Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 07:52, 21 November 2007 (UTC)[edit]
Proteins without matches (21)[edit]
Proteins with a High Potential Match (4)[edit]
Manual Inspection (Parsing Error) (1)[edit]
Created (8)[edit]
Manual Inspection (Page not found) (16)[edit]
Protein Status Grid - Date: 07:52, 21 November 2007 (UTC)[edit]
Vebose Log - Date: 07:52, 21 November 2007 (UTC)[edit]
- INFO: Beginning work on ARHGAP1... {November 20, 2007 11:23:53 PM PST}
- UPLOAD: Added new Image to wiki: File:PBB Protein ARHGAP1 image.jpg {November 20, 2007 11:24:49 PM PST}
- CREATE: Found no pages, creating new page. {November 20, 2007 11:25:07 PM PST}
- CREATED: Created new protein page: ARHGAP1 {November 20, 2007 11:25:15 PM PST}
- INFO: Beginning work on BMP6... {November 20, 2007 11:25:15 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:25:57 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Bone morphogenetic protein 6
| HGNCid = 1073
| Symbol = BMP6
| AltSymbols =; VGR; VGR1
| OMIM = 112266
| ECnumber =
| Homologene = 1300
| MGIid = 88182
| GeneAtlas_image1 = PBB_GE_BMP6_206176_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0001649 |text = osteoblast differentiation}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0030509 |text = BMP signaling pathway}} {{GNF_GO|id=GO:0032349 |text = positive regulation of aldosterone biosynthetic process}} {{GNF_GO|id=GO:0040007 |text = growth}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0051216 |text = cartilage development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 654
| Hs_Ensembl = ENSG00000153162
| Hs_RefseqProtein = NP_001709
| Hs_RefseqmRNA = NM_001718
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 7672009
| Hs_GenLoc_end = 7826752
| Hs_Uniprot = P22004
| Mm_EntrezGene = 12161
| Mm_Ensembl = ENSMUSG00000039004
| Mm_RefseqmRNA = NM_007556
| Mm_RefseqProtein = NP_031582
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 38353399
| Mm_GenLoc_end = 38507780
| Mm_Uniprot = Q3UXB2
}}
}}
'''Bone morphogenetic protein 6''', also known as '''BMP6''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BMP6 bone morphogenetic protein 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=654| 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 bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.<ref name="entrez">{{cite web | title = Entrez Gene: BMP6 bone morphogenetic protein 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=654| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hahn GV, Cohen RB, Wozney JM, ''et al.'' |title=A bone morphogenetic protein subfamily: chromosomal localization of human genes for BMP5, BMP6, and BMP7. |journal=Genomics |volume=14 |issue= 3 |pages= 759-62 |year= 1992 |pmid= 1427904 |doi= }}
*{{cite journal | author=Sauermann U, Meyermann R, Schluesener HJ |title=Cloning of a novel TGF-beta related cytokine, the vgr, from rat brain: cloning of and comparison to homologous human cytokines. |journal=J. Neurosci. Res. |volume=33 |issue= 1 |pages= 142-7 |year= 1993 |pmid= 1453478 |doi= 10.1002/jnr.490330118 }}
*{{cite journal | author=Celeste AJ, Iannazzi JA, Taylor RC, ''et al.'' |title=Identification of transforming growth factor beta family members present in bone-inductive protein purified from bovine bone. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 24 |pages= 9843-7 |year= 1991 |pmid= 2263636 |doi= }}
*{{cite journal | author=Schluesener HJ, Meyermann R |title=Immunolocalization of BMP-6, a novel TGF-beta-related cytokine, in normal and atherosclerotic smooth muscle cells. |journal=Atherosclerosis |volume=113 |issue= 2 |pages= 153-6 |year= 1995 |pmid= 7605353 |doi= }}
*{{cite journal | author=Gitelman SE, Kobrin MS, Ye JQ, ''et al.'' |title=Recombinant Vgr-1/BMP-6-expressing tumors induce fibrosis and endochondral bone formation in vivo. |journal=J. Cell Biol. |volume=126 |issue= 6 |pages= 1595-609 |year= 1994 |pmid= 8089189 |doi= }}
*{{cite journal | author=Barnes J, Anthony CT, Wall N, Steiner MS |title=Bone morphogenetic protein-6 expression in normal and malignant prostate. |journal=World journal of urology |volume=13 |issue= 6 |pages= 337-43 |year= 1997 |pmid= 9116752 |doi= }}
*{{cite journal | author=Hamdy FC, Autzen P, Robinson MC, ''et al.'' |title=Immunolocalization and messenger RNA expression of bone morphogenetic protein-6 in human benign and malignant prostatic tissue. |journal=Cancer Res. |volume=57 |issue= 19 |pages= 4427-31 |year= 1997 |pmid= 9331107 |doi= }}
*{{cite journal | author=Olavesen MG, Bentley E, Mason RV, ''et al.'' |title=Fine mapping of 39 ESTs on human chromosome 6p23-p25. |journal=Genomics |volume=46 |issue= 2 |pages= 303-6 |year= 1998 |pmid= 9417921 |doi= 10.1006/geno.1997.5032 }}
*{{cite journal | author=Rickard DJ, Hofbauer LC, Bonde SK, ''et al.'' |title=Bone morphogenetic protein-6 production in human osteoblastic cell lines. Selective regulation by estrogen. |journal=J. Clin. Invest. |volume=101 |issue= 2 |pages= 413-22 |year= 1998 |pmid= 9435314 |doi= }}
*{{cite journal | author=Tamada H, Kitazawa R, Gohji K, ''et al.'' |title=Molecular cloning and analysis of the 5'-flanking region of the human bone morphogenetic protein-6 (BMP-6). |journal=Biochim. Biophys. Acta |volume=1395 |issue= 3 |pages= 247-51 |year= 1998 |pmid= 9512655 |doi= }}
*{{cite journal | author=Ebisawa T, Tada K, Kitajima I, ''et al.'' |title=Characterization of bone morphogenetic protein-6 signaling pathways in osteoblast differentiation. |journal=J. Cell. Sci. |volume=112 ( Pt 20) |issue= |pages= 3519-27 |year= 2000 |pmid= 10504300 |doi= }}
*{{cite journal | author=Heikinheimo KA, Laine MA, Ritvos OV, ''et al.'' |title=Bone morphogenetic protein-6 is a marker of serous acinar cell differentiation in normal and neoplastic human salivary gland. |journal=Cancer Res. |volume=59 |issue= 22 |pages= 5815-21 |year= 1999 |pmid= 10582704 |doi= }}
*{{cite journal | author=Ahmed N, Sammons J, Carson RJ, ''et al.'' |title=Effect of bone morphogenetic protein-6 on haemopoietic stem cells and cytokine production in normal human bone marrow stroma. |journal=Cell Biol. Int. |volume=25 |issue= 5 |pages= 429-35 |year= 2001 |pmid= 11401330 |doi= 10.1006/cbir.2000.0662 }}
*{{cite journal | author=Shimizu M, Higuchi K, Kasai S, ''et al.'' |title=A congenic mouse and candidate gene at the Chromosome 13 locus regulating bone density. |journal=Mamm. Genome |volume=13 |issue= 7 |pages= 335-40 |year= 2003 |pmid= 12140680 |doi= 10.1007/s00335-001-2129-4 }}
*{{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=Moser M, Binder O, Wu Y, ''et al.'' |title=BMPER, a novel endothelial cell precursor-derived protein, antagonizes bone morphogenetic protein signaling and endothelial cell differentiation. |journal=Mol. Cell. Biol. |volume=23 |issue= 16 |pages= 5664-79 |year= 2003 |pmid= 12897139 |doi= }}
*{{cite journal | author=Bobacz K, Gruber R, Soleiman A, ''et al.'' |title=Expression of bone morphogenetic protein 6 in healthy and osteoarthritic human articular chondrocytes and stimulation of matrix synthesis in vitro. |journal=Arthritis Rheum. |volume=48 |issue= 9 |pages= 2501-8 |year= 2003 |pmid= 13130469 |doi= 10.1002/art.11248 }}
*{{cite journal | author=Lories RJ, Derese I, Ceuppens JL, Luyten FP |title=Bone morphogenetic proteins 2 and 6, expressed in arthritic synovium, are regulated by proinflammatory cytokines and differentially modulate fibroblast-like synoviocyte apoptosis. |journal=Arthritis Rheum. |volume=48 |issue= 10 |pages= 2807-18 |year= 2003 |pmid= 14558086 |doi= 10.1002/art.11389 }}
*{{cite journal | author=Mungall AJ, Palmer SA, Sims SK, ''et al.'' |title=The DNA sequence and analysis of human chromosome 6. |journal=Nature |volume=425 |issue= 6960 |pages= 805-11 |year= 2003 |pmid= 14574404 |doi= 10.1038/nature02055 }}
*{{cite journal | author=Laurikkala J, Kassai Y, Pakkasjärvi L, ''et al.'' |title=Identification of a secreted BMP antagonist, ectodin, integrating BMP, FGF, and SHH signals from the tooth enamel knot. |journal=Dev. Biol. |volume=264 |issue= 1 |pages= 91-105 |year= 2004 |pmid= 14623234 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CCL19... {November 20, 2007 11:47:24 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:48:23 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Chemokine (C-C motif) ligand 19
| HGNCid = 10617
| Symbol = CCL19
| AltSymbols =; CKb11; ELC; MGC34433; MIP-3b; MIP3B; SCYA19
| OMIM = 602227
| ECnumber =
| Homologene = 4569
| MGIid = 1346316
| GeneAtlas_image1 = PBB_GE_CCL19_210072_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:0006874 |text = cellular calcium ion homeostasis}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0009615 |text = response to virus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6363
| Hs_Ensembl = ENSG00000172724
| Hs_RefseqProtein = NP_006265
| Hs_RefseqmRNA = NM_006274
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 34679564
| Hs_GenLoc_end = 34681274
| Hs_Uniprot = Q99731
| Mm_EntrezGene = 24047
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_011888
| Mm_RefseqProtein = NP_036018
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Chemokine (C-C motif) ligand 19''', also known as '''CCL19''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CCL19 chemokine (C-C motif) ligand 19| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6363| 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. The cytokine encoded by this gene may play a role in normal lymphocyte recirculation and homing. It also plays an important role in trafficking of T cells in thymus, and in T cell and B cell migration to secondary lymphoid organs. It specifically binds to chemokine receptor CCR7.<ref name="entrez">{{cite web | title = Entrez Gene: CCL19 chemokine (C-C motif) ligand 19| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6363| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Weber C, Koenen RR |title=Fine-tuning leukocyte responses: towards a chemokine 'interactome'. |journal=Trends Immunol. |volume=27 |issue= 6 |pages= 268-73 |year= 2006 |pmid= 16678487 |doi= 10.1016/j.it.2006.04.002 }}
*{{cite journal | author=Rossi DL, Vicari AP, Franz-Bacon K, ''et al.'' |title=Identification through bioinformatics of two new macrophage proinflammatory human chemokines: MIP-3alpha and MIP-3beta. |journal=J. Immunol. |volume=158 |issue= 3 |pages= 1033-6 |year= 1997 |pmid= 9013939 |doi= }}
*{{cite journal | author=Yoshida R, Imai T, Hieshima K, ''et al.'' |title=Molecular cloning of a novel human CC chemokine EBI1-ligand chemokine that is a specific functional ligand for EBI1, CCR7. |journal=J. Biol. Chem. |volume=272 |issue= 21 |pages= 13803-9 |year= 1997 |pmid= 9153236 |doi= }}
*{{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=Kim CH, Pelus LM, White JR, ''et al.'' |title=CK beta-11/macrophage inflammatory protein-3 beta/EBI1-ligand chemokine is an efficacious chemoattractant for T and B cells. |journal=J. Immunol. |volume=160 |issue= 5 |pages= 2418-24 |year= 1998 |pmid= 9498785 |doi= }}
*{{cite journal | author=Yanagihara S, Komura E, Nagafune J, ''et al.'' |title=EBI1/CCR7 is a new member of dendritic cell chemokine receptor that is up-regulated upon maturation. |journal=J. Immunol. |volume=161 |issue= 6 |pages= 3096-102 |year= 1998 |pmid= 9743376 |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=Ueno T, Hara K, Willis MS, ''et al.'' |title=Role for CCR7 ligands in the emigration of newly generated T lymphocytes from the neonatal thymus. |journal=Immunity |volume=16 |issue= 2 |pages= 205-18 |year= 2002 |pmid= 11869682 |doi= }}
*{{cite journal | author=Phillips R, Ager A |title=Activation of pertussis toxin-sensitive CXCL12 (SDF-1) receptors mediates transendothelial migration of T lymphocytes across lymph node high endothelial cells. |journal=Eur. J. Immunol. |volume=32 |issue= 3 |pages= 837-47 |year= 2002 |pmid= 11870628 |doi= }}
*{{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=Townson JR, Nibbs RJ |title=Characterization of mouse CCX-CKR, a receptor for the lymphocyte-attracting chemokines TECK/mCCL25, SLC/mCCL21 and MIP-3beta/mCCL19: comparison to human CCX-CKR. |journal=Eur. J. Immunol. |volume=32 |issue= 5 |pages= 1230-41 |year= 2002 |pmid= 11981810 |doi= 10.1002/1521-4141(200205)32:5<1230::AID-IMMU1230>3.0.CO;2-L }}
*{{cite journal | author=Page G, Lebecque S, Miossec P |title=Anatomic localization of immature and mature dendritic cells in an ectopic lymphoid organ: correlation with selective chemokine expression in rheumatoid synovium. |journal=J. Immunol. |volume=168 |issue= 10 |pages= 5333-41 |year= 2002 |pmid= 11994492 |doi= }}
*{{cite journal | author=Katou F, Ohtani H, Nakayama T, ''et al.'' |title=Differential expression of CCL19 by DC-Lamp+ mature dendritic cells in human lymph node versus chronically inflamed skin. |journal=J. Pathol. |volume=199 |issue= 1 |pages= 98-106 |year= 2003 |pmid= 12474232 |doi= 10.1002/path.1255 }}
*{{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=Scandella E, Men Y, Legler DF, ''et al.'' |title=CCL19/CCL21-triggered signal transduction and migration of dendritic cells requires prostaglandin E2. |journal=Blood |volume=103 |issue= 5 |pages= 1595-601 |year= 2004 |pmid= 14592837 |doi= 10.1182/blood-2003-05-1643 }}
*{{cite journal | author=Corcione A, Arduino N, Ferretti E, ''et al.'' |title=CCL19 and CXCL12 trigger in vitro chemotaxis of human mantle cell lymphoma B cells. |journal=Clin. Cancer Res. |volume=10 |issue= 3 |pages= 964-71 |year= 2004 |pmid= 14871974 |doi= }}
*{{cite journal | author=Daikoku N, Kitaya K, Nakayama T, ''et al.'' |title=Expression of macrophage inflammatory protein-3beta in human endometrium throughout the menstrual cycle. |journal=Fertil. Steril. |volume=81 Suppl 1 |issue= |pages= 876-81 |year= 2004 |pmid= 15019823 |doi= 10.1016/j.fertnstert.2003.09.036 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal | author=Paoletti S, Petkovic V, Sebastiani S, ''et al.'' |title=A rich chemokine environment strongly enhances leukocyte migration and activities. |journal=Blood |volume=105 |issue= 9 |pages= 3405-12 |year= 2005 |pmid= 15546958 |doi= 10.1182/blood-2004-04-1648 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on COX3... {November 20, 2007 11:26:45 PM PST}
- CREATE: Found no pages, creating new page. {November 20, 2007 11:27:09 PM PST}
- BAD FORMAT: There is a problem with the BOT commands for this protein: COX3. Invoking a Mandantory Inspection. {November 20, 2007 11:27:11 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Cytochrome c oxidase subunit III
| HGNCid = 7422
| Symbol = COX3
| AltSymbols =; MTCO3
| OMIM =
| ECnumber =
| Homologene = 5014
| MGIid = 102502
| Function =
| Component =
