User:ProteinBoxBot/PBB Log Wiki 11-8-2007-B2-3

Log file for Protein Box Bot

Log page index: User:ProteinBoxBot/PBB_Log_Index

Protein Status Quick Log - Date: 18:30, 18 November 2007 (UTC)

Proteins without matches (11)

Proteins with a High Potential Match (7)

Redirected Proteins (7)

Manual Inspection (Page not found) (18)

Updated (7)

Protein Status Grid - Date: 18:30, 18 November 2007 (UTC)

Vebose Log - Date: 18:30, 18 November 2007 (UTC)

ATF1

• INFO: Beginning work on ATF1... {November 17, 2007 11:45:38 PM PST}
• SEARCH REDIRECT: Control Box Found: ATF1 {November 17, 2007 11:46:41 PM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:46:42 PM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:46:42 PM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:46:42 PM PST}
• UPDATED: Updated protein page: ATF1 {November 17, 2007 11:46:54 PM PST}

AXL

• INFO: Beginning work on AXL... {November 17, 2007 11:46:55 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:47:55 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_AXL_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 2c5d.
 | PDB = {{PDB2|2c5d}}
 | Name = AXL receptor tyrosine kinase
 | HGNCid = 905
 | Symbol = AXL
 | AltSymbols =; UFO
 | OMIM = 109135
 | ECnumber =  
 | Homologene = 7583
 | MGIid = 1347244
 | GeneAtlas_image1 = PBB_GE_AXL_202686_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_AXL_202685_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004714 |text = transmembrane receptor protein tyrosine kinase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} 
 | Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} 
 | Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 558
    | Hs_Ensembl = ENSG00000167601
    | Hs_RefseqProtein = NP_001690
    | Hs_RefseqmRNA = NM_001699
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 46416663
    | Hs_GenLoc_end = 46459510
    | Hs_Uniprot = P30530
    | Mm_EntrezGene = 26362
    | Mm_Ensembl = ENSMUSG00000002602
    | Mm_RefseqmRNA = NM_009465
    | Mm_RefseqProtein = NP_033491
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 25466034
    | Mm_GenLoc_end = 25497330
    | Mm_Uniprot = Q3TTM4
  }}
}}
'''AXL receptor tyrosine kinase''', also known as '''AXL''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AXL AXL receptor tyrosine kinase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=558| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = The protein encoded by this gene is a member of the receptor tyrosine kinase subfamily. Although it is similar to other receptor tyrosine kinases, the Axl protein represents a unique structure of the extracellular region that juxtaposes IgL and FNIII repeats. It transduce signals from the extracellular matrix into the cytoplasm by binding growth factors like vitamin K-dependent protein growth-arrest-specific gene 6. It is involved in the stimulation of cell proliferation. This receptor can also mediate cell aggregation by homophilic binding. Axl is a chronic myelogenous leukemia-associated oncogene and also associated with colon cancer and melanoma. It is in close vicinity to the bcl3 oncogene which is at 19q13.1-q13.2. The Axl gene is evolutionarily conserved between vertebrate species. This gene has two different alternatively spliced transcript variants.<ref name="entrez">{{cite web | title = Entrez Gene: AXL AXL receptor tyrosine kinase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=558| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Neubauer A, Burchert A, Maiwald C, ''et al.'' |title=Recent progress on the role of Axl, a receptor tyrosine kinase, in malignant transformation of myeloid leukemias. |journal=Leuk. Lymphoma |volume=25 |issue= 1-2 |pages= 91-6 |year= 1997 |pmid= 9130617 |doi=  }}
*{{cite journal  | author=O'Bryan JP, Frye RA, Cogswell PC, ''et al.'' |title=axl, a transforming gene isolated from primary human myeloid leukemia cells, encodes a novel receptor tyrosine kinase. |journal=Mol. Cell. Biol. |volume=11 |issue= 10 |pages= 5016-31 |year= 1991 |pmid= 1656220 |doi=  }}
*{{cite journal  | author=Bergsagel PL, Victor-Kobrin C, Timblin CR, ''et al.'' |title=A murine cDNA encodes a pan-epithelial glycoprotein that is also expressed on plasma cells. |journal=J. Immunol. |volume=148 |issue= 2 |pages= 590-6 |year= 1992 |pmid= 1729376 |doi=  }}
*{{cite journal  | author=Janssen JW, Schulz AS, Steenvoorden AC, ''et al.'' |title=A novel putative tyrosine kinase receptor with oncogenic potential. |journal=Oncogene |volume=6 |issue= 11 |pages= 2113-20 |year= 1991 |pmid= 1834974 |doi=  }}
*{{cite journal  | author=Partanen J, Mäkelä TP, Alitalo R, ''et al.'' |title=Putative tyrosine kinases expressed in K-562 human leukemia cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 22 |pages= 8913-7 |year= 1991 |pmid= 2247464 |doi=  }}
*{{cite journal  | author=Neubauer A, Fiebeler A, Graham DK, ''et al.'' |title=Expression of axl, a transforming receptor tyrosine kinase, in normal and malignant hematopoiesis. |journal=Blood |volume=84 |issue= 6 |pages= 1931-41 |year= 1994 |pmid= 7521695 |doi=  }}
*{{cite journal  | author=O'Bryan JP, Fridell YW, Koski R, ''et al.'' |title=The transforming receptor tyrosine kinase, Axl, is post-translationally regulated by proteolytic cleavage. |journal=J. Biol. Chem. |volume=270 |issue= 2 |pages= 551-7 |year= 1995 |pmid= 7822279 |doi=  }}
*{{cite journal  | author=Lee ST, Strunk KM, Spritz RA |title=A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes. |journal=Oncogene |volume=8 |issue= 12 |pages= 3403-10 |year= 1993 |pmid= 8247543 |doi=  }}
*{{cite journal  | author=Schulz AS, Schleithoff L, Faust M, ''et al.'' |title=The genomic structure of the human UFO receptor. |journal=Oncogene |volume=8 |issue= 2 |pages= 509-13 |year= 1993 |pmid= 8381225 |doi=  }}
*{{cite journal  | author=O'Bryan JP, Songyang Z, Cantley L, ''et al.'' |title=A mammalian adaptor protein with conserved Src homology 2 and phosphotyrosine-binding domains is related to Shc and is specifically expressed in the brain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 7 |pages= 2729-34 |year= 1996 |pmid= 8610109 |doi=  }}
*{{cite journal  | author=Mark MR, Chen J, Hammonds RG, ''et al.'' |title=Characterization of Gas6, a member of the superfamily of G domain-containing proteins, as a ligand for Rse and Axl. |journal=J. Biol. Chem. |volume=271 |issue= 16 |pages= 9785-9 |year= 1996 |pmid= 8621659 |doi=  }}
*{{cite journal  | author=Braunger J, Schleithoff L, Schulz AS, ''et al.'' |title=Intracellular signaling of the Ufo/Axl receptor tyrosine kinase is mediated mainly by a multi-substrate docking-site. |journal=Oncogene |volume=14 |issue= 22 |pages= 2619-31 |year= 1997 |pmid= 9178760 |doi= 10.1038/sj.onc.1201123 }}
*{{cite journal  | author=Tanaka K, Nagayama Y, Nakano T, ''et al.'' |title=Expression profile of receptor-type protein tyrosine kinase genes in the human thyroid. |journal=Endocrinology |volume=139 |issue= 3 |pages= 852-8 |year= 1998 |pmid= 9492013 |doi=  }}
*{{cite journal  | author=Yanagita M, Arai H, Ishii K, ''et al.'' |title=Gas6 regulates mesangial cell proliferation through Axl in experimental glomerulonephritis. |journal=Am. J. Pathol. |volume=158 |issue= 4 |pages= 1423-32 |year= 2001 |pmid= 11290560 |doi=  }}
*{{cite journal  | author=Sun WS, Misao R, Iwagaki S, ''et al.'' |title=Coexpression of growth arrest-specific gene 6 and receptor tyrosine kinases, Axl and Sky, in human uterine endometrium and ovarian endometriosis. |journal=Mol. Hum. Reprod. |volume=8 |issue= 6 |pages= 552-8 |year= 2003 |pmid= 12029073 |doi=  }}
*{{cite journal  | author=D'Arcangelo D, Gaetano C, Capogrossi MC |title=Acidification prevents endothelial cell apoptosis by Axl activation. |journal=Circ. Res. |volume=91 |issue= 7 |pages= e4-12 |year= 2002 |pmid= 12364394 |doi=  }}
*{{cite journal  | author=Hafizi S, Alindri F, Karlsson R, Dahlbäck B |title=Interaction of Axl receptor tyrosine kinase with C1-TEN, a novel C1 domain-containing protein with homology to tensin. |journal=Biochem. Biophys. Res. Commun. |volume=299 |issue= 5 |pages= 793-800 |year= 2003 |pmid= 12470648 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Ito M, Nakashima M, Nakayama T, ''et al.'' |title=Expression of receptor-type tyrosine kinase, Axl, and its ligand, Gas6, in pediatric thyroid carcinomas around chernobyl. |journal=Thyroid |volume=12 |issue= 11 |pages= 971-5 |year= 2003 |pmid= 12490074 |doi= 10.1089/105072502320908303 }}
}}
{{refend}}

{{protein-stub}}
 

CCL21

• INFO: Beginning work on CCL21... {November 18, 2007 10:21:40 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:22:21 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Chemokine (C-C motif) ligand 21
 | HGNCid = 10620
 | Symbol = CCL21
 | AltSymbols =; 6Ckine; CKb9; ECL; MGC34555; SCYA21; SLC; TCA4
 | OMIM = 602737
 | ECnumber =  
 | Homologene = 88457
 | MGIid =  
 | GeneAtlas_image1 = PBB_GE_CCL21_204606_at_tn.png
 | Function = {{GNF_GO|id=GO:0008009 |text = chemokine activity}} 
 | Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} 
 | Process = {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6366
    | Hs_Ensembl = ENSG00000137077
    | Hs_RefseqProtein = NP_002980
    | Hs_RefseqmRNA = NM_002989
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 9
    | Hs_GenLoc_start = 34699002
    | Hs_GenLoc_end = 34700147
    | Hs_Uniprot = O00585
    | Mm_EntrezGene =  
    | Mm_Ensembl =  
    | Mm_RefseqmRNA =  
    | Mm_RefseqProtein =  
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr =  
    | Mm_GenLoc_start =  
    | Mm_GenLoc_end =  
    | Mm_Uniprot =  
  }}
}}
'''Chemokine (C-C motif) ligand 21''', also known as '''CCL21''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CCL21 chemokine (C-C motif) ligand 21| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6366| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = This gene is one of several CC cytokine genes clustered on the p-arm of chromosome 9. Cytokines are a family of secreted proteins involved in immunoregulatory and inflammatory processes. The CC cytokines are proteins characterized by two adjacent cysteines. Similar to other chemokines the protein encoded by this gene inhibits hemopoiesis and stimulates chemotaxis. This protein is chemotactic in vitro for thymocytes and activated T cells, but not for B cells, macrophages, or neutrophils. The cytokine encoded by this gene may also play a role in mediating homing of lymphocytes to secondary lymphoid organs. It is a high affinity functional ligand for chemokine receptor 7 (CCR7) that is expressed on T and B lymphocytes and a known receptor for another member of the cytokine family (small inducible cytokine A19).<ref name="entrez">{{cite web | title = Entrez Gene: CCL21 chemokine (C-C motif) ligand 21| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6366| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Nagira M, Imai T, Hieshima K, ''et al.'' |title=Molecular cloning of a novel human CC chemokine secondary lymphoid-tissue chemokine that is a potent chemoattractant for lymphocytes and mapped to chromosome 9p13. |journal=J. Biol. Chem. |volume=272 |issue= 31 |pages= 19518-24 |year= 1997 |pmid= 9235955 |doi=  }}
*{{cite journal  | author=Hedrick JA, Zlotnik A |title=Identification and characterization of a novel beta chemokine containing six conserved cysteines. |journal=J. Immunol. |volume=159 |issue= 4 |pages= 1589-93 |year= 1997 |pmid= 9257816 |doi=  }}
*{{cite journal  | author=Hromas R, Kim CH, Klemsz M, ''et al.'' |title=Isolation and characterization of Exodus-2, a novel C-C chemokine with a unique 37-amino acid carboxyl-terminal extension. |journal=J. Immunol. |volume=159 |issue= 6 |pages= 2554-8 |year= 1997 |pmid= 9300671 |doi=  }}
*{{cite journal  | author=Gunn MD, Tangemann K, Tam C, ''et al.'' |title=A chemokine expressed in lymphoid high endothelial venules promotes the adhesion and chemotaxis of naive T lymphocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 1 |pages= 258-63 |year= 1998 |pmid= 9419363 |doi=  }}
*{{cite journal  | author=Yoshida R, Nagira M, Kitaura M, ''et al.'' |title=Secondary lymphoid-tissue chemokine is a functional ligand for the CC chemokine receptor CCR7. |journal=J. Biol. Chem. |volume=273 |issue= 12 |pages= 7118-22 |year= 1998 |pmid= 9507024 |doi=  }}
*{{cite journal  | author=Campbell JJ, Bowman EP, Murphy K, ''et al.'' |title=6-C-kine (SLC), a lymphocyte adhesion-triggering chemokine expressed by high endothelium, is an agonist for the MIP-3beta receptor CCR7. |journal=J. Cell Biol. |volume=141 |issue= 4 |pages= 1053-9 |year= 1998 |pmid= 9585422 |doi=  }}
*{{cite journal  | author=Jenh CH, Cox MA, Kaminski H, ''et al.'' |title=Cutting edge: species specificity of the CC chemokine 6Ckine signaling through the CXC chemokine receptor CXCR3: human 6Ckine is not a ligand for the human or mouse CXCR3 receptors. |journal=J. Immunol. |volume=162 |issue= 7 |pages= 3765-9 |year= 1999 |pmid= 10201891 |doi=  }}
*{{cite journal  | author=Gosling J, Dairaghi DJ, Wang Y, ''et al.'' |title=Cutting edge: identification of a novel chemokine receptor that binds dendritic cell- and T cell-active chemokines including ELC, SLC, and TECK. |journal=J. Immunol. |volume=164 |issue= 6 |pages= 2851-6 |year= 2000 |pmid= 10706668 |doi=  }}
*{{cite journal  | author=Annunziato F, Romagnani P, Cosmi L, ''et al.'' |title=Macrophage-derived chemokine and EBI1-ligand chemokine attract human thymocytes in different stage of development and are produced by distinct subsets of medullary epithelial cells: possible implications for negative selection. |journal=J. Immunol. |volume=165 |issue= 1 |pages= 238-46 |year= 2000 |pmid= 10861057 |doi=  }}
*{{cite journal  | author=Hirose J, Kawashima H, Yoshie O, ''et al.'' |title=Versican interacts with chemokines and modulates cellular responses. |journal=J. Biol. Chem. |volume=276 |issue= 7 |pages= 5228-34 |year= 2001 |pmid= 11083865 |doi= 10.1074/jbc.M007542200 }}
*{{cite journal  | author=Till KJ, Lin K, Zuzel M, Cawley JC |title=The chemokine receptor CCR7 and alpha4 integrin are important for migration of chronic lymphocytic leukemia cells into lymph nodes. |journal=Blood |volume=99 |issue= 8 |pages= 2977-84 |year= 2002 |pmid= 11929789 |doi=  }}
*{{cite journal  | author=Grant AJ, Goddard S, Ahmed-Choudhury J, ''et al.'' |title=Hepatic expression of secondary lymphoid chemokine (CCL21) promotes the development of portal-associated lymphoid tissue in chronic inflammatory liver disease. |journal=Am. J. Pathol. |volume=160 |issue= 4 |pages= 1445-55 |year= 2002 |pmid= 11943728 |doi=  }}
*{{cite journal  | author=Banas B, Wörnle M, Berger T, ''et al.'' |title=Roles of SLC/CCL21 and CCR7 in human kidney for mesangial proliferation, migration, apoptosis, and tissue homeostasis. |journal=J. Immunol. |volume=168 |issue= 9 |pages= 4301-7 |year= 2002 |pmid= 11970971 |doi=  }}
*{{cite journal  | author=Christopherson KW, Hood AF, Travers JB, ''et al.'' |title=Endothelial induction of the T-cell chemokine CCL21 in T-cell autoimmune diseases. |journal=Blood |volume=101 |issue= 3 |pages= 801-6 |year= 2003 |pmid= 12393410 |doi= 10.1182/blood-2002-05-1586 }}
*{{cite journal  | author=Stein JV, Soriano SF, M'rini C, ''et al.'' |title=CCR7-mediated physiological lymphocyte homing involves activation of a tyrosine kinase pathway. |journal=Blood |volume=101 |issue= 1 |pages= 38-44 |year= 2003 |pmid= 12393730 |doi= 10.1182/blood-2002-03-0841 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Wolf M, Clark-Lewis I, Buri C, ''et al.'' |title=Cathepsin D specifically cleaves the chemokines macrophage inflammatory protein-1 alpha, macrophage inflammatory protein-1 beta, and SLC that are expressed in human breast cancer. |journal=Am. J. Pathol. |volume=162 |issue= 4 |pages= 1183-90 |year= 2003 |pmid= 12651610 |doi=  }}
*{{cite journal  | author=Weninger W, Carlsen HS, Goodarzi M, ''et al.'' |title=Naive T cell recruitment to nonlymphoid tissues: a role for endothelium-expressed CC chemokine ligand 21 in autoimmune disease and lymphoid neogenesis. |journal=J. Immunol. |volume=170 |issue= 9 |pages= 4638-48 |year= 2003 |pmid= 12707342 |doi=  }}
*{{cite journal  | author=Nagakubo D, Murai T, Tanaka T, ''et al.'' |title=A high endothelial venule secretory protein, mac25/angiomodulin, interacts with multiple high endothelial venule-associated molecules including chemokines. |journal=J. Immunol. |volume=171 |issue= 2 |pages= 553-61 |year= 2003 |pmid= 12847218 |doi=  }}
*{{cite journal  | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
}}
{{refend}}

