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Log page index: User:ProteinBoxBot/PBB_Log_Index
[edit] Protein Status Quick Log - Date: 23:09, 3 November 2007 (UTC)
[edit] Proteins without matches (13)
[edit] Proteins with a High Potential Match (12)
[edit] Created (4)
[edit] Manual Inspection (Page not found) (21)
[edit] Protein Status Grid - Date: 23:09, 3 November 2007 (UTC)
[edit] Vebose Log - Date: 23:09, 3 November 2007 (UTC)
- INFO: Beginning work on ABCG2... {November 3, 2007 4:06:51 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {November 3, 2007 4:07:58 PM PDT}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = ATP-binding cassette, sub-family G (WHITE), member 2
| HGNCid = 74
| Symbol = ABCG2
| AltSymbols =; MRX; BCRP1; ABC15; ABCP; BCRP; BMDP; CDw338; EST157481; MGC102821; MXR; MXR1
| OMIM = 603756
| ECnumber =
| Homologene = 55852
| MGIid = 1347061
| GeneAtlas_image1 = PBB_GE_ABCG2_209735_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008559 |text = xenobiotic-transporting ATPase activity}} {{GNF_GO|id=GO:0016887 |text = ATPase activity}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0042493 |text = response to drug}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 9429
| Hs_Ensembl = ENSG00000118777
| Hs_RefseqProtein = NP_004818
| Hs_RefseqmRNA = NM_004827
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 89230441
| Hs_GenLoc_end = 89299035
| Hs_Uniprot = Q9UNQ0
| Mm_EntrezGene = 26357
| Mm_Ensembl = ENSMUSG00000029802
| Mm_RefseqmRNA = NM_011920
| Mm_RefseqProtein = NP_036050
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 58526249
| Mm_GenLoc_end = 58622028
| Mm_Uniprot = Q7TMS5
}}
}}
'''ATP-binding cassette, sub-family G (WHITE), member 2''', also known as '''ABCG2''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The membrane-associated protein encoded by this gene is included in the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the White subfamily. Alternatively referred to as a breast cancer resistance protein, this protein functions as a xenobiotic transporter which may play a major role in multi-drug resistance. It likely serves as a cellular defense mechanism in response to mitoxantrone and anthracycline exposure. Significant expression of this protein has been observed in the placenta, which may suggest a potential role for this molecule in placenta tissue.<ref>{{cite web | title = Entrez Gene: ABCG2 ATP-binding cassette, sub-family G (WHITE), member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9429| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schmitz G, Langmann T, Heimerl S |title=Role of ABCG1 and other ABCG family members in lipid metabolism. |journal=J. Lipid Res. |volume=42 |issue= 10 |pages= 1513-20 |year= 2002 |pmid= 11590207 |doi= }}
*{{cite journal | author=Ejendal KF, Hrycyna CA |title=Multidrug resistance and cancer: the role of the human ABC transporter ABCG2. |journal=Curr. Protein Pept. Sci. |volume=3 |issue= 5 |pages= 503-11 |year= 2003 |pmid= 12369998 |doi= }}
*{{cite journal | author=Doyle LA, Ross DD |title=Multidrug resistance mediated by the breast cancer resistance protein BCRP (ABCG2). |journal=Oncogene |volume=22 |issue= 47 |pages= 7340-58 |year= 2003 |pmid= 14576842 |doi= 10.1038/sj.onc.1206938 }}
*{{cite journal | author=Sugimoto Y, Tsukahara S, Ishikawa E, Mitsuhashi J |title=Breast cancer resistance protein: molecular target for anticancer drug resistance and pharmacokinetics/pharmacodynamics. |journal=Cancer Sci. |volume=96 |issue= 8 |pages= 457-65 |year= 2005 |pmid= 16108826 |doi= 10.1111/j.1349-7006.2005.00081.x }}
*{{cite journal | author=Ishikawa T, Tamura A, Saito H, ''et al.'' |title=Pharmacogenomics of the human ABC transporter ABCG2: from functional evaluation to drug molecular design. |journal=Naturwissenschaften |volume=92 |issue= 10 |pages= 451-63 |year= 2006 |pmid= 16160819 |doi= 10.1007/s00114-005-0019-4 }}
*{{cite journal | author=Krishnamurthy P, Schuetz JD |title=Role of ABCG2/BCRP in biology and medicine. |journal=Annu. Rev. Pharmacol. Toxicol. |volume=46 |issue= |pages= 381-410 |year= 2006 |pmid= 16402910 |doi= 10.1146/annurev.pharmtox.46.120604.141238 }}
*{{cite journal | author=Robey RW, Polgar O, Deeken J, ''et al.'' |title=ABCG2: determining its relevance in clinical drug resistance. |journal=Cancer Metastasis Rev. |volume=26 |issue= 1 |pages= 39-57 |year= 2007 |pmid= 17323127 |doi= 10.1007/s10555-007-9042-6 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ADAMTS13... {November 3, 2007 4:07:58 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {November 3, 2007 4:09:01 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_protein_box = yes
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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 = ADAM metallopeptidase with thrombospondin type 1 motif, 13
| HGNCid = 1366
| Symbol = ADAMTS13
| AltSymbols =; TTP; C9orf8; DKFZp434C2322; FLJ42993; MGC118899; MGC118900; VWFCP; vWF-CP
| OMIM = 604134
| ECnumber =
| Homologene = 16372
| MGIid = 2685556
| GeneAtlas_image1 = PBB_GE_ADAMTS13_220208_at_tn.png
| Function = {{GNF_GO|id=GO:0004222 |text = metalloendopeptidase activity}} {{GNF_GO|id=GO:0005178 |text = integrin binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0009986 |text = cell surface}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007160 |text = cell-matrix adhesion}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0009100 |text = glycoprotein metabolic process}} {{GNF_GO|id=GO:0016485 |text = protein processing}} {{GNF_GO|id=GO:0030168 |text = platelet activation}} {{GNF_GO|id=GO:0043171 |text = peptide catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 11093
| Hs_Ensembl = ENSG00000160323
| Hs_RefseqProtein = NP_620597
| Hs_RefseqmRNA = NM_139028
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 135276941
| Hs_GenLoc_end = 135314329
| Hs_Uniprot = Q76LX8
| Mm_EntrezGene = 279028
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_914175
| Mm_RefseqProtein = XP_919268
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''ADAM metallopeptidase with thrombospondin type 1 motif, 13''', also known as '''ADAMTS13''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motif) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The enzyme encoded by this gene is the von Willebrand Factor (vWF)-cleaving protease, which is responsible for cleaving at the site of Tyr842-Met843 of the vWF molecule. A deficiency of this enzyme is associated with thrombotic thrombocytopenic purpura. Alternative splicing of this gene generates at least three transcript variants encoding different isoforms.<ref>{{cite web | title = Entrez Gene: ADAMTS13 ADAM metallopeptidase with thrombospondin type 1 motif, 13| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11093| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tang BL |title=ADAMTS: a novel family of extracellular matrix proteases. |journal=Int. J. Biochem. Cell Biol. |volume=33 |issue= 1 |pages= 33-44 |year= 2001 |pmid= 11167130 |doi= }}
*{{cite journal | author=Fujimura Y, Matsumoto M, Yagi H, ''et al.'' |title=Von Willebrand factor-cleaving protease and Upshaw-Schulman syndrome. |journal=Int. J. Hematol. |volume=75 |issue= 1 |pages= 25-34 |year= 2002 |pmid= 11843286 |doi= }}
*{{cite journal | author=Zheng X, Majerus EM, Sadler JE |title=ADAMTS13 and TTP. |journal=Curr. Opin. Hematol. |volume=9 |issue= 5 |pages= 389-94 |year= 2003 |pmid= 12172456 |doi= }}
*{{cite journal | author=Tsai HM |title=Von Willebrand factor, ADAMTS13, and thrombotic thrombocytopenic purpura. |journal=J. Mol. Med. |volume=80 |issue= 10 |pages= 639-47 |year= 2003 |pmid= 12395148 |doi= 10.1007/s00109-002-0369-8 }}
*{{cite journal | author=Tsai HM |title=Platelet activation and the formation of the platelet plug: deficiency of ADAMTS13 causes thrombotic thrombocytopenic purpura. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=23 |issue= 3 |pages= 388-96 |year= 2003 |pmid= 12615692 |doi= 10.1161/01.ATV.0000058401.34021.D4 }}
*{{cite journal | author=Tsai HM |title=Is severe deficiency of ADAMTS-13 specific for thrombotic thrombocytopenic purpura? Yes. |journal=J. Thromb. Haemost. |volume=1 |issue= 4 |pages= 625-31 |year= 2003 |pmid= 12871390 |doi= }}
*{{cite journal | author=Remuzzi G |title=Is ADAMTS-13 deficiency specific for thrombotic thrombocytopenic purpura? No. |journal=J. Thromb. Haemost. |volume=1 |issue= 4 |pages= 632-4 |year= 2003 |pmid= 12871391 |doi= }}
*{{cite journal | author=Moake JL |title=von Willebrand factor, ADAMTS-13, and thrombotic thrombocytopenic purpura. |journal=Semin. Hematol. |volume=41 |issue= 1 |pages= 4-14 |year= 2004 |pmid= 14727254 |doi= }}
*{{cite journal | author=López JA, Dong JF |title=Cleavage of von Willebrand factor by ADAMTS-13 on endothelial cells. |journal=Semin. Hematol. |volume=41 |issue= 1 |pages= 15-23 |year= 2004 |pmid= 14727255 |doi= }}
*{{cite journal | author=Plaimauer B, Scheiflinger F |title=Expression and characterization of recombinant human ADAMTS-13. |journal=Semin. Hematol. |volume=41 |issue= 1 |pages= 24-33 |year= 2004 |pmid= 14727256 |doi= }}
*{{cite journal | author=Kokame K, Miyata T |title=Genetic defects leading to hereditary thrombotic thrombocytopenic purpura. |journal=Semin. Hematol. |volume=41 |issue= 1 |pages= 34-40 |year= 2004 |pmid= 14727257 |doi= }}
*{{cite journal | author=Schneppenheim R, Budde U, Hassenpflug W, Obser T |title=Severe ADAMTS-13 deficiency in childhood. |journal=Semin. Hematol. |volume=41 |issue= 1 |pages= 83-9 |year= 2004 |pmid= 14727263 |doi= }}
*{{cite journal | author=Kremer Hovinga JA, Studt JD, Lämmle B |title=The von Willebrand factor-cleaving protease (ADAMTS-13) and the diagnosis of thrombotic thrombocytopenic purpura (TTP). |journal=Pathophysiol. Haemost. Thromb. |volume=33 |issue= 5-6 |pages= 417-21 |year= 2005 |pmid= 15692254 |doi= 10.1159/000083839 }}
*{{cite journal | author=Levy GG, Motto DG, Ginsburg D |title=ADAMTS13 turns 3. |journal=Blood |volume=106 |issue= 1 |pages= 11-7 |year= 2005 |pmid= 15774620 |doi= 10.1182/blood-2004-10-4097 }}
*{{cite journal | author=George JN |title=ADAMTS13, thrombotic thrombocytopenic purpura, and hemolytic uremic syndrome. |journal=Curr. Hematol. Rep. |volume=4 |issue= 3 |pages= 167-9 |year= 2005 |pmid= 15865866 |doi= }}