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4514
| Hs_Ensembl = ENSG00000198938
| Hs_RefseqProtein = NP_536849
| Hs_RefseqmRNA =
| Hs_GenLoc_db =
| Hs_GenLoc_chr = MT
| Hs_GenLoc_start = 9208
| Hs_GenLoc_end = 9988
| Hs_Uniprot = P00414
| Mm_EntrezGene = 17710
| Mm_Ensembl = ENSMUSG00000064358
| Mm_RefseqmRNA =
| Mm_RefseqProtein = NP_904334
| Mm_GenLoc_db =
| Mm_GenLoc_chr = MT
| Mm_GenLoc_start = 8607
| Mm_GenLoc_end = 9390
| Mm_Uniprot = Q5MCM2
}}
}}
'''Cytochrome c oxidase subunit III''', also known as '''COX3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: COX3 cytochrome c oxidase subunit III| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4514| 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=Moraes CT, Andreetta F, Bonilla E, ''et al.'' |title=Replication-competent human mitochondrial DNA lacking the heavy-strand promoter region. |journal=Mol. Cell. Biol. |volume=11 |issue= 3 |pages= 1631-7 |year= 1991 |pmid= 1996112 |doi= }}
*{{cite journal | author=Chomyn A, Cleeter MW, Ragan CI, ''et al.'' |title=URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit. |journal=Science |volume=234 |issue= 4776 |pages= 614-8 |year= 1986 |pmid= 3764430 |doi= }}
*{{cite journal | author=Chomyn A, Mariottini P, Cleeter MW, ''et al.'' |title=Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase. |journal=Nature |volume=314 |issue= 6012 |pages= 592-7 |year= 1985 |pmid= 3921850 |doi= }}
*{{cite journal | author=Anderson S, Bankier AT, Barrell BG, ''et al.'' |title=Sequence and organization of the human mitochondrial genome. |journal=Nature |volume=290 |issue= 5806 |pages= 457-65 |year= 1981 |pmid= 7219534 |doi= }}
*{{cite journal | author=Montoya J, Ojala D, Attardi G |title=Distinctive features of the 5'-terminal sequences of the human mitochondrial mRNAs. |journal=Nature |volume=290 |issue= 5806 |pages= 465-70 |year= 1981 |pmid= 7219535 |doi= }}
*{{cite journal | author=Andrews RM, Kubacka I, Chinnery PF, ''et al.'' |title=Reanalysis and revision of the Cambridge reference sequence for human mitochondrial DNA. |journal=Nat. Genet. |volume=23 |issue= 2 |pages= 147 |year= 1999 |pmid= 10508508 |doi= 10.1038/13779 }}
*{{cite journal | author=Ingman M, Kaessmann H, Pääbo S, Gyllensten U |title=Mitochondrial genome variation and the origin of modern humans. |journal=Nature |volume=408 |issue= 6813 |pages= 708-13 |year= 2001 |pmid= 11130070 |doi= 10.1038/35047064 }}
*{{cite journal | author=Maca-Meyer N, González AM, Larruga JM, ''et al.'' |title=Major genomic mitochondrial lineages delineate early human expansions. |journal=BMC Genet. |volume=2 |issue= |pages= 13 |year= 2003 |pmid= 11553319 |doi= }}
*{{cite journal | author=Herrnstadt C, Elson JL, Fahy E, ''et al.'' |title=Reduced-median-network analysis of complete mitochondrial DNA coding-region sequences for the major African, Asian, and European haplogroups. |journal=Am. J. Hum. Genet. |volume=70 |issue= 5 |pages= 1152-71 |year= 2002 |pmid= 11938495 |doi= }}
*{{cite journal | author=Silva WA, Bonatto SL, Holanda AJ, ''et al.'' |title=Mitochondrial genome diversity of Native Americans supports a single early entry of founder populations into America. |journal=Am. J. Hum. Genet. |volume=71 |issue= 1 |pages= 187-92 |year= 2002 |pmid= 12022039 |doi= }}
*{{cite journal | author=Elkon H, Don J, Melamed E, ''et al.'' |title=Mutant and wild-type alpha-synuclein interact with mitochondrial cytochrome C oxidase. |journal=J. Mol. Neurosci. |volume=18 |issue= 3 |pages= 229-38 |year= 2003 |pmid= 12059041 |doi= }}
*{{cite journal | author=Mishmar D, Ruiz-Pesini E, Golik P, ''et al.'' |title=Natural selection shaped regional mtDNA variation in humans. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 1 |pages= 171-6 |year= 2003 |pmid= 12509511 |doi= 10.1073/pnas.0136972100 }}
*{{cite journal | author=Ingman M, Gyllensten U |title=Mitochondrial genome variation and evolutionary history of Australian and New Guinean aborigines. |journal=Genome Res. |volume=13 |issue= 7 |pages= 1600-6 |year= 2003 |pmid= 12840039 |doi= 10.1101/gr.686603 }}
*{{cite journal | author=Kong QP, Yao YG, Sun C, ''et al.'' |title=Phylogeny of east Asian mitochondrial DNA lineages inferred from complete sequences. |journal=Am. J. Hum. Genet. |volume=73 |issue= 3 |pages= 671-6 |year= 2003 |pmid= 12870132 |doi= 10.1086/377718 }}
*{{cite journal | author=Temperley RJ, Seneca SH, Tonska K, ''et al.'' |title=Investigation of a pathogenic mtDNA microdeletion reveals a translation-dependent deadenylation decay pathway in human mitochondria. |journal=Hum. Mol. Genet. |volume=12 |issue= 18 |pages= 2341-8 |year= 2004 |pmid= 12915481 |doi= 10.1093/hmg/ddg238 }}
*{{cite journal | author=Maca-Meyer N, González AM, Pestano J, ''et al.'' |title=Mitochondrial DNA transit between West Asia and North Africa inferred from U6 phylogeography. |journal=BMC Genet. |volume=4 |issue= |pages= 15 |year= 2004 |pmid= 14563219 |doi= 10.1186/1471-2156-4-15 }}
*{{cite journal | author=Coble MD, Just RS, O'Callaghan JE, ''et al.'' |title=Single nucleotide polymorphisms over the entire mtDNA genome that increase the power of forensic testing in Caucasians. |journal=Int. J. Legal Med. |volume=118 |issue= 3 |pages= 137-46 |year= 2004 |pmid= 14760490 |doi= 10.1007/s00414-004-0427-6 }}
*{{cite journal | author=Palanichamy MG, Sun C, Agrawal S, ''et al.'' |title=Phylogeny of mitochondrial DNA macrohaplogroup N in India, based on complete sequencing: implications for the peopling of South Asia. |journal=Am. J. Hum. Genet. |volume=75 |issue= 6 |pages= 966-78 |year= 2005 |pmid= 15467980 |doi= 10.1086/425871 }}
*{{cite journal | author=Starikovskaya EB, Sukernik RI, Derbeneva OA, ''et al.'' |title=Mitochondrial DNA diversity in indigenous populations of the southern extent of Siberia, and the origins of Native American haplogroups. |journal=Ann. Hum. Genet. |volume=69 |issue= Pt 1 |pages= 67-89 |year= 2005 |pmid= 15638829 |doi= 10.1046/j.1529-8817.2003.00127.x }}
*{{cite journal | author=Rajkumar R, Banerjee J, Gunturi HB, ''et al.'' |title=Phylogeny and antiquity of M macrohaplogroup inferred from complete mt DNA sequence of Indian specific lineages. |journal=BMC Evol. Biol. |volume=5 |issue= 1 |pages= 26 |year= 2006 |pmid= 15804362 |doi= 10.1186/1471-2148-5-26 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ENPP2... {November 20, 2007 11:32:40 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:33:55 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 =
| image_source =
| PDB =
| Name = Ectonucleotide pyrophosphatase/phosphodiesterase 2 (autotaxin)
| HGNCid = 3357
| Symbol = ENPP2
| AltSymbols =; ATX; ATX-X; FLJ26803; LysoPLD; NPP2; PD-IALPHA; PDNP2
| OMIM = 601060
| ECnumber =
| Homologene = 4526
| MGIid = 1321390
| GeneAtlas_image1 = PBB_GE_ENPP2_209392_at_tn.png
| GeneAtlas_image2 = PBB_GE_ENPP2_210839_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003676 |text = nucleic acid binding}} {{GNF_GO|id=GO:0004519 |text = endonuclease activity}} {{GNF_GO|id=GO:0004528 |text = phosphodiesterase I activity}} {{GNF_GO|id=GO:0004551 |text = nucleotide diphosphatase activity}} {{GNF_GO|id=GO:0008134 |text = transcription factor binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0006796 |text = phosphate metabolic process}} {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0009117 |text = nucleotide metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5168
| Hs_Ensembl = ENSG00000136960
| Hs_RefseqProtein = NP_001035181
| Hs_RefseqmRNA = NM_001040092
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 120638507
| Hs_GenLoc_end = 120720260
| Hs_Uniprot = Q13822
| Mm_EntrezGene = 18606
| Mm_Ensembl = ENSMUSG00000022425
| Mm_RefseqmRNA = NM_015744
| Mm_RefseqProtein = NP_056559
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 54668984
| Mm_GenLoc_end = 54750085
| Mm_Uniprot = Q6PDE0
}}
}}
'''Ectonucleotide pyrophosphatase/phosphodiesterase 2 (autotaxin)''', also known as '''ENPP2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ENPP2 ectonucleotide pyrophosphatase/phosphodiesterase 2 (autotaxin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5168| 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 functions as both a phosphodiesterase, which cleaves phosphodiester bonds at the 5' end of oligonucleotides, and as a phospholipase, which catalyzes production of lysophosphatidic acid (LPA) in extracellular fluids. LPA evokes growth factor-like responses including stimulation of cell proliferation and chemotaxis. This gene product stimulates the motility of tumor cells, has angiogenic properties, and its expression is upregulated in several kinds of carcinomas. The gene product is secreted and further processed to make the biologically active form. Several alternatively spliced transcript variants have been identified, but the full-length nature of only two transcript variants has been determined.<ref name="entrez">{{cite web | title = Entrez Gene: ENPP2 ectonucleotide pyrophosphatase/phosphodiesterase 2 (autotaxin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5168| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Stracke ML, Krutzsch HC, Unsworth EJ, ''et al.'' |title=Identification, purification, and partial sequence analysis of autotaxin, a novel motility-stimulating protein. |journal=J. Biol. Chem. |volume=267 |issue= 4 |pages= 2524-9 |year= 1992 |pmid= 1733949 |doi= }}
*{{cite journal | author=Stracke ML, Arestad A, Levine M, ''et al.'' |title=Autotaxin is an N-linked glycoprotein but the sugar moieties are not needed for its stimulation of cellular motility. |journal=Melanoma Res. |volume=5 |issue= 4 |pages= 203-9 |year= 1996 |pmid= 7496154 |doi= }}
*{{cite journal | author=Murata J, Lee HY, Clair T, ''et al.'' |title=cDNA cloning of the human tumor motility-stimulating protein, autotaxin, reveals a homology with phosphodiesterases. |journal=J. Biol. Chem. |volume=269 |issue= 48 |pages= 30479-84 |year= 1994 |pmid= 7982964 |doi= }}
*{{cite journal | author=Lee HY, Murata J, Clair T, ''et al.'' |title=Cloning, chromosomal localization, and tissue expression of autotaxin from human teratocarcinoma cells. |journal=Biochem. Biophys. Res. Commun. |volume=218 |issue= 3 |pages= 714-9 |year= 1996 |pmid= 8579579 |doi= 10.1006/bbrc.1996.0127 }}
*{{cite journal | author=Kawagoe H, Soma O, Goji J, ''et al.'' |title=Molecular cloning and chromosomal assignment of the human brain-type phosphodiesterase I/nucleotide pyrophosphatase gene (PDNP2). |journal=Genomics |volume=30 |issue= 2 |pages= 380-4 |year= 1996 |pmid= 8586446 |doi= 10.1006/geno.1995.0036 }}
*{{cite journal | author=Lee HY, Clair T, Mulvaney PT, ''et al.'' |title=Stimulation of tumor cell motility linked to phosphodiesterase catalytic site of autotaxin. |journal=J. Biol. Chem. |volume=271 |issue= 40 |pages= 24408-12 |year= 1996 |pmid= 8798697 |doi= }}
*{{cite journal | author=Clair T, Lee HY, Liotta LA, Stracke ML |title=Autotaxin is an exoenzyme possessing 5'-nucleotide phosphodiesterase/ATP pyrophosphatase and ATPase activities. |journal=J. Biol. Chem. |volume=272 |issue= 2 |pages= 996-1001 |year= 1997 |pmid= 8995394 |doi= }}
*{{cite journal | author=Dias Neto E, Correa RG, Verjovski-Almeida S, ''et al.'' |title=Shotgun sequencing of the human transcriptome with ORF expressed sequence tags. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3491-6 |year= 2000 |pmid= 10737800 |doi= }}
*{{cite journal | author=Nam SW, Clair T, Kim YS, ''et al.'' |title=Autotaxin (NPP-2), a metastasis-enhancing motogen, is an angiogenic factor. |journal=Cancer Res. |volume=61 |issue= 18 |pages= 6938-44 |year= 2001 |pmid= 11559573 |doi= }}
*{{cite journal | author=Umezu-Goto M, Kishi Y, Taira A, ''et al.'' |title=Autotaxin has lysophospholipase D activity leading to tumor cell growth and motility by lysophosphatidic acid production. |journal=J. Cell Biol. |volume=158 |issue= 2 |pages= 227-33 |year= 2002 |pmid= 12119361 |doi= 10.1083/jcb.200204026 }}
*{{cite journal | author=Tokumura A, Majima E, Kariya Y, ''et al.'' |title=Identification of human plasma lysophospholipase D, a lysophosphatidic acid-producing enzyme, as autotaxin, a multifunctional phosphodiesterase. |journal=J. Biol. Chem. |volume=277 |issue= 42 |pages= 39436-42 |year= 2002 |pmid= 12176993 |doi= 10.1074/jbc.M205623200 }}
*{{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=Jung ID, Lee J, Yun SY, ''et al.'' |title=Cdc42 and Rac1 are necessary for autotaxin-induced tumor cell motility in A2058 melanoma cells. |journal=FEBS Lett. |volume=532 |issue= 3 |pages= 351-6 |year= 2003 |pmid= 12482591 |doi= }}
*{{cite journal | author=Yang SY, Lee J, Park CG, ''et al.'' |title=Expression of autotaxin (NPP-2) is closely linked to invasiveness of breast cancer cells. |journal=Clin. Exp. Metastasis |volume=19 |issue= 7 |pages= 603-8 |year= 2003 |pmid= 12498389 |doi= }}
*{{cite journal | author=Gijsbers R, Aoki J, Arai H, Bollen M |title=The hydrolysis of lysophospholipids and nucleotides by autotaxin (NPP2) involves a single catalytic site. |journal=FEBS Lett. |volume=538 |issue= 1-3 |pages= 60-4 |year= 2003 |pmid= 12633853 |doi= }}
*{{cite journal | author=Koh E, Clair T, Woodhouse EC, ''et al.'' |title=Site-directed mutations in the tumor-associated cytokine, autotaxin, eliminate nucleotide phosphodiesterase, lysophospholipase D, and motogenic activities. |journal=Cancer Res. |volume=63 |issue= 9 |pages= 2042-5 |year= 2003 |pmid= 12727817 |doi= }}
*{{cite journal | author=Kehlen A, Englert N, Seifert A, ''et al.'' |title=Expression, regulation and function of autotaxin in thyroid carcinomas. |journal=Int. J. Cancer |volume=109 |issue= 6 |pages= 833-8 |year= 2004 |pmid= 15027116 |doi= 10.1002/ijc.20022 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal | author=Boucher J, Quilliot D, Pradères JP, ''et al.'' |title=Potential involvement of adipocyte insulin resistance in obesity-associated up-regulation of adipocyte lysophospholipase D/autotaxin expression. |journal=Diabetologia |volume=48 |issue= 3 |pages= 569-77 |year= 2005 |pmid= 15700135 |doi= 10.1007/s00125-004-1660-8 }}
*{{cite journal | author=van Meeteren LA, Ruurs P, Christodoulou E, ''et al.'' |title=Inhibition of autotaxin by lysophosphatidic acid and sphingosine 1-phosphate. |journal=J. Biol. Chem. |volume=280 |issue= 22 |pages= 21155-61 |year= 2005 |pmid= 15769751 |doi= 10.1074/jbc.M413183200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FSCN1... {November 20, 2007 11:49:12 PM PST}
- UPLOAD: Added new Image to wiki: File:PBB Protein FSCN1 image.jpg {November 20, 2007 11:50:08 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:50:22 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_FSCN1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dfc.