{{protein-stub}}
 

CXCL9

• INFO: Beginning work on CXCL9... {November 18, 2007 10:12:06 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:12:37 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Chemokine (C-X-C motif) ligand 9
 | HGNCid = 7098
 | Symbol = CXCL9
 | AltSymbols =; CMK; Humig; MIG; SCYB9; crg-10
 | OMIM = 601704
 | ECnumber =  
 | Homologene = 1813
 | MGIid = 1352449
 | GeneAtlas_image1 = PBB_GE_CXCL9_203915_at_tn.png
 | Function = {{GNF_GO|id=GO:0008009 |text = chemokine activity}} 
 | Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} 
 | Process = {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0006968 |text = cellular defense response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4283
    | Hs_Ensembl = ENSG00000138755
    | Hs_RefseqProtein = NP_002407
    | Hs_RefseqmRNA = NM_002416
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 4
    | Hs_GenLoc_start = 77141523
    | Hs_GenLoc_end = 77147648
    | Hs_Uniprot = Q07325
    | Mm_EntrezGene = 17329
    | Mm_Ensembl = ENSMUSG00000029417
    | Mm_RefseqmRNA = NM_008599
    | Mm_RefseqProtein = NP_032625
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 93398190
    | Mm_GenLoc_end = 93403317
    | Mm_Uniprot =  
  }}
}}
'''Chemokine (C-X-C motif) ligand 9''', also known as '''CXCL9''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CXCL9 chemokine (C-X-C motif) ligand 9| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4283| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = The function of this gene has not been specifically defined; however, it is thought to be involved in T cell trafficking. This gene has been localized to 4q21 with INP10, which is also a member of the chemokine family of cytokines.<ref name="entrez">{{cite web | title = Entrez Gene: CXCL9 chemokine (C-X-C motif) ligand 9| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4283| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Farber JM |title=A macrophage mRNA selectively induced by gamma-interferon encodes a member of the platelet factor 4 family of cytokines. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 14 |pages= 5238-42 |year= 1990 |pmid= 2115167 |doi=  }}
*{{cite journal  | author=Liao F, Rabin RL, Yannelli JR, ''et al.'' |title=Human Mig chemokine: biochemical and functional characterization. |journal=J. Exp. Med. |volume=182 |issue= 5 |pages= 1301-14 |year= 1995 |pmid= 7595201 |doi=  }}
*{{cite journal  | author=Farber JM |title=HuMig: a new human member of the chemokine family of cytokines. |journal=Biochem. Biophys. Res. Commun. |volume=192 |issue= 1 |pages= 223-30 |year= 1993 |pmid= 8476424 |doi= 10.1006/bbrc.1993.1403 }}
*{{cite journal  | author=Lee HH, Farber JM |title=Localization of the gene for the human MIG cytokine on chromosome 4q21 adjacent to INP10 reveals a chemokine "mini-cluster". |journal=Cytogenet. Cell Genet. |volume=74 |issue= 4 |pages= 255-8 |year= 1997 |pmid= 8976378 |doi=  }}
*{{cite journal  | author=Weng Y, Siciliano SJ, Waldburger KE, ''et al.'' |title=Binding and functional properties of recombinant and endogenous CXCR3 chemokine receptors. |journal=J. Biol. Chem. |volume=273 |issue= 29 |pages= 18288-91 |year= 1998 |pmid= 9660793 |doi=  }}
*{{cite journal  | author=Erdel M, Laich A, Utermann G, ''et al.'' |title=The human gene encoding SCYB9B, a putative novel CXC chemokine, maps to human chromosome 4q21 like the closely related genes for MIG (SCYB9) and INP10 (SCYB10). |journal=Cytogenet. Cell Genet. |volume=81 |issue= 3-4 |pages= 271-2 |year= 1998 |pmid= 9730616 |doi=  }}
*{{cite journal  | author=Jenh CH, Cox MA, Kaminski H, ''et al.'' |title=Cutting edge: species specificity of the CC chemokine 6Ckine signaling through the CXC chemokine receptor CXCR3: human 6Ckine is not a ligand for the human or mouse CXCR3 receptors. |journal=J. Immunol. |volume=162 |issue= 7 |pages= 3765-9 |year= 1999 |pmid= 10201891 |doi=  }}
*{{cite journal  | author=Rabin RL, Park MK, Liao F, ''et al.'' |title=Chemokine receptor responses on T cells are achieved through regulation of both receptor expression and signaling. |journal=J. Immunol. |volume=162 |issue= 7 |pages= 3840-50 |year= 1999 |pmid= 10201901 |doi=  }}
*{{cite journal  | author=Tensen CP, Flier J, Van Der Raaij-Helmer EM, ''et al.'' |title=Human IP-9: A keratinocyte-derived high affinity CXC-chemokine ligand for the IP-10/Mig receptor (CXCR3). |journal=J. Invest. Dermatol. |volume=112 |issue= 5 |pages= 716-22 |year= 1999 |pmid= 10233762 |doi= 10.1046/j.1523-1747.1999.00581.x }}
*{{cite journal  | author=Shields PL, Morland CM, Salmon M, ''et al.'' |title=Chemokine and chemokine receptor interactions provide a mechanism for selective T cell recruitment to specific liver compartments within hepatitis C-infected liver. |journal=J. Immunol. |volume=163 |issue= 11 |pages= 6236-43 |year= 1999 |pmid= 10570316 |doi=  }}
*{{cite journal  | author=Jinquan T, Jing C, Jacobi HH, ''et al.'' |title=CXCR3 expression and activation of eosinophils: role of IFN-gamma-inducible protein-10 and monokine induced by IFN-gamma. |journal=J. Immunol. |volume=165 |issue= 3 |pages= 1548-56 |year= 2000 |pmid= 10903763 |doi=  }}
*{{cite journal  | author=Loetscher P, Pellegrino A, Gong JH, ''et al.'' |title=The ligands of CXC chemokine receptor 3, I-TAC, Mig, and IP10, are natural antagonists for CCR3. |journal=J. Biol. Chem. |volume=276 |issue= 5 |pages= 2986-91 |year= 2001 |pmid= 11110785 |doi= 10.1074/jbc.M005652200 }}
*{{cite journal  | author=Romagnani P, Annunziato F, Lazzeri E, ''et al.'' |title=Interferon-inducible protein 10, monokine induced by interferon gamma, and interferon-inducible T-cell alpha chemoattractant are produced by thymic epithelial cells and attract T-cell receptor (TCR) alphabeta+ CD8+ single-positive T cells, TCRgammadelta+ T cells, and natural killer-type cells in human thymus. |journal=Blood |volume=97 |issue= 3 |pages= 601-7 |year= 2001 |pmid= 11157474 |doi=  }}
*{{cite journal  | author=Dwinell MB, Lügering N, Eckmann L, Kagnoff MF |title=Regulated production of interferon-inducible T-cell chemoattractants by human intestinal epithelial cells. |journal=Gastroenterology |volume=120 |issue= 1 |pages= 49-59 |year= 2001 |pmid= 11208713 |doi=  }}
*{{cite journal  | author=Lambeir AM, Proost P, Durinx C, ''et al.'' |title=Kinetic investigation of chemokine truncation by CD26/dipeptidyl peptidase IV reveals a striking selectivity within the chemokine family. |journal=J. Biol. Chem. |volume=276 |issue= 32 |pages= 29839-45 |year= 2001 |pmid= 11390394 |doi= 10.1074/jbc.M103106200 }}
*{{cite journal  | author=Stoof TJ, Flier J, Sampat S, ''et al.'' |title=The antipsoriatic drug dimethylfumarate strongly suppresses chemokine production in human keratinocytes and peripheral blood mononuclear cells. |journal=Br. J. Dermatol. |volume=144 |issue= 6 |pages= 1114-20 |year= 2001 |pmid= 11422029 |doi=  }}
*{{cite journal  | author=Campbell JD, Stinson MJ, Simons FE, ''et al.'' |title=In vivo stability of human chemokine and chemokine receptor expression. |journal=Hum. Immunol. |volume=62 |issue= 7 |pages= 668-78 |year= 2001 |pmid= 11423172 |doi=  }}
*{{cite journal  | author=Scapini P, Laudanna C, Pinardi C, ''et al.'' |title=Neutrophils produce biologically active macrophage inflammatory protein-3alpha (MIP-3alpha)/CCL20 and MIP-3beta/CCL19. |journal=Eur. J. Immunol. |volume=31 |issue= 7 |pages= 1981-8 |year= 2001 |pmid= 11449350 |doi=  }}
*{{cite journal  | author=Gillitzer R |title=Inflammation in human skin: a model to study chemokine-mediated leukocyte migration in vivo. |journal=J. Pathol. |volume=194 |issue= 4 |pages= 393-4 |year= 2001 |pmid= 11523044 |doi= 10.1002/1096-9896(200108)194:4<393::AID-PATH907>3.0.CO;2-7 }}
*{{cite journal  | author=Romagnani P, Rotondi M, Lazzeri E, ''et al.'' |title=Expression of IP-10/CXCL10 and MIG/CXCL9 in the thyroid and increased levels of IP-10/CXCL10 in the serum of patients with recent-onset Graves' disease. |journal=Am. J. Pathol. |volume=161 |issue= 1 |pages= 195-206 |year= 2002 |pmid= 12107104 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

HNRPU

• INFO: Beginning work on HNRPU... {November 17, 2007 11:47:55 PM PST}
• SEARCH REDIRECT: Control Box Found: HNRPU {November 17, 2007 11:50:54 PM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 11:51:01 PM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 11:51:01 PM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 11:51:01 PM PST}
• UPDATED: Updated protein page: HNRPU {November 17, 2007 11:51:16 PM PST}

KRT10

• INFO: Beginning work on KRT10... {November 17, 2007 11:51:16 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:10:14 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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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 = Keratin 10 (epidermolytic hyperkeratosis; keratosis palmaris et plantaris)
 | HGNCid = 6413
 | Symbol = KRT10
 | AltSymbols =; CK10; K10; KPP
 | OMIM = 148080
 | ECnumber =  
 | Homologene = 20125
 | MGIid = 96685
 | GeneAtlas_image1 = PBB_GE_KRT10_213287_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_KRT10_207023_x_at_tn.png
 | GeneAtlas_image3 = PBB_GE_KRT10_210633_x_at_tn.png
 | Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0030280 |text = structural constituent of epidermis}} 
 | Component = {{GNF_GO|id=GO:0045095 |text = keratin filament}} 
 | Process = {{GNF_GO|id=GO:0008544 |text = epidermis development}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3858
    | Hs_Ensembl = ENSG00000186395
    | Hs_RefseqProtein = NP_000412
    | Hs_RefseqmRNA = NM_000421
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 36227896
    | Hs_GenLoc_end = 36232373
    | Hs_Uniprot = P13645
    | Mm_EntrezGene = 16661
    | Mm_Ensembl = ENSMUSG00000019761
    | Mm_RefseqmRNA = NM_010660
    | Mm_RefseqProtein = NP_034790
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 99201344
    | Mm_GenLoc_end = 99205454
    | Mm_Uniprot = P02535
  }}
}}
'''Keratin 10 (epidermolytic hyperkeratosis; keratosis palmaris et plantaris)''', also known as '''KRT10''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KRT10 keratin 10 (epidermolytic hyperkeratosis; keratosis palmaris et plantaris)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3858| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = This gene encodes a member of the type I (acidic) cytokeratin family, which belongs to the superfamily of intermediate filament (IF) proteins. Keratins are heteropolymeric structural proteins which form the intermediate filament. These filaments, along with actin microfilaments and microtubules, compose the cytoskeleton of epithelial cells. Mutations in this gene are associated with epidermolytic hyperkeratosis. This gene is located within a cluster of keratin family members on chromosome 17q21.<ref name="entrez">{{cite web | title = Entrez Gene: KRT10 keratin 10 (epidermolytic hyperkeratosis; keratosis palmaris et plantaris)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3858| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Yang JM, Nam K, Kim SW, ''et al.'' |title=Arginine in the beginning of the 1A rod domain of the keratin 10 gene is the hot spot for the mutation in epidermolytic hyperkeratosis. |journal=J. Dermatol. Sci. |volume=19 |issue= 2 |pages= 126-33 |year= 1999 |pmid= 10098704 |doi=  }}
*{{cite journal  | author=Rasmussen HH, van Damme J, Puype M, ''et al.'' |title=Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 960-9 |year= 1993 |pmid= 1286667 |doi=  }}
*{{cite journal  | author=Korge BP, Gan SQ, McBride OW, ''et al.'' |title=Extensive size polymorphism of the human keratin 10 chain resides in the C-terminal V2 subdomain due to variable numbers and sizes of glycine loops. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 3 |pages= 910-4 |year= 1992 |pmid= 1371013 |doi=  }}
*{{cite journal  | author=Tkachenko AV, Buchman VL, Bliskovsky VV, ''et al.'' |title=Exons I and VII of the gene (Ker10) encoding human keratin 10 undergo structural rearrangements within repeats. |journal=Gene |volume=116 |issue= 2 |pages= 245-51 |year= 1992 |pmid= 1378806 |doi=  }}
*{{cite journal  | author=Rothnagel JA, Dominey AM, Dempsey LD, ''et al.'' |title=Mutations in the rod domains of keratins 1 and 10 in epidermolytic hyperkeratosis. |journal=Science |volume=257 |issue= 5073 |pages= 1128-30 |year= 1992 |pmid= 1380725 |doi=  }}
*{{cite journal  | author=Cheng J, Syder AJ, Yu QC, ''et al.'' |title=The genetic basis of epidermolytic hyperkeratosis: a disorder of differentiation-specific epidermal keratin genes. |journal=Cell |volume=70 |issue= 5 |pages= 811-9 |year= 1992 |pmid= 1381287 |doi=  }}
*{{cite journal  | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi=  }}
*{{cite journal  | author=Nazzaro V, Ermacora E, Santucci B, Caputo R |title=Epidermolytic hyperkeratosis: generalized form in children from parents with systematized linear form. |journal=Br. J. Dermatol. |volume=122 |issue= 3 |pages= 417-22 |year= 1990 |pmid= 2182100 |doi=  }}
*{{cite journal  | author=Darmon MY, Sémat A, Darmon MC, Vasseur M |title=Sequence of a cDNA encoding human keratin No 10 selected according to structural homologies of keratins and their tissue-specific expression. |journal=Mol. Biol. Rep. |volume=12 |issue= 4 |pages= 277-83 |year= 1988 |pmid= 2448602 |doi=  }}
*{{cite journal  | author=Zhou XM, Idler WW, Steven AC, ''et al.'' |title=The complete sequence of the human intermediate filament chain keratin 10. Subdomainal divisions and model for folding of end domain sequences. |journal=J. Biol. Chem. |volume=263 |issue= 30 |pages= 15584-9 |year= 1988 |pmid= 2459124 |doi=  }}
*{{cite journal  | author=Lessin SR, Huebner K, Isobe M, ''et al.'' |title=Chromosomal mapping of human keratin genes: evidence of non-linkage. |journal=J. Invest. Dermatol. |volume=91 |issue= 6 |pages= 572-8 |year= 1989 |pmid= 2461420 |doi=  }}
*{{cite journal  | author=Rieger M, Franke WW |title=Identification of an orthologous mammalian cytokeratin gene. High degree of intron sequence conservation during evolution of human cytokeratin 10. |journal=J. Mol. Biol. |volume=204 |issue= 4 |pages= 841-56 |year= 1989 |pmid= 2464696 |doi=  }}
*{{cite journal  | author=van Dongen GA, Braakhuis BJ, Leyva A, ''et al.'' |title=Anti-tumor and differentiation-inducing activity of N,N-dimethylformamide (DMF) in head-and-neck cancer xenografts. |journal=Int. J. Cancer |volume=43 |issue= 2 |pages= 285-92 |year= 1989 |pmid= 2465278 |doi=  }}
*{{cite journal  | author=Rogaev EI, Rogaeva EA, Ginter EK, ''et al.'' |title=Identification of the genetic locus for keratosis palmaris et plantaris on chromosome 17 near the RARA and keratin type I genes. |journal=Nat. Genet. |volume=5 |issue= 2 |pages= 158-62 |year= 1994 |pmid= 7504553 |doi= 10.1038/ng1093-158 }}
*{{cite journal  | author=Rothnagel JA, Longley MA, Holder RA, ''et al.'' |title=Prenatal diagnosis of epidermolytic hyperkeratosis by direct gene sequencing. |journal=J. Invest. Dermatol. |volume=102 |issue= 1 |pages= 13-6 |year= 1994 |pmid= 7507150 |doi=  }}
*{{cite journal  | author=McLean WH, Eady RA, Dopping-Hepenstal PJ, ''et al.'' |title=Mutations in the rod 1A domain of keratins 1 and 10 in bullous congenital ichthyosiform erythroderma (BCIE). |journal=J. Invest. Dermatol. |volume=102 |issue= 1 |pages= 24-30 |year= 1994 |pmid= 7507152 |doi=  }}
*{{cite journal  | author=Chipev CC, Yang JM, DiGiovanna JJ, ''et al.'' |title=Preferential sites in keratin 10 that are mutated in epidermolytic hyperkeratosis. |journal=Am. J. Hum. Genet. |volume=54 |issue= 2 |pages= 179-90 |year= 1994 |pmid= 7508181 |doi=  }}
*{{cite journal  | author=Rothnagel JA, Fisher MP, Axtell SM, ''et al.'' |title=A mutational hot spot in keratin 10 (KRT 10) in patients with epidermolytic hyperkeratosis. |journal=Hum. Mol. Genet. |volume=2 |issue= 12 |pages= 2147-50 |year= 1994 |pmid= 7509230 |doi=  }}
*{{cite journal  | author=Syder AJ, Yu QC, Paller AS, ''et al.'' |title=Genetic mutations in the K1 and K10 genes of patients with epidermolytic hyperkeratosis. Correlation between location and disease severity. |journal=J. Clin. Invest. |volume=93 |issue= 4 |pages= 1533-42 |year= 1994 |pmid= 7512983 |doi=  }}
*{{cite journal  | author=Huber M, Scaletta C, Benathan M, ''et al.'' |title=Abnormal keratin 1 and 10 cytoskeleton in cultured keratinocytes from epidermolytic hyperkeratosis caused by keratin 10 mutations. |journal=J. Invest. Dermatol. |volume=102 |issue= 5 |pages= 691-4 |year= 1994 |pmid= 7513736 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

