Jump to content

User:ProteinBoxBot/PBB Log Wiki 11-9-2007-A2-7

From Wikipedia, the free encyclopedia

Log file for Protein Box Bot

[edit]

Log page index: User:ProteinBoxBot/PBB_Log_Index

Protein Status Quick Log - Date: 08:02, 19 November 2007 (UTC)

[edit]

Proteins without matches (6)

[edit]
DFFB FANCG EXT2 ERG CHRNB2
LTB4R

Proteins with a High Potential Match (6)

[edit]
COL5A1 DSG3 FST CYP11B1 DHCR7
ARX

Redirected Proteins (13)

[edit]
RCC1 DDB2 TPH2 DLG3 ADORA3
AKT3 E2F2 DNMT3A CD69 RAPGEF3
GGA3 ETV4 ABI1

Manual Inspection (Page not found) (12)

[edit]
COL5A1 DSG3 FST CYP11B1 DFFB
FANCG DHCR7 EXT2 ERG CHRNB2
LTB4R ARX

Updated (13)

[edit]
RCC1 DDB2 TPH2 DLG3 ADORA3
AKT3 E2F2 DNMT3A CD69 RAPGEF3
GGA3 ETV4 ABI1


Protein Status Grid - Date: 08:02, 19 November 2007 (UTC)

[edit]
HUGO Symbol Action Summary Target page(s) WP Symbol Search
COL5A1 Manual Inspection (Page not found) Other Pages: Collagen (Unknown Data); COL5A1 (Redirect -> Type-V collagen); Type-V collagen (Protein Template); [1]
RCC1 Updated Other Pages: Regulator of chromosome condensation 1 (No Data); RCC1 (Good Codes + Entrez Match); CHC1 (No Data); Chc1 (No Data); RCC1-I (No Data); Rcc1-i (No Data); [2]
DSG3 Manual Inspection (Page not found) Other Pages: Desmoglein 3 (Redirect -> Desmoglein); DSG3 (No Data); CDHF6 (No Data); Cdhf6 (No Data); DKFZp686P23184 (No Data); Dkfzp686p23184 (No Data); PVA (DisAmbig); Pva (No Data); Desmoglein (Protein Template); [3]
DDB2 Updated Other Pages: Damage-specific DNA binding protein 2 (No Data); DDB2 (Good Codes + Entrez Match); FLJ34321 (No Data); Flj34321 (No Data); [4]
FST Manual Inspection (Page not found) Other Pages: Follistatin (Protein Template); FST (DisAmbig); FS (DisAmbig); Fs (Redirect -> FS); [5]
TPH2 Updated Other Pages: Tryptophan hydroxylase 2 (No Data); TPH2 (Good Codes + Entrez Match); FLJ37295 (No Data); Flj37295 (No Data); MGC138871 (No Data); Mgc138871 (No Data); MGC138872 (No Data); Mgc138872 (No Data); NTPH (No Data); Ntph (No Data); [6]
CYP11B1 Manual Inspection (Page not found) Other Pages: Cytochrome P450 (Unknown Data); CYP11B1 (Redirect -> Steroid 11-beta-hydroxylase); CPN1 (No Data); Cpn1 (No Data); CYP11B (No Data); Cyp11b (No Data); DKFZp686B05283 (No Data); Dkfzp686b05283 (No Data); FHI (DisAmbig); Fhi (No Data); FLJ36771 (No Data); Flj36771 (No Data); P450C11 (No Data); P450c11 (No Data); Steroid 11-beta-hydroxylase (Protein Template); [7]
DLG3 Updated Other Pages: Discs (Redirect -> DLG4); DLG3 (Good Codes + Entrez Match); KIAA1232 (No Data); Kiaa1232 (No Data); MRX (Redirect -> ABCG2); Mrx (Redirect -> ABCG2); MRX90 (No Data); Mrx90 (No Data); NE-Dlg (No Data); Ne-dlg (No Data); NEDLG (No Data); Nedlg (No Data); SAP102 (No Data); Sap102 (No Data); DLG4 (Codes Found, but no match[skip]); ABCG2 (Codes Found, but no match[skip]); [8]
DFFB Manual Inspection (Page not found) Other Pages: DNA fragmentation factor (No Data); DFFB (No Data); CAD (Redirect -> Computer-aided design); Cad (Redirect -> CAD (disambiguation)); CPAN (Unknown Data); Cpan (Redirect -> CPAN); DFF-40 (No Data); Dff-40 (No Data); DFF2 (No Data); Dff2 (No Data); DFF40 (No Data); Dff40 (No Data); Computer-aided design (Unknown Data); CAD (disambiguation) (DisAmbig); [9]
FANCG Manual Inspection (Page not found) Other Pages: Fanconi anemia (Unknown Data); FANCG (No Data); FAG (Redirect -> Fag); Fag (DisAmbig); XRCC9 (No Data); Xrcc9 (No Data); [10]
ADORA3 Updated Other Pages: Adenosine A3 receptor (No Data); ADORA3 (Good Codes + Entrez Match); A3AR (No Data); A3ar (No Data); AD026 (No Data); Ad026 (No Data); RP11-552M11.7 (No Data); Rp11-552m11.7 (No Data); BA552M11.5 (No Data); Ba552m11.5 (No Data); [11]
DHCR7 Manual Inspection (Page not found) Other Pages: 7-dehydrocholesterol reductase (Redirect -> 7-Dehydrocholesterol reductase); DHCR7 (Redirect -> 7-Dehydrocholesterol reductase); SLOS (No Data); Slos (No Data); 7-Dehydrocholesterol reductase (Protein Template); [12]
EXT2 Manual Inspection (Page not found) Other Pages: Exostoses 2 (No Data); EXT2 (Redirect -> Ext2); SOTV (No Data); Sotv (No Data); Ext2 (Unknown Data); [13]
ERG Manual Inspection (Page not found) Other Pages: V-ets erythroblastosis virus E26 oncogene homolog (No Data); ERG (Redirect -> Erg (disambiguation)); Erg-3 (No Data); P55 (Redirect -> CD120); Erg (disambiguation) (DisAmbig); CD120 (Codes Found, but no match[skip]); [14]
AKT3 Updated Other Pages: V-akt murine thymoma viral oncogene homolog 3 (No Data); AKT3 (Good Codes + Entrez Match); DKFZP434N0250 (No Data); Dkfzp434n0250 (No Data); PKBG (No Data); Pkbg (No Data); PRKBG (No Data); Prkbg (No Data); RAC-PK-gamma (No Data); Rac-pk-gamma (No Data); RAC-gamma (No Data); Rac-gamma (No Data); STK-2 (No Data); Stk-2 (No Data); [15]
E2F2 Updated Other Pages: E2F transcription factor 2 (No Data); E2F2 (Good Codes + Entrez Match); E2F-2 (No Data); E2f-2 (No Data); [16]
DNMT3A Updated Other Pages: DNA -methyltransferase 3 alpha (No Data); DNMT3A (Good Codes + Entrez Match); DNMT3A2 (No Data); Dnmt3a2 (No Data); M.HsaIIIA (No Data); M.hsaiiia (No Data); [17]
CHRNB2 Manual Inspection (Page not found) Other Pages: Cholinergic receptor (Redirect -> Acetylcholine receptor); CHRNB2 (No Data); EFNL3 (No Data); Efnl3 (No Data); NAChRB2 (No Data); Nachrb2 (No Data); Acetylcholine receptor (Unknown Data); [18]
CD69 Updated Other Pages: CD69 molecule (No Data); CD69 (Good Codes + Entrez Match); CLEC2C (No Data); Clec2c (No Data); [19]
RAPGEF3 Updated Other Pages: Rap guanine nucleotide exchange factor 3 (No Data); RAPGEF3 (Good Codes + Entrez Match); CAMP-GEFI (No Data); Camp-gefi (No Data); EPAC (No Data); Epac (No Data); EPAC1 (No Data); Epac1 (No Data); MGC21410 (No Data); Mgc21410 (No Data); Bcm910 (No Data); [20]
LTB4R Manual Inspection (Page not found) Other Pages: Leukotriene B4 receptor (Redirect -> Eicosanoid receptor); LTB4R (No Data); BLT1 (No Data); Blt1 (No Data); BLTR (No Data); Bltr (No Data); CMKRL1 (No Data); Cmkrl1 (No Data); GPR16 (No Data); Gpr16 (No Data); LTB4R1 (No Data); Ltb4r1 (No Data); LTBR1 (No Data); Ltbr1 (No Data); P2RY7 (No Data); P2ry7 (No Data); P2Y7 (No Data); P2y7 (No Data); Eicosanoid receptor (Unknown Data); [21]
GGA3 Updated Other Pages: Golgi associated (No Data); GGA3 (Good Codes + Entrez Match); KIAA0154 (No Data); Kiaa0154 (No Data); [22]
ETV4 Updated Other Pages: Ets variant gene 4 (No Data); ETV4 (Good Codes + Entrez Match); E1A-F (No Data); E1a-f (No Data); E1AF (No Data); E1af (No Data); PEA3 (No Data); Pea3 (No Data); PEAS3 (No Data); Peas3 (No Data); [23]
ARX Manual Inspection (Page not found) Other Pages: Aristaless related homeobox (Protein Template); ARX (Redirect -> Arx); ISSX (No Data); Issx (No Data); MRX29 (No Data); Mrx29 (No Data); MRX32 (No Data); Mrx32 (No Data); MRX33 (No Data); Mrx33 (No Data); MRX36 (No Data); Mrx36 (No Data); MRX38 (No Data); Mrx38 (No Data); MRX43 (No Data); Mrx43 (No Data); MRX54 (No Data); Mrx54 (No Data); MRXS1 (No Data); Mrxs1 (No Data); PRTS (No Data); Prts (No Data); Arx (DisAmbig); [24]
ABI1 Updated Other Pages: Abl-interactor 1 (No Data); ABI1 (Good Codes + Entrez Match); ABI-1 (No Data); Abi-1 (No Data); E3B1 (No Data); E3b1 (No Data); NAP1BP (No Data); Nap1bp (No Data); SSH3BP (No Data); Ssh3bp (No Data); SSH3BP1 (No Data); Ssh3bp1 (No Data); [25]

Vebose Log - Date: 08:02, 19 November 2007 (UTC)