| PDB = {{PDB2|1dfc}}
| Name = Fascin homolog 1, actin-bundling protein (Strongylocentrotus purpuratus)
| HGNCid = 11148
| Symbol = FSCN1
| AltSymbols =; p55; FLJ38511; SNL
| OMIM = 602689
| ECnumber =
| Homologene = 48164
| MGIid = 1352745
| GeneAtlas_image1 = PBB_GE_FSCN1_201564_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_FSCN1_210933_s_at_tn.png
| Function = {{GNF_GO|id=GO:0030674 |text = protein binding, bridging}} {{GNF_GO|id=GO:0051015 |text = actin filament binding}}
| Component = {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}}
| Process = {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0030036 |text = actin cytoskeleton organization and biogenesis}} {{GNF_GO|id=GO:0051017 |text = actin filament bundle formation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6624
| Hs_Ensembl = ENSG00000075618
| Hs_RefseqProtein = NP_003079
| Hs_RefseqmRNA = NM_003088
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 5598980
| Hs_GenLoc_end = 5612805
| Hs_Uniprot = Q16658
| Mm_EntrezGene = 14086
| Mm_Ensembl = ENSMUSG00000029581
| Mm_RefseqmRNA = NM_007984
| Mm_RefseqProtein = NP_032010
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 143225496
| Mm_GenLoc_end = 143238322
| Mm_Uniprot = Q05DK3
}}
}}
'''Fascin homolog 1, actin-bundling protein (Strongylocentrotus purpuratus)''', also known as '''FSCN1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FSCN1 fascin homolog 1, actin-bundling protein (Strongylocentrotus purpuratus)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6624| 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=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=Yamashiro-Matsumura S, Matsumura F |title=Purification and characterization of an F-actin-bundling 55-kilodalton protein from HeLa cells. |journal=J. Biol. Chem. |volume=260 |issue= 8 |pages= 5087-97 |year= 1985 |pmid= 3886649 |doi= }}
*{{cite journal | author=Mosialos G, Yamashiro S, Baughman RW, ''et al.'' |title=Epstein-Barr virus infection induces expression in B lymphocytes of a novel gene encoding an evolutionarily conserved 55-kilodalton actin-bundling protein. |journal=J. Virol. |volume=68 |issue= 11 |pages= 7320-8 |year= 1994 |pmid= 7933116 |doi= }}
*{{cite journal | author=Duh FM, Latif F, Weng Y, ''et al.'' |title=cDNA cloning and expression of the human homolog of the sea urchin fascin and Drosophila singed genes which encodes an actin-bundling protein. |journal=DNA Cell Biol. |volume=13 |issue= 8 |pages= 821-7 |year= 1994 |pmid= 8068206 |doi= }}
*{{cite journal | author=Mosialos G, Birkenbach M, Ayehunie S, ''et al.'' |title=Circulating human dendritic cells differentially express high levels of a 55-kd actin-bundling protein. |journal=Am. J. Pathol. |volume=148 |issue= 2 |pages= 593-600 |year= 1996 |pmid= 8579121 |doi= }}
*{{cite journal | author=Yamakita Y, Ono S, Matsumura F, Yamashiro S |title=Phosphorylation of human fascin inhibits its actin binding and bundling activities. |journal=J. Biol. Chem. |volume=271 |issue= 21 |pages= 12632-8 |year= 1996 |pmid= 8647875 |doi= }}
*{{cite journal | author=Lin XH, Grako KA, Burg MA, Stallcup WB |title=NG2 proteoglycan and the actin-binding protein fascin define separate populations of actin-containing filopodia and lamellipodia during cell spreading and migration. |journal=Mol. Biol. Cell |volume=7 |issue= 12 |pages= 1977-93 |year= 1997 |pmid= 8970159 |doi= }}
*{{cite journal | author=Ono S, Yamakita Y, Yamashiro S, ''et al.'' |title=Identification of an actin binding region and a protein kinase C phosphorylation site on human fascin. |journal=J. Biol. Chem. |volume=272 |issue= 4 |pages= 2527-33 |year= 1997 |pmid= 8999969 |doi= }}
*{{cite journal | author=Pinkus GS, Pinkus JL, Langhoff E, ''et al.'' |title=Fascin, a sensitive new marker for Reed-Sternberg cells of hodgkin's disease. Evidence for a dendritic or B cell derivation? |journal=Am. J. Pathol. |volume=150 |issue= 2 |pages= 543-62 |year= 1997 |pmid= 9033270 |doi= }}
*{{cite journal | author=Ross R, Ross XL, Schwing J, ''et al.'' |title=The actin-bundling protein fascin is involved in the formation of dendritic processes in maturing epidermal Langerhans cells. |journal=J. Immunol. |volume=160 |issue= 8 |pages= 3776-82 |year= 1998 |pmid= 9558080 |doi= }}
*{{cite journal | author=Sonderbye L, Meehan S, Palsson R, ''et al.'' |title=Immunohistochemical study of actin binding protein (p55) in the human kidney. |journal=Transplantation |volume=65 |issue= 7 |pages= 1004-8 |year= 1998 |pmid= 9565110 |doi= }}
*{{cite journal | author=Tubb BE, Bardien-Kruger S, Kashork CD, ''et al.'' |title=Characterization of human retinal fascin gene (FSCN2) at 17q25: close physical linkage of fascin and cytoplasmic actin genes. |journal=Genomics |volume=65 |issue= 2 |pages= 146-56 |year= 2000 |pmid= 10783262 |doi= 10.1006/geno.2000.6156 }}
*{{cite journal | author=Kempf W, Levi E, Kamarashev J, ''et al.'' |title=Fascin expression in CD30-positive cutaneous lymphoproliferative disorders. |journal=J. Cutan. Pathol. |volume=29 |issue= 5 |pages= 295-300 |year= 2003 |pmid= 12100631 |doi= }}
*{{cite journal | author=Goncharuk VN, Ross JS, Carlson JA |title=Actin-binding protein fascin expression in skin neoplasia. |journal=J. Cutan. Pathol. |volume=29 |issue= 7 |pages= 430-8 |year= 2003 |pmid= 12139639 |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=Pelosi G, Pastorino U, Pasini F, ''et al.'' |title=Independent prognostic value of fascin immunoreactivity in stage I nonsmall cell lung cancer. |journal=Br. J. Cancer |volume=88 |issue= 4 |pages= 537-47 |year= 2003 |pmid= 12592367 |doi= 10.1038/sj.bjc.6600731 }}
*{{cite journal | author=Shonukan O, Bagayogo I, McCrea P, ''et al.'' |title=Neurotrophin-induced melanoma cell migration is mediated through the actin-bundling protein fascin. |journal=Oncogene |volume=22 |issue= 23 |pages= 3616-23 |year= 2003 |pmid= 12789270 |doi= 10.1038/sj.onc.1206561 }}
*{{cite journal | author=Bros M, Ross XL, Pautz A, ''et al.'' |title=The human fascin gene promoter is highly active in mature dendritic cells due to a stage-specific enhancer. |journal=J. Immunol. |volume=171 |issue= 4 |pages= 1825-34 |year= 2003 |pmid= 12902483 |doi= }}
*{{cite journal | author=Anilkumar N, Parsons M, Monk R, ''et al.'' |title=Interaction of fascin and protein kinase Calpha: a novel intersection in cell adhesion and motility. |journal=EMBO J. |volume=22 |issue= 20 |pages= 5390-402 |year= 2004 |pmid= 14532112 |doi= 10.1093/emboj/cdg521 }}
*{{cite journal | author=Ishikawa R, Sakamoto T, Ando T, ''et al.'' |title=Polarized actin bundles formed by human fascin-1: their sliding and disassembly on myosin II and myosin V in vitro. |journal=J. Neurochem. |volume=87 |issue= 3 |pages= 676-85 |year= 2003 |pmid= 14535950 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GMNN... {November 20, 2007 11:50:22 PM PST}
- UPLOAD: Added new Image to wiki: File:PBB Protein GMNN image.jpg {November 20, 2007 11:51:01 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:51:13 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_GMNN_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1t6f.
| PDB = {{PDB2|1t6f}}, {{PDB2|1uii}}
| Name = Geminin, DNA replication inhibitor
| HGNCid = 17493
| Symbol = GMNN
| AltSymbols =; Gem; RP3-369A17.3
| OMIM = 602842
| ECnumber =
| Homologene = 9292
| MGIid = 1927344
| GeneAtlas_image1 = PBB_GE_GMNN_218350_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0008156 |text = negative regulation of DNA replication}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 51053
| Hs_Ensembl = ENSG00000112312
| Hs_RefseqProtein = NP_056979
| Hs_RefseqmRNA = NM_015895
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 24883138
| Hs_GenLoc_end = 24894306
| Hs_Uniprot = O75496
| Mm_EntrezGene = 57441
| Mm_Ensembl = ENSMUSG00000006715
| Mm_RefseqmRNA = NM_020567
| Mm_RefseqProtein = NP_065592
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 24759311
| Mm_GenLoc_end = 24769328
| Mm_Uniprot = Q5SZV9
}}
}}
'''Geminin, DNA replication inhibitor''', also known as '''GMNN''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GMNN geminin, DNA replication inhibitor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51053| 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=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=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=McGarry TJ, Kirschner MW |title=Geminin, an inhibitor of DNA replication, is degraded during mitosis. |journal=Cell |volume=93 |issue= 6 |pages= 1043-53 |year= 1998 |pmid= 9635433 |doi= }}
*{{cite journal | author=Kroll KL, Salic AN, Evans LM, Kirschner MW |title=Geminin, a neuralizing molecule that demarcates the future neural plate at the onset of gastrulation. |journal=Development |volume=125 |issue= 16 |pages= 3247-58 |year= 1998 |pmid= 9671596 |doi= }}
*{{cite journal | author=Wohlschlegel JA, Dwyer BT, Dhar SK, ''et al.'' |title=Inhibition of eukaryotic DNA replication by geminin binding to Cdt1. |journal=Science |volume=290 |issue= 5500 |pages= 2309-12 |year= 2001 |pmid= 11125146 |doi= 10.1126/science.290.5500.2309 }}
*{{cite journal | author=Bermejo R, Vilaboa N, Calés C |title=Regulation of CDC6, geminin, and CDT1 in human cells that undergo polyploidization. |journal=Mol. Biol. Cell |volume=13 |issue= 11 |pages= 3989-4000 |year= 2003 |pmid= 12429841 |doi= 10.1091/mbc.E02-04-0217 }}
*{{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=Biswas N, Sanchez V, Spector DH |title=Human cytomegalovirus infection leads to accumulation of geminin and inhibition of the licensing of cellular DNA replication. |journal=J. Virol. |volume=77 |issue= 4 |pages= 2369-76 |year= 2003 |pmid= 12551974 |doi= }}
*{{cite journal | author=Kulartz M, Kreitz S, Hiller E, ''et al.'' |title=Expression and phosphorylation of the replication regulator protein geminin. |journal=Biochem. Biophys. Res. Commun. |volume=305 |issue= 2 |pages= 412-20 |year= 2003 |pmid= 12745091 |doi= }}
*{{cite journal | author=Mungall AJ, Palmer SA, Sims SK, ''et al.'' |title=The DNA sequence and analysis of human chromosome 6. |journal=Nature |volume=425 |issue= 6960 |pages= 805-11 |year= 2003 |pmid= 14574404 |doi= 10.1038/nature02055 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Del Bene F, Tessmar-Raible K, Wittbrodt J |title=Direct interaction of geminin and Six3 in eye development. |journal=Nature |volume=427 |issue= 6976 |pages= 745-9 |year= 2004 |pmid= 14973488 |doi= 10.1038/nature02292 }}
*{{cite journal | author=Luo L, Yang X, Takihara Y, ''et al.'' |title=The cell-cycle regulator geminin inhibits Hox function through direct and polycomb-mediated interactions. |journal=Nature |volume=427 |issue= 6976 |pages= 749-53 |year= 2004 |pmid= 14973489 |doi= 10.1038/nature02305 }}
*{{cite journal | author=Sugimoto N, Tatsumi Y, Tsurumi T, ''et al.'' |title=Cdt1 phosphorylation by cyclin A-dependent kinases negatively regulates its function without affecting geminin binding. |journal=J. Biol. Chem. |volume=279 |issue= 19 |pages= 19691-7 |year= 2004 |pmid= 14993212 |doi= 10.1074/jbc.M313175200 }}
*{{cite journal | author=Melixetian M, Ballabeni A, Masiero L, ''et al.'' |title=Loss of Geminin induces rereplication in the presence of functional p53. |journal=J. Cell Biol. |volume=165 |issue= 4 |pages= 473-82 |year= 2004 |pmid= 15159417 |doi= 10.1083/jcb.200403106 }}
*{{cite journal | author=Ramachandran N, Hainsworth E, Bhullar B, ''et al.'' |title=Self-assembling protein microarrays. |journal=Science |volume=305 |issue= 5680 |pages= 86-90 |year= 2004 |pmid= 15232106 |doi= 10.1126/science.1097639 }}
*{{cite journal | author=Ballabeni A, Melixetian M, Zamponi R, ''et al.'' |title=Human geminin promotes pre-RC formation and DNA replication by stabilizing CDT1 in mitosis. |journal=EMBO J. |volume=23 |issue= 15 |pages= 3122-32 |year= 2005 |pmid= 15257290 |doi= 10.1038/sj.emboj.7600314 }}
*{{cite journal | author=Saxena S, Yuan P, Dhar SK, ''et al.'' |title=A dimerized coiled-coil domain and an adjoining part of geminin interact with two sites on Cdt1 for replication inhibition. |journal=Mol. Cell |volume=15 |issue= 2 |pages= 245-58 |year= 2004 |pmid= 15260975 |doi= 10.1016/j.molcel.2004.06.045 }}
*{{cite journal | author=Zhu W, Chen Y, Dutta A |title=Rereplication by depletion of geminin is seen regardless of p53 status and activates a G2/M checkpoint. |journal=Mol. Cell. Biol. |volume=24 |issue= 16 |pages= 7140-50 |year= 2004 |pmid= 15282313 |doi= 10.1128/MCB.24.16.7140-7150.2004 }}
*{{cite journal | author=Kulartz M, Knippers R |title=The replicative regulator protein geminin on chromatin in the HeLa cell cycle. |journal=J. Biol. Chem. |volume=279 |issue= 40 |pages= 41686-94 |year= 2004 |pmid= 15284237 |doi= 10.1074/jbc.M405798200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IL23A... {November 20, 2007 11:51:13 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:52:03 PM PST}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Interleukin 23, alpha subunit p19
| HGNCid = 15488
| Symbol = IL23A
| AltSymbols =; P19; IL-23; IL-23A; IL23P19; MGC79388; SGRF
| OMIM = 605580
| ECnumber =
| Homologene = 12832
| MGIid = 1932410
| GeneAtlas_image1 = PBB_GE_IL23A_220054_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0009615 |text = response to virus}} {{GNF_GO|id=GO:0009888 |text = tissue development}} {{GNF_GO|id=GO:0045087 |text = innate immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 51561
| Hs_Ensembl = ENSG00000110944
| Hs_RefseqProtein = NP_057668
| Hs_RefseqmRNA = NM_016584
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 55018926
| Hs_GenLoc_end = 55020460
| Hs_Uniprot = Q9NPF7
| Mm_EntrezGene = 83430
| Mm_Ensembl = ENSMUSG00000025383
| Mm_RefseqmRNA = NM_031252
| Mm_RefseqProtein = NP_112542
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 127699089
| Mm_GenLoc_end = 127701033
| Mm_Uniprot = Q9EQ14
}}
}}
'''Interleukin 23, alpha subunit p19''', also known as '''IL23A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IL23A interleukin 23, alpha subunit p19| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51561| 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 subunit of the heterodimeric cytokine interleukin 23 (IL23). IL23 is composed of this protein and the p40 subunit of interleukin 12 (IL12B). The receptor of IL23 is formed by the beta 1 subunit of IL12 (IL12RB1) and an IL23 specific subunit, IL23R. Both IL23 and IL12 can activate the transcription activator STAT4, and stimulate the production of interferon-gamma (IFNG). In contrast to IL12, which acts mainly on naive CD4(+) T cells, IL23 preferentially acts on memory CD4(+) T cells.<ref name="entrez">{{cite web | title = Entrez Gene: IL23A interleukin 23, alpha subunit p19| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51561| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lankford CS, Frucht DM |title=A unique role for IL-23 in promoting cellular immunity. |journal=J. Leukoc. Biol. |volume=73 |issue= 1 |pages= 49-56 |year= 2003 |pmid= 12525561 |doi= }}
*{{cite journal | author=van de Vosse E, Lichtenauer-Kaligis EG, van Dissel JT, Ottenhoff TH |title=Genetic variations in the interleukin-12/interleukin-23 receptor (beta1) chain, and implications for IL-12 and IL-23 receptor structure and function. |journal=Immunogenetics |volume=54 |issue= 12 |pages= 817-29 |year= 2003 |pmid= 12671732 |doi= 10.1007/s00251-002-0534-9 }}