LMNB1

• INFO: Beginning work on LMNB1... {November 18, 2007 10:10:55 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:11:26 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Lamin B1
 | HGNCid = 6637
 | Symbol = LMNB1
 | AltSymbols =; LMN; LMN2; LMNB; MGC111419
 | OMIM = 150340
 | ECnumber =  
 | Homologene = 55912
 | MGIid = 96795
 | GeneAtlas_image1 = PBB_GE_LMNB1_203276_at_tn.png
 | Function = {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} 
 | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005638 |text = lamin filament}} 
 | Process = 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4001
    | Hs_Ensembl = ENSG00000113368
    | Hs_RefseqProtein = NP_005564
    | Hs_RefseqmRNA = NM_005573
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 126140214
    | Hs_GenLoc_end = 126200582
    | Hs_Uniprot = P20700
    | Mm_EntrezGene = 16906
    | Mm_Ensembl = ENSMUSG00000024590
    | Mm_RefseqmRNA = XM_993305
    | Mm_RefseqProtein = XP_998399
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 18
    | Mm_GenLoc_start = 56833233
    | Mm_GenLoc_end = 56878791
    | Mm_Uniprot = Q8C553
  }}
}}
'''Lamin B1''', also known as '''LMNB1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LMNB1 lamin B1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4001| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = The nuclear lamina consists of a two-dimensional matrix of proteins located next to the inner nuclear membrane. The lamin family of proteins make up the matrix and are highly conserved in evolution. During mitosis, the lamina matrix is reversibly disassembled as the lamin proteins are phosphorylated. Lamin proteins are thought to be involved in nuclear stability, chromatin structure and gene expression. Vertebrate lamins consist of two types, A and B. This gene encodes one of the two B type proteins, B1.<ref name="entrez">{{cite web | title = Entrez Gene: LMNB1 lamin B1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4001| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Gruenbaum Y, Wilson KL, Harel A, ''et al.'' |title=Review: nuclear lamins--structural proteins with fundamental functions. |journal=J. Struct. Biol. |volume=129 |issue= 2-3 |pages= 313-23 |year= 2000 |pmid= 10806082 |doi= 10.1006/jsbi.2000.4216 }}
*{{cite journal  | author=Worman HJ, Courvalin JC |title=The inner nuclear membrane. |journal=J. Membr. Biol. |volume=177 |issue= 1 |pages= 1-11 |year= 2000 |pmid= 10960149 |doi=  }}
*{{cite journal  | author=Djabali K, Portier MM, Gros F, ''et al.'' |title=Network antibodies identify nuclear lamin B as a physiological attachment site for peripherin intermediate filaments. |journal=Cell |volume=64 |issue= 1 |pages= 109-21 |year= 1991 |pmid= 1986862 |doi=  }}
*{{cite journal  | author=Foisner R, Traub P, Wiche G |title=Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 9 |pages= 3812-6 |year= 1991 |pmid= 2023931 |doi=  }}
*{{cite journal  | author=Pollard KM, Chan EK, Grant BJ, ''et al.'' |title=In vitro posttranslational modification of lamin B cloned from a human T-cell line. |journal=Mol. Cell. Biol. |volume=10 |issue= 5 |pages= 2164-75 |year= 1990 |pmid= 2325650 |doi=  }}
*{{cite journal  | author=Müller WE, Okamoto T, Reuter P, ''et al.'' |title=Functional characterization of Tat protein from human immunodeficiency virus. Evidence that Tat links viral RNAs to nuclear matrix. |journal=J. Biol. Chem. |volume=265 |issue= 7 |pages= 3803-8 |year= 1990 |pmid= 2406262 |doi=  }}
*{{cite journal  | author=Müller WE, Wenger R, Reuter P, ''et al.'' |title=Association of Tat protein and viral mRNA with nuclear matrix from HIV-1-infected H9 cells. |journal=Biochim. Biophys. Acta |volume=1008 |issue= 2 |pages= 208-12 |year= 1989 |pmid= 2544227 |doi=  }}
*{{cite journal  | author=Eldridge R, Anayiotos CP, Schlesinger S, ''et al.'' |title=Hereditary adult-onset leukodystrophy simulating chronic progressive multiple sclerosis. |journal=N. Engl. J. Med. |volume=311 |issue= 15 |pages= 948-53 |year= 1984 |pmid= 6472420 |doi=  }}
*{{cite journal  | author=Lin F, Worman HJ |title=Structural organization of the human gene (LMNB1) encoding nuclear lamin B1. |journal=Genomics |volume=27 |issue= 2 |pages= 230-6 |year= 1995 |pmid= 7557986 |doi= 10.1006/geno.1995.1036 }}
*{{cite journal  | author=Ye Q, Worman HJ |title=Protein-protein interactions between human nuclear lamins expressed in yeast. |journal=Exp. Cell Res. |volume=219 |issue= 1 |pages= 292-8 |year= 1995 |pmid= 7628545 |doi= 10.1006/excr.1995.1230 }}
*{{cite journal  | author=Goss VL, Hocevar BA, Thompson LJ, ''et al.'' |title=Identification of nuclear beta II protein kinase C as a mitotic lamin kinase. |journal=J. Biol. Chem. |volume=269 |issue= 29 |pages= 19074-80 |year= 1994 |pmid= 8034666 |doi=  }}
*{{cite journal  | author=Wydner KL, McNeil JA, Lin F, ''et al.'' |title=Chromosomal assignment of human nuclear envelope protein genes LMNA, LMNB1, and LBR by fluorescence in situ hybridization. |journal=Genomics |volume=32 |issue= 3 |pages= 474-8 |year= 1997 |pmid= 8838815 |doi= 10.1006/geno.1996.0146 }}
*{{cite journal  | author=Broers JL, Machiels BM, Kuijpers HJ, ''et al.'' |title=A- and B-type lamins are differentially expressed in normal human tissues. |journal=Histochem. Cell Biol. |volume=107 |issue= 6 |pages= 505-17 |year= 1997 |pmid= 9243284 |doi=  }}
*{{cite journal  | author=Maison C, Pyrpasopoulou A, Theodoropoulos PA, Georgatos SD |title=The inner nuclear membrane protein LAP1 forms a native complex with B-type lamins and partitions with spindle-associated mitotic vesicles. |journal=EMBO J. |volume=16 |issue= 16 |pages= 4839-50 |year= 1997 |pmid= 9305626 |doi= 10.1093/emboj/16.16.4839 }}
*{{cite journal  | author=Lin F, Worman HJ |title=Expression of nuclear lamins in human tissues and cancer cell lines and transcription from the promoters of the lamin A/C and B1 genes. |journal=Exp. Cell Res. |volume=236 |issue= 2 |pages= 378-84 |year= 1997 |pmid= 9367621 |doi= 10.1006/excr.1997.3735 }}
*{{cite journal  | author=Vodicka MA, Koepp DM, Silver PA, Emerman M |title=HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infection. |journal=Genes Dev. |volume=12 |issue= 2 |pages= 175-85 |year= 1998 |pmid= 9436978 |doi=  }}
*{{cite journal  | author=Furukawa K, Kondo T |title=Identification of the lamina-associated-polypeptide-2-binding domain of B-type lamin. |journal=Eur. J. Biochem. |volume=251 |issue= 3 |pages= 729-33 |year= 1998 |pmid= 9490046 |doi=  }}
*{{cite journal  | author=Kowluru A |title=Evidence for the carboxyl methylation of nuclear lamin-B in the pancreatic beta cell. |journal=Biochem. Biophys. Res. Commun. |volume=268 |issue= 2 |pages= 249-54 |year= 2000 |pmid= 10679189 |doi= 10.1006/bbrc.2000.2107 }}
}}
{{refend}}

{{protein-stub}}
 

LRPAP1

• INFO: Beginning work on LRPAP1... {November 18, 2007 10:11:26 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:12:06 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_LRPAP1_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1lre.
 | PDB = {{PDB2|1lre}}, {{PDB2|1nre}}, {{PDB2|1op1}}, {{PDB2|1ov2}}, {{PDB2|2fcw}}, {{PDB2|2ftu}}, {{PDB2|2fyl}}
 | Name = Low density lipoprotein receptor-related protein associated protein 1
 | HGNCid = 6701
 | Symbol = LRPAP1
 | AltSymbols =; A2MRAP; A2RAP; HBP44; MGC138272; MRAP; RAP
 | OMIM = 104225
 | ECnumber =  
 | Homologene = 37612
 | MGIid = 96829
 | GeneAtlas_image1 = PBB_GE_LRPAP1_201186_at_tn.png
 | Function = {{GNF_GO|id=GO:0004873 |text = asialoglycoprotein receptor activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0008034 |text = lipoprotein binding}} {{GNF_GO|id=GO:0008201 |text = heparin binding}} {{GNF_GO|id=GO:0050750 |text = low-density lipoprotein receptor binding}} {{GNF_GO|id=GO:0051082 |text = unfolded protein binding}} 
 | Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} 
 | Process = {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0016192 |text = vesicle-mediated transport}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4043
    | Hs_Ensembl = ENSG00000163956
    | Hs_RefseqProtein = NP_002328
    | Hs_RefseqmRNA = NM_002337
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 4
    | Hs_GenLoc_start = 3484088
    | Hs_GenLoc_end = 3503947
    | Hs_Uniprot = P30533
    | Mm_EntrezGene = 16976
    | Mm_Ensembl = ENSMUSG00000029103
    | Mm_RefseqmRNA = NM_013587
    | Mm_RefseqProtein = NP_038615
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 35408367
    | Mm_GenLoc_end = 35422558
    | Mm_Uniprot = Q3TL96
  }}
}}
'''Low density lipoprotein receptor-related protein associated protein 1''', also known as '''LRPAP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LRPAP1 low density lipoprotein receptor-related protein associated protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4043| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = 
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Williams SE, Ashcom JD, Argraves WS, Strickland DK |title=A novel mechanism for controlling the activity of alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein. Multiple regulatory sites for 39-kDa receptor-associated protein. |journal=J. Biol. Chem. |volume=267 |issue= 13 |pages= 9035-40 |year= 1992 |pmid= 1374383 |doi=  }}
*{{cite journal  | author=Kounnas MZ, Argraves WS, Strickland DK |title=The 39-kDa receptor-associated protein interacts with two members of the low density lipoprotein receptor family, alpha 2-macroglobulin receptor and glycoprotein 330. |journal=J. Biol. Chem. |volume=267 |issue= 29 |pages= 21162-6 |year= 1992 |pmid= 1400426 |doi=  }}
*{{cite journal  | author=Striekland DK, Ashcom JD, Williams S, ''et al.'' |title=Primary structure of alpha 2-macroglobulin receptor-associated protein. Human homologue of a Heymann nephritis antigen. |journal=J. Biol. Chem. |volume=266 |issue= 20 |pages= 13364-9 |year= 1991 |pmid= 1712782 |doi=  }}
*{{cite journal  | author=Herz J, Goldstein JL, Strickland DK, ''et al.'' |title=39-kDa protein modulates binding of ligands to low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor. |journal=J. Biol. Chem. |volume=266 |issue= 31 |pages= 21232-8 |year= 1991 |pmid= 1718973 |doi=  }}
*{{cite journal  | author=Furukawa T, Ozawa M, Huang RP, Muramatsu T |title=A heparin binding protein whose expression increases during differentiation of embryonal carcinoma cells to parietal endoderm cells: cDNA cloning and sequence analysis. |journal=J. Biochem. |volume=108 |issue= 2 |pages= 297-302 |year= 1990 |pmid= 2229028 |doi=  }}
*{{cite journal  | author=Herz J, Hamann U, Rogne S, ''et al.'' |title=Surface location and high affinity for calcium of a 500-kd liver membrane protein closely related to the LDL-receptor suggest a physiological role as lipoprotein receptor. |journal=EMBO J. |volume=7 |issue= 13 |pages= 4119-27 |year= 1989 |pmid= 3266596 |doi=  }}
*{{cite journal  | author=Zheng G, Bachinsky DR, Stamenkovic I, ''et al.'' |title=Organ distribution in rats of two members of the low-density lipoprotein receptor gene family, gp330 and LRP/alpha 2MR, and the receptor-associated protein (RAP). |journal=J. Histochem. Cytochem. |volume=42 |issue= 4 |pages= 531-42 |year= 1994 |pmid= 7510321 |doi=  }}
*{{cite journal  | author=Orlando RA, Farquhar MG |title=Functional domains of the receptor-associated protein (RAP). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 8 |pages= 3161-5 |year= 1994 |pmid= 7512726 |doi=  }}
*{{cite journal  | author=Jou YS, Goold RD, Myers RM |title=Localization of the alpha 2-macroglobulin receptor-associated protein 1 gene (LRPAP1) and other gene fragments to human chromosome 4p16.3 by direct cDNA selection. |journal=Genomics |volume=24 |issue= 2 |pages= 410-3 |year= 1995 |pmid= 7535288 |doi= 10.1006/geno.1994.1643 }}
*{{cite journal  | author=Argraves KM, Battey FD, MacCalman CD, ''et al.'' |title=The very low density lipoprotein receptor mediates the cellular catabolism of lipoprotein lipase and urokinase-plasminogen activator inhibitor type I complexes. |journal=J. Biol. Chem. |volume=270 |issue= 44 |pages= 26550-7 |year= 1995 |pmid= 7592875 |doi=  }}
*{{cite journal  | author=Bu G, Geuze HJ, Strous GJ, Schwartz AL |title=39 kDa receptor-associated protein is an ER resident protein and molecular chaperone for LDL receptor-related protein. |journal=EMBO J. |volume=14 |issue= 10 |pages= 2269-80 |year= 1995 |pmid= 7774585 |doi=  }}
*{{cite journal  | author=Van Leuven F, Hilliker C, Serneels L, ''et al.'' |title=Cloning, characterization, and chromosomal localization to 4p16 of the human gene (LRPAP1) coding for the alpha 2-macroglobulin receptor-associated protein and structural comparison with the murine gene coding for the 44-kDa heparin-binding protein. |journal=Genomics |volume=25 |issue= 2 |pages= 492-500 |year= 1995 |pmid= 7789983 |doi=  }}
*{{cite journal  | author=Medh JD, Fry GL, Bowen SL, ''et al.'' |title=The 39-kDa receptor-associated protein modulates lipoprotein catabolism by binding to LDL receptors. |journal=J. Biol. Chem. |volume=270 |issue= 2 |pages= 536-40 |year= 1995 |pmid= 7822276 |doi=  }}
*{{cite journal  | author=Korenberg JR, Argraves KM, Chen XN, ''et al.'' |title=Chromosomal localization of human genes for the LDL receptor family member glycoprotein 330 (LRP2) and its associated protein RAP (LRPAP1). |journal=Genomics |volume=22 |issue= 1 |pages= 88-93 |year= 1994 |pmid= 7959795 |doi= 10.1006/geno.1994.1348 }}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal  | author=Willnow TE, Rohlmann A, Horton J, ''et al.'' |title=RAP, a specialized chaperone, prevents ligand-induced ER retention and degradation of LDL receptor-related endocytic receptors. |journal=EMBO J. |volume=15 |issue= 11 |pages= 2632-9 |year= 1996 |pmid= 8654360 |doi=  }}
*{{cite journal  | author=Jacobsen L, Madsen P, Moestrup SK, ''et al.'' |title=Molecular characterization of a novel human hybrid-type receptor that binds the alpha2-macroglobulin receptor-associated protein. |journal=J. Biol. Chem. |volume=271 |issue= 49 |pages= 31379-83 |year= 1997 |pmid= 8940146 |doi=  }}
*{{cite journal  | author=Bu G, Rennke S, Geuze HJ |title=ERD2 proteins mediate ER retention of the HNEL signal of LRP's receptor-associated protein (RAP). |journal=J. Cell. Sci. |volume=110 ( Pt 1) |issue=  |pages= 65-73 |year= 1997 |pmid= 9010785 |doi=  }}
*{{cite journal  | author=Petersen CM, Nielsen MS, Nykjaer A, ''et al.'' |title=Molecular identification of a novel candidate sorting receptor purified from human brain by receptor-associated protein affinity chromatography. |journal=J. Biol. Chem. |volume=272 |issue= 6 |pages= 3599-605 |year= 1997 |pmid= 9013611 |doi=  }}
*{{cite journal  | author=Nielsen PR, Ellgaard L, Etzerodt M, ''et al.'' |title=The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 14 |pages= 7521-5 |year= 1997 |pmid= 9207124 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

NDP

• INFO: Beginning work on NDP... {November 18, 2007 10:12:37 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:13:05 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Norrie disease (pseudoglioma)
 | HGNCid = 7678
 | Symbol = NDP
 | AltSymbols =; EVR2; FEVR; ND
 | OMIM = 310600
 | ECnumber =  
 | Homologene = 225
 | MGIid = 102570
 | GeneAtlas_image1 = PBB_GE_NDP_206022_at_tn.png
 | Function = {{GNF_GO|id=GO:0008083 |text = growth factor activity}} 
 | Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} 
 | Process = {{GNF_GO|id=GO:0001890 |text = placenta development}} {{GNF_GO|id=GO:0007033 |text = vacuole organization and biogenesis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0007601 |text = visual perception}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4693
    | Hs_Ensembl = ENSG00000124479
    | Hs_RefseqProtein = NP_000257
    | Hs_RefseqmRNA = NM_000266
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = X
    | Hs_GenLoc_start = 43692966
    | Hs_GenLoc_end = 43717694
    | Hs_Uniprot = Q00604
    | Mm_EntrezGene = 17986
    | Mm_Ensembl = ENSMUSG00000040138
    | Mm_RefseqmRNA = NM_010883
    | Mm_RefseqProtein = NP_035013
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = X
    | Mm_GenLoc_start = 16042480
    | Mm_GenLoc_end = 16068723
    | Mm_Uniprot = Q5CZY6
  }}
}}
'''Norrie disease (pseudoglioma)''', also known as '''NDP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NDP Norrie disease (pseudoglioma)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4693| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = NDP is the genetic locus identified as harboring mutations that result in Norrie disease. Norrie disease is a rare genetic disorder characterized by bilateral congenital blindness that is caused by a vascularized mass behind each lens due to a maldeveloped retina (pseudoglioma).<ref name="entrez">{{cite web | title = Entrez Gene: NDP Norrie disease (pseudoglioma)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4693| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Berger W, van de Pol D, Warburg M, ''et al.'' |title=Mutations in the candidate gene for Norrie disease. |journal=Hum. Mol. Genet. |volume=1 |issue= 7 |pages= 461-5 |year= 1993 |pmid= 1307245 |doi=  }}
*{{cite journal  | author=Black G, Redmond RM |title=The molecular biology of Norrie's disease. |journal=Eye (London, England) |volume=8 ( Pt 5) |issue=  |pages= 491-6 |year= 1995 |pmid= 7835440 |doi=  }}
*{{cite journal  | author=Masckauchán TN, Kitajewski J |title=Wnt/Frizzled signaling in the vasculature: new angiogenic factors in sight. |journal=Physiology (Bethesda, Md.) |volume=21 |issue=  |pages= 181-8 |year= 2007 |pmid= 16714476 |doi= 10.1152/physiol.00058.2005 }}
*{{cite journal  | author=Berger W, Meindl A, van de Pol TJ, ''et al.'' |title=Isolation of a candidate gene for Norrie disease by positional cloning. |journal=Nat. Genet. |volume=1 |issue= 3 |pages= 199-203 |year= 1993 |pmid= 1303235 |doi= 10.1038/ng0692-199 }}
*{{cite journal  | author=Chen ZY, Hendriks RW, Jobling MA, ''et al.'' |title=Isolation and characterization of a candidate gene for Norrie disease. |journal=Nat. Genet. |volume=1 |issue= 3 |pages= 204-8 |year= 1993 |pmid= 1303236 |doi= 10.1038/ng0692-204 }}
*{{cite journal  | author=Berger W, Meindl A, van de Pol TJ, ''et al.'' |title=Isolation of a candidate gene for Norrie disease by positional cloning. |journal=Nat. Genet. |volume=2 |issue= 1 |pages= 84 |year= 1993 |pmid= 1303256 |doi= 10.1038/ng0992-84 }}
*{{cite journal  | author=Meindl A, Berger W, Meitinger T, ''et al.'' |title=Norrie disease is caused by mutations in an extracellular protein resembling C-terminal globular domain of mucins. |journal=Nat. Genet. |volume=2 |issue= 2 |pages= 139-43 |year= 1993 |pmid= 1303264 |doi= 10.1038/ng1092-139 }}
*{{cite journal  | author=Shastry BS, Hejtmancik JF, Plager DA, ''et al.'' |title=Linkage and candidate gene analysis of X-linked familial exudative vitreoretinopathy. |journal=Genomics |volume=27 |issue= 2 |pages= 341-4 |year= 1995 |pmid= 7558002 |doi= 10.1006/geno.1995.1052 }}
*{{cite journal  | author=Schuback DE, Chen ZY, Craig IW, ''et al.'' |title=Mutations in the Norrie disease gene. |journal=Hum. Mutat. |volume=5 |issue= 4 |pages= 285-92 |year= 1995 |pmid= 7627181 |doi= 10.1002/humu.1380050403 }}
*{{cite journal  | author=Meindl A, Lorenz B, Achatz H, ''et al.'' |title=Missense mutations in the NDP gene in patients with a less severe course of Norrie disease. |journal=Hum. Mol. Genet. |volume=4 |issue= 3 |pages= 489-90 |year= 1995 |pmid= 7795608 |doi=  }}
*{{cite journal  | author=Joos KM, Kimura AE, Vandenburgh K, ''et al.'' |title=Ocular findings associated with a Cys39Arg mutation in the Norrie disease gene. |journal=Arch. Ophthalmol. |volume=112 |issue= 12 |pages= 1574-9 |year= 1995 |pmid= 7993212 |doi=  }}
*{{cite journal  | author=Fuchs S, Xu SY, Caballero M, ''et al.'' |title=A missense point mutation (Leu13Arg) of the Norrie disease gene in a large Cuban kindred with Norrie disease. |journal=Hum. Mol. Genet. |volume=3 |issue= 4 |pages= 655-6 |year= 1994 |pmid= 8069314 |doi=  }}
*{{cite journal  | author=Wong F, Goldberg MF, Hao Y |title=Identification of a nonsense mutation at codon 128 of the Norrie's disease gene in a male infant. |journal=Arch. Ophthalmol. |volume=111 |issue= 11 |pages= 1553-7 |year= 1993 |pmid= 8240113 |doi=  }}
*{{cite journal  | author=Chen ZY, Battinelli EM, Fielder A, ''et al.'' |title=A mutation in the Norrie disease gene (NDP) associated with X-linked familial exudative vitreoretinopathy. |journal=Nat. Genet. |volume=5 |issue= 2 |pages= 180-3 |year= 1994 |pmid= 8252044 |doi= 10.1038/ng1093-180 }}
*{{cite journal  | author=Chen ZY, Battinelli EM, Woodruff G, ''et al.'' |title=Characterization of a mutation within the NDP gene in a family with a manifesting female carrier. |journal=Hum. Mol. Genet. |volume=2 |issue= 10 |pages= 1727-9 |year= 1994 |pmid= 8268931 |doi=  }}
*{{cite journal  | author=Meitinger T, Meindl A, Bork P, ''et al.'' |title=Molecular modelling of the Norrie disease protein predicts a cystine knot growth factor tertiary structure. |journal=Nat. Genet. |volume=5 |issue= 4 |pages= 376-80 |year= 1994 |pmid= 8298646 |doi= 10.1038/ng1293-376 }}
*{{cite journal  | author=Strasberg P, Liede HA, Stein T, ''et al.'' |title=A novel mutation in the Norrie disease gene predicted to disrupt the cystine knot growth factor motif. |journal=Hum. Mol. Genet. |volume=4 |issue= 11 |pages= 2179-80 |year= 1996 |pmid= 8589700 |doi=  }}
*{{cite journal  | author=Johnson K, Mintz-Hittner HA, Conley YP, Ferrell RE |title=X-linked exudative vitreoretinopathy caused by an arginine to leucine substitution (R121L) in the Norrie disease protein. |journal=Clin. Genet. |volume=50 |issue= 3 |pages= 113-5 |year= 1997 |pmid= 8946107 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

