User:ProteinBoxBot/PBB Log Wiki 11-8-2007-A2-3

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Contents 1 Log file for Protein Box Bot 2 Protein Status Quick Log - Date: 19:30, 17 November 2007 (UTC) 2.1 Proteins without matches (7) 2.2 Proteins with a High Potential Match (8) 2.3 Redirected Proteins (10) 2.4 Manual Inspection (Page not found) (15) 2.5 Updated (10) 3 Protein Status Grid - Date: 19:30, 17 November 2007 (UTC) 4 Vebose Log - Date: 19:30, 17 November 2007 (UTC) 4.1 CALCRL 4.2 CCL11 4.3 CTSS 4.4 DEFA1 4.5 DUSP1 4.6 ENPP1 4.7 FABP2 4.8 FES 4.9 FTH1 4.10 GCH1 4.11 HAMP 4.12 IL11 4.13 MICB 4.14 NOTCH3 4.15 PDGFA 4.16 PDX1 4.17 PTPRA 4.18 RANBP2 4.19 RANBP5 4.20 RUNX3 4.21 SDC4 4.22 TERC 4.23 TRADD 4.24 UTRN 4.25 WASL

[edit] Log file for Protein Box Bot

Log page index: User:ProteinBoxBot/PBB_Log_Index

[edit] Protein Status Quick Log - Date: 19:30, 17 November 2007 (UTC)

[edit] Proteins without matches (7)

DEFA1	NOTCH3	TERC	FES	WASL
ENPP1	CTSS

[edit] Proteins with a High Potential Match (8)

GCH1	HAMP	FTH1	UTRN	IL11
PTPRA	TRADD	CCL11

[edit] Redirected Proteins (10)

PDGFA	MICB	RANBP5	RUNX3	RANBP2
CALCRL	PDX1	FABP2	SDC4	DUSP1

[edit] Manual Inspection (Page not found) (15)

DEFA1	GCH1	NOTCH3	TERC	HAMP
FTH1	UTRN	FES	WASL	IL11
ENPP1	PTPRA	TRADD	CTSS	CCL11

[edit] Updated (10)

PDGFA	MICB	RANBP5	RUNX3	RANBP2
CALCRL	PDX1	FABP2	SDC4	DUSP1

[edit] Protein Status Grid - Date: 19:30, 17 November 2007 (UTC)

HUGO Symbol	Action Summary	Target page(s)	WP Symbol Search
DEFA1	Manual Inspection (Page not found)	Other Pages: Defensin (Unknown Data); DEFA1 (No Data); DEF1 (No Data); Def1 (No Data); DEFA2 (No Data); Defa2 (No Data); HNP-1 (No Data); Hnp-1 (No Data); HP-1 (No Data); Hp-1 (No Data); MGC138393 (No Data); Mgc138393 (No Data); MRS (DisAmbig); Mrs (Redirect -> Mrs.); DEF3 (No Data); Def3 (No Data); HNP-3 (No Data); Hnp-3 (No Data); HNP3 (No Data); Hnp3 (No Data); HP-3 (No Data); Hp-3 (No Data); Mrs. (Unknown Data);	[1]
GCH1	Manual Inspection (Page not found)	Other Pages: GTP cyclohydrolase 1 (Redirect -> GTP cyclohydrolase I); GCH1 (No Data); DYT5 (No Data); Dyt5 (No Data); GCH (DisAmbig); Gch (No Data); GTP-CH-1 (No Data); Gtp-ch-1 (No Data); GTPCH1 (No Data); Gtpch1 (No Data); GTP cyclohydrolase I (Protein Template);	[2]
NOTCH3	Manual Inspection (Page not found)	Other Pages: Notch homolog 3 (No Data); NOTCH3 (No Data); CADASIL (Unknown Data); Cadasil (Redirect -> CADASIL); CASIL (No Data); Casil (No Data);	[3]
TERC	Manual Inspection (Page not found)	Other Pages: Telomerase RNA component (No Data); TERC (Redirect -> Investigations in Numbers, Data, and Space); TR (DisAmbig); Tr (Redirect -> TR); SCARNA19 (No Data); Scarna19 (No Data); TRC3 (No Data); Trc3 (No Data); HTR (Redirect -> Very high temperature reactor); Htr (No Data); Investigations in Numbers, Data, and Space (Unknown Data); Very high temperature reactor (Unknown Data);	[4]
HAMP	Manual Inspection (Page not found)	Other Pages: Hepcidin antimicrobial peptide (No Data); HAMP (Redirect -> Hepcidin); HEPC (No Data); Hepc (No Data); HFE2B (No Data); Hfe2b (No Data); LEAP-1 (Redirect -> Hepcidin); Leap-1 (No Data); LEAP1 (No Data); Leap1 (No Data); Hepcidin (Protein Template);	[5]
PDGFA	Updated	Other Pages: Platelet-derived growth factor alpha polypeptide (No Data); PDGFA (Good Codes + Entrez Match); PDGF-A (No Data); Pdgf-a (No Data); PDGF1 (No Data); Pdgf1 (No Data);	[6]
MICB	Updated	Other Pages: MHC class I polypeptide-related sequence B (No Data); MICB (Good Codes + Entrez Match); PERB11.2 (No Data); Perb11.2 (No Data);	[7]
RANBP5	Updated	Other Pages: RAN binding protein 5 (No Data); RANBP5 (Good Codes + Entrez Match); DKFZp686O1576 (No Data); Dkfzp686o1576 (No Data); FLJ43041 (No Data); Flj43041 (No Data); IMB3 (No Data); Imb3 (No Data); IPO5 (No Data); Ipo5 (No Data); KPNB3 (No Data); Kpnb3 (No Data); MGC2068 (No Data); Mgc2068 (No Data);	[8]
RUNX3	Updated	Other Pages: Runt-related transcription factor 3 (No Data); RUNX3 (Good Codes + Entrez Match); AML2 (No Data); Aml2 (No Data); CBFA3 (No Data); Cbfa3 (No Data); FLJ34510 (No Data); Flj34510 (No Data); MGC16070 (No Data); Mgc16070 (No Data); PEBP2aC (No Data); Pebp2ac (No Data);	[9]
RANBP2	Updated	Other Pages: RAN binding protein 2 (No Data); RANBP2 (Good Codes + Entrez Match); TRP1 (No Data); Trp1 (No Data); NUP358 (No Data); Nup358 (No Data); TRP2 (No Data); Trp2 (No Data);	[10]
CALCRL	Updated	Other Pages: Calcitonin receptor-like (No Data); CALCRL (Good Codes + Entrez Match); CGRPR (No Data); Cgrpr (No Data); CRLR (No Data); Crlr (No Data);	[11]
FTH1	Manual Inspection (Page not found)	Other Pages: Ferritin (Protein Template); FTH1 (No Data); FTH (No Data); Fth (No Data); FTHL6 (No Data); Fthl6 (No Data); MGC104426 (No Data); Mgc104426 (No Data); PIG15 (No Data); Pig15 (No Data); PLIF (DisAmbig); Plif (No Data);	[12]
UTRN	Manual Inspection (Page not found)	Other Pages: Utrophin (Protein Template); UTRN (No Data); DRP1 (No Data); Drp1 (No Data); DMDL (No Data); Dmdl (No Data); DRP (DisAmbig); Drp (No Data); FLJ23678 (No Data); Flj23678 (No Data);	[13]
FES	Manual Inspection (Page not found)	Other Pages: Feline sarcoma oncogene (No Data); FES (DisAmbig); FPS (DisAmbig); Fps (Redirect -> FPS);	[14]
PDX1	Updated	Other Pages: Pancreatic and duodenal homeobox 1 (No Data); PDX1 (Good Codes + Entrez Match); IDX-1 (No Data); Idx-1 (No Data); IPF1 (No Data); Ipf1 (No Data); IUF1 (No Data); Iuf1 (No Data); MODY4 (No Data); Mody4 (No Data); PDX-1 (No Data); Pdx-1 (No Data); STF-1 (No Data); Stf-1 (No Data);	[15]
WASL	Manual Inspection (Page not found)	Other Pages: Wiskott-Aldrich syndrome-like (No Data); WASL (DisAmbig); DKFZp779G0847 (No Data); Dkfzp779g0847 (No Data); MGC48327 (No Data); Mgc48327 (No Data); N-WASP (No Data); N-wasp (No Data);	[16]
FABP2	Updated	Other Pages: Fatty acid binding protein 2 (No Data); FABP2 (Good Codes + Entrez Match); FABPI (No Data); Fabpi (No Data); I-FABP (No Data); I-fabp (No Data); MGC133132 (No Data); Mgc133132 (No Data);	[17]
IL11	Manual Inspection (Page not found)	Other Pages: Interleukin 11 (Protein Template); IL11 (No Data); AGIF (Redirect -> American GI Forum); Agif (No Data); IL-11 (Redirect -> interleukin 11); Il-11 (No Data); American GI Forum (Unknown Data);	[18]
ENPP1	Manual Inspection (Page not found)	Other Pages: Ectonucleotide pyrophosphatase/phosphodiesterase 1 (No Data); ENPP1 (No Data); M6S1 (No Data); M6s1 (No Data); NPP1 (No Data); Npp1 (No Data); NPPS (No Data); Npps (No Data); PC-1 (Redirect -> PC-1 (cable system)); Pc-1 (No Data); PCA1 (No Data); Pca1 (No Data); PDNP1 (No Data); Pdnp1 (No Data); PC-1 (cable system) (Unknown Data);	[19]
PTPRA	Manual Inspection (Page not found)	Other Pages: Protein tyrosine phosphatase (Protein Template); PTPRA (No Data); LRP (DisAmbig); Lrp (No Data); PTPA (No Data); Ptpa (No Data); HEPTP (No Data); Heptp (No Data); HLPR (No Data); Hlpr (No Data); HPTPA (No Data); Hptpa (No Data); HPTPalpha (No Data); Hptpalpha (No Data); PTPRL2 (No Data); Ptprl2 (No Data); R-PTP-alpha (No Data); R-ptp-alpha (No Data); RPTPA (No Data); Rptpa (No Data);	[20]
SDC4	Updated	Other Pages: Syndecan 4 (No Data); SDC4 (Good Codes + Entrez Match); MGC22217 (No Data); Mgc22217 (No Data); SYND4 (No Data); Synd4 (No Data);	[21]
TRADD	Manual Inspection (Page not found)	Other Pages: TNFRSF1A-associated via death domain (No Data); TRADD (Protein Template); Hs.89862 (No Data); MGC11078 (No Data); Mgc11078 (No Data);	[22]
DUSP1	Updated	Other Pages: Dual specificity phosphatase 1 (No Data); DUSP1 (Good Codes + Entrez Match); CL100 (No Data); Cl100 (No Data); HVH1 (No Data); Hvh1 (No Data); MKP-1 (No Data); Mkp-1 (No Data); PTPN10 (No Data); Ptpn10 (No Data);	[23]
CTSS	Manual Inspection (Page not found)	Other Pages: Cathepsin S (Redirect -> Cathepsin); CTSS (Redirect -> Compatible Time-Sharing System); MGC3886 (No Data); Mgc3886 (No Data); Cathepsin (Unknown Data); Compatible Time-Sharing System (Unknown Data);	[24]
CCL11	Manual Inspection (Page not found)	Other Pages: Chemokine ligand 11 (No Data); CCL11 (Protein Template); MGC22554 (No Data); Mgc22554 (No Data); SCYA11 (No Data); Scya11 (No Data);	[25]

[edit] Vebose Log - Date: 19:30, 17 November 2007 (UTC)

[edit] CALCRL

• INFO: Beginning work on CALCRL... {November 17, 2007 11:21:55 AM PST}
• SEARCH REDIRECT: Control Box Found: CALCRL {November 17, 2007 11:22:35 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:22:38 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:22:38 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:22:38 AM PST}
• UPDATED: Updated protein page: CALCRL {November 17, 2007 11:22:44 AM PST}

[edit] CCL11

• INFO: Beginning work on CCL11... {November 17, 2007 11:19:01 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:19:28 AM 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_CCL11_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1eot.
 | PDB = {{PDB2|1eot}}, {{PDB2|2eot}}
 | Name = Chemokine (C-C motif) ligand 11
 | HGNCid = 10610
 | Symbol = CCL11
 | AltSymbols =; MGC22554; SCYA11
 | OMIM = 601156
 | ECnumber =  
 | Homologene = 7929
 | MGIid = 103576
 | GeneAtlas_image1 = PBB_GE_CCL11_210133_at_tn.png
 | Function = {{GNF_GO|id=GO:0008009 |text = chemokine activity}} 
 | Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} 
 | Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006874 |text = cellular calcium ion homeostasis}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0006968 |text = cellular defense response}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0009314 |text = response to radiation}} {{GNF_GO|id=GO:0009615 |text = response to virus}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6356
    | Hs_Ensembl = ENSG00000172156
    | Hs_RefseqProtein = NP_002977
    | Hs_RefseqmRNA = NM_002986
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 29636800
    | Hs_GenLoc_end = 29639312
    | Hs_Uniprot = P51671
    | Mm_EntrezGene = 20292
    | Mm_Ensembl = ENSMUSG00000020676
    | Mm_RefseqmRNA = NM_011330
    | Mm_RefseqProtein = NP_035460
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 81874046
    | Mm_GenLoc_end = 81879144
    | Mm_Uniprot = Q5SVB5
  }}
}}
'''Chemokine (C-C motif) ligand 11''', also known as '''CCL11''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CCL11 chemokine (C-C motif) ligand 11| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6356| 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 one of several Cys-Cys (CC) cytokine genes clustered on the q-arm of chromosome 17. Cytokines are a family of secreted proteins involved in immunoregulatory and inflammatory processes. The CC cytokines are proteins characterized by two adjacent cysteines. The cytokine encoded by this gene displays chemotactic activity for eosinophils, but not mononuclear cells or neutrophils. This eosinophil specific chemokine assumed to be involved in eosinophilic inflammatory diseases such as atopic dermatitis, allergic rhinitis, asthma and parasitic infections.<ref name="entrez">{{cite web | title = Entrez Gene: CCL11 chemokine (C-C motif) ligand 11| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6356| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Garcia-Zepeda EA, Rothenberg ME, Ownbey RT, ''et al.'' |title=Human eotaxin is a specific chemoattractant for eosinophil cells and provides a new mechanism to explain tissue eosinophilia. |journal=Nat. Med. |volume=2 |issue= 4 |pages= 449-56 |year= 1996 |pmid= 8597956 |doi=  }}
*{{cite journal  | author=Ponath PD, Qin S, Ringler DJ, ''et al.'' |title=Cloning of the human eosinophil chemoattractant, eotaxin. Expression, receptor binding, and functional properties suggest a mechanism for the selective recruitment of eosinophils. |journal=J. Clin. Invest. |volume=97 |issue= 3 |pages= 604-12 |year= 1996 |pmid= 8609214 |doi=  }}
*{{cite journal  | author=Kitaura M, Nakajima T, Imai T, ''et al.'' |title=Molecular cloning of human eotaxin, an eosinophil-selective CC chemokine, and identification of a specific eosinophil eotaxin receptor, CC chemokine receptor 3. |journal=J. Biol. Chem. |volume=271 |issue= 13 |pages= 7725-30 |year= 1996 |pmid= 8631813 |doi=  }}
*{{cite journal  | author=Daugherty BL, Siciliano SJ, DeMartino JA, ''et al.'' |title=Cloning, expression, and characterization of the human eosinophil eotaxin receptor. |journal=J. Exp. Med. |volume=183 |issue= 5 |pages= 2349-54 |year= 1996 |pmid= 8642344 |doi=  }}
*{{cite journal  | author=Choe H, Farzan M, Sun Y, ''et al.'' |title=The beta-chemokine receptors CCR3 and CCR5 facilitate infection by primary HIV-1 isolates. |journal=Cell |volume=85 |issue= 7 |pages= 1135-48 |year= 1996 |pmid= 8674119 |doi=  }}
*{{cite journal  | author=Ponath PD, Qin S, Post TW, ''et al.'' |title=Molecular cloning and characterization of a human eotaxin receptor expressed selectively on eosinophils. |journal=J. Exp. Med. |volume=183 |issue= 6 |pages= 2437-48 |year= 1996 |pmid= 8676064 |doi=  }}
*{{cite journal  | author=Bartels J, Schlüter C, Richter E, ''et al.'' |title=Human dermal fibroblasts express eotaxin: molecular cloning, mRNA expression, and identification of eotaxin sequence variants. |journal=Biochem. Biophys. Res. Commun. |volume=225 |issue= 3 |pages= 1045-51 |year= 1996 |pmid= 8780731 |doi= 10.1006/bbrc.1996.1292 }}
*{{cite journal  | author=Garcia-Zepeda EA, Rothenberg ME, Weremowicz S, ''et al.'' |title=Genomic organization, complete sequence, and chromosomal location of the gene for human eotaxin (SCYA11), an eosinophil-specific CC chemokine. |journal=Genomics |volume=41 |issue= 3 |pages= 471-6 |year= 1997 |pmid= 9169149 |doi= 10.1006/geno.1997.4656 }}
*{{cite journal  | author=Hein H, Schlüter C, Kulke R, ''et al.'' |title=Genomic organization, sequence, and transcriptional regulation of the human eotaxin gene. |journal=Biochem. Biophys. Res. Commun. |volume=237 |issue= 3 |pages= 537-42 |year= 1997 |pmid= 9299399 |doi= 10.1006/bbrc.1997.7169 }}
*{{cite journal  | author=Nibbs RJ, Wylie SM, Yang J, ''et al.'' |title=Cloning and characterization of a novel promiscuous human beta-chemokine receptor D6. |journal=J. Biol. Chem. |volume=272 |issue= 51 |pages= 32078-83 |year= 1998 |pmid= 9405404 |doi=  }}
*{{cite journal  | author=Rubbert A, Combadiere C, Ostrowski M, ''et al.'' |title=Dendritic cells express multiple chemokine receptors used as coreceptors for HIV entry. |journal=J. Immunol. |volume=160 |issue= 8 |pages= 3933-41 |year= 1998 |pmid= 9558100 |doi=  }}
*{{cite journal  | author=Noso N, Bartels J, Mallet AI, ''et al.'' |title=Delayed production of biologically active O-glycosylated forms of human eotaxin by tumor-necrosis-factor-alpha-stimulated dermal fibroblasts. |journal=Eur. J. Biochem. |volume=253 |issue= 1 |pages= 114-22 |year= 1998 |pmid= 9578468 |doi=  }}
*{{cite journal  | author=Crump MP, Rajarathnam K, Kim KS, ''et al.'' |title=Solution structure of eotaxin, a chemokine that selectively recruits eosinophils in allergic inflammation. |journal=J. Biol. Chem. |volume=273 |issue= 35 |pages= 22471-9 |year= 1998 |pmid= 9712872 |doi=  }}
*{{cite journal  | author=Sabroe I, Hartnell A, Jopling LA, ''et al.'' |title=Differential regulation of eosinophil chemokine signaling via CCR3 and non-CCR3 pathways. |journal=J. Immunol. |volume=162 |issue= 5 |pages= 2946-55 |year= 1999 |pmid= 10072545 |doi=  }}
*{{cite journal  | author=Jinquan T, Quan S, Feili G, ''et al.'' |title=Eotaxin activates T cells to chemotaxis and adhesion only if induced to express CCR3 by IL-2 together with IL-4. |journal=J. Immunol. |volume=162 |issue= 7 |pages= 4285-92 |year= 1999 |pmid= 10201960 |doi=  }}
*{{cite journal  | author=Klein RS, Williams KC, Alvarez-Hernandez X, ''et al.'' |title=Chemokine receptor expression and signaling in macaque and human fetal neurons and astrocytes: implications for the neuropathogenesis of AIDS. |journal=J. Immunol. |volume=163 |issue= 3 |pages= 1636-46 |year= 1999 |pmid= 10415069 |doi=  }}
*{{cite journal  | author=Blanpain C, Migeotte I, Lee B, ''et al.'' |title=CCR5 binds multiple CC-chemokines: MCP-3 acts as a natural antagonist. |journal=Blood |volume=94 |issue= 6 |pages= 1899-905 |year= 1999 |pmid= 10477718 |doi=  }}
*{{cite journal  | author=Zhang J, Lathbury LJ, Salamonsen LA |title=Expression of the chemokine eotaxin and its receptor, CCR3, in human endometrium. |journal=Biol. Reprod. |volume=62 |issue= 2 |pages= 404-11 |year= 2000 |pmid= 10642580 |doi=  }}
*{{cite journal  | author=Kampen GT, Stafford S, Adachi T, ''et al.'' |title=Eotaxin induces degranulation and chemotaxis of eosinophils through the activation of ERK2 and p38 mitogen-activated protein kinases. |journal=Blood |volume=95 |issue= 6 |pages= 1911-7 |year= 2000 |pmid= 10706854 |doi=  }}
*{{cite journal  | author=Huber MA, Kraut N, Addicks T, Peter RU |title=Cell-type-dependent induction of eotaxin and CCR3 by ionizing radiation. |journal=Biochem. Biophys. Res. Commun. |volume=269 |issue= 2 |pages= 546-52 |year= 2000 |pmid= 10708591 |doi= 10.1006/bbrc.2000.2287 }}
}}
{{refend}}

