with protein kinase C mu. |journal=FEBS Lett. |volume=461 |issue= 1-2 |pages= 68-72 |year= 1999 |pmid= 10561498 |doi= }}
*{{cite journal | author=Storz P, Hausser A, Link G, ''et al.'' |title=Protein kinase C [micro] is regulated by the multifunctional chaperon protein p32. |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24601-7 |year= 2000 |pmid= 10831594 |doi= 10.1074/jbc.M002964200 }}
*{{cite journal | author=Mayne M, Holden CP, Nath A, Geiger JD |title=Release of calcium from inositol 1,4,5-trisphosphate receptor-regulated stores by HIV-1 Tat regulates TNF-alpha production in human macrophages. |journal=J. Immunol. |volume=164 |issue= 12 |pages= 6538-42 |year= 2000 |pmid= 10843712 |doi= }}
*{{cite journal | author=Matthews SA, Iglesias T, Rozengurt E, Cantrell D |title=Spatial and temporal regulation of protein kinase D (PKD). |journal=EMBO J. |volume=19 |issue= 12 |pages= 2935-45 |year= 2000 |pmid= 10856238 |doi= 10.1093/emboj/19.12.2935 }}
*{{cite journal | author=Vertommen D, Rider M, Ni Y, ''et al.'' |title=Regulation of protein kinase D by multisite phosphorylation. Identification of phosphorylation sites by mass spectrometry and characterization by site-directed mutagenesis. |journal=J. Biol. Chem. |volume=275 |issue= 26 |pages= 19567-76 |year= 2000 |pmid= 10867018 |doi= 10.1074/jbc.M001357200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RYR2... {November 15, 2007 6:43:42 PM PST}
- SEARCH REDIRECT: Control Box Found: RYR2 {November 15, 2007 6:44:06 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 6:44:08 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 6:44:08 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 6:44:08 PM PST}
- UPDATED: Updated protein page: RYR2 {November 15, 2007 6:44:14 PM PST}
- INFO: Beginning work on SFRS2... {November 15, 2007 6:44:14 PM PST}
- SEARCH REDIRECT: Control Box Found: SFRS2 {November 15, 2007 6:44:46 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 6:44:49 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 6:44:49 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 6:44:49 PM PST}
- UPDATED: Updated protein page: SFRS2 {November 15, 2007 6:44:55 PM PST}
- INFO: Beginning work on SLC3A2... {November 15, 2007 6:44:55 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:45:30 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_SLC3A2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2dh2.
| PDB = {{PDB2|2dh2}}, {{PDB2|2dh3}}
| Name = Solute carrier family 3 (activators of dibasic and neutral amino acid transport), member 2
| HGNCid = 11026
| Symbol = SLC3A2
| AltSymbols =; 4F2; 4F2HC; 4T2HC; CD98; CD98HC; MDU1; NACAE
| OMIM = 158070
| ECnumber =
| Homologene = 1795
| MGIid = 96955
| GeneAtlas_image1 = PBB_GE_SLC3A2_200924_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003824 |text = catalytic activity}} {{GNF_GO|id=GO:0005432 |text = calcium:sodium antiporter activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0015171 |text = amino acid transmembrane transporter activity}} {{GNF_GO|id=GO:0043169 |text = cation binding}}
| Component = {{GNF_GO|id=GO:0009986 |text = cell surface}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006816 |text = calcium ion transport}} {{GNF_GO|id=GO:0006865 |text = amino acid transport}} {{GNF_GO|id=GO:0015827 |text = tryptophan transport}} {{GNF_GO|id=GO:0016049 |text = cell growth}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6520
| Hs_Ensembl = ENSG00000168003
| Hs_RefseqProtein = NP_001012679
| Hs_RefseqmRNA = NM_001012661
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 62380094
| Hs_GenLoc_end = 62412928
| Hs_Uniprot = P08195
| Mm_EntrezGene = 17254
| Mm_Ensembl = ENSMUSG00000010095
| Mm_RefseqmRNA = NM_008577
| Mm_RefseqProtein = NP_032603
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 8773927
| Mm_GenLoc_end = 8780921
| Mm_Uniprot = Q3TIP1
}}
}}
