Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 19:01, 18 November 2007 (UTC)[edit]
Proteins without matches (12)[edit]
Proteins with a High Potential Match (4)[edit]
Redirected Proteins (9)[edit]
Manual Inspection (Page not found) (16)[edit]
Updated (9)[edit]
Protein Status Grid - Date: 19:01, 18 November 2007 (UTC)[edit]
Vebose Log - Date: 19:01, 18 November 2007 (UTC)[edit]
- INFO: Beginning work on CASK... {November 18, 2007 10:49:07 AM PST}
- SEARCH REDIRECT: Control Box Found: CASK {November 18, 2007 10:49:46 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:49:47 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:49:47 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:49:47 AM PST}
- UPDATED: Updated protein page: CASK {November 18, 2007 10:49:54 AM PST}
- INFO: Beginning work on CD27... {November 18, 2007 10:29:51 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:30:54 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = CD27 molecule
| HGNCid = 11922
| Symbol = CD27
| AltSymbols =; MGC20393; S152; T14; TNFRSF7; Tp55
| OMIM = 186711
| ECnumber =
| Homologene = 74386
| MGIid = 88326
| GeneAtlas_image1 = PBB_GE_CD27_206150_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0004888 |text = transmembrane receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0043027 |text = caspase inhibitor activity}}
| Component = {{GNF_GO|id=GO:0000786 |text = nucleosome}} {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007001 |text = chromosome organization and biogenesis (sensu Eukaryota)}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0007283 |text = spermatogenesis}} {{GNF_GO|id=GO:0008588 |text = release of cytoplasmic sequestered NF-kappaB}} {{GNF_GO|id=GO:0016064 |text = immunoglobulin mediated immune response}} {{GNF_GO|id=GO:0042100 |text = B cell proliferation}} {{GNF_GO|id=GO:0045078 |text = positive regulation of interferon-gamma biosynthetic process}} {{GNF_GO|id=GO:0045579 |text = positive regulation of B cell differentiation}} {{GNF_GO|id=GO:0045582 |text = positive regulation of T cell differentiation}} {{GNF_GO|id=GO:0046330 |text = positive regulation of JNK cascade}} {{GNF_GO|id=GO:0048305 |text = immunoglobulin secretion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 939
| Hs_Ensembl = ENSG00000139193
| Hs_RefseqProtein = NP_001233
| Hs_RefseqmRNA = NM_001242
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 6424327
| Hs_GenLoc_end = 6431144
| Hs_Uniprot = P26842
| Mm_EntrezGene = 21940
| Mm_Ensembl = ENSMUSG00000030336
| Mm_RefseqmRNA = NM_001033126
| Mm_RefseqProtein = NP_001028298
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 125198242
| Mm_GenLoc_end = 125202629
| Mm_Uniprot = Q3U4X0
}}
}}
'''CD27 molecule''', also known as '''CD27''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CD27 CD27 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=939| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor is required for generation and long-term maintenance of T cell immunity. It binds to ligand CD70, and plays a key role in regulating B-cell activation and immunoglobulin synthesis. This receptor transduces signals that lead to the activation of NF-kappaB and MAPK8/JNK. Adaptor proteins TRAF2 and TRAF5 have been shown to mediate the signaling process of this receptor. CD27-binding protein (SIVA), a proapoptotic protein, can bind to this receptor and is thought to play an important role in the apoptosis induced by this receptor.<ref name="entrez">{{cite web | title = Entrez Gene: CD27 CD27 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=939| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lens SM, de Jong R, Hintzen RQ, ''et al.'' |title=CD27-CD70 interaction: unravelling its implication in normal and neoplastic B-cell growth. |journal=Leuk. Lymphoma |volume=18 |issue= 1-2 |pages= 51-9 |year= 1996 |pmid= 8580829 |doi= }}
*{{cite journal | author=Agematsu K |title=Memory B cells and CD27. |journal=Histol. Histopathol. |volume=15 |issue= 2 |pages= 573-6 |year= 2000 |pmid= 10809378 |doi= }}
*{{cite journal | author=van Baarle D, Kostense S, van Oers MH, ''et al.'' |title=Failing immune control as a result of impaired CD8+ T-cell maturation: CD27 might provide a clue. |journal=Trends Immunol. |volume=23 |issue= 12 |pages= 586-91 |year= 2003 |pmid= 12464570 |doi= }}
*{{cite journal | author=Dörner T, Lipsky PE |title=Correlation of circulating CD27high plasma cells and disease activity in systemic lupus erythematosus. |journal=Lupus |volume=13 |issue= 5 |pages= 283-9 |year= 2005 |pmid= 15230280 |doi= }}
*{{cite journal | author=Loenen WA, Gravestein LA, Beumer S, ''et al.'' |title=Genomic organization and chromosomal localization of the human CD27 gene. |journal=J. Immunol. |volume=149 |issue= 12 |pages= 3937-43 |year= 1993 |pmid= 1334106 |doi= }}
*{{cite journal | author=Camerini D, Walz G, Loenen WA, ''et al.'' |title=The T cell activation antigen CD27 is a member of the nerve growth factor/tumor necrosis factor receptor gene family. |journal=J. Immunol. |volume=147 |issue= 9 |pages= 3165-9 |year= 1991 |pmid= 1655907 |doi= }}
*{{cite journal | author=van Lier RA, Borst J, Vroom TM, ''et al.'' |title=Tissue distribution and biochemical and functional properties of Tp55 (CD27), a novel T cell differentiation antigen. |journal=J. Immunol. |volume=139 |issue= 5 |pages= 1589-96 |year= 1987 |pmid= 2442250 |doi= }}
*{{cite journal | author=Bigler RD, Bushkin Y, Chiorazzi N |title=S152 (CD27). A modulating disulfide-linked T cell activation antigen. |journal=J. Immunol. |volume=141 |issue= 1 |pages= 21-8 |year= 1988 |pmid= 2837508 |doi= }}
*{{cite journal | author=Kobata T, Jacquot S, Kozlowski S, ''et al.'' |title=CD27-CD70 interactions regulate B-cell activation by T cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 24 |pages= 11249-53 |year= 1995 |pmid= 7479974 |doi= }}
*{{cite journal | author=Bowman MR, Crimmins MA, Yetz-Aldape J, ''et al.'' |title=The cloning of CD70 and its identification as the ligand for CD27. |journal=J. Immunol. |volume=152 |issue= 4 |pages= 1756-61 |year= 1994 |pmid= 8120384 |doi= }}
*{{cite journal | author=Hintzen RQ, Lens SM, Koopman G, ''et al.'' |title=CD70 represents the human ligand for CD27. |journal=Int. Immunol. |volume=6 |issue= 3 |pages= 477-80 |year= 1994 |pmid= 8186199 |doi= }}
*{{cite journal | author=Baens M, Aerssens J, van Zand K, ''et al.'' |title=Isolation and regional assignment of human chromosome 12p cDNAs. |journal=Genomics |volume=29 |issue= 1 |pages= 44-52 |year= 1996 |pmid= 8530100 |doi= 10.1006/geno.1995.1213 }}
*{{cite journal | author=Prasad KV, Ao Z, Yoon Y, ''et al.'' |title=CD27, a member of the tumor necrosis factor receptor family, induces apoptosis and binds to Siva, a proapoptotic protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 12 |pages= 6346-51 |year= 1997 |pmid= 9177220 |doi= }}
*{{cite journal | author=Feito MJ, Bragardo M, Buonfiglio D, ''et al.'' |title=gp 120s derived from four syncytium-inducing HIV-1 strains induce different patterns of CD4 association with lymphocyte surface molecules. |journal=Int. Immunol. |volume=9 |issue= 8 |pages= 1141-7 |year= 1997 |pmid= 9263011 |doi= }}