*{{cite journal | author=Kreymborg K, Böhlmann U, Becher B |title=IL-23: changing the verdict on IL-12 function in inflammation and autoimmunity. |journal=Expert Opin. Ther. Targets |volume=9 |issue= 6 |pages= 1123-36 |year= 2006 |pmid= 16300465 |doi= 10.1517/14728222.9.6.1123 }}
*{{cite journal | author=Peluso I, Pallone F, Monteleone G |title=Interleukin-12 and Th1 immune response in Crohn's disease: pathogenetic relevance and therapeutic implication. |journal=World J. Gastroenterol. |volume=12 |issue= 35 |pages= 5606-10 |year= 2006 |pmid= 17007011 |doi= }}
*{{cite journal | author=Prashar Y, Weissman SM |title=Analysis of differential gene expression by display of 3' end restriction fragments of cDNAs. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 2 |pages= 659-63 |year= 1996 |pmid= 8570611 |doi= }}
*{{cite journal | author=Oppmann B, Lesley R, Blom B, ''et al.'' |title=Novel p19 protein engages IL-12p40 to form a cytokine, IL-23, with biological activities similar as well as distinct from IL-12. |journal=Immunity |volume=13 |issue= 5 |pages= 715-25 |year= 2001 |pmid= 11114383 |doi= }}
*{{cite journal | author=Wiekowski MT, Leach MW, Evans EW, ''et al.'' |title=Ubiquitous transgenic expression of the IL-23 subunit p19 induces multiorgan inflammation, runting, infertility, and premature death. |journal=J. Immunol. |volume=166 |issue= 12 |pages= 7563-70 |year= 2001 |pmid= 11390512 |doi= }}
*{{cite journal | author=Parham C, Chirica M, Timans J, ''et al.'' |title=A receptor for the heterodimeric cytokine IL-23 is composed of IL-12Rbeta1 and a novel cytokine receptor subunit, IL-23R. |journal=J. Immunol. |volume=168 |issue= 11 |pages= 5699-708 |year= 2002 |pmid= 12023369 |doi= }}
*{{cite journal | author=Broberg EK, Setälä N, Erälinna JP, ''et al.'' |title=Herpes simplex virus type 1 infection induces upregulation of interleukin-23 (p19) mRNA expression in trigeminal ganglia of BALB/c mice. |journal=J. Interferon Cytokine Res. |volume=22 |issue= 6 |pages= 641-51 |year= 2003 |pmid= 12162874 |doi= 10.1089/10799900260100123 }}
*{{cite journal | author=Pirhonen J, Matikainen S, Julkunen I |title=Regulation of virus-induced IL-12 and IL-23 expression in human macrophages. |journal=J. Immunol. |volume=169 |issue= 10 |pages= 5673-8 |year= 2003 |pmid= 12421946 |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=Lo CH, Lee SC, Wu PY, ''et al.'' |title=Antitumor and antimetastatic activity of IL-23. |journal=J. Immunol. |volume=171 |issue= 2 |pages= 600-7 |year= 2003 |pmid= 12847224 |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 }}
*{{cite journal | author=Lee E, Trepicchio WL, Oestreicher JL, ''et al.'' |title=Increased expression of interleukin 23 p19 and p40 in lesional skin of patients with psoriasis vulgaris. |journal=J. Exp. Med. |volume=199 |issue= 1 |pages= 125-30 |year= 2004 |pmid= 14707118 |doi= 10.1084/jem.20030451 }}
*{{cite journal | author=Verreck FA, de Boer T, Langenberg DM, ''et al.'' |title=Human IL-23-producing type 1 macrophages promote but IL-10-producing type 2 macrophages subvert immunity to (myco)bacteria. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 13 |pages= 4560-5 |year= 2004 |pmid= 15070757 |doi= 10.1073/pnas.0400983101 }}
*{{cite journal | author=Smits HH, van Beelen AJ, Hessle C, ''et al.'' |title=Commensal Gram-negative bacteria prime human dendritic cells for enhanced IL-23 and IL-27 expression and enhanced Th1 development. |journal=Eur. J. Immunol. |volume=34 |issue= 5 |pages= 1371-80 |year= 2004 |pmid= 15114670 |doi= 10.1002/eji.200324815 }}
*{{cite journal | author=Schnurr M, Toy T, Shin A, ''et al.'' |title=Extracellular nucleotide signaling by P2 receptors inhibits IL-12 and enhances IL-23 expression in human dendritic cells: a novel role for the cAMP pathway. |journal=Blood |volume=105 |issue= 4 |pages= 1582-9 |year= 2005 |pmid= 15486065 |doi= 10.1182/blood-2004-05-1718 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LTB... {November 20, 2007 11:25:57 PM PST}
- CREATE: Found no pages, creating new page. {November 20, 2007 11:26:37 PM PST}
- CREATED: Created new protein page: LTB {November 20, 2007 11:26:45 PM PST}
- INFO: Beginning work on NEU1... {November 20, 2007 11:27:11 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:27:51 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Sialidase 1 (lysosomal sialidase)
| HGNCid = 7758
| Symbol = NEU1
| AltSymbols =; NEU; SIAL1
| OMIM = 608272
| ECnumber =
| Homologene = 375
| MGIid = 97305
| GeneAtlas_image1 = PBB_GE_NEU1_208926_at_tn.png
| Function = {{GNF_GO|id=GO:0004308 |text = exo-alpha-sialidase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016798 |text = hydrolase activity, acting on glycosyl bonds}}
| Component = {{GNF_GO|id=GO:0005764 |text = lysosome}}
| Process = {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4758
| Hs_Ensembl = ENSG00000184494
| Hs_RefseqProtein = NP_000425
| Hs_RefseqmRNA = NM_000434
| Hs_GenLoc_db =
| Hs_GenLoc_chr = c6_QBL
| Hs_GenLoc_start = 31960200
| Hs_GenLoc_end = 31963930
| Hs_Uniprot = Q99519
| Mm_EntrezGene = 18010
| Mm_Ensembl = ENSMUSG00000007038
| Mm_RefseqmRNA = NM_010893
| Mm_RefseqProtein = NP_035023
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 34539370
| Mm_GenLoc_end = 34544009
| Mm_Uniprot = Q3UL64
}}
}}
'''Sialidase 1 (lysosomal sialidase)''', also known as '''NEU1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NEU1 sialidase 1 (lysosomal sialidase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4758| 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 encodes the lysosomal enzyme, which cleaves terminal sialic acid residues from substrates such as glycoproteins and glycolipids. In the lysosome, this enzyme is part of a heterotrimeric complex together with beta-galactosidase and cathepsin A (the latter also referred to as 'protective protein'). Mutations in this gene can lead to sialidosis.<ref name="entrez">{{cite web | title = Entrez Gene: NEU1 sialidase 1 (lysosomal sialidase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4758| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Okamura-Oho Y, Zhang S, Callahan JW |title=The biochemistry and clinical features of galactosialidosis. |journal=Biochim. Biophys. Acta |volume=1225 |issue= 3 |pages= 244-54 |year= 1994 |pmid= 8312369 |doi= }}
*{{cite journal | author=Seyrantepe V, Poupetova H, Froissart R, ''et al.'' |title=Molecular pathology of NEU1 gene in sialidosis. |journal=Hum. Mutat. |volume=22 |issue= 5 |pages= 343-52 |year= 2004 |pmid= 14517945 |doi= 10.1002/humu.10268 }}
*{{cite journal | author=Verheijen FW, Palmeri S, Galjaard H |title=Purification and partial characterization of lysosomal neuraminidase from human placenta. |journal=Eur. J. Biochem. |volume=162 |issue= 1 |pages= 63-7 |year= 1987 |pmid= 3102233 |doi= }}
*{{cite journal | author=Verheijen FW, Palmeri S, Hoogeveen AT, Galjaard H |title=Human placental neuraminidase. Activation, stabilization and association with beta-galactosidase and its protective protein. |journal=Eur. J. Biochem. |volume=149 |issue= 2 |pages= 315-21 |year= 1985 |pmid= 3922758 |doi= }}
*{{cite journal | author=Hu H, Shioda T, Moriya C, ''et al.'' |title=Infectivities of human and other primate lentiviruses are activated by desialylation of the virion surface. |journal=J. Virol. |volume=70 |issue= 11 |pages= 7462-70 |year= 1996 |pmid= 8892864 |doi= }}
*{{cite journal | author=Pshezhetsky AV, Potier M |title=Association of N-acetylgalactosamine-6-sulfate sulfatase with the multienzyme lysosomal complex of beta-galactosidase, cathepsin A, and neuraminidase. Possible implication for intralysosomal catabolism of keratan sulfate. |journal=J. Biol. Chem. |volume=271 |issue= 45 |pages= 28359-65 |year= 1996 |pmid= 8910459 |doi= }}
*{{cite journal | author=Bonten E, van der Spoel A, Fornerod M, ''et al.'' |title=Characterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis. |journal=Genes Dev. |volume=10 |issue= 24 |pages= 3156-69 |year= 1997 |pmid= 8985184 |doi= }}
*{{cite journal | author=Milner CM, Smith SV, Carrillo MB, ''et al.'' |title=Identification of a sialidase encoded in the human major histocompatibility complex. |journal=J. Biol. Chem. |volume=272 |issue= 7 |pages= 4549-58 |year= 1997 |pmid= 9020182 |doi= }}
*{{cite journal | author=Pshezhetsky AV, Richard C, Michaud L, ''et al.'' |title=Cloning, expression and chromosomal mapping of human lysosomal sialidase and characterization of mutations in sialidosis. |journal=Nat. Genet. |volume=15 |issue= 3 |pages= 316-20 |year= 1997 |pmid= 9054950 |doi= 10.1038/ng0397-316 }}
*{{cite journal | author=Vinogradova MV, Michaud L, Mezentsev AV, ''et al.'' |title=Molecular mechanism of lysosomal sialidase deficiency in galactosialidosis involves its rapid degradation. |journal=Biochem. J. |volume=330 ( Pt 2) |issue= |pages= 641-50 |year= 1998 |pmid= 9480870 |doi= }}
*{{cite journal | author=van der Spoel A, Bonten E, d'Azzo A |title=Transport of human lysosomal neuraminidase to mature lysosomes requires protective protein/cathepsin A. |journal=EMBO J. |volume=17 |issue= 6 |pages= 1588-97 |year= 1998 |pmid= 9501080 |doi= 10.1093/emboj/17.6.1588 }}
*{{cite journal | author=Lukong KE, Elsliger MA, Chang Y, ''et al.'' |title=Characterization of the sialidase molecular defects in sialidosis patients suggests the structural organization of the lysosomal multienzyme complex. |journal=Hum. Mol. Genet. |volume=9 |issue= 7 |pages= 1075-85 |year= 2000 |pmid= 10767332 |doi= }}
*{{cite journal | author=Naganawa Y, Itoh K, Shimmoto M, ''et al.'' |title=Molecular and structural studies of Japanese patients with sialidosis type 1. |journal=J. Hum. Genet. |volume=45 |issue= 4 |pages= 241-9 |year= 2000 |pmid= 10944856 |doi= }}
*{{cite journal | author=Bonten EJ, Arts WF, Beck M, ''et al.'' |title=Novel mutations in lysosomal neuraminidase identify functional domains and determine clinical severity in sialidosis. |journal=Hum. Mol. Genet. |volume=9 |issue= 18 |pages= 2715-25 |year= 2000 |pmid= 11063730 |doi= }}
*{{cite journal | author=Lukong KE, Landry K, Elsliger MA, ''et al.'' |title=Mutations in sialidosis impair sialidase binding to the lysosomal multienzyme complex. |journal=J. Biol. Chem. |volume=276 |issue= 20 |pages= 17286-90 |year= 2001 |pmid= 11279074 |doi= 10.1074/jbc.M100460200 }}
*{{cite journal | author=Penzel R, Uhl J, Kopitz J, ''et al.'' |title=Splice donor site mutation in the lysosomal neuraminidase gene causing exon skipping and complete loss of enzyme activity in a sialidosis patient. |journal=FEBS Lett. |volume=501 |issue= 2-3 |pages= 135-8 |year= 2001 |pmid= 11470272 |doi= }}
*{{cite journal | author=Lukong KE, Seyrantepe V, Landry K, ''et al.'' |title=Intracellular distribution of lysosomal sialidase is controlled by the internalization signal in its cytoplasmic tail. |journal=J. Biol. Chem. |volume=276 |issue= 49 |pages= 46172-81 |year= 2002 |pmid= 11571282 |doi= 10.1074/jbc.M104547200 }}
*{{cite journal | author=Sergi C, Penzel R, Uhl J, ''et al.'' |title=Prenatal diagnosis and fetal pathology in a Turkish family harboring a novel nonsense mutation in the lysosomal alpha-N-acetyl-neuraminidase (sialidase) gene. |journal=Hum. Genet. |volume=109 |issue= 4 |pages= 421-8 |year= 2001 |pmid= 11702224 |doi= 10.1007/s004390100592 }}
*{{cite journal | author=Itoh K, Naganawa Y, Matsuzawa F, ''et al.'' |title=Novel missense mutations in the human lysosomal sialidase gene in sialidosis patients and prediction of structural alterations of mutant enzymes. |journal=J. Hum. Genet. |volume=47 |issue= 1 |pages= 29-37 |year= 2002 |pmid= 11829139 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NOV... {November 20, 2007 11:27:51 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:28:55 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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| update_page = yes
| 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 = Nephroblastoma overexpressed gene
| HGNCid = 7885
| Symbol = NOV
| AltSymbols =; CCN3; IGFBP9; NOVH
| OMIM = 164958
| ECnumber =
| Homologene = 1884
| MGIid = 109185
| GeneAtlas_image1 = PBB_GE_NOV_214321_at_tn.png
| GeneAtlas_image2 = PBB_GE_NOV_204501_at_tn.png
| Function = {{GNF_GO|id=GO:0005520 |text = insulin-like growth factor binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0001558 |text = regulation of cell growth}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4856
| Hs_Ensembl = ENSG00000136999
| Hs_RefseqProtein = NP_002505
| Hs_RefseqmRNA = NM_002514
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 120497882
| Hs_GenLoc_end = 120505776
| Hs_Uniprot = P48745
| Mm_EntrezGene = 18133
| Mm_Ensembl = ENSMUSG00000037362
| Mm_RefseqmRNA = NM_010930
| Mm_RefseqProtein = NP_035060
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 54576005
| Mm_GenLoc_end = 54583847
| Mm_Uniprot = Q3U2X7
}}
}}
'''Nephroblastoma overexpressed gene''', also known as '''NOV''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NOV nephroblastoma overexpressed gene| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4856| 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=Perbal B |title=The CCN3 protein and cancer. |journal=Adv. Exp. Med. Biol. |volume=587 |issue= |pages= 23-40 |year= 2007 |pmid= 17163153 |doi= }}
*{{cite journal | author=Martinerie C, Viegas-Pequignot E, Guenard I, ''et al.'' |title=Physical mapping of human loci homologous to the chicken nov proto-oncogene. |journal=Oncogene |volume=7 |issue= 12 |pages= 2529-34 |year= 1993 |pmid= 1334251 |doi= }}
*{{cite journal | author=Martinerie C, Huff V, Joubert I, ''et al.'' |title=Structural analysis of the human nov proto-oncogene and expression in Wilms tumor. |journal=Oncogene |volume=9 |issue= 9 |pages= 2729-32 |year= 1994 |pmid= 7520150 |doi= }}
*{{cite journal | author=Martinerie C, Chevalier G, Rauscher FJ, Perbal B |title=Regulation of nov by WT1: a potential role for nov in nephrogenesis. |journal=Oncogene |volume=12 |issue= 7 |pages= 1479-92 |year= 1996 |pmid= 8622864 |doi= }}
*{{cite journal | author=Perbal B, Martinerie C, Sainson R, ''et al.'' |title=The C-terminal domain of the regulatory protein NOVH is sufficient to promote interaction with fibulin 1C: a clue for a role of NOVH in cell-adhesion signaling. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 3 |pages= 869-74 |year= 1999 |pmid= 9927660 |doi= }}
*{{cite journal | author=Burren CP, Wilson EM, Hwa V, ''et al.'' |title=Binding properties and distribution of insulin-like growth factor binding protein-related protein 3 (IGFBP-rP3/NovH), an additional member of the IGFBP Superfamily. |journal=J. Clin. Endocrinol. Metab. |volume=84 |issue= 3 |pages= 1096-103 |year= 1999 |pmid= 10084601 |doi= }}
*{{cite journal | author=Perbal B |title=Nuclear localisation of NOVH protein: a potential role for NOV in the regulation of gene expression. |journal=MP, Mol. Pathol. |volume=52 |issue= 2 |pages= 84-91 |year= 1999 |pmid= 10474687 |doi= }}
*{{cite journal | author=Albrecht C, von Der Kammer H, Mayhaus M, ''et al.'' |title=Muscarinic acetylcholine receptors induce the expression of the immediate early growth regulatory gene CYR61. |journal=J. Biol. Chem. |volume=275 |issue= 37 |pages= 28929-36 |year= 2000 |pmid= 10852911 |doi= 10.1074/jbc.M003053200 }}
*{{cite journal | author=Martinerie C, Gicquel C, Louvel A, ''et al.'' |title=Altered expression of novH is associated with human adrenocortical tumorigenesis. |journal=J. Clin. Endocrinol. Metab. |volume=86 |issue= 8 |pages= 3929-40 |year= 2001 |pmid= 11502835 |doi= }}