'''Solute carrier family 3 (activators of dibasic and neutral amino acid transport), member 2''', also known as '''SLC3A2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SLC3A2 solute carrier family 3 (activators of dibasic and neutral amino acid transport), member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6520| 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 is a member of the solute carrier family and encodes a cell surface, transmembrane protein with an alpha amylase domain. The protein exists as the heavy chain of a heterodimer, covalently bound through di-sulfide bonds to one of several possible light chains. It associates with integrins and mediates integrin-dependent signaling related to normal cell growth and tumorigenesis. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.<ref name="entrez">{{cite web | title = Entrez Gene: SLC3A2 solute carrier family 3 (activators of dibasic and neutral amino acid transport), member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6520| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Rochelle JM, Watson ML, Oakey RJ, Seldin MF |title=A linkage map of mouse chromosome 19: definition of comparative mapping relationships with human chromosomes 10 and 11 including the MEN1 locus. |journal=Genomics |volume=14 |issue= 1 |pages= 26-31 |year= 1992 |pmid= 1358795 |doi= }}
*{{cite journal | author=Michalak M, Quackenbush EJ, Letarte M |title=Inhibition of Na+/Ca2+ exchanger activity in cardiac and skeletal muscle sarcolemmal vesicles by monoclonal antibody 44D7. |journal=J. Biol. Chem. |volume=261 |issue= 1 |pages= 92-5 |year= 1986 |pmid= 2416754 |doi= }}
*{{cite journal | author=Teixeira S, Di Grandi S, Kühn LC |title=Primary structure of the human 4F2 antigen heavy chain predicts a transmembrane protein with a cytoplasmic NH2 terminus. |journal=J. Biol. Chem. |volume=262 |issue= 20 |pages= 9574-80 |year= 1987 |pmid= 3036867 |doi= }}
*{{cite journal | author=Gottesdiener KM, Karpinski BA, Lindsten T, ''et al.'' |title=Isolation and structural characterization of the human 4F2 heavy-chain gene, an inducible gene involved in T-lymphocyte activation. |journal=Mol. Cell. Biol. |volume=8 |issue= 9 |pages= 3809-19 |year= 1989 |pmid= 3265470 |doi= }}
*{{cite journal | author=Lindsten T, June CH, Thompson CB, Leiden JM |title=Regulation of 4F2 heavy-chain gene expression during normal human T-cell activation can be mediated by multiple distinct molecular mechanisms. |journal=Mol. Cell. Biol. |volume=8 |issue= 9 |pages= 3820-6 |year= 1989 |pmid= 3265471 |doi= }}
*{{cite journal | author=Quackenbush E, Clabby M, Gottesdiener KM, ''et al.'' |title=Molecular cloning of complementary DNAs encoding the heavy chain of the human 4F2 cell-surface antigen: a type II membrane glycoprotein involved in normal and neoplastic cell growth. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 18 |pages= 6526-30 |year= 1987 |pmid= 3476959 |doi= }}
*{{cite journal | author=Lumadue JA, Glick AB, Ruddle FH |title=Cloning, sequence analysis, and expression of the large subunit of the human lymphocyte activation antigen 4F2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 24 |pages= 9204-8 |year= 1988 |pmid= 3480538 |doi= }}
*{{cite journal | author=Posillico JT, Srikanta S, Eisenbarth G, ''et al.'' |title=Binding of monoclonal antibody (4F2) to its cell surface antigen on dispersed adenomatous parathyroid cells raises cytosolic calcium and inhibits parathyroid hormone secretion. |journal=J. Clin. Endocrinol. Metab. |volume=64 |issue= 1 |pages= 43-50 |year= 1987 |pmid= 3782435 |doi= }}
*{{cite journal | author=Hemler ME, Strominger JL |title=Characterization of antigen recognized by the monoclonal antibody (4F2): different molecular forms on human T and B lymphoblastoid cell lines. |journal=J. Immunol. |volume=129 |issue= 2 |pages= 623-8 |year= 1982 |pmid= 6177771 |doi= }}
*{{cite journal | author=Peters PG, Kamarck ME, Hemler ME, ''et al.'' |title=Genetic and biochemical characterization of a human surface determinant on somatic cell hybrids: the 4F2 antigen. |journal=Somatic Cell Genet. |volume=8 |issue= 6 |pages= 825-34 |year= 1983 |pmid= 6187076 |doi= }}
*{{cite journal | author=Francke U, Foellmer BE, Haynes BF |title=Chromosome mapping of human cell surface molecules: monoclonal anti-human lymphocyte antibodies 4F2, A3D8, and A1G3 define antigens controlled by different regions of chromosome 11. |journal=Somatic Cell Genet. |volume=9 |issue= 3 |pages= 333-44 |year= 1983 |pmid= 6190235 |doi= }}