{{protein-stub}}
 

[edit] CTSS

• INFO: Beginning work on CTSS... {November 17, 2007 11:08:28 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:08:56 AM 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_CTSS_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1glo.
 | PDB = {{PDB2|1glo}}, {{PDB2|1ms6}}, {{PDB2|1npz}}, {{PDB2|1nqc}}, {{PDB2|2c0y}}, {{PDB2|2f1g}}, {{PDB2|2fq9}}, {{PDB2|2fra}}, {{PDB2|2frq}}, {{PDB2|2ft2}}, {{PDB2|2fud}}, {{PDB2|2fye}}, {{PDB2|2g6d}}, {{PDB2|2g7y}}, {{PDB2|2h7j}}, {{PDB2|2hh5}}, {{PDB2|2hhn}}, {{PDB2|2hxz}}, {{PDB2|2op3}}
 | Name = Cathepsin S
 | HGNCid = 2545
 | Symbol = CTSS
 | AltSymbols =; MGC3886
 | OMIM = 116845
 | ECnumber =  
 | Homologene = 20867
 | MGIid = 107341
 | GeneAtlas_image1 = PBB_GE_CTSS_202902_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_CTSS_202901_x_at_tn.png
 | Function = {{GNF_GO|id=GO:0004218 |text = cathepsin S activity}} 
 | Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0016020 |text = membrane}} 
 | Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006955 |text = immune response}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1520
    | Hs_Ensembl = ENSG00000163131
    | Hs_RefseqProtein = NP_004070
    | Hs_RefseqmRNA = NM_004079
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 148969296
    | Hs_GenLoc_end = 149005057
    | Hs_Uniprot = P25774
    | Mm_EntrezGene = 13040
    | Mm_Ensembl = ENSMUSG00000038642
    | Mm_RefseqmRNA = NM_021281
    | Mm_RefseqProtein = NP_067256
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 95612190
    | Mm_GenLoc_end = 95641804
    | Mm_Uniprot = Q3U5K1
  }}
}}
'''Cathepsin S''', also known as '''CTSS''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CTSS cathepsin S| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1520| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = The protein encoded by this gene, a member of the peptidase C1 family, is a lysosomal cysteine proteinase that may participate in the degradation of antigenic proteins to peptides for presentation on MHC class II molecules. The encoded protein can function as an elastase over a broad pH range in alveolar macrophages. Transcript variants utilizing alternative polyadenylation signals exist for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: CTSS cathepsin S| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1520| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Shi GP, Munger JS, Meara JP, ''et al.'' |title=Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease. |journal=J. Biol. Chem. |volume=267 |issue= 11 |pages= 7258-62 |year= 1992 |pmid= 1373132 |doi=  }}
*{{cite journal  | author=Wiederanders B, Brömme D, Kirschke H, ''et al.'' |title=Phylogenetic conservation of cysteine proteinases. Cloning and expression of a cDNA coding for human cathepsin S. |journal=J. Biol. Chem. |volume=267 |issue= 19 |pages= 13708-13 |year= 1992 |pmid= 1377692 |doi=  }}
*{{cite journal  | author=Ritonja A, Colić A, Dolenc I, ''et al.'' |title=The complete amino acid sequence of bovine cathepsin S and a partial sequence of bovine cathepsin L. |journal=FEBS Lett. |volume=283 |issue= 2 |pages= 329-31 |year= 1991 |pmid= 2044774 |doi=  }}
*{{cite journal  | author=Munger JS, Haass C, Lemere CA, ''et al.'' |title=Lysosomal processing of amyloid precursor protein to A beta peptides: a distinct role for cathepsin S. |journal=Biochem. J. |volume=311 ( Pt 1) |issue=  |pages= 299-305 |year= 1995 |pmid= 7575468 |doi=  }}
*{{cite journal  | author=Lemere CA, Munger JS, Shi GP, ''et al.'' |title=The lysosomal cysteine protease, cathepsin S, is increased in Alzheimer's disease and Down syndrome brain. An immunocytochemical study. |journal=Am. J. Pathol. |volume=146 |issue= 4 |pages= 848-60 |year= 1995 |pmid= 7717452 |doi=  }}
*{{cite journal  | author=Hall A, Håkansson K, Mason RW, ''et al.'' |title=Structural basis for the biological specificity of cystatin C. Identification of leucine 9 in the N-terminal binding region as a selectivity-conferring residue in the inhibition of mammalian cysteine peptidases. |journal=J. Biol. Chem. |volume=270 |issue= 10 |pages= 5115-21 |year= 1995 |pmid= 7890620 |doi=  }}
*{{cite journal  | author=Balbín M, Hall A, Grubb A, ''et al.'' |title=Structural and functional characterization of two allelic variants of human cystatin D sharing a characteristic inhibition spectrum against mammalian cysteine proteinases. |journal=J. Biol. Chem. |volume=269 |issue= 37 |pages= 23156-62 |year= 1994 |pmid= 8083219 |doi=  }}
*{{cite journal  | author=Shi GP, Webb AC, Foster KE, ''et al.'' |title=Human cathepsin S: chromosomal localization, gene structure, and tissue distribution. |journal=J. Biol. Chem. |volume=269 |issue= 15 |pages= 11530-6 |year= 1994 |pmid= 8157683 |doi=  }}
*{{cite journal  | author=Turk B, Stoka V, Turk V, ''et al.'' |title=High-molecular-weight kininogen binds two molecules of cysteine proteinases with different rate constants. |journal=FEBS Lett. |volume=391 |issue= 1-2 |pages= 109-12 |year= 1996 |pmid= 8706894 |doi=  }}
*{{cite journal  | author=Baumgrass R, Williamson MK, Price PA |title=Identification of peptide fragments generated by digestion of bovine and human osteocalcin with the lysosomal proteinases cathepsin B, D, L, H, and S. |journal=J. Bone Miner. Res. |volume=12 |issue= 3 |pages= 447-55 |year= 1997 |pmid= 9076588 |doi=  }}
*{{cite journal  | author=Würl P, Taubert H, Meye A, ''et al.'' |title=Immunohistochemical and clinical evaluation of cathepsin expression in soft tissue sarcomas. |journal=Virchows Arch. |volume=430 |issue= 3 |pages= 221-5 |year= 1997 |pmid= 9099979 |doi=  }}
*{{cite journal  | author=Gelb BD, Shi GP, Heller M, ''et al.'' |title=Structure and chromosomal assignment of the human cathepsin K gene. |journal=Genomics |volume=41 |issue= 2 |pages= 258-62 |year= 1997 |pmid= 9143502 |doi= 10.1006/geno.1997.4631 }}
*{{cite journal  | author=Baldassare JJ, Henderson PA, Tarver A, Fisher GJ |title=Thrombin activation of human platelets dissociates a complex containing gelsolin and actin from phosphatidylinositide-specific phospholipase Cgamma1. |journal=Biochem. J. |volume=324 ( Pt 1) |issue=  |pages= 283-7 |year= 1997 |pmid= 9164868 |doi=  }}
*{{cite journal  | author=Nissler K, Kreusch S, Rommerskirch W, ''et al.'' |title=Sorting of non-glycosylated human procathepsin S in mammalian cells. |journal=Biol. Chem. |volume=379 |issue= 2 |pages= 219-24 |year= 1998 |pmid= 9524075 |doi=  }}
*{{cite journal  | author=Claus V, Jahraus A, Tjelle T, ''et al.'' |title=Lysosomal enzyme trafficking between phagosomes, endosomes, and lysosomes in J774 macrophages. Enrichment of cathepsin H in early endosomes. |journal=J. Biol. Chem. |volume=273 |issue= 16 |pages= 9842-51 |year= 1998 |pmid= 9545324 |doi=  }}
*{{cite journal  | author=Schick C, Pemberton PA, Shi GP, ''et al.'' |title=Cross-class inhibition of the cysteine proteinases cathepsins K, L, and S by the serpin squamous cell carcinoma antigen 1: a kinetic analysis. |journal=Biochemistry |volume=37 |issue= 15 |pages= 5258-66 |year= 1998 |pmid= 9548757 |doi= 10.1021/bi972521d }}
*{{cite journal  | author=Fengler A, Brandt W |title=Three-dimensional structures of the cysteine proteases cathepsins K and S deduced by knowledge-based modelling and active site characteristics. |journal=Protein Eng. |volume=11 |issue= 11 |pages= 1007-13 |year= 1999 |pmid= 9876921 |doi=  }}
*{{cite journal  | author=Söderström M, Salminen H, Glumoff V, ''et al.'' |title=Cathepsin expression during skeletal development. |journal=Biochim. Biophys. Acta |volume=1446 |issue= 1-2 |pages= 35-46 |year= 1999 |pmid= 10395917 |doi=  }}
*{{cite journal  | author=Cao H, Hegele RA |title=Human cathepsin S gene (CTSS) promoter -25G/A polymorphism. |journal=J. Hum. Genet. |volume=45 |issue= 2 |pages= 94-5 |year= 2000 |pmid= 10721671 |doi=  }}
*{{cite journal  | author=Luke C, Schick C, Tsu C, ''et al.'' |title=Simple modifications of the serpin reactive site loop convert SCCA2 into a cysteine proteinase inhibitor: a critical role for the P3' proline in facilitating RSL cleavage. |journal=Biochemistry |volume=39 |issue= 24 |pages= 7081-91 |year= 2000 |pmid= 10852705 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] DEFA1

• INFO: Beginning work on DEFA1... {November 17, 2007 11:08:56 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:09:42 AM 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_DEFA1_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dfn.
 | PDB = {{PDB2|1dfn}}, {{PDB2|1zmh}}, {{PDB2|1zmi}}, {{PDB2|1zmk}}, {{PDB2|2pm1}}, {{PDB2|2pm4}}, {{PDB2|2pm5}}
 | Name = Defensin, alpha 1
 | HGNCid = 2761
 | Symbol = DEFA1
 | AltSymbols =; DEF1; DEFA2; HNP-1; HP-1; MGC138393; MRS; DEF3; HNP-3; HNP3; HP-3
 | OMIM = 125220
 | ECnumber =  
 | Homologene = 37877
 | MGIid =  
 | GeneAtlas_image1 = PBB_GE_DEFA1_205033_s_at_tn.png
 | Function = 
 | Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} 
 | Process = {{GNF_GO|id=GO:0006805 |text = xenobiotic metabolic process}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0009615 |text = response to virus}} {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}} {{GNF_GO|id=GO:0050832 |text = defense response to fungus}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1667
    | Hs_Ensembl = ENSG00000185918
    | Hs_RefseqProtein = NP_004075
    | Hs_RefseqmRNA = NM_004084
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 8
    | Hs_GenLoc_start = 6860801
    | Hs_GenLoc_end = 6863233
    | Hs_Uniprot = P59666
    | Mm_EntrezGene =  
    | Mm_Ensembl =  
    | Mm_RefseqmRNA =  
    | Mm_RefseqProtein =  
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr =  
    | Mm_GenLoc_start =  
    | Mm_GenLoc_end =  
    | Mm_Uniprot =  
  }}
}}
'''Defensin, alpha 1''', also known as '''DEFA1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DEFA1 defensin, alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1667| 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 = Defensins are a family of microbicidal and cytotoxic peptides thought to be involved in host defense. They are abundant in the granules of neutrophils and also found in the epithelia of mucosal surfaces such as those of the intestine, respiratory tract, urinary tract, and vagina. Members of the defensin family are highly similar in protein sequence and distinguished by a conserved cysteine motif. Several alpha defensin genes appear to be clustered on chromosome 8. The protein encoded by this gene, defensin, alpha 1, is found in the microbicidal granules of neutrophils and likely plays a role in phagocyte-mediated host defense. It differs from defensin, alpha 3 by only one amino acid.<ref name="entrez">{{cite web | title = Entrez Gene: DEFA1 defensin, alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1667| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Lehrer RI, Lichtenstein AK, Ganz T |title=Defensins: antimicrobial and cytotoxic peptides of mammalian cells. |journal=Annu. Rev. Immunol. |volume=11 |issue=  |pages= 105-28 |year= 1993 |pmid= 8476558 |doi= 10.1146/annurev.iy.11.040193.000541 }}
*{{cite journal  | author=Corda D, Di Girolamo M |title=Mono-ADP-ribosylation: a tool for modulating immune response and cell signaling. |journal=Sci. STKE |volume=2002 |issue= 163 |pages= PE53 |year= 2003 |pmid= 12488509 |doi= 10.1126/stke.2002.163.pe53 }}
*{{cite journal  | author=Valore EV, Ganz T |title=Posttranslational processing of defensins in immature human myeloid cells. |journal=Blood |volume=79 |issue= 6 |pages= 1538-44 |year= 1992 |pmid= 1339298 |doi=  }}
*{{cite journal  | author=Zhang XL, Selsted ME, Pardi A |title=NMR studies of defensin antimicrobial peptides. 1. Resonance assignment and secondary structure determination of rabbit NP-2 and human HNP-1. |journal=Biochemistry |volume=31 |issue= 46 |pages= 11348-56 |year= 1992 |pmid= 1445872 |doi=  }}
*{{cite journal  | author=Pardi A, Zhang XL, Selsted ME, ''et al.'' |title=NMR studies of defensin antimicrobial peptides. 2. Three-dimensional structures of rabbit NP-2 and human HNP-1. |journal=Biochemistry |volume=31 |issue= 46 |pages= 11357-64 |year= 1992 |pmid= 1445873 |doi=  }}
*{{cite journal  | author=Hill CP, Yee J, Selsted ME, Eisenberg D |title=Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization. |journal=Science |volume=251 |issue= 5000 |pages= 1481-5 |year= 1991 |pmid= 2006422 |doi=  }}
*{{cite journal  | author=Bateman A, Singh A, Shustik C, ''et al.'' |title=The isolation and identification of multiple forms of the neutrophil granule peptides from human leukemic cells. |journal=J. Biol. Chem. |volume=266 |issue= 12 |pages= 7524-30 |year= 1991 |pmid= 2019582 |doi=  }}
*{{cite journal  | author=Wagner MJ, Ge Y, Siciliano M, Wells DE |title=A hybrid cell mapping panel for regional localization of probes to human chromosome 8. |journal=Genomics |volume=10 |issue= 1 |pages= 114-25 |year= 1991 |pmid= 2045096 |doi=  }}
*{{cite journal  | author=Sparkes RS, Kronenberg M, Heinzmann C, ''et al.'' |title=Assignment of defensin gene(s) to human chromosome 8p23. |journal=Genomics |volume=5 |issue= 2 |pages= 240-4 |year= 1989 |pmid= 2793180 |doi=  }}
*{{cite journal  | author=Selsted ME, Harwig SS |title=Determination of the disulfide array in the human defensin HNP-2. A covalently cyclized peptide. |journal=J. Biol. Chem. |volume=264 |issue= 7 |pages= 4003-7 |year= 1989 |pmid= 2917986 |doi=  }}
*{{cite journal  | author=Wiedemann LM, Francis GE, Lamb RF, ''et al.'' |title=Differentiation stage-specific expression of a gene during granulopoiesis. |journal=Leukemia |volume=3 |issue= 3 |pages= 227-34 |year= 1989 |pmid= 2918759 |doi=  }}
*{{cite journal  | author=Ganz T, Selsted ME, Szklarek D, ''et al.'' |title=Defensins. Natural peptide antibiotics of human neutrophils. |journal=J. Clin. Invest. |volume=76 |issue= 4 |pages= 1427-35 |year= 1985 |pmid= 2997278 |doi=  }}
*{{cite journal  | author=Daher KA, Lehrer RI, Ganz T, Kronenberg M |title=Isolation and characterization of human defensin cDNA clones. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 19 |pages= 7327-31 |year= 1988 |pmid= 3174637 |doi=  }}
*{{cite journal  | author=Mars WM, van Tuinen P, Drabkin HA, ''et al.'' |title=A myeloid-related sequence that localizes to human chromosome 8q21.1-22. |journal=Blood |volume=71 |issue= 6 |pages= 1713-9 |year= 1988 |pmid= 3370315 |doi=  }}
*{{cite journal  | author=Selsted ME, Harwig SS, Ganz T, ''et al.'' |title=Primary structures of three human neutrophil defensins. |journal=J. Clin. Invest. |volume=76 |issue= 4 |pages= 1436-9 |year= 1985 |pmid= 4056036 |doi=  }}
*{{cite journal  | author=Panyutich AV, Hiemstra PS, van Wetering S, Ganz T |title=Human neutrophil defensin and serpins form complexes and inactivate each other. |journal=Am. J. Respir. Cell Mol. Biol. |volume=12 |issue= 3 |pages= 351-7 |year= 1995 |pmid= 7873202 |doi=  }}
*{{cite journal  | author=Date Y, Nakazato M, Shiomi K, ''et al.'' |title=Localization of human neutrophil peptide (HNP) and its messenger RNA in neutrophil series. |journal=Ann. Hematol. |volume=69 |issue= 2 |pages= 73-7 |year= 1994 |pmid= 8080882 |doi=  }}
*{{cite journal  | author=Linzmeier R, Michaelson D, Liu L, Ganz T |title=The structure of neutrophil defensin genes. |journal=FEBS Lett. |volume=326 |issue= 1-3 |pages= 299-300 |year= 1993 |pmid= 8325384 |doi=  }}
*{{cite journal  | author=Linzmeier R, Michaelson D, Liu L, Ganz T |title=The structure of neutrophil defensin genes. |journal=FEBS Lett. |volume=321 |issue= 2-3 |pages= 267-73 |year= 1993 |pmid= 8477861 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] DUSP1