NUMA1

• INFO: Beginning work on NUMA1... {November 18, 2007 10:13:05 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:13:33 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Nuclear mitotic apparatus protein 1
 | HGNCid = 8059
 | Symbol = NUMA1
 | AltSymbols =; NUMA
 | OMIM = 164009
 | ECnumber =  
 | Homologene = 38150
 | MGIid = 2443665
 | GeneAtlas_image1 = PBB_GE_NUMA1_200747_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_NUMA1_214251_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} 
 | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005876 |text = spindle microtubule}} 
 | Process = {{GNF_GO|id=GO:0000090 |text = mitotic anaphase}} {{GNF_GO|id=GO:0006997 |text = nuclear organization and biogenesis}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4926
    | Hs_Ensembl = ENSG00000137497
    | Hs_RefseqProtein = NP_006176
    | Hs_RefseqmRNA = NM_006185
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 71391559
    | Hs_GenLoc_end = 71469221
    | Hs_Uniprot = Q14980
    | Mm_EntrezGene = 101706
    | Mm_Ensembl = ENSMUSG00000066306
    | Mm_RefseqmRNA = NM_133947
    | Mm_RefseqProtein = NP_598708
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 101807932
    | Mm_GenLoc_end = 101887774
    | Mm_Uniprot =  
  }}
}}
'''Nuclear mitotic apparatus protein 1''', also known as '''NUMA1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NUMA1 nuclear mitotic apparatus protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4926| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = 
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Sun QY, Schatten H |title=Role of NuMA in vertebrate cells: review of an intriguing multifunctional protein. |journal=Front. Biosci. |volume=11 |issue=  |pages= 1137-46 |year= 2006 |pmid= 16146802 |doi=  }}
*{{cite journal  | author=Yang CH, Lambie EJ, Snyder M |title=NuMA: an unusually long coiled-coil related protein in the mammalian nucleus. |journal=J. Cell Biol. |volume=116 |issue= 6 |pages= 1303-17 |year= 1992 |pmid= 1541630 |doi=  }}
*{{cite journal  | author=Compton DA, Szilak I, Cleveland DW |title=Primary structure of NuMA, an intranuclear protein that defines a novel pathway for segregation of proteins at mitosis. |journal=J. Cell Biol. |volume=116 |issue= 6 |pages= 1395-408 |year= 1992 |pmid= 1541636 |doi=  }}
*{{cite journal  | author=Lydersen BK, Pettijohn DE |title=Human-specific nuclear protein that associates with the polar region of the mitotic apparatus: distribution in a human/hamster hybrid cell. |journal=Cell |volume=22 |issue= 2 Pt 2 |pages= 489-99 |year= 1981 |pmid= 7004645 |doi=  }}
*{{cite journal  | author=Sparks CA, Bangs PL, McNeil GP, ''et al.'' |title=Assignment of the nuclear mitotic apparatus protein NuMA gene to human chromosome 11q13. |journal=Genomics |volume=17 |issue= 1 |pages= 222-4 |year= 1993 |pmid= 8406455 |doi= 10.1006/geno.1993.1307 }}
*{{cite journal  | author=Maekawa T, Kuriyama R |title=Primary structure and microtubule-interacting domain of the SP-H antigen: a mitotic MAP located at the spindle pole and characterized as a homologous protein to NuMA. |journal=J. Cell. Sci. |volume=105 ( Pt 2) |issue=  |pages= 589-600 |year= 1993 |pmid= 8408288 |doi=  }}
*{{cite journal  | author=Tang TK, Tang CJ, Chen YL, Wu CW |title=Nuclear proteins of the bovine esophageal epithelium. II. The NuMA gene gives rise to multiple mRNAs and gene products reactive with monoclonal antibody W1. |journal=J. Cell. Sci. |volume=104 ( Pt 2) |issue=  |pages= 249-60 |year= 1993 |pmid= 8505359 |doi=  }}
*{{cite journal  | author=Wells RA, Catzavelos C, Kamel-Reid S |title=Fusion of retinoic acid receptor alpha to NuMA, the nuclear mitotic apparatus protein, by a variant translocation in acute promyelocytic leukaemia. |journal=Nat. Genet. |volume=17 |issue= 1 |pages= 109-13 |year= 1997 |pmid= 9288109 |doi= 10.1038/ng0997-109 }}
*{{cite journal  | author=Andrade F, Roy S, Nicholson D, ''et al.'' |title=Granzyme B directly and efficiently cleaves several downstream caspase substrates: implications for CTL-induced apoptosis. |journal=Immunity |volume=8 |issue= 4 |pages= 451-60 |year= 1998 |pmid= 9586635 |doi=  }}
*{{cite journal  | author=Novick D, Kim SH, Fantuzzi G, ''et al.'' |title=Interleukin-18 binding protein: a novel modulator of the Th1 cytokine response. |journal=Immunity |volume=10 |issue= 1 |pages= 127-36 |year= 1999 |pmid= 10023777 |doi=  }}
*{{cite journal  | author=Mattagajasingh SN, Huang SC, Hartenstein JS, ''et al.'' |title=A nonerythroid isoform of protein 4.1R interacts with the nuclear mitotic apparatus (NuMA) protein. |journal=J. Cell Biol. |volume=145 |issue= 1 |pages= 29-43 |year= 1999 |pmid= 10189366 |doi=  }}
*{{cite journal  | author=Clark IB, Meyer DI |title=Overexpression of normal and mutant Arp1alpha (centractin) differentially affects microtubule organization during mitosis and interphase. |journal=J. Cell. Sci. |volume=112 ( Pt 20) |issue=  |pages= 3507-18 |year= 2000 |pmid= 10504299 |doi=  }}
*{{cite journal  | author=Ye K, Compton DA, Lai MM, ''et al.'' |title=Protein 4.1N binding to nuclear mitotic apparatus protein in PC12 cells mediates the antiproliferative actions of nerve growth factor. |journal=J. Neurosci. |volume=19 |issue= 24 |pages= 10747-56 |year= 2000 |pmid= 10594058 |doi=  }}
*{{cite journal  | author=Taimen P, Viljamaa M, Kallajoki M |title=Preferential expression of NuMA in the nuclei of proliferating cells. |journal=Exp. Cell Res. |volume=256 |issue= 1 |pages= 140-9 |year= 2000 |pmid= 10739661 |doi= 10.1006/excr.2000.4799 }}
*{{cite journal  | author=Harborth J, Weber K, Osborn M |title=GAS41, a highly conserved protein in eukaryotic nuclei, binds to NuMA. |journal=J. Biol. Chem. |volume=275 |issue= 41 |pages= 31979-85 |year= 2000 |pmid= 10913114 |doi= 10.1074/jbc.M000994200 }}
*{{cite journal  | author=Gregson HC, Schmiesing JA, Kim JS, ''et al.'' |title=A potential role for human cohesin in mitotic spindle aster assembly. |journal=J. Biol. Chem. |volume=276 |issue= 50 |pages= 47575-82 |year= 2002 |pmid= 11590136 |doi= 10.1074/jbc.M103364200 }}
*{{cite journal  | author=Du Q, Stukenberg PT, Macara IG |title=A mammalian Partner of inscuteable binds NuMA and regulates mitotic spindle organization. |journal=Nat. Cell Biol. |volume=3 |issue= 12 |pages= 1069-75 |year= 2002 |pmid= 11781568 |doi= 10.1038/ncb1201-1069 }}
*{{cite journal  | author=Andersen JS, Lyon CE, Fox AH, ''et al.'' |title=Directed proteomic analysis of the human nucleolus. |journal=Curr. Biol. |volume=12 |issue= 1 |pages= 1-11 |year= 2002 |pmid= 11790298 |doi=  }}
*{{cite journal  | author=Haren L, Merdes A |title=Direct binding of NuMA to tubulin is mediated by a novel sequence motif in the tail domain that bundles and stabilizes microtubules. |journal=J. Cell. Sci. |volume=115 |issue= Pt 9 |pages= 1815-24 |year= 2002 |pmid= 11956313 |doi=  }}
*{{cite journal  | author=Sbodio JI, Chi NW |title=Identification of a tankyrase-binding motif shared by IRAP, TAB182, and human TRF1 but not mouse TRF1. NuMA contains this RXXPDG motif and is a novel tankyrase partner. |journal=J. Biol. Chem. |volume=277 |issue= 35 |pages= 31887-92 |year= 2002 |pmid= 12080061 |doi= 10.1074/jbc.M203916200 }}
}}
{{refend}}

{{protein-stub}}
 

OXTR

• INFO: Beginning work on OXTR... {November 18, 2007 10:13:33 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:14:00 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Oxytocin receptor
 | HGNCid = 8529
 | Symbol = OXTR
 | AltSymbols =; OT-R
 | OMIM = 167055
 | ECnumber =  
 | Homologene = 20255
 | MGIid = 109147
 | GeneAtlas_image1 = PBB_GE_OXTR_206825_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:0004990 |text = oxytocin receptor activity}} {{GNF_GO|id=GO:0005000 |text = vasopressin receptor activity}} 
 | Component = {{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}} 
 | Process = {{GNF_GO|id=GO:0006936 |text = muscle contraction}} {{GNF_GO|id=GO:0007200 |text = G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)}} {{GNF_GO|id=GO:0007565 |text = female pregnancy}} {{GNF_GO|id=GO:0007595 |text = lactation}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5021
    | Hs_Ensembl = ENSG00000180914
    | Hs_RefseqProtein = NP_000907
    | Hs_RefseqmRNA = NM_000916
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 8765419
    | Hs_GenLoc_end = 8786300
    | Hs_Uniprot = P30559
    | Mm_EntrezGene = 18430
    | Mm_Ensembl = ENSMUSG00000049112
    | Mm_RefseqmRNA = XM_001001627
    | Mm_RefseqProtein = XP_001001627
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 6
    | Mm_GenLoc_start = 112442851
    | Mm_GenLoc_end = 112455574
    | Mm_Uniprot = Q3UPP9
  }}
}}
'''Oxytocin receptor''', also known as '''OXTR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: OXTR oxytocin receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5021| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = The protein encoded by this gene belongs to the G-protein coupled receptor family and acts as a receptor for oxytocin. Its activity is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system. The oxytocin-oxytocin receptor system plays an important role in the uterus during parturition.<ref name="entrez">{{cite web | title = Entrez Gene: OXTR oxytocin receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5021| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Kimura T, Ivell R |title=The oxytocin receptor. |journal=Results and problems in cell differentiation |volume=26 |issue=  |pages= 135-68 |year= 1999 |pmid= 10453463 |doi=  }}
*{{cite journal  | author=Cassoni P, Sapino A, Marrocco T, ''et al.'' |title=Oxytocin and oxytocin receptors in cancer cells and proliferation. |journal=J. Neuroendocrinol. |volume=16 |issue= 4 |pages= 362-4 |year= 2004 |pmid= 15089975 |doi= 10.1111/j.0953-8194.2004.01165.x }}
*{{cite journal  | author=Devost D, Zingg HH |title=Homo- and hetero-dimeric complex formations of the human oxytocin receptor. |journal=J. Neuroendocrinol. |volume=16 |issue= 4 |pages= 372-7 |year= 2004 |pmid= 15089977 |doi= 10.1111/j.0953-8194.2004.01188.x }}
*{{cite journal  | author=Kimura T, Tanizawa O, Mori K, ''et al.'' |title=Structure and expression of a human oxytocin receptor. |journal=Nature |volume=356 |issue= 6369 |pages= 526-9 |year= 1992 |pmid= 1313946 |doi= 10.1038/356526a0 }}
*{{cite journal  | author=Simmons CF, Clancy TE, Quan R, Knoll JH |title=The oxytocin receptor gene (OXTR) localizes to human chromosome 3p25 by fluorescence in situ hybridization and PCR analysis of somatic cell hybrids. |journal=Genomics |volume=26 |issue= 3 |pages= 623-5 |year= 1995 |pmid= 7607693 |doi=  }}
*{{cite journal  | author=Inoue T, Kimura T, Azuma C, ''et al.'' |title=Structural organization of the human oxytocin receptor gene. |journal=J. Biol. Chem. |volume=269 |issue= 51 |pages= 32451-6 |year= 1995 |pmid= 7798245 |doi=  }}
*{{cite journal  | author=Kjaer A, Knigge U, Warberg J |title=Histamine- and stress-induced prolactin secretion: importance of vasopressin V1- and V2-receptors. |journal=Eur. J. Endocrinol. |volume=131 |issue= 4 |pages= 391-7 |year= 1994 |pmid= 7921229 |doi=  }}
*{{cite journal  | author=Mayerhofer A, Sterzik K, Link H, ''et al.'' |title=Effect of oxytocin on free intracellular Ca2+ levels and progesterone release by human granulosa-lutein cells. |journal=J. Clin. Endocrinol. Metab. |volume=77 |issue= 5 |pages= 1209-14 |year= 1994 |pmid= 8077313 |doi=  }}
*{{cite journal  | author=Ito Y, Kobayashi T, Kimura T, ''et al.'' |title=Investigation of the oxytocin receptor expression in human breast cancer tissue using newly established monoclonal antibodies. |journal=Endocrinology |volume=137 |issue= 2 |pages= 773-9 |year= 1996 |pmid= 8593829 |doi=  }}
*{{cite journal  | author=Kimura T, Takemura M, Nomura S, ''et al.'' |title=Expression of oxytocin receptor in human pregnant myometrium. |journal=Endocrinology |volume=137 |issue= 2 |pages= 780-5 |year= 1996 |pmid= 8593830 |doi=  }}
*{{cite journal  | author=Gimpl G, Burger K, Fahrenholz F |title=Cholesterol as modulator of receptor function. |journal=Biochemistry |volume=36 |issue= 36 |pages= 10959-74 |year= 1997 |pmid= 9283088 |doi= 10.1021/bi963138w }}
*{{cite journal  | author=Kimura T, Makino Y, Bathgate R, ''et al.'' |title=The role of N-terminal glycosylation in the human oxytocin receptor. |journal=Mol. Hum. Reprod. |volume=3 |issue= 11 |pages= 957-63 |year= 1998 |pmid= 9433921 |doi=  }}
*{{cite journal  | author=Kimura T |title=Regulation of the human oxytocin receptor in the uterus: a molecular approach. |journal=Hum. Reprod. Update |volume=4 |issue= 5 |pages= 615-24 |year= 1999 |pmid= 10027615 |doi=  }}
*{{cite journal  | author=Politowska E, Czaplewski C, Ciarkowski J |title=Molecular modeling of the oxytocin receptor/bioligand interactions. |journal=Acta Biochim. Pol. |volume=46 |issue= 3 |pages= 581-90 |year= 2000 |pmid= 10698266 |doi=  }}
*{{cite journal  | author=Berrada K, Plesnicher CL, Luo X, Thibonnier M |title=Dynamic interaction of human vasopressin/oxytocin receptor subtypes with G protein-coupled receptor kinases and protein kinase C after agonist stimulation. |journal=J. Biol. Chem. |volume=275 |issue= 35 |pages= 27229-37 |year= 2000 |pmid= 10858434 |doi= 10.1074/jbc.M002288200 }}
*{{cite journal  | author=Novak JF, Judkins MB, Chernin MI, ''et al.'' |title=A plasmin-derived hexapeptide from the carboxyl end of osteocalcin counteracts oxytocin-mediated growth inhibition [corrected] of osteosarcoma cells. |journal=Cancer Res. |volume=60 |issue= 13 |pages= 3470-6 |year= 2000 |pmid= 10910058 |doi=  }}
*{{cite journal  | author=Oakley RH, Laporte SA, Holt JA, ''et al.'' |title=Molecular determinants underlying the formation of stable intracellular G protein-coupled receptor-beta-arrestin complexes after receptor endocytosis*. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 19452-60 |year= 2001 |pmid= 11279203 |doi= 10.1074/jbc.M101450200 }}
*{{cite journal  | author=Wesley VJ, Hawtin SR, Howard HC, Wheatley M |title=Agonist-specific, high-affinity binding epitopes are contributed by an arginine in the N-terminus of the human oxytocin receptor. |journal=Biochemistry |volume=41 |issue= 16 |pages= 5086-92 |year= 2002 |pmid= 11955056 |doi=  }}
*{{cite journal  | author=Petersson M, Lagumdzija A, Stark A, Bucht E |title=Oxytocin stimulates proliferation of human osteoblast-like cells. |journal=Peptides |volume=23 |issue= 6 |pages= 1121-6 |year= 2003 |pmid= 12126740 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

PBX1

• INFO: Beginning work on PBX1... {November 18, 2007 10:14:00 AM PST}
• SEARCH REDIRECT: Control Box Found: PBX1 {November 18, 2007 10:14:25 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:14:26 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:14:26 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:14:26 AM PST}
• UPDATED: Updated protein page: PBX1 {November 18, 2007 10:14:33 AM PST}