*{{cite journal | author=Haynes BF, Hemler ME, Mann DL, ''et al.'' |title=Characterization of a monoclonal antibody (4F2) that binds to human monocytes and to a subset of activated lymphocytes. |journal=J. Immunol. |volume=126 |issue= 4 |pages= 1409-14 |year= 1981 |pmid= 7204970 |doi= }}
*{{cite journal | author=Ohgimoto S, Tabata N, Suga S, ''et al.'' |title=Molecular characterization of fusion regulatory protein-1 (FRP-1) that induces multinucleated giant cell formation of monocytes and HIV gp160-mediated cell fusion. FRP-1 and 4F2/CD98 are identical molecules. |journal=J. Immunol. |volume=155 |issue= 7 |pages= 3585-92 |year= 1995 |pmid= 7561057 |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=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=Ohgimoto S, Tabata N, Suga S, ''et al.'' |title=Regulation of human immunodeficiency virus gp160-mediated cell fusion by antibodies against fusion regulatory protein 1. |journal=J. Gen. Virol. |volume=77 ( Pt 11) |issue= |pages= 2747-56 |year= 1996 |pmid= 8922468 |doi= }}
*{{cite journal | author=Courseaux A, Grosgeorge J, Gaudray P, ''et al.'' |title=Definition of the minimal MEN1 candidate area based on a 5-Mb integrated map of proximal 11q13. The European Consortium on Men1, (GENEM 1; Groupe d'Etude des Néoplasies Endocriniennes Multiples de type 1). |journal=Genomics |volume=37 |issue= 3 |pages= 354-65 |year= 1997 |pmid= 8938448 |doi= }}
*{{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=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=Tabata N, Ido M, Suga S, ''et al.'' |title=Protein tyrosine kinase activation provides an early and obligatory signal in anti-FRP-1/CD98/4F2 monoclonal antibody induced cell fusion mediated by HIV gp160. |journal=Med. Microbiol. Immunol. |volume=186 |issue= 2-3 |pages= 115-23 |year= 1998 |pmid= 9403839 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SLC9A1... {November 15, 2007 6:45:30 PM PST}
- SEARCH REDIRECT: Control Box Found: SLC9A1 {November 15, 2007 6:45:57 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 6:45:58 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 6:45:58 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 6:45:58 PM PST}
- UPDATED: Updated protein page: SLC9A1 {November 15, 2007 6:46:04 PM PST}
- INFO: Beginning work on STMN1... {November 15, 2007 6:39:36 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:40:16 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
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| 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 = Stathmin 1/oncoprotein 18
| HGNCid = 6510
| Symbol = STMN1
| AltSymbols =; LAP18; Lag; OP18; PP17; PP19; PR22; SMN
| OMIM = 151442
| ECnumber =
| Homologene = 4063
| MGIid = 96739
| GeneAtlas_image1 = PBB_GE_STMN1_200783_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0015631 |text = tubulin binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005874 |text = microtubule}}
| Process = {{GNF_GO|id=GO:0007019 |text = microtubule depolymerization}} {{GNF_GO|id=GO:0007052 |text = mitotic spindle organization and biogenesis}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3925
| Hs_Ensembl = ENSG00000117632
| Hs_RefseqProtein = NP_005554
| Hs_RefseqmRNA = NM_005563
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 26099180
| Hs_GenLoc_end = 26105955
| Hs_Uniprot = P16949
| Mm_EntrezGene = 16765
| Mm_Ensembl = ENSMUSG00000028832
| Mm_RefseqmRNA = NM_019641
| Mm_RefseqProtein = NP_062615
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 133740475
| Mm_GenLoc_end = 133745914
| Mm_Uniprot = Q545B6
}}
}}
'''Stathmin 1/oncoprotein 18''', also known as '''STMN1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: STMN1 stathmin 1/oncoprotein 18| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3925| 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 belongs to the stathmin family of genes. It encodes a ubiquitous cytosolic phosphoprotein proposed to function as an intracellular relay integrating regulatory signals of the cellular environment. The encoded protein is involved in the regulation of the microtubule filament system by destabilizing microtubules. It prevents assembly and promotes disassembly of microtubules. Alternatively spliced transcript variants encoding the same protein have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: STMN1 stathmin 1/oncoprotein 18| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3925| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Sobel A |title=Stathmin: a relay phosphoprotein for multiple signal transduction? |journal=Trends Biochem. Sci. |volume=16 |issue= 8 |pages= 301-5 |year= 1991 |pmid= 1957351 |doi= }}