• INFO: Beginning work on DUSP1... {November 17, 2007 11:09:42 AM PST}
• SEARCH REDIRECT: Control Box Found: DUSP1 {November 17, 2007 11:10:15 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:10:18 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:10:18 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:10:18 AM PST}
• UPDATED: Updated protein page: DUSP1 {November 17, 2007 11:10:25 AM PST}

[edit] ENPP1

• INFO: Beginning work on ENPP1... {November 17, 2007 11:16:30 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:17:41 AM 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 = Ectonucleotide pyrophosphatase/phosphodiesterase 1
 | HGNCid = 3356
 | Symbol = ENPP1
 | AltSymbols =; M6S1; NPP1; NPPS; PC-1; PCA1; PDNP1
 | OMIM = 173335
 | ECnumber =  
 | Homologene = 38151
 | MGIid = 97370
 | GeneAtlas_image1 = PBB_GE_ENPP1_205066_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_ENPP1_205065_at_tn.png
 | Function = {{GNF_GO|id=GO:0003676 |text = nucleic acid binding}} {{GNF_GO|id=GO:0004519 |text = endonuclease activity}} {{GNF_GO|id=GO:0004528 |text = phosphodiesterase I activity}} {{GNF_GO|id=GO:0004551 |text = nucleotide diphosphatase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} 
 | Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} 
 | Process = {{GNF_GO|id=GO:0006091 |text = generation of precursor metabolites and energy}} {{GNF_GO|id=GO:0006796 |text = phosphate metabolic process}} {{GNF_GO|id=GO:0007584 |text = response to nutrient}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0009117 |text = nucleotide metabolic process}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5167
    | Hs_Ensembl = ENSG00000197594
    | Hs_RefseqProtein = NP_006199
    | Hs_RefseqmRNA = NM_006208
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 132170849
    | Hs_GenLoc_end = 132257988
    | Hs_Uniprot = P22413
    | Mm_EntrezGene = 18605
    | Mm_Ensembl = ENSMUSG00000037370
    | Mm_RefseqmRNA = NM_008813
    | Mm_RefseqProtein = NP_032839
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 24330827
    | Mm_GenLoc_end = 24401518
    | Mm_Uniprot = Q3V3C8
  }}
}}
'''Ectonucleotide pyrophosphatase/phosphodiesterase 1''', also known as '''ENPP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ENPP1 ectonucleotide pyrophosphatase/phosphodiesterase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5167| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = This gene is a member of the ecto-nucleotide pyrophosphatase/phosphodiesterase (ENPP) family. The encoded protein is a type II transmembrane glycoprotein comprising two identical disulfide-bonded subunits. This protein has broad specificity and cleaves a variety of substrates, including phosphodiester bonds of nucleotides and nucleotide sugars and pyrophosphate bonds of nucleotides and nucleotide sugars. This protein may function to hydrolyze nucleoside 5' triphosphates to their corresponding monophosphates and may also hydrolyze diadenosine polyphosphates. Mutations in this gene have been associated with 'idiopathic' infantile arterial calcification, ossification of the posterior longitudinal ligament of the spine (OPLL), and insulin resistance.<ref name="entrez">{{cite web | title = Entrez Gene: ENPP1 ectonucleotide pyrophosphatase/phosphodiesterase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5167| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Abate N, Chandalia M, Di Paola R, ''et al.'' |title=Mechanisms of disease: Ectonucleotide pyrophosphatase phosphodiesterase 1 as a 'gatekeeper' of insulin receptors. |journal=Nature clinical practice. Endocrinology & metabolism |volume=2 |issue= 12 |pages= 694-701 |year= 2007 |pmid= 17143316 |doi= 10.1038/ncpendmet0367 }}
*{{cite journal  | author=Bacci S, De Cosmo S, Prudente S, Trischitta V |title=ENPP1 gene, insulin resistance and related clinical outcomes. |journal=Current opinion in clinical nutrition and metabolic care |volume=10 |issue= 4 |pages= 403-9 |year= 2007 |pmid= 17563456 |doi= 10.1097/MCO.0b013e3281e386c9 }}
*{{cite journal  | author=Fadini GP, Pauletto P, Avogaro A, Rattazzi M |title=The good and the bad in the link between insulin resistance and vascular calcification. |journal=Atherosclerosis |volume=193 |issue= 2 |pages= 241-4 |year= 2007 |pmid= 17606264 |doi= 10.1016/j.atherosclerosis.2007.05.015 }}
*{{cite journal  | author=Funakoshi I, Kato H, Horie K, ''et al.'' |title=Molecular cloning of cDNAs for human fibroblast nucleotide pyrophosphatase. |journal=Arch. Biochem. Biophys. |volume=295 |issue= 1 |pages= 180-7 |year= 1992 |pmid= 1315502 |doi=  }}
*{{cite journal  | author=Buckley MF, Loveland KA, McKinstry WJ, ''et al.'' |title=Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human molecule, amino acid sequence, and chromosomal location. |journal=J. Biol. Chem. |volume=265 |issue= 29 |pages= 17506-11 |year= 1990 |pmid= 2211644 |doi=  }}
*{{cite journal  | author=Belli SI, Mercuri FA, Sali A, Goding JW |title=Autophosphorylation of PC-1 (alkaline phosphodiesterase I/nucleotide pyrophosphatase) and analysis of the active site. |journal=Eur. J. Biochem. |volume=228 |issue= 3 |pages= 669-76 |year= 1995 |pmid= 7737162 |doi=  }}
*{{cite journal  | author=Maddux BA, Sbraccia P, Kumakura S, ''et al.'' |title=Membrane glycoprotein PC-1 and insulin resistance in non-insulin-dependent diabetes mellitus. |journal=Nature |volume=373 |issue= 6513 |pages= 448-51 |year= 1995 |pmid= 7830796 |doi= 10.1038/373448a0 }}
*{{cite journal  | author=Belli SI, Goding JW |title=Biochemical characterization of human PC-1, an enzyme possessing alkaline phosphodiesterase I and nucleotide pyrophosphatase activities. |journal=Eur. J. Biochem. |volume=226 |issue= 2 |pages= 433-43 |year= 1995 |pmid= 8001561 |doi=  }}
*{{cite journal  | author=Huang R, Rosenbach M, Vaughn R, ''et al.'' |title=Expression of the murine plasma cell nucleotide pyrophosphohydrolase PC-1 is shared by human liver, bone, and cartilage cells. Regulation of PC-1 expression in osteosarcoma cells by transforming growth factor-beta. |journal=J. Clin. Invest. |volume=94 |issue= 2 |pages= 560-7 |year= 1994 |pmid= 8040311 |doi=  }}
*{{cite journal  | author=Jin-Hua P, Goding JW, Nakamura H, Sano K |title=Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. |journal=Genomics |volume=45 |issue= 2 |pages= 412-5 |year= 1998 |pmid= 9344668 |doi= 10.1006/geno.1997.4949 }}
*{{cite journal  | author=Nakamura I, Ikegawa S, Okawa A, ''et al.'' |title=Association of the human NPPS gene with ossification of the posterior longitudinal ligament of the spine (OPLL). |journal=Hum. Genet. |volume=104 |issue= 6 |pages= 492-7 |year= 1999 |pmid= 10453738 |doi=  }}
*{{cite journal  | author=Pizzuti A, Frittitta L, Argiolas A, ''et al.'' |title=A polymorphism (K121Q) of the human glycoprotein PC-1 gene coding region is strongly associated with insulin resistance. |journal=Diabetes |volume=48 |issue= 9 |pages= 1881-4 |year= 1999 |pmid= 10480624 |doi=  }}
*{{cite journal  | author=Andoh K, Piao JH, Terashima K, ''et al.'' |title=Genomic structure and promoter analysis of the ecto-phosphodiesterase I gene (PDNP3) expressed in glial cells. |journal=Biochim. Biophys. Acta |volume=1446 |issue= 3 |pages= 213-24 |year= 1999 |pmid= 10524196 |doi=  }}
*{{cite journal  | author=Maddux BA, Goldfine ID |title=Membrane glycoprotein PC-1 inhibition of insulin receptor function occurs via direct interaction with the receptor alpha-subunit. |journal=Diabetes |volume=49 |issue= 1 |pages= 13-9 |year= 2000 |pmid= 10615944 |doi=  }}
*{{cite journal  | author=Rutsch F, Vaingankar S, Johnson K, ''et al.'' |title=PC-1 nucleoside triphosphate pyrophosphohydrolase deficiency in idiopathic infantile arterial calcification. |journal=Am. J. Pathol. |volume=158 |issue= 2 |pages= 543-54 |year= 2001 |pmid= 11159191 |doi=  }}
*{{cite journal  | author=Frittitta L, Baratta R, Spampinato D, ''et al.'' |title=The Q121 PC-1 variant and obesity have additive and independent effects in causing insulin resistance. |journal=J. Clin. Endocrinol. Metab. |volume=86 |issue= 12 |pages= 5888-91 |year= 2001 |pmid= 11739459 |doi=  }}
*{{cite journal  | author=Koshizuka Y, Kawaguchi H, Ogata N, ''et al.'' |title=Nucleotide pyrophosphatase gene polymorphism associated with ossification of the posterior longitudinal ligament of the spine. |journal=J. Bone Miner. Res. |volume=17 |issue= 1 |pages= 138-44 |year= 2002 |pmid= 11771660 |doi=  }}
*{{cite journal  | author=de Azevedo MJ, Dalmáz CA, Caramori ML, ''et al.'' |title=ACE and PC-1 gene polymorphisms in normoalbuminuric Type 1 diabetic patients: a 10-year prospective study. |journal=J. Diabetes Complicat. |volume=16 |issue= 4 |pages= 255-62 |year= 2003 |pmid= 12126783 |doi=  }}
*{{cite journal  | author=De Cosmo S, Miscio G, Zucaro L, ''et al.'' |title=The role of PC-1 and ACE genes in diabetic nephropathy in type 1 diabetic patients: evidence for a polygenic control of kidney disease progression. |journal=Nephrol. Dial. Transplant. |volume=17 |issue= 8 |pages= 1402-7 |year= 2003 |pmid= 12147786 |doi=  }}
*{{cite journal  | author=Jacobsen P, Grarup N, Tarnow L, ''et al.'' |title=PC-1 amino acid variant (K121Q) has no impact on progression of diabetic nephropathy in type 1 diabetic patients. |journal=Nephrol. Dial. Transplant. |volume=17 |issue= 8 |pages= 1408-12 |year= 2003 |pmid= 12147787 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] FABP2

• INFO: Beginning work on FABP2... {November 17, 2007 11:10:26 AM PST}
• SEARCH REDIRECT: Control Box Found: FABP2 {November 17, 2007 11:10:51 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:10:53 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:10:53 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:10:53 AM PST}
• UPDATED: Updated protein page: FABP2 {November 17, 2007 11:10:58 AM PST}