PFN1

• INFO: Beginning work on PFN1... {November 18, 2007 10:14:33 AM PST}
• SEARCH REDIRECT: Control Box Found: PFN1 {November 18, 2007 10:14:56 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:14:57 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:14:57 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:14:57 AM PST}
• UPDATED: Updated protein page:
  PFN1
  {November 18, 2007 10:15:04 AM PST}

PKM2

• INFO: Beginning work on PKM2... {November 18, 2007 10:15:05 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:15:47 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_PKM2_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a49.
 | PDB = {{PDB2|1a49}}, {{PDB2|1a5u}}, {{PDB2|1aqf}}, {{PDB2|1f3w}}, {{PDB2|1f3x}}, {{PDB2|1pkm}}, {{PDB2|1pkn}}, {{PDB2|1t5a}}, {{PDB2|1zjh}}, {{PDB2|2g50}}
 | Name = Pyruvate kinase, muscle
 | HGNCid = 9021
 | Symbol = PKM2
 | AltSymbols =; CTHBP; MGC3932; OIP3; PK3; PKM; TCB; THBP1
 | OMIM = 179050
 | ECnumber =  
 | Homologene = 37650
 | MGIid = 97591
 | GeneAtlas_image1 = PBB_GE_PKM2_201251_at_tn.png
 | Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004743 |text = pyruvate kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} 
 | Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}} 
 | Process = {{GNF_GO|id=GO:0006096 |text = glycolysis}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5315
    | Hs_Ensembl = ENSG00000067225
    | Hs_RefseqProtein = NP_002645
    | Hs_RefseqmRNA = NM_002654
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 15
    | Hs_GenLoc_start = 70278424
    | Hs_GenLoc_end = 70310738
    | Hs_Uniprot = P14618
    | Mm_EntrezGene = 18746
    | Mm_Ensembl = ENSMUSG00000032294
    | Mm_RefseqmRNA = XM_979537
    | Mm_RefseqProtein = XP_984631
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 59454614
    | Mm_GenLoc_end = 59477381
    | Mm_Uniprot = Q3TBV8
  }}
}}
'''Pyruvate kinase, muscle''', also known as '''PKM2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PKM2 pyruvate kinase, muscle| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5315| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = The protein encoded by this gene is a pyruvate kinase that catalyzes the production of phosphoenolpyruvate from pyruvate and ATP. This protein has been shown to interact with thyroid hormone, and thus may mediate cellular metabolic effects induced by thyroid hormones. This protein has been found to bind Opa protein, a bacterial outer membrane protein involved in gonococcal adherence to and invasion of human cells, suggesting a role of this protein in bacterial pathogenesis. Three alternatively spliced transcript variants encoding two distinct isoforms have been reported.<ref name="entrez">{{cite web | title = Entrez Gene: PKM2 pyruvate kinase, muscle| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5315| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Garfinkel L, Garfinkel D |title=Magnesium regulation of the glycolytic pathway and the enzymes involved. |journal=Magnesium |volume=4 |issue= 2-3 |pages= 60-72 |year= 1985 |pmid= 2931560 |doi=  }}
*{{cite journal  | author=Mazurek S, Grimm H, Boschek CB, ''et al.'' |title=Pyruvate kinase type M2: a crossroad in the tumor metabolome. |journal=Br. J. Nutr. |volume=87 Suppl 1 |issue=  |pages= S23-9 |year= 2002 |pmid= 11895152 |doi=  }}
*{{cite journal  | author=Takenaka M, Noguchi T, Sadahiro S, ''et al.'' |title=Isolation and characterization of the human pyruvate kinase M gene. |journal=Eur. J. Biochem. |volume=198 |issue= 1 |pages= 101-6 |year= 1991 |pmid= 2040271 |doi=  }}
*{{cite journal  | author=Marjanovic S, Eriksson I, Nelson BD |title=Expression of a new set of glycolytic isozymes in activated human peripheral lymphocytes. |journal=Biochim. Biophys. Acta |volume=1087 |issue= 1 |pages= 1-6 |year= 1990 |pmid= 2169315 |doi=  }}
*{{cite journal  | author=Liu JB |title=[M2-type pyruvate kinase in the diagnosis of hepatocarcinoma--a pilot study] |journal=Zhonghua Zhong Liu Za Zhi |volume=12 |issue= 3 |pages= 166-9 |year= 1991 |pmid= 2174328 |doi=  }}
*{{cite journal  | author=Kato H, Fukuda T, Parkison C, ''et al.'' |title=Cytosolic thyroid hormone-binding protein is a monomer of pyruvate kinase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 20 |pages= 7861-5 |year= 1989 |pmid= 2813362 |doi=  }}
*{{cite journal  | author=Tsutsumi H, Tani K, Fujii H, Miwa S |title=Expression of L- and M-type pyruvate kinase in human tissues. |journal=Genomics |volume=2 |issue= 1 |pages= 86-9 |year= 1988 |pmid= 2838416 |doi=  }}
*{{cite journal  | author=Tani K, Yoshida MC, Satoh H, ''et al.'' |title=Human M2-type pyruvate kinase: cDNA cloning, chromosomal assignment and expression in hepatoma. |journal=Gene |volume=73 |issue= 2 |pages= 509-16 |year= 1989 |pmid= 2854097 |doi=  }}
*{{cite journal  | author=Kechemir D, Max-Audit I, Calvin-Preval MC, Rosa R |title=Purification of human leucocyte pyruvate kinase. |journal=J. Chromatogr. |volume=383 |issue= 1 |pages= 43-50 |year= 1987 |pmid= 3102533 |doi=  }}
*{{cite journal  | author=Junien C, Rubinson-Skala H, Dreyfus JC, ''et al.'' |title=PK3: a new chromosome enzyme marker for gene dosage studies in chromosome 15 imbalance. |journal=Hum. Genet. |volume=54 |issue= 2 |pages= 191-6 |year= 1980 |pmid= 6930359 |doi=  }}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal  | author=Gress TM, Müller-Pillasch F, Geng M, ''et al.'' |title=A pancreatic cancer-specific expression profile. |journal=Oncogene |volume=13 |issue= 8 |pages= 1819-30 |year= 1996 |pmid= 8895530 |doi=  }}
*{{cite journal  | author=Eigenbrodt E, Basenau D, Holthusen S, ''et al.'' |title=Quantification of tumor type M2 pyruvate kinase (Tu M2-PK) in human carcinomas. |journal=Anticancer Res. |volume=17 |issue= 4B |pages= 3153-6 |year= 1997 |pmid= 9329624 |doi=  }}
*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{cite journal  | author=Williams JM, Chen GC, Zhu L, Rest RF |title=Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth. |journal=Mol. Microbiol. |volume=27 |issue= 1 |pages= 171-86 |year= 1998 |pmid= 9466265 |doi=  }}
*{{cite journal  | author=Demina A, Varughese KI, Barbot J, ''et al.'' |title=Six previously undescribed pyruvate kinase mutations causing enzyme deficiency. |journal=Blood |volume=92 |issue= 2 |pages= 647-52 |year= 1998 |pmid= 9657767 |doi=  }}
*{{cite journal  | author=Lowrie DJ, Stickney JT, Ip W |title=Properties of the nonhelical end domains of vimentin suggest a role in maintaining intermediate filament network structure. |journal=J. Struct. Biol. |volume=132 |issue= 2 |pages= 83-94 |year= 2001 |pmid= 11162730 |doi= 10.1006/jsbi.2000.4315 }}
*{{cite journal  | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
}}
{{refend}}

{{protein-stub}}
 

PRKAR2B

• INFO: Beginning work on PRKAR2B... {November 18, 2007 10:15:47 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:16:22 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_PRKAR2B_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cx4.
 | PDB = {{PDB2|1cx4}}
 | Name = Protein kinase, cAMP-dependent, regulatory, type II, beta
 | HGNCid = 9392
 | Symbol = PRKAR2B
 | AltSymbols =; PRKAR2; RII-BETA
 | OMIM = 176912
 | ECnumber =  
 | Homologene = 37666
 | MGIid = 97760
 | GeneAtlas_image1 = PBB_GE_PRKAR2B_203680_at_tn.png
 | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0008603 |text = cAMP-dependent protein kinase regulator activity}} {{GNF_GO|id=GO:0030552 |text = cAMP binding}} 
 | Component = {{GNF_GO|id=GO:0005952 |text = cAMP-dependent protein kinase complex}} 
 | Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006631 |text = fatty acid metabolic process}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0007612 |text = learning}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5577
    | Hs_Ensembl = ENSG00000005249
    | Hs_RefseqProtein = NP_002727
    | Hs_RefseqmRNA = NM_002736
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 106472375
    | Hs_GenLoc_end = 106589491
    | Hs_Uniprot = P31323
    | Mm_EntrezGene = 19088
    | Mm_Ensembl = ENSMUSG00000002997
    | Mm_RefseqmRNA = NM_011158
    | Mm_RefseqProtein = NP_035288
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 12
    | Mm_GenLoc_start = 32543731
    | Mm_GenLoc_end = 32646499
    | Mm_Uniprot = Q3V2X9
  }}
}}
'''Protein kinase, cAMP-dependent, regulatory, type II, beta''', also known as '''PRKAR2B''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRKAR2B protein kinase, cAMP-dependent, regulatory, type II, beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5577| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase (AMPK), which transduces the signal through phosphorylation of different target proteins. The inactive holoenzyme of AMPK is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits of AMPK have been identified in humans. The protein encoded by this gene is one of the regulatory subunits. This subunit can be phosphorylated by the activated catalytic subunit. This subunit has been shown to interact with and suppress the transcriptional activity of the cAMP responsive element binding protein 1 (CREB1) in activated T cells. Knockout studies in mice suggest that this subunit may play an important role in regulating energy balance and adiposity. The studies also suggest that this subunit may mediate the gene induction and cataleptic behavior induced by haloperidol.<ref name="entrez">{{cite web | title = Entrez Gene: PRKAR2B protein kinase, cAMP-dependent, regulatory, type II, beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5577| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Harrich D, McMillan N, Munoz L, ''et al.'' |title=Will diverse Tat interactions lead to novel antiretroviral drug targets? |journal=Current drug targets |volume=7 |issue= 12 |pages= 1595-606 |year= 2007 |pmid= 17168834 |doi=  }}
*{{cite journal  | author=Luo Z, Singh IS, Fujihira T, Erlichman J |title=Characterization of a minimal promoter element required for transcription of the mouse type II beta regulatory subunit (RII beta) of cAMP-dependent protein kinase. |journal=J. Biol. Chem. |volume=267 |issue= 34 |pages= 24738-47 |year= 1992 |pmid= 1332964 |doi=  }}
*{{cite journal  | author=Solberg R, Sistonen P, Träskelin AL, ''et al.'' |title=Mapping of the regulatory subunits RI beta and RII beta of cAMP-dependent protein kinase genes on human chromosome 7. |journal=Genomics |volume=14 |issue= 1 |pages= 63-9 |year= 1992 |pmid= 1358799 |doi=  }}
*{{cite journal  | author=Rios RM, Celati C, Lohmann SM, ''et al.'' |title=Identification of a high affinity binding protein for the regulatory subunit RII beta of cAMP-dependent protein kinase in Golgi enriched membranes of human lymphoblasts. |journal=EMBO J. |volume=11 |issue= 5 |pages= 1723-31 |year= 1992 |pmid= 1582408 |doi=  }}
*{{cite journal  | author=Tortora G, Clair T, Cho-Chung YS |title=An antisense oligodeoxynucleotide targeted against the type II beta regulatory subunit mRNA of protein kinase inhibits cAMP-induced differentiation in HL-60 leukemia cells without affecting phorbol ester effects. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 2 |pages= 705-8 |year= 1990 |pmid= 1689049 |doi=  }}
*{{cite journal  | author=Hofmann B, Nishanian P, Baldwin RL, ''et al.'' |title=HIV inhibits the early steps of lymphocyte activation, including initiation of inositol phospholipid metabolism. |journal=J. Immunol. |volume=145 |issue= 11 |pages= 3699-705 |year= 1991 |pmid= 1978848 |doi=  }}
*{{cite journal  | author=Levy FO, Oyen O, Sandberg M, ''et al.'' |title=Molecular cloning, complementary deoxyribonucleic acid structure and predicted full-length amino acid sequence of the hormone-inducible regulatory subunit of 3'-5'-cyclic adenosine monophosphate-dependent protein kinase from human testis. |journal=Mol. Endocrinol. |volume=2 |issue= 12 |pages= 1364-73 |year= 1989 |pmid= 2851102 |doi=  }}
*{{cite journal  | author=Scambler P, Oyen O, Wainwright B, ''et al.'' |title=Exclusion of catalytic and regulatory subunits of cAMP-dependent protein kinase as candidate genes for the defect causing cystic fibrosis. |journal=Am. J. Hum. Genet. |volume=41 |issue= 5 |pages= 925-32 |year= 1987 |pmid= 3479018 |doi=  }}
*{{cite journal  | author=Wainwright B, Lench N, Davies K, ''et al.'' |title=A human regulatory subunit of type II cAMP-dependent protein kinase localized by its linkage relationship to several cloned chromosome 7q markers. |journal=Cytogenet. Cell Genet. |volume=45 |issue= 3-4 |pages= 237-9 |year= 1988 |pmid= 3691190 |doi=  }}
*{{cite journal  | author=Budillon A, Cereseto A, Kondrashin A, ''et al.'' |title=Point mutation of the autophosphorylation site or in the nuclear location signal causes protein kinase A RII beta regulatory subunit to lose its ability to revert transformed fibroblasts. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 23 |pages= 10634-8 |year= 1995 |pmid= 7479855 |doi=  }}
*{{cite journal  | author=Hofmann B, Nishanian P, Nguyen T, ''et al.'' |title=Human immunodeficiency virus proteins induce the inhibitory cAMP/protein kinase A pathway in normal lymphocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 14 |pages= 6676-80 |year= 1993 |pmid= 7688126 |doi=  }}
*{{cite journal  | author=Berg JP, Ree AH, Sandvik JA, ''et al.'' |title=1,25-dihydroxyvitamin D3 alters the effect of cAMP in thyroid cells by increasing the regulatory subunit type II beta of the cAMP-dependent protein kinase. |journal=J. Biol. Chem. |volume=269 |issue= 51 |pages= 32233-8 |year= 1995 |pmid= 7798223 |doi=  }}
*{{cite journal  | author=Li Y, Rubin CS |title=Mutagenesis of the regulatory subunit (RII beta) of cAMP-dependent protein kinase II beta reveals hydrophobic amino acids that are essential for RII beta dimerization and/or anchoring RII beta to the cytoskeleton. |journal=J. Biol. Chem. |volume=270 |issue= 4 |pages= 1935-44 |year= 1995 |pmid= 7829531 |doi=  }}
*{{cite journal  | author=Hofmann B, Nishanian P, Fan J, ''et al.'' |title=HIV Gag p17 protein impairs proliferation of normal lymphocytes in vitro. |journal=AIDS |volume=8 |issue= 7 |pages= 1016-7 |year= 1994 |pmid= 7946090 |doi=  }}
*{{cite journal  | author=Glantz SB, Li Y, Rubin CS |title=Characterization of distinct tethering and intracellular targeting domains in AKAP75, a protein that links cAMP-dependent protein kinase II beta to the cytoskeleton. |journal=J. Biol. Chem. |volume=268 |issue= 17 |pages= 12796-804 |year= 1993 |pmid= 8509414 |doi=  }}
*{{cite journal  | author=Keryer G, Luo Z, Cavadore JC, ''et al.'' |title=Phosphorylation of the regulatory subunit of type II beta cAMP-dependent protein kinase by cyclin B/p34cdc2 kinase impairs its binding to microtubule-associated protein 2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 12 |pages= 5418-22 |year= 1993 |pmid= 8516283 |doi=  }}
*{{cite journal  | author=Swingler S, Gallay P, Camaur D, ''et al.'' |title=The Nef protein of human immunodeficiency virus type 1 enhances serine phosphorylation of the viral matrix. |journal=J. Virol. |volume=71 |issue= 6 |pages= 4372-7 |year= 1997 |pmid= 9151826 |doi=  }}
*{{cite journal  | author=Chen P, Mayne M, Power C, Nath A |title=The Tat protein of HIV-1 induces tumor necrosis factor-alpha production. Implications for HIV-1-associated neurological diseases. |journal=J. Biol. Chem. |volume=272 |issue= 36 |pages= 22385-8 |year= 1997 |pmid= 9278385 |doi=  }}
*{{cite journal  | author=Huang LJ, Durick K, Weiner JA, ''et al.'' |title=D-AKAP2, a novel protein kinase A anchoring protein with a putative RGS domain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 21 |pages= 11184-9 |year= 1997 |pmid= 9326583 |doi=  }}
*{{cite journal  | author=Zidovetzki R, Wang JL, Chen P, ''et al.'' |title=Human immunodeficiency virus Tat protein induces interleukin 6 mRNA expression in human brain endothelial cells via protein kinase C- and cAMP-dependent protein kinase pathways. |journal=AIDS Res. Hum. Retroviruses |volume=14 |issue= 10 |pages= 825-33 |year= 1998 |pmid= 9671211 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

PSMB4

• INFO: Beginning work on PSMB4... {November 18, 2007 10:16:22 AM PST}
• SEARCH REDIRECT: Control Box Found: PSMB4 {November 18, 2007 10:16:57 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:16:58 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:16:58 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:16:58 AM PST}
• UPDATED: Updated protein page: PSMB4 {November 18, 2007 10:17:05 AM PST}

PSMD10

• INFO: Beginning work on PSMD10... {November 18, 2007 10:17:05 AM PST}
• SEARCH REDIRECT: Control Box Found: PSMD10 {November 18, 2007 10:17:41 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:17:44 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:17:44 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:17:44 AM PST}
• UPDATED: Updated protein page: PSMD10 {November 18, 2007 10:17:51 AM PST}