*{{cite journal | author=Dong JF |title=Cleavage of ultra-large von Willebrand factor by ADAMTS-13 under flow conditions. |journal=J. Thromb. Haemost. |volume=3 |issue= 8 |pages= 1710-6 |year= 2005 |pmid= 16102037 |doi= 10.1111/j.1538-7836.2005.01360.x }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on AGER... {November 3, 2007 3:39:26 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {November 3, 2007 3:40:25 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Advanced glycosylation end product-specific receptor
| HGNCid = 320
| Symbol = AGER
| AltSymbols =; MGC22357; RAGE
| OMIM = 600214
| ECnumber =
| Homologene = 883
| MGIid = 893592
| GeneAtlas_image1 = PBB_GE_AGER_210081_at_tn.png
| GeneAtlas_image2 = PBB_GE_AGER_217046_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004888 |text = transmembrane receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{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:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 177
| Hs_Ensembl = ENSG00000204305
| Hs_RefseqProtein = NP_001127
| Hs_RefseqmRNA = NM_001136
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 32256723
| Hs_GenLoc_end = 32260079
| Hs_Uniprot = Q15109
| Mm_EntrezGene = 11596
| Mm_Ensembl = ENSMUSG00000015452
| Mm_RefseqmRNA = NM_007425
| Mm_RefseqProtein = NP_031451
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 34205918
| Mm_GenLoc_end = 34208988
| Mm_Uniprot = O35444
}}
}}
'''Advanced glycosylation end product-specific receptor''', also known as '''AGER''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the immunoglobulin superfamily of cell surface molecules. It is a receptor for various molecules, including the amyloidogenic form of serum amyloid A, amyloid-beta protein, members of the S100/calgranulin superfamily and advanced glycation end products. The gene lies within the major histocompatibility complex (MHC) class III region on chromosome 6. Alternative splicing results in two transcript variants encoding different isoforms.<ref>{{cite web | title = Entrez Gene: AGER advanced glycosylation end product-specific receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=177| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Naka Y, Bucciarelli LG, Wendt T, ''et al.'' |title=RAGE axis: Animal models and novel insights into the vascular complications of diabetes. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=24 |issue= 8 |pages= 1342-9 |year= 2005 |pmid= 15155381 |doi= 10.1161/01.ATV.0000133191.71196.90 }}
*{{cite journal | author=Simm A, Bartling B, Silber RE |title=RAGE: a new pleiotropic antagonistic gene? |journal=Ann. N. Y. Acad. Sci. |volume=1019 |issue= |pages= 228-31 |year= 2004 |pmid= 15247020 |doi= 10.1196/annals.1297.038 }}
*{{cite journal | author=Nawroth P, Bierhaus A, Marrero M, ''et al.'' |title=Atherosclerosis and restenosis: is there a role for RAGE? |journal=Curr. Diab. Rep. |volume=5 |issue= 1 |pages= 11-6 |year= 2005 |pmid= 15663911 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ATP7B... {November 3, 2007 3:40:25 PM PDT}
- UPLOAD: Added new Image to wiki:
{November 3, 2007 3:41:01 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {November 3, 2007 3:41:23 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ATP7B_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2arf.
| PDB = {{PDB2|2arf}}, {{PDB2|2ew9}}
| Name = ATPase, Cu++ transporting, beta polypeptide
| HGNCid = 870
| Symbol = ATP7B
| AltSymbols =; PWD; WC1; WD; WND
| OMIM = 606882
| ECnumber =
| Homologene = 20063
| MGIid = 103297
| GeneAtlas_image1 = PBB_GE_ATP7B_204624_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0003824 |text = catalytic activity}} {{GNF_GO|id=GO:0004008 |text = copper-exporting ATPase activity}} {{GNF_GO|id=GO:0005375 |text = copper ion transmembrane transporter activity}} {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0015662 |text = ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016820 |text = hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0046873 |text = metal ion transmembrane transporter activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005770 |text = late endosome}} {{GNF_GO|id=GO:0005802 |text = trans-Golgi network}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0016023 |text = cytoplasmic membrane-bound vesicle}} {{GNF_GO|id=GO:0016323 |text = basolateral plasma membrane}} {{GNF_GO|id=GO:0048471 |text = perinuclear region of cytoplasm}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006825 |text = copper ion transport}} {{GNF_GO|id=GO:0006878 |text = cellular copper ion homeostasis}} {{GNF_GO|id=GO:0006882 |text = cellular zinc ion homeostasis}} {{GNF_GO|id=GO:0007595 |text = lactation}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0015677 |text = copper ion import}} {{GNF_GO|id=GO:0015680 |text = intracellular copper ion transport}} {{GNF_GO|id=GO:0030001 |text = metal ion transport}} {{GNF_GO|id=GO:0046688 |text = response to copper ion}} {{GNF_GO|id=GO:0051208 |text = sequestering of calcium ion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 540
| Hs_Ensembl = ENSG00000123191
| Hs_RefseqProtein = NP_000044
| Hs_RefseqmRNA = NM_000053
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 13
| Hs_GenLoc_start = 51406893
| Hs_GenLoc_end = 51447305
| Hs_Uniprot = P35670
| Mm_EntrezGene = 11979
| Mm_Ensembl = ENSMUSG00000006567
| Mm_RefseqmRNA = NM_007511
| Mm_RefseqProtein = NP_031537
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 23459893
| Mm_GenLoc_end = 23525621
| Mm_Uniprot = Q64446
}}
}}
'''ATPase, Cu++ transporting, beta polypeptide''', also known as '''ATP7B''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is a member of the P-type cation transport ATPase family and encodes a protein with several membrane-spanning domains, an ATPase consensus sequence, a hinge domain, a phosphorylation site, and at least 2 putative copper-binding sites. This protein functions as a monomer, exporting copper out of the cells, such as the efflux of hepatic copper into the bile. Alternate transcriptional splice variants, encoding different isoforms with distinct cellular localizations, have been characterized. Mutations in this gene have been associated with Wilson disease (WD).<ref>{{cite web | title = Entrez Gene: ATP7B ATPase, Cu++ transporting, beta polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=540| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Harris ED |title=Cellular copper transport and metabolism. |journal=Annu. Rev. Nutr. |volume=20 |issue= |pages= 291-310 |year= 2000 |pmid= 10940336 |doi= 10.1146/annurev.nutr.20.1.291 }}
*{{cite journal | author=Cox DW, Moore SD |title=Copper transporting P-type ATPases and human disease. |journal=J. Bioenerg. Biomembr. |volume=34 |issue= 5 |pages= 333-8 |year= 2003 |pmid= 12539960 |doi= }}
*{{cite journal | author=Lutsenko S, Efremov RG, Tsivkovskii R, Walker JM |title=Human copper-transporting ATPase ATP7B (the Wilson's disease protein): biochemical properties and regulation. |journal=J. Bioenerg. Biomembr. |volume=34 |issue= 5 |pages= 351-62 |year= 2003 |pmid= 12539962 |doi= }}
*{{cite journal | author=Chappuis P, Bost M, Misrahi M, ''et al.'' |title=[Wilson disease: clinical and biological aspects] |journal=Ann. Biol. Clin. (Paris) |volume=63 |issue= 5 |pages= 457-66 |year= 2006 |pmid= 16230279 |doi= }}
*{{cite journal | author=La Fontaine S, Mercer JF |title=Trafficking of the copper-ATPases, ATP7A and ATP7B: role in copper homeostasis. |journal=Arch. Biochem. Biophys. |volume=463 |issue= 2 |pages= 149-67 |year= 2007 |pmid= 17531189 |doi= 10.1016/j.abb.2007.04.021 }}
*{{cite journal | author=Lutsenko S, LeShane ES, Shinde U |title=Biochemical basis of regulation of human copper-transporting ATPases. |journal=Arch. Biochem. Biophys. |volume=463 |issue= 2 |pages= 134-48 |year= 2007 |pmid= 17562324 |doi= 10.1016/j.abb.2007.04.013 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CFLAR... {November 3, 2007 4:00:39 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {November 3, 2007 4:06:51 PM PDT}
<!-- 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 = CASP8 and FADD-like apoptosis regulator
| HGNCid = 1876
| Symbol = CFLAR
| AltSymbols =; CASH; CASP8AP1; CLARP; Casper; FLAME; FLAME-1; FLIP; I-FLICE; MRIT; USURPIN; c-FLIP; c-FLIPL; c-FLIPR; c-FLIPS
| OMIM = 603599
| ECnumber =
| Homologene = 7652
| MGIid = 1336166
| GeneAtlas_image1 = PBB_GE_CFLAR_211317_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CFLAR_208485_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_CFLAR_209508_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0030693 |text = caspase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0008624 |text = induction of apoptosis by extracellular signals}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8837
| Hs_Ensembl = ENSG00000003402
| Hs_RefseqProtein = NP_003870
| Hs_RefseqmRNA = NM_003879
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 201689135
| Hs_GenLoc_end = 201737246
| Hs_Uniprot = O15519
| Mm_EntrezGene = 12633
| Mm_Ensembl = ENSMUSG00000026031
| Mm_RefseqmRNA = NM_009805
| Mm_RefseqProtein = NP_033935
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 58656054
| Mm_GenLoc_end = 58699719
| Mm_Uniprot = Q812G4
}}
}}
'''CASP8 and FADD-like apoptosis regulator''', also known as '''CFLAR''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Abe K, Kurakin A, Mohseni-Maybodi M, ''et al.'' |title=The complexity of TNF-related apoptosis-inducing ligand. |journal=Ann. N. Y. Acad. Sci. |volume=926 |issue= |pages= 52-63 |year= 2001 |pmid= 11193041 |doi= }}
*{{cite journal | author=Dutton A, Young LS, Murray PG |title=The role of cellular FLICE inhibitory protein (c-FLIP) in the pathogenesis and treatment of cancer. |journal=Expert Opin. Ther. Targets |volume=10 |issue= 1 |pages= 27-35 |year= 2006 |pmid= 16441226 |doi= 10.1517/14728222.10.1.27 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CSK... {November 3, 2007 3:41:23 PM PDT}
- UPLOAD: Added new Image to wiki:
{November 3, 2007 3:41:56 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {November 3, 2007 3:42:06 PM PDT}
<!-- 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_CSK_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1byg.