[edit] FES

• INFO: Beginning work on FES... {November 17, 2007 11:10:58 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:11:19 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_FES_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1wqu.
 | PDB = {{PDB2|1wqu}}, {{PDB2|2dcr}}
 | Name = Feline sarcoma oncogene
 | HGNCid = 3657
 | Symbol = FES
 | AltSymbols =; FPS
 | OMIM = 190030
 | ECnumber =  
 | Homologene = 37563
 | MGIid = 95514
 | GeneAtlas_image1 = PBB_GE_FES_205418_at_tn.png
 | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} 
 | Component = 
 | Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2242
    | Hs_Ensembl = ENSG00000182511
    | Hs_RefseqProtein = NP_001996
    | Hs_RefseqmRNA = NM_002005
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 15
    | Hs_GenLoc_start = 89228713
    | Hs_GenLoc_end = 89240010
    | Hs_Uniprot = P07332
    | Mm_EntrezGene = 14159
    | Mm_Ensembl = ENSMUSG00000053158
    | Mm_RefseqmRNA = XM_981464
    | Mm_RefseqProtein = XP_986558
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 80251268
    | Mm_GenLoc_end = 80261449
    | Mm_Uniprot = Q3TD20
  }}
}}
'''Feline sarcoma oncogene''', also known as '''FES''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FES feline sarcoma oncogene| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2242| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = This gene encodes the human cellular counterpart of a feline sarcoma retrovirus protein with transforming capabilities. The gene product has tyrosine-specific protein kinase activity and that activity is required for maintenance of cellular transformation. Its chromosomal location has linked it to a specific translocation event identified in patients with acute promyelocytic leukemia but it is also involved in normal hematopoiesis. A truncated transcript has been identified that is generated utilizing a start site in one of the far downstream exons but a protein product associated with this transcript has not been identified.<ref name="entrez">{{cite web | title = Entrez Gene: FES feline sarcoma oncogene| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2242| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Smithgall TE, Rogers JA, Peters KL, ''et al.'' |title=The c-Fes family of protein-tyrosine kinases. |journal=Critical reviews in oncogenesis |volume=9 |issue= 1 |pages= 43-62 |year= 1998 |pmid= 9754447 |doi=  }}
*{{cite journal  | author=Jiang H, Harris MB, Rothman P |title=IL-4/IL-13 signaling beyond JAK/STAT. |journal=J. Allergy Clin. Immunol. |volume=105 |issue= 6 Pt 1 |pages= 1063-70 |year= 2000 |pmid= 10856136 |doi=  }}
*{{cite journal  | author=Greer P |title=Closing in on the biological functions of Fps/Fes and Fer. |journal=Nat. Rev. Mol. Cell Biol. |volume=3 |issue= 4 |pages= 278-89 |year= 2002 |pmid= 11994747 |doi= 10.1038/nrm783 }}
*{{cite journal  | author=Jücker M, Roebroek AJ, Mautner J, ''et al.'' |title=Expression of truncated transcripts of the proto-oncogene c-fps/fes in human lymphoma and lymphoid leukemia cell lines. |journal=Oncogene |volume=7 |issue= 5 |pages= 943-52 |year= 1992 |pmid= 1373879 |doi=  }}
*{{cite journal  | author=Polymeropoulos MH, Rath DS, Xiao H, Merril CR |title=Tetranucleotide repeat polymorphism at the human c-fes/fps proto-oncogene (FES). |journal=Nucleic Acids Res. |volume=19 |issue= 14 |pages= 4018 |year= 1991 |pmid= 1862005 |doi=  }}
*{{cite journal  | author=Bowden DW, Akots G, Rothschild CB |title=An insertion deletion polymorphism associated with C-FES. |journal=Nucleic Acids Res. |volume=19 |issue= 15 |pages= 4311 |year= 1991 |pmid= 1870997 |doi=  }}
*{{cite journal  | author=Alcalay M, Antolini F, Van de Ven WJ, ''et al.'' |title=Characterization of human and mouse c-fes cDNA clones and identification of the 5' end of the gene. |journal=Oncogene |volume=5 |issue= 3 |pages= 267-75 |year= 1990 |pmid= 2179816 |doi=  }}
*{{cite journal  | author=MacDonald I, Levy J, Pawson T |title=Expression of the mammalian c-fes protein in hematopoietic cells and identification of a distinct fes-related protein. |journal=Mol. Cell. Biol. |volume=5 |issue= 10 |pages= 2543-51 |year= 1986 |pmid= 2426571 |doi=  }}
*{{cite journal  | author=Roebroek AJ, Schalken JA, Bussemakers MJ, ''et al.'' |title=Characterization of human c-fes/fps reveals a new transcription unit (fur) in the immediately upstream region of the proto-oncogene. |journal=Mol. Biol. Rep. |volume=11 |issue= 2 |pages= 117-25 |year= 1986 |pmid= 3488499 |doi=  }}
*{{cite journal  | author=Emilia G, Donelli A, Ferrari S, ''et al.'' |title=Cellular levels of mRNA from c-myc, c-myb and c-fes onc-genes in normal myeloid and erythroid precursors of human bone marrow: an in situ hybridization study. |journal=Br. J. Haematol. |volume=62 |issue= 2 |pages= 287-92 |year= 1986 |pmid= 3947550 |doi=  }}
*{{cite journal  | author=Roebroek AJ, Schalken JA, Verbeek JS, ''et al.'' |title=The structure of the human c-fes/fps proto-oncogene. |journal=EMBO J. |volume=4 |issue= 11 |pages= 2897-903 |year= 1986 |pmid= 4065096 |doi=  }}
*{{cite journal  | author=Hampe A, Laprevotte I, Galibert F, ''et al.'' |title=Nucleotide sequences of feline retroviral oncogenes (v-fes) provide evidence for a family of tyrosine-specific protein kinase genes. |journal=Cell |volume=30 |issue= 3 |pages= 775-85 |year= 1983 |pmid= 6183005 |doi=  }}
*{{cite journal  | author=Wong-Staal F, Dalla-Favera R, Franchini G, ''et al.'' |title=Three distinct genes in human DNA related to the transforming genes of mammalian sarcoma retroviruses. |journal=Science |volume=213 |issue= 4504 |pages= 226-8 |year= 1981 |pmid= 6264598 |doi=  }}
*{{cite journal  | author=Jhanwar SC, Neel BG, Hayward WS, Chaganti RS |title=Localization of the cellular oncogenes ABL, SIS, and FES on human germ-line chromosomes. |journal=Cytogenet. Cell Genet. |volume=38 |issue= 1 |pages= 73-5 |year= 1984 |pmid= 6323103 |doi=  }}
*{{cite journal  | author=Izuhara K, Feldman RA, Greer P, Harada N |title=Interaction of the c-fes proto-oncogene product with the interleukin-4 receptor. |journal=J. Biol. Chem. |volume=269 |issue= 28 |pages= 18623-9 |year= 1994 |pmid= 7518439 |doi=  }}
*{{cite journal  | author=Greer P, Haigh J, Mbamalu G, ''et al.'' |title=The Fps/Fes protein-tyrosine kinase promotes angiogenesis in transgenic mice. |journal=Mol. Cell. Biol. |volume=14 |issue= 10 |pages= 6755-63 |year= 1994 |pmid= 7523858 |doi=  }}
*{{cite journal  | author=Maru Y, Peters KL, Afar DE, ''et al.'' |title=Tyrosine phosphorylation of BCR by FPS/FES protein-tyrosine kinases induces association of BCR with GRB-2/SOS. |journal=Mol. Cell. Biol. |volume=15 |issue= 2 |pages= 835-42 |year= 1995 |pmid= 7529874 |doi=  }}
*{{cite journal  | author=Hjermstad SJ, Briggs SD, Smithgall TE |title=Phosphorylation of the ras GTPase-activating protein (GAP) by the p93c-fes protein-tyrosine kinase in vitro and formation of GAP-fes complexes via an SH2 domain-dependent mechanism. |journal=Biochemistry |volume=32 |issue= 39 |pages= 10519-25 |year= 1993 |pmid= 7691175 |doi=  }}
*{{cite journal  | author=Yates KE, Lynch MR, Wong SG, ''et al.'' |title=Human c-FES is a nuclear tyrosine kinase. |journal=Oncogene |volume=10 |issue= 6 |pages= 1239-42 |year= 1995 |pmid= 7700650 |doi=  }}
*{{cite journal  | author=Areces LB, Dello Sbarba P, Jücker M, ''et al.'' |title=Functional specificity of cytoplasmic and transmembrane tyrosine kinases: identification of 130- and 75-kilodalton substrates of c-fps/fes tyrosine kinase in macrophages. |journal=Mol. Cell. Biol. |volume=14 |issue= 7 |pages= 4606-15 |year= 1994 |pmid= 8007965 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] FTH1

• INFO: Beginning work on FTH1... {November 17, 2007 11:11:19 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:11:56 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_FTH1_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1fha.
 | PDB = {{PDB2|1fha}}, {{PDB2|2cei}}, {{PDB2|2chi}}, {{PDB2|2cih}}, {{PDB2|2clu}}, {{PDB2|2cn6}}, {{PDB2|2cn7}}, {{PDB2|2fha}}, {{PDB2|2iu2}}
 | Name = Ferritin, heavy polypeptide 1
 | HGNCid = 3976
 | Symbol = FTH1
 | AltSymbols =; FTH; FTHL6; MGC104426; PIG15; PLIF
 | OMIM = 134770
 | ECnumber =  
 | Homologene = 74295
 | MGIid = 95588
 | GeneAtlas_image1 = PBB_GE_FTH1_200748_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_FTH1_214211_at_tn.png
 | Function = {{GNF_GO|id=GO:0004322 |text = ferroxidase activity}} {{GNF_GO|id=GO:0005488 |text = binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008199 |text = ferric iron binding}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0019900 |text = kinase binding}} 
 | Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0008043 |text = ferritin complex}} 
 | Process = {{GNF_GO|id=GO:0006826 |text = iron ion transport}} {{GNF_GO|id=GO:0006879 |text = cellular iron ion homeostasis}} {{GNF_GO|id=GO:0006880 |text = intracellular sequestering of iron ion}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2495
    | Hs_Ensembl = ENSG00000167996
    | Hs_RefseqProtein = NP_002023
    | Hs_RefseqmRNA = NM_002032
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 61488335
    | Hs_GenLoc_end = 61491679
    | Hs_Uniprot = P02794
    | Mm_EntrezGene = 14319
    | Mm_Ensembl = ENSMUSG00000024661
    | Mm_RefseqmRNA = NM_010239
    | Mm_RefseqProtein = NP_034369
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 10049748
    | Mm_GenLoc_end = 10052137
    | Mm_Uniprot = P09528
  }}
}}
'''Ferritin, heavy polypeptide 1''', also known as '''FTH1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FTH1 ferritin, heavy polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2495| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = This gene encodes the heavy subunit of ferritin, the major intracellular iron storage protein in prokaryotes and eukaryotes. It is composed of 24 subunits of the heavy and light ferritin chains. Variation in ferritin subunit composition may affect the rates of iron uptake and release in different tissues. A major function of ferritin is the storage of iron in a soluble and nontoxic state. Defects in ferritin proteins are associated with several neurodegenerative diseases. This gene has multiple pseudogenes. Several alternatively spliced transcript variants have been observed, but their biological validity has not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: FTH1 ferritin, heavy polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2495| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Percy ME, Wong S, Bauer S, ''et al.'' |title=Iron metabolism and human ferritin heavy chain cDNA from adult brain with an elongated untranslated region: new findings and insights. |journal=The Analyst |volume=123 |issue= 1 |pages= 41-50 |year= 1998 |pmid= 9581019 |doi=  }}
*{{cite journal  | author=Arosio P, Adelman TG, Drysdale JW |title=On ferritin heterogeneity. Further evidence for heteropolymers. |journal=J. Biol. Chem. |volume=253 |issue= 12 |pages= 4451-8 |year= 1978 |pmid= 659425 |doi=  }}
*{{cite journal  | author=Lawson DM, Artymiuk PJ, Yewdall SJ, ''et al.'' |title=Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts. |journal=Nature |volume=349 |issue= 6309 |pages= 541-4 |year= 1991 |pmid= 1992356 |doi= 10.1038/349541a0 }}
*{{cite journal  | author=Costanzo F, Colombo M, Staempfli S, ''et al.'' |title=Structure of gene and pseudogenes of human apoferritin H. |journal=Nucleic Acids Res. |volume=14 |issue= 2 |pages= 721-36 |year= 1986 |pmid= 3003694 |doi=  }}
*{{cite journal  | author=Hentze MW, Keim S, Papadopoulos P, ''et al.'' |title=Cloning, characterization, expression, and chromosomal localization of a human ferritin heavy-chain gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 19 |pages= 7226-30 |year= 1986 |pmid= 3020541 |doi=  }}
*{{cite journal  | author=Chou CC, Gatti RA, Fuller ML, ''et al.'' |title=Structure and expression of ferritin genes in a human promyelocytic cell line that differentiates in vitro. |journal=Mol. Cell. Biol. |volume=6 |issue= 2 |pages= 566-73 |year= 1987 |pmid= 3023856 |doi=  }}
*{{cite journal  | author=Hentze MW, Caughman SW, Rouault TA, ''et al.'' |title=Identification of the iron-responsive element for the translational regulation of human ferritin mRNA. |journal=Science |volume=238 |issue= 4833 |pages= 1570-3 |year= 1988 |pmid= 3685996 |doi=  }}
*{{cite journal  | author=Boyd D, Vecoli C, Belcher DM, ''et al.'' |title=Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones. |journal=J. Biol. Chem. |volume=260 |issue= 21 |pages= 11755-61 |year= 1985 |pmid= 3840162 |doi=  }}
*{{cite journal  | author=Worwood M, Brook JD, Cragg SJ, ''et al.'' |title=Assignment of human ferritin genes to chromosomes 11 and 19q13.3----19qter. |journal=Hum. Genet. |volume=69 |issue= 4 |pages= 371-4 |year= 1985 |pmid= 3857215 |doi=  }}
*{{cite journal  | author=Dörner MH, Salfeld J, Will H, ''et al.'' |title=Structure of human ferritin light subunit messenger RNA: comparison with heavy subunit message and functional implications. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 10 |pages= 3139-43 |year= 1985 |pmid= 3858810 |doi=  }}
*{{cite journal  | author=Costanzo F, Santoro C, Colantuoni V, ''et al.'' |title=Cloning and sequencing of a full length cDNA coding for a human apoferritin H chain: evidence for a multigene family. |journal=EMBO J. |volume=3 |issue= 1 |pages= 23-7 |year= 1984 |pmid= 6323167 |doi=  }}
*{{cite journal  | author=Boyd D, Jain SK, Crampton J, ''et al.'' |title=Isolation and characterization of a cDNA clone for human ferritin heavy chain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=81 |issue= 15 |pages= 4751-5 |year= 1984 |pmid= 6589621 |doi=  }}
*{{cite journal  | author=Addison JM, Fitton JE, Lewis WG, ''et al.'' |title=The amino acid sequence of human liver apoferritin. |journal=FEBS Lett. |volume=164 |issue= 1 |pages= 139-44 |year= 1984 |pmid= 6653779 |doi=  }}
*{{cite journal  | author=Dhar MS, Joshi JG |title=Differential processing of the ferritin heavy chain mRNA in human liver and adult human brain. |journal=J. Neurochem. |volume=61 |issue= 6 |pages= 2140-6 |year= 1993 |pmid= 7504084 |doi=  }}
*{{cite journal  | author=Connor JR, Snyder BS, Arosio P, ''et al.'' |title=A quantitative analysis of isoferritins in select regions of aged, parkinsonian, and Alzheimer's diseased brains. |journal=J. Neurochem. |volume=65 |issue= 2 |pages= 717-24 |year= 1995 |pmid= 7616228 |doi=  }}
*{{cite journal  | author=Kato S, Sekine S, Oh SW, ''et al.'' |title=Construction of a human full-length cDNA bank. |journal=Gene |volume=150 |issue= 2 |pages= 243-50 |year= 1995 |pmid= 7821789 |doi=  }}
*{{cite journal  | author=Dhar M, Chauthaiwale V, Joshi JG |title=Sequence of a cDNA encoding the ferritin H-chain from an 11-week-old human fetal brain. |journal=Gene |volume=126 |issue= 2 |pages= 275-8 |year= 1993 |pmid= 7916709 |doi=  }}
*{{cite journal  | author=Qi Y, Dawson G |title=Hypoxia specifically and reversibly induces the synthesis of ferritin in oligodendrocytes and human oligodendrogliomas. |journal=J. Neurochem. |volume=63 |issue= 4 |pages= 1485-90 |year= 1994 |pmid= 7931301 |doi=  }}
*{{cite journal  | author=Rogers JT |title=Ferritin translation by interleukin-1and interleukin-6: the role of sequences upstream of the start codons of the heavy and light subunit genes. |journal=Blood |volume=87 |issue= 6 |pages= 2525-37 |year= 1996 |pmid= 8630420 |doi=  }}
*{{cite journal  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] GCH1

• INFO: Beginning work on GCH1... {November 17, 2007 11:11:56 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:12:28 AM 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_GCH1_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1fb1.
 | PDB = {{PDB2|1fb1}}, {{PDB2|1is7}}, {{PDB2|1is8}}, {{PDB2|1wpl}}
 | Name = GTP cyclohydrolase 1 (dopa-responsive dystonia)
 | HGNCid = 4193
 | Symbol = GCH1
 | AltSymbols =; DYT5; GCH; GTP-CH-1; GTPCH1
 | OMIM = 600225
 | ECnumber =  
 | Homologene = 132
 | MGIid = 95675
 | GeneAtlas_image1 = PBB_GE_GCH1_204224_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0003934 |text = GTP cyclohydrolase I activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} 
 | Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} 
 | Process = {{GNF_GO|id=GO:0006559 |text = L-phenylalanine catabolic process}} {{GNF_GO|id=GO:0006729 |text = tetrahydrobiopterin biosynthetic process}} {{GNF_GO|id=GO:0006809 |text = nitric oxide biosynthetic process}} {{GNF_GO|id=GO:0019438 |text = aromatic compound biosynthetic process}} {{GNF_GO|id=GO:0042133 |text = neurotransmitter metabolic process}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2643
    | Hs_Ensembl = ENSG00000131979
    | Hs_RefseqProtein = NP_000152
    | Hs_RefseqmRNA = NM_000161
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 14
    | Hs_GenLoc_start = 54378476
    | Hs_GenLoc_end = 54439292
    | Hs_Uniprot = P30793
    | Mm_EntrezGene = 14528
    | Mm_Ensembl = ENSMUSG00000037580
    | Mm_RefseqmRNA = NM_008102
    | Mm_RefseqProtein = NP_032128
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 14
    | Mm_GenLoc_start = 46075772
    | Mm_GenLoc_end = 46111279
    | Mm_Uniprot = Q3U7P6
  }}
}}
'''GTP cyclohydrolase 1 (dopa-responsive dystonia)''', also known as '''GCH1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GCH1 GTP cyclohydrolase 1 (dopa-responsive dystonia)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2643| 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 GTP cyclohydrolase family. The encoded protein is the first and rate-limiting enzyme in tetrahydrobiopterin (BH4) biosynthesis, catalyzing the conversion of GTP into 7,8-dihydroneopterin triphosphate. BH4 is an essential cofactor required by aromatic amino acid hydroxylases as well as nitric oxide synthases. Mutations in this gene are associated with malignant hyperphenylalaninemia and dopa-responsive dystonia. Several alternatively spliced transcript variants encoding different isoforms have been described; however, not all variants give rise to a functional enzyme.<ref name="entrez">{{cite web | title = Entrez Gene: GCH1 GTP cyclohydrolase 1 (dopa-responsive dystonia)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2643| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Thöny B, Blau N |title=Mutations in the GTP cyclohydrolase I and 6-pyruvoyl-tetrahydropterin synthase genes. |journal=Hum. Mutat. |volume=10 |issue= 1 |pages= 11-20 |year= 1997 |pmid= 9222755 |doi= 10.1002/(SICI)1098-1004(1997)10:1<11::AID-HUMU2>3.0.CO;2-P }}
*{{cite journal  | author=Müller U, Steinberger D, Topka H |title=Mutations of GCH1 in Dopa-responsive dystonia. |journal=Journal of neural transmission (Vienna, Austria : 1996) |volume=109 |issue= 3 |pages= 321-8 |year= 2002 |pmid= 11956954 |doi= 10.1007/s007020200026 }}
*{{cite journal  | author=Gütlich M, Schott K, Werner T, ''et al.'' |title=Species and tissue specificity of mammalian GTP cyclohydrolase I messenger RNA. |journal=Biochim. Biophys. Acta |volume=1171 |issue= 2 |pages= 133-40 |year= 1993 |pmid= 1482676 |doi=  }}
*{{cite journal  | author=Togari A, Ichinose H, Matsumoto S, ''et al.'' |title=Multiple mRNA forms of human GTP cyclohydrolase I. |journal=Biochem. Biophys. Res. Commun. |volume=187 |issue= 1 |pages= 359-65 |year= 1992 |pmid= 1520321 |doi=  }}
*{{cite journal  | author=Ichinose H, Ohye T, Segawa M, ''et al.'' |title=GTP cyclohydrolase I gene in hereditary progressive dystonia with marked diurnal fluctuation. |journal=Neurosci. Lett. |volume=196 |issue= 1-2 |pages= 5-8 |year= 1996 |pmid= 7501255 |doi=  }}
*{{cite journal  | author=Ichinose H, Ohye T, Matsuda Y, ''et al.'' |title=Characterization of mouse and human GTP cyclohydrolase I genes. Mutations in patients with GTP cyclohydrolase I deficiency. |journal=J. Biol. Chem. |volume=270 |issue= 17 |pages= 10062-71 |year= 1995 |pmid= 7730309 |doi=  }}
*{{cite journal  | author=Imazumi K, Sasaki T, Takahashi K, Takai Y |title=Identification of a rabphilin-3A-interacting protein as GTP cyclohydrolase I in PC12 cells. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 2 |pages= 1409-16 |year= 1995 |pmid= 7802677 |doi= 10.1006/bbrc.1994.2822 }}
*{{cite journal  | author=Ichinose H, Ohye T, Takahashi E, ''et al.'' |title=Hereditary progressive dystonia with marked diurnal fluctuation caused by mutations in the GTP cyclohydrolase I gene. |journal=Nat. Genet. |volume=8 |issue= 3 |pages= 236-42 |year= 1995 |pmid= 7874165 |doi= 10.1038/ng1194-236 }}
*{{cite journal  | author=Gütlich M, Jaeger E, Rücknagel KP, ''et al.'' |title=Human GTP cyclohydrolase I: only one out of three cDNA isoforms gives rise to the active enzyme. |journal=Biochem. J. |volume=302 ( Pt 1) |issue=  |pages= 215-21 |year= 1994 |pmid= 8068008 |doi=  }}
*{{cite journal  | author=Nygaard TG, Wilhelmsen KC, Risch NJ, ''et al.'' |title=Linkage mapping of dopa-responsive dystonia (DRD) to chromosome 14q. |journal=Nat. Genet. |volume=5 |issue= 4 |pages= 386-91 |year= 1994 |pmid= 8298648 |doi= 10.1038/ng1293-386 }}
*{{cite journal  | author=Witter K, Werner T, Blusch JH, ''et al.'' |title=Cloning, sequencing and functional studies of the gene encoding human GTP cyclohydrolase I. |journal=Gene |volume=171 |issue= 2 |pages= 285-90 |year= 1996 |pmid= 8666288 |doi=  }}
*{{cite journal  | author=Nomura T, Ohtsuki M, Matsui S, ''et al.'' |title=Isolation of a full-length cDNA clone for human GTP cyclohydrolase I type 1 from pheochromocytoma. |journal=J. Neural Transm. Gen. Sect. |volume=101 |issue= 1-3 |pages= 237-42 |year= 1996 |pmid= 8695054 |doi=  }}
*{{cite journal  | author=Milstien S, Jaffe H, Kowlessur D, Bonner TI |title=Purification and cloning of the GTP cyclohydrolase I feedback regulatory protein, GFRP. |journal=J. Biol. Chem. |volume=271 |issue= 33 |pages= 19743-51 |year= 1996 |pmid= 8702680 |doi=  }}
*{{cite journal  | author=Bandmann O, Nygaard TG, Surtees R, ''et al.'' |title=Dopa-responsive dystonia in British patients: new mutations of the GTP-cyclohydrolase I gene and evidence for genetic heterogeneity. |journal=Hum. Mol. Genet. |volume=5 |issue= 3 |pages= 403-6 |year= 1997 |pmid= 8852666 |doi=  }}
*{{cite journal  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi=  }}
*{{cite journal  | author=Hirano M, Tamaru Y, Ito H, ''et al.'' |title=Mutant GTP cyclohydrolase I mRNA levels contribute to dopa-responsive dystonia onset. |journal=Ann. Neurol. |volume=40 |issue= 5 |pages= 796-8 |year= 1997 |pmid= 8957022 |doi= 10.1002/ana.410400517 }}
*{{cite journal  | author=Katusic ZS, Stelter A, Milstien S |title=Cytokines stimulate GTP cyclohydrolase I gene expression in cultured human umbilical vein endothelial cells. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=18 |issue= 1 |pages= 27-32 |year= 1998 |pmid= 9445252 |doi=  }}
*{{cite journal  | author=Tamaru Y, Hirano M, Ito H, ''et al.'' |title=Clinical similarities of hereditary progressive/dopa responsive dystonia caused by different types of mutations in the GTP cyclohydrolase I gene. |journal=J. Neurol. Neurosurg. Psychiatr. |volume=64 |issue= 4 |pages= 469-73 |year= 1998 |pmid= 9576537 |doi=  }}
*{{cite journal  | author=Furukawa Y, Kish SJ, Bebin EM, ''et al.'' |title=Dystonia with motor delay in compound heterozygotes for GTP-cyclohydrolase I gene mutations. |journal=Ann. Neurol. |volume=44 |issue= 1 |pages= 10-6 |year= 1998 |pmid= 9667588 |doi= 10.1002/ana.410440107 }}
}}
{{refend}}