PSME2

• INFO: Beginning work on PSME2... {November 18, 2007 10:17:51 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:18:28 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Proteasome (prosome, macropain) activator subunit 2 (PA28 beta)
 | HGNCid = 9569
 | Symbol = PSME2
 | AltSymbols =; PA28B; PA28beta; REGbeta
 | OMIM = 602161
 | ECnumber =  
 | Homologene = 86889
 | MGIid =  
 | GeneAtlas_image1 = PBB_GE_PSME2_201762_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0008538 |text = proteasome activator activity}} 
 | Component = {{GNF_GO|id=GO:0000502 |text = proteasome complex (sensu Eukaryota)}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0008537 |text = proteasome activator complex}} 
 | Process = {{GNF_GO|id=GO:0006955 |text = immune response}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5721
    | Hs_Ensembl = ENSG00000100911
    | Hs_RefseqProtein = NP_002809
    | Hs_RefseqmRNA = NM_002818
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 14
    | Hs_GenLoc_start = 23682449
    | Hs_GenLoc_end = 23686270
    | Hs_Uniprot = Q9UL46
    | Mm_EntrezGene =  
    | Mm_Ensembl =  
    | Mm_RefseqmRNA =  
    | Mm_RefseqProtein =  
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr =  
    | Mm_GenLoc_start =  
    | Mm_GenLoc_end =  
    | Mm_Uniprot =  
  }}
}}
'''Proteasome (prosome, macropain) activator subunit 2 (PA28 beta)''', also known as '''PSME2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSME2 proteasome (prosome, macropain) activator subunit 2 (PA28 beta)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5721| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway.  An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. This gene encodes the beta subunit of the 11S regulator, one of the two 11S subunits that is induced by gamma-interferon. Three beta and three alpha subunits combine to form a heterohexameric ring. Six pseudogenes have been identified on chromosomes 4, 5, 8, 10 and 13.<ref name="entrez">{{cite web | title = Entrez Gene: PSME2 proteasome (prosome, macropain) activator subunit 2 (PA28 beta)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5721| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Coux O, Tanaka K, Goldberg AL |title=Structure and functions of the 20S and 26S proteasomes. |journal=Annu. Rev. Biochem. |volume=65 |issue=  |pages= 801-47 |year= 1996 |pmid= 8811196 |doi= 10.1146/annurev.bi.65.070196.004101 }}
*{{cite journal  | author=Sijts A, Sun Y, Janek K, ''et al.'' |title=The role of the proteasome activator PA28 in MHC class I antigen processing. |journal=Mol. Immunol. |volume=39 |issue= 3-4 |pages= 165-9 |year= 2002 |pmid= 12200048 |doi=  }}
*{{cite journal  | author=Goff SP |title=Death by deamination: a novel host restriction system for HIV-1. |journal=Cell |volume=114 |issue= 3 |pages= 281-3 |year= 2003 |pmid= 12914693 |doi=  }}
*{{cite journal  | author=Dubiel W, Pratt G, Ferrell K, Rechsteiner M |title=Purification of an 11 S regulator of the multicatalytic protease. |journal=J. Biol. Chem. |volume=267 |issue= 31 |pages= 22369-77 |year= 1992 |pmid= 1429590 |doi=  }}
*{{cite journal  | author=Ahn JY, Tanahashi N, Akiyama K, ''et al.'' |title=Primary structures of two homologous subunits of PA28, a gamma-interferon-inducible protein activator of the 20S proteasome. |journal=FEBS Lett. |volume=366 |issue= 1 |pages= 37-42 |year= 1995 |pmid= 7789512 |doi=  }}
*{{cite journal  | author=Mott JD, Pramanik BC, Moomaw CR, ''et al.'' |title=PA28, an activator of the 20 S proteasome, is composed of two nonidentical but homologous subunits. |journal=J. Biol. Chem. |volume=269 |issue= 50 |pages= 31466-71 |year= 1995 |pmid= 7989312 |doi=  }}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal  | author=Ahn K, Erlander M, Leturcq D, ''et al.'' |title=In vivo characterization of the proteasome regulator PA28. |journal=J. Biol. Chem. |volume=271 |issue= 30 |pages= 18237-42 |year= 1996 |pmid= 8663520 |doi=  }}
*{{cite journal  | author=Seeger M, Ferrell K, Frank R, Dubiel W |title=HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8145-8 |year= 1997 |pmid= 9079628 |doi=  }}
*{{cite journal  | author=McCusker D, Jones T, Sheer D, Trowsdale J |title=Genetic relationships of the genes encoding the human proteasome beta subunits and the proteasome PA28 complex. |journal=Genomics |volume=45 |issue= 2 |pages= 362-7 |year= 1998 |pmid= 9344661 |doi= 10.1006/geno.1997.4948 }}
*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{cite journal  | author=Hendil KB, Khan S, Tanaka K |title=Simultaneous binding of PA28 and PA700 activators to 20 S proteasomes. |journal=Biochem. J. |volume=332 ( Pt 3) |issue=  |pages= 749-54 |year= 1998 |pmid= 9620878 |doi=  }}
*{{cite journal  | author=Madani N, Kabat D |title=An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. |journal=J. Virol. |volume=72 |issue= 12 |pages= 10251-5 |year= 1998 |pmid= 9811770 |doi=  }}
*{{cite journal  | author=Wójcik C, Tanaka K, Paweletz N, ''et al.'' |title=Proteasome activator (PA28) subunits, alpha, beta and gamma (Ki antigen) in NT2 neuronal precursor cells and HeLa S3 cells. |journal=Eur. J. Cell Biol. |volume=77 |issue= 2 |pages= 151-60 |year= 1999 |pmid= 9840465 |doi=  }}
*{{cite journal  | author=Simon JH, Gaddis NC, Fouchier RA, Malim MH |title=Evidence for a newly discovered cellular anti-HIV-1 phenotype. |journal=Nat. Med. |volume=4 |issue= 12 |pages= 1397-400 |year= 1998 |pmid= 9846577 |doi= 10.1038/3987 }}
*{{cite journal  | author=McCusker D, Wilson M, Trowsdale J |title=Organization of the genes encoding the human proteasome activators PA28alpha and beta. |journal=Immunogenetics |volume=49 |issue= 5 |pages= 438-45 |year= 1999 |pmid= 10199920 |doi=  }}
*{{cite journal  | author=Tanahashi N, Murakami Y, Minami Y, ''et al.'' |title=Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis. |journal=J. Biol. Chem. |volume=275 |issue= 19 |pages= 14336-45 |year= 2000 |pmid= 10799514 |doi=  }}
*{{cite journal  | author=Mulder LC, Muesing MA |title=Degradation of HIV-1 integrase by the N-end rule pathway. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29749-53 |year= 2000 |pmid= 10893419 |doi= 10.1074/jbc.M004670200 }}
*{{cite journal  | author=Sheehy AM, Gaddis NC, Choi JD, Malim MH |title=Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. |journal=Nature |volume=418 |issue= 6898 |pages= 646-50 |year= 2002 |pmid= 12167863 |doi= 10.1038/nature00939 }}
}}
{{refend}}

{{protein-stub}}
 

PTAFR

• INFO: Beginning work on PTAFR... {November 18, 2007 10:18:29 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:19:04 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- 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 = Platelet-activating factor receptor
 | HGNCid = 9582
 | Symbol = PTAFR
 | AltSymbols =; PAFR
 | OMIM = 173393
 | ECnumber =  
 | Homologene = 20260
 | MGIid = 106066
 | GeneAtlas_image1 = PBB_GE_PTAFR_206278_at_tn.png
 | GeneAtlas_image2 = PBB_GE_PTAFR_211661_x_at_tn.png
 | Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004992 |text = platelet activating factor receptor activity}} {{GNF_GO|id=GO:0005543 |text = phospholipid binding}} 
 | Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} 
 | Process = {{GNF_GO|id=GO:0001816 |text = cytokine production}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0019735 |text = antimicrobial humoral response}} {{GNF_GO|id=GO:0048015 |text = phosphoinositide-mediated signaling}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5724
    | Hs_Ensembl = ENSG00000169403
    | Hs_RefseqProtein = NP_000943
    | Hs_RefseqmRNA = NM_000952
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 28346264
    | Hs_GenLoc_end = 28392971
    | Hs_Uniprot = P25105
    | Mm_EntrezGene = 19204
    | Mm_Ensembl = ENSMUSG00000056529
    | Mm_RefseqmRNA = XM_357441
    | Mm_RefseqProtein = XP_357441
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 131836299
    | Mm_GenLoc_end = 131852935
    | Mm_Uniprot = Q62035
  }}
}}
'''Platelet-activating factor receptor''', also known as '''PTAFR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTAFR platelet-activating factor receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5724| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = PTAFR shows structural characteristics of the rhodopsin (MIM 180380) gene family and binds platelet-activating factor (PAF). PAF is a phospholipid (1-0-alkyl-2-acetyl-sn-glycero-3-phosphorylcholine) that has been implicated as a mediator in diverse pathologic processes, such as allergy, asthma, septic shock, arterial thrombosis, and inflammatory processes.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: PTAFR platelet-activating factor receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5724| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Shukla SD |title=Platelet-activating factor receptor and signal transduction mechanisms. |journal=FASEB J. |volume=6 |issue= 6 |pages= 2296-301 |year= 1992 |pmid= 1312046 |doi=  }}
*{{cite journal  | author=Sugimoto T, Tsuchimochi H, McGregor CG, ''et al.'' |title=Molecular cloning and characterization of the platelet-activating factor receptor gene expressed in the human heart. |journal=Biochem. Biophys. Res. Commun. |volume=189 |issue= 2 |pages= 617-24 |year= 1993 |pmid= 1281995 |doi=  }}
*{{cite journal  | author=Seyfried CE, Schweickart VL, Godiska R, Gray PW |title=The human platelet-activating factor receptor gene (PTAFR) contains no introns and maps to chromosome 1. |journal=Genomics |volume=13 |issue= 3 |pages= 832-4 |year= 1992 |pmid= 1322356 |doi=  }}
*{{cite journal  | author=Kunz D, Gerard NP, Gerard C |title=The human leukocyte platelet-activating factor receptor. cDNA cloning, cell surface expression, and construction of a novel epitope-bearing analog. |journal=J. Biol. Chem. |volume=267 |issue= 13 |pages= 9101-6 |year= 1992 |pmid= 1374385 |doi=  }}
*{{cite journal  | author=Ye RD, Prossnitz ER, Zou AH, Cochrane CG |title=Characterization of a human cDNA that encodes a functional receptor for platelet activating factor. |journal=Biochem. Biophys. Res. Commun. |volume=180 |issue= 1 |pages= 105-11 |year= 1991 |pmid= 1656963 |doi=  }}
*{{cite journal  | author=Nakamura M, Honda Z, Izumi T, ''et al.'' |title=Molecular cloning and expression of platelet-activating factor receptor from human leukocytes. |journal=J. Biol. Chem. |volume=266 |issue= 30 |pages= 20400-5 |year= 1991 |pmid= 1657923 |doi=  }}
*{{cite journal  | author=Haslam RJ, Williams KA, Davidson MM |title=Receptor-effector coupling in platelets: roles of guanine nucleotides. |journal=Adv. Exp. Med. Biol. |volume=192 |issue=  |pages= 265-80 |year= 1986 |pmid= 3010668 |doi=  }}
*{{cite journal  | author=Valone FH |title=Isolation of a platelet membrane protein which binds the platelet-activating factor 1-0-hexadecyl-2-acetyl-SN-glycero-3-phosphorylcholine. |journal=Immunology |volume=52 |issue= 1 |pages= 169-74 |year= 1984 |pmid= 6325330 |doi=  }}
*{{cite journal  | author=Cundell DR, Gerard NP, Gerard C, ''et al.'' |title=Streptococcus pneumoniae anchor to activated human cells by the receptor for platelet-activating factor. |journal=Nature |volume=377 |issue= 6548 |pages= 435-8 |year= 1995 |pmid= 7566121 |doi= 10.1038/377435a0 }}
*{{cite journal  | author=Izumi T, Kishimoto S, Takano T, ''et al.'' |title=Expression of human platelet-activating factor receptor gene in EoL-1 cells following butyrate-induced differentiation. |journal=Biochem. J. |volume=305 ( Pt 3) |issue=  |pages= 829-35 |year= 1995 |pmid= 7848283 |doi=  }}
*{{cite journal  | author=Bito H, Honda Z, Nakamura M, Shimizu T |title=Cloning, expression and tissue distribution of rat platelet-activating-factor-receptor cDNA. |journal=Eur. J. Biochem. |volume=221 |issue= 1 |pages= 211-8 |year= 1994 |pmid= 8168510 |doi=  }}
*{{cite journal  | author=Chase PB, Halonen M, Regan JW |title=Cloning of a human platelet-activating factor receptor gene: evidence for an intron in the 5'-untranslated region. |journal=Am. J. Respir. Cell Mol. Biol. |volume=8 |issue= 3 |pages= 240-4 |year= 1993 |pmid= 8383507 |doi=  }}
*{{cite journal  | author=Mutoh H, Bito H, Minami M, ''et al.'' |title=Two different promoters direct expression of two distinct forms of mRNAs of human platelet-activating factor receptor. |journal=FEBS Lett. |volume=322 |issue= 2 |pages= 129-34 |year= 1993 |pmid= 8387031 |doi=  }}
*{{cite journal  | author=Nakamura M, Honda Z, Matsumoto T, ''et al.'' |title=Isolation and properties of platelet-activating factor receptor cDNAs. |journal=Journal of lipid mediators |volume=6 |issue= 1-3 |pages= 163-8 |year= 1993 |pmid= 8395240 |doi=  }}
*{{cite journal  | author=Kishimoto S, Shimadzu W, Izumi T, ''et al.'' |title=Regulation by IL-5 of expression of functional platelet-activating factor receptors on human eosinophils. |journal=J. Immunol. |volume=157 |issue= 9 |pages= 4126-32 |year= 1996 |pmid= 8892648 |doi=  }}
*{{cite journal  | author=Chase PB, Yang JM, Thompson FH, ''et al.'' |title=Regional mapping of the human platelet-activating factor receptor gene (PTAFR) to 1p35-->p34.3 by fluorescence in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=72 |issue= 2-3 |pages= 205-7 |year= 1997 |pmid= 8978777 |doi=  }}
*{{cite journal  | author=Le Gouill C, Parent JL, Rola-Pleszczynski M, Stanková J |title=Role of the Cys90, Cys95 and Cys173 residues in the structure and function of the human platelet-activating factor receptor. |journal=FEBS Lett. |volume=402 |issue= 2-3 |pages= 203-8 |year= 1997 |pmid= 9037196 |doi=  }}
*{{cite journal  | author=Ahmed A, Dearn S, Shams M, ''et al.'' |title=Localization, quantification, and activation of platelet-activating factor receptor in human endometrium during the menstrual cycle: PAF stimulates NO, VEGF, and FAKpp125. |journal=FASEB J. |volume=12 |issue= 10 |pages= 831-43 |year= 1998 |pmid= 9657523 |doi=  }}
*{{cite journal  | author=Cargill M, Altshuler D, Ireland J, ''et al.'' |title=Characterization of single-nucleotide polymorphisms in coding regions of human genes. |journal=Nat. Genet. |volume=22 |issue= 3 |pages= 231-8 |year= 1999 |pmid= 10391209 |doi= 10.1038/10290 }}
}}
{{refend}}

{{protein-stub}}
 

RHCE

• INFO: Beginning work on RHCE... {November 18, 2007 10:19:04 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:21:03 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Rh blood group, CcEe antigens
 | HGNCid = 10008
 | Symbol = RHCE
 | AltSymbols =; RHC; CD240CE; MGC103977; RH; RH30A; RHE; RHIXB; RHPI; Rh4; RhIVb(J); RhVI; RhVIII; CD240D; DIIIc; RH30; RHCED; RHDVA(TT); RHDel; RHPII; RHXIII; RhDCw; RhII; RhK562-II; RhPI
 | OMIM = 111700
 | ECnumber =  
 | Homologene = 7918
 | MGIid = 1202882
 | GeneAtlas_image1 = PBB_GE_RHCE_215819_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_RHCE_216317_x_at_tn.png
 | GeneAtlas_image3 = PBB_GE_RHCE_210429_at_tn.png
 | Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0003674 |text = molecular_function}} 
 | 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:0006810 |text = transport}} {{GNF_GO|id=GO:0008150 |text = biological_process}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6006
    | Hs_Ensembl = ENSG00000188672
    | Hs_RefseqProtein = XP_001130486
    | Hs_RefseqmRNA = XM_001130486
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 25561328
    | Hs_GenLoc_end = 25629270
    | Hs_Uniprot = P18577
    | Mm_EntrezGene = 19746
    | Mm_Ensembl = ENSMUSG00000028825
    | Mm_RefseqmRNA = NM_011270
    | Mm_RefseqProtein = NP_035400
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 134136660
    | Mm_GenLoc_end = 134168248
    | Mm_Uniprot =  
  }}
}}
'''Rh blood group, CcEe antigens''', also known as '''RHCE''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RHCE Rh blood group, CcEe antigens| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6006| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = The Rh blood group system is the second most clinically significant of the blood groups, second only to ABO. It is also the most polymorphic of the blood groups, with variations due to deletions, gene conversions, and missense mutations. The Rh blood group includes this gene which encodes both the RhC and RhE antigens on a single polypeptide and a second gene which encodes the RhD protein. The classification of Rh-positive and Rh-negative individuals is determined by the presence or absence of the highly immunogenic RhD protein on the surface of erythrocytes. Alternative splicing of this gene results in four transcript variants encoding four different isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: RHCE Rh blood group, CcEe antigens| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6006| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Agre P, Cartron JP |title=Molecular biology of the Rh antigens. |journal=Blood |volume=78 |issue= 3 |pages= 551-63 |year= 1991 |pmid= 1907207 |doi=  }}
*{{cite journal  | author=Avent ND, Reid ME |title=The Rh blood group system: a review. |journal=Blood |volume=95 |issue= 2 |pages= 375-87 |year= 2000 |pmid= 10627438 |doi=  }}
*{{cite journal  | author=Flegel WA, Wagner FF |title=Molecular genetics of RH. |journal=Vox Sang. |volume=78 Suppl 2 |issue=  |pages= 109-15 |year= 2000 |pmid= 10938938 |doi=  }}
*{{cite journal  | author=Wagner FF, Flegel WA |title=Review: the molecular basis of the Rh blood group phenotypes. |journal=Immunohematology / American Red Cross |volume=20 |issue= 1 |pages= 23-36 |year= 2004 |pmid= 15373666 |doi=  }}
*{{cite journal  | author=Callebaut I, Dulin F, Bertrand O, ''et al.'' |title=Hydrophobic cluster analysis and modeling of the human Rh protein three-dimensional structures. |journal=Transfusion clinique et biologique : journal de la Société française de transfusion sanguine |volume=13 |issue= 1-2 |pages= 70-84 |year= 2006 |pmid= 16584906 |doi= 10.1016/j.tracli.2006.02.001 }}
*{{cite journal  | author=Le Van Kim C, Chérif-Zahar B, Raynal V, ''et al.'' |title=Multiple Rh messenger RNA isoforms are produced by alternative splicing. |journal=Blood |volume=80 |issue= 4 |pages= 1074-8 |year= 1992 |pmid= 1379850 |doi=  }}
*{{cite journal  | author=Le van Kim C, Mouro I, Chérif-Zahar B, ''et al.'' |title=Molecular cloning and primary structure of the human blood group RhD polypeptide. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 22 |pages= 10925-9 |year= 1992 |pmid= 1438298 |doi=  }}
*{{cite journal  | author=Chérif-Zahar B, Bloy C, Le Van Kim C, ''et al.'' |title=Molecular cloning and protein structure of a human blood group Rh polypeptide. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 16 |pages= 6243-7 |year= 1990 |pmid= 1696722 |doi=  }}
*{{cite journal  | author=Suyama K, Goldstein J, Aebersold R, Kent S |title=Regarding the size of Rh proteins. |journal=Blood |volume=77 |issue= 2 |pages= 411 |year= 1991 |pmid= 1898705 |doi=  }}
*{{cite journal  | author=Chérif-Zahar B, Mattéi MG, Le Van Kim C, ''et al.'' |title=Localization of the human Rh blood group gene structure to chromosome region 1p34.3-1p36.1 by in situ hybridization. |journal=Hum. Genet. |volume=86 |issue= 4 |pages= 398-400 |year= 1991 |pmid= 1900257 |doi=  }}
*{{cite journal  | author=Sawamura D, Li KH, Nomura K, ''et al.'' |title=Bullous pemphigoid antigen: cDNA cloning, cellular expression, and evidence for polymorphism of the human gene. |journal=J. Invest. Dermatol. |volume=96 |issue= 6 |pages= 908-15 |year= 1991 |pmid= 2045679 |doi=  }}
*{{cite journal  | author=Avent ND, Ridgwell K, Tanner MJ, Anstee DJ |title=cDNA cloning of a 30 kDa erythrocyte membrane protein associated with Rh (Rhesus)-blood-group-antigen expression. |journal=Biochem. J. |volume=271 |issue= 3 |pages= 821-5 |year= 1990 |pmid= 2123099 |doi=  }}
*{{cite journal  | author=Bloy C, Blanchard D, Dahr W, ''et al.'' |title=Determination of the N-terminal sequence of human red cell Rh(D) polypeptide and demonstration that the Rh(D), (c), and (E) antigens are carried by distinct polypeptide chains. |journal=Blood |volume=72 |issue= 2 |pages= 661-6 |year= 1988 |pmid= 3135863 |doi=  }}
*{{cite journal  | author=Avent ND, Ridgwell K, Mawby WJ, ''et al.'' |title=Protein-sequence studies on Rh-related polypeptides suggest the presence of at least two groups of proteins which associate in the human red-cell membrane. |journal=Biochem. J. |volume=256 |issue= 3 |pages= 1043-6 |year= 1989 |pmid= 3146980 |doi=  }}
*{{cite journal  | author=Kajii E, Umenishi F, Iwamoto S, Ikemoto S |title=Isolation of a new cDNA clone encoding an Rh polypeptide associated with the Rh blood group system. |journal=Hum. Genet. |volume=91 |issue= 2 |pages= 157-62 |year= 1993 |pmid= 7916743 |doi=  }}
*{{cite journal  | author=Chérif-Zahar B, Le Van Kim C, Rouillac C, ''et al.'' |title=Organization of the gene (RHCE) encoding the human blood group RhCcEe antigens and characterization of the promoter region. |journal=Genomics |volume=19 |issue= 1 |pages= 68-74 |year= 1994 |pmid= 8188244 |doi= 10.1006/geno.1994.1014 }}
*{{cite journal  | author=Mouro I, Colin Y, Chérif-Zahar B, ''et al.'' |title=Molecular genetic basis of the human Rhesus blood group system. |journal=Nat. Genet. |volume=5 |issue= 1 |pages= 62-5 |year= 1993 |pmid= 8220426 |doi= 10.1038/ng0993-62 }}
*{{cite journal  | author=Huang CH, Chen Y, Reid M, Ghosh S |title=Genetic recombination at the human RH locus: a family study of the red-cell Evans phenotype reveals a transfer of exons 2-6 from the RHD to the RHCE gene. |journal=Am. J. Hum. Genet. |volume=59 |issue= 4 |pages= 825-33 |year= 1996 |pmid= 8808597 |doi=  }}
*{{cite journal  | author=Huang CH |title=Alteration of RH gene structure and expression in human dCCee and DCW-red blood cells: phenotypic homozygosity versus genotypic heterozygosity. |journal=Blood |volume=88 |issue= 6 |pages= 2326-33 |year= 1996 |pmid= 8822955 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