*{{cite journal | author=Manara MC, Perbal B, Benini S, ''et al.'' |title=The expression of ccn3(nov) gene in musculoskeletal tumors. |journal=Am. J. Pathol. |volume=160 |issue= 3 |pages= 849-59 |year= 2002 |pmid= 11891184 |doi= }}
*{{cite journal | author=Sakamoto K, Yamaguchi S, Ando R, ''et al.'' |title=The nephroblastoma overexpressed gene (NOV/ccn3) protein associates with Notch1 extracellular domain and inhibits myoblast differentiation via Notch signaling pathway. |journal=J. Biol. Chem. |volume=277 |issue= 33 |pages= 29399-405 |year= 2002 |pmid= 12050162 |doi= 10.1074/jbc.M203727200 }}
*{{cite journal | author=Li CL, Martinez V, He B, ''et al.'' |title=A role for CCN3 (NOV) in calcium signalling. |journal=MP, Mol. Pathol. |volume=55 |issue= 4 |pages= 250-61 |year= 2002 |pmid= 12147716 |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=Thibout H, Martinerie C, Créminon C, ''et al.'' |title=Characterization of human NOV in biological fluids: an enzyme immunoassay for the quantification of human NOV in sera from patients with diseases of the adrenal gland and of the nervous system. |journal=J. Clin. Endocrinol. Metab. |volume=88 |issue= 1 |pages= 327-36 |year= 2003 |pmid= 12519873 |doi= }}
*{{cite journal | author=Lin CG, Leu SJ, Chen N, ''et al.'' |title=CCN3 (NOV) is a novel angiogenic regulator of the CCN protein family. |journal=J. Biol. Chem. |volume=278 |issue= 26 |pages= 24200-8 |year= 2003 |pmid= 12695522 |doi= 10.1074/jbc.M302028200 }}
*{{cite journal | author=Ellis PD, Metcalfe JC, Hyvönen M, Kemp PR |title=Adhesion of endothelial cells to NOV is mediated by the integrins alphavbeta3 and alpha5beta1. |journal=J. Vasc. Res. |volume=40 |issue= 3 |pages= 234-43 |year= 2003 |pmid= 12902636 |doi= 10.1159/000071887 }}
*{{cite journal | author=Laurent M, Martinerie C, Thibout H, ''et al.'' |title=NOVH increases MMP3 expression and cell migration in glioblastoma cells via a PDGFR-alpha-dependent mechanism. |journal=FASEB J. |volume=17 |issue= 13 |pages= 1919-21 |year= 2003 |pmid= 14519668 |doi= 10.1096/fj.02-1023fje }}
*{{cite journal | author=Lombet A, Planque N, Bleau AM, ''et al.'' |title=CCN3 and calcium signaling. |journal= |volume=1 |issue= 1 |pages= 1 |year= |pmid= 14606958 |doi= 10.1186/1478-811X-1-1 }}
*{{cite journal | author=Schild C, Trueb B |title=Three members of the connective tissue growth factor family CCN are differentially regulated by mechanical stress. |journal=Biochim. Biophys. Acta |volume=1691 |issue= 1 |pages= 33-40 |year= 2004 |pmid= 15053922 |doi= 10.1016/j.bbamcr.2003.12.001 }}
*{{cite journal | author=Gellhaus A, Dong X, Propson S, ''et al.'' |title=Connexin43 interacts with NOV: a possible mechanism for negative regulation of cell growth in choriocarcinoma cells. |journal=J. Biol. Chem. |volume=279 |issue= 35 |pages= 36931-42 |year= 2004 |pmid= 15181016 |doi= 10.1074/jbc.M404073200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NP... {November 20, 2007 11:28:55 PM PST}
- UPLOAD: Added new Image to wiki: File:PBB Protein NP image.jpg {November 20, 2007 11:29:28 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:29:50 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_NP_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1m73.
| PDB = {{PDB2|1m73}}, {{PDB2|1pf7}}, {{PDB2|1pwy}}, {{PDB2|1rct}}, {{PDB2|1rfg}}, {{PDB2|1rr6}}, {{PDB2|1rsz}}, {{PDB2|1rt9}}, {{PDB2|1ula}}, {{PDB2|1ulb}}, {{PDB2|1v2h}}, {{PDB2|1v3q}}, {{PDB2|1v41}}, {{PDB2|1v45}}, {{PDB2|1yry}}, {{PDB2|2a0w}}, {{PDB2|2a0x}}, {{PDB2|2a0y}}, {{PDB2|2oc4}}, {{PDB2|2oc9}}, {{PDB2|2on6}}
| Name = Nucleoside phosphorylase
| HGNCid = 7892
| Symbol = NP
| AltSymbols =; MGC117396; MGC125915; MGC125916; PNP; PRO1837; PUNP
| OMIM = 164050
| ECnumber =
| Homologene = 227
| MGIid =
| GeneAtlas_image1 = PBB_GE_NP_201695_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004731 |text = purine-nucleoside phosphorylase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006139 |text = nucleobase, nucleoside, nucleotide and nucleic acid metabolic process}} {{GNF_GO|id=GO:0006304 |text = DNA modification}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4860
| Hs_Ensembl = ENSG00000198805
| Hs_RefseqProtein = NP_000261
| Hs_RefseqmRNA = NM_000270
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 20007409
| Hs_GenLoc_end = 20015082
| Hs_Uniprot = P00491
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Nucleoside phosphorylase''', also known as '''NP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NP nucleoside phosphorylase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4860| 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 = NP encodes the enzyme purine nucleoside phosphorylase that together with adenosine deaminase (ADA) serves a key role in purine catabolism, referred to as the salvage pathway. Mutations in either enzyme result in a severe combined immunodeficiency (SCID).<ref name="entrez">{{cite web | title = Entrez Gene: NP nucleoside phosphorylase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4860| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Markert ML |title=Purine nucleoside phosphorylase deficiency. |journal=Immunodeficiency reviews |volume=3 |issue= 1 |pages= 45-81 |year= 1991 |pmid= 1931007 |doi= }}
*{{cite journal | author=Borgers M, Verhaegen H, De Brabander M, ''et al.'' |title=Purine nucleoside phosphorylase in chronic lymphocytic leukemia (CLL). |journal=Blood |volume=52 |issue= 5 |pages= 886-95 |year= 1978 |pmid= 100152 |doi= }}
*{{cite journal | author=Aust MR, Andrews LG, Barrett MJ, ''et al.'' |title=Molecular analysis of mutations in a patient with purine nucleoside phosphorylase deficiency. |journal=Am. J. Hum. Genet. |volume=51 |issue= 4 |pages= 763-72 |year= 1992 |pmid= 1384322 |doi= }}
*{{cite journal | author=Andrews LG, Markert ML |title=Exon skipping in purine nucleoside phosphorylase mRNA processing leading to severe immunodeficiency. |journal=J. Biol. Chem. |volume=267 |issue= 11 |pages= 7834-8 |year= 1992 |pmid= 1560016 |doi= }}
*{{cite journal | author=Jonsson JJ, Williams SR, McIvor RS |title=Sequence and functional characterization of the human purine nucleoside phosphorylase promoter. |journal=Nucleic Acids Res. |volume=19 |issue= 18 |pages= 5015-20 |year= 1991 |pmid= 1923769 |doi= }}
*{{cite journal | author=Ealick SE, Rule SA, Carter DC, ''et al.'' |title=Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution. |journal=J. Biol. Chem. |volume=265 |issue= 3 |pages= 1812-20 |year= 1990 |pmid= 2104852 |doi= }}
*{{cite journal | author=Williams SR, Gekeler V, McIvor RS, Martin DW |title=A human purine nucleoside phosphorylase deficiency caused by a single base change. |journal=J. Biol. Chem. |volume=262 |issue= 5 |pages= 2332-8 |year= 1987 |pmid= 3029074 |doi= }}
*{{cite journal | author=Williams SR, Goddard JM, Martin DW |title=Human purine nucleoside phosphorylase cDNA sequence and genomic clone characterization. |journal=Nucleic Acids Res. |volume=12 |issue= 14 |pages= 5779-87 |year= 1984 |pmid= 6087295 |doi= }}
*{{cite journal | author=Pannicke U, Tuchschmid P, Friedrich W, ''et al.'' |title=Two novel missense and frameshift mutations in exons 5 and 6 of the purine nucleoside phosphorylase (PNP) gene in a severe combined immunodeficiency (SCID) patient. |journal=Hum. Genet. |volume=98 |issue= 6 |pages= 706-9 |year= 1997 |pmid= 8931706 |doi= }}
*{{cite journal | author=Markert ML, Finkel BD, McLaughlin TM, ''et al.'' |title=Mutations in purine nucleoside phosphorylase deficiency. |journal=Hum. Mutat. |volume=9 |issue= 2 |pages= 118-21 |year= 1997 |pmid= 9067751 |doi= 10.1002/(SICI)1098-1004(1997)9:2<118::AID-HUMU3>3.0.CO;2-5 }}
*{{cite journal | author=Erion MD, Takabayashi K, Smith HB, ''et al.'' |title=Purine nucleoside phosphorylase. 1. Structure-function studies. |journal=Biochemistry |volume=36 |issue= 39 |pages= 11725-34 |year= 1997 |pmid= 9305962 |doi= 10.1021/bi961969w }}
*{{cite journal | author=Erion MD, Stoeckler JD, Guida WC, ''et al.'' |title=Purine nucleoside phosphorylase. 2. Catalytic mechanism. |journal=Biochemistry |volume=36 |issue= 39 |pages= 11735-48 |year= 1997 |pmid= 9305963 |doi= 10.1021/bi961970v }}
*{{cite journal | author=Stoeckler JD, Poirot AF, Smith RM, ''et al.'' |title=Purine nucleoside phosphorylase. 3. Reversal of purine base specificity by site-directed mutagenesis. |journal=Biochemistry |volume=36 |issue= 39 |pages= 11749-56 |year= 1997 |pmid= 9305964 |doi= 10.1021/bi961971n }}
*{{cite journal | author=Sasaki Y, Iseki M, Yamaguchi S, ''et al.'' |title=Direct evidence of autosomal recessive inheritance of Arg24 to termination codon in purine nucleoside phosphorylase gene in a family with a severe combined immunodeficiency patient. |journal=Hum. Genet. |volume=103 |issue= 1 |pages= 81-5 |year= 1998 |pmid= 9737781 |doi= }}
*{{cite journal | author=Sheppard TL, Ordoukhanian P, Joyce GF |title=A DNA enzyme with N-glycosylase activity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 14 |pages= 7802-7 |year= 2000 |pmid= 10884411 |doi= }}
*{{cite journal | author=Dalal I, Grunebaum E, Cohen A, Roifman CM |title=Two novel mutations in a purine nucleoside phosphorylase (PNP)-deficient patient. |journal=Clin. Genet. |volume=59 |issue= 6 |pages= 430-7 |year= 2001 |pmid= 11453975 |doi= }}
*{{cite journal | author=Ivings L, Pennington SR, Jenkins R, ''et al.'' |title=Identification of Ca2+-dependent binding partners for the neuronal calcium sensor protein neurocalcin delta: interaction with actin, clathrin and tubulin. |journal=Biochem. J. |volume=363 |issue= Pt 3 |pages= 599-608 |year= 2002 |pmid= 11964161 |doi= }}
*{{cite journal | author=Falkenberg M, Gaspari M, Rantanen A, ''et al.'' |title=Mitochondrial transcription factors B1 and B2 activate transcription of human mtDNA. |journal=Nat. Genet. |volume=31 |issue= 3 |pages= 289-94 |year= 2002 |pmid= 12068295 |doi= 10.1038/ng909 }}
*{{cite journal | author=Stoychev G, Kierdaszuk B, Shugar D |title=Xanthosine and xanthine. Substrate properties with purine nucleoside phosphorylases, and relevance to other enzyme systems. |journal=Eur. J. Biochem. |volume=269 |issue= 16 |pages= 4048-57 |year= 2002 |pmid= 12180982 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NPPC... {November 20, 2007 11:29:50 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:30:32 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Natriuretic peptide precursor C
| HGNCid = 7941
| Symbol = NPPC
| AltSymbols =; CNP
| OMIM = 600296
| ECnumber =
| Homologene = 7867
| MGIid = 97369
| GeneAtlas_image1 = PBB_GE_NPPC_221348_at_tn.png
| Function = {{GNF_GO|id=GO:0005179 |text = hormone activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006182 |text = cGMP biosynthetic process}} {{GNF_GO|id=GO:0008217 |text = blood pressure regulation}} {{GNF_GO|id=GO:0019229 |text = regulation of vasoconstriction}} {{GNF_GO|id=GO:0050880 |text = regulation of blood vessel size}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4880
| Hs_Ensembl = ENSG00000163273
| Hs_RefseqProtein = NP_077720
| Hs_RefseqmRNA = NM_024409
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 232498379
| Hs_GenLoc_end = 232499203
| Hs_Uniprot = P23582
| Mm_EntrezGene = 18159
| Mm_Ensembl = ENSMUSG00000026241
| Mm_RefseqmRNA = NM_010933
| Mm_RefseqProtein = NP_035063
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 88497462
| Mm_GenLoc_end = 88501743
| Mm_Uniprot = Q544K5
}}
}}
'''Natriuretic peptide precursor C''', also known as '''NPPC''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NPPC natriuretic peptide precursor C| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4880| 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 = Natriuretic peptides comprise a family of 3 structurally related molecules: atrial natriuretic peptide (ANP; MIM 108780), brain natriuretic peptide (BNP; MIM 600295), and C-type natriuretic peptide, CNP, encoded by a gene symbolized NPPC. These peptides possess potent natriuretic, diuretic, and vasodilating activities and are implicated in body fluid homeostasis and blood pressure control.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: NPPC natriuretic peptide precursor C| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4880| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schulz S |title=C-type natriuretic peptide and guanylyl cyclase B receptor. |journal=Peptides |volume=26 |issue= 6 |pages= 1024-34 |year= 2005 |pmid= 15911070 |doi= 10.1016/j.peptides.2004.08.027 }}
*{{cite journal | author=Suga S, Nakao K, Hosoda K, ''et al.'' |title=Receptor selectivity of natriuretic peptide family, atrial natriuretic peptide, brain natriuretic peptide, and C-type natriuretic peptide. |journal=Endocrinology |volume=130 |issue= 1 |pages= 229-39 |year= 1992 |pmid= 1309330 |doi= }}
*{{cite journal | author=Ogawa Y, Nakao K, Nakagawa O, ''et al.'' |title=Human C-type natriuretic peptide. Characterization of the gene and peptide. |journal=Hypertension |volume=19 |issue= 6 Pt 2 |pages= 809-13 |year= 1992 |pmid= 1339402 |doi= }}
*{{cite journal | author=Ishizaka Y, Kangawa K, Minamino N, ''et al.'' |title=Isolation and identification of C-type natriuretic peptide in human monocytic cell line, THP-1. |journal=Biochem. Biophys. Res. Commun. |volume=189 |issue= 2 |pages= 697-704 |year= 1993 |pmid= 1472040 |doi= }}
*{{cite journal | author=Komatsu Y, Nakao K, Suga S, ''et al.'' |title=C-type natriuretic peptide (CNP) in rats and humans. |journal=Endocrinology |volume=129 |issue= 2 |pages= 1104-6 |year= 1991 |pmid= 1855454 |doi= }}
*{{cite journal | author=Tawaragi Y, Fuchimura K, Tanaka S, ''et al.'' |title=Gene and precursor structures of human C-type natriuretic peptide. |journal=Biochem. Biophys. Res. Commun. |volume=175 |issue= 2 |pages= 645-51 |year= 1991 |pmid= 2018508 |doi= }}
*{{cite journal | author=Ogawa Y, Itoh H, Yoshitake Y, ''et al.'' |title=Molecular cloning and chromosomal assignment of the mouse C-type natriuretic peptide (CNP) gene (Nppc): comparison with the human CNP gene (NPPC). |journal=Genomics |volume=24 |issue= 2 |pages= 383-7 |year= 1995 |pmid= 7698765 |doi= 10.1006/geno.1994.1633 }}
*{{cite journal | author=Kaneko T, Shirakami G, Nakao K, ''et al.'' |title=C-type natriuretic peptide (CNP) is the major natriuretic peptide in human cerebrospinal fluid. |journal=Brain Res. |volume=612 |issue= 1-2 |pages= 104-9 |year= 1993 |pmid= 8330189 |doi= }}
*{{cite journal | author=Wei CM, Heublein DM, Perrella MA, ''et al.'' |title=Natriuretic peptide system in human heart failure. |journal=Circulation |volume=88 |issue= 3 |pages= 1004-9 |year= 1993 |pmid= 8353861 |doi= }}
*{{cite journal | author=Igaki T, Itoh H, Suga S, ''et al.'' |title=Insulin suppresses endothelial secretion of C-type natriuretic peptide, a novel endothelium-derived relaxing peptide. |journal=Diabetes |volume=45 Suppl 3 |issue= |pages= S62-4 |year= 1996 |pmid= 8674895 |doi= }}
*{{cite journal | author=Igaki T, Itoh H, Suga S, ''et al.'' |title=C-type natriuretic peptide in chronic renal failure and its action in humans. |journal=Kidney Int. Suppl. |volume=55 |issue= |pages= S144-7 |year= 1996 |pmid= 8743538 |doi= }}
*{{cite journal | author=Vollmar AM, Paumgartner G, Gerbes AL |title=Differential gene expression of the three natriuretic peptides and natriuretic peptide receptor subtypes in human liver. |journal=Gut |volume=40 |issue= 1 |pages= 145-50 |year= 1997 |pmid= 9155593 |doi= }}
*{{cite journal | author=Watanabe Y, Nakajima K, Shimamori Y, Fujimoto Y |title=Comparison of the hydrolysis of the three types of natriuretic peptides by human kidney neutral endopeptidase 24.11. |journal=Biochem. Mol. Med. |volume=61 |issue= 1 |pages= 47-51 |year= 1997 |pmid= 9232196 |doi= }}