*{{cite journal | author=Akiba H, Nakano H, Nishinaka S, ''et al.'' |title=CD27, a member of the tumor necrosis factor receptor superfamily, activates NF-kappaB and stress-activated protein kinase/c-Jun N-terminal kinase via TRAF2, TRAF5, and NF-kappaB-inducing kinase. |journal=J. Biol. Chem. |volume=273 |issue= 21 |pages= 13353-8 |year= 1998 |pmid= 9582383 |doi= }}
*{{cite journal | author=Gravestein LA, Amsen D, Boes M, ''et al.'' |title=The TNF receptor family member CD27 signals to Jun N-terminal kinase via Traf-2. |journal=Eur. J. Immunol. |volume=28 |issue= 7 |pages= 2208-16 |year= 1998 |pmid= 9692890 |doi= }}
*{{cite journal | author=Nagumo H, Agematsu K |title=Synergistic augmentative effect of interleukin-10 and CD27/CD70 interactions on B-cell immunoglobulin synthesis. |journal=Immunology |volume=94 |issue= 3 |pages= 388-94 |year= 1998 |pmid= 9767422 |doi= }}
*{{cite journal | author=Yamamoto H, Kishimoto T, Minamoto S |title=NF-kappaB activation in CD27 signaling: involvement of TNF receptor-associated factors in its signaling and identification of functional region of CD27. |journal=J. Immunol. |volume=161 |issue= 9 |pages= 4753-9 |year= 1998 |pmid= 9794406 |doi= }}
*{{cite journal | author=Nagumo H, Agematsu K, Shinozaki K, ''et al.'' |title=CD27/CD70 interaction augments IgE secretion by promoting the differentiation of memory B cells into plasma cells. |journal=J. Immunol. |volume=161 |issue= 12 |pages= 6496-502 |year= 1999 |pmid= 9862673 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CD274... {November 18, 2007 10:52:50 AM PST}
- SEARCH REDIRECT: Control Box Found: CD274 {November 18, 2007 10:53:35 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:53:38 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:53:38 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:53:38 AM PST}
- UPDATED: Updated protein page: CD274 {November 18, 2007 10:53:45 AM PST}
- INFO: Beginning work on CDH13... {November 18, 2007 10:30:54 AM PST}
- SEARCH REDIRECT: Control Box Found: CDH13 {November 18, 2007 10:31:55 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:32:03 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:32:03 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:32:03 AM PST}
- UPDATED: Updated protein page: CDH13 {November 18, 2007 10:32:17 AM PST}
- INFO: Beginning work on CHI3L1... {November 18, 2007 10:32:17 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:33:33 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CHI3L1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hjv.
| PDB = {{PDB2|1hjv}}, {{PDB2|1hjw}}, {{PDB2|1hjx}}, {{PDB2|1nwr}}, {{PDB2|1nws}}, {{PDB2|1nwt}}, {{PDB2|1nwu}}
| Name = Chitinase 3-like 1 (cartilage glycoprotein-39)
| HGNCid = 1932
| Symbol = CHI3L1
| AltSymbols =; GP39; HC-gp39; HCGP-3P; YKL40; YYL-40
| OMIM = 601525
| ECnumber =
| Homologene = 55569
| MGIid = 1340899
| GeneAtlas_image1 = PBB_GE_CHI3L1_209396_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CHI3L1_209395_at_tn.png
| GeneAtlas_image3 = PBB_GE_CHI3L1_216546_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003824 |text = catalytic activity}} {{GNF_GO|id=GO:0004553 |text = hydrolase activity, hydrolyzing O-glycosyl compounds}} {{GNF_GO|id=GO:0004568 |text = chitinase activity}} {{GNF_GO|id=GO:0005201 |text = extracellular matrix structural constituent}} {{GNF_GO|id=GO:0005529 |text = sugar binding}} {{GNF_GO|id=GO:0043169 |text = cation binding}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006032 |text = chitin catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1116
| Hs_Ensembl = ENSG00000133048
| Hs_RefseqProtein = NP_001267
| Hs_RefseqmRNA = NM_001276
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 201414553
| Hs_GenLoc_end = 201422500
| Hs_Uniprot = P36222
| Mm_EntrezGene = 12654
| Mm_Ensembl = ENSMUSG00000064246
| Mm_RefseqmRNA = NM_007695
| Mm_RefseqProtein = NP_031721
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 135998875
| Mm_GenLoc_end = 136006439
| Mm_Uniprot = Q3U291
}}
}}
'''Chitinase 3-like 1 (cartilage glycoprotein-39)''', also known as '''CHI3L1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CHI3L1 chitinase 3-like 1 (cartilage glycoprotein-39)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1116| 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=Rathcke CN, Vestergaard H |title=YKL-40, a new inflammatory marker with relation to insulin resistance and with a role in endothelial dysfunction and atherosclerosis. |journal=Inflamm. Res. |volume=55 |issue= 6 |pages= 221-7 |year= 2007 |pmid= 16955240 |doi= 10.1007/s00011-006-0076-y }}
*{{cite journal | author=Nyirkos P, Golds EE |title=Human synovial cells secrete a 39 kDa protein similar to a bovine mammary protein expressed during the non-lactating period. |journal=Biochem. J. |volume=269 |issue= 1 |pages= 265-8 |year= 1990 |pmid= 2375755 |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=Hakala BE, White C, Recklies AD |title=Human cartilage gp-39, a major secretory product of articular chondrocytes and synovial cells, is a mammalian member of a chitinase protein family. |journal=J. Biol. Chem. |volume=268 |issue= 34 |pages= 25803-10 |year= 1994 |pmid= 8245017 |doi= }}
*{{cite journal | author=Rehli M, Krause SW, Andreesen R |title=Molecular characterization of the gene for human cartilage gp-39 (CHI3L1), a member of the chitinase protein family and marker for late stages of macrophage differentiation. |journal=Genomics |volume=43 |issue= 2 |pages= 221-5 |year= 1997 |pmid= 9244440 |doi= 10.1006/geno.1997.4778 }}
*{{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=Kirkpatrick RB, Emery JG, Connor JR, ''et al.'' |title=Induction and expression of human cartilage glycoprotein 39 in rheumatoid inflammatory and peripheral blood monocyte-derived macrophages. |journal=Exp. Cell Res. |volume=237 |issue= 1 |pages= 46-54 |year= 1998 |pmid= 9417865 |doi= 10.1006/excr.1997.3764 }}
*{{cite journal | author=Renkema GH, Boot RG, Au FL, ''et al.'' |title=Chitotriosidase, a chitinase, and the 39-kDa human cartilage glycoprotein, a chitin-binding lectin, are homologues of family 18 glycosyl hydrolases secreted by human macrophages. |journal=Eur. J. Biochem. |volume=251 |issue= 1-2 |pages= 504-9 |year= 1998 |pmid= 9492324 |doi= }}
*{{cite journal | author=Johansen JS, Stoltenberg M, Hansen M, ''et al.'' |title=Serum YKL-40 concentrations in patients with rheumatoid arthritis: relation to disease activity. |journal=Rheumatology (Oxford) |volume=38 |issue= 7 |pages= 618-26 |year= 1999 |pmid= 10461474 |doi= }}
*{{cite journal | author=Nordenbaek C, Johansen JS, Junker P, ''et al.'' |title=YKL-40, a matrix protein of specific granules in neutrophils, is elevated in serum of patients with community-acquired pneumonia requiring hospitalization. |journal=J. Infect. Dis. |volume=180 |issue= 5 |pages= 1722-6 |year= 1999 |pmid= 10515841 |doi= }}
*{{cite journal | author=Connor JR, Dodds RA, Emery JG, ''et al.'' |title=Human cartilage glycoprotein 39 (HC gp-39) mRNA expression in adult and fetal chondrocytes, osteoblasts and osteocytes by in-situ hybridization. |journal=Osteoarthr. Cartil. |volume=8 |issue= 2 |pages= 87-95 |year= 2000 |pmid= 10772238 |doi= 10.1053/joca.1999.0276 }}