RPSA

• INFO: Beginning work on RPSA... {November 18, 2007 10:10:14 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:10:54 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Ribosomal protein SA
 | HGNCid = 6502
 | Symbol = RPSA
 | AltSymbols =; 37LRP; 67LR; LAMBR; LAMR1; LRP; p40
 | OMIM = 150370
 | ECnumber =  
 | Homologene = 68249
 | MGIid = 105381
 | Function = {{GNF_GO|id=GO:0003735 |text = structural constituent of ribosome}} {{GNF_GO|id=GO:0005055 |text = laminin receptor activity}} 
 | Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005843 |text = cytosolic small ribosomal subunit (sensu Eukaryota)}} {{GNF_GO|id=GO:0008305 |text = integrin complex}} {{GNF_GO|id=GO:0015935 |text = small ribosomal subunit}} 
 | Process = {{GNF_GO|id=GO:0006412 |text = translation}} {{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 = 3921
    | Hs_Ensembl =  
    | Hs_RefseqProtein = NP_001012321
    | Hs_RefseqmRNA = NM_001012321
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr =  
    | Hs_GenLoc_start =  
    | Hs_GenLoc_end =  
    | Hs_Uniprot =  
    | Mm_EntrezGene = 16785
    | Mm_Ensembl =  
    | Mm_RefseqmRNA = NM_011029
    | Mm_RefseqProtein = NP_035159
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr =  
    | Mm_GenLoc_start =  
    | Mm_GenLoc_end =  
    | Mm_Uniprot =  
  }}
}}
'''Ribosomal protein SA''', also known as '''RPSA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RPSA ribosomal protein SA| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3921| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Many of the effects of laminin are mediated through interactions with cell surface receptors. These receptors include members of the integrin family, as well as non-integrin laminin-binding proteins. This gene encodes a high-affinity, non-integrin family, laminin receptor 1. This receptor has been variously called 67 kD laminin receptor, 37 kD laminin receptor precursor (37LRP) and p40 ribosome-associated protein. The amino acid sequence of laminin receptor 1 is highly conserved through evolution, suggesting a key biological function. It has been observed that the level of the laminin receptor transcript is higher in colon carcinoma tissue and lung cancer cell line than their normal counterparts. Also, there is a correlation between the upregulation of this polypeptide in cancer cells and their invasive and metastatic phenotype. Multiple copies of this gene exist, however, most of them are pseudogenes thought to have arisen from retropositional events. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: RPSA ribosomal protein SA| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3921| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Belkin AM, Stepp MA |title=Integrins as receptors for laminins. |journal=Microsc. Res. Tech. |volume=51 |issue= 3 |pages= 280-301 |year= 2000 |pmid= 11054877 |doi= 10.1002/1097-0029(20001101)51:3<280::AID-JEMT7>3.0.CO;2-O }}
*{{cite journal  | author=Satoh K, Narumi K, Sakai T, ''et al.'' |title=Cloning of 67-kDa laminin receptor cDNA and gene expression in normal and malignant cell lines of the human lung. |journal=Cancer Lett. |volume=62 |issue= 3 |pages= 199-203 |year= 1992 |pmid= 1534510 |doi=  }}
*{{cite journal  | author=Wewer UM, Liotta LA, Jaye M, ''et al.'' |title=Altered levels of laminin receptor mRNA in various human carcinoma cells that have different abilities to bind laminin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 19 |pages= 7137-41 |year= 1986 |pmid= 2429301 |doi=  }}
*{{cite journal  | author=Van den Ouweland AM, Van Duijnhoven HL, Deichmann KA, ''et al.'' |title=Characteristics of a multicopy gene family predominantly consisting of processed pseudogenes. |journal=Nucleic Acids Res. |volume=17 |issue= 10 |pages= 3829-43 |year= 1989 |pmid= 2543954 |doi=  }}
*{{cite journal  | author=Yow HK, Wong JM, Chen HS, ''et al.'' |title=Increased mRNA expression of a laminin-binding protein in human colon carcinoma: complete sequence of a full-length cDNA encoding the protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 17 |pages= 6394-8 |year= 1988 |pmid= 2970639 |doi=  }}
*{{cite journal  | author=Gehlsen KR, Dillner L, Engvall E, Ruoslahti E |title=The human laminin receptor is a member of the integrin family of cell adhesion receptors. |journal=Science |volume=241 |issue= 4870 |pages= 1228-9 |year= 1988 |pmid= 2970671 |doi=  }}
*{{cite journal  | author=Selvamurugan N, Eliceiri GL |title=The gene for human E2 small nucleolar RNA resides in an intron of a laminin-binding protein gene. |journal=Genomics |volume=30 |issue= 2 |pages= 400-1 |year= 1996 |pmid= 8586453 |doi=  }}
*{{cite journal  | author=Vladimirov SN, Ivanov AV, Karpova GG, ''et al.'' |title=Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry. |journal=Eur. J. Biochem. |volume=239 |issue= 1 |pages= 144-9 |year= 1996 |pmid= 8706699 |doi=  }}
*{{cite journal  | author=Jackers P, Minoletti F, Belotti D, ''et al.'' |title=Isolation from a multigene family of the active human gene of the metastasis-associated multifunctional protein 37LRP/p40 at chromosome 3p21.3. |journal=Oncogene |volume=13 |issue= 3 |pages= 495-503 |year= 1996 |pmid= 8760291 |doi=  }}
*{{cite journal  | author=Clausse N, Jackers P, Jarès P, ''et al.'' |title=Identification of the active gene coding for the metastasis-associated 37LRP/p40 multifunctional protein. |journal=DNA Cell Biol. |volume=15 |issue= 12 |pages= 1009-23 |year= 1997 |pmid= 8985115 |doi=  }}
*{{cite journal  | author=Daidone MG, Silvestrini R, Benini E, ''et al.'' |title=Expression of high-affinity 67-kDa laminin receptors in primary breast cancers and metachronous metastatic lesions or contralateral cancers. |journal=Br. J. Cancer |volume=76 |issue= 1 |pages= 52-3 |year= 1997 |pmid= 9218732 |doi=  }}
*{{cite journal  | author=Kenmochi N, Kawaguchi T, Rozen S, ''et al.'' |title=A map of 75 human ribosomal protein genes. |journal=Genome Res. |volume=8 |issue= 5 |pages= 509-23 |year= 1998 |pmid= 9582194 |doi=  }}
*{{cite journal  | author=de Manzoni G, Guglielmi A, Verlato G, ''et al.'' |title=Prognostic significance of 67-kDa laminin receptor expression in advanced gastric cancer. |journal=Oncology |volume=55 |issue= 5 |pages= 456-60 |year= 1998 |pmid= 9732225 |doi=  }}
*{{cite journal  | author=Sato M, Saeki Y, Tanaka K, Kaneda Y |title=Ribosome-associated protein LBP/p40 binds to S21 protein of 40S ribosome: analysis using a yeast two-hybrid system. |journal=Biochem. Biophys. Res. Commun. |volume=256 |issue= 2 |pages= 385-90 |year= 1999 |pmid= 10079194 |doi= 10.1006/bbrc.1999.0343 }}
*{{cite journal  | author=Canfield SM, Khakoo AY |title=The nonintegrin laminin binding protein (p67 LBP) is expressed on a subset of activated human T lymphocytes and, together with the integrin very late activation antigen-6, mediates avid cellular adherence to laminin. |journal=J. Immunol. |volume=163 |issue= 6 |pages= 3430-40 |year= 1999 |pmid= 10477615 |doi=  }}
*{{cite journal  | author=Donaldson EA, McKenna DJ, McMullen CB, ''et al.'' |title=The expression of membrane-associated 67-kDa laminin receptor (67LR) is modulated in vitro by cell-contact inhibition. |journal=Mol. Cell Biol. Res. Commun. |volume=3 |issue= 1 |pages= 53-9 |year= 2000 |pmid= 10683318 |doi= 10.1006/mcbr.2000.0191 }}
*{{cite journal  | author=Pedraza C, Geberhiwot T, Ingerpuu S, ''et al.'' |title=Monocytic cells synthesize, adhere to, and migrate on laminin-8 (alpha 4 beta 1 gamma 1). |journal=J. Immunol. |volume=165 |issue= 10 |pages= 5831-8 |year= 2000 |pmid= 11067943 |doi=  }}
*{{cite journal  | author=Vande Broek I, Vanderkerken K, De Greef C, ''et al.'' |title=Laminin-1-induced migration of multiple myeloma cells involves the high-affinity 67 kD laminin receptor. |journal=Br. J. Cancer |volume=85 |issue= 9 |pages= 1387-95 |year= 2001 |pmid= 11720479 |doi= 10.1054/bjoc.2001.2078 }}
*{{cite journal  | author=Waltregny D, de Leval L, Coppens L, ''et al.'' |title=Detection of the 67-kD laminin receptor in prostate cancer biopsies as a predictor of recurrence after radical prostatectomy. |journal=Eur. Urol. |volume=40 |issue= 5 |pages= 495-503 |year= 2002 |pmid= 11752855 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

S100A7

• INFO: Beginning work on S100A7... {November 18, 2007 10:21:03 AM PST}
• SEARCH REDIRECT: Control Box Found: S100A7 {November 18, 2007 10:21:29 AM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:21:30 AM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:21:30 AM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:21:30 AM PST}
• UPDATED: Updated protein page: S100A7 {November 18, 2007 10:21:40 AM PST}

SFPQ

• INFO: Beginning work on SFPQ... {November 18, 2007 10:22:21 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:23:06 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Splicing factor proline/glutamine-rich (polypyrimidine tract binding protein associated)
 | HGNCid = 10774
 | Symbol = SFPQ
 | AltSymbols =; PSF; POMP100
 | OMIM = 605199
 | ECnumber =  
 | Homologene = 3714
 | MGIid = 1918764
 | GeneAtlas_image1 = PBB_GE_SFPQ_201586_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_SFPQ_201585_s_at_tn.png
 | GeneAtlas_image3 = PBB_GE_SFPQ_214016_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} 
 | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} 
 | Process = {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006310 |text = DNA recombination}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006397 |text = mRNA processing}} {{GNF_GO|id=GO:0008380 |text = RNA splicing}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6421
    | Hs_Ensembl = ENSG00000116560
    | Hs_RefseqProtein = NP_005057
    | Hs_RefseqmRNA = NM_005066
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 35414571
    | Hs_GenLoc_end = 35431336
    | Hs_Uniprot = P23246
    | Mm_EntrezGene = 71514
    | Mm_Ensembl = ENSMUSG00000028820
    | Mm_RefseqmRNA = XM_981759
    | Mm_RefseqProtein = XP_986853
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 126523639
    | Mm_GenLoc_end = 126533100
    | Mm_Uniprot = Q3TZL2
  }}
}}
'''Splicing factor proline/glutamine-rich (polypyrimidine tract binding protein associated)''', also known as '''SFPQ''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SFPQ splicing factor proline/glutamine-rich (polypyrimidine tract binding protein associated)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6421| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = 
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Shav-Tal Y, Zipori D |title=PSF and p54(nrb)/NonO--multi-functional nuclear proteins. |journal=FEBS Lett. |volume=531 |issue= 2 |pages= 109-14 |year= 2002 |pmid= 12417296 |doi=  }}
*{{cite journal  | author=Gower HJ, Moore SE, Dickson G, ''et al.'' |title=Cloning and characterization of a myoblast cell surface antigen defined by 24.1D5 monoclonal antibody. |journal=Development |volume=105 |issue= 4 |pages= 723-31 |year= 1990 |pmid= 2480877 |doi=  }}
*{{cite journal  | author=Gozani O, Patton JG, Reed R |title=A novel set of spliceosome-associated proteins and the essential splicing factor PSF bind stably to pre-mRNA prior to catalytic step II of the splicing reaction. |journal=EMBO J. |volume=13 |issue= 14 |pages= 3356-67 |year= 1994 |pmid= 8045264 |doi=  }}
*{{cite journal  | author=Zhang WW, Zhang LX, Busch RK, ''et al.'' |title=Purification and characterization of a DNA-binding heterodimer of 52 and 100 kDa from HeLa cells. |journal=Biochem. J. |volume=290 ( Pt 1) |issue=  |pages= 267-72 |year= 1993 |pmid= 8439294 |doi=  }}
*{{cite journal  | author=Patton JG, Porro EB, Galceran J, ''et al.'' |title=Cloning and characterization of PSF, a novel pre-mRNA splicing factor. |journal=Genes Dev. |volume=7 |issue= 3 |pages= 393-406 |year= 1993 |pmid= 8449401 |doi=  }}
*{{cite journal  | author=Clark J, Lu YJ, Sidhar SK, ''et al.'' |title=Fusion of splicing factor genes PSF and NonO (p54nrb) to the TFE3 gene in papillary renal cell carcinoma. |journal=Oncogene |volume=15 |issue= 18 |pages= 2233-9 |year= 1997 |pmid= 9393982 |doi= 10.1038/sj.onc.1201394 }}
*{{cite journal  | author=Teigelkamp S, Mundt C, Achsel T, ''et al.'' |title=The human U5 snRNP-specific 100-kD protein is an RS domain-containing, putative RNA helicase with significant homology to the yeast splicing factor Prp28p. |journal=RNA |volume=3 |issue= 11 |pages= 1313-26 |year= 1998 |pmid= 9409622 |doi=  }}
*{{cite journal  | author=Straub T, Grue P, Uhse A, ''et al.'' |title=The RNA-splicing factor PSF/p54 controls DNA-topoisomerase I activity by a direct interaction. |journal=J. Biol. Chem. |volume=273 |issue= 41 |pages= 26261-4 |year= 1998 |pmid= 9756848 |doi=  }}
*{{cite journal  | author=Lutz CS, Cooke C, O'Connor JP, ''et al.'' |title=The snRNP-free U1A (SF-A) complex(es): identification of the largest subunit as PSF, the polypyrimidine-tract binding protein-associated splicing factor. |journal=RNA |volume=4 |issue= 12 |pages= 1493-9 |year= 1998 |pmid= 9848648 |doi=  }}
*{{cite journal  | author=Meissner M, Dechat T, Gerner C, ''et al.'' |title=Differential nuclear localization and nuclear matrix association of the splicing factors PSF and PTB. |journal=J. Cell. Biochem. |volume=76 |issue= 4 |pages= 559-66 |year= 2000 |pmid= 10653975 |doi=  }}
*{{cite journal  | author=Urban RJ, Bodenburg Y, Kurosky A, ''et al.'' |title=Polypyrimidine tract-binding protein-associated splicing factor is a negative regulator of transcriptional activity of the porcine p450scc insulin-like growth factor response element. |journal=Mol. Endocrinol. |volume=14 |issue= 6 |pages= 774-82 |year= 2000 |pmid= 10847580 |doi=  }}
*{{cite journal  | author=Straub T, Knudsen BR, Boege F |title=PSF/p54(nrb) stimulates "jumping" of DNA topoisomerase I between separate DNA helices. |journal=Biochemistry |volume=39 |issue= 25 |pages= 7552-8 |year= 2000 |pmid= 10858305 |doi=  }}
*{{cite journal  | author=Akhmedov AT, Lopez BS |title=Human 100-kDa homologous DNA-pairing protein is the splicing factor PSF and promotes DNA strand invasion. |journal=Nucleic Acids Res. |volume=28 |issue= 16 |pages= 3022-30 |year= 2000 |pmid= 10931916 |doi=  }}
*{{cite journal  | author=de Vries H, Rüegsegger U, Hübner W, ''et al.'' |title=Human pre-mRNA cleavage factor II(m) contains homologs of yeast proteins and bridges two other cleavage factors. |journal=EMBO J. |volume=19 |issue= 21 |pages= 5895-904 |year= 2000 |pmid= 11060040 |doi= 10.1093/emboj/19.21.5895 }}
*{{cite journal  | author=Dye BT, Patton JG |title=An RNA recognition motif (RRM) is required for the localization of PTB-associated splicing factor (PSF) to subnuclear speckles. |journal=Exp. Cell Res. |volume=263 |issue= 1 |pages= 131-44 |year= 2001 |pmid= 11161712 |doi= 10.1006/excr.2000.5097 }}
*{{cite journal  | author=Mathur M, Tucker PW, Samuels HH |title=PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors. |journal=Mol. Cell. Biol. |volume=21 |issue= 7 |pages= 2298-311 |year= 2001 |pmid= 11259580 |doi= 10.1128/MCB.21.7.2298-2311.2001 }}
*{{cite journal  | author=Shav-Tal Y, Cohen M, Lapter S, ''et al.'' |title=Nuclear relocalization of the pre-mRNA splicing factor PSF during apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and changes in protein interactions. |journal=Mol. Biol. Cell |volume=12 |issue= 8 |pages= 2328-40 |year= 2002 |pmid= 11514619 |doi=  }}
*{{cite journal  | author=Zhang Z, Carmichael GG |title=The fate of dsRNA in the nucleus: a p54(nrb)-containing complex mediates the nuclear retention of promiscuously A-to-I edited RNAs. |journal=Cell |volume=106 |issue= 4 |pages= 465-75 |year= 2001 |pmid= 11525732 |doi=  }}
*{{cite journal  | author=Andersen JS, Lyon CE, Fox AH, ''et al.'' |title=Directed proteomic analysis of the human nucleolus. |journal=Curr. Biol. |volume=12 |issue= 1 |pages= 1-11 |year= 2002 |pmid= 11790298 |doi=  }}
*{{cite journal  | author=Sewer MB, Nguyen VQ, Huang CJ, ''et al.'' |title=Transcriptional activation of human CYP17 in H295R adrenocortical cells depends on complex formation among p54(nrb)/NonO, protein-associated splicing factor, and SF-1, a complex that also participates in repression of transcription. |journal=Endocrinology |volume=143 |issue= 4 |pages= 1280-90 |year= 2002 |pmid= 11897684 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