[edit]
  • INFO: Beginning work on ABI1... {November 18, 2007 11:52:11 PM PST}
  • SEARCH REDIRECT: Control Box Found: ABI1 {November 18, 2007 11:52:49 PM PST}
  • UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:52:52 PM PST}
  • UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:52:52 PM PST}
  • UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:52:52 PM PST}
  • UPDATED: Updated protein page: ABI1 {November 18, 2007 11:52:58 PM PST}
  • INFO: Beginning work on ADORA3... {November 18, 2007 11:39:45 PM PST}
  • SEARCH REDIRECT: Control Box Found: ADORA3 {November 18, 2007 11:40:20 PM PST}
  • UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:40:22 PM PST}
  • UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:40:22 PM PST}
  • UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:40:22 PM PST}
  • UPDATED: Updated protein page: ADORA3 {November 18, 2007 11:40:28 PM PST}
  • INFO: Beginning work on AKT3... {November 18, 2007 11:51:19 PM PST}
  • SEARCH REDIRECT: Control Box Found: AKT3 {November 18, 2007 11:52:03 PM PST}
  • UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:52:05 PM PST}
  • UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:52:05 PM PST}
  • UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:52:05 PM PST}
  • UPDATED: Updated protein page: AKT3 {November 18, 2007 11:52:11 PM PST}
  • INFO: Beginning work on ARX... {November 18, 2007 11:55:14 PM PST}
  • AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:55:59 PM PST}
 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Aristaless related homeobox
 | HGNCid = 18060
 | Symbol = ARX
 | AltSymbols =; ISSX; MRX29; MRX32; MRX33; MRX36; MRX38; MRX43; MRX54; MRXS1; PRTS
 | OMIM = 300382
 | ECnumber =  
 | Homologene = 68998
 | MGIid = 1097716
 | GeneAtlas_image1 = PBB_GE_ARX_gnf1h01283_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_ARX_gnf1h01284_x_at_tn.png
 | Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} 
 | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} 
 | Process = {{GNF_GO|id=GO:0001764 |text = neuron migration}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0030900 |text = forebrain development}} {{GNF_GO|id=GO:0042127 |text = regulation of cell proliferation}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 170302
    | Hs_Ensembl = ENSG00000004848
    | Hs_RefseqProtein = NP_620689
    | Hs_RefseqmRNA = NM_139058
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = X
    | Hs_GenLoc_start = 24931732
    | Hs_GenLoc_end = 24943986
    | Hs_Uniprot = Q96QS3
    | Mm_EntrezGene = 11878
    | Mm_Ensembl = ENSMUSG00000035277
    | Mm_RefseqmRNA = XM_979717
    | Mm_RefseqProtein = XP_984811
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = X
    | Mm_GenLoc_start = 89539365
    | Mm_GenLoc_end = 89551080
    | Mm_Uniprot = O35085
  }}
}}
'''Aristaless related homeobox''', also known as '''ARX''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ARX aristaless related homeobox| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=170302| 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 homeobox-containing gene expressed during development. The expressed protein contains two conserved domains, a C-peptide (or aristaless domain) and the prd-like class homeobox domain. It is a member of the group-II aristaless-related protein family whose members are expressed primarily in the central and/or peripheral nervous system. This gene is thought to be involved in CNS development. Mutations in this gene cause X-linked mental retardation and epilepsy.<ref name="entrez">{{cite web | title = Entrez Gene: ARX aristaless related homeobox| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=170302| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Mulley JC, Kerr B, Stevenson R, Lubs H |title=Nomenclature guidelines for X-linked mental retardation. |journal=Am. J. Med. Genet. |volume=43 |issue= 1-2 |pages= 383-91 |year= 1992 |pmid= 1605216 |doi=  }}
*{{cite journal  | author=Häne B, Schroer RJ, Arena JF, ''et al.'' |title=Nonsyndromic X-linked mental retardation: review and mapping of MRX29 to Xp21. |journal=Clin. Genet. |volume=50 |issue= 4 |pages= 176-83 |year= 1997 |pmid= 9001795 |doi=  }}
*{{cite journal  | author=Suri M |title=The phenotypic spectrum of ARX mutations. |journal=Developmental medicine and child neurology |volume=47 |issue= 2 |pages= 133-7 |year= 2005 |pmid= 15707237 |doi=  }}
*{{cite journal  | author=Partington MW, Mulley JC, Sutherland GR, ''et al.'' |title=X-linked mental retardation with dystonic movements of the hands. |journal=Am. J. Med. Genet. |volume=30 |issue= 1-2 |pages= 251-62 |year= 1988 |pmid= 3177452 |doi=  }}
*{{cite journal  | author=Schutz CK, Ives EJ, Chalifoux M, ''et al.'' |title=Regional localization of an X-linked mental retardation gene to Xp21.1-Xp22.13 (MRX38). |journal=Am. J. Med. Genet. |volume=64 |issue= 1 |pages= 89-96 |year= 1996 |pmid= 8826457 |doi= 10.1002/(SICI)1096-8628(19960712)64:1<89::AID-AJMG16>3.0.CO;2-O }}
*{{cite journal  | author=Holinski-Feder E, Golla A, Rost I, ''et al.'' |title=Regional localization of two MRX genes to Xq28 (MRX28) and to Xp11.4-Xp22.12 (MRX33). |journal=Am. J. Med. Genet. |volume=64 |issue= 1 |pages= 125-30 |year= 1996 |pmid= 8826462 |doi= 10.1002/(SICI)1096-8628(19960712)64:1<125::AID-AJMG21>3.0.CO;2-O }}
*{{cite journal  | author=Claes S, Gu XX, Legius E, ''et al.'' |title=Linkage analysis in three families with nonspecific X-linked mental retardation. |journal=Am. J. Med. Genet. |volume=64 |issue= 1 |pages= 137-46 |year= 1996 |pmid= 8826464 |doi= 10.1002/(SICI)1096-8628(19960712)64:1<137::AID-AJMG24>3.0.CO;2-N }}
*{{cite journal  | author=Jemaa LB, des Portes V, Zemni R, ''et al.'' |title=Refined 2.7 centimorgan locus in Xp21.3-22.1 for a nonspecific X-linked mental retardation gene (MRX54). |journal=Am. J. Med. Genet. |volume=85 |issue= 3 |pages= 276-82 |year= 2000 |pmid= 10398243 |doi=  }}
*{{cite journal  | author=Hamel BC, Smits AP, van den Helm B, ''et al.'' |title=Four families (MRX43, MRX44, MRX45, MRX52) with nonspecific X-linked mental retardation: clinical and psychometric data and results of linkage analysis. |journal=Am. J. Med. Genet. |volume=85 |issue= 3 |pages= 290-304 |year= 2000 |pmid= 10398246 |doi=  }}
*{{cite journal  | author=Blair HJ, Reed V, Gormally E, ''et al.'' |title=Positioning of five genes (CASK, ARX, SAT, IMAGE cDNAs 248928 and 253949) from the human X chromosome short arm with respect to evolutionary breakpoints on the mouse X chromosome. |journal=Mamm. Genome |volume=11 |issue= 8 |pages= 710-2 |year= 2000 |pmid= 10920247 |doi=  }}
*{{cite journal  | author=Strømme P, Mangelsdorf ME, Shaw MA, ''et al.'' |title=Mutations in the human ortholog of Aristaless cause X-linked mental retardation and epilepsy. |journal=Nat. Genet. |volume=30 |issue= 4 |pages= 441-5 |year= 2002 |pmid= 11889467 |doi= 10.1038/ng862 }}
*{{cite journal  | author=Bienvenu T, Poirier K, Friocourt G, ''et al.'' |title=ARX, a novel Prd-class-homeobox gene highly expressed in the telencephalon, is mutated in X-linked mental retardation. |journal=Hum. Mol. Genet. |volume=11 |issue= 8 |pages= 981-91 |year= 2003 |pmid= 11971879 |doi=  }}
*{{cite journal  | author=Strømme P, Mangelsdorf ME, Scheffer IE, Gécz J |title=Infantile spasms, dystonia, and other X-linked phenotypes caused by mutations in Aristaless related homeobox gene, ARX. |journal=Brain Dev. |volume=24 |issue= 5 |pages= 266-8 |year= 2002 |pmid= 12142061 |doi=  }}
*{{cite journal  | author=Scheffer IE, Wallace RH, Phillips FL, ''et al.'' |title=X-linked myoclonic epilepsy with spasticity and intellectual disability: mutation in the homeobox gene ARX. |journal=Neurology |volume=59 |issue= 3 |pages= 348-56 |year= 2002 |pmid= 12177367 |doi=  }}
*{{cite journal  | author=Ohira R, Zhang YH, Guo W, ''et al.'' |title=Human ARX gene: genomic characterization and expression. |journal=Mol. Genet. Metab. |volume=77 |issue= 1-2 |pages= 179-88 |year= 2003 |pmid= 12359145 |doi=  }}
*{{cite journal  | author=Turner G, Partington M, Kerr B, ''et al.'' |title=Variable expression of mental retardation, autism, seizures, and dystonic hand movements in two families with an identical ARX gene mutation. |journal=Am. J. Med. Genet. |volume=112 |issue= 4 |pages= 405-11 |year= 2003 |pmid= 12376946 |doi= 10.1002/ajmg.10714 }}
*{{cite journal  | author=Frints SG, Froyen G, Marynen P, ''et al.'' |title=Re-evaluation of MRX36 family after discovery of an ARX gene mutation reveals mild neurological features of Partington syndrome. |journal=Am. J. Med. Genet. |volume=112 |issue= 4 |pages= 427-8 |year= 2003 |pmid= 12376949 |doi= 10.1002/ajmg.10628 }}
*{{cite journal  | author=Kitamura K, Yanazawa M, Sugiyama N, ''et al.'' |title=Mutation of ARX causes abnormal development of forebrain and testes in mice and X-linked lissencephaly with abnormal genitalia in humans. |journal=Nat. Genet. |volume=32 |issue= 3 |pages= 359-69 |year= 2002 |pmid= 12379852 |doi= 10.1038/ng1009 }}
}}
{{refend}}

{{protein-stub}}
 
  • INFO: Beginning work on CD69... {November 18, 2007 11:40:28 PM PST}
  • SEARCH REDIRECT: Control Box Found: CD69 {November 18, 2007 11:40:52 PM PST}
  • UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:40:53 PM PST}
  • UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:40:53 PM PST}
  • UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:40:53 PM PST}
  • UPDATED: Updated protein page: CD69 {November 18, 2007 11:40:59 PM PST}
  • INFO: Beginning work on CHRNB2... {November 18, 2007 11:41:27 PM PST}
  • AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:42:35 PM PST}
 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Cholinergic receptor, nicotinic, beta 2 (neuronal)
 | HGNCid = 1962
 | Symbol = CHRNB2
 | AltSymbols =; EFNL3; nAChRB2
 | OMIM = 118507
 | ECnumber =  
 | Homologene = 595
 | MGIid = 87891
 | GeneAtlas_image1 = PBB_GE_CHRNB2_206635_at_tn.png
 | Function = {{GNF_GO|id=GO:0004889 |text = nicotinic acetylcholine-activated cation-selective channel activity}} {{GNF_GO|id=GO:0005216 |text = ion channel activity}} {{GNF_GO|id=GO:0005230 |text = extracellular ligand-gated ion channel activity}} {{GNF_GO|id=GO:0015464 |text = acetylcholine receptor activity}} 
 | Component = {{GNF_GO|id=GO:0005892 |text = nicotinic acetylcholine-gated receptor-channel complex}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0045211 |text = postsynaptic membrane}} 
 | Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007600 |text = sensory perception}} {{GNF_GO|id=GO:0007613 |text = memory}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1141
    | Hs_Ensembl = ENSG00000160716
    | Hs_RefseqProtein = NP_000739
    | Hs_RefseqmRNA = NM_000748
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 152806881
    | Hs_GenLoc_end = 152819126
    | Hs_Uniprot = P17787
    | Mm_EntrezGene = 11444
    | Mm_Ensembl = ENSMUSG00000027950
    | Mm_RefseqmRNA = NM_009602
    | Mm_RefseqProtein = NP_033732
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 89839375
    | Mm_GenLoc_end = 89850512
    | Mm_Uniprot = Q61943
  }}
}}
'''Cholinergic receptor, nicotinic, beta 2 (neuronal)''', also known as '''CHRNB2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CHRNB2 cholinergic receptor, nicotinic, beta 2 (neuronal)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1141| 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 = Neuronal acetylcholine receptors are homo- or heteropentameric complexes composed of homologous alpha and beta subunits. They belong to a superfamily of ligand-gated ion channels which allow the flow of sodium and potassium across the plasma membrane in response to ligands such as acetylcholine and nicotine. This gene encodes one of several beta subunits. Mutations in this gene are associated with autosomal dominant nocturnal frontal lobe epilepsy.<ref name="entrez">{{cite web | title = Entrez Gene: CHRNB2 cholinergic receptor, nicotinic, beta 2 (neuronal)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1141| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Skorupska E, Rózycka A, Trzeciak WH |title=[Molecular and genetic basis of idiopathic nocturnal frontal lobe epilepsy] |journal=Neurol. Neurochir. Pol. |volume=36 |issue= 3 |pages= 513-25 |year= 2002 |pmid= 12185808 |doi=  }}
*{{cite journal  | author=Bracci L, Lozzi L, Rustici M, Neri P |title=Binding of HIV-1 gp120 to the nicotinic receptor. |journal=FEBS Lett. |volume=311 |issue= 2 |pages= 115-8 |year= 1992 |pmid= 1397297 |doi=  }}
*{{cite journal  | author=Anand R, Lindstrom J |title=Chromosomal localization of seven neuronal nicotinic acetylcholine receptor subunit genes in humans. |journal=Genomics |volume=13 |issue= 4 |pages= 962-7 |year= 1992 |pmid= 1505988 |doi=  }}
*{{cite journal  | author=Anand R, Lindstrom J |title=Nucleotide sequence of the human nicotinic acetylcholine receptor beta 2 subunit gene. |journal=Nucleic Acids Res. |volume=18 |issue= 14 |pages= 4272 |year= 1990 |pmid= 2377478 |doi=  }}
*{{cite journal  | author=Elliott KJ, Ellis SB, Berckhan KJ, ''et al.'' |title=Comparative structure of human neuronal alpha 2-alpha 7 and beta 2-beta 4 nicotinic acetylcholine receptor subunits and functional expression of the alpha 2, alpha 3, alpha 4, alpha 7, beta 2, and beta 4 subunits. |journal=J. Mol. Neurosci. |volume=7 |issue= 3 |pages= 217-28 |year= 1997 |pmid= 8906617 |doi=  }}
*{{cite journal  | author=Groot Kormelink PJ, Luyten WH |title=Cloning and sequence of full-length cDNAs encoding the human neuronal nicotinic acetylcholine receptor (nAChR) subunits beta3 and beta4 and expression of seven nAChR subunits in the human neuroblastoma cell line SH-SY5Y and/or IMR-32. |journal=FEBS Lett. |volume=400 |issue= 3 |pages= 309-14 |year= 1997 |pmid= 9009220 |doi=  }}
*{{cite journal  | author=Rempel N, Heyers S, Engels H, ''et al.'' |title=The structures of the human neuronal nicotinic acetylcholine receptor beta2- and alpha3-subunit genes (CHRNB2 and CHRNA3). |journal=Hum. Genet. |volume=103 |issue= 6 |pages= 645-53 |year= 1999 |pmid= 9921897 |doi=  }}
*{{cite journal  | author=Lueders KK, Elliott RW, Marenholz I, ''et al.'' |title=Genomic organization and mapping of the human and mouse neuronal beta2-nicotinic acetylcholine receptor genes. |journal=Mamm. Genome |volume=10 |issue= 9 |pages= 900-5 |year= 1999 |pmid= 10441742 |doi=  }}
*{{cite journal  | author=Steinlein OK |title=Neuronal nicotinic receptors in human epilepsy. |journal=Eur. J. Pharmacol. |volume=393 |issue= 1-3 |pages= 243-7 |year= 2000 |pmid= 10771020 |doi=  }}
*{{cite journal  | author=De Fusco M, Becchetti A, Patrignani A, ''et al.'' |title=The nicotinic receptor beta 2 subunit is mutant in nocturnal frontal lobe epilepsy. |journal=Nat. Genet. |volume=26 |issue= 3 |pages= 275-6 |year= 2000 |pmid= 11062464 |doi= 10.1038/81566 }}
*{{cite journal  | author=Phillips HA, Favre I, Kirkpatrick M, ''et al.'' |title=CHRNB2 is the second acetylcholine receptor subunit associated with autosomal dominant nocturnal frontal lobe epilepsy. |journal=Am. J. Hum. Genet. |volume=68 |issue= 1 |pages= 225-31 |year= 2001 |pmid= 11104662 |doi=  }}
*{{cite journal  | author=Samochocki M, Zerlin M, Jostock R, ''et al.'' |title=Galantamine is an allosterically potentiating ligand of the human alpha4/beta2 nAChR. |journal=Acta Neurol. Scand., Suppl. |volume=176 |issue=  |pages= 68-73 |year= 2001 |pmid= 11261808 |doi=  }}
*{{cite journal  | author=Engidawork E, Gulesserian T, Balic N, ''et al.'' |title=Changes in nicotinic acetylcholine receptor subunits expression in brain of patients with Down syndrome and Alzheimer's disease. |journal=J. Neural Transm. Suppl. |volume= |issue= 61 |pages= 211-22 |year= 2002 |pmid= 11771745 |doi=  }}
*{{cite journal  | author=Lueders KK, Hu S, McHugh L, ''et al.'' |title=Genetic and functional analysis of single nucleotide polymorphisms in the beta2-neuronal nicotinic acetylcholine receptor gene (CHRNB2). |journal=Nicotine Tob. Res. |volume=4 |issue= 1 |pages= 115-25 |year= 2002 |pmid= 11906688 |doi= 10.1080/14622200110098419 }}
*{{cite journal  | author=Duga S, Asselta R, Bonati MT, ''et al.'' |title=Mutational analysis of nicotinic acetylcholine receptor beta2 subunit gene (CHRNB2) in a representative cohort of Italian probands affected by autosomal dominant nocturnal frontal lobe epilepsy. |journal=Epilepsia |volume=43 |issue= 4 |pages= 362-4 |year= 2002 |pmid= 11952766 |doi=  }}
*{{cite journal  | author=Heeschen C, Weis M, Aicher A, ''et al.'' |title=A novel angiogenic pathway mediated by non-neuronal nicotinic acetylcholine receptors. |journal=J. Clin. Invest. |volume=110 |issue= 4 |pages= 527-36 |year= 2002 |pmid= 12189247 |doi=  }}
*{{cite journal  | author=Lin L, Jeanclos EM, Treuil M, ''et al.'' |title=The calcium sensor protein visinin-like protein-1 modulates the surface expression and agonist sensitivity of the alpha 4beta 2 nicotinic acetylcholine receptor. |journal=J. Biol. Chem. |volume=277 |issue= 44 |pages= 41872-8 |year= 2003 |pmid= 12202488 |doi= 10.1074/jbc.M206857200 }}
*{{cite journal  | author=Kawamata J, Shimohama S |title=Association of novel and established polymorphisms in neuronal nicotinic acetylcholine receptors with sporadic Alzheimer's disease. |journal=J. Alzheimers Dis. |volume=4 |issue= 2 |pages= 71-6 |year= 2002 |pmid= 12214130 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}