*{{cite journal | author=Steinmetz MO |title=Structure and thermodynamics of the tubulin-stathmin interaction. |journal=J. Struct. Biol. |volume=158 |issue= 2 |pages= 137-47 |year= 2007 |pmid= 17029844 |doi= 10.1016/j.jsb.2006.07.018 }}
*{{cite journal | author=Doye V, Le Gouvello S, Dobransky T, ''et al.'' |title=Expression of transfected stathmin cDNA reveals novel phosphorylated forms associated with developmental and functional cell regulation. |journal=Biochem. J. |volume=287 ( Pt 2) |issue= |pages= 549-54 |year= 1992 |pmid= 1445213 |doi= }}
*{{cite journal | author=Labdon JE, Nieves E, Schubart UK |title=Analysis of phosphoprotein p19 by liquid chromatography/mass spectrometry. Identification of two proline-directed serine phosphorylation sites and a blocked amino terminus. |journal=J. Biol. Chem. |volume=267 |issue= 5 |pages= 3506-13 |year= 1992 |pmid= 1737801 |doi= }}
*{{cite journal | author=Melhem RF, Zhu XX, Hailat N, ''et al.'' |title=Characterization of the gene for a proliferation-related phosphoprotein (oncoprotein 18) expressed in high amounts in acute leukemia. |journal=J. Biol. Chem. |volume=266 |issue= 27 |pages= 17747-53 |year= 1991 |pmid= 1917919 |doi= }}
*{{cite journal | author=Ferrari AC, Seuanez HN, Hanash SM, Atweh GF |title=A gene that encodes for a leukemia-associated phosphoprotein (p18) maps to chromosome bands 1p35-36.1. |journal=Genes Chromosomes Cancer |volume=2 |issue= 2 |pages= 125-9 |year= 1991 |pmid= 2278968 |doi= }}
*{{cite journal | author=Maucuer A, Doye V, Sobel A |title=A single amino acid difference distinguishes the human and the rat sequences of stathmin, a ubiquitous intracellular phosphoprotein associated with cell regulations. |journal=FEBS Lett. |volume=264 |issue= 2 |pages= 275-8 |year= 1990 |pmid= 2358074 |doi= }}
*{{cite journal | author=Zhu XX, Kozarsky K, Strahler JR, ''et al.'' |title=Molecular cloning of a novel human leukemia-associated gene. Evidence of conservation in animal species. |journal=J. Biol. Chem. |volume=264 |issue= 24 |pages= 14556-60 |year= 1989 |pmid= 2760073 |doi= }}
*{{cite journal | author=Sobel A, Boutterin MC, Beretta L, ''et al.'' |title=Intracellular substrates for extracellular signaling. Characterization of a ubiquitous, neuron-enriched phosphoprotein (stathmin). |journal=J. Biol. Chem. |volume=264 |issue= 7 |pages= 3765-72 |year= 1989 |pmid= 2917975 |doi= }}
*{{cite journal | author=Maucuer A, Camonis JH, Sobel A |title=Stathmin interaction with a putative kinase and coiled-coil-forming protein domains. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 8 |pages= 3100-4 |year= 1995 |pmid= 7724523 |doi= }}
*{{cite journal | author=Kato S, Sekine S, Oh SW, ''et al.'' |title=Construction of a human full-length cDNA bank. |journal=Gene |volume=150 |issue= 2 |pages= 243-50 |year= 1995 |pmid= 7821789 |doi= }}
*{{cite journal | author=Curmi PA, Maucuer A, Asselin S, ''et al.'' |title=Molecular characterization of human stathmin expressed in Escherichia coli: site-directed mutagenesis of two phosphorylatable serines (Ser-25 and Ser-63). |journal=Biochem. J. |volume=300 ( Pt 2) |issue= |pages= 331-8 |year= 1994 |pmid= 8002936 |doi= }}
*{{cite journal | author=Kumar R, Haugen JD |title=Human and rat osteoblast-like cells express stathmin, a growth-regulatory protein. |journal=Biochem. Biophys. Res. Commun. |volume=201 |issue= 2 |pages= 861-5 |year= 1994 |pmid= 8003023 |doi= 10.1006/bbrc.1994.1780 }}
*{{cite journal | author=Brattsand G, Marklund U, Nylander K, ''et al.'' |title=Cell-cycle-regulated phosphorylation of oncoprotein 18 on Ser16, Ser25 and Ser38. |journal=Eur. J. Biochem. |volume=220 |issue= 2 |pages= 359-68 |year= 1994 |pmid= 8125092 |doi= }}