| PDB = {{PDB2|1byg}}, {{PDB2|1csk}}, {{PDB2|1jeg}}, {{PDB2|1k9a}}
| Name = C-src tyrosine kinase
| HGNCid = 2444
| Symbol = CSK
| AltSymbols =; MGC117393
| OMIM = 124095
| ECnumber =
| Homologene = 55818
| MGIid = 88537
| GeneAtlas_image1 = PBB_GE_CSK_202329_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:0008022 |text = protein C-terminus binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005911 |text = intercellular junction}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1445
| Hs_Ensembl = ENSG00000103653
| Hs_RefseqProtein = NP_004374
| Hs_RefseqmRNA = NM_004383
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 72861489
| Hs_GenLoc_end = 72882524
| Hs_Uniprot = P41240
| Mm_EntrezGene = 12988
| Mm_Ensembl = ENSMUSG00000032312
| Mm_RefseqmRNA = NM_007783
| Mm_RefseqProtein = NP_031809
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 57424784
| Mm_GenLoc_end = 57443375
| Mm_Uniprot = Q3UVH2
}}
}}
'''C-src tyrosine kinase''', also known as '''CSK''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Mustelin T, Taskén K |title=Positive and negative regulation of T-cell activation through kinases and phosphatases. |journal=Biochem. J. |volume=371 |issue= Pt 1 |pages= 15-27 |year= 2003 |pmid= 12485116 |doi= 10.1042/BJ20021637 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CYP17A1... {November 3, 2007 3:44:04 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {November 3, 2007 3:44:48 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Cytochrome P450, family 17, subfamily A, polypeptide 1
| HGNCid = 2593
| Symbol = CYP17A1
| AltSymbols =; CPT7; CYP17; P450C17; S17AH
| OMIM = 609300
| ECnumber =
| Homologene = 73875
| MGIid = 88586
| GeneAtlas_image1 = PBB_GE_CYP17A1_205502_at_tn.png
| Function = {{GNF_GO|id=GO:0004497 |text = monooxygenase activity}} {{GNF_GO|id=GO:0004508 |text = steroid 17-alpha-monooxygenase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0019825 |text = oxygen binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006700 |text = C21-steroid hormone biosynthetic process}} {{GNF_GO|id=GO:0007548 |text = sex differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1586
| Hs_Ensembl = ENSG00000148795
| Hs_RefseqProtein = NP_000093
| Hs_RefseqmRNA = NM_000102
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 104580278
| Hs_GenLoc_end = 104587280
| Hs_Uniprot = P05093
| Mm_EntrezGene = 13074
| Mm_Ensembl = ENSMUSG00000003555
| Mm_RefseqmRNA = NM_007809
| Mm_RefseqProtein = NP_031835
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 46720489
| Mm_GenLoc_end = 46726285
| Mm_Uniprot = Q3UYU1
}}
}}
'''Cytochrome P450, family 17, subfamily A, polypeptide 1''', also known as '''CYP17A1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum. It has both 17alpha-hydroxylase and 17,20-lyase activities and is a key enzyme in the steroidogenic pathway that produces progestins, mineralocorticoids, glucocorticoids, androgens, and estrogens. Mutations in this gene are associated with isolated steroid-17 alpha-hydroxylase deficiency, 17-alpha-hydroxylase/17,20-lyase deficiency, pseudohermaphroditism, and adrenal hyperplasia.<ref>{{cite web | title = Entrez Gene: CYP17A1 cytochrome P450, family 17, subfamily A, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1586| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Miura K, Yasuda K, Yanase T, ''et al.'' |title=Mutation of cytochrome P-45017 alpha gene (CYP17) in a Japanese patient previously reported as having glucocorticoid-responsive hyperaldosteronism: with a review of Japanese patients with mutations of CYP17. |journal=J. Clin. Endocrinol. Metab. |volume=81 |issue= 10 |pages= 3797-801 |year= 1996 |pmid= 8855840 |doi= }}
*{{cite journal | author=Miller WL, Geller DH, Auchus RJ |title=The molecular basis of isolated 17,20 lyase deficiency. |journal=Endocr. Res. |volume=24 |issue= 3-4 |pages= 817-25 |year= 1999 |pmid= 9888582 |doi= }}
*{{cite journal | author=Strauss JF |title=Some new thoughts on the pathophysiology and genetics of polycystic ovary syndrome. |journal=Ann. N. Y. Acad. Sci. |volume=997 |issue= |pages= 42-8 |year= 2004 |pmid= 14644808 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CYP2C9... {November 3, 2007 3:42:06 PM PDT}
- UPLOAD: Added new Image to wiki:
{November 3, 2007 3:43:39 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {November 3, 2007 3:44:04 PM PDT}
<!-- 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_CYP2C9_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1og2.
| PDB = {{PDB2|1og2}}, {{PDB2|1og5}}, {{PDB2|1r9o}}
| Name = Cytochrome P450, family 2, subfamily C, polypeptide 9
| HGNCid = 2623
| Symbol = CYP2C9
| AltSymbols =; CYP2C; CPC9; CYP2C10; MGC149605; MGC88320; P450 MP-4; P450 PB-1; P450IIC9
| OMIM = 601130
| ECnumber =
| Homologene = 86657
| MGIid = 103238
| GeneAtlas_image1 = PBB_GE_CYP2C9_214421_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_CYP2C9_216025_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_CYP2C9_216661_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0016712 |text = oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen}} {{GNF_GO|id=GO:0018675 |text = (S)-limonene 6-monooxygenase activity}} {{GNF_GO|id=GO:0018676 |text = (S)-limonene 7-monooxygenase activity}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1559
| Hs_Ensembl = ENSG00000138109
| Hs_RefseqProtein = NP_000762
| Hs_RefseqmRNA = NM_000771
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 96688418
| Hs_GenLoc_end = 96739137
| Hs_Uniprot = P11712
| Mm_EntrezGene = 13095
| Mm_Ensembl = ENSMUSG00000003053
| Mm_RefseqmRNA = NM_007815
| Mm_RefseqProtein = NP_031841
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 39340422
| Mm_GenLoc_end = 39384010
| Mm_Uniprot = Q3UEF2
}}
}}
'''Cytochrome P450, family 2, subfamily C, polypeptide 9''', also known as '''CYP2C9''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum and its expression is induced by rifampin. The enzyme is known to metabolize many xenobiotics, including phenytoin, tolbutamide, ibuprofen and S-warfarin. Studies identifying individuals who are poor metabolizers of phenytoin and tolbutamide suggest that this gene is polymorphic. The gene is located within a cluster of cytochrome P450 genes on chromosome 10q24.<ref>{{cite web | title = Entrez Gene: CYP2C9 cytochrome P450, family 2, subfamily C, polypeptide 9| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1559| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Goldstein JA, de Morais SM |title=Biochemistry and molecular biology of the human CYP2C subfamily. |journal=Pharmacogenetics |volume=4 |issue= 6 |pages= 285-99 |year= 1995 |pmid= 7704034 |doi= }}
*{{cite journal | author=Miners JO, Birkett DJ |title=Cytochrome P4502C9: an enzyme of major importance in human drug metabolism. |journal=British journal of clinical pharmacology |volume=45 |issue= 6 |pages= 525-38 |year= 1998 |pmid= 9663807 |doi= }}
*{{cite journal | author=Smith G, Stubbins MJ, Harries LW, Wolf CR |title=Molecular genetics of the human cytochrome P450 monooxygenase superfamily. |journal=Xenobiotica |volume=28 |issue= 12 |pages= 1129-65 |year= 1999 |pmid= 9890157 |doi= }}
*{{cite journal | author=Henderson RF |title=Species differences in the metabolism of olefins: implications for risk assessment. |journal=Chem. Biol. Interact. |volume=135-136 |issue= |pages= 53-64 |year= 2001 |pmid= 11397381 |doi= }}
*{{cite journal | author=Xie HG, Prasad HC, Kim RB, Stein CM |title=CYP2C9 allelic variants: ethnic distribution and functional significance. |journal=Adv. Drug Deliv. Rev. |volume=54 |issue= 10 |pages= 1257-70 |year= 2003 |pmid= 12406644 |doi= }}
*{{cite journal | author=Palkimas MP, Skinner HM, Gandhi PJ, Gardner AJ |title=Polymorphism induced sensitivity to warfarin: a review of the literature. |journal=J. Thromb. Thrombolysis |volume=15 |issue= 3 |pages= 205-12 |year= 2004 |pmid= 14739630 |doi= 10.1023/B:THRO.0000011376.12309.af }}
*{{cite journal | author=Daly AK, Aithal GP |title=Genetic regulation of warfarin metabolism and response. |journal=Seminars in vascular medicine |volume=3 |issue= 3 |pages= 231-8 |year= 2004 |pmid= 15199455 |doi= 10.1055/s-2003-44458 }}
*{{cite journal | author=García-Martín E, Martínez C, Ladero JM, Agúndez JA |title=Interethnic and intraethnic variability of CYP2C8 and CYP2C9 polymorphisms in healthy individuals. |journal=Molecular diagnosis & therapy |volume=10 |issue= 1 |pages= 29-40 |year= 2007 |pmid= 16646575 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ELA2... {November 3, 2007 3:44:48 PM PDT}
- UPLOAD: Added new Image to wiki:
{November 3, 2007 3:45:27 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {November 3, 2007 3:45:48 PM PDT}
<!-- 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_ELA2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1b0f.