{{protein-stub}}
 
  • INFO: Beginning work on COL5A1... {November 18, 2007 11:43:14 PM PST}
  • AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:43:35 PM PST}
 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Collagen, type V, alpha 1
 | HGNCid = 2209
 | Symbol = COL5A1
 | AltSymbols =; 
 | OMIM = 120215
 | ECnumber =  
 | Homologene = 55434
 | MGIid = 88457
 | GeneAtlas_image1 = PBB_GE_COL5A1_203325_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_COL5A1_212488_at_tn.png
 | GeneAtlas_image3 = PBB_GE_COL5A1_212489_at_tn.png
 | Function = {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005201 |text = extracellular matrix structural constituent}} {{GNF_GO|id=GO:0008201 |text = heparin binding}} 
 | Component = {{GNF_GO|id=GO:0005581 |text = collagen}} {{GNF_GO|id=GO:0005588 |text = collagen type V}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} 
 | Process = {{GNF_GO|id=GO:0006817 |text = phosphate transport}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1289
    | Hs_Ensembl = ENSG00000130635
    | Hs_RefseqProtein = NP_000084
    | Hs_RefseqmRNA = NM_000093
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 9
    | Hs_GenLoc_start = 136673473
    | Hs_GenLoc_end = 136876507
    | Hs_Uniprot = P20908
    | Mm_EntrezGene = 12831
    | Mm_Ensembl = ENSMUSG00000026837
    | Mm_RefseqmRNA = NM_015734
    | Mm_RefseqProtein = NP_056549
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 27708694
    | Mm_GenLoc_end = 27861166
    | Mm_Uniprot = Q6F6B0
  }}
}}
'''Collagen, type V, alpha 1''', also known as '''COL5A1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: COL5A1 collagen, type V, alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1289| 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 chain for one of the low abundance fibrillar collagens. Fibrillar collagen molecules are trimers that can be composed of one or more types of alpha chains. Type V collagen is found in tissues containing type I collagen and appears to regulate the assembly of heterotypic fibers composed of both type I and type V collagen. This gene product is closely related to type XI collagen and it is possible that the collagen chains of types V and XI constitute a single collagen type with tissue-specific chain combinations. Mutations in this gene are associated with Ehlers-Danlos syndrome, types I and II.<ref name="entrez">{{cite web | title = Entrez Gene: COL5A1 collagen, type V, alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1289| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Mann K |title=Isolation of the alpha 3-chain of human type V collagen and characterization by partial sequencing. |journal=Biol. Chem. Hoppe-Seyler |volume=373 |issue= 2 |pages= 69-75 |year= 1992 |pmid= 1571108 |doi=  }}
*{{cite journal  | author=Greenspan DS, Byers MG, Eddy RL, ''et al.'' |title=Human collagen gene COL5A1 maps to the q34.2----q34.3 region of chromosome 9, near the locus for nail-patella syndrome. |journal=Genomics |volume=12 |issue= 4 |pages= 836-7 |year= 1992 |pmid= 1572660 |doi=  }}
*{{cite journal  | author=Greenspan DS, Cheng W, Hoffman GG |title=The pro-alpha 1(V) collagen chain. Complete primary structure, distribution of expression, and comparison with the pro-alpha 1(XI) collagen chain. |journal=J. Biol. Chem. |volume=266 |issue= 36 |pages= 24727-33 |year= 1992 |pmid= 1722213 |doi=  }}
*{{cite journal  | author=Takahara K, Sato Y, Okazawa K, ''et al.'' |title=Complete primary structure of human collagen alpha 1 (V) chain. |journal=J. Biol. Chem. |volume=266 |issue= 20 |pages= 13124-9 |year= 1991 |pmid= 2071595 |doi=  }}
*{{cite journal  | author=Yaoi Y, Hashimoto K, Koitabashi H, ''et al.'' |title=Primary structure of the heparin-binding site of type V collagen. |journal=Biochim. Biophys. Acta |volume=1035 |issue= 2 |pages= 139-45 |year= 1990 |pmid= 2203476 |doi=  }}
*{{cite journal  | author=Seyer JM, Kang AH |title=Covalent structure of collagen: amino acid sequence of three cyanogen bromide-derived peptides from human alpha 1(V) collagen chain. |journal=Arch. Biochem. Biophys. |volume=271 |issue= 1 |pages= 120-9 |year= 1989 |pmid= 2496661 |doi=  }}
*{{cite journal  | author=Niyibizi C, Fietzek PP, van der Rest M |title=Human placenta type V collagens. Evidence for the existence of an alpha 1(V) alpha 2(V) alpha 3(V) collagen molecule. |journal=J. Biol. Chem. |volume=259 |issue= 22 |pages= 14170-4 |year= 1984 |pmid= 6501291 |doi=  }}
*{{cite journal  | author=Mumby SM, Raugi GJ, Bornstein P |title=Interactions of thrombospondin with extracellular matrix proteins: selective binding to type V collagen. |journal=J. Cell Biol. |volume=98 |issue= 2 |pages= 646-52 |year= 1984 |pmid= 6693501 |doi=  }}
*{{cite journal  | author=Rhodes RK, Miller EJ |title=Evidence for the existence of an alpha 1(V) alpha 2(V) alpha 3(V) collagen molecule in human placental tissue. |journal=Coll. Relat. Res. |volume=1 |issue= 4 |pages= 337-43 |year= 1982 |pmid= 7346227 |doi=  }}
*{{cite journal  | author=Lee S, Greenspan DS |title=Transcriptional promoter of the human alpha 1(V) collagen gene (COL5A1). |journal=Biochem. J. |volume=310 ( Pt 1) |issue=  |pages= 15-22 |year= 1995 |pmid= 7646438 |doi=  }}
*{{cite journal  | author=Moradi-Améli M, Rousseau JC, Kleman JP, ''et al.'' |title=Diversity in the processing events at the N-terminus of type-V collagen. |journal=Eur. J. Biochem. |volume=221 |issue= 3 |pages= 987-95 |year= 1994 |pmid= 8181482 |doi=  }}
*{{cite journal  | author=Takahara K, Hoffman GG, Greenspan DS |title=Complete structural organization of the human alpha 1 (V) collagen gene (COL5A1): divergence from the conserved organization of other characterized fibrillar collagen genes. |journal=Genomics |volume=29 |issue= 3 |pages= 588-97 |year= 1996 |pmid= 8575750 |doi= 10.1006/geno.1995.9961 }}
*{{cite journal  | author=De Paepe A, Nuytinck L, Hausser I, ''et al.'' |title=Mutations in the COL5A1 gene are causal in the Ehlers-Danlos syndromes I and II. |journal=Am. J. Hum. Genet. |volume=60 |issue= 3 |pages= 547-54 |year= 1997 |pmid= 9042913 |doi=  }}
*{{cite journal  | author=Tillet E, Ruggiero F, Nishiyama A, Stallcup WB |title=The membrane-spanning proteoglycan NG2 binds to collagens V and VI through the central nonglobular domain of its core protein. |journal=J. Biol. Chem. |volume=272 |issue= 16 |pages= 10769-76 |year= 1997 |pmid= 9099729 |doi=  }}
*{{cite journal  | author=Sasaki T, Brakebusch C, Engel J, Timpl R |title=Mac-2 binding protein is a cell-adhesive protein of the extracellular matrix which self-assembles into ring-like structures and binds beta1 integrins, collagens and fibronectin. |journal=EMBO J. |volume=17 |issue= 6 |pages= 1606-13 |year= 1998 |pmid= 9501082 |doi= 10.1093/emboj/17.6.1606 }}
*{{cite journal  | author=Wu YL, Sumiyoshi H, Khaleduzzaman M, ''et al.'' |title=cDNA sequence and expression of the mouse alpha1(V) collagen gene (Col5a1). |journal=Biochim. Biophys. Acta |volume=1397 |issue= 3 |pages= 275-84 |year= 1998 |pmid= 9582436 |doi=  }}
*{{cite journal  | author=Burrows NP, Nicholls AC, Richards AJ, ''et al.'' |title=A point mutation in an intronic branch site results in aberrant splicing of COL5A1 and in Ehlers-Danlos syndrome type II in two British families. |journal=Am. J. Hum. Genet. |volume=63 |issue= 2 |pages= 390-8 |year= 1998 |pmid= 9683580 |doi=  }}
*{{cite journal  | author=Aho S, Uitto J |title=Two-hybrid analysis reveals multiple direct interactions for thrombospondin 1. |journal=Matrix Biol. |volume=17 |issue= 6 |pages= 401-12 |year= 1999 |pmid= 9840442 |doi=  }}
*{{cite journal  | author=Giunta C, Steinmann B |title=Compound heterozygosity for a disease-causing G1489E [correction of G1489D] and disease-modifying G530S substitution in COL5A1 of a patient with the classical type of Ehlers-Danlos syndrome: an explanation of intrafamilial variability? |journal=Am. J. Med. Genet. |volume=90 |issue= 1 |pages= 72-9 |year= 2000 |pmid= 10602121 |doi=  }}
*{{cite journal  | author=Imamura Y, Scott IC, Greenspan DS |title=The pro-alpha3(V) collagen chain. Complete primary structure, expression domains in adult and developing tissues, and comparison to the structures and expression domains of the other types V and XI procollagen chains. |journal=J. Biol. Chem. |volume=275 |issue= 12 |pages= 8749-59 |year= 2000 |pmid= 10722718 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 
  • INFO: Beginning work on CYP11B1... {November 18, 2007 11:43:35 PM PST}
  • AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:44:23 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 = Cytochrome P450, family 11, subfamily B, polypeptide 1
 | HGNCid = 2591
 | Symbol = CYP11B1
 | AltSymbols =; CPN1; CYP11B; DKFZp686B05283; FHI; FLJ36771; P450C11
 | OMIM = 610613
 | ECnumber =  
 | Homologene = 88331
 | MGIid = 88584
 | GeneAtlas_image1 = PBB_GE_CYP11B1_214610_at_tn.png
 | Function = {{GNF_GO|id=GO:0004497 |text = monooxygenase activity}} {{GNF_GO|id=GO:0004507 |text = steroid 11-beta-monooxygenase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} 
 | Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}} 
 | Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006700 |text = C21-steroid hormone biosynthetic process}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1584
    | Hs_Ensembl = ENSG00000160882
    | Hs_RefseqProtein = NP_000488
    | Hs_RefseqmRNA = NM_000497
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 8
    | Hs_GenLoc_start = 143950780
    | Hs_GenLoc_end = 143958238
    | Hs_Uniprot = P15538
    | Mm_EntrezGene = 13072
    | Mm_Ensembl = ENSMUSG00000022589
    | Mm_RefseqmRNA = NM_009991
    | Mm_RefseqProtein = NP_034121
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 15
    | Mm_GenLoc_start = 74678294
    | Mm_GenLoc_end = 74683480
    | Mm_Uniprot = Q14AB5
  }}
}}
'''Cytochrome P450, family 11, subfamily B, polypeptide 1''', also known as '''CYP11B1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CYP11B1 cytochrome P450, family 11, subfamily B, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1584| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the mitochondrial inner membrane and is involved in the conversion of progesterone to cortisol in the adrenal cortex. Mutations in this gene cause congenital adrenal hyperplasia due to 11-beta-hydroxylase deficiency. Transcript variants encoding different isoforms have been noted for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: CYP11B1 cytochrome P450, family 11, subfamily B, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1584| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Helmberg A |title=Twin genes and endocrine disease: CYP21 and CYP11B genes. |journal=Acta Endocrinol. |volume=129 |issue= 2 |pages= 97-108 |year= 1993 |pmid= 8372604 |doi=  }}
*{{cite journal  | author=Stowasser M, Gunasekera TG, Gordon RD |title=Familial varieties of primary aldosteronism. |journal=Clin. Exp. Pharmacol. Physiol. |volume=28 |issue= 12 |pages= 1087-90 |year= 2002 |pmid= 11903322 |doi=  }}
*{{cite journal  | author=Lifton RP, Dluhy RG, Powers M, ''et al.'' |title=Hereditary hypertension caused by chimaeric gene duplications and ectopic expression of aldosterone synthase. |journal=Nat. Genet. |volume=2 |issue= 1 |pages= 66-74 |year= 1993 |pmid= 1303253 |doi= 10.1038/ng0992-66 }}
*{{cite journal  | author=Helmberg A, Ausserer B, Kofler R |title=Frame shift by insertion of 2 basepairs in codon 394 of CYP11B1 causes congenital adrenal hyperplasia due to steroid 11 beta-hydroxylase deficiency. |journal=J. Clin. Endocrinol. Metab. |volume=75 |issue= 5 |pages= 1278-81 |year= 1992 |pmid= 1430088 |doi=  }}
*{{cite journal  | author=Pascoe L, Curnow KM, Slutsker L, ''et al.'' |title=Glucocorticoid-suppressible hyperaldosteronism results from hybrid genes created by unequal crossovers between CYP11B1 and CYP11B2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 17 |pages= 8327-31 |year= 1992 |pmid= 1518866 |doi=  }}
*{{cite journal  | author=Kawamoto T, Mitsuuchi Y, Toda K, ''et al.'' |title=Role of steroid 11 beta-hydroxylase and steroid 18-hydroxylase in the biosynthesis of glucocorticoids and mineralocorticoids in humans. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 4 |pages= 1458-62 |year= 1992 |pmid= 1741400 |doi=  }}