*{{cite journal | author=Marklund U, Brattsand G, Osterman O, ''et al.'' |title=Multiple signal transduction pathways induce phosphorylation of serines 16, 25, and 38 of oncoprotein 18 in T lymphocytes. |journal=J. Biol. Chem. |volume=268 |issue= 34 |pages= 25671-80 |year= 1994 |pmid= 8245003 |doi= }}
*{{cite journal | author=Marklund U, Brattsand G, Shingler V, Gullberg M |title=Serine 25 of oncoprotein 18 is a major cytosolic target for the mitogen-activated protein kinase. |journal=J. Biol. Chem. |volume=268 |issue= 20 |pages= 15039-47 |year= 1993 |pmid= 8325880 |doi= }}
*{{cite journal | author=Beretta L, Dobránsky T, Sobel A |title=Multiple phosphorylation of stathmin. Identification of four sites phosphorylated in intact cells and in vitro by cyclic AMP-dependent protein kinase and p34cdc2. |journal=J. Biol. Chem. |volume=268 |issue= 27 |pages= 20076-84 |year= 1993 |pmid= 8376365 |doi= }}
*{{cite journal | author=Hosoya H, Ishikawa K, Dohi N, Marunouchi T |title=Transcriptional and post-transcriptional regulation of pr22 (Op18) with proliferation control. |journal=Cell Struct. Funct. |volume=21 |issue= 4 |pages= 237-43 |year= 1997 |pmid= 8906359 |doi= }}
*{{cite journal | author=Larsson N, Marklund U, Gradin HM, ''et al.'' |title=Control of microtubule dynamics by oncoprotein 18: dissection of the regulatory role of multisite phosphorylation during mitosis. |journal=Mol. Cell. Biol. |volume=17 |issue= 9 |pages= 5530-9 |year= 1997 |pmid= 9271428 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TG... {November 15, 2007 6:46:04 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:46:23 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Thyroglobulin
| HGNCid = 11764
| Symbol = TG
| AltSymbols =; AITD3; TGN
| OMIM = 188450
| ECnumber =
| Homologene = 2430
| MGIid = 98733
| Function = {{GNF_GO|id=GO:0004759 |text = carboxylesterase activity}} {{GNF_GO|id=GO:0005179 |text = hormone activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006590 |text = thyroid hormone generation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0042446 |text = hormone biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7038
| Hs_Ensembl = ENSG00000042832
| Hs_RefseqProtein = NP_003226
| Hs_RefseqmRNA = NM_003235
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 133948387
| Hs_GenLoc_end = 134216325
| Hs_Uniprot = P01266
| Mm_EntrezGene = 21819
| Mm_Ensembl = ENSMUSG00000053469
| Mm_RefseqmRNA = NM_009375
| Mm_RefseqProtein = NP_033401
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 66500422
| Mm_GenLoc_end = 66680286
| Mm_Uniprot = Q2NKY1
}}
}}
'''Thyroglobulin''', also known as '''TG''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TG thyroglobulin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7038| 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=Mazzaferri EL, Robbins RJ, Spencer CA, ''et al.'' |title=A consensus report of the role of serum thyroglobulin as a monitoring method for low-risk patients with papillary thyroid carcinoma. |journal=J. Clin. Endocrinol. Metab. |volume=88 |issue= 4 |pages= 1433-41 |year= 2003 |pmid= 12679418 |doi= }}
*{{cite journal | author=Henry M, Zanelli E, Piechaczyk M, ''et al.'' |title=A major human thyroglobulin epitope defined with monoclonal antibodies is mainly recognized by human autoantibodies. |journal=Eur. J. Immunol. |volume=22 |issue= 2 |pages= 315-9 |year= 1992 |pmid= 1371467 |doi= }}
*{{cite journal | author=Targovnik HM, Cochaux P, Corach D, Vassart G |title=Identification of a minor Tg mRNA transcript in RNA from normal and goitrous thyroids. |journal=Mol. Cell. Endocrinol. |volume=84 |issue= 1-2 |pages= R23-6 |year= 1992 |pmid= 1639210 |doi= }}
*{{cite journal | author=Dunn AD, Crutchfield HE, Dunn JT |title=Thyroglobulin processing by thyroidal proteases. Major sites of cleavage by cathepsins B, D, and L. |journal=J. Biol. Chem. |volume=266 |issue= 30 |pages= 20198-204 |year= 1991 |pmid= 1939080 |doi= }}
*{{cite journal | author=Lamas L, Anderson PC, Fox JW, Dunn JT |title=Consensus sequences for early iodination and hormonogenesis in human thyroglobulin. |journal=J. Biol. Chem. |volume=264 |issue= 23 |pages= 13541-5 |year= 1989 |pmid= 2760035 |doi= }}