| PDB = {{PDB2|1b0f}}, {{PDB2|1h1b}}, {{PDB2|1hne}}, {{PDB2|1ppf}}, {{PDB2|1ppg}}
| Name = Elastase 2, neutrophil
| HGNCid = 3309
| Symbol = ELA2
| AltSymbols =; HLE; HNE; NE; PMN-E
| OMIM = 130130
| ECnumber =
| Homologene = 20455
| MGIid = 2679229
| GeneAtlas_image1 = PBB_GE_ELA2_206871_at_tn.png
| Function = {{GNF_GO|id=GO:0004252 |text = serine-type endopeptidase activity}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}} {{GNF_GO|id=GO:0008367 |text = bacterial binding}} {{GNF_GO|id=GO:0019955 |text = cytokine binding}} {{GNF_GO|id=GO:0042708 |text = elastase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0009986 |text = cell surface}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006874 |text = cellular calcium ion homeostasis}} {{GNF_GO|id=GO:0006909 |text = phagocytosis}} {{GNF_GO|id=GO:0009411 |text = response to UV}} {{GNF_GO|id=GO:0030163 |text = protein catabolic process}} {{GNF_GO|id=GO:0043406 |text = positive regulation of MAPK activity}} {{GNF_GO|id=GO:0045079 |text = negative regulation of chemokine biosynthetic process}} {{GNF_GO|id=GO:0045415 |text = negative regulation of interleukin-8 biosynthetic process}} {{GNF_GO|id=GO:0045416 |text = positive regulation of interleukin-8 biosynthetic process}} {{GNF_GO|id=GO:0048661 |text = positive regulation of smooth muscle cell proliferation}} {{GNF_GO|id=GO:0050728 |text = negative regulation of inflammatory response}} {{GNF_GO|id=GO:0050900 |text = leukocyte migration}} {{GNF_GO|id=GO:0050922 |text = negative regulation of chemotaxis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1991
| Hs_Ensembl = ENSG00000197561
| Hs_RefseqProtein = NP_001963
| Hs_RefseqmRNA = NM_001972
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 803291
| Hs_GenLoc_end = 807242
| Hs_Uniprot = P08246
| Mm_EntrezGene = 50701
| Mm_Ensembl = ENSMUSG00000020125
| Mm_RefseqmRNA = NM_015779
| Mm_RefseqProtein = NP_056594
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 79289464
| Mm_GenLoc_end = 79291246
| Mm_Uniprot = Q9Z284
}}
}}
'''Elastase 2, neutrophil''', also known as '''ELA2''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six elastase genes which encode the structurally similar proteins elastase 1, 2, 2A, 2B, 3A, and 3B. Elastase 2 hydrolyzes proteins within specialized neutrophil lysosomes, called azurophil granules, as well as proteins of the extracellular matrix following the protein's release from activated neutrophils. Elastase 2 may play a role in degenerative and inflammatory diseases by its proteolysis of collagen-IV and elastin of the extracellular matrix. This protein degrades the outer membrane protein A (OmpA) of E. coli as well as the virulence factors of such bacteria as Shigella, Salmonella and Yersinia. Mutations in this gene are associated with cyclic neutropenia and severe congenital neutropenia (SCN). This gene is clustered with other serine protease gene family members, azurocidin 1 and proteinase 3 genes, at chromosome 19pter. All 3 genes are expressed coordinately and their protein products are packaged together into azurophil granules during neutrophil differentiation.<ref>{{cite web | title = Entrez Gene: ELA2 elastase 2, neutrophil| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1991| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Dale DC, Liles WC, Garwicz D, Aprikyan AG |title=Clinical implications of mutations of neutrophil elastase in congenital and cyclic neutropenia. |journal=J. Pediatr. Hematol. Oncol. |volume=23 |issue= 4 |pages= 208-10 |year= 2002 |pmid= 11846296 |doi= }}
*{{cite journal | author=Horwitz M, Benson KF, Duan Z, ''et al.'' |title=Role of neutrophil elastase in bone marrow failure syndromes: molecular genetic revival of the chalone hypothesis. |journal=Curr. Opin. Hematol. |volume=10 |issue= 1 |pages= 49-54 |year= 2003 |pmid= 12483111 |doi= }}
*{{cite journal | author=Ancliff PJ, Gale RE, Linch DC |title=Neutrophil elastase mutations in congenital neutropenia. |journal=Hematology |volume=8 |issue= 3 |pages= 165-71 |year= 2003 |pmid= 12745650 |doi= 10.1080/1024533031000107497 }}
*{{cite journal | author=Horwitz M, Benson KF, Duan Z, ''et al.'' |title=Hereditary neutropenia: dogs explain human neutrophil elastase mutations. |journal=Trends in molecular medicine |volume=10 |issue= 4 |pages= 163-70 |year= 2004 |pmid= 15059607 |doi= 10.1016/j.molmed.2004.02.002 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ETS1... {November 3, 2007 3:45:48 PM PDT}
- UPLOAD: Added new Image to wiki:
{November 3, 2007 3:46:29 PM PDT}
- CREATE: Found no pages, creating new page. {November 3, 2007 3:46:45 PM PDT}
- CREATED: Created new protein page: ETS1 {November 3, 2007 3:46:55 PM PDT}
- INFO: Beginning work on F10... {November 3, 2007 3:46:55 PM PDT}
- UPLOAD: Added new Image to wiki:
{November 3, 2007 3:47:29 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {November 3, 2007 3:47:40 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_F10_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1c5m.
| PDB = {{PDB2|1c5m}}, {{PDB2|1ezq}}, {{PDB2|1f0r}}, {{PDB2|1f0s}}, {{PDB2|1fax}}, {{PDB2|1fjs}}, {{PDB2|1g2l}}, {{PDB2|1g2m}}, {{PDB2|1hcg}}, {{PDB2|1ioe}}, {{PDB2|1iqe}}, {{PDB2|1iqf}}, {{PDB2|1iqg}}, {{PDB2|1iqh}}, {{PDB2|1iqi}}, {{PDB2|1iqj}}, {{PDB2|1iqk}}, {{PDB2|1iql}}, {{PDB2|1iqm}}, {{PDB2|1iqn}}, {{PDB2|1ksn}}, {{PDB2|1kye}}, {{PDB2|1lpg}}, {{PDB2|1lpk}}, {{PDB2|1lpz}}, {{PDB2|1lqd}}, {{PDB2|1mq5}}, {{PDB2|1mq6}}, {{PDB2|1nfu}}, {{PDB2|1nfw}}, {{PDB2|1nfx}}, {{PDB2|1nfy}}, {{PDB2|1p0s}}, {{PDB2|1v3x}}, {{PDB2|1wu1}}, {{PDB2|1xka}}, {{PDB2|1xkb}}, {{PDB2|1z6e}}, {{PDB2|2bmg}}, {{PDB2|2boh}}, {{PDB2|2bok}}, {{PDB2|2bq6}}, {{PDB2|2bq7}}, {{PDB2|2bqw}}, {{PDB2|2cji}}, {{PDB2|2d1j}}, {{PDB2|2fzz}}, {{PDB2|2g00}}, {{PDB2|2gd4}}, {{PDB2|2h9e}}, {{PDB2|2j2u}}, {{PDB2|2j34}}, {{PDB2|2j38}}, {{PDB2|2j4i}}, {{PDB2|2j94}}, {{PDB2|2j95}}, {{PDB2|2uwl}}, {{PDB2|2uwo}}, {{PDB2|2uwp}}
| Name = Coagulation factor X
| HGNCid = 3528
| Symbol = F10
| AltSymbols =; FX; FXA
| OMIM = 227600
| ECnumber =
| Homologene = 30976
| MGIid = 103107
| GeneAtlas_image1 = PBB_GE_F10_205620_at_tn.png
| Function = {{GNF_GO|id=GO:0003804 |text = coagulation factor Xa activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2159
| Hs_Ensembl = ENSG00000126218
| Hs_RefseqProtein = NP_000495
| Hs_RefseqmRNA = NM_000504
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 13
| Hs_GenLoc_start = 112825114
| Hs_GenLoc_end = 112851844
| Hs_Uniprot = P00742
| Mm_EntrezGene = 14058
| Mm_Ensembl = ENSMUSG00000031444
| Mm_RefseqmRNA = NM_007972
| Mm_RefseqProtein = NP_031998
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 13037299
| Mm_GenLoc_end = 13055859
| Mm_Uniprot = Q3TBR2
}}
}}
'''Coagulation factor X''', also known as '''F10''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes the vitamin K-dependent coagulation factor X of the blood coagulation cascade. This factor undergoes multiple processing steps before its preproprotein is converted to a mature two-chain form by the excision of the tripeptide RKR. Two chains of the factor are held together by 1 or more disulfide bonds; the light chain contains 2 EGF-like domains, while the heavy chain contains the catalytic domain which is structurally homologous to those of the other hemostatic serine proteases. The mature factor is activated by the cleavage of the activation peptide by factor IXa (in the intrisic pathway), or by factor VIIa (in the extrinsic pathway). The activated factor then converts prothrombin to thrombin in the presence of factor Va, Ca+2, and phospholipid during blood clotting. Mutations of this gene result in factor X deficiency, a hemorrhagic condition of variable severity.<ref>{{cite web | title = Entrez Gene: F10 coagulation factor X| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2159| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Cooper DN, Millar DS, Wacey A, ''et al.'' |title=Inherited factor X deficiency: molecular genetics and pathophysiology. |journal=Thromb. Haemost. |volume=78 |issue= 1 |pages= 161-72 |year= 1997 |pmid= 9198147 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GJB1... {November 3, 2007 3:47:40 PM PDT}
- CREATE: Found no pages, creating new page. {November 3, 2007 3:48:19 PM PDT}
- CREATED: Created new protein page: GJB1 {November 3, 2007 3:48:29 PM PDT}
- INFO: Beginning work on HBD... {November 3, 2007 3:48:29 PM PDT}
- UPLOAD: Added new Image to wiki:
{November 3, 2007 3:48:47 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {November 3, 2007 3:48:56 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_HBD_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a00.