*{{cite journal  | author=White PC, Dupont J, New MI, ''et al.'' |title=A mutation in CYP11B1 (Arg-448----His) associated with steroid 11 beta-hydroxylase deficiency in Jews of Moroccan origin. |journal=J. Clin. Invest. |volume=87 |issue= 5 |pages= 1664-7 |year= 1991 |pmid= 2022736 |doi=  }}
*{{cite journal  | author=Kawamoto T, Mitsuuchi Y, Toda K, ''et al.'' |title=Cloning of cDNA and genomic DNA for human cytochrome P-45011 beta. |journal=FEBS Lett. |volume=269 |issue= 2 |pages= 345-9 |year= 1990 |pmid= 2401360 |doi=  }}
*{{cite journal  | author=Mornet E, Dupont J, Vitek A, White PC |title=Characterization of two genes encoding human steroid 11 beta-hydroxylase (P-450(11) beta). |journal=J. Biol. Chem. |volume=264 |issue= 35 |pages= 20961-7 |year= 1990 |pmid= 2592361 |doi=  }}
*{{cite journal  | author=Chua SC, Szabo P, Vitek A, ''et al.'' |title=Cloning of cDNA encoding steroid 11 beta-hydroxylase (P450c11). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 20 |pages= 7193-7 |year= 1987 |pmid= 3499608 |doi=  }}
*{{cite journal  | author=Naiki Y, Kawamoto T, Mitsuuchi Y, ''et al.'' |title=A nonsense mutation (TGG [Trp116]-->TAG [Stop]) in CYP11B1 causes steroid 11 beta-hydroxylase deficiency. |journal=J. Clin. Endocrinol. Metab. |volume=77 |issue= 6 |pages= 1677-82 |year= 1994 |pmid= 7903314 |doi=  }}
*{{cite journal  | author=Joehrer K, Geley S, Strasser-Wozak EM, ''et al.'' |title=CYP11B1 mutations causing non-classic adrenal hyperplasia due to 11 beta-hydroxylase deficiency. |journal=Hum. Mol. Genet. |volume=6 |issue= 11 |pages= 1829-34 |year= 1998 |pmid= 9302260 |doi=  }}
*{{cite journal  | author=Cargill M, Altshuler D, Ireland J, ''et al.'' |title=Characterization of single-nucleotide polymorphisms in coding regions of human genes. |journal=Nat. Genet. |volume=22 |issue= 3 |pages= 231-8 |year= 1999 |pmid= 10391209 |doi= 10.1038/10290 }}
*{{cite journal  | author=Halushka MK, Fan JB, Bentley K, ''et al.'' |title=Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. |journal=Nat. Genet. |volume=22 |issue= 3 |pages= 239-47 |year= 1999 |pmid= 10391210 |doi= 10.1038/10297 }}
*{{cite journal  | author=Cao PR, Bernhardt R |title=Interaction of CYP11B1 (cytochrome P-45011 beta) with CYP11A1 (cytochrome P-450scc) in COS-1 cells. |journal=Eur. J. Biochem. |volume=262 |issue= 3 |pages= 720-6 |year= 1999 |pmid= 10411633 |doi=  }}
*{{cite journal  | author=Loidi L, Quinteiro C, Barros F, ''et al.'' |title=The C494F variant in the CYP11B1 gene is a sequence polymorphism in the Spanish population. |journal=J. Clin. Endocrinol. Metab. |volume=84 |issue= 12 |pages= 4749 |year= 2000 |pmid= 10599751 |doi=  }}
*{{cite journal  | author=Chabre O, Portrat-Doyen S, Chaffanjon P, ''et al.'' |title=Bilateral laparoscopic adrenalectomy for congenital adrenal hyperplasia with severe hypertension, resulting from two novel mutations in splice donor sites of CYP11B1. |journal=J. Clin. Endocrinol. Metab. |volume=85 |issue= 11 |pages= 4060-8 |year= 2000 |pmid= 11095433 |doi=  }}
*{{cite journal  | author=Fisher A, Friel EC, Bernhardt R, ''et al.'' |title=Effects of 18-hydroxylated steroids on corticosteroid production by human aldosterone synthase and 11beta-hydroxylase. |journal=J. Clin. Endocrinol. Metab. |volume=86 |issue= 9 |pages= 4326-9 |year= 2001 |pmid= 11549669 |doi=  }}
*{{cite journal  | author=Hampf M, Dao NT, Hoan NT, Bernhardt R |title=Unequal crossing-over between aldosterone synthase and 11beta-hydroxylase genes causes congenital adrenal hyperplasia. |journal=J. Clin. Endocrinol. Metab. |volume=86 |issue= 9 |pages= 4445-52 |year= 2001 |pmid= 11549691 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 
  • INFO: Beginning work on DDB2... {November 18, 2007 11:44:23 PM PST}
  • SEARCH REDIRECT: Control Box Found: DDB2 {November 18, 2007 11:44:46 PM PST}
  • UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:44:48 PM PST}
  • UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:44:48 PM PST}
  • UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:44:48 PM PST}
  • UPDATED: Updated protein page: DDB2 {November 18, 2007 11:44:55 PM PST}
  • INFO: Beginning work on DFFB... {November 18, 2007 11:44:55 PM PST}
  • AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:45:31 PM PST}
 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_DFFB_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ibx.
 | PDB = {{PDB2|1ibx}}
 | Name = DNA fragmentation factor, 40kDa, beta polypeptide (caspase-activated DNase)
 | HGNCid = 2773
 | Symbol = DFFB
 | AltSymbols =; CAD; CPAN; DFF-40; DFF2; DFF40
 | OMIM = 601883
 | ECnumber =  
 | Homologene = 3241
 | MGIid = 1196287
 | GeneAtlas_image1 = PBB_GE_DFFB_206752_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0004516 |text = nicotinate phosphoribosyltransferase activity}} {{GNF_GO|id=GO:0004518 |text = nuclease activity}} {{GNF_GO|id=GO:0004537 |text = caspase-activated deoxyribonuclease activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0019899 |text = enzyme binding}} 
 | Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005829 |text = cytosol}} 
 | Process = {{GNF_GO|id=GO:0006309 |text = DNA fragmentation during apoptosis}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0030263 |text = apoptotic chromosome condensation}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1677
    | Hs_Ensembl = ENSG00000169598
    | Hs_RefseqProtein = NP_001004285
    | Hs_RefseqmRNA = NM_001004285
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 3763705
    | Hs_GenLoc_end = 3791853
    | Hs_Uniprot = O76075
    | Mm_EntrezGene = 13368
    | Mm_Ensembl = ENSMUSG00000029027
    | Mm_RefseqmRNA = NM_007859
    | Mm_RefseqProtein = NP_031885
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 152808255
    | Mm_GenLoc_end = 152818926
    | Mm_Uniprot = Q7TS81
  }}
}}
'''DNA fragmentation factor, 40kDa, beta polypeptide (caspase-activated DNase)''', also known as '''DFFB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DFFB DNA fragmentation factor, 40kDa, beta polypeptide (caspase-activated DNase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1677| 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 = Apoptosis is a cell death process that removes toxic and/or useless cells during mammalian development. The apoptotic process is accompanied by shrinkage and fragmentation of the cells and nuclei and degradation of the chromosomal DNA into nucleosomal units. DNA fragmentation factor (DFF) is a heterodimeric protein of 40-kD (DFFB) and 45-kD (DFFA) subunits. DFFA is the substrate for caspase-3 and triggers DNA fragmentation during apoptosis. DFF becomes activated when DFFA is cleaved by caspase-3. The cleaved fragments of DFFA dissociate from DFFB, the active component of DFF. DFFB has been found to trigger both DNA fragmentation and chromatin condensation during apoptosis. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for this gene, but the biological validity of some variants has not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: DFFB DNA fragmentation factor, 40kDa, beta polypeptide (caspase-activated DNase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1677| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Liu X, Zou H, Slaughter C, Wang X |title=DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. |journal=Cell |volume=89 |issue= 2 |pages= 175-84 |year= 1997 |pmid= 9108473 |doi=  }}
*{{cite journal  | author=Enari M, Sakahira H, Yokoyama H, ''et al.'' |title=A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. |journal=Nature |volume=391 |issue= 6662 |pages= 43-50 |year= 1998 |pmid= 9422506 |doi= 10.1038/34112 }}
*{{cite journal  | author=Halenbeck R, MacDonald H, Roulston A, ''et al.'' |title=CPAN, a human nuclease regulated by the caspase-sensitive inhibitor DFF45. |journal=Curr. Biol. |volume=8 |issue= 9 |pages= 537-40 |year= 1998 |pmid= 9560346 |doi=  }}
*{{cite journal  | author=Liu X, Li P, Widlak P, ''et al.'' |title=The 40-kDa subunit of DNA fragmentation factor induces DNA fragmentation and chromatin condensation during apoptosis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 15 |pages= 8461-6 |year= 1998 |pmid= 9671700 |doi=  }}
*{{cite journal  | author=Mukae N, Enari M, Sakahira H, ''et al.'' |title=Molecular cloning and characterization of human caspase-activated DNase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 16 |pages= 9123-8 |year= 1998 |pmid= 9689044 |doi=  }}
*{{cite journal  | author=Gu J, Dong RP, Zhang C, ''et al.'' |title=Functional interaction of DFF35 and DFF45 with caspase-activated DNA fragmentation nuclease DFF40. |journal=J. Biol. Chem. |volume=274 |issue= 30 |pages= 20759-62 |year= 1999 |pmid= 10409614 |doi=  }}
*{{cite journal  | author=McCarty JS, Toh SY, Li P |title=Study of DFF45 in its role of chaperone and inhibitor: two independent inhibitory domains of DFF40 nuclease activity. |journal=Biochem. Biophys. Res. Commun. |volume=264 |issue= 1 |pages= 176-80 |year= 1999 |pmid= 10527860 |doi= 10.1006/bbrc.1999.1497 }}
*{{cite journal  | author=McCarty JS, Toh SY, Li P |title=Multiple domains of DFF45 bind synergistically to DFF40: roles of caspase cleavage and sequestration of activator domain of DFF40. |journal=Biochem. Biophys. Res. Commun. |volume=264 |issue= 1 |pages= 181-5 |year= 1999 |pmid= 10527861 |doi= 10.1006/bbrc.1999.1498 }}
*{{cite journal  | author=Lugovskoy AA, Zhou P, Chou JJ, ''et al.'' |title=Solution structure of the CIDE-N domain of CIDE-B and a model for CIDE-N/CIDE-N interactions in the DNA fragmentation pathway of apoptosis. |journal=Cell |volume=99 |issue= 7 |pages= 747-55 |year= 2000 |pmid= 10619428 |doi=  }}
*{{cite journal  | author=Judson H, van Roy N, Strain L, ''et al.'' |title=Structure and mutation analysis of the gene encoding DNA fragmentation factor 40 (caspase-activated nuclease), a candidate neuroblastoma tumour suppressor gene. |journal=Hum. Genet. |volume=106 |issue= 4 |pages= 406-13 |year= 2000 |pmid= 10830907 |doi=  }}
*{{cite journal  | author=Otomo T, Sakahira H, Uegaki K, ''et al.'' |title=Structure of the heterodimeric complex between CAD domains of CAD and ICAD. |journal=Nat. Struct. Biol. |volume=7 |issue= 8 |pages= 658-62 |year= 2000 |pmid= 10932250 |doi= 10.1038/77957 }}
*{{cite journal  | author=Durrieu F, Samejima K, Fortune JM, ''et al.'' |title=DNA topoisomerase IIalpha interacts with CAD nuclease and is involved in chromatin condensation during apoptotic execution. |journal=Curr. Biol. |volume=10 |issue= 15 |pages= 923-6 |year= 2001 |pmid= 10959840 |doi=  }}
*{{cite journal  | author=Zhou P, Lugovskoy AA, McCarty JS, ''et al.'' |title=Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 11 |pages= 6051-5 |year= 2001 |pmid= 11371636 |doi= 10.1073/pnas.111145098 }}
*{{cite journal  | author=Nie Z, Phenix BN, Lum JJ, ''et al.'' |title=HIV-1 protease processes procaspase 8 to cause mitochondrial release of cytochrome c, caspase cleavage and nuclear fragmentation. |journal=Cell Death Differ. |volume=9 |issue= 11 |pages= 1172-84 |year= 2003 |pmid= 12404116 |doi= 10.1038/sj.cdd.4401094 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Hsieh SY, Liaw SF, Lee SN, ''et al.'' |title=Aberrant caspase-activated DNase (CAD) transcripts in human hepatoma cells. |journal=Br. J. Cancer |volume=88 |issue= 2 |pages= 210-6 |year= 2003 |pmid= 12610505 |doi= 10.1038/sj.bjc.6600695 }}
*{{cite journal  | author=Liu QL, Kishi H, Ohtsuka K, Muraguchi A |title=Heat shock protein 70 binds caspase-activated DNase and enhances its activity in TCR-stimulated T cells. |journal=Blood |volume=102 |issue= 5 |pages= 1788-96 |year= 2003 |pmid= 12738667 |doi= 10.1182/blood-2002-11-3499 }}
*{{cite journal  | author=Widlak P, Lanuszewska J, Cary RB, Garrard WT |title=Subunit structures and stoichiometries of human DNA fragmentation factor proteins before and after induction of apoptosis. |journal=J. Biol. Chem. |volume=278 |issue= 29 |pages= 26915-22 |year= 2003 |pmid= 12748178 |doi= 10.1074/jbc.M303807200 }}
*{{cite journal  | author=Hillman RT, Green RE, Brenner SE |title=An unappreciated role for RNA surveillance. |journal=Genome Biol. |volume=5 |issue= 2 |pages= R8 |year= 2005 |pmid= 14759258 |doi= 10.1186/gb-2004-5-2-r8 }}
*{{cite journal  | author=Bayascas JR, Yuste VJ, Solé C, ''et al.'' |title=Characterization of splice variants of human caspase-activated DNase with CIDE-N structure and function. |journal=FEBS Lett. |volume=566 |issue= 1-3 |pages= 234-40 |year= 2004 |pmid= 15147901 |doi= 10.1016/j.febslet.2004.04.050 }}
}}
{{refend}}