{{protein-stub}}
 

[edit] HAMP

• INFO: Beginning work on HAMP... {November 17, 2007 11:22:44 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:23:18 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_HAMP_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1m4f.
 | PDB = {{PDB2|1m4f}}
 | Name = Hepcidin antimicrobial peptide
 | HGNCid = 15598
 | Symbol = HAMP
 | AltSymbols =; HEPC; HFE2B; LEAP-1; LEAP1
 | OMIM = 606464
 | ECnumber =  
 | Homologene = 81623
 | MGIid =  
 | GeneAtlas_image1 = PBB_GE_HAMP_220491_at_tn.png
 | Function = {{GNF_GO|id=GO:0005179 |text = hormone activity}} 
 | Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} 
 | Process = {{GNF_GO|id=GO:0006805 |text = xenobiotic metabolic process}} {{GNF_GO|id=GO:0006879 |text = cellular iron ion homeostasis}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}} {{GNF_GO|id=GO:0050832 |text = defense response to fungus}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 57817
    | Hs_Ensembl = ENSG00000105697
    | Hs_RefseqProtein = NP_066998
    | Hs_RefseqmRNA = NM_021175
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 40465250
    | Hs_GenLoc_end = 40467886
    | Hs_Uniprot = P81172
    | Mm_EntrezGene =  
    | Mm_Ensembl =  
    | Mm_RefseqmRNA =  
    | Mm_RefseqProtein =  
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr =  
    | Mm_GenLoc_start =  
    | Mm_GenLoc_end =  
    | Mm_Uniprot =  
  }}
}}
'''Hepcidin antimicrobial peptide''', also known as '''HAMP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HAMP hepcidin antimicrobial peptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=57817| 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=Ganz T |title=Hepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation. |journal=Blood |volume=102 |issue= 3 |pages= 783-8 |year= 2003 |pmid= 12663437 |doi= 10.1182/blood-2003-03-0672 }}
*{{cite journal  | author=Roy CN, Andrews NC |title=Anemia of inflammation: the hepcidin link. |journal=Curr. Opin. Hematol. |volume=12 |issue= 2 |pages= 107-11 |year= 2005 |pmid= 15725899 |doi=  }}
*{{cite journal  | author=Fleming RE, Britton RS, Waheed A, ''et al.'' |title=Pathophysiology of hereditary hemochromatosis. |journal=Semin. Liver Dis. |volume=25 |issue= 4 |pages= 411-9 |year= 2006 |pmid= 16315135 |doi= 10.1055/s-2005-923313 }}
*{{cite journal  | author=Krause A, Neitz S, Mägert HJ, ''et al.'' |title=LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity. |journal=FEBS Lett. |volume=480 |issue= 2-3 |pages= 147-50 |year= 2000 |pmid= 11034317 |doi=  }}
*{{cite journal  | author=Park CH, Valore EV, Waring AJ, Ganz T |title=Hepcidin, a urinary antimicrobial peptide synthesized in the liver. |journal=J. Biol. Chem. |volume=276 |issue= 11 |pages= 7806-10 |year= 2001 |pmid= 11113131 |doi= 10.1074/jbc.M008922200 }}
*{{cite journal  | author=Pigeon C, Ilyin G, Courselaud B, ''et al.'' |title=A new mouse liver-specific gene, encoding a protein homologous to human antimicrobial peptide hepcidin, is overexpressed during iron overload. |journal=J. Biol. Chem. |volume=276 |issue= 11 |pages= 7811-9 |year= 2001 |pmid= 11113132 |doi= 10.1074/jbc.M008923200 }}
*{{cite journal  | author=Majore S, Binni F, Ricerca BM, ''et al.'' |title=Absence of hepcidin gene mutations in 10 Italian patients with primary iron overload. |journal=Haematologica |volume=87 |issue= 2 |pages= 221-2 |year= 2002 |pmid= 11836175 |doi=  }}
*{{cite journal  | author=Klüver E, Schulz A, Forssmann WG, Adermann K |title=Chemical synthesis of beta-defensins and LEAP-1/hepcidin. |journal=J. Pept. Res. |volume=59 |issue= 6 |pages= 241-8 |year= 2002 |pmid= 12010514 |doi=  }}
*{{cite journal  | author=Hunter HN, Fulton DB, Ganz T, Vogel HJ |title=The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis. |journal=J. Biol. Chem. |volume=277 |issue= 40 |pages= 37597-603 |year= 2002 |pmid= 12138110 |doi= 10.1074/jbc.M205305200 }}
*{{cite journal  | author=Weinstein DA, Roy CN, Fleming MD, ''et al.'' |title=Inappropriate expression of hepcidin is associated with iron refractory anemia: implications for the anemia of chronic disease. |journal=Blood |volume=100 |issue= 10 |pages= 3776-81 |year= 2003 |pmid= 12393428 |doi= 10.1182/blood-2002-04-1260 }}
*{{cite journal  | author=Nemeth E, Valore EV, Territo M, ''et al.'' |title=Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein. |journal=Blood |volume=101 |issue= 7 |pages= 2461-3 |year= 2003 |pmid= 12433676 |doi= 10.1182/blood-2002-10-3235 }}
*{{cite journal  | author=Roetto A, Papanikolaou G, Politou M, ''et al.'' |title=Mutant antimicrobial peptide hepcidin is associated with severe juvenile hemochromatosis. |journal=Nat. Genet. |volume=33 |issue= 1 |pages= 21-2 |year= 2003 |pmid= 12469120 |doi= 10.1038/ng1053 }}
*{{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=Gehrke SG, Kulaksiz H, Herrmann T, ''et al.'' |title=Expression of hepcidin in hereditary hemochromatosis: evidence for a regulation in response to the serum transferrin saturation and to non-transferrin-bound iron. |journal=Blood |volume=102 |issue= 1 |pages= 371-6 |year= 2003 |pmid= 12637325 |doi= 10.1182/blood-2002-11-3610 }}
*{{cite journal  | author=Merryweather-Clarke AT, Cadet E, Bomford A, ''et al.'' |title=Digenic inheritance of mutations in HAMP and HFE results in different types of haemochromatosis. |journal=Hum. Mol. Genet. |volume=12 |issue= 17 |pages= 2241-7 |year= 2004 |pmid= 12915468 |doi= 10.1093/hmg/ddg225 }}
*{{cite journal  | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
*{{cite journal  | author=Roetto A, Daraio F, Porporato P, ''et al.'' |title=Screening hepcidin for mutations in juvenile hemochromatosis: identification of a new mutation (C70R). |journal=Blood |volume=103 |issue= 6 |pages= 2407-9 |year= 2004 |pmid= 14630809 |doi= 10.1182/blood-2003-10-3390 }}
*{{cite journal  | author=Jacolot S, Le Gac G, Scotet V, ''et al.'' |title=HAMP as a modifier gene that increases the phenotypic expression of the HFE pC282Y homozygous genotype. |journal=Blood |volume=103 |issue= 7 |pages= 2835-40 |year= 2004 |pmid= 14670915 |doi= 10.1182/blood-2003-10-3366 }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
}}
{{refend}}

{{protein-stub}}
 

[edit] IL11

• INFO: Beginning work on IL11... {November 17, 2007 11:12:28 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:13:12 AM 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 = Interleukin 11
 | HGNCid = 5966
 | Symbol = IL11
 | AltSymbols =; AGIF; IL-11
 | OMIM = 147681
 | ECnumber =  
 | Homologene = 535
 | MGIid = 107613
 | GeneAtlas_image1 = PBB_GE_IL11_206926_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_IL11_206924_at_tn.png
 | Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005142 |text = interleukin-11 receptor binding}} 
 | Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} 
 | Process = {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0030168 |text = platelet activation}} {{GNF_GO|id=GO:0030183 |text = B cell differentiation}} {{GNF_GO|id=GO:0030219 |text = megakaryocyte differentiation}} {{GNF_GO|id=GO:0045444 |text = fat cell differentiation}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3589
    | Hs_Ensembl = ENSG00000095752
    | Hs_RefseqProtein = NP_000632
    | Hs_RefseqmRNA = NM_000641
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 60567569
    | Hs_GenLoc_end = 60573626
    | Hs_Uniprot = P20809
    | Mm_EntrezGene = 16156
    | Mm_Ensembl = ENSMUSG00000004371
    | Mm_RefseqmRNA = NM_008350
    | Mm_RefseqProtein = NP_032376
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 4376654
    | Mm_GenLoc_end = 4379588
    | Mm_Uniprot = Q3V0U3
  }}
}}
'''Interleukin 11''', also known as '''IL11''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IL11 interleukin 11| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3589| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = The protein encoded by this gene is a member of the gp130 family of cytokines. These cytokines drive the assembly of multisubunit receptor complexes, all of which contain at least one molecule of the transmembrane signaling receptor IL6ST (gp130). This cytokine is shown to stimulate the T-cell-dependent development of immunoglobulin-producing B cells. It is also found to support the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells.<ref name="entrez">{{cite web | title = Entrez Gene: IL11 interleukin 11| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3589| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Yang YC, Yin T |title=Interleukin-11 and its receptor. |journal=Biofactors |volume=4 |issue= 1 |pages= 15-21 |year= 1993 |pmid= 1292471 |doi=  }}
*{{cite journal  | author=Bhatia M, Davenport V, Cairo MS |title=The role of interleukin-11 to prevent chemotherapy-induced thrombocytopenia in patients with solid tumors, lymphoma, acute myeloid leukemia and bone marrow failure syndromes. |journal=Leuk. Lymphoma |volume=48 |issue= 1 |pages= 9-15 |year= 2007 |pmid= 17325843 |doi= 10.1080/10428190600909115 }}
*{{cite journal  | author=McKinley D, Wu Q, Yang-Feng T, Yang YC |title=Genomic sequence and chromosomal location of human interleukin-11 gene (IL11). |journal=Genomics |volume=13 |issue= 3 |pages= 814-9 |year= 1992 |pmid= 1386338 |doi=  }}
*{{cite journal  | author=Kawashima I, Ohsumi J, Mita-Honjo K, ''et al.'' |title=Molecular cloning of cDNA encoding adipogenesis inhibitory factor and identity with interleukin-11. |journal=FEBS Lett. |volume=283 |issue= 2 |pages= 199-202 |year= 1991 |pmid= 1828438 |doi=  }}
*{{cite journal  | author=Paul SR, Bennett F, Calvetti JA, ''et al.'' |title=Molecular cloning of a cDNA encoding interleukin 11, a stromal cell-derived lymphopoietic and hematopoietic cytokine. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 19 |pages= 7512-6 |year= 1990 |pmid= 2145578 |doi=  }}
*{{cite journal  | author=Wang XY, Fuhrer DK, Marshall MS, Yang YC |title=Interleukin-11 induces complex formation of Grb2, Fyn, and JAK2 in 3T3L1 cells. |journal=J. Biol. Chem. |volume=270 |issue= 47 |pages= 27999-8002 |year= 1996 |pmid= 7499280 |doi=  }}
*{{cite journal  | author=Chérel M, Sorel M, Lebeau B, ''et al.'' |title=Molecular cloning of two isoforms of a receptor for the human hematopoietic cytokine interleukin-11. |journal=Blood |volume=86 |issue= 7 |pages= 2534-40 |year= 1995 |pmid= 7670098 |doi=  }}
*{{cite journal  | author=Yamaguchi M, Miki N, Ono M, ''et al.'' |title=Inhibition of growth hormone-releasing factor production in mouse placenta by cytokines using gp130 as a signal transducer. |journal=Endocrinology |volume=136 |issue= 3 |pages= 1072-8 |year= 1995 |pmid= 7867561 |doi=  }}
*{{cite journal  | author=Mehler MF, Rozental R, Dougherty M, ''et al.'' |title=Cytokine regulation of neuronal differentiation of hippocampal progenitor cells. |journal=Nature |volume=362 |issue= 6415 |pages= 62-5 |year= 1993 |pmid= 8383296 |doi= 10.1038/362062a0 }}
*{{cite journal  | author=Morris JC, Neben S, Bennett F, ''et al.'' |title=Molecular cloning and characterization of murine interleukin-11. |journal=Exp. Hematol. |volume=24 |issue= 12 |pages= 1369-76 |year= 1996 |pmid= 8913282 |doi=  }}
*{{cite journal  | author=Neddermann P, Graziani R, Ciliberto G, Paonessa G |title=Functional expression of soluble human interleukin-11 (IL-11) receptor alpha and stoichiometry of in vitro IL-11 receptor complexes with gp130. |journal=J. Biol. Chem. |volume=271 |issue= 48 |pages= 30986-91 |year= 1997 |pmid= 8940087 |doi=  }}
*{{cite journal  | author=Barton VA, Hudson KR, Heath JK |title=Identification of three distinct receptor binding sites of murine interleukin-11. |journal=J. Biol. Chem. |volume=274 |issue= 9 |pages= 5755-61 |year= 1999 |pmid= 10026196 |doi=  }}
*{{cite journal  | author=Tacken I, Dahmen H, Boisteau O, ''et al.'' |title=Definition of receptor binding sites on human interleukin-11 by molecular modeling-guided mutagenesis. |journal=Eur. J. Biochem. |volume=265 |issue= 2 |pages= 645-55 |year= 1999 |pmid= 10504396 |doi=  }}
*{{cite journal  | author=Mahboubi K, Biedermann BC, Carroll JM, Pober JS |title=IL-11 activates human endothelial cells to resist immune-mediated injury. |journal=J. Immunol. |volume=164 |issue= 7 |pages= 3837-46 |year= 2000 |pmid= 10725745 |doi=  }}
*{{cite journal  | author=Barton VA, Hall MA, Hudson KR, Heath JK |title=Interleukin-11 signals through the formation of a hexameric receptor complex. |journal=J. Biol. Chem. |volume=275 |issue= 46 |pages= 36197-203 |year= 2000 |pmid= 10948192 |doi= 10.1074/jbc.M004648200 }}
*{{cite journal  | author=Curti A, Tafuri A, Ricciardi MR, ''et al.'' |title=Interleukin-11 induces proliferation of human T-cells and its activity is associated with downregulation of p27(kip1). |journal=Haematologica |volume=87 |issue= 4 |pages= 373-80 |year= 2002 |pmid= 11940481 |doi=  }}
*{{cite journal  | author=Van der Meeren A, Mouthon MA, Gaugler MH, ''et al.'' |title=Administration of recombinant human IL11 after supralethal radiation exposure promotes survival in mice: interactive effect with thrombopoietin. |journal=Radiat. Res. |volume=157 |issue= 6 |pages= 642-9 |year= 2002 |pmid= 12005542 |doi=  }}
*{{cite journal  | author=McCloy MP, Roberts IA, Howarth LJ, ''et al.'' |title=Interleukin-11 levels in healthy and thrombocytopenic neonates. |journal=Pediatr. Res. |volume=51 |issue= 6 |pages= 756-60 |year= 2002 |pmid= 12032273 |doi=  }}
*{{cite journal  | author=Bartz H, Büning-Pfaue F, Türkel O, Schauer U |title=Respiratory syncytial virus induces prostaglandin E2, IL-10 and IL-11 generation in antigen presenting cells. |journal=Clin. Exp. Immunol. |volume=129 |issue= 3 |pages= 438-45 |year= 2002 |pmid= 12197884 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] MICB