| PDB = {{PDB2|1a00}}, {{PDB2|1a01}}, {{PDB2|1a0u}}, {{PDB2|1a0z}}, {{PDB2|1a3n}}, {{PDB2|1a3o}}, {{PDB2|1abw}}, {{PDB2|1aby}}, {{PDB2|1aj9}}, {{PDB2|1b86}}, {{PDB2|1bab}}, {{PDB2|1bbb}}, {{PDB2|1bij}}, {{PDB2|1buw}}, {{PDB2|1bz0}}, {{PDB2|1bz1}}, {{PDB2|1bzz}}, {{PDB2|1c7b}}, {{PDB2|1c7c}}, {{PDB2|1c7d}}, {{PDB2|1cbl}}, {{PDB2|1cbm}}, {{PDB2|1cls}}, {{PDB2|1cmy}}, {{PDB2|1coh}}, {{PDB2|1dke}}, {{PDB2|1dxt}}, {{PDB2|1dxu}}, {{PDB2|1dxv}}, {{PDB2|1fn3}}, {{PDB2|1g9v}}, {{PDB2|1gbu}}, {{PDB2|1gbv}}, {{PDB2|1gli}}, {{PDB2|1gzx}}, {{PDB2|1hab}}, {{PDB2|1hac}}, {{PDB2|1hba}}, {{PDB2|1hbb}}, {{PDB2|1hbs}}, {{PDB2|1hco}}, {{PDB2|1hdb}}, {{PDB2|1hga}}, {{PDB2|1hgb}}, {{PDB2|1hgc}}, {{PDB2|1hho}}, {{PDB2|1ird}}, {{PDB2|1j3y}}, {{PDB2|1j3z}}, {{PDB2|1j40}}, {{PDB2|1j41}}, {{PDB2|1j7s}}, {{PDB2|1j7w}}, {{PDB2|1j7y}}, {{PDB2|1jy7}}, {{PDB2|1k0y}}, {{PDB2|1k1k}}, {{PDB2|1kd2}}, {{PDB2|1lfl}}, {{PDB2|1lfq}}, {{PDB2|1lft}}, {{PDB2|1lfv}}, {{PDB2|1lfy}}, {{PDB2|1lfz}}, {{PDB2|1ljw}}, {{PDB2|1m9p}}, {{PDB2|1mko}}, {{PDB2|1nej}}, {{PDB2|1nih}}, {{PDB2|1nqp}}, {{PDB2|1o1i}}, {{PDB2|1o1j}}, {{PDB2|1o1k}}, {{PDB2|1o1l}}, {{PDB2|1o1m}}, {{PDB2|1o1n}}, {{PDB2|1o1o}}, {{PDB2|1o1p}}, {{PDB2|1qi8}}, {{PDB2|1qsh}}, {{PDB2|1qsi}}, {{PDB2|1qxd}}, {{PDB2|1qxe}}, {{PDB2|1r1x}}, {{PDB2|1r1y}}, {{PDB2|1rps}}, {{PDB2|1rq3}}, {{PDB2|1rq4}}, {{PDB2|1rqa}}, {{PDB2|1rvw}}, {{PDB2|1sdk}}, {{PDB2|1sdl}}, {{PDB2|1shr}}, {{PDB2|1si4}}, {{PDB2|1thb}}, {{PDB2|1uiw}}, {{PDB2|1vwt}}, {{PDB2|1xxt}}, {{PDB2|1xy0}}, {{PDB2|1xye}}, {{PDB2|1xz2}}, {{PDB2|1xz4}}, {{PDB2|1xz5}}, {{PDB2|1xz7}}, {{PDB2|1xzu}}, {{PDB2|1xzv}}, {{PDB2|1y09}}, {{PDB2|1y0a}}, {{PDB2|1y0c}}, {{PDB2|1y0d}}, {{PDB2|1y0t}}, {{PDB2|1y0w}}, {{PDB2|1y22}}, {{PDB2|1y2z}}, {{PDB2|1y31}}, {{PDB2|1y35}}, {{PDB2|1y45}}, {{PDB2|1y46}}, {{PDB2|1y4b}}, {{PDB2|1y4f}}, {{PDB2|1y4g}}, {{PDB2|1y4p}}, {{PDB2|1y4q}}, {{PDB2|1y4r}}, {{PDB2|1y4v}}, {{PDB2|1y5f}}, {{PDB2|1y5j}}, {{PDB2|1y5k}}, {{PDB2|1y7c}}, {{PDB2|1y7d}}, {{PDB2|1y7g}}, {{PDB2|1y7z}}, {{PDB2|1y83}}, {{PDB2|1y85}}, {{PDB2|1y8w}}, {{PDB2|1ydz}}, {{PDB2|1ye0}}, {{PDB2|1ye1}}, {{PDB2|1ye2}}, {{PDB2|1yen}}, {{PDB2|1yeo}}, {{PDB2|1yeq}}, {{PDB2|1yeu}}, {{PDB2|1yev}}, {{PDB2|1yff}}, {{PDB2|1yg5}}, {{PDB2|1ygd}}, {{PDB2|1ygf}}, {{PDB2|1yh9}}, {{PDB2|1yhe}}, {{PDB2|1yhr}}, {{PDB2|1yie}}, {{PDB2|1yih}}, {{PDB2|1yvq}}, {{PDB2|1yvt}}, {{PDB2|1yzi}}, {{PDB2|2d5z}}, {{PDB2|2d60}}, {{PDB2|2dn1}}, {{PDB2|2dn2}}, {{PDB2|2dn3}}, {{PDB2|2h35}}, {{PDB2|2hbc}}, {{PDB2|2hbd}}, {{PDB2|2hbe}}, {{PDB2|2hbf}}, {{PDB2|2hbs}}, {{PDB2|2hco}}, {{PDB2|2hhb}}, {{PDB2|2hhd}}, {{PDB2|2hhe}}, {{PDB2|3hhb}}, {{PDB2|4hhb}}, {{PDB2|6hbw}}
| Name = Hemoglobin, delta
| HGNCid = 4829
| Symbol = HBD
| AltSymbols =;
| OMIM = 142000
| ECnumber =
| Homologene = 73881
| MGIid = 96021
| Function = {{GNF_GO|id=GO:0005344 |text = oxygen transporter activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0019825 |text = oxygen binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005833 |text = hemoglobin complex}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0015671 |text = oxygen transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3045
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000510
| Hs_RefseqmRNA = NM_000519
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 15129
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_973056
| Mm_RefseqProtein = XP_978150
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Hemoglobin, delta''', also known as '''HBD''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The delta (HBD) and beta (HBB) genes are normally expressed in the adult: two alpha chains plus two beta chains constitute HbA, which in normal adult life comprises about 97% of the total hemoglobin. Two alpha chains plus two delta chains constitute HbA-2, which with HbF comprises the remaining 3% of adult hemoglobin. Five beta-like globin genes are found within a 45 kb cluster on chromosome 11 in the following order: 5'-epsilon--Ggamma--Agamma--delta--beta-3'. Mutations in the delta-globin gene are associated with beta-thalassemia.<ref>{{cite web | title = Entrez Gene: HBD hemoglobin, delta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3045| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schillirò G, Russo-Mancuso G, Dibenedetto SP, ''et al.'' |title=Six rare hemoglobin variants found in Sicily. |journal=Hemoglobin |volume=15 |issue= 5 |pages= 431-7 |year= 1992 |pmid= 1802885 |doi= }}
*{{cite journal | author=Higgs DR, Vickers MA, Wilkie AO, ''et al.'' |title=A review of the molecular genetics of the human alpha-globin gene cluster. |journal=Blood |volume=73 |issue= 5 |pages= 1081-104 |year= 1989 |pmid= 2649166 |doi= }}
*{{cite journal | author=Collins FS, Weissman SM |title=The molecular genetics of human hemoglobin. |journal=Prog. Nucleic Acid Res. Mol. Biol. |volume=31 |issue= |pages= 315-462 |year= 1985 |pmid= 6397774 |doi= }}
*{{cite journal | author=Giardina B, Messana I, Scatena R, Castagnola M |title=The multiple functions of hemoglobin. |journal=Crit. Rev. Biochem. Mol. Biol. |volume=30 |issue= 3 |pages= 165-96 |year= 1995 |pmid= 7555018 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HTR2A... {November 3, 2007 3:48:56 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {November 3, 2007 3:49:58 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_summary = yes
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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 = 5-hydroxytryptamine (serotonin) receptor 2A
| HGNCid = 5293
| Symbol = HTR2A
| AltSymbols =; 5-HT2A; HTR2
| OMIM = 182135
| ECnumber =
| Homologene = 68073
| MGIid = 109521
| GeneAtlas_image1 = PBB_GE_HTR2A_207135_at_tn.png
| GeneAtlas_image2 = PBB_GE_HTR2A_211616_s_at_tn.png
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004993 |text = serotonin receptor activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007210 |text = serotonin receptor signaling pathway}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3356
| Hs_Ensembl = ENSG00000102468
| Hs_RefseqProtein = NP_000612
| Hs_RefseqmRNA = NM_000621
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 13
| Hs_GenLoc_start = 46305514
| Hs_GenLoc_end = 46368179
| Hs_Uniprot = P28223
| Mm_EntrezGene = 15558
| Mm_Ensembl = ENSMUSG00000034997
| Mm_RefseqmRNA = NM_172812
| Mm_RefseqProtein = NP_766400
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 73374995
| Mm_GenLoc_end = 73441014
| Mm_Uniprot = Q543D4
}}
}}
'''5-hydroxytryptamine (serotonin) receptor 2A''', also known as '''HTR2A''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Raymond JR, Mukhin YV, Gelasco A, ''et al.'' |title=Multiplicity of mechanisms of serotonin receptor signal transduction. |journal=Pharmacol. Ther. |volume=92 |issue= 2-3 |pages= 179-212 |year= 2002 |pmid= 11916537 |doi= }}
*{{cite journal | author=Schins A, Honig A, Crijns H, ''et al.'' |title=Increased coronary events in depressed cardiovascular patients: 5-HT2A receptor as missing link? |journal=Psychosomatic medicine |volume=65 |issue= 5 |pages= 729-37 |year= 2004 |pmid= 14508013 |doi= }}
*{{cite journal | author=Correa H, De Marco L, Boson W, ''et al.'' |title=Association study of T102C 5-HT(2A) polymorphism in schizophrenic patients: diagnosis, psychopathology, and suicidal behavior. |journal=Dialogues in clinical neuroscience |volume=9 |issue= 1 |pages= 97-101 |year= 2007 |pmid= 17506229 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MBL2... {November 3, 2007 3:49:58 PM PDT}
- UPLOAD: Added new Image to wiki:
{November 3, 2007 3:50:37 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {November 3, 2007 3:51:03 PM PDT}
<!-- 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_MBL2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hup.