{{protein-stub}}
 
  • INFO: Beginning work on DHCR7... {November 18, 2007 11:45:31 PM PST}
  • AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:45:54 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 = 7-dehydrocholesterol reductase
 | HGNCid = 2860
 | Symbol = DHCR7
 | AltSymbols =; SLOS
 | OMIM = 602858
 | ECnumber =  
 | Homologene = 1042
 | MGIid = 1298378
 | GeneAtlas_image1 = PBB_GE_DHCR7_201791_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_DHCR7_201790_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0047598 |text = 7-dehydrocholesterol reductase activity}} 
 | Component = {{GNF_GO|id=GO:0005640 |text = nuclear outer membrane}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} 
 | Process = {{GNF_GO|id=GO:0001568 |text = blood vessel development}} {{GNF_GO|id=GO:0006695 |text = cholesterol biosynthetic process}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0030324 |text = lung development}} {{GNF_GO|id=GO:0042127 |text = regulation of cell proliferation}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1717
    | Hs_Ensembl = ENSG00000172893
    | Hs_RefseqProtein = NP_001351
    | Hs_RefseqmRNA = NM_001360
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 70823111
    | Hs_GenLoc_end = 70837050
    | Hs_Uniprot = Q9UBM7
    | Mm_EntrezGene = 13360
    | Mm_Ensembl = ENSMUSG00000058454
    | Mm_RefseqmRNA = XM_001002212
    | Mm_RefseqProtein = XP_001002212
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 143632557
    | Mm_GenLoc_end = 143657800
    | Mm_Uniprot = Q3UIQ5
  }}
}}
'''7-dehydrocholesterol reductase''', also known as '''DHCR7''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DHCR7 7-dehydrocholesterol reductase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1717| 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=Waterham HR, Wanders RJ |title=Biochemical and genetic aspects of 7-dehydrocholesterol reductase and Smith-Lemli-Opitz syndrome. |journal=Biochim. Biophys. Acta |volume=1529 |issue= 1-3 |pages= 340-56 |year= 2001 |pmid= 11111101 |doi=  }}
*{{cite journal  | author=Nowaczyk MJ, Nakamura LM, Waye JS |title=DHCR7 and Smith-Lemli-Opitz syndrome. |journal=Clinical and investigative medicine. Médecine clinique et experimentale |volume=24 |issue= 6 |pages= 311-7 |year= 2002 |pmid= 11767235 |doi=  }}
*{{cite journal  | author=Shefer S, Salen G, Batta AK, ''et al.'' |title=Markedly inhibited 7-dehydrocholesterol-delta 7-reductase activity in liver microsomes from Smith-Lemli-Opitz homozygotes. |journal=J. Clin. Invest. |volume=96 |issue= 4 |pages= 1779-85 |year= 1995 |pmid= 7560069 |doi=  }}
*{{cite journal  | author=Moebius FF, Fitzky BU, Lee JN, ''et al.'' |title=Molecular cloning and expression of the human delta7-sterol reductase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 4 |pages= 1899-902 |year= 1998 |pmid= 9465114 |doi=  }}
*{{cite journal  | author=Wassif CA, Maslen C, Kachilele-Linjewile S, ''et al.'' |title=Mutations in the human sterol delta7-reductase gene at 11q12-13 cause Smith-Lemli-Opitz syndrome. |journal=Am. J. Hum. Genet. |volume=63 |issue= 1 |pages= 55-62 |year= 1998 |pmid= 9634533 |doi=  }}
*{{cite journal  | author=Fitzky BU, Witsch-Baumgartner M, Erdel M, ''et al.'' |title=Mutations in the Delta7-sterol reductase gene in patients with the Smith-Lemli-Opitz syndrome. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 14 |pages= 8181-6 |year= 1998 |pmid= 9653161 |doi=  }}
*{{cite journal  | author=Waterham HR, Wijburg FA, Hennekam RC, ''et al.'' |title=Smith-Lemli-Opitz syndrome is caused by mutations in the 7-dehydrocholesterol reductase gene. |journal=Am. J. Hum. Genet. |volume=63 |issue= 2 |pages= 329-38 |year= 1998 |pmid= 9683613 |doi=  }}
*{{cite journal  | author=Holmer L, Pezhman A, Worman HJ |title=The human lamin B receptor/sterol reductase multigene family. |journal=Genomics |volume=54 |issue= 3 |pages= 469-76 |year= 1999 |pmid= 9878250 |doi= 10.1006/geno.1998.5615 }}
*{{cite journal  | author=De Brasi D, Esposito T, Rossi M, ''et al.'' |title=Smith-Lemli-Opitz syndrome: evidence of T93M as a common mutation of delta7-sterol reductase in Italy and report of three novel mutations. |journal=Eur. J. Hum. Genet. |volume=7 |issue= 8 |pages= 937-40 |year= 2000 |pmid= 10602371 |doi= 10.1038/sj.ejhg.5200390 }}
*{{cite journal  | author=Witsch-Baumgartner M, Fitzky BU, Ogorelkova M, ''et al.'' |title=Mutational spectrum in the Delta7-sterol reductase gene and genotype-phenotype correlation in 84 patients with Smith-Lemli-Opitz syndrome. |journal=Am. J. Hum. Genet. |volume=66 |issue= 2 |pages= 402-12 |year= 2000 |pmid= 10677299 |doi=  }}
*{{cite journal  | author=Linck LM, Hayflick SJ, Lin DS, ''et al.'' |title=Fetal demise with Smith-Lemli-Opitz syndrome confirmed by tissue sterol analysis and the absence of measurable 7-dehydrocholesterol Delta(7)-reductase activity in chorionic villi. |journal=Prenat. Diagn. |volume=20 |issue= 3 |pages= 238-40 |year= 2000 |pmid= 10719329 |doi=  }}
*{{cite journal  | author=Yu H, Lee MH, Starck L, ''et al.'' |title=Spectrum of Delta(7)-dehydrocholesterol reductase mutations in patients with the Smith-Lemli-Opitz (RSH) syndrome. |journal=Hum. Mol. Genet. |volume=9 |issue= 9 |pages= 1385-91 |year= 2000 |pmid= 10814720 |doi=  }}
*{{cite journal  | author=Krakowiak PA, Nwokoro NA, Wassif CA, ''et al.'' |title=Mutation analysis and description of sixteen RSH/Smith-Lemli-Opitz syndrome patients: polymerase chain reaction-based assays to simplify genotyping. |journal=Am. J. Med. Genet. |volume=94 |issue= 3 |pages= 214-27 |year= 2000 |pmid= 10995508 |doi=  }}
*{{cite journal  | author=Löffler J, Trojovsky A, Casati B, ''et al.'' |title=Homozygosity for the W151X stop mutation in the delta7-sterol reductase gene (DHCR7) causing a lethal form of Smith-Lemli-Opitz syndrome: retrospective molecular diagnosis. |journal=Am. J. Med. Genet. |volume=95 |issue= 2 |pages= 174-7 |year= 2001 |pmid= 11078571 |doi=  }}
*{{cite journal  | author=Witsch-Baumgartner M, Ciara E, Löffler J, ''et al.'' |title=Frequency gradients of DHCR7 mutations in patients with Smith-Lemli-Opitz syndrome in Europe: evidence for different origins of common mutations. |journal=Eur. J. Hum. Genet. |volume=9 |issue= 1 |pages= 45-50 |year= 2001 |pmid= 11175299 |doi= 10.1038/sj.ejhg.5200579 }}
*{{cite journal  | author=Nowaczyk MJ, Heshka T, Eng B, ''et al.'' |title=DHCR7 genotypes of cousins with Smith-Lemli-Opitz syndrome. |journal=Am. J. Med. Genet. |volume=100 |issue= 2 |pages= 162-3 |year= 2001 |pmid= 11298379 |doi=  }}
*{{cite journal  | author=Jira PE, Wanders RJ, Smeitink JA, ''et al.'' |title=Novel mutations in the 7-dehydrocholesterol reductase gene of 13 patients with Smith--Lemli--Opitz syndrome. |journal=Ann. Hum. Genet. |volume=65 |issue= Pt 3 |pages= 229-36 |year= 2001 |pmid= 11427181 |doi= doi:10.1017/S0003480001008600 }}
*{{cite journal  | author=Nowaczyk MJ, Farrell SA, Sirkin WL, ''et al.'' |title=Smith-Lemli-Opitz (RHS) syndrome: holoprosencephaly and homozygous IVS8-1G-->C genotype. |journal=Am. J. Med. Genet. |volume=103 |issue= 1 |pages= 75-80 |year= 2001 |pmid= 11562938 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 
  • INFO: Beginning work on DLG3... {November 18, 2007 11:45:54 PM PST}
  • SEARCH REDIRECT: Control Box Found: DLG3 {November 18, 2007 11:46:42 PM PST}
  • UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:46:43 PM PST}
  • UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:46:43 PM PST}
  • UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:46:43 PM PST}
  • UPDATED: Updated protein page: DLG3 {November 18, 2007 11:46:48 PM PST}
  • INFO: Beginning work on DNMT3A... {November 18, 2007 11:46:49 PM PST}
  • SEARCH REDIRECT: Control Box Found: DNMT3A {November 18, 2007 11:47:21 PM PST}
  • UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:47:24 PM PST}
  • UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:47:24 PM PST}
  • UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:47:24 PM PST}
  • UPDATED: Updated protein page: DNMT3A {November 18, 2007 11:47:33 PM PST}
  • INFO: Beginning work on DSG3... {November 18, 2007 11:47:33 PM PST}
  • AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:48:01 PM PST}
 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Desmoglein 3 (pemphigus vulgaris antigen)
 | HGNCid = 3050
 | Symbol = DSG3
 | AltSymbols =; CDHF6; DKFZp686P23184; PVA
 | OMIM = 169615
 | ECnumber =  
 | Homologene = 55513
 | MGIid = 99499
 | GeneAtlas_image1 = PBB_GE_DSG3_205595_at_tn.png
 | Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} 
 | Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005911 |text = intercellular junction}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} 
 | Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007156 |text = homophilic cell adhesion}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1830
    | Hs_Ensembl = ENSG00000134757
    | Hs_RefseqProtein = NP_001935
    | Hs_RefseqmRNA = NM_001944
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 18
    | Hs_GenLoc_start = 27281756
    | Hs_GenLoc_end = 27310474
    | Hs_Uniprot = P32926
    | Mm_EntrezGene = 13512
    | Mm_Ensembl = ENSMUSG00000056632
    | Mm_RefseqmRNA = XM_984295
    | Mm_RefseqProtein = XP_989389
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 18
    | Mm_GenLoc_start = 20653284
    | Mm_GenLoc_end = 20683759
    | Mm_Uniprot = Q3UFC6
  }}
}}
'''Desmoglein 3 (pemphigus vulgaris antigen)''', also known as '''DSG3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DSG3 desmoglein 3 (pemphigus vulgaris antigen)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1830| 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 = Desmosomes are cell-cell junctions between epithelial, myocardial, and certain other cell types. Desmoglein 3 is a calcium-binding transmembrane glycoprotein component of desmosomes in vertebrate epithelial cells. Currently, three desmoglein subfamily members have been identified and all are members of the cadherin cell adhesion molecule superfamily. These desmoglein gene family members are located in a cluster on chromosome 18. This protein has been identified as the autoantigen of the autoimmune skin blistering disease pemphigus vulgaris.<ref name="entrez">{{cite web | title = Entrez Gene: DSG3 desmoglein 3 (pemphigus vulgaris antigen)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1830| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Arnemann J, Spurr NK, Buxton RS |title=The human gene (DSG3) coding for the pemphigus vulgaris antigen is, like the genes coding for the other two known desmogleins, assigned to chromosome 18. |journal=Hum. Genet. |volume=89 |issue= 3 |pages= 347-50 |year= 1992 |pmid= 1601426 |doi=  }}
*{{cite journal  | author=Amagai M, Klaus-Kovtun V, Stanley JR |title=Autoantibodies against a novel epithelial cadherin in pemphigus vulgaris, a disease of cell adhesion. |journal=Cell |volume=67 |issue= 5 |pages= 869-77 |year= 1992 |pmid= 1720352 |doi=  }}
*{{cite journal  | author=Roh JY, Stanley JR |title=Plakoglobin binding by human Dsg3 (pemphigus vulgaris antigen) in keratinocytes requires the cadherin-like intracytoplasmic segment. |journal=J. Invest. Dermatol. |volume=104 |issue= 5 |pages= 720-4 |year= 1995 |pmid= 7738346 |doi=  }}
*{{cite journal  | author=Wang Y, Amagai M, Minoshima S, ''et al.'' |title=The human genes for desmogleins (DSG1 and DSG3) are located in a small region on chromosome 18q12. |journal=Genomics |volume=20 |issue= 3 |pages= 492-5 |year= 1994 |pmid= 8034325 |doi= 10.1006/geno.1994.1207 }}
*{{cite journal  | author=Schäfer S, Koch PJ, Franke WW |title=Identification of the ubiquitous human desmoglein, Dsg2, and the expression catalogue of the desmoglein subfamily of desmosomal cadherins. |journal=Exp. Cell Res. |volume=211 |issue= 2 |pages= 391-9 |year= 1994 |pmid= 8143788 |doi= 10.1006/excr.1994.1103 }}
*{{cite journal  | author=Kárpáti S, Amagai M, Prussick R, ''et al.'' |title=Pemphigus vulgaris antigen, a desmoglein type of cadherin, is localized within keratinocyte desmosomes. |journal=J. Cell Biol. |volume=122 |issue= 2 |pages= 409-15 |year= 1993 |pmid= 8320263 |doi=  }}
*{{cite journal  | author=Silos SA, Tamai K, Li K, ''et al.'' |title=Cloning of the gene for human pemphigus vulgaris antigen (desmoglein 3), a desmosomal cadherin. Characterization of the promoter region and identification of a keratinocyte-specific cis-element. |journal=J. Biol. Chem. |volume=271 |issue= 29 |pages= 17504-11 |year= 1996 |pmid= 8663392 |doi=  }}
*{{cite journal  | author=Marsden MD, Collins JE, Greenwood MD, ''et al.'' |title=Cloning and transcriptional analysis of the promoter of the human type 2 desmocollin gene (DSC2). |journal=Gene |volume=186 |issue= 2 |pages= 237-47 |year= 1997 |pmid= 9074502 |doi=  }}
*{{cite journal  | author=Adams MJ, Reichel MB, King IA, ''et al.'' |title=Characterization of the regulatory regions in the human desmoglein genes encoding the pemphigus foliaceous and pemphigus vulgaris antigens. |journal=Biochem. J. |volume=329 ( Pt 1) |issue=  |pages= 165-74 |year= 1998 |pmid= 9405290 |doi=  }}
*{{cite journal  | author=Shirakata Y, Amagai M, Hanakawa Y, ''et al.'' |title=Lack of mucosal involvement in pemphigus foliaceus may be due to low expression of desmoglein 1. |journal=J. Invest. Dermatol. |volume=110 |issue= 1 |pages= 76-8 |year= 1998 |pmid= 9424092 |doi= 10.1046/j.1523-1747.1998.00085.x }}
*{{cite journal  | author=Amagai M, Nishikawa T, Nousari HC, ''et al.'' |title=Antibodies against desmoglein 3 (pemphigus vulgaris antigen) are present in sera from patients with paraneoplastic pemphigus and cause acantholysis in vivo in neonatal mice. |journal=J. Clin. Invest. |volume=102 |issue= 4 |pages= 775-82 |year= 1998 |pmid= 9710446 |doi=  }}
*{{cite journal  | author=Ishikawa H, Li K, Tamai K, ''et al.'' |title=Cloning of the mouse desmoglein 3 gene (Dsg3): interspecies conservation within the cadherin superfamily. |journal=Exp. Dermatol. |volume=9 |issue= 4 |pages= 229-39 |year= 2001 |pmid= 10949543 |doi=  }}
*{{cite journal  | author=Czerwenka KF, Manavi M, Hosmann J, ''et al.'' |title=Comparative analysis of two-dimensional protein patterns in malignant and normal human breast tissue. |journal=Cancer Detect. Prev. |volume=25 |issue= 3 |pages= 268-79 |year= 2001 |pmid= 11425269 |doi=  }}
*{{cite journal  | author=Weiske J, Schöneberg T, Schröder W, ''et al.'' |title=The fate of desmosomal proteins in apoptotic cells. |journal=J. Biol. Chem. |volume=276 |issue= 44 |pages= 41175-81 |year= 2001 |pmid= 11500511 |doi= 10.1074/jbc.M105769200 }}
*{{cite journal  | author=Andl CD, Stanley JR |title=Central role of the plakoglobin-binding domain for desmoglein 3 incorporation into desmosomes. |journal=J. Invest. Dermatol. |volume=117 |issue= 5 |pages= 1068-74 |year= 2001 |pmid= 11710914 |doi= 10.1046/j.0022-202x.2001.01528.x }}
*{{cite journal  | author=Merritt AJ, Berika MY, Zhai W, ''et al.'' |title=Suprabasal desmoglein 3 expression in the epidermis of transgenic mice results in hyperproliferation and abnormal differentiation. |journal=Mol. Cell. Biol. |volume=22 |issue= 16 |pages= 5846-58 |year= 2002 |pmid= 12138195 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Hanakawa Y, Amagai M, Shirakata Y, ''et al.'' |title=Differential effects of desmoglein 1 and desmoglein 3 on desmosome formation. |journal=J. Invest. Dermatol. |volume=119 |issue= 6 |pages= 1231-6 |year= 2003 |pmid= 12485422 |doi= 10.1046/j.1523-1747.2002.19648.x }}
*{{cite journal  | author=Veldman C, Stauber A, Wassmuth R, ''et al.'' |title=Dichotomy of autoreactive Th1 and Th2 cell responses to desmoglein 3 in patients with pemphigus vulgaris (PV) and healthy carriers of PV-associated HLA class II alleles. |journal=J. Immunol. |volume=170 |issue= 1 |pages= 635-42 |year= 2003 |pmid= 12496453 |doi=  }}
*{{cite journal  | author=Posthaus H, Dubois CM, Müller E |title=Novel insights into cadherin processing by subtilisin-like convertases. |journal=FEBS Lett. |volume=536 |issue= 1-3 |pages= 203-8 |year= 2003 |pmid= 12586364 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 
  • INFO: Beginning work on E2F2... {November 18, 2007 11:48:01 PM PST}
  • SEARCH REDIRECT: Control Box Found: E2F2 {November 18, 2007 11:48:28 PM PST}
  • UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:48:30 PM PST}
  • UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:48:30 PM PST}
  • UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:48:30 PM PST}
  • UPDATED: Updated protein page: E2F2 {November 18, 2007 11:48:36 PM PST}
  • INFO: Beginning work on ERG... {November 18, 2007 11:48:36 PM PST}
  • AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:49:16 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_ERG_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1fli.
 | PDB = {{PDB2|1fli}}, {{PDB2|1sxe}}
 | Name = V-ets erythroblastosis virus E26 oncogene homolog (avian)
 | HGNCid = 3446
 | Symbol = ERG
 | AltSymbols =; erg-3; p55
 | OMIM = 165080
 | ECnumber =  
 | Homologene = 15848
 | MGIid = 95415
 | GeneAtlas_image1 = PBB_GE_ERG_211626_x_at_tn.png
 | GeneAtlas_image2 = PBB_GE_ERG_213541_s_at_tn.png
 | GeneAtlas_image3 = PBB_GE_ERG_222079_at_tn.png
 | Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} 
 | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} 
 | Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2078
    | Hs_Ensembl = ENSG00000157554
    | Hs_RefseqProtein = NP_004440
    | Hs_RefseqmRNA = NM_004449
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 21
    | Hs_GenLoc_start = 38675671
    | Hs_GenLoc_end = 38955488
    | Hs_Uniprot = P11308
    | Mm_EntrezGene = 13876
    | Mm_Ensembl = ENSMUSG00000040732
    | Mm_RefseqmRNA = XM_001004957
    | Mm_RefseqProtein = XP_001004957
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 16
    | Mm_GenLoc_start = 95469604
    | Mm_GenLoc_end = 95518756
    | Mm_Uniprot = Q3UQJ4
  }}
}}
'''V-ets erythroblastosis virus E26 oncogene homolog (avian)''', also known as '''ERG''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ERG v-ets erythroblastosis virus E26 oncogene homolog (avian)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2078| 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=Rao VN, Modi WS, Drabkin HD, ''et al.'' |title=The human erg gene maps to chromosome 21, band q22: relationship to the 8; 21 translocation of acute myelogenous leukemia. |journal=Oncogene |volume=3 |issue= 5 |pages= 497-500 |year= 1990 |pmid= 3274086 |doi=  }}
*{{cite journal  | author=Rao VN, Papas TS, Reddy ES |title=erg, a human ets-related gene on chromosome 21: alternative splicing, polyadenylation, and translation. |journal=Science |volume=237 |issue= 4815 |pages= 635-9 |year= 1987 |pmid= 3299708 |doi=  }}
*{{cite journal  | author=Reddy ES, Rao VN, Papas TS |title=The erg gene: a human gene related to the ets oncogene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 17 |pages= 6131-5 |year= 1987 |pmid= 3476934 |doi=  }}
*{{cite journal  | author=Giovannini M, Biegel JA, Serra M, ''et al.'' |title=EWS-erg and EWS-Fli1 fusion transcripts in Ewing's sarcoma and primitive neuroectodermal tumors with variant translocations. |journal=J. Clin. Invest. |volume=94 |issue= 2 |pages= 489-96 |year= 1994 |pmid= 8040301 |doi=  }}
*{{cite journal  | author=Dunn T, Praissman L, Hagag N, Viola MV |title=ERG gene is translocated in an Ewing's sarcoma cell line. |journal=Cancer Genet. Cytogenet. |volume=76 |issue= 1 |pages= 19-22 |year= 1994 |pmid= 8076344 |doi=  }}
*{{cite journal  | author=Ichikawa H, Shimizu K, Hayashi Y, Ohki M |title=An RNA-binding protein gene, TLS/FUS, is fused to ERG in human myeloid leukemia with t(16;21) chromosomal translocation. |journal=Cancer Res. |volume=54 |issue= 11 |pages= 2865-8 |year= 1994 |pmid= 8187069 |doi=  }}
*{{cite journal  | author=Prasad DD, Rao VN, Lee L, Reddy ES |title=Differentially spliced erg-3 product functions as a transcriptional activator. |journal=Oncogene |volume=9 |issue= 2 |pages= 669-73 |year= 1994 |pmid= 8290279 |doi=  }}
*{{cite journal  | author=Murakami K, Mavrothalassitis G, Bhat NK, ''et al.'' |title=Human ERG-2 protein is a phosphorylated DNA-binding protein--a distinct member of the ets family. |journal=Oncogene |volume=8 |issue= 6 |pages= 1559-66 |year= 1993 |pmid= 8502479 |doi=  }}
*{{cite journal  | author=Duterque-Coquillaud M, Niel C, Plaza S, Stehelin D |title=New human erg isoforms generated by alternative splicing are transcriptional activators. |journal=Oncogene |volume=8 |issue= 7 |pages= 1865-73 |year= 1993 |pmid= 8510931 |doi=  }}
*{{cite journal  | author=Basuyaux JP, Ferreira E, Stéhelin D, Butticè G |title=The Ets transcription factors interact with each other and with the c-Fos/c-Jun complex via distinct protein domains in a DNA-dependent and -independent manner. |journal=J. Biol. Chem. |volume=272 |issue= 42 |pages= 26188-95 |year= 1997 |pmid= 9334186 |doi=  }}
*{{cite journal  | author=Carrère S, Verger A, Flourens A, ''et al.'' |title=Erg proteins, transcription factors of the Ets family, form homo, heterodimers and ternary complexes via two distinct domains. |journal=Oncogene |volume=16 |issue= 25 |pages= 3261-8 |year= 1998 |pmid= 9681824 |doi= 10.1038/sj.onc.1201868 }}
*{{cite journal  | author=McLaughlin F, Ludbrook VJ, Kola I, ''et al.'' |title=Characterisation of the tumour necrosis factor (TNF)-(alpha) response elements in the human ICAM-2 promoter. |journal=J. Cell. Sci. |volume=112 ( Pt 24) |issue=  |pages= 4695-703 |year= 2000 |pmid= 10574717 |doi=  }}
*{{cite journal  | author=Hattori M, Fujiyama A, Taylor TD, ''et al.'' |title=The DNA sequence of human chromosome 21. |journal=Nature |volume=405 |issue= 6784 |pages= 311-9 |year= 2000 |pmid= 10830953 |doi= 10.1038/35012518 }}
*{{cite journal  | author=Mastrangelo T, Modena P, Tornielli S, ''et al.'' |title=A novel zinc finger gene is fused to EWS in small round cell tumor. |journal=Oncogene |volume=19 |issue= 33 |pages= 3799-804 |year= 2000 |pmid= 10949935 |doi= 10.1038/sj.onc.1203762 }}
*{{cite journal  | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi=  }}
*{{cite journal  | author=Verger A, Buisine E, Carrère S, ''et al.'' |title=Identification of amino acid residues in the ETS transcription factor Erg that mediate Erg-Jun/Fos-DNA ternary complex formation. |journal=J. Biol. Chem. |volume=276 |issue= 20 |pages= 17181-9 |year= 2001 |pmid= 11278640 |doi= 10.1074/jbc.M010208200 }}
*{{cite journal  | author=Yang L, Xia L, Wu DY, ''et al.'' |title=Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factor. |journal=Oncogene |volume=21 |issue= 1 |pages= 148-52 |year= 2002 |pmid= 11791185 |doi= 10.1038/sj.onc.1204998 }}
*{{cite journal  | author=Mackereth CD, Schärpf M, Gentile LN, McIntosh LP |title=Chemical shift and secondary structure conservation of the PNT/SAM domains from the ets family of transcription factors. |journal=J. Biomol. NMR |volume=24 |issue= 1 |pages= 71-2 |year= 2003 |pmid= 12449421 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Matsui Y, Chansky HA, Barahmand-Pour F, ''et al.'' |title=COL11A2 collagen gene transcription is differentially regulated by EWS/ERG sarcoma fusion protein and wild-type ERG. |journal=J. Biol. Chem. |volume=278 |issue= 13 |pages= 11369-75 |year= 2003 |pmid= 12554743 |doi= 10.1074/jbc.M300164200 }}
}}
{{refend}}