*{{cite journal | author=Marriq C, Lejeune PJ, Venot N, Vinet L |title=Hormone synthesis in human thyroglobulin: possible cleavage of the polypeptide chain at the tyrosine donor site. |journal=FEBS Lett. |volume=242 |issue= 2 |pages= 414-8 |year= 1989 |pmid= 2914619 |doi= }}
*{{cite journal | author=Christophe D, Cabrer B, Bacolla A, ''et al.'' |title=An unusually long poly(purine)-poly(pyrimidine) sequence is located upstream from the human thyroglobulin gene. |journal=Nucleic Acids Res. |volume=13 |issue= 14 |pages= 5127-44 |year= 1985 |pmid= 2991855 |doi= }}
*{{cite journal | author=Baas F, van Ommen GJ, Bikker H, ''et al.'' |title=The human thyroglobulin gene is over 300 kb long and contains introns of up to 64 kb. |journal=Nucleic Acids Res. |volume=14 |issue= 13 |pages= 5171-86 |year= 1986 |pmid= 3016640 |doi= }}
*{{cite journal | author=Kubak BM, Potempa LA, Anderson B, ''et al.'' |title=Evidence that serum amyloid P component binds to mannose-terminated sequences of polysaccharides and glycoproteins. |journal=Mol. Immunol. |volume=25 |issue= 9 |pages= 851-8 |year= 1989 |pmid= 3211159 |doi= }}
*{{cite journal | author=Malthiéry Y, Lissitzky S |title=Primary structure of human thyroglobulin deduced from the sequence of its 8448-base complementary DNA. |journal=Eur. J. Biochem. |volume=165 |issue= 3 |pages= 491-8 |year= 1987 |pmid= 3595599 |doi= }}
*{{cite journal | author=Parma J, Christophe D, Pohl V, Vassart G |title=Structural organization of the 5' region of the thyroglobulin gene. Evidence for intron loss and "exonization" during evolution. |journal=J. Mol. Biol. |volume=196 |issue= 4 |pages= 769-79 |year= 1988 |pmid= 3681978 |doi= }}
*{{cite journal | author=Bergé-Lefranc JL, Cartouzou G, Mattéi MG, ''et al.'' |title=Localization of the thyroglobulin gene by in situ hybridization to human chromosomes. |journal=Hum. Genet. |volume=69 |issue= 1 |pages= 28-31 |year= 1985 |pmid= 3967888 |doi= }}
*{{cite journal | author=Malthiéry Y, Lissitzky S |title=Sequence of the 5'-end quarter of the human-thyroglobulin messenger ribonucleic acid and of its deduced amino-acid sequence. |journal=Eur. J. Biochem. |volume=147 |issue= 1 |pages= 53-8 |year= 1985 |pmid= 3971976 |doi= }}
*{{cite journal | author=Avvedimento VE, Di Lauro R, Monticelli A, ''et al.'' |title=Mapping of human thyroglobulin gene on the long arm of chromosome 8 by in situ hybridization. |journal=Hum. Genet. |volume=71 |issue= 2 |pages= 163-6 |year= 1985 |pmid= 4043966 |doi= }}
*{{cite journal | author=Xiao S, Pollock HG, Taurog A, Rawitch AB |title=Characterization of hormonogenic sites in an N-terminal, cyanogen bromide fragment of human thyroglobulin. |journal=Arch. Biochem. Biophys. |volume=320 |issue= 1 |pages= 96-105 |year= 1995 |pmid= 7793989 |doi= }}
*{{cite journal | author=Corral J, Martín C, Pérez R, ''et al.'' |title=Thyroglobulin gene point mutation associated with non-endemic simple goitre. |journal=Lancet |volume=341 |issue= 8843 |pages= 462-4 |year= 1993 |pmid= 8094490 |doi= }}
*{{cite journal | author=Gentile F, Salvatore G |title=Preferential sites of proteolytic cleavage of bovine, human and rat thyroglobulin. The use of limited proteolysis to detect solvent-exposed regions of the primary structure. |journal=Eur. J. Biochem. |volume=218 |issue= 2 |pages= 603-21 |year= 1994 |pmid= 8269951 |doi= }}
*{{cite journal | author=Mallet B, Lejeune PJ, Baudry N, ''et al.'' |title=N-glycans modulate in vivo and in vitro thyroid hormone synthesis. Study at the N-terminal domain of thyroglobulin. |journal=J. Biol. Chem. |volume=270 |issue= 50 |pages= 29881-8 |year= 1996 |pmid= 8530385 |doi= }}
*{{cite journal | author=Yang SX, Pollock HG, Rawitch AB |title=Glycosylation in human thyroglobulin: location of the N-linked oligosaccharide units and comparison with bovine thyroglobulin. |journal=Arch. Biochem. Biophys. |volume=327 |issue= 1 |pages= 61-70 |year= 1996 |pmid= 8615697 |doi= 10.1006/abbi.1996.0093 }}
*{{cite journal | author=Molina F, Bouanani M, Pau B, Granier C |title=Characterization of the type-1 repeat from thyroglobulin, a cysteine-rich module found in proteins from different families. |journal=Eur. J. Biochem. |volume=240 |issue= 1 |pages= 125-33 |year= 1996 |pmid= 8797845 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TNFRSF8... {November 15, 2007 6:36:18 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 6:36:45 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Tumor necrosis factor receptor superfamily, member 8