*{{cite journal | author=Østergaard C, Johansen JS, Benfield T, ''et al.'' |title=YKL-40 is elevated in cerebrospinal fluid from patients with purulent meningitis. |journal=Clin. Diagn. Lab. Immunol. |volume=9 |issue= 3 |pages= 598-604 |year= 2002 |pmid= 11986266 |doi= }}
*{{cite journal | author=Kronborg G, Ostergaard C, Weis N, ''et al.'' |title=Serum level of YKL-40 is elevated in patients with Streptococcus pneumoniae bacteremia and is associated with the outcome of the disease. |journal=Scand. J. Infect. Dis. |volume=34 |issue= 5 |pages= 323-6 |year= 2003 |pmid= 12069012 |doi= }}
*{{cite journal | author=Recklies AD, White C, Ling H |title=The chitinase 3-like protein human cartilage glycoprotein 39 (HC-gp39) stimulates proliferation of human connective-tissue cells and activates both extracellular signal-regulated kinase- and protein kinase B-mediated signalling pathways. |journal=Biochem. J. |volume=365 |issue= Pt 1 |pages= 119-26 |year= 2002 |pmid= 12071845 |doi= 10.1042/BJ20020075 }}
*{{cite journal | author=Cintin C, Johansen JS, Christensen IJ, ''et al.'' |title=High serum YKL-40 level after surgery for colorectal carcinoma is related to short survival. |journal=Cancer |volume=95 |issue= 2 |pages= 267-74 |year= 2002 |pmid= 12124825 |doi= 10.1002/cncr.10644 }}
*{{cite journal | author=Steck E, Breit S, Breusch SJ, ''et al.'' |title=Enhanced expression of the human chitinase 3-like 2 gene (YKL-39) but not chitinase 3-like 1 gene (YKL-40) in osteoarthritic cartilage. |journal=Biochem. Biophys. Res. Commun. |volume=299 |issue= 1 |pages= 109-15 |year= 2003 |pmid= 12435396 |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=Steenbakkers PG, Baeten D, Rovers E, ''et al.'' |title=Localization of MHC class II/human cartilage glycoprotein-39 complexes in synovia of rheumatoid arthritis patients using complex-specific monoclonal antibodies. |journal=J. Immunol. |volume=170 |issue= 11 |pages= 5719-27 |year= 2003 |pmid= 12759455 |doi= }}
*{{cite journal | author=Houston DR, Recklies AD, Krupa JC, van Aalten DM |title=Structure and ligand-induced conformational change of the 39-kDa glycoprotein from human articular chondrocytes. |journal=J. Biol. Chem. |volume=278 |issue= 32 |pages= 30206-12 |year= 2003 |pmid= 12775711 |doi= 10.1074/jbc.M303371200 }}
*{{cite journal | author=Nishikawa KC, Millis AJ |title=gp38k (CHI3L1) is a novel adhesion and migration factor for vascular cells. |journal=Exp. Cell Res. |volume=287 |issue= 1 |pages= 79-87 |year= 2003 |pmid= 12799184 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CLDN1... {November 18, 2007 10:49:54 AM PST}
- SEARCH REDIRECT: Control Box Found: CLDN1 {November 18, 2007 10:50:34 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:50:37 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:50:37 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:50:37 AM PST}
- UPDATED: Updated protein page: CLDN1 {November 18, 2007 10:50:44 AM PST}
- INFO: Beginning work on CNR2... {November 18, 2007 10:33:33 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:34:47 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Cannabinoid receptor 2 (macrophage)
| HGNCid = 2160
| Symbol = CNR2
| AltSymbols =; CB2; CX5
| OMIM = 605051
| ECnumber =
| Homologene = 1389
| MGIid = 104650
| GeneAtlas_image1 = PBB_GE_CNR2_206586_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004949 |text = cannabinoid receptor 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:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007187 |text = G-protein signaling, coupled to cyclic nucleotide second messenger}} {{GNF_GO|id=GO:0007610 |text = behavior}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1269
| Hs_Ensembl = ENSG00000188822
| Hs_RefseqProtein = NP_001832
| Hs_RefseqmRNA = NM_001841
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 24069603
| Hs_GenLoc_end = 24112439
| Hs_Uniprot = P34972
| Mm_EntrezGene = 12802
| Mm_Ensembl = ENSMUSG00000062585
| Mm_RefseqmRNA = NM_009924
| Mm_RefseqProtein = NP_034054
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 135167470
| Mm_GenLoc_end = 135192284
| Mm_Uniprot = Q544H5
}}
}}
'''Cannabinoid receptor 2 (macrophage)''', also known as '''CNR2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CNR2 cannabinoid receptor 2 (macrophage)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1269| 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 cannabinoid delta-9-tetrahydrocannabinol is the principal psychoactive ingredient of marijuana. The proteins encoded by this gene and the cannabinoid receptor 1 (brain) (CNR1) gene have the characteristics of a guanine nucleotide-binding protein (G-protein)-coupled receptor for cannabinoids. They inhibit adenylate cyclase activity in a dose-dependent, stereoselective, and pertussis toxin-sensitive manner. These proteins have been found to be involved in the cannabinoid-induced CNS effects (including alterations in mood and cognition) experienced by users of marijuana. The cannabinoid receptors are members of family 1 of the G-protein-coupled receptors.<ref name="entrez">{{cite web | title = Entrez Gene: CNR2 cannabinoid receptor 2 (macrophage)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1269| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Oddi S, Spagnuolo P, Bari M, ''et al.'' |title=Differential modulation of type 1 and type 2 cannabinoid receptors along the neuroimmune axis. |journal=Int. Rev. Neurobiol. |volume=82 |issue= |pages= 327-37 |year= 2007 |pmid= 17678969 |doi= 10.1016/S0074-7742(07)82017-4 }}
*{{cite journal | author=Galiègue S, Mary S, Marchand J, ''et al.'' |title=Expression of central and peripheral cannabinoid receptors in human immune tissues and leukocyte subpopulations. |journal=Eur. J. Biochem. |volume=232 |issue= 1 |pages= 54-61 |year= 1995 |pmid= 7556170 |doi= }}
*{{cite journal | author=Munro S, Thomas KL, Abu-Shaar M |title=Molecular characterization of a peripheral receptor for cannabinoids. |journal=Nature |volume=365 |issue= 6441 |pages= 61-5 |year= 1993 |pmid= 7689702 |doi= 10.1038/365061a0 }}
*{{cite journal | author=Shire D, Calandra B, Rinaldi-Carmona M, ''et al.'' |title=Molecular cloning, expression and function of the murine CB2 peripheral cannabinoid receptor. |journal=Biochim. Biophys. Acta |volume=1307 |issue= 2 |pages= 132-6 |year= 1996 |pmid= 8679694 |doi= }}
*{{cite journal | author=Tao Q, McAllister SD, Andreassi J, ''et al.'' |title=Role of a conserved lysine residue in the peripheral cannabinoid receptor (CB2): evidence for subtype specificity. |journal=Mol. Pharmacol. |volume=55 |issue= 3 |pages= 605-13 |year= 1999 |pmid= 10051546 |doi= }}
*{{cite journal | author=Nong L, Newton C, Friedman H, Klein TW |title=CB1 and CB2 receptor mRNA expression in human peripheral blood mononuclear cells (PBMC) from various donor types. |journal=Adv. Exp. Med. Biol. |volume=493 |issue= |pages= 229-33 |year= 2002 |pmid= 11727770 |doi= }}
*{{cite journal | author=Ho BY, Current L, Drewett JG |title=Role of intracellular loops of cannabinoid CB(1) receptor in functional interaction with G(alpha16). |journal=FEBS Lett. |volume=522 |issue= 1-3 |pages= 130-4 |year= 2002 |pmid= 12095632 |doi= }}