*{{cite journal | author=He Xl , Chow Dc , Martick MM, Garcia KC |title=Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone. |journal=Science |volume=293 |issue= 5535 |pages= 1657-62 |year= 2001 |pmid= 11533490 |doi= 10.1126/science.1062246 }}
*{{cite journal | author=Cataliotti A, Giordano M, De Pascale E, ''et al.'' |title=CNP production in the kidney and effects of protein intake restriction in nephrotic syndrome. |journal=Am. J. Physiol. Renal Physiol. |volume=283 |issue= 3 |pages= F464-72 |year= 2002 |pmid= 12167597 |doi= 10.1152/ajprenal.00372.2001 }}
*{{cite journal | author=Evans JJ, Youssef AH, Yandle TG, ''et al.'' |title=Effects of endothelin-1 on release of adrenomedullin and C-type natriuretic peptide from individual human vascular endothelial cells. |journal=J. Endocrinol. |volume=175 |issue= 1 |pages= 225-32 |year= 2002 |pmid= 12379507 |doi= }}
*{{cite journal | author=Ono K, Mannami T, Baba S, ''et al.'' |title=A single-nucleotide polymorphism in C-type natriuretic peptide gene may be associated with hypertension. |journal=Hypertens. Res. |volume=25 |issue= 5 |pages= 727-30 |year= 2003 |pmid= 12452325 |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=Hirsch JR, Skutta N, Schlatter E |title=Signaling and distribution of NPR-Bi, the human splice form of the natriuretic peptide receptor type B. |journal=Am. J. Physiol. Renal Physiol. |volume=285 |issue= 2 |pages= F370-4 |year= 2003 |pmid= 12709393 |doi= 10.1152/ajprenal.00049.2003 }}
*{{cite journal | author=Wu C, Wu F, Pan J, ''et al.'' |title=Furin-mediated processing of Pro-C-type natriuretic peptide. |journal=J. Biol. Chem. |volume=278 |issue= 28 |pages= 25847-52 |year= 2003 |pmid= 12736257 |doi= 10.1074/jbc.M301223200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PCM1... {November 20, 2007 11:30:32 PM PST}
- CREATE: Found no pages, creating new page. {November 20, 2007 11:32:32 PM PST}
- CREATED: Created new protein page: PCM1 {November 20, 2007 11:32:40 PM PST}
- INFO: Beginning work on PLSCR1... {November 20, 2007 11:33:55 PM PST}
- CREATE: Found no pages, creating new page. {November 20, 2007 11:34:49 PM PST}
- CREATED: Created new protein page: PLSCR1 {November 20, 2007 11:34:57 PM PST}
- INFO: Beginning work on PPOX... {November 20, 2007 11:34:57 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:35:40 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Protoporphyrinogen oxidase
| HGNCid = 9280
| Symbol = PPOX
| AltSymbols =; VP; MGC8485; PPO; V290M
| OMIM = 600923
| ECnumber =
| Homologene = 262
| MGIid = 104968
| GeneAtlas_image1 = PBB_GE_PPOX_204788_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004729 |text = protoporphyrinogen oxidase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0050660 |text = FAD binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0031304 |text = intrinsic to mitochondrial inner membrane}} {{GNF_GO|id=GO:0031966 |text = mitochondrial membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006783 |text = heme biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5498
| Hs_Ensembl = ENSG00000143224
| Hs_RefseqProtein = NP_000300
| Hs_RefseqmRNA = NM_000309
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 159402818
| Hs_GenLoc_end = 159407634
| Hs_Uniprot = P50336
| Mm_EntrezGene = 19044
| Mm_Ensembl = ENSMUSG00000062729
| Mm_RefseqmRNA = NM_008911
| Mm_RefseqProtein = NP_032937
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 173113667
| Mm_GenLoc_end = 173117835
| Mm_Uniprot = Q3UQA3
}}
}}
'''Protoporphyrinogen oxidase''', also known as '''PPOX''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PPOX protoporphyrinogen oxidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5498| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes the penultimate enzyme of heme biosynthesis, which catalyzes the 6-electron oxidation of protoporphyrinogen IX to form protoporphyrin IX. This protein is a flavoprotein associated with the outer surface of the inner mitochondrial membrane. Mutations in this gene cause variegate porphyria.<ref name="entrez">{{cite web | title = Entrez Gene: PPOX protoporphyrinogen oxidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5498| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nishimura K, Taketani S, Inokuchi H |title=Cloning of a human cDNA for protoporphyrinogen oxidase by complementation in vivo of a hemG mutant of Escherichia coli. |journal=J. Biol. Chem. |volume=270 |issue= 14 |pages= 8076-80 |year= 1995 |pmid= 7713909 |doi= }}
*{{cite journal | author=Dailey TA, Meissner P, Dailey HA |title=Expression of a cloned protoporphyrinogen oxidase. |journal=J. Biol. Chem. |volume=269 |issue= 2 |pages= 813-5 |year= 1994 |pmid= 8288631 |doi= }}
*{{cite journal | author=Dailey TA, Dailey HA, Meissner P, Prasad AR |title=Cloning, sequence, and expression of mouse protoporphyrinogen oxidase. |journal=Arch. Biochem. Biophys. |volume=324 |issue= 2 |pages= 379-84 |year= 1996 |pmid= 8554330 |doi= 10.1006/abbi.1995.0051 }}
*{{cite journal | author=Taketani S, Inazawa J, Abe T, ''et al.'' |title=The human protoporphyrinogen oxidase gene (PPOX): organization and location to chromosome 1. |journal=Genomics |volume=29 |issue= 3 |pages= 698-703 |year= 1996 |pmid= 8575762 |doi= 10.1006/geno.1995.9949 }}
*{{cite journal | author=Meissner PN, Dailey TA, Hift RJ, ''et al.'' |title=A R59W mutation in human protoporphyrinogen oxidase results in decreased enzyme activity and is prevalent in South Africans with variegate porphyria. |journal=Nat. Genet. |volume=13 |issue= 1 |pages= 95-7 |year= 1996 |pmid= 8673113 |doi= 10.1038/ng0596-95 }}
*{{cite journal | author=Dailey TA, Dailey HA |title=Human protoporphyrinogen oxidase: expression, purification, and characterization of the cloned enzyme. |journal=Protein Sci. |volume=5 |issue= 1 |pages= 98-105 |year= 1996 |pmid= 8771201 |doi= }}
*{{cite journal | author=Puy H, Robréau AM, Rosipal R, ''et al.'' |title=Protoporphyrinogen oxidase: complete genomic sequence and polymorphisms in the human gene. |journal=Biochem. Biophys. Res. Commun. |volume=226 |issue= 1 |pages= 226-30 |year= 1996 |pmid= 8806618 |doi= 10.1006/bbrc.1996.1337 }}
*{{cite journal | author=Deybach JC, Puy H, Robréau AM, ''et al.'' |title=Mutations in the protoporphyrinogen oxidase gene in patients with variegate porphyria. |journal=Hum. Mol. Genet. |volume=5 |issue= 3 |pages= 407-10 |year= 1997 |pmid= 8852667 |doi= }}
*{{cite journal | author=Lam H, Dragan L, Tsou HC, ''et al.'' |title=Molecular basis of variegate porphyria: a de novo insertion mutation in the protoporphyrinogen oxidase gene. |journal=Hum. Genet. |volume=99 |issue= 1 |pages= 126-9 |year= 1997 |pmid= 9003509 |doi= }}
*{{cite journal | author=Dailey HA, Dailey TA |title=Characteristics of human protoporphyrinogen oxidase in controls and variegate porphyrias. |journal=Cell. Mol. Biol. (Noisy-le-grand) |volume=43 |issue= 1 |pages= 67-73 |year= 1997 |pmid= 9074790 |doi= }}
*{{cite journal | author=Frank J, Poh-Fitzpatrick MB, King LE, Christiano AM |title=The genetic basis of "Scarsdale Gourmet Diet" variegate porphyria: a missense mutation in the protoporphyrinogen oxidase gene. |journal=Arch. Dermatol. Res. |volume=290 |issue= 8 |pages= 441-5 |year= 1998 |pmid= 9763307 |doi= }}
*{{cite journal | author=Roberts AG, Puy H, Dailey TA, ''et al.'' |title=Molecular characterization of homozygous variegate porphyria. |journal=Hum. Mol. Genet. |volume=7 |issue= 12 |pages= 1921-5 |year= 1998 |pmid= 9811936 |doi= }}
*{{cite journal | author=Frank J, McGrath JA, Poh-Fitzpatrick MB, ''et al.'' |title=Mutations in the translation initiation codon of the protoporphyrinogen oxidase gene underlie variegate porphyria. |journal=Clin. Exp. Dermatol. |volume=24 |issue= 4 |pages= 296-301 |year= 1999 |pmid= 10457135 |doi= }}
*{{cite journal | author=Whatley SD, Puy H, Morgan RR, ''et al.'' |title=Variegate porphyria in Western Europe: identification of PPOX gene mutations in 104 families, extent of allelic heterogeneity, and absence of correlation between phenotype and type of mutation. |journal=Am. J. Hum. Genet. |volume=65 |issue= 4 |pages= 984-94 |year= 2000 |pmid= 10486317 |doi= }}
*{{cite journal | author=Suzuki Y, Ishihara D, Sasaki M, ''et al.'' |title=Statistical analysis of the 5' untranslated region of human mRNA using "Oligo-Capped" cDNA libraries. |journal=Genomics |volume=64 |issue= 3 |pages= 286-97 |year= 2000 |pmid= 10756096 |doi= 10.1006/geno.2000.6076 }}
*{{cite journal | author=Corrigall AV, Hift RJ, Davids LM, ''et al.'' |title=Homozygous variegate porphyria in South Africa: genotypic analysis in two cases. |journal=Mol. Genet. Metab. |volume=69 |issue= 4 |pages= 323-30 |year= 2000 |pmid= 10870850 |doi= 10.1006/mgme.2000.2975 }}
*{{cite journal | author=Kauppinen R, Timonen K, von und zu Fraunberg M, ''et al.'' |title=Homozygous variegate porphyria: 20 y follow-up and characterization of molecular defect. |journal=J. Invest. Dermatol. |volume=116 |issue= 4 |pages= 610-3 |year= 2001 |pmid= 11286631 |doi= 10.1046/j.1523-1747.2001.01293.x }}
*{{cite journal | author=Palmer RA, Elder GH, Barrett DF, Keohane SG |title=Homozygous variegate porphyria: a compound heterozygote with novel mutations in the protoporphyrinogen oxidase gene. |journal=Br. J. Dermatol. |volume=144 |issue= 4 |pages= 866-9 |year= 2001 |pmid= 11298551 |doi= }}
*{{cite journal | author=Corrigall AV, Hift RJ, Davids LM, ''et al.'' |title=Identification of the first variegate porphyria mutation in an indigenous black South African and further evidence for heterogeneity in variegate porphyria. |journal=Mol. Genet. Metab. |volume=73 |issue= 1 |pages= 91-6 |year= 2001 |pmid= 11350188 |doi= 10.1006/mgme.2001.3163 }}
*{{cite journal | author=Donnelly JG, Detombe S, Hindmarsh JT |title=Single-strand conformational polymorphism and denaturing gradient gel electrophoresis in screening for variegate porphyria: identification of two new mutations. |journal=Ann. Clin. Lab. Sci. |volume=32 |issue= 2 |pages= 107-13 |year= 2002 |pmid= 12017191 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PPP2R5C... {November 20, 2007 11:35:40 PM PST}
- UPLOAD: Added new Image to wiki: File:PBB Protein PPP2R5C image.jpg {November 20, 2007 11:37:09 PM PST}
- CREATE: Found no pages, creating new page. {November 20, 2007 11:37:24 PM PST}
- CREATED: Created new protein page: PPP2R5C {November 20, 2007 11:37:32 PM PST}
- INFO: Beginning work on PSMD3... {November 20, 2007 11:37:32 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:40:05 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Proteasome (prosome, macropain) 26S subunit, non-ATPase, 3
| HGNCid = 9560
| Symbol = PSMD3
| AltSymbols =; P58; RPN3; S3
| OMIM =
| ECnumber =
| Homologene = 2102
| MGIid = 98858
| GeneAtlas_image1 = PBB_GE_PSMD3_201388_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0000502 |text = proteasome complex (sensu Eukaryota)}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0043234 |text = protein complex}}
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5709
| Hs_Ensembl = ENSG00000108344
| Hs_RefseqProtein = NP_002800
| Hs_RefseqmRNA = NM_002809
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 35390586
| Hs_GenLoc_end = 35407738
| Hs_Uniprot = O43242
| Mm_EntrezGene = 22123
| Mm_Ensembl = ENSMUSG00000017221
| Mm_RefseqmRNA = NM_009439
| Mm_RefseqProtein = NP_033465
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 98498644
| Mm_GenLoc_end = 98512068
| Mm_Uniprot = Q3TP95
}}
}}
'''Proteasome (prosome, macropain) 26S subunit, non-ATPase, 3''', also known as '''PSMD3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMD3 proteasome (prosome, macropain) 26S subunit, non-ATPase, 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5709| 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. This gene encodes one of the non-ATPase subunits of the 19S regulator lid.<ref name="entrez">{{cite web | title = Entrez Gene: PSMD3 proteasome (prosome, macropain) 26S subunit, non-ATPase, 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5709| 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=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=Kominami K, Okura N, Kawamura M, ''et al.'' |title=Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1. |journal=Mol. Biol. Cell |volume=8 |issue= 1 |pages= 171-87 |year= 1997 |pmid= 9017604 |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=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=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=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 }}
*{{cite journal | author=Huang X, Seifert U, Salzmann U, ''et al.'' |title=The RTP site shared by the HIV-1 Tat protein and the 11S regulator subunit alpha is crucial for their effects on proteasome function including antigen processing. |journal=J. Mol. Biol. |volume=323 |issue= 4 |pages= 771-82 |year= 2002 |pmid= 12419264 |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=Gaddis NC, Chertova E, Sheehy AM, ''et al.'' |title=Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions. |journal=J. Virol. |volume=77 |issue= 10 |pages= 5810-20 |year= 2003 |pmid= 12719574 |doi= }}
*{{cite journal | author=Lecossier D, Bouchonnet F, Clavel F, Hance AJ |title=Hypermutation of HIV-1 DNA in the absence of the Vif protein. |journal=Science |volume=300 |issue= 5622 |pages= 1112 |year= 2003 |pmid= 12750511 |doi= 10.1126/science.1083338 }}
*{{cite journal | author=Zhang H, Yang B, Pomerantz RJ, ''et al.'' |title=The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. |journal=Nature |volume=424 |issue= 6944 |pages= 94-8 |year= 2003 |pmid= 12808465 |doi= 10.1038/nature01707 }}
*{{cite journal | author=Mangeat B, Turelli P, Caron G, ''et al.'' |title=Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. |journal=Nature |volume=424 |issue= 6944 |pages= 99-103 |year= 2003 |pmid= 12808466 |doi= 10.1038/nature01709 }}
*{{cite journal | author=Harris RS, Bishop KN, Sheehy AM, ''et al.'' |title=DNA deamination mediates innate immunity to retroviral infection. |journal=Cell |volume=113 |issue= 6 |pages= 803-9 |year= 2003 |pmid= 12809610 |doi= }}
*{{cite journal | author=Harris RS, Sheehy AM, Craig HM, ''et al.'' |title=DNA deamination: not just a trigger for antibody diversification but also a mechanism for defense against retroviruses. |journal=Nat. Immunol. |volume=4 |issue= 7 |pages= 641-3 |year= 2003 |pmid= 12830140 |doi= 10.1038/ni0703-641 }}
*{{cite journal | author=Gu Y, Sundquist WI |title=Good to CU. |journal=Nature |volume=424 |issue= 6944 |pages= 21-2 |year= 2003 |pmid= 12840737 |doi= 10.1038/424021a }}
*{{cite journal | author=Mariani R, Chen D, Schröfelbauer B, ''et al.'' |title=Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif. |journal=Cell |volume=114 |issue= 1 |pages= 21-31 |year= 2003 |pmid= 12859895 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PVRL2... {November 20, 2007 11:40:05 PM PST}
- CREATE: Found no pages, creating new page. {November 20, 2007 11:40:58 PM PST}
- CREATED: Created new protein page: PVRL2 {November 20, 2007 11:41:08 PM PST}
- INFO: Beginning work on QDPR... {November 20, 2007 11:41:08 PM PST}
- UPLOAD: Added new Image to wiki: File:PBB Protein QDPR image.jpg {November 20, 2007 11:41:42 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:41:58 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_QDPR_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dhr.