• INFO: Beginning work on MICB... {November 17, 2007 11:14:55 AM PST}
• SEARCH REDIRECT: Control Box Found: MICB {November 17, 2007 11:15:20 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:15:21 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:15:21 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:15:21 AM PST}
• UPDATED: Updated protein page: MICB {November 17, 2007 11:15:27 AM PST}

[edit] NOTCH3

• INFO: Beginning work on NOTCH3... {November 17, 2007 11:15:27 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:15:54 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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| update_page = yes 
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| update_protein_box = yes
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| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Notch homolog 3 (Drosophila)
 | HGNCid = 7883
 | Symbol = NOTCH3
 | AltSymbols =; CADASIL; CASIL
 | OMIM = 600276
 | ECnumber =  
 | Homologene = 376
 | MGIid = 99460
 | GeneAtlas_image1 = PBB_GE_NOTCH3_203238_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_NOTCH3_203237_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} 
 | Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} 
 | Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007219 |text = Notch signaling pathway}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0009653 |text = anatomical structure morphogenesis}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0030900 |text = forebrain development}} {{GNF_GO|id=GO:0045665 |text = negative regulation of neuron differentiation}} {{GNF_GO|id=GO:0048663 |text = neuron fate commitment}} {{GNF_GO|id=GO:0050793 |text = regulation of developmental process}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4854
    | Hs_Ensembl = ENSG00000074181
    | Hs_RefseqProtein = NP_000426
    | Hs_RefseqmRNA = NM_000435
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 15131445
    | Hs_GenLoc_end = 15172792
    | Hs_Uniprot = Q9UM47
    | Mm_EntrezGene = 18131
    | Mm_Ensembl =  
    | Mm_RefseqmRNA = NM_008716
    | Mm_RefseqProtein = NP_032742
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr =  
    | Mm_GenLoc_start =  
    | Mm_GenLoc_end =  
    | Mm_Uniprot =  
  }}
}}
'''Notch homolog 3 (Drosophila)''', also known as '''NOTCH3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NOTCH3 Notch homolog 3 (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4854| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = This gene encodes the third discovered human homologue of the Drosophilia melanogaster type I membrane protein notch. In Drosophilia, notch interaction with its cell-bound ligands (delta, serrate) establishes an intercellular signalling pathway that plays a key role in neural development. Homologues of the notch-ligands have also been identified in human, but precise interactions between these ligands and the human notch homologues remains to be determined. Mutations in NOTCH3 have been identified as the underlying cause of cerebral autosomal dominant arteriopathy with subcortical infarcts and leukoencephalopathy (CADASIL).<ref name="entrez">{{cite web | title = Entrez Gene: NOTCH3 Notch homolog 3 (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4854| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Lewis J |title=Neurogenic genes and vertebrate neurogenesis. |journal=Curr. Opin. Neurobiol. |volume=6 |issue= 1 |pages= 3-10 |year= 1996 |pmid= 8794055 |doi=  }}
*{{cite journal  | author=Joutel A, Tournier-Lasserve E |title=[Molecular basis and physiopathogenic mechanisms of CADASIL: a model of small vessel diseases of the brain] |journal=J. Soc. Biol. |volume=196 |issue= 1 |pages= 109-15 |year= 2002 |pmid= 12134625 |doi=  }}
*{{cite journal  | author=Guidetti D, Casali B, Mazzei RL, Dotti MT |title=Cerebral autosomal dominant arteriopathy with subcortical infarcts and leukoencephalopathy. |journal=Clin. Exp. Hypertens. |volume=28 |issue= 3-4 |pages= 271-7 |year= 2006 |pmid= 16833034 |doi=  }}
*{{cite journal  | author=Beleil OM, Mickey MR, Terasaki PI |title=Comparison of male and female kidney transplant survival rates. |journal=Transplantation |volume=13 |issue= 5 |pages= 493-500 |year= 1972 |pmid= 4557798 |doi=  }}
*{{cite journal  | author=Larsson C, Lardelli M, White I, Lendahl U |title=The human NOTCH1, 2, and 3 genes are located at chromosome positions 9q34, 1p13-p11, and 19p13.2-p13.1 in regions of neoplasia-associated translocation. |journal=Genomics |volume=24 |issue= 2 |pages= 253-8 |year= 1995 |pmid= 7698746 |doi= 10.1006/geno.1994.1613 }}
*{{cite journal  | author=Sugaya K, Fukagawa T, Matsumoto K, ''et al.'' |title=Three genes in the human MHC class III region near the junction with the class II: gene for receptor of advanced glycosylation end products, PBX2 homeobox gene and a notch homolog, human counterpart of mouse mammary tumor gene int-3. |journal=Genomics |volume=23 |issue= 2 |pages= 408-19 |year= 1995 |pmid= 7835890 |doi=  }}
*{{cite journal  | author=Tournier-Lasserve E, Joutel A, Melki J, ''et al.'' |title=Cerebral autosomal dominant arteriopathy with subcortical infarcts and leukoencephalopathy maps to chromosome 19q12. |journal=Nat. Genet. |volume=3 |issue= 3 |pages= 256-9 |year= 1993 |pmid= 8485581 |doi= 10.1038/ng0393-256 }}
*{{cite journal  | author=Joutel A, Corpechot C, Ducros A, ''et al.'' |title=Notch3 mutations in CADASIL, a hereditary adult-onset condition causing stroke and dementia. |journal=Nature |volume=383 |issue= 6602 |pages= 707-10 |year= 1996 |pmid= 8878478 |doi= 10.1038/383707a0 }}
*{{cite journal  | author=Joutel A, Vahedi K, Corpechot C, ''et al.'' |title=Strong clustering and stereotyped nature of Notch3 mutations in CADASIL patients. |journal=Lancet |volume=350 |issue= 9090 |pages= 1511-5 |year= 1997 |pmid= 9388399 |doi=  }}
*{{cite journal  | author=Gray GE, Mann RS, Mitsiadis E, ''et al.'' |title=Human ligands of the Notch receptor. |journal=Am. J. Pathol. |volume=154 |issue= 3 |pages= 785-94 |year= 1999 |pmid= 10079256 |doi=  }}
*{{cite journal  | author=Joutel A, Andreux F, Gaulis S, ''et al.'' |title=The ectodomain of the Notch3 receptor accumulates within the cerebrovasculature of CADASIL patients. |journal=J. Clin. Invest. |volume=105 |issue= 5 |pages= 597-605 |year= 2000 |pmid= 10712431 |doi=  }}
*{{cite journal  | author=Joutel A, Dodick DD, Parisi JE, ''et al.'' |title=De novo mutation in the Notch3 gene causing CADASIL. |journal=Ann. Neurol. |volume=47 |issue= 3 |pages= 388-91 |year= 2000 |pmid= 10716263 |doi=  }}
*{{cite journal  | author=Joutel A, Chabriat H, Vahedi K, ''et al.'' |title=Splice site mutation causing a seven amino acid Notch3 in-frame deletion in CADASIL. |journal=Neurology |volume=54 |issue= 9 |pages= 1874-5 |year= 2000 |pmid= 10802807 |doi=  }}
*{{cite journal  | author=Shimizu K, Chiba S, Saito T, ''et al.'' |title=Physical interaction of Delta1, Jagged1, and Jagged2 with Notch1 and Notch3 receptors. |journal=Biochem. Biophys. Res. Commun. |volume=276 |issue= 1 |pages= 385-9 |year= 2000 |pmid= 11006133 |doi= 10.1006/bbrc.2000.3469 }}
*{{cite journal  | author=Wu L, Aster JC, Blacklow SC, ''et al.'' |title=MAML1, a human homologue of Drosophila mastermind, is a transcriptional co-activator for NOTCH receptors. |journal=Nat. Genet. |volume=26 |issue= 4 |pages= 484-9 |year= 2001 |pmid= 11101851 |doi= 10.1038/82644 }}
*{{cite journal  | author=Beatus P, Lundkvist J, Oberg C, ''et al.'' |title=The origin of the ankyrin repeat region in Notch intracellular domains is critical for regulation of HES promoter activity. |journal=Mech. Dev. |volume=104 |issue= 1-2 |pages= 3-20 |year= 2001 |pmid= 11404076 |doi=  }}
*{{cite journal  | author=Saxena MT, Schroeter EH, Mumm JS, Kopan R |title=Murine notch homologs (N1-4) undergo presenilin-dependent proteolysis. |journal=J. Biol. Chem. |volume=276 |issue= 43 |pages= 40268-73 |year= 2001 |pmid= 11518718 |doi= 10.1074/jbc.M107234200 }}
*{{cite journal  | author=Oliveri RL, Muglia M, De Stefano N, ''et al.'' |title=A novel mutation in the Notch3 gene in an Italian family with cerebral autosomal dominant arteriopathy with subcortical infarcts and leukoencephalopathy: genetic and magnetic resonance spectroscopic findings. |journal=Arch. Neurol. |volume=58 |issue= 9 |pages= 1418-22 |year= 2001 |pmid= 11559313 |doi=  }}
*{{cite journal  | author=Dichgans M, Herzog J, Gasser T |title=NOTCH3 mutation involving three cysteine residues in a family with typical CADASIL. |journal=Neurology |volume=57 |issue= 9 |pages= 1714-7 |year= 2001 |pmid= 11706120 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] PDGFA

• INFO: Beginning work on PDGFA... {November 17, 2007 11:15:54 AM PST}
• SEARCH REDIRECT: Control Box Found: PDGFA {November 17, 2007 11:16:20 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:16:22 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:16:22 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:16:22 AM PST}
• UPDATED: Updated protein page: PDGFA {November 17, 2007 11:16:30 AM PST}

[edit] PDX1

• INFO: Beginning work on PDX1... {November 17, 2007 11:13:12 AM PST}
• SEARCH REDIRECT: Control Box Found: PDX1 {November 17, 2007 11:13:54 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:13:55 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:13:55 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:13:55 AM PST}
• UPDATED: Updated protein page: PDX1 {November 17, 2007 11:14:01 AM PST}

[edit] PTPRA

• INFO: Beginning work on PTPRA... {November 17, 2007 11:17:41 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:18:20 AM 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_PTPRA_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1p15.
 | PDB = {{PDB2|1p15}}, {{PDB2|1yfo}}
 | Name = Protein tyrosine phosphatase, receptor type, A
 | HGNCid = 9664
 | Symbol = PTPRA
 | AltSymbols =; LRP; PTPA; HEPTP; HLPR; HPTPA; HPTPalpha; PTPRL2; R-PTP-alpha; RPTPA
 | OMIM = 176884
 | ECnumber =  
 | Homologene = 20621
 | MGIid = 97808
 | Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005001 |text = transmembrane receptor protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} 
 | Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} 
 | Process = {{GNF_GO|id=GO:0006470 |text = protein amino acid dephosphorylation}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5786
    | Hs_Ensembl =  
    | Hs_RefseqProtein = NP_002827
    | Hs_RefseqmRNA = NM_002836
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr =  
    | Hs_GenLoc_start =  
    | Hs_GenLoc_end =  
    | Hs_Uniprot =  
    | Mm_EntrezGene = 19262
    | Mm_Ensembl = ENSMUSG00000027303
    | Mm_RefseqmRNA = NM_008980
    | Mm_RefseqProtein = NP_033006
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 130141723
    | Mm_GenLoc_end = 130245741
    | Mm_Uniprot = Q3TRY9
  }}
}}
'''Protein tyrosine phosphatase, receptor type, A''', also known as '''PTPRA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTPRA protein tyrosine phosphatase, receptor type, A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5786| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an extracellular domain, a single transmembrane segment and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. This PTP has been shown to dephosphorylate and activate Src family tyrosine kinases, and is implicated in the regulation of integrin signaling, cell adhesion and proliferation. Three alternatively spliced variants of this gene, which encode two distinct isoforms, have been reported.<ref name="entrez">{{cite web | title = Entrez Gene: PTPRA protein tyrosine phosphatase, receptor type, A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5786| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Mustelin T, Hunter T |title=Meeting at mitosis: cell cycle-specific regulation of c-Src by RPTPalpha. |journal=Sci. STKE |volume=2002 |issue= 115 |pages= PE3 |year= 2002 |pmid= 11796915 |doi= 10.1126/stke.2002.115.pe3 }}
*{{cite journal  | author=Zheng XM, Wang Y, Pallen CJ |title=Cell transformation and activation of pp60c-src by overexpression of a protein tyrosine phosphatase. |journal=Nature |volume=359 |issue= 6393 |pages= 336-9 |year= 1992 |pmid= 1383828 |doi= 10.1038/359336a0 }}
*{{cite journal  | author=Jirik FR, Anderson LL, Duncan AM |title=The human protein-tyrosine phosphatase PTP alpha/LRP gene (PTPA) is assigned to chromosome 20p13. |journal=Cytogenet. Cell Genet. |volume=60 |issue= 2 |pages= 117-8 |year= 1992 |pmid= 1611910 |doi=  }}
*{{cite journal  | author=Rao VV, Löffler C, Sap J, ''et al.'' |title=The gene for receptor-linked protein-tyrosine-phosphatase (PTPA) is assigned to human chromosome 20p12-pter by in situ hybridization (ISH and FISH). |journal=Genomics |volume=13 |issue= 3 |pages= 906-7 |year= 1992 |pmid= 1639427 |doi=  }}
*{{cite journal  | author=Sap J, D'Eustachio P, Givol D, Schlessinger J |title=Cloning and expression of a widely expressed receptor tyrosine phosphatase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 16 |pages= 6112-6 |year= 1990 |pmid= 2166945 |doi=  }}
*{{cite journal  | author=Kaplan R, Morse B, Huebner K, ''et al.'' |title=Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine-phosphatases expressed in brain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 18 |pages= 7000-4 |year= 1990 |pmid= 2169617 |doi=  }}
*{{cite journal  | author=Krueger NX, Streuli M, Saito H |title=Structural diversity and evolution of human receptor-like protein tyrosine phosphatases. |journal=EMBO J. |volume=9 |issue= 10 |pages= 3241-52 |year= 1990 |pmid= 2170109 |doi=  }}
*{{cite journal  | author=Jirik FR, Janzen NM, Melhado IG, Harder KW |title=Cloning and chromosomal assignment of a widely expressed human receptor-like protein-tyrosine phosphatase. |journal=FEBS Lett. |volume=273 |issue= 1-2 |pages= 239-42 |year= 1990 |pmid= 2172030 |doi=  }}
*{{cite journal  | author=Ohagi S, Nishi M, Steiner DF |title=Sequence of a cDNA encoding human LRP (leukocyte common antigen-related peptide). |journal=Nucleic Acids Res. |volume=18 |issue= 23 |pages= 7159 |year= 1991 |pmid= 2175890 |doi=  }}
*{{cite journal  | author=den Hertog J, Tracy S, Hunter T |title=Phosphorylation of receptor protein-tyrosine phosphatase alpha on Tyr789, a binding site for the SH3-SH2-SH3 adaptor protein GRB-2 in vivo. |journal=EMBO J. |volume=13 |issue= 13 |pages= 3020-32 |year= 1994 |pmid= 7518772 |doi=  }}
*{{cite journal  | author=den Hertog J, Pals CE, Peppelenbosch MP, ''et al.'' |title=Receptor protein tyrosine phosphatase alpha activates pp60c-src and is involved in neuronal differentiation. |journal=EMBO J. |volume=12 |issue= 10 |pages= 3789-98 |year= 1993 |pmid= 7691597 |doi=  }}
*{{cite journal  | author=Stover DR, Furet P, Lydon NB |title=Modulation of the SH2 binding specificity and kinase activity of Src by tyrosine phosphorylation within its SH2 domain. |journal=J. Biol. Chem. |volume=271 |issue= 21 |pages= 12481-7 |year= 1996 |pmid= 8647855 |doi=  }}
*{{cite journal  | author=den Hertog J, Hunter T |title=Tight association of GRB2 with receptor protein-tyrosine phosphatase alpha is mediated by the SH2 and C-terminal SH3 domains. |journal=EMBO J. |volume=15 |issue= 12 |pages= 3016-27 |year= 1996 |pmid= 8670803 |doi=  }}
*{{cite journal  | author=Shimizu Y, Sugiyama H, Fujii Y, ''et al.'' |title=Lineage- and differentiation stage-specific expression of LSM-1 (LPAP), a possible substrate for CD45, in human hematopoietic cells. |journal=Am. J. Hematol. |volume=54 |issue= 1 |pages= 1-11 |year= 1997 |pmid= 8980254 |doi=  }}
*{{cite journal  | author=Lim KL, Lai DS, Kalousek MB, ''et al.'' |title=Kinetic analysis of two closely related receptor-like protein-tyrosine-phosphatases, PTP alpha and PTP epsilon. |journal=Eur. J. Biochem. |volume=245 |issue= 3 |pages= 693-700 |year= 1997 |pmid= 9183007 |doi=  }}
*{{cite journal  | author=Somani AK, Bignon JS, Mills GB, ''et al.'' |title=Src kinase activity is regulated by the SHP-1 protein-tyrosine phosphatase. |journal=J. Biol. Chem. |volume=272 |issue= 34 |pages= 21113-9 |year= 1997 |pmid= 9261115 |doi=  }}
*{{cite journal  | author=Feito MJ, Bragardo M, Buonfiglio D, ''et al.'' |title=gp 120s derived from four syncytium-inducing HIV-1 strains induce different patterns of CD4 association with lymphocyte surface molecules. |journal=Int. Immunol. |volume=9 |issue= 8 |pages= 1141-7 |year= 1997 |pmid= 9263011 |doi=  }}
*{{cite journal  | author=Norris K, Norris F, Kono DH, ''et al.'' |title=Expression of protein-tyrosine phosphatases in the major insulin target tissues. |journal=FEBS Lett. |volume=415 |issue= 3 |pages= 243-8 |year= 1997 |pmid= 9357975 |doi=  }}
*{{cite journal  | author=Bhandari V, Lim KL, Pallen CJ |title=Physical and functional interactions between receptor-like protein-tyrosine phosphatase alpha and p59fyn. |journal=J. Biol. Chem. |volume=273 |issue= 15 |pages= 8691-8 |year= 1998 |pmid= 9535845 |doi=  }}
*{{cite journal  | author=Harder KW, Moller NP, Peacock JW, Jirik FR |title=Protein-tyrosine phosphatase alpha regulates Src family kinases and alters cell-substratum adhesion. |journal=J. Biol. Chem. |volume=273 |issue= 48 |pages= 31890-900 |year= 1998 |pmid= 9822658 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] RANBP2