*{{cite journal | author=Matias I, Pochard P, Orlando P, ''et al.'' |title=Presence and regulation of the endocannabinoid system in human dendritic cells. |journal=Eur. J. Biochem. |volume=269 |issue= 15 |pages= 3771-8 |year= 2002 |pmid= 12153574 |doi= }}
*{{cite journal | author=Song ZH, Feng W |title=Absence of a conserved proline and presence of a conserved tyrosine in the CB2 cannabinoid receptor are crucial for its function. |journal=FEBS Lett. |volume=531 |issue= 2 |pages= 290-4 |year= 2002 |pmid= 12417328 |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=Casanova ML, Blázquez C, Martínez-Palacio J, ''et al.'' |title=Inhibition of skin tumor growth and angiogenesis in vivo by activation of cannabinoid receptors. |journal=J. Clin. Invest. |volume=111 |issue= 1 |pages= 43-50 |year= 2003 |pmid= 12511587 |doi= }}
*{{cite journal | author=Feng W, Song ZH |title=Effects of D3.49A, R3.50A, and A6.34E mutations on ligand binding and activation of the cannabinoid-2 (CB2) receptor. |journal=Biochem. Pharmacol. |volume=65 |issue= 7 |pages= 1077-85 |year= 2003 |pmid= 12663043 |doi= }}
*{{cite journal | author=Kishimoto S, Gokoh M, Oka S, ''et al.'' |title=2-arachidonoylglycerol induces the migration of HL-60 cells differentiated into macrophage-like cells and human peripheral blood monocytes through the cannabinoid CB2 receptor-dependent mechanism. |journal=J. Biol. Chem. |volume=278 |issue= 27 |pages= 24469-75 |year= 2003 |pmid= 12711605 |doi= 10.1074/jbc.M301359200 }}
*{{cite journal | author=Jorda MA, Rayman N, Valk P, ''et al.'' |title=Identification, characterization, and function of a novel oncogene: the peripheral cannabinoid receptor Cb2. |journal=Ann. N. Y. Acad. Sci. |volume=996 |issue= |pages= 10-6 |year= 2003 |pmid= 12799277 |doi= }}
*{{cite journal | author=Benito C, Núñez E, Tolón RM, ''et al.'' |title=Cannabinoid CB2 receptors and fatty acid amide hydrolase are selectively overexpressed in neuritic plaque-associated glia in Alzheimer's disease brains. |journal=J. Neurosci. |volume=23 |issue= 35 |pages= 11136-41 |year= 2003 |pmid= 14657172 |doi= }}
*{{cite journal | author=Rayman N, Lam KH, Laman JD, ''et al.'' |title=Distinct expression profiles of the peripheral cannabinoid receptor in lymphoid tissues depending on receptor activation status. |journal=J. Immunol. |volume=172 |issue= 4 |pages= 2111-7 |year= 2004 |pmid= 14764676 |doi= }}
*{{cite journal | author=Rao GK, Zhang W, Kaminski NE |title=Cannabinoid receptor-mediated regulation of intracellular calcium by delta(9)-tetrahydrocannabinol in resting T cells. |journal=J. Leukoc. Biol. |volume=75 |issue= 5 |pages= 884-92 |year= 2004 |pmid= 14966196 |doi= 10.1189/jlb.1203638 }}
*{{cite journal | author=Alberich Jordà M, Rayman N, Tas M, ''et al.'' |title=The peripheral cannabinoid receptor Cb2, frequently expressed on AML blasts, either induces a neutrophilic differentiation block or confers abnormal migration properties in a ligand-dependent manner. |journal=Blood |volume=104 |issue= 2 |pages= 526-34 |year= 2004 |pmid= 15039279 |doi= 10.1182/blood-2003-12-4357 }}
*{{cite journal | author=Núñez E, Benito C, Pazos MR, ''et al.'' |title=Cannabinoid CB2 receptors are expressed by perivascular microglial cells in the human brain: an immunohistochemical study. |journal=Synapse |volume=53 |issue= 4 |pages= 208-13 |year= 2004 |pmid= 15266552 |doi= 10.1002/syn.20050 }}
*{{cite journal | author=Gokoh M, Kishimoto S, Oka S, ''et al.'' |title=2-arachidonoylglycerol, an endogenous cannabinoid receptor ligand, induces rapid actin polymerization in HL-60 cells differentiated into macrophage-like cells. |journal=Biochem. J. |volume=386 |issue= Pt 3 |pages= 583-9 |year= 2005 |pmid= 15456404 |doi= 10.1042/BJ20041163 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on COPB1... {November 18, 2007 10:34:48 AM PST}
- SEARCH REDIRECT: Control Box Found: COPB1 {November 18, 2007 10:35:51 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:35:58 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:35:58 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:35:58 AM PST}
- UPDATED: Updated protein page: COPB1 {November 18, 2007 10:36:12 AM PST}
- INFO: Beginning work on CSF2RA... {November 18, 2007 10:36:12 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:37:47 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Colony stimulating factor 2 receptor, alpha, low-affinity (granulocyte-macrophage)
| HGNCid = 2435
| Symbol = CSF2RA
| AltSymbols =; CD116; CDw116; CSF2R; CSF2RAX; CSF2RAY; CSF2RX; CSF2RY; GM-CSF-R-alpha; GMCSFR; GMR; MGC3848; MGC4838
| OMIM = 306250
| ECnumber =
| Homologene = 48406
| MGIid = 1339754
| GeneAtlas_image1 = PBB_GE_CSF2RA_210340_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CSF2RA_207085_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_CSF2RA_211286_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004896 |text = hematopoietin/interferon-class (D200-domain) cytokine receptor activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1438
| Hs_Ensembl = ENSG00000198223
| Hs_RefseqProtein = XP_001133962
| Hs_RefseqmRNA = XM_001133962
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 1347693
| Hs_GenLoc_end = 1389274
| Hs_Uniprot = P15509
| Mm_EntrezGene = 12982
| Mm_Ensembl = ENSMUSG00000059326
| Mm_RefseqmRNA = XM_977426
| Mm_RefseqProtein = XP_982520
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 61279667
| Mm_GenLoc_end = 61282028
| Mm_Uniprot = Q00941
}}
}}
'''Colony stimulating factor 2 receptor, alpha, low-affinity (granulocyte-macrophage)''', also known as '''CSF2RA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CSF2RA colony stimulating factor 2 receptor, alpha, low-affinity (granulocyte-macrophage)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1438| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is the alpha subunit of the heterodimeric receptor for colony stimulating factor 2, a cytokine which controls the production, differentiation, and function of granulocytes and macrophages. The encoded protein is a member of the cytokine family of receptors. This gene is found in the pseudoautosomal region (PAR) of the X and Y chromosomes. Multiple transcript variants encoding different isoforms have been found for this gene, with some of the isoforms being membrane-bound and others being soluble.<ref name="entrez">{{cite web | title = Entrez Gene: CSF2RA colony stimulating factor 2 receptor, alpha, low-affinity (granulocyte-macrophage)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1438| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Rappold G, Willson TA, Henke A, Gough NM |title=Arrangement and localization of the human GM-CSF receptor alpha chain gene CSF2RA within the X-Y pseudoautosomal region. |journal=Genomics |volume=14 |issue= 2 |pages= 455-61 |year= 1992 |pmid= 1358805 |doi= }}
*{{cite journal | author=Hayashida K, Kitamura T, Gorman DM, ''et al.'' |title=Molecular cloning of a second subunit of the receptor for human granulocyte-macrophage colony-stimulating factor (GM-CSF): reconstitution of a high-affinity GM-CSF receptor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 24 |pages= 9655-9 |year= 1991 |pmid= 1702217 |doi= }}