| PDB = {{PDB2|1dhr}}, {{PDB2|1dir}}, {{PDB2|1hdr}}
| Name = Quinoid dihydropteridine reductase
| HGNCid = 9752
| Symbol = QDPR
| AltSymbols =; DHPR; FLJ42391; PKU2
| OMIM = 261630
| ECnumber =
| Homologene = 271
| MGIid = 97836
| GeneAtlas_image1 = PBB_GE_QDPR_209123_at_tn.png
| Function = {{GNF_GO|id=GO:0004155 |text = 6,7-dihydropteridine reductase activity}} {{GNF_GO|id=GO:0009055 |text = electron carrier activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006520 |text = amino acid metabolic process}} {{GNF_GO|id=GO:0006559 |text = L-phenylalanine catabolic process}} {{GNF_GO|id=GO:0006729 |text = tetrahydrobiopterin biosynthetic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0051066 |text = dihydrobiopterin metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5860
| Hs_Ensembl = ENSG00000151552
| Hs_RefseqProtein = NP_000311
| Hs_RefseqmRNA = NM_000320
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 17097119
| Hs_GenLoc_end = 17122955
| Hs_Uniprot = P09417
| Mm_EntrezGene = 110391
| Mm_Ensembl = ENSMUSG00000015806
| Mm_RefseqmRNA = NM_024236
| Mm_RefseqProtein = NP_077198
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 45722300
| Mm_GenLoc_end = 45738429
| Mm_Uniprot = Q8BVI4
}}
}}
'''Quinoid dihydropteridine reductase''', also known as '''QDPR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: QDPR quinoid dihydropteridine reductase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5860| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes the enzyme dihydropteridine reductase, which catalyzes the NADH-mediated reduction of quinonoid dihydrobiopterin. This enzyme is an essential component of the pterin-dependent aromatic amino acid hydroxylating systems. Mutations in this gene resulting in QDPR deficiency include aberrant splicing, amino acid substitutions, insertions, or premature terminations. Dihydropteridine reductase deficiency presents as atypical phenylketonuria due to insufficient production of biopterin, a cofactor for phenylalanine hydroxylase.<ref name="entrez">{{cite web | title = Entrez Gene: QDPR quinoid dihydropteridine reductase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5860| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Smooker PM, Cotton RG |title=Molecular basis of dihydropteridine reductase deficiency. |journal=Hum. Mutat. |volume=5 |issue= 4 |pages= 279-84 |year= 1995 |pmid= 7627180 |doi= 10.1002/humu.1380050402 }}
*{{cite journal | author=Kaufman S, Holtzman NA, Milstien S, ''et al.'' |title=Phenylketonuria due to a deficiency of dihydropteridine reductase. |journal=N. Engl. J. Med. |volume=293 |issue= 16 |pages= 785-90 |year= 1975 |pmid= 1160969 |doi= }}
*{{cite journal | author=Howells DW, Forrest SM, Dahl HH, Cotton RG |title=Insertion of an extra codon for threonine is a cause of dihydropteridine reductase deficiency. |journal=Am. J. Hum. Genet. |volume=47 |issue= 2 |pages= 279-85 |year= 1990 |pmid= 2116088 |doi= }}
*{{cite journal | author=Sumi S, Ishikawa T, Ito Y, ''et al.'' |title=Probable assignment of the dihydropteridine reductase gene to 4p15.31. |journal=Tohoku J. Exp. Med. |volume=160 |issue= 1 |pages= 93-4 |year= 1990 |pmid= 2330583 |doi= }}
*{{cite journal | author=Dahl HH, Hutchison W, McAdam W, ''et al.'' |title=Human dihydropteridine reductase: characterisation of a cDNA clone and its use in analysis of patients with dihydropteridine reductase deficiency. |journal=Nucleic Acids Res. |volume=15 |issue= 5 |pages= 1921-32 |year= 1987 |pmid= 3031582 |doi= }}
*{{cite journal | author=Lockyer J, Cook RG, Milstien S, ''et al.'' |title=Structure and expression of human dihydropteridine reductase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 10 |pages= 3329-33 |year= 1987 |pmid= 3033643 |doi= }}
*{{cite journal | author=Altmann P, Al-Salihi F, Butter K, ''et al.'' |title=Serum aluminum levels and erythrocyte dihydropteridine reductase activity in patients on hemodialysis. |journal=N. Engl. J. Med. |volume=317 |issue= 2 |pages= 80-4 |year= 1987 |pmid= 3587329 |doi= }}
*{{cite journal | author=Brown RM, Dahl HH |title=Localization of the human dihydropteridine reductase gene to band p15.3 of chromosome 4 by in situ hybridization. |journal=Genomics |volume=1 |issue= 1 |pages= 67-70 |year= 1987 |pmid= 3666748 |doi= }}
*{{cite journal | author=Nakanishi N, Hasegawa H, Yamada S, Akino M |title=Purification and physicochemical properties of NADPH-specific dihydropteridine reductase from bovine and human livers. |journal=J. Biochem. |volume=99 |issue= 3 |pages= 635-44 |year= 1986 |pmid= 3711039 |doi= }}
*{{cite journal | author=Armarego WL, Ohnishi A, Taguchi H |title=New pteridine substrates for dihydropteridine reductase and horseradish peroxidase. |journal=Biochem. J. |volume=234 |issue= 2 |pages= 335-42 |year= 1986 |pmid= 3718470 |doi= }}
*{{cite journal | author=Shen RS, Smith RV, Davis PJ, Abell CW |title=Inhibition of dihydropteridine reductase from human liver and rat striatal synaptosomes by apomorphine and its analogs. |journal=J. Biol. Chem. |volume=259 |issue= 14 |pages= 8994-9000 |year= 1984 |pmid= 6746636 |doi= }}
*{{cite journal | author=Firgaira FA, Choo KH, Cotton RG, Danks DM |title=Molecular and immunological comparison of human dihydropteridine reductase in liver, cultured fibroblasts and continuous lymphoid cells. |journal=Biochem. J. |volume=197 |issue= 1 |pages= 45-53 |year= 1982 |pmid= 6797415 |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=Katoh S, Sueoka T, Yamamoto Y, Takahashi SY |title=Phosphorylation by Ca2+/calmodulin-dependent protein kinase II and protein kinase C of sepiapterin reductase, the terminal enzyme in the biosynthetic pathway of tetrahydrobiopterin. |journal=FEBS Lett. |volume=341 |issue= 2-3 |pages= 227-32 |year= 1994 |pmid= 8137944 |doi= }}
*{{cite journal | author=Su Y, Varughese KI, Xuong NH, ''et al.'' |title=The crystallographic structure of a human dihydropteridine reductase NADH binary complex expressed in Escherichia coli by a cDNA constructed from its rat homologue. |journal=J. Biol. Chem. |volume=268 |issue= 36 |pages= 26836-41 |year= 1994 |pmid= 8262916 |doi= }}
*{{cite journal | author=Dianzani I, Howells DW, Ponzone A, ''et al.'' |title=Two new mutations in the dihydropteridine reductase gene in patients with tetrahydrobiopterin deficiency. |journal=J. Med. Genet. |volume=30 |issue= 6 |pages= 465-9 |year= 1993 |pmid= 8326489 |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=Lin CM, Tan Y, Lee YM, ''et al.'' |title=Expression of human phenylalanine hydroxylase activity in T lymphocytes of classical phenylketonuria children by retroviral-mediated gene transfer. |journal=J. Inherit. Metab. Dis. |volume=20 |issue= 6 |pages= 742-54 |year= 1998 |pmid= 9427141 |doi= }}
*{{cite journal | author=Dianzani I, de Sanctis L, Smooker PM, ''et al.'' |title=Dihydropteridine reductase deficiency: physical structure of the QDPR gene, identification of two new mutations and genotype-phenotype correlations. |journal=Hum. Mutat. |volume=12 |issue= 4 |pages= 267-73 |year= 1998 |pmid= 9744478 |doi= 10.1002/(SICI)1098-1004(1998)12:4<267::AID-HUMU8>3.0.CO;2-C }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RANGAP1... {November 20, 2007 11:41:58 PM PST}
- UPLOAD: Added new Image to wiki: File:PBB Protein RANGAP1 image.jpg {November 20, 2007 11:42:50 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:43:06 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_RANGAP1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1z5s.