{{protein-stub}}
 
  • INFO: Beginning work on ETV4... {November 18, 2007 11:49:16 PM PST}
  • SEARCH REDIRECT: Control Box Found: ETV4 {November 18, 2007 11:50:04 PM PST}
  • UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:50:07 PM PST}
  • UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:50:07 PM PST}
  • UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:50:07 PM PST}
  • UPDATED: Updated protein page: ETV4 {November 18, 2007 11:50:13 PM PST}
  • INFO: Beginning work on EXT2... {November 18, 2007 11:50:13 PM PST}
  • AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:50:51 PM PST}
 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Exostoses (multiple) 2
 | HGNCid = 3513
 | Symbol = EXT2
 | AltSymbols =; SOTV
 | OMIM = 608210
 | ECnumber =  
 | Homologene = 345
 | MGIid = 108050
 | GeneAtlas_image1 = PBB_GE_EXT2_202012_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_EXT2_202013_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}} {{GNF_GO|id=GO:0050508 |text = glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity}} {{GNF_GO|id=GO:0050509 |text = N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity}} 
 | Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005789 |text = endoplasmic reticulum membrane}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} 
 | Process = {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0006024 |text = glycosaminoglycan biosynthetic process}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2132
    | Hs_Ensembl = ENSG00000151348
    | Hs_RefseqProtein = NP_000392
    | Hs_RefseqmRNA = NM_000401
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 44073675
    | Hs_GenLoc_end = 44223555
    | Hs_Uniprot = Q93063
    | Mm_EntrezGene = 14043
    | Mm_Ensembl = ENSMUSG00000027198
    | Mm_RefseqmRNA = NM_010163
    | Mm_RefseqProtein = NP_034293
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 93496472
    | Mm_GenLoc_end = 93623384
    | Mm_Uniprot = Q3TPI7
  }}
}}
'''Exostoses (multiple) 2''', also known as '''EXT2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EXT2 exostoses (multiple) 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2132| 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 one of two glycosyltransferases involved in the chain elongation step of heparan sulfate biosynthesis. Mutations in this gene cause the type II form of multiple exostoses.<ref name="entrez">{{cite web | title = Entrez Gene: EXT2 exostoses (multiple) 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2132| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Wuyts W, Van Hul W |title=Molecular basis of multiple exostoses: mutations in the EXT1 and EXT2 genes. |journal=Hum. Mutat. |volume=15 |issue= 3 |pages= 220-7 |year= 2000 |pmid= 10679937 |doi= 10.1002/(SICI)1098-1004(200003)15:3<220::AID-HUMU2>3.0.CO;2-K }}
*{{cite journal  | author=Wuyts W, Ramlakhan S, Van Hul W, ''et al.'' |title=Refinement of the multiple exostoses locus (EXT2) to a 3-cM interval on chromosome 11. |journal=Am. J. Hum. Genet. |volume=57 |issue= 2 |pages= 382-7 |year= 1995 |pmid= 7668264 |doi=  }}
*{{cite journal  | author=Wu YQ, Heutink P, de Vries BB, ''et al.'' |title=Assignment of a second locus for multiple exostoses to the pericentromeric region of chromosome 11. |journal=Hum. Mol. Genet. |volume=3 |issue= 1 |pages= 167-71 |year= 1994 |pmid= 8162019 |doi=  }}
*{{cite journal  | author=Stickens D, Clines G, Burbee D, ''et al.'' |title=The EXT2 multiple exostoses gene defines a family of putative tumour suppressor genes. |journal=Nat. Genet. |volume=14 |issue= 1 |pages= 25-32 |year= 1996 |pmid= 8782816 |doi= 10.1038/ng0996-25 }}
*{{cite journal  | author=Wuyts W, Van Hul W, Wauters J, ''et al.'' |title=Positional cloning of a gene involved in hereditary multiple exostoses. |journal=Hum. Mol. Genet. |volume=5 |issue= 10 |pages= 1547-57 |year= 1997 |pmid= 8894688 |doi=  }}
*{{cite journal  | author=Clines GA, Ashley JA, Shah S, Lovett M |title=The structure of the human multiple exostoses 2 gene and characterization of homologs in mouse and Caenorhabditis elegans. |journal=Genome Res. |volume=7 |issue= 4 |pages= 359-67 |year= 1997 |pmid= 9110175 |doi=  }}
*{{cite journal  | author=Philippe C, Porter DE, Emerton ME, ''et al.'' |title=Mutation screening of the EXT1 and EXT2 genes in patients with hereditary multiple exostoses. |journal=Am. J. Hum. Genet. |volume=61 |issue= 3 |pages= 520-8 |year= 1997 |pmid= 9326317 |doi=  }}
*{{cite journal  | author=Wuyts W, Van Hul W, De Boulle K, ''et al.'' |title=Mutations in the EXT1 and EXT2 genes in hereditary multiple exostoses. |journal=Am. J. Hum. Genet. |volume=62 |issue= 2 |pages= 346-54 |year= 1998 |pmid= 9463333 |doi=  }}
*{{cite journal  | author=Bridge JA, Nelson M, Orndal C, ''et al.'' |title=Clonal karyotypic abnormalities of the hereditary multiple exostoses chromosomal loci 8q24.1 (EXT1) and 11p11-12 (EXT2) in patients with sporadic and hereditary osteochondromas. |journal=Cancer |volume=82 |issue= 9 |pages= 1657-63 |year= 1998 |pmid= 9576285 |doi=  }}
*{{cite journal  | author=McCormick C, Leduc Y, Martindale D, ''et al.'' |title=The putative tumour suppressor EXT1 alters the expression of cell-surface heparan sulfate. |journal=Nat. Genet. |volume=19 |issue= 2 |pages= 158-61 |year= 1998 |pmid= 9620772 |doi= 10.1038/514 }}
*{{cite journal  | author=Lind T, Tufaro F, McCormick C, ''et al.'' |title=The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate. |journal=J. Biol. Chem. |volume=273 |issue= 41 |pages= 26265-8 |year= 1998 |pmid= 9756849 |doi=  }}
*{{cite journal  | author=Park KJ, Shin KH, Ku JL, ''et al.'' |title=Germline mutations in the EXT1 and EXT2 genes in Korean patients with hereditary multiple exostoses. |journal=J. Hum. Genet. |volume=44 |issue= 4 |pages= 230-4 |year= 1999 |pmid= 10429361 |doi=  }}
*{{cite journal  | author=Xu L, Xia J, Jiang H, ''et al.'' |title=Mutation analysis of hereditary multiple exostoses in the Chinese. |journal=Hum. Genet. |volume=105 |issue= 1-2 |pages= 45-50 |year= 1999 |pmid= 10480354 |doi=  }}
*{{cite journal  | author=Simmons AD, Musy MM, Lopes CS, ''et al.'' |title=A direct interaction between EXT proteins and glycosyltransferases is defective in hereditary multiple exostoses. |journal=Hum. Mol. Genet. |volume=8 |issue= 12 |pages= 2155-64 |year= 1999 |pmid= 10545594 |doi=  }}
*{{cite journal  | author=McCormick C, Duncan G, Goutsos KT, Tufaro F |title=The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 2 |pages= 668-73 |year= 2000 |pmid= 10639137 |doi=  }}
*{{cite journal  | author=Kobayashi S, Morimoto K, Shimizu T, ''et al.'' |title=Association of EXT1 and EXT2, hereditary multiple exostoses gene products, in Golgi apparatus. |journal=Biochem. Biophys. Res. Commun. |volume=268 |issue= 3 |pages= 860-7 |year= 2000 |pmid= 10679296 |doi= 10.1006/bbrc.2000.2219 }}
*{{cite journal  | author=Shi YR, Wu JY, Tsai FJ, ''et al.'' |title=An R223P mutation in EXT2 gene causes hereditary multiple exostoses. |journal=Hum. Mutat. |volume=15 |issue= 4 |pages= 390-1 |year= 2000 |pmid= 10738008 |doi= 10.1002/(SICI)1098-1004(200004)15:4<390::AID-HUMU35>3.0.CO;2-E }}
*{{cite journal  | author=Stickens D, Brown D, Evans GA |title=EXT genes are differentially expressed in bone and cartilage during mouse embryogenesis. |journal=Dev. Dyn. |volume=218 |issue= 3 |pages= 452-64 |year= 2000 |pmid= 10878610 |doi= 10.1002/1097-0177(200007)218:3<452::AID-DVDY1000>3.0.CO;2-P }}
*{{cite journal  | author=Bernard MA, Hall CE, Hogue DA, ''et al.'' |title=Diminished levels of the putative tumor suppressor proteins EXT1 and EXT2 in exostosis chondrocytes. |journal=Cell Motil. Cytoskeleton |volume=48 |issue= 2 |pages= 149-62 |year= 2001 |pmid= 11169766 |doi= 10.1002/1097-0169(200102)48:2<149::AID-CM1005>3.0.CO;2-3 }}
}}
{{refend}}