*{{cite journal | author=Crosier KE, Wong GG, Mathey-Prevot B, ''et al.'' |title=A functional isoform of the human granulocyte/macrophage colony-stimulating factor receptor has an unusual cytoplasmic domain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 17 |pages= 7744-8 |year= 1991 |pmid= 1715577 |doi= }}
*{{cite journal | author=Raines MA, Liu L, Quan SG, ''et al.'' |title=Identification and molecular cloning of a soluble human granulocyte-macrophage colony-stimulating factor receptor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 18 |pages= 8203-7 |year= 1991 |pmid= 1832774 |doi= }}
*{{cite journal | author=Gough NM, Gearing DP, Nicola NA, ''et al.'' |title=Localization of the human GM-CSF receptor gene to the X-Y pseudoautosomal region. |journal=Nature |volume=345 |issue= 6277 |pages= 734-6 |year= 1990 |pmid= 1972780 |doi= 10.1038/345734a0 }}
*{{cite journal | author=Ashworth A, Kraft A |title=Cloning of a potentially soluble receptor for human GM-CSF. |journal=Nucleic Acids Res. |volume=18 |issue= 23 |pages= 7178 |year= 1991 |pmid= 2148207 |doi= }}
*{{cite journal | author=Gearing DP, King JA, Gough NM, Nicola NA |title=Expression cloning of a receptor for human granulocyte-macrophage colony-stimulating factor. |journal=EMBO J. |volume=8 |issue= 12 |pages= 3667-76 |year= 1990 |pmid= 2555171 |doi= }}
*{{cite journal | author=DiPersio J, Billing P, Kaufman S, ''et al.'' |title=Characterization of the human granulocyte-macrophage colony-stimulating factor receptor. |journal=J. Biol. Chem. |volume=263 |issue= 4 |pages= 1834-41 |year= 1988 |pmid= 2828352 |doi= }}
*{{cite journal | author=Williams WV, VonFeldt JM, Rosenbaum H, ''et al.'' |title=Molecular cloning of a soluble form of the granulocyte-macrophage colony-stimulating factor receptor alpha chain from a myelomonocytic cell line. Expression, biologic activity, and preliminary analysis of transcript distribution. |journal=Arthritis Rheum. |volume=37 |issue= 10 |pages= 1468-78 |year= 1994 |pmid= 7945472 |doi= }}
*{{cite journal | author=Jubinsky PT, Laurie AS, Nathan DG, ''et al.'' |title=Expression and function of the human granulocyte-macrophage colony-stimulating factor receptor alpha subunit. |journal=Blood |volume=84 |issue= 12 |pages= 4174-85 |year= 1995 |pmid= 7994031 |doi= }}
*{{cite journal | author=Hu X, Emanuel PD, Zuckerman KS |title=Cloning and sequencing of the cDNAs encoding two alternative splicing-derived variants of the alpha subunit of the granulocyte-macrophage colony-stimulating factor receptor. |journal=Biochim. Biophys. Acta |volume=1223 |issue= 2 |pages= 306-8 |year= 1994 |pmid= 8086503 |doi= }}
*{{cite journal | author=Nakagawa Y, Kosugi H, Miyajima A, ''et al.'' |title=Structure of the gene encoding the alpha subunit of the human granulocyte-macrophage colony stimulating factor receptor. Implications for the evolution of the cytokine receptor superfamily. |journal=J. Biol. Chem. |volume=269 |issue= 14 |pages= 10905-12 |year= 1994 |pmid= 8144676 |doi= }}
*{{cite journal | author=Zhao Y, Rong H, Chegini N |title=Expression and selective cellular localization of granulocyte-macrophage colony-stimulating factor (GM-CSF) and GM-CSF alpha and beta receptor messenger ribonucleic acid and protein in human ovarian tissue. |journal=Biol. Reprod. |volume=53 |issue= 4 |pages= 923-30 |year= 1996 |pmid= 8547489 |doi= }}
*{{cite journal | author=Lia F, Rajotte D, Clark SC, Hoang T |title=A dominant negative granulocyte-macrophage colony-stimulating factor receptor alpha chain reveals the multimeric structure of the receptor complex. |journal=J. Biol. Chem. |volume=271 |issue= 45 |pages= 28287-93 |year= 1996 |pmid= 8910448 |doi= }}
*{{cite journal | author=Wei S, Liu JH, Epling-Burnette PK, ''et al.'' |title=Critical role of Lyn kinase in inhibition of neutrophil apoptosis by granulocyte-macrophage colony-stimulating factor. |journal=J. Immunol. |volume=157 |issue= 11 |pages= 5155-62 |year= 1996 |pmid= 8943427 |doi= }}
*{{cite journal | author=Soldi R, Primo L, Brizzi MF, ''et al.'' |title=Activation of JAK2 in human vascular endothelial cells by granulocyte-macrophage colony-stimulating factor. |journal=Blood |volume=89 |issue= 3 |pages= 863-72 |year= 1997 |pmid= 9028317 |doi= }}
*{{cite journal | author=Matsuguchi T, Zhao Y, Lilly MB, Kraft AS |title=The cytoplasmic domain of granulocyte-macrophage colony-stimulating factor (GM-CSF) receptor alpha subunit is essential for both GM-CSF-mediated growth and differentiation. |journal=J. Biol. Chem. |volume=272 |issue= 28 |pages= 17450-9 |year= 1997 |pmid= 9211889 |doi= }}
*{{cite journal | author=Rivas CI, Vera JC, Delgado-López F, ''et al.'' |title=Expression of granulocyte-macrophage colony-stimulating factor receptors in human prostate cancer. |journal=Blood |volume=91 |issue= 3 |pages= 1037-43 |year= 1998 |pmid= 9446667 |doi= }}
*{{cite journal | author=Hu X, Zuckerman KS |title=Cloning and sequencing of an alternative splicing-derived cDNA variant of the GM-CSF receptor alpha subunit, which encodes a truncated protein. |journal=Am. J. Hematol. |volume=58 |issue= 2 |pages= 145-7 |year= 1998 |pmid= 9625584 |doi= }}
*{{cite journal | author=Taha RA, Leung DY, Ghaffar O, ''et al.'' |title=In vivo expression of cytokine receptor mRNA in atopic dermatitis. |journal=J. Allergy Clin. Immunol. |volume=102 |issue= 2 |pages= 245-50 |year= 1998 |pmid= 9723668 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CSNK1A1... {November 18, 2007 10:37:47 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:39:37 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Casein kinase 1, alpha 1
| HGNCid = 2451
| Symbol = CSNK1A1
| AltSymbols =; CK1; HLCDGP1; PRO2975
| OMIM = 600505
| ECnumber =
| Homologene = 37546
| MGIid = 1934950
| GeneAtlas_image1 = PBB_GE_CSNK1A1_206562_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CSNK1A1_213086_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_CSNK1A1_208865_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004681 |text = casein kinase I activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0016055 |text = Wnt receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1452
| Hs_Ensembl = ENSG00000113712
| Hs_RefseqProtein = NP_001020276
| Hs_RefseqmRNA = NM_001025105
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 148855038
| Hs_GenLoc_end = 148911200
| Hs_Uniprot = P48729
| Mm_EntrezGene = 93687
| Mm_Ensembl = ENSMUSG00000024576
| Mm_RefseqmRNA = NM_146087
| Mm_RefseqProtein = NP_666199
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 18
| Mm_GenLoc_start = 61680702
| Mm_GenLoc_end = 61713672
| Mm_Uniprot = Q3TVX1
}}
}}
'''Casein kinase 1, alpha 1''', also known as '''CSNK1A1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CSNK1A1 casein kinase 1, alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1452| 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=Veis A, Sfeir C, Wu CB |title=Phosphorylation of the proteins of the extracellular matrix of mineralized tissues by casein kinase-like activity. |journal=Crit. Rev. Oral Biol. Med. |volume=8 |issue= 4 |pages= 360-79 |year= 1998 |pmid= 9391750 |doi= }}