• INFO: Beginning work on RANBP2... {November 17, 2007 11:18:20 AM PST}
• SEARCH REDIRECT: Control Box Found: RANBP2 {November 17, 2007 11:18:50 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:18:51 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:18:51 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:18:51 AM PST}
• UPDATED: Updated protein page: RANBP2 {November 17, 2007 11:19:01 AM PST}

[edit] RANBP5

• INFO: Beginning work on RANBP5... {November 17, 2007 11:14:01 AM PST}
• SEARCH REDIRECT: Control Box Found: RANBP5 {November 17, 2007 11:14:45 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:14:48 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:14:48 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:14:48 AM PST}
• UPDATED: Updated protein page: RANBP5 {November 17, 2007 11:14:55 AM PST}

[edit] RUNX3

• INFO: Beginning work on RUNX3... {November 17, 2007 11:07:49 AM PST}
• SEARCH REDIRECT: Control Box Found: RUNX3 {November 17, 2007 11:08:20 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:08:21 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:08:21 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:08:21 AM PST}
• UPDATED: Updated protein page: RUNX3 {November 17, 2007 11:08:28 AM PST}

[edit] SDC4

• INFO: Beginning work on SDC4... {November 17, 2007 11:19:28 AM PST}
• SEARCH REDIRECT: Control Box Found: SDC4 {November 17, 2007 11:19:53 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:19:54 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:19:54 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:19:54 AM PST}
• UPDATED: Updated protein page: SDC4 {November 17, 2007 11:20:01 AM PST}

[edit] TERC

• INFO: Beginning work on TERC... {November 17, 2007 11:20:01 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:20:29 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
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| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Telomerase RNA component
 | HGNCid = 11727
 | Symbol = TERC
 | AltSymbols =; TR; SCARNA19; TRC3; hTR
 | OMIM = 602322
 | ECnumber =  
 | Homologene =  
 | MGIid =  
 | Function = 
 | Component = 
 | Process = 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7012
    | Hs_Ensembl =  
    | Hs_RefseqProtein =  
    | Hs_RefseqmRNA =  
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr =  
    | Hs_GenLoc_start =  
    | Hs_GenLoc_end =  
    | Hs_Uniprot =  
    | Mm_EntrezGene =  
    | Mm_Ensembl =  
    | Mm_RefseqmRNA =  
    | Mm_RefseqProtein =  
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr =  
    | Mm_GenLoc_start =  
    | Mm_GenLoc_end =  
    | Mm_Uniprot =  
  }}
}}
'''Telomerase RNA component''', also known as '''TERC''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TERC telomerase RNA component| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7012| 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 = Telomerase is a ribonucleoprotein polymerase that maintains telomere ends by addition of the telomere repeat TTAGGG. The enzyme consists of a protein component with reverse transcriptase activity, and an RNA component, encoded by this gene, that serves as a template for the telomere repeat. Telomerase expression plays a role in cellular senescence, as it is normally repressed in postnatal somatic cells resulting in progressive shortening of telomeres. Deregulation of telomerase expression in somatic cells may be involved in oncogenesis. Studies in mouse suggest that telomerase also participates in chromosomal repair, since de novo synthesis of telomere repeats may occur at double-stranded breaks. Mutations in this gene cause autosomal dominant dyskeratosis congenita, and may also be associated with some cases of aplastic anemia.<ref name="entrez">{{cite web | title = Entrez Gene: TERC telomerase RNA component| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7012| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=de Lange T, Jacks T |title=For better or worse? Telomerase inhibition and cancer. |journal=Cell |volume=98 |issue= 3 |pages= 273-5 |year= 1999 |pmid= 10458601 |doi=  }}
*{{cite journal  | author=Marrone A, Dokal I |title=Dyskeratosis congenita: molecular insights into telomerase function, ageing and cancer. |journal=Expert reviews in molecular medicine |volume=6 |issue= 26 |pages= 1-23 |year= 2007 |pmid= 15613268 |doi= 10.1017/S1462399404008671 }}
*{{cite journal  | author=Yamaguchi H |title=Mutations of telomerase complex genes linked to bone marrow failures. |journal=Journal of Nippon Medical School = Nihon Ika Daigaku zasshi |volume=74 |issue= 3 |pages= 202-9 |year= 2007 |pmid= 17625368 |doi=  }}
*{{cite journal  | author=Feng J, Funk WD, Wang SS, ''et al.'' |title=The RNA component of human telomerase. |journal=Science |volume=269 |issue= 5228 |pages= 1236-41 |year= 1995 |pmid= 7544491 |doi=  }}
*{{cite journal  | author=Zaug AJ, Linger J, Cech TR |title=Method for determining RNA 3' ends and application to human telomerase RNA. |journal=Nucleic Acids Res. |volume=24 |issue= 3 |pages= 532-3 |year= 1996 |pmid= 8602368 |doi=  }}
*{{cite journal  | author=Soder AI, Hoare SF, Muire S, ''et al.'' |title=Mapping of the gene for the mouse telomerase RNA component, Terc, to chromosome 3 by fluorescence in situ hybridization and mouse chromosome painting. |journal=Genomics |volume=41 |issue= 2 |pages= 293-4 |year= 1997 |pmid= 9143511 |doi= 10.1006/geno.1997.4621 }}
*{{cite journal  | author=Zhao JQ, Hoare SF, McFarlane R, ''et al.'' |title=Cloning and characterization of human and mouse telomerase RNA gene promoter sequences. |journal=Oncogene |volume=16 |issue= 10 |pages= 1345-50 |year= 1998 |pmid= 9546436 |doi= 10.1038/sj.onc.1201892 }}
*{{cite journal  | author=Mitchell JR, Wood E, Collins K |title=A telomerase component is defective in the human disease dyskeratosis congenita. |journal=Nature |volume=402 |issue= 6761 |pages= 551-5 |year= 1999 |pmid= 10591218 |doi= 10.1038/990141 }}
*{{cite journal  | author=Chen JL, Blasco MA, Greider CW |title=Secondary structure of vertebrate telomerase RNA. |journal=Cell |volume=100 |issue= 5 |pages= 503-14 |year= 2000 |pmid= 10721988 |doi=  }}
*{{cite journal  | author=Wong KK, Chang S, Weiler SR, ''et al.'' |title=Telomere dysfunction impairs DNA repair and enhances sensitivity to ionizing radiation. |journal=Nat. Genet. |volume=26 |issue= 1 |pages= 85-8 |year= 2000 |pmid= 10973255 |doi= 10.1038/79232 }}
*{{cite journal  | author=Mitchell JR, Collins K |title=Human telomerase activation requires two independent interactions between telomerase RNA and telomerase reverse transcriptase. |journal=Mol. Cell |volume=6 |issue= 2 |pages= 361-71 |year= 2000 |pmid= 10983983 |doi=  }}
*{{cite journal  | author=Imoto I, Pimkhaokham A, Fukuda Y, ''et al.'' |title=SNO is a probable target for gene amplification at 3q26 in squamous-cell carcinomas of the esophagus. |journal=Biochem. Biophys. Res. Commun. |volume=286 |issue= 3 |pages= 559-65 |year= 2001 |pmid= 11511096 |doi= 10.1006/bbrc.2001.5428 }}
*{{cite journal  | author=Vulliamy T, Marrone A, Goldman F, ''et al.'' |title=The RNA component of telomerase is mutated in autosomal dominant dyskeratosis congenita. |journal=Nature |volume=413 |issue= 6854 |pages= 432-5 |year= 2001 |pmid= 11574891 |doi= 10.1038/35096585 }}
*{{cite journal  | author=Pruzan R, Pongracz K, Gietzen K, ''et al.'' |title=Allosteric inhibitors of telomerase: oligonucleotide N3'-->P5' phosphoramidates. |journal=Nucleic Acids Res. |volume=30 |issue= 2 |pages= 559-68 |year= 2002 |pmid= 11788719 |doi=  }}
*{{cite journal  | author=Zhang RG, Zhang RP, Wang XW, Xie H |title=Effects of cisplatin on telomerase activity and telomere length in BEL-7404 human hepatoma cells. |journal=Cell Res. |volume=12 |issue= 1 |pages= 55-62 |year= 2004 |pmid= 11942411 |doi= 10.1038/sj.cr.7290110 }}
*{{cite journal  | author=Yang Y, Chen Y, Zhang C, ''et al.'' |title=Nucleolar localization of hTERT protein is associated with telomerase function. |journal=Exp. Cell Res. |volume=277 |issue= 2 |pages= 201-9 |year= 2002 |pmid= 12083802 |doi=  }}
*{{cite journal  | author=Chang JT, Chen YL, Yang HT, ''et al.'' |title=Differential regulation of telomerase activity by six telomerase subunits. |journal=Eur. J. Biochem. |volume=269 |issue= 14 |pages= 3442-50 |year= 2002 |pmid= 12135483 |doi=  }}
*{{cite journal  | author=Gavory G, Farrow M, Balasubramanian S |title=Minimum length requirement of the alignment domain of human telomerase RNA to sustain catalytic activity in vitro. |journal=Nucleic Acids Res. |volume=30 |issue= 20 |pages= 4470-80 |year= 2002 |pmid= 12384594 |doi=  }}
*{{cite journal  | author=Sood AK, Coffin J, Jabbari S, ''et al.'' |title=p53 null mutations are associated with a telomerase negative phenotype in ovarian carcinoma. |journal=Cancer Biol. Ther. |volume=1 |issue= 5 |pages= 511-7 |year= 2003 |pmid= 12496479 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] TRADD

• INFO: Beginning work on TRADD... {November 17, 2007 11:21:04 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:21:25 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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| require_manual_inspection = no 
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| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_TRADD_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1f2h.
 | PDB = {{PDB2|1f2h}}, {{PDB2|1f3v}}
 | Name = TNFRSF1A-associated via death domain
 | HGNCid = 12030
 | Symbol = TRADD
 | AltSymbols =; Hs.89862; MGC11078
 | OMIM = 603500
 | ECnumber =  
 | Homologene = 2807
 | MGIid = 109200
 | GeneAtlas_image1 = PBB_GE_TRADD_1729_at_tn.png
 | GeneAtlas_image2 = PBB_GE_TRADD_205641_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}} 
 | Component = 
 | Process = {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8717
    | Hs_Ensembl = ENSG00000102871
    | Hs_RefseqProtein = NP_700474
    | Hs_RefseqmRNA = NM_153425
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 65745605
    | Hs_GenLoc_end = 65751306
    | Hs_Uniprot = Q15628
    | Mm_EntrezGene = 71609
    | Mm_Ensembl = ENSMUSG00000031887
    | Mm_RefseqmRNA = NM_001033161
    | Mm_RefseqProtein = NP_001028333
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 108147415
    | Mm_GenLoc_end = 108153738
    | Mm_Uniprot =  
  }}
}}
'''TNFRSF1A-associated via death domain''', also known as '''TRADD''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TRADD TNFRSF1A-associated via death domain| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8717| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = The protein encoded by this gene is a death domain containing adaptor molecule that interacts with TNFRSF1A/TNFR1 and mediates programmed cell death signaling and NF-kappaB activation. This protein binds adaptor protein TRAF2, reduces the recruitment of inhibitor-of-apoptosis proteins (IAPs) by TRAF2, and thus suppresses TRAF2 mediated apoptosis. This protein can also interact with receptor TNFRSF6/FAS and adaptor protein FADD/MORT1, and is involved in the Fas-induced cell death pathway.<ref name="entrez">{{cite web | title = Entrez Gene: TRADD TNFRSF1A-associated via death domain| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8717| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Baker SJ, Reddy EP |title=Modulation of life and death by the TNF receptor superfamily. |journal=Oncogene |volume=17 |issue= 25 |pages= 3261-70 |year= 1999 |pmid= 9916988 |doi= 10.1038/sj.onc.1202568 }}
*{{cite journal  | author=Hsu H, Xiong J, Goeddel DV |title=The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation. |journal=Cell |volume=81 |issue= 4 |pages= 495-504 |year= 1995 |pmid= 7758105 |doi=  }}
*{{cite journal  | author=Hsu H, Shu HB, Pan MG, Goeddel DV |title=TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways. |journal=Cell |volume=84 |issue= 2 |pages= 299-308 |year= 1996 |pmid= 8565075 |doi=  }}
*{{cite journal  | author=Hsu H, Huang J, Shu HB, ''et al.'' |title=TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. |journal=Immunity |volume=4 |issue= 4 |pages= 387-96 |year= 1996 |pmid= 8612133 |doi=  }}
*{{cite journal  | author=Boldin MP, Goncharov TM, Goltsev YV, Wallach D |title=Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death. |journal=Cell |volume=85 |issue= 6 |pages= 803-15 |year= 1996 |pmid= 8681376 |doi=  }}
*{{cite journal  | author=Takeuchi M, Rothe M, Goeddel DV |title=Anatomy of TRAF2. Distinct domains for nuclear factor-kappaB activation and association with tumor necrosis factor signaling proteins. |journal=J. Biol. Chem. |volume=271 |issue= 33 |pages= 19935-42 |year= 1996 |pmid= 8702708 |doi=  }}
*{{cite journal  | author=Kitson J, Raven T, Jiang YP, ''et al.'' |title=A death-domain-containing receptor that mediates apoptosis. |journal=Nature |volume=384 |issue= 6607 |pages= 372-5 |year= 1996 |pmid= 8934525 |doi= 10.1038/384372a0 }}
*{{cite journal  | author=Shu HB, Takeuchi M, Goeddel DV |title=The tumor necrosis factor receptor 2 signal transducers TRAF2 and c-IAP1 are components of the tumor necrosis factor receptor 1 signaling complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 24 |pages= 13973-8 |year= 1997 |pmid= 8943045 |doi=  }}
*{{cite journal  | author=Izumi KM, Kieff ED |title=The Epstein-Barr virus oncogene product latent membrane protein 1 engages the tumor necrosis factor receptor-associated death domain protein to mediate B lymphocyte growth transformation and activate NF-kappaB. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 23 |pages= 12592-7 |year= 1997 |pmid= 9356494 |doi=  }}
*{{cite journal  | author=Wajant H, Johannes FJ, Haas E, ''et al.'' |title=Dominant-negative FADD inhibits TNFR60-, Fas/Apo1- and TRAIL-R/Apo2-mediated cell death but not gene induction. |journal=Curr. Biol. |volume=8 |issue= 2 |pages= 113-6 |year= 1998 |pmid= 9427646 |doi=  }}
*{{cite journal  | author=Chaudhary PM, Eby M, Jasmin A, ''et al.'' |title=Death receptor 5, a new member of the TNFR family, and DR4 induce FADD-dependent apoptosis and activate the NF-kappaB pathway. |journal=Immunity |volume=7 |issue= 6 |pages= 821-30 |year= 1998 |pmid= 9430227 |doi=  }}
*{{cite journal  | author=Pan G, Bauer JH, Haridas V, ''et al.'' |title=Identification and functional characterization of DR6, a novel death domain-containing TNF receptor. |journal=FEBS Lett. |volume=431 |issue= 3 |pages= 351-6 |year= 1998 |pmid= 9714541 |doi=  }}
*{{cite journal  | author=Jones SJ, Ledgerwood EC, Prins JB, ''et al.'' |title=TNF recruits TRADD to the plasma membrane but not the trans-Golgi network, the principal subcellular location of TNF-R1. |journal=J. Immunol. |volume=162 |issue= 2 |pages= 1042-8 |year= 1999 |pmid= 9916731 |doi=  }}
*{{cite journal  | author=Schütze S, Machleidt T, Adam D, ''et al.'' |title=Inhibition of receptor internalization by monodansylcadaverine selectively blocks p55 tumor necrosis factor receptor death domain signaling. |journal=J. Biol. Chem. |volume=274 |issue= 15 |pages= 10203-12 |year= 1999 |pmid= 10187805 |doi=  }}
*{{cite journal  | author=Sanz L, Sanchez P, Lallena MJ, ''et al.'' |title=The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation. |journal=EMBO J. |volume=18 |issue= 11 |pages= 3044-53 |year= 1999 |pmid= 10356400 |doi= 10.1093/emboj/18.11.3044 }}
*{{cite journal  | author=Costanzo A, Guiet C, Vito P |title=c-E10 is a caspase-recruiting domain-containing protein that interacts with components of death receptors signaling pathway and activates nuclear factor-kappaB. |journal=J. Biol. Chem. |volume=274 |issue= 29 |pages= 20127-32 |year= 1999 |pmid= 10400625 |doi=  }}
*{{cite journal  | author=Wang Y, Wu TR, Cai S, ''et al.'' |title=Stat1 as a component of tumor necrosis factor alpha receptor 1-TRADD signaling complex to inhibit NF-kappaB activation. |journal=Mol. Cell. Biol. |volume=20 |issue= 13 |pages= 4505-12 |year= 2000 |pmid= 10848577 |doi=  }}
*{{cite journal  | author=Park YC, Ye H, Hsia C, ''et al.'' |title=A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD-TRAF2 interaction. |journal=Cell |volume=101 |issue= 7 |pages= 777-87 |year= 2000 |pmid= 10892748 |doi=  }}
*{{cite journal  | author=Tsao DH, McDonagh T, Telliez JB, ''et al.'' |title=Solution structure of N-TRADD and characterization of the interaction of N-TRADD and C-TRAF2, a key step in the TNFR1 signaling pathway. |journal=Mol. Cell |volume=5 |issue= 6 |pages= 1051-7 |year= 2000 |pmid= 10911999 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] UTRN