| PDB = {{PDB2|1z5s}}, {{PDB2|2grn}}, {{PDB2|2gro}}, {{PDB2|2grp}}, {{PDB2|2grq}}, {{PDB2|2grr}}, {{PDB2|2io2}}, {{PDB2|2io3}}, {{PDB2|2iy0}}
| Name = Ran GTPase activating protein 1
| HGNCid = 9854
| Symbol = RANGAP1
| AltSymbols =; Fug1; KIAA1835; MGC20266; SD
| OMIM = 602362
| ECnumber =
| Homologene = 55700
| MGIid = 103071
| GeneAtlas_image1 = PBB_GE_RANGAP1_212125_at_tn.png
| GeneAtlas_image2 = PBB_GE_RANGAP1_212127_at_tn.png
| Function = {{GNF_GO|id=GO:0005096 |text = GTPase activator activity}} {{GNF_GO|id=GO:0005098 |text = Ran GTPase activator activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005643 |text = nuclear pore}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0048471 |text = perinuclear region of cytoplasm}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5905
| Hs_Ensembl = ENSG00000100401
| Hs_RefseqProtein = NP_002874
| Hs_RefseqmRNA = NM_002883
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 39971562
| Hs_GenLoc_end = 40028909
| Hs_Uniprot = P46060
| Mm_EntrezGene = 19387
| Mm_Ensembl = ENSMUSG00000022391
| Mm_RefseqmRNA = NM_011241
| Mm_RefseqProtein = NP_035371
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 81531509
| Mm_GenLoc_end = 81557138
| Mm_Uniprot = Q3UZD8
}}
}}
'''Ran GTPase activating protein 1''', also known as '''RANGAP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RANGAP1 Ran GTPase activating protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5905| 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 = RanGAP1, is a homodimeric 65-kD polypeptide that specifically induces the GTPase activity of RAN, but not of RAS by over 1,000-fold. RanGAP1 is the immediate antagonist of RCC1, a regulator molecule that keeps RAN in the active, GTP-bound state. The RANGAP1 gene encodes a 587-amino acid polypeptide. The sequence is unrelated to that of GTPase activators for other RAS-related proteins, but is 88% identical to Fug1, the murine homolog of yeast Rna1p. RanGAP1 and RCC1 control RAN-dependent transport between the nucleus and cytoplasm. RanGAP1 is a key regulator of the RAN GTP/GDP cycle.<ref name="entrez">{{cite web | title = Entrez Gene: RANGAP1 Ran GTPase activating protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5905| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Becker J, Melchior F, Gerke V, ''et al.'' |title=RNA1 encodes a GTPase-activating protein specific for Gsp1p, the Ran/TC4 homologue of Saccharomyces cerevisiae. |journal=J. Biol. Chem. |volume=270 |issue= 20 |pages= 11860-5 |year= 1995 |pmid= 7744835 |doi= }}
*{{cite journal | author=Bischoff FR, Krebber H, Kempf T, ''et al.'' |title=Human RanGTPase-activating protein RanGAP1 is a homologue of yeast Rna1p involved in mRNA processing and transport. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 5 |pages= 1749-53 |year= 1995 |pmid= 7878053 |doi= }}
*{{cite journal | author=Bischoff FR, Klebe C, Kretschmer J, ''et al.'' |title=RanGAP1 induces GTPase activity of nuclear Ras-related Ran. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 7 |pages= 2587-91 |year= 1994 |pmid= 8146159 |doi= }}
*{{cite journal | author=Krebber H, Ponstingl H |title=Ubiquitous expression and testis-specific alternative polyadenylation of mRNA for the human Ran GTPase activator RanGAP1. |journal=Gene |volume=180 |issue= 1-2 |pages= 7-11 |year= 1997 |pmid= 8973340 |doi= }}
*{{cite journal | author=Matunis MJ, Coutavas E, Blobel G |title=A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. |journal=J. Cell Biol. |volume=135 |issue= 6 Pt 1 |pages= 1457-70 |year= 1997 |pmid= 8978815 |doi= }}
*{{cite journal | author=Mahajan R, Delphin C, Guan T, ''et al.'' |title=A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. |journal=Cell |volume=88 |issue= 1 |pages= 97-107 |year= 1997 |pmid= 9019411 |doi= }}
*{{cite journal | author=Görlich D, Dabrowski M, Bischoff FR, ''et al.'' |title=A novel class of RanGTP binding proteins. |journal=J. Cell Biol. |volume=138 |issue= 1 |pages= 65-80 |year= 1997 |pmid= 9214382 |doi= }}
*{{cite journal | author=Scheffzek K, Ahmadian MR, Kabsch W, ''et al.'' |title=The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. |journal=Science |volume=277 |issue= 5324 |pages= 333-8 |year= 1998 |pmid= 9219684 |doi= }}
*{{cite journal | author=Mahajan R, Gerace L, Melchior F |title=Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association. |journal=J. Cell Biol. |volume=140 |issue= 2 |pages= 259-70 |year= 1998 |pmid= 9442102 |doi= }}
*{{cite journal | author=Kamitani T, Kito K, Nguyen HP, ''et al.'' |title=Characterization of a second member of the sentrin family of ubiquitin-like proteins. |journal=J. Biol. Chem. |volume=273 |issue= 18 |pages= 11349-53 |year= 1998 |pmid= 9556629 |doi= }}
*{{cite journal | author=Okuma T, Honda R, Ichikawa G, ''et al.'' |title=In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2. |journal=Biochem. Biophys. Res. Commun. |volume=254 |issue= 3 |pages= 693-8 |year= 1999 |pmid= 9920803 |doi= 10.1006/bbrc.1998.9995 }}
*{{cite journal | author=Hillig RC, Renault L, Vetter IR, ''et al.'' |title=The crystal structure of rna1p: a new fold for a GTPase-activating protein. |journal=Mol. Cell |volume=3 |issue= 6 |pages= 781-91 |year= 1999 |pmid= 10394366 |doi= }}
*{{cite journal | author=Dunham I, Shimizu N, Roe BA, ''et al.'' |title=The DNA sequence of human chromosome 22. |journal=Nature |volume=402 |issue= 6761 |pages= 489-95 |year= 1999 |pmid= 10591208 |doi= 10.1038/990031 }}
*{{cite journal | author=Nagase T, Nakayama M, Nakajima D, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=8 |issue= 2 |pages= 85-95 |year= 2001 |pmid= 11347906 |doi= }}
*{{cite journal | author=Bernier-Villamor V, Sampson DA, Matunis MJ, Lima CD |title=Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1. |journal=Cell |volume=108 |issue= 3 |pages= 345-56 |year= 2002 |pmid= 11853669 |doi= }}
*{{cite journal | author=Joseph J, Tan SH, Karpova TS, ''et al.'' |title=SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles. |journal=J. Cell Biol. |volume=156 |issue= 4 |pages= 595-602 |year= 2002 |pmid= 11854305 |doi= 10.1083/jcb.200110109 }}
*{{cite journal | author=Zhang H, Saitoh H, Matunis MJ |title=Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex. |journal=Mol. Cell. Biol. |volume=22 |issue= 18 |pages= 6498-508 |year= 2002 |pmid= 12192048 |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=Beausoleil SA, Jedrychowski M, Schwartz D, ''et al.'' |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130-5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 }}
*{{cite journal | author=Macauley MS, Errington WJ, Okon M, ''et al.'' |title=Structural and dynamic independence of isopeptide-linked RanGAP1 and SUMO-1. |journal=J. Biol. Chem. |volume=279 |issue= 47 |pages= 49131-7 |year= 2005 |pmid= 15355965 |doi= 10.1074/jbc.M408705200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RAPSN... {November 20, 2007 11:43:06 PM PST}
- CREATE: Found no pages, creating new page. {November 20, 2007 11:44:03 PM PST}
- CREATED: Created new protein page: RAPSN {November 20, 2007 11:44:14 PM PST}
- INFO: Beginning work on RPLP0... {November 20, 2007 11:44:14 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:46:15 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Ribosomal protein, large, P0
| HGNCid = 10371
| Symbol = RPLP0
| AltSymbols =; P0; L10E; MGC111226; MGC88175; PRLP0; RPP0
| OMIM = 180510
| ECnumber =
| Homologene = 6517
| MGIid = 88066
| GeneAtlas_image1 = PBB_GE_RPLP0_214167_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_RPLP0_201033_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_RPLP0_208856_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0003735 |text = structural constituent of ribosome}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005840 |text = ribosome}} {{GNF_GO|id=GO:0005842 |text = cytosolic large ribosomal subunit (sensu Eukaryota)}}
| Process = {{GNF_GO|id=GO:0006414 |text = translational elongation}} {{GNF_GO|id=GO:0042254 |text = ribosome biogenesis and assembly}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6175
| Hs_Ensembl = ENSG00000089157
| Hs_RefseqProtein = NP_000993
| Hs_RefseqmRNA = NM_001002
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 119118893
| Hs_GenLoc_end = 119123397
| Hs_Uniprot = P05388
| Mm_EntrezGene = 11837
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_007475
| Mm_RefseqProtein = NP_031501
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Ribosomal protein, large, P0''', also known as '''RPLP0''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RPLP0 ribosomal protein, large, P0| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6175| 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 = Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 60S subunit. The protein, which is the functional equivalent of the E. coli L10 ribosomal protein, belongs to the L10P family of ribosomal proteins. It is a neutral phosphoprotein with a C-terminal end that is nearly identical to the C-terminal ends of the acidic ribosomal phosphoproteins P1 and P2. The P0 protein can interact with P1 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. Transcript variants derived from alternative splicing exist; they encode the same protein. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.<ref name="entrez">{{cite web | title = Entrez Gene: RPLP0 ribosomal protein, large, P0| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6175| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wool IG, Chan YL, Glück A |title=Structure and evolution of mammalian ribosomal proteins. |journal=Biochem. Cell Biol. |volume=73 |issue= 11-12 |pages= 933-47 |year= 1996 |pmid= 8722009 |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=Rich BE, Steitz JA |title=Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of cDNA clones, in vitro synthesis, and assembly. |journal=Mol. Cell. Biol. |volume=7 |issue= 11 |pages= 4065-74 |year= 1988 |pmid= 3323886 |doi= }}
*{{cite journal | author=Towbin H, Ramjoué HP, Kuster H, ''et al.'' |title=Monoclonal antibodies against eucaryotic ribosomes. Use to characterize a ribosomal protein not previously identified and antigenically related to the acidic phosphoproteins P1/P2. |journal=J. Biol. Chem. |volume=257 |issue= 21 |pages= 12709-15 |year= 1982 |pmid= 6182142 |doi= }}
*{{cite journal | author=Kato S, Sekine S, Oh SW, ''et al.'' |title=Construction of a human full-length cDNA bank. |journal=Gene |volume=150 |issue= 2 |pages= 243-50 |year= 1995 |pmid= 7821789 |doi= }}
*{{cite journal | author=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=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=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= |title=Toward a complete human genome sequence. |journal=Genome Res. |volume=8 |issue= 11 |pages= 1097-108 |year= 1999 |pmid= 9847074 |doi= }}
*{{cite journal | author=Tchórzewski M, Boldyreff B, Issinger O, Grankowski N |title=Analysis of the protein-protein interactions between the human acidic ribosomal P-proteins: evaluation by the two hybrid system. |journal=Int. J. Biochem. Cell Biol. |volume=32 |issue= 7 |pages= 737-46 |year= |pmid= 10856704 |doi= }}
*{{cite journal | author=Chan SH, Hung FS, Chan DS, Shaw PC |title=Trichosanthin interacts with acidic ribosomal proteins P0 and P1 and mitotic checkpoint protein MAD2B. |journal=Eur. J. Biochem. |volume=268 |issue= 7 |pages= 2107-12 |year= 2001 |pmid= 11277934 |doi= }}
*{{cite journal | author=Uechi T, Tanaka T, Kenmochi N |title=A complete map of the human ribosomal protein genes: assignment of 80 genes to the cytogenetic map and implications for human disorders. |journal=Genomics |volume=72 |issue= 3 |pages= 223-30 |year= 2001 |pmid= 11401437 |doi= 10.1006/geno.2000.6470 }}
*{{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=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=Tchórzewski M, Krokowski D, Rzeski W, ''et al.'' |title=The subcellular distribution of the human ribosomal "stalk" components: P1, P2 and P0 proteins. |journal=Int. J. Biochem. Cell Biol. |volume=35 |issue= 2 |pages= 203-11 |year= 2003 |pmid= 12479870 |doi= }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Shu H, Chen S, Bi Q, ''et al.'' |title=Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line. |journal=Mol. Cell Proteomics |volume=3 |issue= 3 |pages= 279-86 |year= 2004 |pmid= 14729942 |doi= 10.1074/mcp.D300003-MCP200 }}
*{{cite journal | author=Bouwmeester T, Bauch A, Ruffner H, ''et al.'' |title=A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. |journal=Nat. Cell Biol. |volume=6 |issue= 2 |pages= 97-105 |year= 2004 |pmid= 14743216 |doi= 10.1038/ncb1086 }}
*{{cite journal | author=Villacé P, Marión RM, Ortín J |title=The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs. |journal=Nucleic Acids Res. |volume=32 |issue= 8 |pages= 2411-20 |year= 2004 |pmid= 15121898 |doi= 10.1093/nar/gkh552 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SGTA... {November 20, 2007 11:48:23 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 20, 2007 11:49:12 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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| update_protein_box = yes
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{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Small glutamine-rich tetratricopeptide repeat (TPR)-containing, alpha
| HGNCid = 10819
| Symbol = SGTA
| AltSymbols =; SGT; hSGT
| OMIM = 603419
| ECnumber =
| Homologene = 31122
| MGIid = 1098703
| GeneAtlas_image1 = PBB_GE_SGTA_201396_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0008150 |text = biological_process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6449
| Hs_Ensembl = ENSG00000104969
| Hs_RefseqProtein = NP_003012
| Hs_RefseqmRNA = NM_003021
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 2705712
| Hs_GenLoc_end = 2734354
| Hs_Uniprot = O43765
| Mm_EntrezGene = 52551
| Mm_Ensembl = ENSMUSG00000004937
| Mm_RefseqmRNA = NM_024499
| Mm_RefseqProtein = NP_078775
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 80447204
| Mm_GenLoc_end = 80463291
| Mm_Uniprot = Q3TN35
}}
}}
'''Small glutamine-rich tetratricopeptide repeat (TPR)-containing, alpha''', also known as '''SGTA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SGTA small glutamine-rich tetratricopeptide repeat (TPR)-containing, alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6449| 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 protein which is capable of interacting with the major nonstructural protein of parvovirus H-1 and 70-kDa heat shock cognate protein; however, its function is not known. Since this transcript is expressed ubiquitously in various tissues, this protein may serve a housekeeping function.<ref name="entrez">{{cite web | title = Entrez Gene: SGTA small glutamine-rich tetratricopeptide repeat (TPR)-containing, alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6449| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Heavner GA, Audhya T, Goldstein G |title=Peptide analogs of thymopentin distinguish distinct thymopoietin receptor specificities on two human T cell lines. |journal=Regul. Pept. |volume=27 |issue= 2 |pages= 257-62 |year= 1990 |pmid= 2158125 |doi= }}
*{{cite journal | author=Geraghty RJ, Talbot KJ, Callahan M, ''et al.'' |title=Cell type-dependence for Vpu function. |journal=J. Med. Primatol. |volume=23 |issue= 2-3 |pages= 146-50 |year= 1994 |pmid= 7966229 |doi= }}
*{{cite journal | author=Cziepluch C, Kordes E, Poirey R, ''et al.'' |title=Identification of a novel cellular TPR-containing protein, SGT, that interacts with the nonstructural protein NS1 of parvovirus H-1. |journal=J. Virol. |volume=72 |issue= 5 |pages= 4149-56 |year= 1998 |pmid= 9557704 |doi= }}
*{{cite journal | author=Callahan MA, Handley MA, Lee YH, ''et al.'' |title=Functional interaction of human immunodeficiency virus type 1 Vpu and Gag with a novel member of the tetratricopeptide repeat protein family. |journal=J. Virol. |volume=72 |issue= 6 |pages= 5189-97 |year= 1998 |pmid= 9573291 |doi= }}
*{{cite journal | author=Kordes E, Savelyeva L, Schwab M, ''et al.'' |title=Isolation and characterization of human SGT and identification of homologues in Saccharomyces cerevisiae and Caenorhabditis elegans. |journal=Genomics |volume=52 |issue= 1 |pages= 90-4 |year= 1999 |pmid= 9740675 |doi= 10.1006/geno.1998.5385 }}
*{{cite journal | author=Callahan MA, Handley MA, Lee YH, ''et al.'' |title=Functional interaction of human immunodeficiency virus type 1 Vpu and Gag with a novel member of the tetratricopeptide repeat protein family. |journal=J. Virol. |volume=72 |issue= 10 |pages= 8461 |year= 1998 |pmid= 9766974 |doi= }}
*{{cite journal | author=Liu FH, Wu SJ, Hu SM, ''et al.'' |title=Specific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeats. |journal=J. Biol. Chem. |volume=274 |issue= 48 |pages= 34425-32 |year= 1999 |pmid= 10567422 |doi= }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
*{{cite journal | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
*{{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 }}
*{{cite journal | author=Handley MA, Paddock S, Dall A, Panganiban AT |title=Association of Vpu-binding protein with microtubules and Vpu-dependent redistribution of HIV-1 Gag protein. |journal=Virology |volume=291 |issue= 2 |pages= 198-207 |year= 2002 |pmid= 11878889 |doi= 10.1006/viro.2001.1166 }}
*{{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=Angeletti PC, Walker D, Panganiban AT |title=Small glutamine-rich protein/viral protein U-binding protein is a novel cochaperone that affects heat shock protein 70 activity. |journal=Cell Stress Chaperones |volume=7 |issue= 3 |pages= 258-68 |year= 2003 |pmid= 12482202 |doi= }}
*{{cite journal | author=Schantl JA, Roza M, De Jong AP, Strous GJ |title=Small glutamine-rich tetratricopeptide repeat-containing protein (SGT) interacts with the ubiquitin-dependent endocytosis (UbE) motif of the growth hormone receptor. |journal=Biochem. J. |volume=373 |issue= Pt 3 |pages= 855-63 |year= 2003 |pmid= 12735788 |doi= 10.1042/BJ20021591 }}
*{{cite journal | author=Pai MT, Yang CS, Tzeng SR, ''et al.'' |title=1H, 15N and 13C resonance assignments of the tetratricopeptide repeat (TPR) domain of hSGT. |journal=J. Biomol. NMR |volume=26 |issue= 4 |pages= 381-2 |year= 2004 |pmid= 12815268 |doi= }}
*{{cite journal | author=Wang H, Zhang Q, Zhu D |title=hSGT interacts with the N-terminal region of myostatin. |journal=Biochem. Biophys. Res. Commun. |volume=311 |issue= 4 |pages= 877-83 |year= 2004 |pmid= 14623262 |doi= }}
*{{cite journal | author=Lehner B, Semple JI, Brown SE, ''et al.'' |title=Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region. |journal=Genomics |volume=83 |issue= 1 |pages= 153-67 |year= 2004 |pmid= 14667819 |doi= }}
*{{cite journal | author=Winnefeld M, Rommelaere J, Cziepluch C |title=The human small glutamine-rich TPR-containing protein is required for progress through cell division. |journal=Exp. Cell Res. |volume=293 |issue= 1 |pages= 43-57 |year= 2004 |pmid= 14729056 |doi= }}
*{{cite journal | author=Grimwood J, Gordon LA, Olsen A, ''et al.'' |title=The DNA sequence and biology of human chromosome 19. |journal=Nature |volume=428 |issue= 6982 |pages= 529-35 |year= 2004 |pmid= 15057824 |doi= 10.1038/nature02399 }}
*{{cite journal | author=Beausoleil SA, Jedrychowski M, Schwartz D, ''et al.'' |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130-5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SORT1... {November 20, 2007 11:46:15 PM PST}
- CREATE: Found no pages, creating new page. {November 20, 2007 11:47:16 PM PST}
- CREATED: Created new protein page: SORT1 {November 20, 2007 11:47:24 PM PST}
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