*{{cite journal | author=Giaccia AJ, Kastan MB |title=The complexity of p53 modulation: emerging patterns from divergent signals. |journal=Genes Dev. |volume=12 |issue= 19 |pages= 2973-83 |year= 1998 |pmid= 9765199 |doi= }}
*{{cite journal | author=Brockman JL, Gross SD, Sussman MR, Anderson RA |title=Cell cycle-dependent localization of casein kinase I to mitotic spindles. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 20 |pages= 9454-8 |year= 1992 |pmid= 1409656 |doi= }}
*{{cite journal | author=Beyaert R, Vanhaesebroeck B, Declercq W, ''et al.'' |title=Casein kinase-1 phosphorylates the p75 tumor necrosis factor receptor and negatively regulates tumor necrosis factor signaling for apoptosis. |journal=J. Biol. Chem. |volume=270 |issue= 40 |pages= 23293-9 |year= 1995 |pmid= 7559483 |doi= }}
*{{cite journal | author=Gross SD, Hoffman DP, Fisette PL, ''et al.'' |title=A phosphatidylinositol 4,5-bisphosphate-sensitive casein kinase I alpha associates with synaptic vesicles and phosphorylates a subset of vesicle proteins. |journal=J. Cell Biol. |volume=130 |issue= 3 |pages= 711-24 |year= 1995 |pmid= 7622570 |doi= }}
*{{cite journal | author=Fish KJ, Cegielska A, Getman ME, ''et al.'' |title=Isolation and characterization of human casein kinase I epsilon (CKI), a novel member of the CKI gene family. |journal=J. Biol. Chem. |volume=270 |issue= 25 |pages= 14875-83 |year= 1995 |pmid= 7797465 |doi= }}
*{{cite journal | author=Tapia C, Featherstone T, Gómez C, ''et al.'' |title=Cloning and chromosomal localization of the gene coding for human protein kinase CK1. |journal=FEBS Lett. |volume=349 |issue= 2 |pages= 307-12 |year= 1994 |pmid= 8050587 |doi= }}
*{{cite journal | author=Huflejt ME, Turck CW, Lindstedt R, ''et al.'' |title=L-29, a soluble lactose-binding lectin, is phosphorylated on serine 6 and serine 12 in vivo and by casein kinase I. |journal=J. Biol. Chem. |volume=268 |issue= 35 |pages= 26712-8 |year= 1994 |pmid= 8253806 |doi= }}
*{{cite journal | author=de Groot RP, den Hertog J, Vandenheede JR, ''et al.'' |title=Multiple and cooperative phosphorylation events regulate the CREM activator function. |journal=EMBO J. |volume=12 |issue= 10 |pages= 3903-11 |year= 1993 |pmid= 8404858 |doi= }}
*{{cite journal | author=Walter J, Capell A, Grünberg J, ''et al.'' |title=The Alzheimer's disease-associated presenilins are differentially phosphorylated proteins located predominantly within the endoplasmic reticulum. |journal=Mol. Med. |volume=2 |issue= 6 |pages= 673-91 |year= 1997 |pmid= 8972483 |doi= }}
*{{cite journal | author=Krantz DE, Peter D, Liu Y, Edwards RH |title=Phosphorylation of a vesicular monoamine transporter by casein kinase II. |journal=J. Biol. Chem. |volume=272 |issue= 10 |pages= 6752-9 |year= 1997 |pmid= 9045708 |doi= }}
*{{cite journal | author=Dubois T, Rommel C, Howell S, ''et al.'' |title=14-3-3 is phosphorylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction. |journal=J. Biol. Chem. |volume=272 |issue= 46 |pages= 28882-8 |year= 1997 |pmid= 9360956 |doi= }}
*{{cite journal | author=Zhu J, Shibasaki F, Price R, ''et al.'' |title=Intramolecular masking of nuclear import signal on NF-AT4 by casein kinase I and MEKK1. |journal=Cell |volume=93 |issue= 5 |pages= 851-61 |year= 1998 |pmid= 9630228 |doi= }}
*{{cite journal | author=Gross SD, Loijens JC, Anderson RA |title=The casein kinase Ialpha isoform is both physically positioned and functionally competent to regulate multiple events of mRNA metabolism. |journal=J. Cell. Sci. |volume=112 ( Pt 16) |issue= |pages= 2647-56 |year= 1999 |pmid= 10413673 |doi= }}
*{{cite journal | author=Budd DC, McDonald JE, Tobin AB |title=Phosphorylation and regulation of a Gq/11-coupled receptor by casein kinase 1alpha. |journal=J. Biol. Chem. |volume=275 |issue= 26 |pages= 19667-75 |year= 2000 |pmid= 10777483 |doi= 10.1074/jbc.M000492200 }}
*{{cite journal | author=Faundez VV, Kelly RB |title=The AP-3 complex required for endosomal synaptic vesicle biogenesis is associated with a casein kinase Ialpha-like isoform. |journal=Mol. Biol. Cell |volume=11 |issue= 8 |pages= 2591-604 |year= 2000 |pmid= 10930456 |doi= }}
*{{cite journal | author=Mazurek N, Conklin J, Byrd JC, ''et al.'' |title=Phosphorylation of the beta-galactoside-binding protein galectin-3 modulates binding to its ligands. |journal=J. Biol. Chem. |volume=275 |issue= 46 |pages= 36311-5 |year= 2000 |pmid= 10961987 |doi= 10.1074/jbc.M003831200 }}
*{{cite journal | author=Dubois T, Kerai P, Zemlickova E, ''et al.'' |title=Casein kinase I associates with members of the centaurin-alpha family of phosphatidylinositol 3,4,5-trisphosphate-binding proteins. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 18757-64 |year= 2001 |pmid= 11278595 |doi= 10.1074/jbc.M010005200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CTAG1B... {November 18, 2007 10:39:37 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:41:31 AM 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 = Cancer/testis antigen 1B
| HGNCid = 2491
| Symbol = CTAG1B
| AltSymbols =; CTAG; CTAG1; ESO1; LAGE-2; LAGE2B; NY-ESO-1; CAMEL; ESO2; LAGE-1; LAGE-2b; MGC138724; MGC3803; LAGE2A
| OMIM = 300156
| ECnumber =
| Homologene = 37469
| MGIid =
| GeneAtlas_image1 = PBB_GE_CTAG1B_207337_at_tn.png
| GeneAtlas_image2 = PBB_GE_CTAG1B_210546_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_CTAG1B_211674_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005813 |text = centrosome}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0008150 |text = biological_process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1485
| Hs_Ensembl = ENSG00000126890
| Hs_RefseqProtein = NP_001318
| Hs_RefseqmRNA = NM_001327
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 153533440
| Hs_GenLoc_end = 153535047
| Hs_Uniprot = O75638
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Cancer/testis antigen 1B''', also known as '''CTAG1B''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CTAG1B cancer/testis antigen 1B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1485| 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=Scanlan MJ, Gure AO, Jungbluth AA, ''et al.'' |title=Cancer/testis antigens: an expanding family of targets for cancer immunotherapy. |journal=Immunol. Rev. |volume=188 |issue= |pages= 22-32 |year= 2003 |pmid= 12445278 |doi= }}
*{{cite journal | author=Chen YT, Scanlan MJ, Sahin U, ''et al.'' |title=A testicular antigen aberrantly expressed in human cancers detected by autologous antibody screening. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 5 |pages= 1914-8 |year= 1997 |pmid= 9050879 |doi= }}
*{{cite journal | author=Chen YT, Boyer AD, Viars CS, ''et al.'' |title=Genomic cloning and localization of CTAG, a gene encoding an autoimmunogenic cancer-testis antigen NY-ESO-1, to human chromosome Xq28. |journal=Cytogenet. Cell Genet. |volume=79 |issue= 3-4 |pages= 237-40 |year= 1998 |pmid= 9605863 |doi= }}
*{{cite journal | author=Lethé B, Lucas S, Michaux L, ''et al.'' |title=LAGE-1, a new gene with tumor specificity. |journal=Int. J. Cancer |volume=76 |issue= 6 |pages= 903-8 |year= 1998 |pmid= 9626360 |doi= }}