{{protein-stub}}
 
  • INFO: Beginning work on FANCG... {November 18, 2007 11:50:51 PM PST}
  • AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:51:19 PM PST}
 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Fanconi anemia, complementation group G
 | HGNCid = 3588
 | Symbol = FANCG
 | AltSymbols =; FAG; XRCC9
 | OMIM = 602956
 | ECnumber =  
 | Homologene = 3402
 | MGIid = 1926471
 | GeneAtlas_image1 = PBB_GE_FANCG_203564_at_tn.png
 | Function = {{GNF_GO|id=GO:0003684 |text = damaged DNA binding}} {{GNF_GO|id=GO:0005488 |text = binding}} 
 | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} 
 | Process = {{GNF_GO|id=GO:0000075 |text = cell cycle checkpoint}} {{GNF_GO|id=GO:0001541 |text = ovarian follicle development}} {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0007286 |text = spermatid development}} {{GNF_GO|id=GO:0009314 |text = response to radiation}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2189
    | Hs_Ensembl = ENSG00000165281
    | Hs_RefseqProtein = NP_004620
    | Hs_RefseqmRNA = NM_004629
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 9
    | Hs_GenLoc_start = 35063835
    | Hs_GenLoc_end = 35070013
    | Hs_Uniprot = O15287
    | Mm_EntrezGene = 60534
    | Mm_Ensembl = ENSMUSG00000028453
    | Mm_RefseqmRNA = NM_053081
    | Mm_RefseqProtein = NP_444311
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 43023444
    | Mm_GenLoc_end = 43031588
    | Mm_Uniprot = Q8VHS1
  }}
}}
'''Fanconi anemia, complementation group G''', also known as '''FANCG''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FANCG Fanconi anemia, complementation group G| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2189| 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 = FANCG, involved in  Fanconi anemia, confers resistance to both hygromycin and mitomycin C. FANCG contains a 5-prime GC-rich untranslated region characteristic of housekeeping genes. The putative 622-amino acid protein has a leucine-zipper motif at its N-terminus.  Fanconi anemia is an autosomal recessive disorder with diverse clinical symptoms, including developmental anomalies, bone marrow failure, and early occurrence of malignancies. A minimum of 8 FA genes have been identified. The FANCG gene is responsible for complementation group G.<ref name="entrez">{{cite web | title = Entrez Gene: FANCG Fanconi anemia, complementation group G| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2189| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Liu N, Lamerdin JE, Tucker JD, ''et al.'' |title=The human XRCC9 gene corrects chromosomal instability and mutagen sensitivities in CHO UV40 cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 17 |pages= 9232-7 |year= 1997 |pmid= 9256465 |doi=  }}
*{{cite journal  | author=Joenje H, Oostra AB, Wijker M, ''et al.'' |title=Evidence for at least eight Fanconi anemia genes. |journal=Am. J. Hum. Genet. |volume=61 |issue= 4 |pages= 940-4 |year= 1997 |pmid= 9382107 |doi=  }}
*{{cite journal  | author=de Winter JP, Waisfisz Q, Rooimans MA, ''et al.'' |title=The Fanconi anaemia group G gene FANCG is identical with XRCC9. |journal=Nat. Genet. |volume=20 |issue= 3 |pages= 281-3 |year= 1998 |pmid= 9806548 |doi= 10.1038/3093 }}
*{{cite journal  | author=Garcia-Higuera I, Kuang Y, Näf D, ''et al.'' |title=Fanconi anemia proteins FANCA, FANCC, and FANCG/XRCC9 interact in a functional nuclear complex. |journal=Mol. Cell. Biol. |volume=19 |issue= 7 |pages= 4866-73 |year= 1999 |pmid= 10373536 |doi=  }}
*{{cite journal  | author=Jelesko JG, Harper R, Furuya M, Gruissem W |title=Rare germinal unequal crossing-over leading to recombinant gene formation and gene duplication in Arabidopsis thaliana. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 18 |pages= 10302-7 |year= 1999 |pmid= 10468603 |doi=  }}
*{{cite journal  | author=Waisfisz Q, de Winter JP, Kruyt FA, ''et al.'' |title=A physical complex of the Fanconi anemia proteins FANCG/XRCC9 and FANCA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 18 |pages= 10320-5 |year= 1999 |pmid= 10468606 |doi=  }}
*{{cite journal  | author=Kruyt FA, Abou-Zahr F, Mok H, Youssoufian H |title=Resistance to mitomycin C requires direct interaction between the Fanconi anemia proteins FANCA and FANCG in the nucleus through an arginine-rich domain. |journal=J. Biol. Chem. |volume=274 |issue= 48 |pages= 34212-8 |year= 1999 |pmid= 10567393 |doi=  }}
*{{cite journal  | author=Reuter T, Herterich S, Bernhard O, ''et al.'' |title=Strong FANCA/FANCG but weak FANCA/FANCC interaction in the yeast 2-hybrid system. |journal=Blood |volume=95 |issue= 2 |pages= 719-20 |year= 2000 |pmid= 10627486 |doi=  }}
*{{cite journal  | author=Huber PA, Medhurst AL, Youssoufian H, Mathew CG |title=Investigation of Fanconi anemia protein interactions by yeast two-hybrid analysis. |journal=Biochem. Biophys. Res. Commun. |volume=268 |issue= 1 |pages= 73-7 |year= 2000 |pmid= 10652215 |doi= 10.1006/bbrc.1999.2055 }}
*{{cite journal  | author=Yamada T, Tachibana A, Shimizu T, ''et al.'' |title=Novel mutations of the FANCG gene causing alternative splicing in Japanese Fanconi anemia. |journal=J. Hum. Genet. |volume=45 |issue= 3 |pages= 159-66 |year= 2000 |pmid= 10807541 |doi=  }}
*{{cite journal  | author=Kuang Y, Garcia-Higuera I, Moran A, ''et al.'' |title=Carboxy terminal region of the Fanconi anemia protein, FANCG/XRCC9, is required for functional activity. |journal=Blood |volume=96 |issue= 5 |pages= 1625-32 |year= 2000 |pmid= 10961856 |doi=  }}
*{{cite journal  | author=Garcia-Higuera I, Kuang Y, Denham J, D'Andrea AD |title=The fanconi anemia proteins FANCA and FANCG stabilize each other and promote the nuclear accumulation of the Fanconi anemia complex. |journal=Blood |volume=96 |issue= 9 |pages= 3224-30 |year= 2000 |pmid= 11050007 |doi=  }}
*{{cite journal  | author=de Winter JP, van der Weel L, de Groot J, ''et al.'' |title=The Fanconi anemia protein FANCF forms a nuclear complex with FANCA, FANCC and FANCG. |journal=Hum. Mol. Genet. |volume=9 |issue= 18 |pages= 2665-74 |year= 2000 |pmid= 11063725 |doi=  }}
*{{cite journal  | author=Demuth I, Wlodarski M, Tipping AJ, ''et al.'' |title=Spectrum of mutations in the Fanconi anaemia group G gene, FANCG/XRCC9. |journal=Eur. J. Hum. Genet. |volume=8 |issue= 11 |pages= 861-8 |year= 2000 |pmid= 11093276 |doi= 10.1038/sj.ejhg.5200552 }}
*{{cite journal  | author=Medhurst AL, Huber PA, Waisfisz Q, ''et al.'' |title=Direct interactions of the five known Fanconi anaemia proteins suggest a common functional pathway. |journal=Hum. Mol. Genet. |volume=10 |issue= 4 |pages= 423-9 |year= 2001 |pmid= 11157805 |doi=  }}
*{{cite journal  | author=McMahon LW, Sangerman J, Goodman SR, ''et al.'' |title=Human alpha spectrin II and the FANCA, FANCC, and FANCG proteins bind to DNA containing psoralen interstrand cross-links. |journal=Biochemistry |volume=40 |issue= 24 |pages= 7025-34 |year= 2001 |pmid= 11401546 |doi=  }}
*{{cite journal  | author=Yagasaki H, Adachi D, Oda T, ''et al.'' |title=A cytoplasmic serine protein kinase binds and may regulate the Fanconi anemia protein FANCA. |journal=Blood |volume=98 |issue= 13 |pages= 3650-7 |year= 2002 |pmid= 11739169 |doi=  }}
*{{cite journal  | author=Futaki M, Igarashi T, Watanabe S, ''et al.'' |title=The FANCG Fanconi anemia protein interacts with CYP2E1: possible role in protection against oxidative DNA damage. |journal=Carcinogenesis |volume=23 |issue= 1 |pages= 67-72 |year= 2002 |pmid= 11756225 |doi=  }}
*{{cite journal  | author=van de Vrugt HJ, Koomen M, Berns MA, ''et al.'' |title=Characterization, expression and complex formation of the murine Fanconi anaemia gene product Fancg. |journal=Genes Cells |volume=7 |issue= 3 |pages= 333-42 |year= 2002 |pmid= 11918676 |doi=  }}
*{{cite journal  | author=Pace P, Johnson M, Tan WM, ''et al.'' |title=FANCE: the link between Fanconi anaemia complex assembly and activity. |journal=EMBO J. |volume=21 |issue= 13 |pages= 3414-23 |year= 2002 |pmid= 12093742 |doi= 10.1093/emboj/cdf355 }}
}}
{{refend}}