| HGNCid = 11923
| Symbol = TNFRSF8
| AltSymbols =; CD30; D1S166E; KI-1
| OMIM = 153243
| ECnumber =
| Homologene = 949
| MGIid = 99908
| GeneAtlas_image1 = PBB_GE_TNFRSF8_206729_at_tn.png
| Function = {{GNF_GO|id=GO:0004888 |text = transmembrane receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 943
| Hs_Ensembl = ENSG00000120949
| Hs_RefseqProtein = NP_001234
| Hs_RefseqmRNA = NM_001243
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 12046021
| Hs_GenLoc_end = 12126851
| Hs_Uniprot = P28908
| Mm_EntrezGene = 21941
| Mm_Ensembl = ENSMUSG00000028602
| Mm_RefseqmRNA = NM_009401
| Mm_RefseqProtein = NP_033427
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 144535663
| Mm_GenLoc_end = 144581834
| Mm_Uniprot = Q60846
}}
}}
'''Tumor necrosis factor receptor superfamily, member 8''', also known as '''TNFRSF8''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TNFRSF8 tumor necrosis factor receptor superfamily, member 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=943| 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 TNF-receptor superfamily. This receptor is expressed by activated, but not by resting, T and B cells. TRAF2 and TRAF5 can interact with this receptor, and mediate the signal transduction that leads to the activation of NF-kappaB. This receptor is a positive regulator of apoptosis, and also has been shown to limit the proliferative potential of autoreactive CD8 effector T cells and protect the body against autoimmunity. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.<ref name="entrez">{{cite web | title = Entrez Gene: TNFRSF8 tumor necrosis factor receptor superfamily, member 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=943| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schneider C, Hübinger G |title=Pleiotropic signal transduction mediated by human CD30: a member of the tumor necrosis factor receptor (TNFR) family. |journal=Leuk. Lymphoma |volume=43 |issue= 7 |pages= 1355-66 |year= 2003 |pmid= 12389614 |doi= }}
*{{cite journal | author=Horie R, Higashihara M, Watanabe T |title=Hodgkin's lymphoma and CD30 signal transduction. |journal=Int. J. Hematol. |volume=77 |issue= 1 |pages= 37-47 |year= 2003 |pmid= 12568298 |doi= }}
*{{cite journal | author=Tarkowski M |title=Expression and a role of CD30 in regulation of T-cell activity. |journal=Curr. Opin. Hematol. |volume=10 |issue= 4 |pages= 267-71 |year= 2004 |pmid= 12799531 |doi= }}
*{{cite journal | author=Granados S, Hwang ST |title=Roles for CD30 in the biology and treatment of CD30 lymphoproliferative diseases. |journal=J. Invest. Dermatol. |volume=122 |issue= 6 |pages= 1345-7 |year= 2004 |pmid= 15175022 |doi= 10.1111/j.0022-202X.2004.22616.x }}
*{{cite journal | author=Dürkop H, Latza U, Hummel M, ''et al.'' |title=Molecular cloning and expression of a new member of the nerve growth factor receptor family that is characteristic for Hodgkin's disease. |journal=Cell |volume=68 |issue= 3 |pages= 421-7 |year= 1992 |pmid= 1310894 |doi= }}
*{{cite journal | author=Fonatsch C, Latza U, Dürkop H, ''et al.'' |title=Assignment of the human CD30 (Ki-1) gene to 1p36. |journal=Genomics |volume=14 |issue= 3 |pages= 825-6 |year= 1992 |pmid= 1330892 |doi= }}
*{{cite journal | author=Josimovic-Alasevic O, Dürkop H, Schwarting R, ''et al.'' |title=Ki-1 (CD30) antigen is released by Ki-1-positive tumor cells in vitro and in vivo. I. Partial characterization of soluble Ki-1 antigen and detection of the antigen in cell culture supernatants and in serum by an enzyme-linked immunosorbent assay. |journal=Eur. J. Immunol. |volume=19 |issue= 1 |pages= 157-62 |year= 1989 |pmid= 2537734 |doi= }}
*{{cite journal | author=Stein H, Gerdes J, Schwab U, ''et al.'' |title=Identification of Hodgkin and Sternberg-reed cells as a unique cell type derived from a newly-detected small-cell population. |journal=Int. J. Cancer |volume=30 |issue= 4 |pages= 445-59 |year= 1983 |pmid= 6754630 |doi= }}