*{{cite journal | author=Wang RF, Johnston SL, Zeng G, ''et al.'' |title=A breast and melanoma-shared tumor antigen: T cell responses to antigenic peptides translated from different open reading frames. |journal=J. Immunol. |volume=161 |issue= 7 |pages= 3598-606 |year= 1998 |pmid= 9759882 |doi= }}
*{{cite journal | author=De Smet C, Lurquin C, Lethé B, ''et al.'' |title=DNA methylation is the primary silencing mechanism for a set of germ line- and tumor-specific genes with a CpG-rich promoter. |journal=Mol. Cell. Biol. |volume=19 |issue= 11 |pages= 7327-35 |year= 1999 |pmid= 10523621 |doi= }}
*{{cite journal | author=Schultz-Thater E, Noppen C, Gudat F, ''et al.'' |title=NY-ESO-1 tumour associated antigen is a cytoplasmic protein detectable by specific monoclonal antibodies in cell lines and clinical specimens. |journal=Br. J. Cancer |volume=83 |issue= 2 |pages= 204-8 |year= 2000 |pmid= 10901371 |doi= 10.1054/bjoc.2000.1251 }}
*{{cite journal | author=Rimoldi D, Rubio-Godoy V, Dutoit V, ''et al.'' |title=Efficient simultaneous presentation of NY-ESO-1/LAGE-1 primary and nonprimary open reading frame-derived CTL epitopes in melanoma. |journal=J. Immunol. |volume=165 |issue= 12 |pages= 7253-61 |year= 2001 |pmid= 11120859 |doi= }}
*{{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=Jungbluth AA, Chen YT, Stockert E, ''et al.'' |title=Immunohistochemical analysis of NY-ESO-1 antigen expression in normal and malignant human tissues. |journal=Int. J. Cancer |volume=92 |issue= 6 |pages= 856-60 |year= 2001 |pmid= 11351307 |doi= 10.1002/ijc.1282 }}
*{{cite journal | author=Goydos JS, Patel M, Shih W |title=NY-ESO-1 and CTp11 expression may correlate with stage of progression in melanoma. |journal=J. Surg. Res. |volume=98 |issue= 2 |pages= 76-80 |year= 2001 |pmid= 11397121 |doi= 10.1006/jsre.2001.6148 }}
*{{cite journal | author=Aradhya S, Bardaro T, Galgóczy P, ''et al.'' |title=Multiple pathogenic and benign genomic rearrangements occur at a 35 kb duplication involving the NEMO and LAGE2 genes. |journal=Hum. Mol. Genet. |volume=10 |issue= 22 |pages= 2557-67 |year= 2002 |pmid= 11709543 |doi= }}
*{{cite journal | author=Zarour HM, Maillere B, Brusic V, ''et al.'' |title=NY-ESO-1 119-143 is a promiscuous major histocompatibility complex class II T-helper epitope recognized by Th1- and Th2-type tumor-reactive CD4+ T cells. |journal=Cancer Res. |volume=62 |issue= 1 |pages= 213-8 |year= 2002 |pmid= 11782380 |doi= }}
*{{cite journal | author=Satie AP, Rajpert-De Meyts E, Spagnoli GC, ''et al.'' |title=The cancer-testis gene, NY-ESO-1, is expressed in normal fetal and adult testes and in spermatocytic seminomas and testicular carcinoma in situ. |journal=Lab. Invest. |volume=82 |issue= 6 |pages= 775-80 |year= 2002 |pmid= 12065688 |doi= }}
*{{cite journal | author=Nagata Y, Ono S, Matsuo M, ''et al.'' |title=Differential presentation of a soluble exogenous tumor antigen, NY-ESO-1, by distinct human dendritic cell populations. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 16 |pages= 10629-34 |year= 2002 |pmid= 12138174 |doi= 10.1073/pnas.112331099 }}
*{{cite journal | author=Resnick MB, Sabo E, Kondratev S, ''et al.'' |title=Cancer-testis antigen expression in uterine malignancies with an emphasis on carcinosarcomas and papillary serous carcinomas. |journal=Int. J. Cancer |volume=101 |issue= 2 |pages= 190-5 |year= 2002 |pmid= 12209997 |doi= 10.1002/ijc.10585 }}
*{{cite journal | author=Peng LP, Liu HY, Ran YL, ''et al.'' |title=[Expression of NY-ESO-1 gene in human esophageal carcinoma and its cloning] |journal=Ai Zheng |volume=21 |issue= 5 |pages= 469-72 |year= 2003 |pmid= 12452034 |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=Gnjatic S, Atanackovic D, Jäger E, ''et al.'' |title=Survey of naturally occurring CD4+ T cell responses against NY-ESO-1 in cancer patients: correlation with antibody responses. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 15 |pages= 8862-7 |year= 2003 |pmid= 12853579 |doi= 10.1073/pnas.1133324100 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DDB1... {November 18, 2007 10:41:31 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:42:05 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_DDB1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2b5l.
| PDB = {{PDB2|2b5l}}, {{PDB2|2b5m}}, {{PDB2|2b5n}}, {{PDB2|2hye}}
| Name = Damage-specific DNA binding protein 1, 127kDa
| HGNCid = 2717
| Symbol = DDB1
| AltSymbols =; DDBA; UV-DDB1; XAP1; XPCE; XPE; XPE-BF
| OMIM = 600045
| ECnumber =
| Homologene = 1448
| MGIid = 1202384
| Function = {{GNF_GO|id=GO:0003676 |text = nucleic acid binding}} {{GNF_GO|id=GO:0003684 |text = damaged DNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006289 |text = nucleotide-excision repair}} {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1642
| Hs_Ensembl =
| Hs_RefseqProtein = XP_001128974
| Hs_RefseqmRNA = XM_001128974
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 13194
| Mm_Ensembl = ENSMUSG00000024740
| Mm_RefseqmRNA = NM_015735
| Mm_RefseqProtein = NP_056550
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 10672670
| Mm_GenLoc_end = 10696867
| Mm_Uniprot =
}}
}}
'''Damage-specific DNA binding protein 1, 127kDa''', also known as '''DDB1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DDB1 damage-specific DNA binding protein 1, 127kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1642| 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 large subunit of DNA damage-binding protein which is a heterodimer composed of a large and a small subunit. This protein functions in nucleotide-excision repair. Its defective activity causes the repair defect in the patients with xeroderma pigmentosum complementation group E (XPE). However, it remains for mutation analysis to demonstrate whether the defect in XPE patients is in this gene or the gene encoding the small subunit. In addition, Best vitelliform mascular dystrophy is mapped to the same region as this gene on 11q, but no sequence alternations of this gene are demonstrated in Best disease patients.<ref name="entrez">{{cite web | title = Entrez Gene: DDB1 damage-specific DNA binding protein 1, 127kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1642| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Chu G, Chang E |title=Xeroderma pigmentosum group E cells lack a nuclear factor that binds to damaged DNA. |journal=Science |volume=242 |issue= 4878 |pages= 564-7 |year= 1988 |pmid= 3175673 |doi= }}
*{{cite journal | author=Lee TH, Elledge SJ, Butel JS |title=Hepatitis B virus X protein interacts with a probable cellular DNA repair protein. |journal=J. Virol. |volume=69 |issue= 2 |pages= 1107-14 |year= 1995 |pmid= 7815490 |doi= }}
*{{cite journal | author=Keeney S, Eker AP, Brody T, ''et al.'' |title=Correction of the DNA repair defect in xeroderma pigmentosum group E by injection of a DNA damage-binding protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 9 |pages= 4053-6 |year= 1994 |pmid= 8171034 |doi= }}