STS

• INFO: Beginning work on STS... {November 17, 2007 11:44:30 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 11:45:37 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_STS_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1p49.
 | PDB = {{PDB2|1p49}}
 | Name = Steroid sulfatase (microsomal), arylsulfatase C, isozyme S
 | HGNCid = 11425
 | Symbol = STS
 | AltSymbols =; ARSC; ARSC1; ASC; ES; SSDD
 | OMIM = 308100
 | ECnumber =  
 | Homologene = 47918
 | MGIid =  
 | GeneAtlas_image1 = PBB_GE_STS_203767_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_STS_203768_s_at_tn.png
 | GeneAtlas_image3 = PBB_GE_STS_203769_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0004773 |text = steryl-sulfatase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} 
 | Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0005768 |text = endosome}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} 
 | Process = {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006706 |text = steroid catabolic process}} {{GNF_GO|id=GO:0007565 |text = female pregnancy}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0008544 |text = epidermis development}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 412
    | Hs_Ensembl = ENSG00000101846
    | Hs_RefseqProtein = NP_000342
    | Hs_RefseqmRNA = NM_000351
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = X
    | Hs_GenLoc_start = 7147497
    | Hs_GenLoc_end = 7282851
    | Hs_Uniprot = P08842
    | Mm_EntrezGene =  
    | Mm_Ensembl =  
    | Mm_RefseqmRNA =  
    | Mm_RefseqProtein =  
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr =  
    | Mm_GenLoc_start =  
    | Mm_GenLoc_end =  
    | Mm_Uniprot =  
  }}
}}
'''Steroid sulfatase (microsomal), arylsulfatase C, isozyme S''', also known as '''STS''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: STS steroid sulfatase (microsomal), arylsulfatase C, isozyme S| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=412| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = The protein encoded by this gene catalyzes the conversion of sulfated steroid precursors to estrogens during pregnancy. The encoded protein is found in the endoplasmic reticulum, where it acts as a homodimer. Mutations in this gene are known to cause X-linked ichthyosis (XLI).<ref name="entrez">{{cite web | title = Entrez Gene: STS steroid sulfatase (microsomal), arylsulfatase C, isozyme S| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=412| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Elias PM, Crumrine D, Rassner U, ''et al.'' |title=Basis for abnormal desquamation and permeability barrier dysfunction in RXLI. |journal=J. Invest. Dermatol. |volume=122 |issue= 2 |pages= 314-9 |year= 2004 |pmid= 15009711 |doi= 10.1046/j.1523-1747.2003.22258.x }}
*{{cite journal  | author=Basler E, Grompe M, Parenti G, ''et al.'' |title=Identification of point mutations in the steroid sulfatase gene of three patients with X-linked ichthyosis. |journal=Am. J. Hum. Genet. |volume=50 |issue= 3 |pages= 483-91 |year= 1992 |pmid= 1539590 |doi=  }}
*{{cite journal  | author=Shankaran R, Ameen M, Daniel WL, ''et al.'' |title=Characterization of arylsulfatase C isozymes from human liver and placenta. |journal=Biochim. Biophys. Acta |volume=1078 |issue= 2 |pages= 251-7 |year= 1991 |pmid= 2065092 |doi=  }}
*{{cite journal  | author=Stein C, Hille A, Seidel J, ''et al.'' |title=Cloning and expression of human steroid-sulfatase. Membrane topology, glycosylation, and subcellular distribution in BHK-21 cells. |journal=J. Biol. Chem. |volume=264 |issue= 23 |pages= 13865-72 |year= 1989 |pmid= 2668275 |doi=  }}
*{{cite journal  | author=Kawano J, Kotani T, Ohtaki S, ''et al.'' |title=Characterization of rat and human steroid sulfatases. |journal=Biochim. Biophys. Acta |volume=997 |issue= 3 |pages= 199-205 |year= 1989 |pmid= 2765556 |doi=  }}
*{{cite journal  | author=Yen PH, Allen E, Marsh B, ''et al.'' |title=Cloning and expression of steroid sulfatase cDNA and the frequent occurrence of deletions in STS deficiency: implications for X-Y interchange. |journal=Cell |volume=49 |issue= 4 |pages= 443-54 |year= 1987 |pmid= 3032454 |doi=  }}
*{{cite journal  | author=Conary JT, Lorkowski G, Schmidt B, ''et al.'' |title=Genetic heterogeneity of steroid sulfatase deficiency revealed with cDNA for human steroid sulfatase. |journal=Biochem. Biophys. Res. Commun. |volume=144 |issue= 2 |pages= 1010-7 |year= 1987 |pmid= 3034252 |doi=  }}
*{{cite journal  | author=Ballabio A, Parenti G, Carrozzo R, ''et al.'' |title=X/Y translocation in a family with X-linked ichthyosis, chondrodysplasia punctata, and mental retardation: DNA analysis reveals deletion of the steroid sulphatase gene and translocation of its Y pseudogene. |journal=Clin. Genet. |volume=34 |issue= 1 |pages= 31-7 |year= 1988 |pmid= 3165728 |doi=  }}
*{{cite journal  | author=Yen PH, Marsh B, Allen E, ''et al.'' |title=The human X-linked steroid sulfatase gene and a Y-encoded pseudogene: evidence for an inversion of the Y chromosome during primate evolution. |journal=Cell |volume=55 |issue= 6 |pages= 1123-35 |year= 1989 |pmid= 3203382 |doi=  }}
*{{cite journal  | author=Chang PL, Varey PA, Rosa NE, ''et al.'' |title=Association of steroid sulfatase with one of the arylsulfatase C isozymes in human fibroblasts. |journal=J. Biol. Chem. |volume=261 |issue= 31 |pages= 14443-7 |year= 1986 |pmid= 3464600 |doi=  }}
*{{cite journal  | author=Munroe DG, Chang PL |title=Tissue-specific expression of human arylsulfatase-C isozymes and steroid sulfatase. |journal=Am. J. Hum. Genet. |volume=40 |issue= 2 |pages= 102-14 |year= 1987 |pmid= 3471087 |doi=  }}
*{{cite journal  | author=Müller CR, Wahlström J, Ropers HH |title=Further evidence for the assignment of the steroid sulfatase X-linked ichthyosis locus to the telomer of Xp. |journal=Hum. Genet. |volume=58 |issue= 4 |pages= 446 |year= 1982 |pmid= 6948769 |doi=  }}
*{{cite journal  | author=Migeon BR, Shapiro LJ, Norum RA, ''et al.'' |title=Differential expression of steroid sulphatase locus on active and inactive human X chromosome. |journal=Nature |volume=299 |issue= 5886 |pages= 838-40 |year= 1982 |pmid= 6957717 |doi=  }}
*{{cite journal  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi=  }}
*{{cite journal  | author=Alperin ES, Shapiro LJ |title=Characterization of point mutations in patients with X-linked ichthyosis. Effects on the structure and function of the steroid sulfatase protein. |journal=J. Biol. Chem. |volume=272 |issue= 33 |pages= 20756-63 |year= 1997 |pmid= 9252398 |doi=  }}
*{{cite journal  | author=Sugawara T, Shimizu H, Hoshi N, ''et al.'' |title=PCR diagnosis of X-linked ichthyosis: identification of a novel mutation (E560P) of the steroid sulfatase gene. |journal=Hum. Mutat. |volume=15 |issue= 3 |pages= 296 |year= 2000 |pmid= 10679952 |doi= 10.1002/(SICI)1098-1004(200003)15:3<296::AID-HUMU17>3.0.CO;2-# }}
*{{cite journal  | author=Oyama N, Satoh M, Iwatsuki K, Kaneko F |title=Novel point mutations in the steroid sulfatase gene in patients with X-linked ichthyosis: transfection analysis using the mutated genes. |journal=J. Invest. Dermatol. |volume=114 |issue= 6 |pages= 1195-9 |year= 2000 |pmid= 10844566 |doi= 10.1046/j.1523-1747.2000.00004.x }}
*{{cite journal  | author=Jimenez Vaca AL, Valdes-Flores Mdel R, Rivera-Vega MR, ''et al.'' |title=Deletion pattern of the STS gene in X-linked ichthyosis in a Mexican population. |journal=Mol. Med. |volume=7 |issue= 12 |pages= 845-9 |year= 2002 |pmid= 11844872 |doi=  }}
*{{cite journal  | author=Hoffmann R, Rot A, Niiyama S, Billich A |title=Steroid sulfatase in the human hair follicle concentrates in the dermal papilla. |journal=J. Invest. Dermatol. |volume=117 |issue= 6 |pages= 1342-8 |year= 2002 |pmid= 11886493 |doi= 10.1046/j.0022-202x.2001.01547.x }}
*{{cite journal  | author=Matsuoka R, Yanaihara A, Saito H, ''et al.'' |title=Regulation of estrogen activity in human endometrium: effect of IL-1beta on steroid sulfatase activity in human endometrial stromal cells. |journal=Steroids |volume=67 |issue= 7 |pages= 655-9 |year= 2002 |pmid= 11996939 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

WWOX

• INFO: Beginning work on WWOX... {November 18, 2007 10:23:06 AM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:23:48 AM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_WWOX_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1wmv.
 | PDB = {{PDB2|1wmv}}
 | Name = WW domain containing oxidoreductase
 | HGNCid = 12799
 | Symbol = WWOX
 | AltSymbols =; FRA16D; D16S432E; FOR; HHCMA56; PRO0128; WOX1; WWOX v8
 | OMIM = 605131
 | ECnumber =  
 | Homologene = 56334
 | MGIid = 1931237
 | GeneAtlas_image1 = PBB_GE_WWOX_221147_x_at_tn.png
 | Function = {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0046983 |text = protein dimerization activity}} {{GNF_GO|id=GO:0050662 |text = coenzyme binding}} 
 | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} 
 | Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0008202 |text = steroid metabolic process}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 51741
    | Hs_Ensembl = ENSG00000186153
    | Hs_RefseqProtein = NP_057457
    | Hs_RefseqmRNA = NM_016373
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 76691177
    | Hs_GenLoc_end = 77803532
    | Hs_Uniprot =  
    | Mm_EntrezGene = 80707
    | Mm_Ensembl = ENSMUSG00000004637
    | Mm_RefseqmRNA = NM_019573
    | Mm_RefseqProtein = NP_062519
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 117325749
    | Mm_GenLoc_end = 118237803
    | Mm_Uniprot = Q91WL8
  }}
}}
'''WW domain containing oxidoreductase''', also known as '''WWOX''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: WWOX WW domain containing oxidoreductase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51741| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = WW domain-containing proteins are found in all eukaryotes and play an important role in the regulation of a wide variety of cellular functions such as protein degradation, transcription, and RNA splicing. This gene encodes a protein which contains 2 WW domains and a short-chain dehydrogenase/reductase domain (SRD). The highest normal expression of this gene is detected in hormonally regulated tissues such as testis, ovary, and prostate. This expression pattern and the presence of an SRD domain suggest a role for this gene in steroid metabolism. The encoded protein is more than 90% identical to the mouse protein, which is an essential mediator of tumor necrosis factor-alpha-induced apoptosis, suggesting a similar, important role in apoptosis for the human protein. In addition, there is evidence that this gene behaves as a suppressor of tumor growth. Alternative splicing of this gene generates transcript variants that encode different isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: WWOX WW domain containing oxidoreductase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51741| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Ramos D, Aldaz CM |title=WWOX, a chromosomal fragile site gene and its role in cancer. |journal=Adv. Exp. Med. Biol. |volume=587 |issue=  |pages= 149-59 |year= 2007 |pmid= 17163164 |doi=  }}
*{{cite journal  | author=Bednarek AK, Laflin KJ, Daniel RL, ''et al.'' |title=WWOX, a novel WW domain-containing protein mapping to human chromosome 16q23.3-24.1, a region frequently affected in breast cancer. |journal=Cancer Res. |volume=60 |issue= 8 |pages= 2140-5 |year= 2000 |pmid= 10786676 |doi=  }}
*{{cite journal  | author=Ried K, Finnis M, Hobson L, ''et al.'' |title=Common chromosomal fragile site FRA16D sequence: identification of the FOR gene spanning FRA16D and homozygous deletions and translocation breakpoints in cancer cells. |journal=Hum. Mol. Genet. |volume=9 |issue= 11 |pages= 1651-63 |year= 2000 |pmid= 10861292 |doi=  }}
*{{cite journal  | author=Chang NS, Pratt N, Heath J, ''et al.'' |title=Hyaluronidase induction of a WW domain-containing oxidoreductase that enhances tumor necrosis factor cytotoxicity. |journal=J. Biol. Chem. |volume=276 |issue= 5 |pages= 3361-70 |year= 2001 |pmid= 11058590 |doi= 10.1074/jbc.M007140200 }}
*{{cite journal  | author=Paige AJ, Taylor KJ, Taylor C, ''et al.'' |title=WWOX: a candidate tumor suppressor gene involved in multiple tumor types. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 20 |pages= 11417-22 |year= 2001 |pmid= 11572989 |doi= 10.1073/pnas.191175898 }}
*{{cite journal  | author=Bednarek AK, Keck-Waggoner CL, Daniel RL, ''et al.'' |title=WWOX, the FRA16D gene, behaves as a suppressor of tumor growth. |journal=Cancer Res. |volume=61 |issue= 22 |pages= 8068-73 |year= 2001 |pmid= 11719429 |doi=  }}
*{{cite journal  | author=Kuroki T, Trapasso F, Shiraishi T, ''et al.'' |title=Genetic alterations of the tumor suppressor gene WWOX in esophageal squamous cell carcinoma. |journal=Cancer Res. |volume=62 |issue= 8 |pages= 2258-60 |year= 2002 |pmid= 11956080 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Chang NS, Doherty J, Ensign A |title=JNK1 physically interacts with WW domain-containing oxidoreductase (WOX1) and inhibits WOX1-mediated apoptosis. |journal=J. Biol. Chem. |volume=278 |issue= 11 |pages= 9195-202 |year= 2003 |pmid= 12514174 |doi= 10.1074/jbc.M208373200 }}
*{{cite journal  | author=Ludes-Meyers JH, Bednarek AK, Popescu NC, ''et al.'' |title=WWOX, the common chromosomal fragile site, FRA16D, cancer gene. |journal=Cytogenet. Genome Res. |volume=100 |issue= 1-4 |pages= 101-10 |year= 2004 |pmid= 14526170 |doi= 10.1159/000072844 }}
*{{cite journal  | author=Watanabe A, Hippo Y, Taniguchi H, ''et al.'' |title=An opposing view on WWOX protein function as a tumor suppressor. |journal=Cancer Res. |volume=63 |issue= 24 |pages= 8629-33 |year= 2004 |pmid= 14695174 |doi=  }}
*{{cite journal  | author=Chen ST, Chuang JI, Wang JP, ''et al.'' |title=Expression of WW domain-containing oxidoreductase WOX1 in the developing murine nervous system. |journal=Neuroscience |volume=124 |issue= 4 |pages= 831-9 |year= 2004 |pmid= 15026124 |doi= 10.1016/j.neuroscience.2003.12.036 }}
*{{cite journal  | author=Ishii H, Mimori K, Vecchione A, ''et al.'' |title=Effect of exogenous E2F-1 on the expression of common chromosome fragile site genes, FHIT and WWOX. |journal=Biochem. Biophys. Res. Commun. |volume=316 |issue= 4 |pages= 1088-93 |year= 2004 |pmid= 15044096 |doi= 10.1016/j.bbrc.2004.02.159 }}
*{{cite journal  | author=Ludes-Meyers JH, Kil H, Bednarek AK, ''et al.'' |title=WWOX binds the specific proline-rich ligand PPXY: identification of candidate interacting proteins. |journal=Oncogene |volume=23 |issue= 29 |pages= 5049-55 |year= 2004 |pmid= 15064722 |doi= 10.1038/sj.onc.1207680 }}
*{{cite journal  | author=Aqeilan RI, Pekarsky Y, Herrero JJ, ''et al.'' |title=Functional association between Wwox tumor suppressor protein and p73, a p53 homolog. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 13 |pages= 4401-6 |year= 2004 |pmid= 15070730 |doi= 10.1073/pnas.0400805101 }}
*{{cite journal  | author=Kuroki T, Yendamuri S, Trapasso F, ''et al.'' |title=The tumor suppressor gene WWOX at FRA16D is involved in pancreatic carcinogenesis. |journal=Clin. Cancer Res. |volume=10 |issue= 7 |pages= 2459-65 |year= 2004 |pmid= 15073125 |doi=  }}
*{{cite journal  | author=Guler G, Uner A, Guler N, ''et al.'' |title=The fragile genes FHIT and WWOX are inactivated coordinately in invasive breast carcinoma. |journal=Cancer |volume=100 |issue= 8 |pages= 1605-14 |year= 2004 |pmid= 15073846 |doi= 10.1002/cncr.20137 }}
*{{cite journal  | author=Sze CI, Su M, Pugazhenthi S, ''et al.'' |title=Down-regulation of WW domain-containing oxidoreductase induces Tau phosphorylation in vitro. A potential role in Alzheimer's disease. |journal=J. Biol. Chem. |volume=279 |issue= 29 |pages= 30498-506 |year= 2004 |pmid= 15126504 |doi= 10.1074/jbc.M401399200 }}
*{{cite journal  | author=Aqeilan RI, Kuroki T, Pekarsky Y, ''et al.'' |title=Loss of WWOX expression in gastric carcinoma. |journal=Clin. Cancer Res. |volume=10 |issue= 9 |pages= 3053-8 |year= 2004 |pmid= 15131042 |doi=  }}
*{{cite journal  | author=Park SW, Ludes-Meyers J, Zimonjic DB, ''et al.'' |title=Frequent downregulation and loss of WWOX gene expression in human hepatocellular carcinoma. |journal=Br. J. Cancer |volume=91 |issue= 4 |pages= 753-9 |year= 2004 |pmid= 15266310 |doi= 10.1038/sj.bjc.6602023 }}
}}
{{refend}}

{{protein-stub}}
 

end log.