*{{cite journal | author=Jung W, Krueger S, Renner C, ''et al.'' |title=Opposite effects of the CD30 ligand are not due to CD30 mutations: results from cDNA cloning and sequence comparison of the CD30 antigen from different sources. |journal=Mol. Immunol. |volume=31 |issue= 17 |pages= 1329-34 |year= 1995 |pmid= 7527901 |doi= }}
*{{cite journal | author=Shiota M, Fujimoto J, Semba T, ''et al.'' |title=Hyperphosphorylation of a novel 80 kDa protein-tyrosine kinase similar to Ltk in a human Ki-1 lymphoma cell line, AMS3. |journal=Oncogene |volume=9 |issue= 6 |pages= 1567-74 |year= 1994 |pmid= 8183550 |doi= }}
*{{cite journal | author=Lee SY, Park CG, Choi Y |title=T cell receptor-dependent cell death of T cell hybridomas mediated by the CD30 cytoplasmic domain in association with tumor necrosis factor receptor-associated factors. |journal=J. Exp. Med. |volume=183 |issue= 2 |pages= 669-74 |year= 1996 |pmid= 8627180 |doi= }}
*{{cite journal | author=Gedrich RW, Gilfillan MC, Duckett CS, ''et al.'' |title=CD30 contains two binding sites with different specificities for members of the tumor necrosis factor receptor-associated factor family of signal transducing proteins. |journal=J. Biol. Chem. |volume=271 |issue= 22 |pages= 12852-8 |year= 1996 |pmid= 8662842 |doi= }}
*{{cite journal | author=Horie R, Ito K, Tatewaki M, ''et al.'' |title=A variant CD30 protein lacking extracellular and transmembrane domains is induced in HL-60 by tetradecanoylphorbol acetate and is expressed in alveolar macrophages. |journal=Blood |volume=88 |issue= 7 |pages= 2422-32 |year= 1996 |pmid= 8839832 |doi= }}
*{{cite journal | author=Ansieau S, Scheffrahn I, Mosialos G, ''et al.'' |title=Tumor necrosis factor receptor-associated factor (TRAF)-1, TRAF-2, and TRAF-3 interact in vivo with the CD30 cytoplasmic domain; TRAF-2 mediates CD30-induced nuclear factor kappa B activation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 24 |pages= 14053-8 |year= 1997 |pmid= 8943059 |doi= }}
*{{cite journal | author=Aizawa S, Nakano H, Ishida T, ''et al.'' |title=Tumor necrosis factor receptor-associated factor (TRAF) 5 and TRAF2 are involved in CD30-mediated NFkappaB activation. |journal=J. Biol. Chem. |volume=272 |issue= 4 |pages= 2042-5 |year= 1997 |pmid= 8999898 |doi= }}
*{{cite journal | author=Lee SY, Lee SY, Choi Y |title=TRAF-interacting protein (TRIP): a novel component of the tumor necrosis factor receptor (TNFR)- and CD30-TRAF signaling complexes that inhibits TRAF2-mediated NF-kappaB activation. |journal=J. Exp. Med. |volume=185 |issue= 7 |pages= 1275-85 |year= 1997 |pmid= 9104814 |doi= }}
*{{cite journal | author=Boucher LM, Marengère LE, Lu Y, ''et al.'' |title=Binding sites of cytoplasmic effectors TRAF1, 2, and 3 on CD30 and other members of the TNF receptor superfamily. |journal=Biochem. Biophys. Res. Commun. |volume=233 |issue= 3 |pages= 592-600 |year= 1997 |pmid= 9168896 |doi= 10.1006/bbrc.1997.6509 }}
*{{cite journal | author=Duckett CS, Thompson CB |title=CD30-dependent degradation of TRAF2: implications for negative regulation of TRAF signaling and the control of cell survival. |journal=Genes Dev. |volume=11 |issue= 21 |pages= 2810-21 |year= 1997 |pmid= 9353251 |doi= }}
*{{cite journal | author=Mizushima S, Fujita M, Ishida T, ''et al.'' |title=Cloning and characterization of a cDNA encoding the human homolog of tumor necrosis factor receptor-associated factor 5 (TRAF5). |journal=Gene |volume=207 |issue= 2 |pages= 135-40 |year= 1998 |pmid= 9511754 |doi= }}
*{{cite journal | author=Kurts C, Carbone FR, Krummel MF, ''et al.'' |title=Signalling through CD30 protects against autoimmune diabetes mediated by CD8 T cells. |journal=Nature |volume=398 |issue= 6725 |pages= 341-4 |year= 1999 |pmid= 10192335 |doi= 10.1038/18692 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ZBTB16... {November 15, 2007 6:46:23 PM PST}
- SEARCH REDIRECT: Control Box Found: ZBTB16 {November 15, 2007 6:46:43 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 6:46:44 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 6:46:44 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 6:46:44 PM PST}
- UPDATED: Updated protein page: ZBTB16 {November 15, 2007 6:46:51 PM PST}
end log.