| PDB = {{PDB2|1hup}}
| Name = Mannose-binding lectin (protein C) 2, soluble (opsonic defect)
| HGNCid = 6922
| Symbol = MBL2
| AltSymbols =; COLEC1; HSMBPC; MBL; MBP; MBP1; MGC116832; MGC116833
| OMIM = 154545
| ECnumber =
| Homologene = 88328
| MGIid = 96924
| GeneAtlas_image1 = PBB_GE_MBL2_207256_at_tn.png
| Function = {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005529 |text = sugar binding}} {{GNF_GO|id=GO:0005537 |text = mannose binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0001867 |text = complement activation, lectin pathway}} {{GNF_GO|id=GO:0006817 |text = phosphate transport}} {{GNF_GO|id=GO:0006958 |text = complement activation, classical pathway}} {{GNF_GO|id=GO:0006979 |text = response to oxidative stress}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4153
| Hs_Ensembl = ENSG00000165471
| Hs_RefseqProtein = NP_000233
| Hs_RefseqmRNA = NM_000242
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 54195146
| Hs_GenLoc_end = 54201466
| Hs_Uniprot = P11226
| Mm_EntrezGene = 17195
| Mm_Ensembl = ENSMUSG00000024863
| Mm_RefseqmRNA = NM_010776
| Mm_RefseqProtein = NP_034906
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 30298939
| Mm_GenLoc_end = 30305678
| Mm_Uniprot = Q3UEK1
}}
}}
'''Mannose-binding lectin (protein C) 2, soluble (opsonic defect)''', also known as '''MBL2''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = MBL2 encodes the soluble mannose-binding protein found in serum. MBL2 recognizes mannose and N-acetylglucosamine on bacterial pathogens, and is capable of activating the classical complement pathway.<ref>{{cite web | title = Entrez Gene: MBL2 mannose-binding lectin (protein C) 2, soluble (opsonic defect)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4153| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Fraser IP, Koziel H, Ezekowitz RA |title=The serum mannose-binding protein and the macrophage mannose receptor are pattern recognition molecules that link innate and adaptive immunity. |journal=Semin. Immunol. |volume=10 |issue= 5 |pages= 363-72 |year= 1998 |pmid= 9799711 |doi= 10.1006/smim.1998.0141 }}
*{{cite journal | author=Ji X, Gewurz H, Spear GT |title=Mannose binding lectin (MBL) and HIV. |journal=Mol. Immunol. |volume=42 |issue= 2 |pages= 145-52 |year= 2005 |pmid= 15488604 |doi= 10.1016/j.molimm.2004.06.015 }}
*{{cite journal | author=Worthley DL, Bardy PG, Mullighan CG |title=Mannose-binding lectin: biology and clinical implications. |journal=Internal medicine journal |volume=35 |issue= 9 |pages= 548-55 |year= 2005 |pmid= 16105157 |doi= 10.1111/j.1445-5994.2005.00908.x }}
*{{cite journal | author=Worthley DL, Bardy PG, Gordon DL, Mullighan CG |title=Mannose-binding lectin and maladies of the bowel and liver. |journal=World J. Gastroenterol. |volume=12 |issue= 40 |pages= 6420-8 |year= 2007 |pmid= 17072973 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MGMT... {November 3, 2007 3:51:03 PM PDT}
- UPLOAD: Added new Image to wiki:
{November 3, 2007 3:51:37 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {November 3, 2007 3:51:46 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_MGMT_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1eh6.
| PDB = {{PDB2|1eh6}}, {{PDB2|1eh7}}, {{PDB2|1eh8}}, {{PDB2|1qnt}}, {{PDB2|1t38}}, {{PDB2|1t39}}, {{PDB2|1yfh}}
| Name = O-6-methylguanine-DNA methyltransferase
| HGNCid = 7059
| Symbol = MGMT
| AltSymbols =;
| OMIM = 156569
| ECnumber =
| Homologene = 31089
| MGIid = 96977
| GeneAtlas_image1 = PBB_GE_MGMT_204880_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003908 |text = methylated-DNA-[protein]-cysteine S-methyltransferase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0009008 |text = DNA-methyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006266 |text = DNA ligation}} {{GNF_GO|id=GO:0006307 |text = DNA dealkylation}} {{GNF_GO|id=GO:0043281 |text = regulation of caspase activity}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4255
| Hs_Ensembl = ENSG00000170430
| Hs_RefseqProtein = NP_002403
| Hs_RefseqmRNA = NM_002412
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 131155481
| Hs_GenLoc_end = 131455352
| Hs_Uniprot = P16455
| Mm_EntrezGene = 17314
| Mm_Ensembl = ENSMUSG00000054612
| Mm_RefseqmRNA = NM_008598
| Mm_RefseqProtein = NP_032624
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 136732967
| Mm_GenLoc_end = 136968609
| Mm_Uniprot = Q4VA39
}}
}}
'''O-6-methylguanine-DNA methyltransferase''', also known as '''MGMT''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Margison GP, Povey AC, Kaina B, Santibáñez Koref MF |title=Variability and regulation of O6-alkylguanine-DNA alkyltransferase. |journal=Carcinogenesis |volume=24 |issue= 4 |pages= 625-35 |year= 2003 |pmid= 12727789 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MICA... {November 3, 2007 3:51:46 PM PDT}
- UPLOAD: Added new Image to wiki:
{November 3, 2007 3:52:39 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {November 3, 2007 3:52:52 PM PDT}
<!-- 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_MICA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1b3j.
| PDB = {{PDB2|1b3j}}, {{PDB2|1hyr}}
| Name = MHC class I polypeptide-related sequence A
| HGNCid = 7090
| Symbol = MICA
| AltSymbols =; MGC111087; PERB11.1
| OMIM = 600169
| ECnumber =
| Homologene = 88329
| MGIid = 2179989
| GeneAtlas_image1 = PBB_GE_MICA_205904_at_tn.png
| GeneAtlas_image2 = PBB_GE_MICA_205905_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0032393 |text = MHC class I receptor activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0042612 |text = MHC class I protein complex}}
| Process = {{GNF_GO|id=GO:0002474 |text = antigen processing and presentation of peptide antigen via MHC class I}} {{GNF_GO|id=GO:0006950 |text = response to stress}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0006968 |text = cellular defense response}} {{GNF_GO|id=GO:0008037 |text = cell recognition}} {{GNF_GO|id=GO:0019882 |text = antigen processing and presentation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4276
| Hs_Ensembl = ENSG00000183214
| Hs_RefseqProtein = XP_001124652
| Hs_RefseqmRNA = XM_001124652
| Hs_GenLoc_db =
| Hs_GenLoc_chr = c6_QBL
| Hs_GenLoc_start = 31504273
| Hs_GenLoc_end = 31516090
| Hs_Uniprot =
| Mm_EntrezGene = 243864
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_985890
| Mm_RefseqProtein = XP_990984
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''MHC class I polypeptide-related sequence A''', also known as '''MICA''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = MICA encodes the higly polymorphic MHC (HLA) class I chain-related gene A. The protein product is expressed on the cell surface, although unlike canonical class I molecules does not seem to associate with beta-2-microglobulin. It is thought that MICA functions as a stress-induced antigen that is broadly recognized by intestinal epithelial gamma delta T cells.<ref>{{cite web | title = Entrez Gene: MICA MHC class I polypeptide-related sequence A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4276| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Klein J, O'hUigin C |title=The conundrum of nonclassical major histocompatibility complex genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 14 |pages= 6251-2 |year= 1994 |pmid= 8022769 |doi= }}
*{{cite journal | author=Bahram S, Spies T |title=The MIC gene family. |journal=Res. Immunol. |volume=147 |issue= 5 |pages= 328-33 |year= 1997 |pmid= 8876061 |doi= }}
*{{cite journal | author=Blumberg RS |title=Current concepts in mucosal immunity. II. One size fits all: nonclassical MHC molecules fulfill multiple roles in epithelial cell function. |journal=Am. J. Physiol. |volume=274 |issue= 2 Pt 1 |pages= G227-31 |year= 1998 |pmid= 9486173 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on POMC... {November 3, 2007 3:52:52 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {November 3, 2007 3:53:43 PM PDT}
<!-- 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 = Proopiomelanocortin (adrenocorticotropin/ beta-lipotropin/ alpha-melanocyte stimulating hormone/ beta-melanocyte stimulating hormone/ beta-endorphin)
| HGNCid = 9201
| Symbol = POMC
| AltSymbols =; LPH; MSH; ACTH; CLIP; NPP; POC
| OMIM = 176830
| ECnumber =
| Homologene = 723
| MGIid = 97742
| GeneAtlas_image1 = PBB_GE_POMC_205720_at_tn.png
| Function = {{GNF_GO|id=GO:0005179 |text = hormone activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}}
| Process = {{GNF_GO|id=GO:0006091 |text = generation of precursor metabolites and energy}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007218 |text = neuropeptide signaling pathway}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0008217 |text = blood pressure regulation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5443
| Hs_Ensembl = ENSG00000115138
| Hs_RefseqProtein = NP_000930
| Hs_RefseqmRNA = NM_000939
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 25237226
| Hs_GenLoc_end = 25245063
| Hs_Uniprot = P01189
| Mm_EntrezGene = 18976
| Mm_Ensembl = ENSMUSG00000020660
| Mm_RefseqmRNA = NM_008895
| Mm_RefseqProtein = NP_032921
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 3954967
| Mm_GenLoc_end = 3960634
| Mm_Uniprot = P01193
}}
}}