{{protein-stub}}
 
  • INFO: Beginning work on FST... {November 18, 2007 11:53:37 PM PST}
  • AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:54:02 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_FST_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1lr7.
 | PDB = {{PDB2|1lr7}}, {{PDB2|1lr8}}, {{PDB2|1lr9}}, {{PDB2|2arp}}, {{PDB2|2b0u}}, {{PDB2|2p6a}}
 | Name = Follistatin
 | HGNCid = 3971
 | Symbol = FST
 | AltSymbols =; FS
 | OMIM = 136470
 | ECnumber =  
 | Homologene = 7324
 | MGIid = 95586
 | GeneAtlas_image1 = PBB_GE_FST_204948_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0017106 |text = activin inhibitor activity}} 
 | Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} 
 | Process = {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0007276 |text = gamete generation}} {{GNF_GO|id=GO:0007389 |text = pattern specification process}} {{GNF_GO|id=GO:0008585 |text = female gonad development}} {{GNF_GO|id=GO:0030509 |text = BMP signaling pathway}} {{GNF_GO|id=GO:0042475 |text = odontogenesis (sensu Vertebrata)}} {{GNF_GO|id=GO:0045596 |text = negative regulation of cell differentiation}} {{GNF_GO|id=GO:0046882 |text = negative regulation of follicle-stimulating hormone secretion}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10468
    | Hs_Ensembl = ENSG00000134363
    | Hs_RefseqProtein = NP_006341
    | Hs_RefseqmRNA = NM_006350
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 52812174
    | Hs_GenLoc_end = 52817659
    | Hs_Uniprot = P19883
    | Mm_EntrezGene = 14313
    | Mm_Ensembl = ENSMUSG00000021765
    | Mm_RefseqmRNA = NM_008046
    | Mm_RefseqProtein = NP_032072
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 13
    | Mm_GenLoc_start = 115574301
    | Mm_GenLoc_end = 115579608
    | Mm_Uniprot = Q8BNY0
  }}
}}
'''Follistatin''', also known as '''FST''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FST follistatin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10468| 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 = Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release.  The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA.  In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin.<ref name="entrez">{{cite web | title = Entrez Gene: FST follistatin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10468| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Peng C, Ohno T, Khorasheh S, Leung PC |title=Activin and follistatin as local regulators in the human ovary. |journal=Biol. Signals |volume=5 |issue= 2 |pages= 81-9 |year= 1996 |pmid= 8836491 |doi=  }}
*{{cite journal  | author=Phillips DJ, de Kretser DM |title=Follistatin: a multifunctional regulatory protein. |journal=Frontiers in neuroendocrinology |volume=19 |issue= 4 |pages= 287-322 |year= 1998 |pmid= 9799587 |doi= 10.1006/frne.1998.0169 }}
*{{cite journal  | author=Shimonaka M, Inouye S, Shimasaki S, Ling N |title=Follistatin binds to both activin and inhibin through the common subunit. |journal=Endocrinology |volume=128 |issue= 6 |pages= 3313-5 |year= 1991 |pmid= 2036994 |doi=  }}
*{{cite journal  | author=Shimasaki S, Koga M, Esch F, ''et al.'' |title=Primary structure of the human follistatin precursor and its genomic organization. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 12 |pages= 4218-22 |year= 1988 |pmid= 3380788 |doi=  }}
*{{cite journal  | author=Sumitomo S, Inouye S, Liu XJ, ''et al.'' |title=The heparin binding site of follistatin is involved in its interaction with activin. |journal=Biochem. Biophys. Res. Commun. |volume=208 |issue= 1 |pages= 1-9 |year= 1995 |pmid= 7887917 |doi= 10.1006/bbrc.1995.1297 }}
*{{cite journal  | author=Petraglia F, Gallinelli A, Grande A, ''et al.'' |title=Local production and action of follistatin in human placenta. |journal=J. Clin. Endocrinol. Metab. |volume=78 |issue= 1 |pages= 205-10 |year= 1994 |pmid= 8288705 |doi=  }}
*{{cite journal  | author=Schneyer AL, Hall HA, Lambert-Messerlian G, ''et al.'' |title=Follistatin-activin complexes in human serum and follicular fluid differ immunologically and biochemically. |journal=Endocrinology |volume=137 |issue= 1 |pages= 240-7 |year= 1996 |pmid= 8536619 |doi=  }}
*{{cite journal  | author=Jhaveri S, Erzurumlu RS, Chiaia N, ''et al.'' |title=Defective whisker follicles and altered brainstem patterns in activin and follistatin knockout mice. |journal=Mol. Cell. Neurosci. |volume=12 |issue= 4-5 |pages= 206-19 |year= 1999 |pmid= 9828086 |doi= 10.1006/mcne.1998.0710 }}
*{{cite journal  | author=Urbanek M, Legro RS, Driscoll DA, ''et al.'' |title=Thirty-seven candidate genes for polycystic ovary syndrome: strongest evidence for linkage is with follistatin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 15 |pages= 8573-8 |year= 1999 |pmid= 10411917 |doi=  }}
*{{cite journal  | author=Bondestam J, Horelli-Kuitunen N, Hildén K, ''et al.'' |title=Assignment of ACVR2 and ACVR2B the human activin receptor type II and IIB genes to chromosome bands 2q22.2-->q23.3 and 3p22 and the human follistatin gene (FST) to chromosome 5q11.2 by FISH. |journal=Cytogenet. Cell Genet. |volume=87 |issue= 3-4 |pages= 219-20 |year= 2000 |pmid= 10702675 |doi=  }}
*{{cite journal  | author=Beck HN, Drahushuk K, Jacoby DB, ''et al.'' |title=Bone morphogenetic protein-5 (BMP-5) promotes dendritic growth in cultured sympathetic neurons. |journal=BMC neuroscience |volume=2 |issue=  |pages= 12 |year= 2003 |pmid= 11580864 |doi=  }}
*{{cite journal  | author=Bartholin L, Maguer-Satta V, Hayette S, ''et al.'' |title=Transcription activation of FLRG and follistatin by activin A, through Smad proteins, participates in a negative feedback loop to modulate activin A function. |journal=Oncogene |volume=21 |issue= 14 |pages= 2227-35 |year= 2002 |pmid= 11948405 |doi= 10.1038/sj.onc.1205294 }}
*{{cite journal  | author=Hashimoto O, Tsuchida K, Ushiro Y, ''et al.'' |title=cDNA cloning and expression of human activin betaE subunit. |journal=Mol. Cell. Endocrinol. |volume=194 |issue= 1-2 |pages= 117-22 |year= 2003 |pmid= 12242034 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Nakamura M, Matzuk MM, Gerstmayer B, ''et al.'' |title=Control of pelage hair follicle development and cycling by complex interactions between follistatin and activin. |journal=FASEB J. |volume=17 |issue= 3 |pages= 497-9 |year= 2003 |pmid= 12514121 |doi= 10.1096/fj.02-0247fje }}
*{{cite journal  | author=Maguer-Satta V, Bartholin L, Jeanpierre S, ''et al.'' |title=Regulation of human erythropoiesis by activin A, BMP2, and BMP4, members of the TGFbeta family. |journal=Exp. Cell Res. |volume=282 |issue= 2 |pages= 110-20 |year= 2003 |pmid= 12531697 |doi=  }}
*{{cite journal  | author=Casagrandi D, Bearfield C, Geary J, ''et al.'' |title=Inhibin, activin, follistatin, activin receptors and beta-glycan gene expression in the placental tissue of patients with pre-eclampsia. |journal=Mol. Hum. Reprod. |volume=9 |issue= 4 |pages= 199-203 |year= 2003 |pmid= 12651901 |doi=  }}
*{{cite journal  | author=Schneyer A, Schoen A, Quigg A, Sidis Y |title=Differential binding and neutralization of activins A and B by follistatin and follistatin like-3 (FSTL-3/FSRP/FLRG). |journal=Endocrinology |volume=144 |issue= 5 |pages= 1671-4 |year= 2003 |pmid= 12697670 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 
  • INFO: Beginning work on GGA3... {November 18, 2007 11:54:02 PM PST}
  • SEARCH REDIRECT: Control Box Found: GGA3 {November 18, 2007 11:54:29 PM PST}
  • UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:54:30 PM PST}
  • UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:54:30 PM PST}
  • UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:54:30 PM PST}
  • UPDATED: Updated protein page: GGA3 {November 18, 2007 11:54:36 PM PST}
  • INFO: Beginning work on LTB4R... {November 18, 2007 11:42:35 PM PST}
  • AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:43:14 PM PST}
 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Leukotriene B4 receptor
 | HGNCid = 6713
 | Symbol = LTB4R
 | AltSymbols =; BLT1; BLTR; CMKRL1; GPR16; LTB4R1; LTBR1; P2RY7; P2Y7
 | OMIM = 601531
 | ECnumber =  
 | Homologene = 22477
 | MGIid = 1309472
 | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004974 |text = leukotriene receptor activity}} 
 | Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} 
 | Process = {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0006936 |text = muscle contraction}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007200 |text = G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1241
    | Hs_Ensembl =  
    | Hs_RefseqProtein = NP_858043
    | Hs_RefseqmRNA = NM_181657
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr =  
    | Hs_GenLoc_start =  
    | Hs_GenLoc_end =  
    | Hs_Uniprot =  
    | Mm_EntrezGene = 16995
    | Mm_Ensembl = ENSMUSG00000046908
    | Mm_RefseqmRNA = NM_008519
    | Mm_RefseqProtein = NP_032545
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 14
    | Mm_GenLoc_start = 54720038
    | Mm_GenLoc_end = 54722563
    | Mm_Uniprot = Q3U2P2
  }}
}}
'''Leukotriene B4 receptor''', also known as '''LTB4R''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LTB4R leukotriene B4 receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1241| 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=Raport CJ, Schweickart VL, Chantry D, ''et al.'' |title=New members of the chemokine receptor gene family. |journal=J. Leukoc. Biol. |volume=59 |issue= 1 |pages= 18-23 |year= 1996 |pmid= 8558062 |doi=  }}
*{{cite journal  | author=Tager AM, Luster AD |title=BLT1 and BLT2: the leukotriene B(4) receptors. |journal=Prostaglandins Leukot. Essent. Fatty Acids |volume=69 |issue= 2-3 |pages= 123-34 |year= 2004 |pmid= 12895595 |doi=  }}
*{{cite journal  | author=Miyahara N, Miyahara S, Takeda K, Gelfand EW |title=Role of the LTB4/BLT1 pathway in allergen-induced airway hyperresponsiveness and inflammation. |journal=Allergology international : official journal of the Japanese Society of Allergology |volume=55 |issue= 2 |pages= 91-7 |year= 2006 |pmid= 17075244 |doi= 10.2332/allergolint.55.91 }}
*{{cite journal  | author=Akbar GK, Dasari VR, Webb TE, ''et al.'' |title=Molecular cloning of a novel P2 purinoceptor from human erythroleukemia cells. |journal=J. Biol. Chem. |volume=271 |issue= 31 |pages= 18363-7 |year= 1996 |pmid= 8702478 |doi=  }}
*{{cite journal  | author=Hillier LD, Lennon G, Becker M, ''et al.'' |title=Generation and analysis of 280,000 human expressed sequence tags. |journal=Genome Res. |volume=6 |issue= 9 |pages= 807-28 |year= 1997 |pmid= 8889549 |doi=  }}
*{{cite journal  | author=Owman C, Nilsson C, Lolait SJ |title=Cloning of cDNA encoding a putative chemoattractant receptor. |journal=Genomics |volume=37 |issue= 2 |pages= 187-94 |year= 1997 |pmid= 8921391 |doi= 10.1006/geno.1996.0541 }}
*{{cite journal  | author=Yokomizo T, Izumi T, Chang K, ''et al.'' |title=A G-protein-coupled receptor for leukotriene B4 that mediates chemotaxis. |journal=Nature |volume=387 |issue= 6633 |pages= 620-4 |year= 1997 |pmid= 9177352 |doi= 10.1038/42506 }}
*{{cite journal  | author=Maier R, Glatz A, Mosbacher J, Bilbe G |title=Cloning of P2Y6 cDNAs and identification of a pseudogene: comparison of P2Y receptor subtype expression in bone and brain tissues. |journal=Biochem. Biophys. Res. Commun. |volume=237 |issue= 2 |pages= 297-302 |year= 1997 |pmid= 9268704 |doi= 10.1006/bbrc.1997.7135 }}
*{{cite journal  | author=Gaudreau R, Le Gouill C, Métaoui S, ''et al.'' |title=Signalling through the leukotriene B4 receptor involves both alphai and alpha16, but not alphaq or alpha11 G-protein subunits. |journal=Biochem. J. |volume=335 ( Pt 1) |issue=  |pages= 15-8 |year= 1998 |pmid= 9742207 |doi=  }}
*{{cite journal  | author=Kato K, Yokomizo T, Izumi T, Shimizu T |title=Cell-specific transcriptional regulation of human leukotriene B(4) receptor gene. |journal=J. Exp. Med. |volume=192 |issue= 3 |pages= 413-20 |year= 2000 |pmid= 10934229 |doi=  }}
*{{cite journal  | author=Yokomizo T, Kato K, Terawaki K, ''et al.'' |title=A second leukotriene B(4) receptor, BLT2. A new therapeutic target in inflammation and immunological disorders. |journal=J. Exp. Med. |volume=192 |issue= 3 |pages= 421-32 |year= 2000 |pmid= 10934230 |doi=  }}
*{{cite journal  | author=Stankova J, Turcotte S, Harris J, Rola-Pleszczynski M |title=Modulation of leukotriene B4 receptor-1 expression by dexamethasone: potential mechanism for enhanced neutrophil survival. |journal=J. Immunol. |volume=168 |issue= 7 |pages= 3570-6 |year= 2002 |pmid= 11907121 |doi=  }}
*{{cite journal  | author=Gaudreau R, Le Gouill C, Venne MH, ''et al.'' |title=Threonine 308 within a putative casein kinase 2 site of the cytoplasmic tail of leukotriene B(4) receptor (BLT1) is crucial for ligand-induced, G-protein-coupled receptor-specific kinase 6-mediated desensitization. |journal=J. Biol. Chem. |volume=277 |issue= 35 |pages= 31567-76 |year= 2002 |pmid= 12077128 |doi= 10.1074/jbc.M202723200 }}
*{{cite journal  | author=Hennig R, Ding XZ, Tong WG, ''et al.'' |title=5-Lipoxygenase and leukotriene B(4) receptor are expressed in human pancreatic cancers but not in pancreatic ducts in normal tissue. |journal=Am. J. Pathol. |volume=161 |issue= 2 |pages= 421-8 |year= 2002 |pmid= 12163367 |doi=  }}
*{{cite journal  | author=Ito N, Yokomizo T, Sasaki T, ''et al.'' |title=Requirement of phosphatidylinositol 3-kinase activation and calcium influx for leukotriene B4-induced enzyme release. |journal=J. Biol. Chem. |volume=277 |issue= 47 |pages= 44898-904 |year= 2003 |pmid= 12244116 |doi= 10.1074/jbc.M208051200 }}
*{{cite journal  | author=Tong WG, Ding XZ, Hennig R, ''et al.'' |title=Leukotriene B4 receptor antagonist LY293111 inhibits proliferation and induces apoptosis in human pancreatic cancer cells. |journal=Clin. Cancer Res. |volume=8 |issue= 10 |pages= 3232-42 |year= 2003 |pmid= 12374694 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Yokomizo T, Noiri E, Izumi T, Shimizu T |title=In vivo chemotaxis using CHO cells expressing human leukotriene B4 receptor. |journal=Adv. Exp. Med. Biol. |volume=507 |issue=  |pages= 357-61 |year= 2003 |pmid= 12664610 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 
  • INFO: Beginning work on RAPGEF3... {November 18, 2007 11:52:58 PM PST}
  • SEARCH REDIRECT: Control Box Found: RAPGEF3 {November 18, 2007 11:53:27 PM PST}
  • UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:53:30 PM PST}
  • UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:53:30 PM PST}
  • UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:53:30 PM PST}
  • UPDATED: Updated protein page: RAPGEF3 {November 18, 2007 11:53:37 PM PST}
  • INFO: Beginning work on RCC1... {November 18, 2007 11:40:59 PM PST}
  • SEARCH REDIRECT: Control Box Found: RCC1 {November 18, 2007 11:41:20 PM PST}
  • UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:41:21 PM PST}
  • UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:41:21 PM PST}
  • UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:41:21 PM PST}
  • UPDATED: Updated protein page: RCC1 {November 18, 2007 11:41:27 PM PST}
  • INFO: Beginning work on TPH2... {November 18, 2007 11:54:36 PM PST}
  • SEARCH REDIRECT: Control Box Found: TPH2 {November 18, 2007 11:55:05 PM PST}
  • UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:55:08 PM PST}
  • UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:55:08 PM PST}
  • UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:55:08 PM PST}
  • UPDATED: Updated protein page: TPH2 {November 18, 2007 11:55:14 PM PST}

end log.