• INFO: Beginning work on UTRN... {November 17, 2007 11:20:29 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:21:04 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_UTRN_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bhd.
 | PDB = {{PDB2|1bhd}}, {{PDB2|1qag}}
 | Name = Utrophin
 | HGNCid = 12635
 | Symbol = UTRN
 | AltSymbols =; DRP1; DMDL; DRP; FLJ23678
 | OMIM = 128240
 | ECnumber =  
 | Homologene = 21398
 | MGIid = 104631
 | GeneAtlas_image1 = PBB_GE_UTRN_213023_at_tn.png
 | GeneAtlas_image2 = PBB_GE_UTRN_213022_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} 
 | Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0030054 |text = cell junction}} {{GNF_GO|id=GO:0045202 |text = synapse}} 
 | Process = {{GNF_GO|id=GO:0006936 |text = muscle contraction}} {{GNF_GO|id=GO:0007517 |text = muscle development}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7402
    | Hs_Ensembl = ENSG00000152818
    | Hs_RefseqProtein = NP_009055
    | Hs_RefseqmRNA = NM_007124
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 144654658
    | Hs_GenLoc_end = 145215863
    | Hs_Uniprot = P46939
    | Mm_EntrezGene = 22288
    | Mm_Ensembl = ENSMUSG00000019820
    | Mm_RefseqmRNA = NM_011682
    | Mm_RefseqProtein = NP_035812
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 12075702
    | Mm_GenLoc_end = 12551836
    | Mm_Uniprot =  
  }}
}}
'''Utrophin''', also known as '''UTRN''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: UTRN utrophin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7402| 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 shares both structural and functional similarities with the dystrophin gene. It contains an actin-binding N-terminus, a triple coiled-coil repeat central region, and a C-terminus that consists of protein-protein interaction motifs which interact with dystroglycan protein components. The protein encoded by this gene is located at the neuromuscular synapse and myotendinous junctions, where it participates in post-synaptic membrane maintenance and acetylcholine receptor clustering. Mouse studies suggest that this gene may serve as a functional substitute for the dystrophin gene and therefore, may serve as a potential therapeutic alternative to muscular dystrophy which is caused by mutations in the dystrophin gene. Alternative splicing of the utrophin gene has been described; however, the full-length nature of these variants has not yet been determined.<ref name="entrez">{{cite web | title = Entrez Gene: UTRN utrophin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7402| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Haenggi T, Fritschy JM |title=Role of dystrophin and utrophin for assembly and function of the dystrophin glycoprotein complex in non-muscle tissue. |journal=Cell. Mol. Life Sci. |volume=63 |issue= 14 |pages= 1614-31 |year= 2006 |pmid= 16710609 |doi= 10.1007/s00018-005-5461-0 }}
*{{cite journal  | author=Khurana TS, Watkins SC, Kunkel LM |title=The subcellular distribution of chromosome 6-encoded dystrophin-related protein in the brain. |journal=J. Cell Biol. |volume=119 |issue= 2 |pages= 357-66 |year= 1992 |pmid= 1400579 |doi=  }}
*{{cite journal  | author=Nguyen TM, Le TT, Blake DJ, ''et al.'' |title=Utrophin, the autosomal homologue of dystrophin, is widely-expressed and membrane-associated in cultured cell lines. |journal=FEBS Lett. |volume=313 |issue= 1 |pages= 19-22 |year= 1992 |pmid= 1426262 |doi=  }}
*{{cite journal  | author=Tinsley JM, Blake DJ, Roche A, ''et al.'' |title=Primary structure of dystrophin-related protein. |journal=Nature |volume=360 |issue= 6404 |pages= 591-3 |year= 1993 |pmid= 1461283 |doi= 10.1038/360591a0 }}
*{{cite journal  | author=Love DR, Morris GE, Ellis JM, ''et al.'' |title=Tissue distribution of the dystrophin-related gene product and expression in the mdx and dy mouse. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 8 |pages= 3243-7 |year= 1991 |pmid= 2014247 |doi=  }}
*{{cite journal  | author=Buckle VJ, Guenet JL, Simon-Chazottes D, ''et al.'' |title=Localisation of a dystrophin-related autosomal gene to 6q24 in man, and to mouse chromosome 10 in the region of the dystrophia muscularis (dy) locus. |journal=Hum. Genet. |volume=85 |issue= 3 |pages= 324-6 |year= 1990 |pmid= 2203673 |doi=  }}
*{{cite journal  | author=Love DR, Hill DF, Dickson G, ''et al.'' |title=An autosomal transcript in skeletal muscle with homology to dystrophin. |journal=Nature |volume=339 |issue= 6219 |pages= 55-8 |year= 1989 |pmid= 2541343 |doi= 10.1038/339055a0 }}
*{{cite journal  | author=Belkin AM, Burridge K |title=Localization of utrophin and aciculin at sites of cell-matrix and cell-cell adhesion in cultured cells. |journal=Exp. Cell Res. |volume=221 |issue= 1 |pages= 132-40 |year= 1995 |pmid= 7589238 |doi= 10.1006/excr.1995.1360 }}
*{{cite journal  | author=Ahn AH, Kunkel LM |title=Syntrophin binds to an alternatively spliced exon of dystrophin. |journal=J. Cell Biol. |volume=128 |issue= 3 |pages= 363-71 |year= 1995 |pmid= 7844150 |doi=  }}
*{{cite journal  | author=Belkin AM, Burridge K |title=Association of aciculin with dystrophin and utrophin. |journal=J. Biol. Chem. |volume=270 |issue= 11 |pages= 6328-37 |year= 1995 |pmid= 7890770 |doi=  }}
*{{cite journal  | author=Pearce M, Blake DJ, Tinsley JM, ''et al.'' |title=The utrophin and dystrophin genes share similarities in genomic structure. |journal=Hum. Mol. Genet. |volume=2 |issue= 11 |pages= 1765-72 |year= 1994 |pmid= 8281135 |doi=  }}
*{{cite journal  | author=Ahn AH, Freener CA, Gussoni E, ''et al.'' |title=The three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives. |journal=J. Biol. Chem. |volume=271 |issue= 5 |pages= 2724-30 |year= 1996 |pmid= 8576247 |doi=  }}
*{{cite journal  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi=  }}
*{{cite journal  | author=Guo WX, Nichol M, Merlie JP |title=Cloning and expression of full length mouse utrophin: the differential association of utrophin and dystrophin with AChR clusters. |journal=FEBS Lett. |volume=398 |issue= 2-3 |pages= 259-64 |year= 1997 |pmid= 8977119 |doi=  }}
*{{cite journal  | author=Deconinck AE, Rafael JA, Skinner JA, ''et al.'' |title=Utrophin-dystrophin-deficient mice as a model for Duchenne muscular dystrophy. |journal=Cell |volume=90 |issue= 4 |pages= 717-27 |year= 1997 |pmid= 9288751 |doi=  }}
*{{cite journal  | author=Nawrotzki R, Loh NY, Ruegg MA, ''et al.'' |title=Characterisation of alpha-dystrobrevin in muscle. |journal=J. Cell. Sci. |volume=111 ( Pt 17) |issue=  |pages= 2595-605 |year= 1999 |pmid= 9701558 |doi=  }}
*{{cite journal  | author=Keep NH, Norwood FL, Moores CA, ''et al.'' |title=The 2.0 A structure of the second calponin homology domain from the actin-binding region of the dystrophin homologue utrophin. |journal=J. Mol. Biol. |volume=285 |issue= 3 |pages= 1257-64 |year= 1999 |pmid= 9887274 |doi= 10.1006/jmbi.1998.2406 }}
*{{cite journal  | author=Wilson J, Putt W, Jimenez C, Edwards YH |title=Up71 and up140, two novel transcripts of utrophin that are homologues of short forms of dystrophin. |journal=Hum. Mol. Genet. |volume=8 |issue= 7 |pages= 1271-8 |year= 1999 |pmid= 10369873 |doi=  }}
*{{cite journal  | author=Blake DJ, Hawkes R, Benson MA, Beesley PW |title=Different dystrophin-like complexes are expressed in neurons and glia. |journal=J. Cell Biol. |volume=147 |issue= 3 |pages= 645-58 |year= 1999 |pmid= 10545507 |doi=  }}
*{{cite journal  | author=Keep NH, Winder SJ, Moores CA, ''et al.'' |title=Crystal structure of the actin-binding region of utrophin reveals a head-to-tail dimer. |journal=Structure |volume=7 |issue= 12 |pages= 1539-46 |year= 2000 |pmid= 10647184 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

[edit] WASL

• INFO: Beginning work on WASL... {November 17, 2007 11:21:25 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:21:55 AM 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 = Wiskott-Aldrich syndrome-like
 | HGNCid = 12735
 | Symbol = WASL
 | AltSymbols =; DKFZp779G0847; MGC48327; N-WASP
 | OMIM = 605056
 | ECnumber =  
 | Homologene = 74515
 | MGIid = 1920428
 | GeneAtlas_image1 = PBB_GE_WASL_205810_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005083 |text = small GTPase regulator activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} 
 | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}} {{GNF_GO|id=GO:0030027 |text = lamellipodium}} 
 | Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0008154 |text = actin polymerization and/or depolymerization}} {{GNF_GO|id=GO:0009617 |text = response to bacterium}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8976
    | Hs_Ensembl = ENSG00000106299
    | Hs_RefseqProtein = NP_003932
    | Hs_RefseqmRNA = NM_003941
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 123109237
    | Hs_GenLoc_end = 123176352
    | Hs_Uniprot = O00401
    | Mm_EntrezGene = 73178
    | Mm_Ensembl = ENSMUSG00000029684
    | Mm_RefseqmRNA = NM_028459
    | Mm_RefseqProtein = NP_082735
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 6
    | Mm_GenLoc_start = 24563813
    | Mm_GenLoc_end = 24614998
    | Mm_Uniprot = Q05CX6
  }}
}}
'''Wiskott-Aldrich syndrome-like''', also known as '''WASL''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: WASL Wiskott-Aldrich syndrome-like| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8976| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = The Wiskott-Aldrich syndrome (WAS) family of proteins share similar domain structure, and are involved in transduction of signals from receptors on the cell surface to the actin cytoskeleton. The presence of a number of different motifs suggests that they are regulated by a number of different stimuli, and interact with multiple proteins. Recent studies have demonstrated that these proteins, directly or indirectly, associate with the small GTPase, Cdc42, known to regulate formation of actin filaments, and the cytoskeletal organizing complex, Arp2/3. The WASL gene product is a homolog of WAS protein, however, unlike the latter, it is ubiquitously expressed and shows highest expression in neural tissues. It has been shown to bind Cdc42 directly, and induce formation of long actin microspikes.<ref name="entrez">{{cite web | title = Entrez Gene: WASL Wiskott-Aldrich syndrome-like| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8976| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Ramesh N, Antón IM, Martínez-Quiles N, Geha RS |title=Waltzing with WASP. |journal=Trends Cell Biol. |volume=9 |issue= 1 |pages= 15-9 |year= 1999 |pmid= 10087612 |doi=  }}
*{{cite journal  | author=Carlier MF, Ducruix A, Pantaloni D |title=Signalling to actin: the Cdc42-N-WASP-Arp2/3 connection. |journal=Chem. Biol. |volume=6 |issue= 9 |pages= R235-40 |year= 1999 |pmid= 10467124 |doi=  }}
*{{cite journal  | author=Fukuoka M, Miki H, Takenawa T |title=Identification of N-WASP homologs in human and rat brain. |journal=Gene |volume=196 |issue= 1-2 |pages= 43-8 |year= 1997 |pmid= 9322739 |doi=  }}
*{{cite journal  | author=Miki H, Sasaki T, Takai Y, Takenawa T |title=Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP. |journal=Nature |volume=391 |issue= 6662 |pages= 93-6 |year= 1998 |pmid= 9422512 |doi= 10.1038/34208 }}
*{{cite journal  | author=Suzuki T, Miki H, Takenawa T, Sasakawa C |title=Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri. |journal=EMBO J. |volume=17 |issue= 10 |pages= 2767-76 |year= 1998 |pmid= 9582270 |doi= 10.1093/emboj/17.10.2767 }}
*{{cite journal  | author=Suetsugu S, Miki H, Takenawa T |title=The essential role of profilin in the assembly of actin for microspike formation. |journal=EMBO J. |volume=17 |issue= 22 |pages= 6516-26 |year= 1999 |pmid= 9822597 |doi= 10.1093/emboj/17.22.6516 }}
*{{cite journal  | author=Qualmann B, Roos J, DiGregorio PJ, Kelly RB |title=Syndapin I, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein. |journal=Mol. Biol. Cell |volume=10 |issue= 2 |pages= 501-13 |year= 1999 |pmid= 9950691 |doi=  }}
*{{cite journal  | author=Suetsugu S, Miki H, Takenawa T |title=Identification of two human WAVE/SCAR homologues as general actin regulatory molecules which associate with the Arp2/3 complex. |journal=Biochem. Biophys. Res. Commun. |volume=260 |issue= 1 |pages= 296-302 |year= 1999 |pmid= 10381382 |doi= 10.1006/bbrc.1999.0894 }}
*{{cite journal  | author=Egile C, Loisel TP, Laurent V, ''et al.'' |title=Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility. |journal=J. Cell Biol. |volume=146 |issue= 6 |pages= 1319-32 |year= 1999 |pmid= 10491394 |doi=  }}
*{{cite journal  | author=Higgs HN, Blanchoin L, Pollard TD |title=Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2/3 complex on actin polymerization. |journal=Biochemistry |volume=38 |issue= 46 |pages= 15212-22 |year= 1999 |pmid= 10563804 |doi=  }}
*{{cite journal  | author=Qualmann B, Kelly RB |title=Syndapin isoforms participate in receptor-mediated endocytosis and actin organization. |journal=J. Cell Biol. |volume=148 |issue= 5 |pages= 1047-62 |year= 2000 |pmid= 10704453 |doi=  }}
*{{cite journal  | author=Kim AS, Kakalis LT, Abdul-Manan N, ''et al.'' |title=Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. |journal=Nature |volume=404 |issue= 6774 |pages= 151-8 |year= 2000 |pmid= 10724160 |doi= 10.1038/35004513 }}
*{{cite journal  | author=Carlier MF, Nioche P, Broutin-L'Hermite I, ''et al.'' |title=GRB2 links signaling to actin assembly by enhancing interaction of neural Wiskott-Aldrich syndrome protein (N-WASp) with actin-related protein (ARP2/3) complex. |journal=J. Biol. Chem. |volume=275 |issue= 29 |pages= 21946-52 |year= 2000 |pmid= 10781580 |doi= 10.1074/jbc.M000687200 }}
*{{cite journal  | author=Mimuro H, Suzuki T, Suetsugu S, ''et al.'' |title=Profilin is required for sustaining efficient intra- and intercellular spreading of Shigella flexneri. |journal=J. Biol. Chem. |volume=275 |issue= 37 |pages= 28893-901 |year= 2000 |pmid= 10867004 |doi= 10.1074/jbc.M003882200 }}
*{{cite journal  | author=Prehoda KE, Scott JA, Mullins RD, Lim WA |title=Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex. |journal=Science |volume=290 |issue= 5492 |pages= 801-6 |year= 2000 |pmid= 11052943 |doi=  }}
*{{cite journal  | author=Modregger J, Ritter B, Witter B, ''et al.'' |title=All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis. |journal=J. Cell. Sci. |volume=113 Pt 24 |issue=  |pages= 4511-21 |year= 2001 |pmid= 11082044 |doi=  }}
*{{cite journal  | author=Marchand JB, Kaiser DA, Pollard TD, Higgs HN |title=Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex. |journal=Nat. Cell Biol. |volume=3 |issue= 1 |pages= 76-82 |year= 2001 |pmid= 11146629 |doi= 10.1038/35050590 }}
*{{cite journal  | author=Fukuoka M, Suetsugu S, Miki H, ''et al.'' |title=A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein, WISH, induces Arp2/3 complex activation independent of Cdc42. |journal=J. Cell Biol. |volume=152 |issue= 3 |pages= 471-82 |year= 2001 |pmid= 11157975 |doi=  }}
}}
{{refend}}

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