'''Proopiomelanocortin (adrenocorticotropin/ beta-lipotropin/ alpha-melanocyte stimulating hormone/ beta-melanocyte stimulating hormone/ beta-endorphin)''', also known as '''POMC''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a polypeptide hormone precursor that undergoes extensive, tissue-specific, post-translational processing via cleavage by subtilisin-like enzymes known as prohormone convertases. There are eight potential cleavage sites within the polypeptide precursor and, depending on tissue type and the available convertases, processing may yield as many as ten biologically active peptides involved in diverse cellular functions. The encoded protein is synthesized mainly in corticotroph cells of the anterior pituitary where four cleavage sites are used; adrenocorticotrophin, essential for normal steroidogenesis and the maintenance of normal adrenal weight, and lipotropin beta are the major end products. In other tissues, including the hypothalamus, placenta, and epithelium, all cleavage sites may be used, giving rise to peptides with roles in pain and energy homeostasis, melanocyte stimulation, and immune modulation. These include several distinct melanotropins, lipotropins, and endorphins that are contained within the adrenocorticotrophin and beta-lipotropin peptides. Mutations in this gene have been associated with early onset obesity, adrenal insufficiency, and red hair pigmentation. Alternatively spliced transcript variants encoding the same protein have been described.<ref>{{cite web | title = Entrez Gene: POMC proopiomelanocortin (adrenocorticotropin/ beta-lipotropin/ alpha-melanocyte stimulating hormone/ beta-melanocyte stimulating hormone/ beta-endorphin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5443| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bhardwaj RS, Luger TA |title=Proopiomelanocortin production by epidermal cells: evidence for an immune neuroendocrine network in the epidermis. |journal=Arch. Dermatol. Res. |volume=287 |issue= 1 |pages= 85-90 |year= 1995 |pmid= 7726641 |doi= }}
*{{cite journal | author=Raffin-Sanson ML, de Keyzer Y, Bertagna X |title=Proopiomelanocortin, a polypeptide precursor with multiple functions: from physiology to pathological conditions. |journal=Eur. J. Endocrinol. |volume=149 |issue= 2 |pages= 79-90 |year= 2003 |pmid= 12887283 |doi= }}
*{{cite journal | author=Dores RM, Lecaude S |title=Trends in the evolution of the proopiomelanocortin gene. |journal=Gen. Comp. Endocrinol. |volume=142 |issue= 1-2 |pages= 81-93 |year= 2005 |pmid= 15862552 |doi= 10.1016/j.ygcen.2005.02.003 }}
*{{cite journal | author=König S, Luger TA, Scholzen TE |title=Monitoring neuropeptide-specific proteases: processing of the proopiomelanocortin peptides adrenocorticotropin and alpha-melanocyte-stimulating hormone in the skin. |journal=Exp. Dermatol. |volume=15 |issue= 10 |pages= 751-61 |year= 2006 |pmid= 16984256 |doi= 10.1111/j.1600-0625.2006.00472.x }}
*{{cite journal | author=Farooqi S, O'Rahilly S |title=Genetics of obesity in humans. |journal=Endocr. Rev. |volume=27 |issue= 7 |pages= 710-18 |year= 2007 |pmid= 17122358 |doi= 10.1210/er.2006-0040 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SMN1... {November 3, 2007 3:53:43 PM PDT}
- UPLOAD: Added new Image to wiki:
{November 3, 2007 3:53:57 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {November 3, 2007 3:54:36 PM PDT}
<!-- 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_SMN1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1g5v.
| PDB = {{PDB2|1g5v}}, {{PDB2|1mhn}}
| Name = Survival of motor neuron 1, telomeric
| HGNCid = 11117
| Symbol = SMN1
| AltSymbols =; SMN; BCD541; SMA1; SMA2; SMA3; SMA4; SMNT; T-BCD541; C-BCD541; SMNC
| OMIM = 600354
| ECnumber =
| Homologene = 292
| MGIid = 109257
| Function = {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005681 |text = spliceosome}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0015030 |text = Cajal body}}
| Process = {{GNF_GO|id=GO:0000245 |text = spliceosome assembly}} {{GNF_GO|id=GO:0006397 |text = mRNA processing}} {{GNF_GO|id=GO:0008380 |text = RNA splicing}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6606
| Hs_Ensembl =
| Hs_RefseqProtein = XP_001126655
| Hs_RefseqmRNA = XM_001126655
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 20595
| Mm_Ensembl = ENSMUSG00000021645
| Mm_RefseqmRNA = NM_011420
| Mm_RefseqProtein = NP_035550
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 101225134
| Mm_GenLoc_end = 101237947
| Mm_Uniprot = Q3UMN7
}}
}}
'''Survival of motor neuron 1, telomeric''', also known as '''SMN1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is part of a 500 kb inverted duplication on chromosome 5q13. This duplicated region contains at least four genes and repetitive elements which make it prone to rearrangements and deletions. The repetitiveness and complexity of the sequence have also caused difficulty in determining the organization of this genomic region. The telomeric and centromeric copies of this gene are nearly identical and encode the same protein. However, mutations in this gene, the telomeric copy, are associated with spinal muscular atrophy; mutations in the centromeric copy do not lead to disease. The centromeric copy may be a modifier of disease caused by mutation in the telomeric copy. The critical sequence difference between the two genes is a single nucleotide in exon 7 which is thought to be an exon splice enhancer. It is thought that gene conversion events may involve the two genes, leading to varying copy numbers of each gene. The protein encoded by this gene localizes to both the cytoplasm and the nucleus. Within the nucleus, the protein localizes to subnuclear bodies called gems which are found near coiled bodies containing high concentrations of small ribonucleoproteins (snRNPs). This protein forms heteromeric complexes with proteins such as SIP1 and GEMIN4, and also interacts with several proteins known to be involved in the biogenesis of snRNPs, such as hnRNP U protein and the small nucleolar RNA binding protein. Two transcript variants are produced by this gene.<ref>{{cite web | title = Entrez Gene: SMN1 survival of motor neuron 1, telomeric| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6606| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hausmanowa-Petrusewicz I, Jedrzejowska M |title=Spinal muscular atrophy of childhood at the edge of the centuries. |journal=Funct. Neurol. |volume=16 |issue= 4 Suppl |pages= 247-53 |year= 2002 |pmid= 11996521 |doi= }}
*{{cite journal | author=Paushkin S, Gubitz AK, Massenet S, Dreyfuss G |title=The SMN complex, an assemblyosome of ribonucleoproteins. |journal=Curr. Opin. Cell Biol. |volume=14 |issue= 3 |pages= 305-12 |year= 2002 |pmid= 12067652 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TF... {November 3, 2007 3:54:36 PM PDT}
- UPLOAD: Added new Image to wiki:
{November 3, 2007 3:55:29 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {November 3, 2007 3:55:43 PM PDT}
<!-- 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_TF_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a8e.
| PDB = {{PDB2|1a8e}}, {{PDB2|1a8f}}, {{PDB2|1b3e}}, {{PDB2|1bp5}}, {{PDB2|1btj}}, {{PDB2|1d3k}}, {{PDB2|1d4n}}, {{PDB2|1dtg}}, {{PDB2|1fqe}}, {{PDB2|1fqf}}, {{PDB2|1jqf}}, {{PDB2|1n7w}}, {{PDB2|1n7x}}, {{PDB2|1n84}}, {{PDB2|1oqg}}, {{PDB2|1oqh}}, {{PDB2|1ryo}}, {{PDB2|1suv}}, {{PDB2|2hau}}, {{PDB2|2hav}}, {{PDB2|2o7u}}, {{PDB2|2o84}}
| Name = Transferrin
| HGNCid = 11740
| Symbol = TF
| AltSymbols =; DKFZp781D0156; PRO1557; PRO2086
| OMIM = 190000
| ECnumber =
| Homologene = 68153
| MGIid = 98821
| GeneAtlas_image1 = PBB_GE_TF_203400_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_TF_214063_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008199 |text = ferric iron binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005768 |text = endosome}} {{GNF_GO|id=GO:0030139 |text = endocytic vesicle}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006826 |text = iron ion transport}} {{GNF_GO|id=GO:0006879 |text = cellular iron ion homeostasis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7018
| Hs_Ensembl = ENSG00000091513
| Hs_RefseqProtein = NP_001054
| Hs_RefseqmRNA = NM_001063
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 134947925
| Hs_GenLoc_end = 134980325
| Hs_Uniprot = P02787
| Mm_EntrezGene = 22041
| Mm_Ensembl = ENSMUSG00000032554
| Mm_RefseqmRNA = NM_133977
| Mm_RefseqProtein = NP_598738
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 103067024
| Mm_GenLoc_end = 103088436
| Mm_Uniprot = Q3UBW7
}}
}}
'''Transferrin''', also known as '''TF''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a glycoprotein with an approximate molecular weight of 76.5 kDa. It is thought to have been created as a result of an ancient gene duplication event that led to generation of homologous C and N-terminal domains each of which binds 1 ion of ferric iron. The function of this encoded protein is to transport iron from the intestine, reticuloendothelial system, and liver parenchymal cells to all proliferating cells in the body. In addition to its function in iron transport, this protein may also have a physiologic role as granulocyte/pollen-binding protein (GPBP) involved in the removal of certain organic matter/allergins from serum.<ref>{{cite web | title = Entrez Gene: TF transferrin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7018| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hershberger CL, Larson JL, Arnold B, ''et al.'' |title=A cloned gene for human transferrin. |journal=Ann. N. Y. Acad. Sci. |volume=646 |issue= |pages= 140-54 |year= 1992 |pmid= 1809186 |doi= }}
*{{cite journal | author=Bowman BH, Yang FM, Adrian GS |title=Transferrin: evolution and genetic regulation of expression. |journal=Adv. Genet. |volume=25 |issue= |pages= 1-38 |year= 1989 |pmid= 3057819 |doi= }}
*{{cite journal | author=Parkkinen J, von Bonsdorff L, Ebeling F, Sahlstedt L |title=Function and therapeutic development of apotransferrin. |journal=Vox Sang. |volume=83 Suppl 1 |issue= |pages= 321-6 |year= 2003 |pmid= 12617162 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TFRC... {November 3, 2007 3:55:43 PM PDT}
- UPLOAD: Added new Image to wiki:
{November 3, 2007 3:57:00 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {November 3, 2007 3:57:16 PM PDT}
<!-- 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_TFRC_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cx8.
| PDB = {{PDB2|1cx8}}, {{PDB2|1de4}}, {{PDB2|1suv}}, {{PDB2|2nsu}}
| Name = Transferrin receptor (p90, CD71)
| HGNCid = 11763
| Symbol = TFRC
| AltSymbols =; CD71; TFR; TFR1; TRFR
| OMIM = 190010
| ECnumber =
| Homologene = 2429
| MGIid = 98822
| GeneAtlas_image1 = PBB_GE_TFRC_208691_at_tn.png
| GeneAtlas_image2 = PBB_GE_TFRC_207332_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004998 |text = transferrin receptor activity}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005768 |text = endosome}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016023 |text = cytoplasmic membrane-bound vesicle}} {{GNF_GO|id=GO:0048471 |text = perinuclear region of cytoplasm}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006826 |text = iron ion transport}} {{GNF_GO|id=GO:0006879 |text = cellular iron ion homeostasis}} {{GNF_GO|id=GO:0006897 |text = endocytosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7037
| Hs_Ensembl = ENSG00000072274
| Hs_RefseqProtein = NP_003225
| Hs_RefseqmRNA = NM_003234
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 197260553
| Hs_GenLoc_end = 197293343
| Hs_Uniprot = P02786
| Mm_EntrezGene = 22042
| Mm_Ensembl = ENSMUSG00000022797
| Mm_RefseqmRNA = NM_011638
| Mm_RefseqProtein = NP_035768
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 32528764
| Mm_GenLoc_end = 32552537
| Mm_Uniprot = Q542D9
}}
}}
'''Transferrin receptor (p90, CD71)''', also known as '''TFRC''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Moos T |title=Brain iron homeostasis. |journal=Danish medical bulletin |volume=49 |issue= 4 |pages= 279-301 |year= 2003 |pmid= 12553165 |doi= }}
*{{cite journal | author=Aisen P |title=Transferrin receptor 1. |journal=Int. J. Biochem. Cell Biol. |volume=36 |issue= 11 |pages= 2137-43 |year= 2005 |pmid= 15313461 |doi= 10.1016/j.biocel.2004.02.007 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TOP1... {November 3, 2007 3:57:16 PM PDT}
- UPLOAD: Added new Image to wiki:
{November 3, 2007 3:57:31 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {November 3, 2007 3:57:43 PM PDT}
<!-- 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_TOP1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a31.
| PDB = {{PDB2|1a31}}, {{PDB2|1a35}}, {{PDB2|1a36}}, {{PDB2|1ej9}}, {{PDB2|1k4s}}, {{PDB2|1k4t}}, {{PDB2|1lpq}}, {{PDB2|1nh3}}, {{PDB2|1r49}}, {{PDB2|1rr8}}, {{PDB2|1rrj}}, {{PDB2|1sc7}}, {{PDB2|1seu}}, {{PDB2|1t8i}}, {{PDB2|1tl8}}
| Name = Topoisomerase (DNA) I
| HGNCid = 11986
| Symbol = TOP1
| AltSymbols =; TOPI
| OMIM = 126420
| ECnumber =
| Homologene = 2467
| MGIid = 98788
| Function = {{GNF_GO|id=GO:0003682 |text = chromatin binding}} {{GNF_GO|id=GO:0003917 |text = DNA topoisomerase type I activity}} {{GNF_GO|id=GO:0003918 |text = DNA topoisomerase (ATP-hydrolyzing) activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005654 |text = nucleoplasm}} {{GNF_GO|id=GO:0005694 |text = chromosome}} {{GNF_GO|id=GO:0005730 |text = nucleolus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0043204 |text = perikaryon}}
| Process = {{GNF_GO|id=GO:0006260 |text = DNA replication}} {{GNF_GO|id=GO:0006265 |text = DNA topological change}} {{GNF_GO|id=GO:0040016 |text = embryonic cleavage}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7150
| Hs_Ensembl = ENSG00000198900
| Hs_RefseqProtein = NP_003277
| Hs_RefseqmRNA = NM_003286
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 39090876
| Hs_GenLoc_end = 39186541
| Hs_Uniprot = P11387
| Mm_EntrezGene = 21969
| Mm_Ensembl = ENSMUSG00000070544
| Mm_RefseqmRNA = NM_009408
| Mm_RefseqProtein = NP_033434
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 160337671
| Mm_GenLoc_end = 160414202
| Mm_Uniprot = Q3TPX7
}}
}}
'''Topoisomerase (DNA) I''', also known as '''TOP1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a DNA topoisomerase, an enzyme that controls and alters the topologic states of DNA during transcription. This enzyme catalyzes the transient breaking and rejoining of a single strand of DNA which allows the strands to pass through one another, thus altering the topology of DNA. This gene is localized to chromosome 20 and has pseudogenes which reside on chromosomes 1 and 22.<ref>{{cite web | title = Entrez Gene: TOP1 topoisomerase (DNA) I| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7150| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Friedberg EC |title=Relationships between DNA repair and transcription. |journal=Annu. Rev. Biochem. |volume=65 |issue= |pages= 15-42 |year= 1996 |pmid= 8811173 |doi= 10.1146/annurev.bi.65.070196.000311 }}
*{{cite journal | author=Leppard JB, Champoux JJ |title=Human DNA topoisomerase I: relaxation, roles, and damage control. |journal=Chromosoma |volume=114 |issue= 2 |pages= 75-85 |year= 2005 |pmid= 15830206 |doi= 10.1007/s00412-005-0345-5 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on UGT1A1... {November 3, 2007 4:09:01 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {November 3, 2007 4:09:41 PM PDT}
<!-- 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 = UDP glucuronosyltransferase 1 family, polypeptide A1
| HGNCid = 12530
| Symbol = UGT1A1
| AltSymbols =; UGT1; GNT1; UGT1A; UDPGT; HUG-BR1; UGT1*1
| OMIM = 191740
| ECnumber =
| Homologene = 83117
| MGIid = 98898
| Function = {{GNF_GO|id=GO:0015020 |text = glucuronosyltransferase activity}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006789 |text = bilirubin conjugation}} {{GNF_GO|id=GO:0007586 |text = digestion}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0008210 |text = estrogen metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 54658
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000454
| Hs_RefseqmRNA = NM_000463
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 394436
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_201645
| Mm_RefseqProtein = NP_964007
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''UDP glucuronosyltransferase 1 family, polypeptide A1''', also known as '''UGT1A1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a UDP-glucuronosyltransferase, an enzyme of the glucuronidation pathway that transforms small lipophilic molecules, such as steroids, bilirubin, hormones, and drugs, into water-soluble, excretable metabolites. This gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. The locus includes thirteen unique alternate first exons followed by four common exons. Four of the alternate first exons are considered pseudogenes. Each of the remaining nine 5' exons may be spliced to the four common exons, resulting in nine proteins with different N-termini and identical C-termini. Each first exon encodes the substrate binding site, and is regulated by its own promoter. The preferred substrate of this enzyme is bilirubin, although it also has moderate activity with simple phenols, flavones, and C18 steroids. Mutations in this gene result in Crigler-Najjar syndromes types I and II and in Gilbert syndrome.<ref>{{cite web | title = Entrez Gene: UGT1A1 UDP glucuronosyltransferase 1 family, polypeptide A1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54658| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Mackenzie PI, Owens IS, Burchell B, ''et al.'' |title=The UDP glycosyltransferase gene superfamily: recommended nomenclature update based on evolutionary divergence. |journal=Pharmacogenetics |volume=7 |issue= 4 |pages= 255-69 |year= 1997 |pmid= 9295054 |doi= }}
*{{cite journal | author=Tukey RH, Strassburg CP |title=Human UDP-glucuronosyltransferases: metabolism, expression, and disease. |journal=Annu. Rev. Pharmacol. Toxicol. |volume=40 |issue= |pages= 581-616 |year= 2000 |pmid= 10836148 |doi= 10.1146/annurev.pharmtox.40.1.581 }}
*{{cite journal | author=Kadakol A, Ghosh SS, Sappal BS, ''et al.'' |title=Genetic lesions of bilirubin uridine-diphosphoglucuronate glucuronosyltransferase (UGT1A1) causing Crigler-Najjar and Gilbert syndromes: correlation of genotype to phenotype. |journal=Hum. Mutat. |volume=16 |issue= 4 |pages= 297-306 |year= 2000 |pmid= 11013440 |doi= 10.1002/1098-1004(200010)16:4<297::AID-HUMU2>3.0.CO;2-Z }}
*{{cite journal | author=King CD, Rios GR, Green MD, Tephly TR |title=UDP-glucuronosyltransferases. |journal=Curr. Drug Metab. |volume=1 |issue= 2 |pages= 143-61 |year= 2001 |pmid= 11465080 |doi= }}
*{{cite journal | author=Bosma PJ |title=Inherited disorders of bilirubin metabolism. |journal=J. Hepatol. |volume=38 |issue= 1 |pages= 107-17 |year= 2003 |pmid= 12480568 |doi= }}
*{{cite journal | author=Innocenti F, Ratain MJ |title=Irinotecan treatment in cancer patients with UGT1A1 polymorphisms. |journal=Oncology (Williston Park, N.Y.) |volume=17 |issue= 5 Suppl 5 |pages= 52-5 |year= 2003 |pmid= 12800608 |doi= }}
*{{cite journal | author=Lee W, Lockhart AC, Kim RB, Rothenberg ML |title=Cancer pharmacogenomics: powerful tools in cancer chemotherapy and drug development. |journal=Oncologist |volume=10 |issue= 2 |pages= 104-11 |year= 2005 |pmid= 15709212 |doi= 10.1634/theoncologist.10-2-104 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on VIL2... {November 3, 2007 3:57:44 PM PDT}
- UPLOAD: Added new Image to wiki:
{November 3, 2007 3:59:14 PM PDT}
- CREATE: Found no pages, creating new page. {November 3, 2007 3:59:32 PM PDT}
- CREATED: Created new protein page: VIL2 {November 3, 2007 3:59:40 PM PDT}
- INFO: Beginning work on XPO1... {November 3, 2007 3:59:40 PM PDT}
- UPLOAD: Added new Image to wiki:
{November 3, 2007 4:00:17 PM PDT}
- CREATE: Found no pages, creating new page. {November 3, 2007 4:00:29 PM PDT}
- CREATED: Created new protein page: XPO1 {November 3, 2007 4:00:39 PM PDT}
end log.