*{{cite journal | author=Keeney S, Chang GJ, Linn S |title=Characterization of a human DNA damage binding protein implicated in xeroderma pigmentosum E. |journal=J. Biol. Chem. |volume=268 |issue= 28 |pages= 21293-300 |year= 1993 |pmid= 8407967 |doi= }}
*{{cite journal | author=Dualan R, Brody T, Keeney S, ''et al.'' |title=Chromosomal localization and cDNA cloning of the genes (DDB1 and DDB2) for the p127 and p48 subunits of a human damage-specific DNA binding protein. |journal=Genomics |volume=29 |issue= 1 |pages= 62-9 |year= 1996 |pmid= 8530102 |doi= 10.1006/geno.1995.1215 }}
*{{cite journal | author=Hwang BJ, Liao JC, Chu G |title=Isolation of a cDNA encoding a UV-damaged DNA binding factor defective in xeroderma pigmentosum group E cells. |journal=Mutat. Res. |volume=362 |issue= 1 |pages= 105-17 |year= 1996 |pmid= 8538642 |doi= }}
*{{cite journal | author=Nichols AF, Ong P, Linn S |title=Mutations specific to the xeroderma pigmentosum group E Ddb- phenotype. |journal=J. Biol. Chem. |volume=271 |issue= 40 |pages= 24317-20 |year= 1996 |pmid= 8798680 |doi= }}
*{{cite journal | author=Seki N, Hayashi A, Hattori A, ''et al.'' |title=cDNA cloning, tissue expression, and chromosomal assignment of a mouse gene, encoding a 127 kDa UV-damaged DNA binding protein which is defective in XPE cells. |journal=DNA Res. |volume=6 |issue= 5 |pages= 319-22 |year= 2000 |pmid= 10574459 |doi= }}
*{{cite journal | author=Liu W, Nichols AF, Graham JA, ''et al.'' |title=Nuclear transport of human DDB protein induced by ultraviolet light. |journal=J. Biol. Chem. |volume=275 |issue= 28 |pages= 21429-34 |year= 2000 |pmid= 10777491 |doi= 10.1074/jbc.M000961200 }}
*{{cite journal | author=Martinez E, Palhan VB, Tjernberg A, ''et al.'' |title=Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo. |journal=Mol. Cell. Biol. |volume=21 |issue= 20 |pages= 6782-95 |year= 2001 |pmid= 11564863 |doi= 10.1128/MCB.21.20.6782-6795.2001 }}
*{{cite journal | author=Chen X, Zhang Y, Douglas L, Zhou P |title=UV-damaged DNA-binding proteins are targets of CUL-4A-mediated ubiquitination and degradation. |journal=J. Biol. Chem. |volume=276 |issue= 51 |pages= 48175-82 |year= 2002 |pmid= 11673459 |doi= 10.1074/jbc.M106808200 }}
*{{cite journal | author=Rapić-Otrin V, McLenigan MP, Bisi DC, ''et al.'' |title=Sequential binding of UV DNA damage binding factor and degradation of the p48 subunit as early events after UV irradiation. |journal=Nucleic Acids Res. |volume=30 |issue= 11 |pages= 2588-98 |year= 2002 |pmid= 12034848 |doi= }}
*{{cite journal | author=Bergametti F, Sitterlin D, Transy C |title=Turnover of hepatitis B virus X protein is regulated by damaged DNA-binding complex. |journal=J. Virol. |volume=76 |issue= 13 |pages= 6495-501 |year= 2002 |pmid= 12050362 |doi= }}
*{{cite journal | author=Bontron S, Lin-Marq N, Strubin M |title=Hepatitis B virus X protein associated with UV-DDB1 induces cell death in the nucleus and is functionally antagonized by UV-DDB2. |journal=J. Biol. Chem. |volume=277 |issue= 41 |pages= 38847-54 |year= 2002 |pmid= 12151405 |doi= 10.1074/jbc.M205722200 }}
*{{cite journal | author=Andrejeva J, Poole E, Young DF, ''et al.'' |title=The p127 subunit (DDB1) of the UV-DNA damage repair binding protein is essential for the targeted degradation of STAT1 by the V protein of the paramyxovirus simian virus 5. |journal=J. Virol. |volume=76 |issue= 22 |pages= 11379-86 |year= 2002 |pmid= 12388698 |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=Groisman R, Polanowska J, Kuraoka I, ''et al.'' |title=The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. |journal=Cell |volume=113 |issue= 3 |pages= 357-67 |year= 2003 |pmid= 12732143 |doi= }}
*{{cite journal | author=Leupin O, Bontron S, Strubin M |title=Hepatitis B virus X protein and simian virus 5 V protein exhibit similar UV-DDB1 binding properties to mediate distinct activities. |journal=J. Virol. |volume=77 |issue= 11 |pages= 6274-83 |year= 2003 |pmid= 12743284 |doi= }}
*{{cite journal | author=Wertz IE, O'Rourke KM, Zhang Z, ''et al.'' |title=Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin ligase. |journal=Science |volume=303 |issue= 5662 |pages= 1371-4 |year= 2004 |pmid= 14739464 |doi= 10.1126/science.1093549 }}
*{{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 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on EFNA1... {November 18, 2007 10:42:05 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:42:42 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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| update_protein_box = yes
| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Ephrin-A1
| HGNCid = 3221
| Symbol = EFNA1
| AltSymbols =; B61; ECKLG; EFL1; EPLG1; LERK1; TNFAIP4
| OMIM = 191164
| ECnumber =
| Homologene = 3262
| MGIid = 103236
| GeneAtlas_image1 = PBB_GE_EFNA1_202023_at_tn.png
| Function = {{GNF_GO|id=GO:0046875 |text = ephrin receptor binding}} {{GNF_GO|id=GO:0048503 |text = GPI anchor binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0000187 |text = activation of MAPK activity}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0030182 |text = neuron differentiation}} {{GNF_GO|id=GO:0048013 |text = ephrin receptor signaling pathway}} {{GNF_GO|id=GO:0050770 |text = regulation of axonogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1942
| Hs_Ensembl = ENSG00000169242
| Hs_RefseqProtein = NP_004419
| Hs_RefseqmRNA = NM_004428
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 153366560
| Hs_GenLoc_end = 153373957
| Hs_Uniprot = P20827
| Mm_EntrezGene = 13636
| Mm_Ensembl = ENSMUSG00000027954
| Mm_RefseqmRNA = NM_010107
| Mm_RefseqProtein = NP_034237
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 89357663
| Mm_GenLoc_end = 89365568
| Mm_Uniprot = Q9D7K8
}}
}}
'''Ephrin-A1''', also known as '''EFNA1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EFNA1 ephrin-A1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1942| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the ephrin (EPH) family. The ephrins and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. This gene encodes an EFNA class ephrin which binds to the EPHA2, EPHA4, EPHA5, EPHA6, and EPHA7 receptors. Two transcript variants that encode different isoforms were identified through sequence analysis.<ref name="entrez">{{cite web | title = Entrez Gene: EFNA1 ephrin-A1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1942| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Pandey A, Lindberg RA, Dixit VM |title=Cell signalling. Receptor orphans find a family. |journal=Curr. Biol. |volume=5 |issue= 9 |pages= 986-9 |year= 1996 |pmid= 8542290 |doi= }}
*{{cite journal | author=Flanagan JG, Vanderhaeghen P |title=The ephrins and Eph receptors in neural development. |journal=Annu. Rev. Neurosci. |volume=21 |issue= |pages= 309-45 |year= 1998 |pmid= 9530499 |doi= 10.1146/annurev.neuro.21.1.309 }}
*{{cite journal | author=Zhou R |title=The Eph family receptors and ligands. |journal=Pharmacol. Ther. |volume=77 |issue= 3 |pages= 151-81 |year= 1998 |pmid= 9576626 |doi= }}
*{{cite journal | author=Holder N, Klein R |title=Eph receptors and ephrins: effectors of morphogenesis. |journal=Development |volume=126 |issue= 10 |pages= 2033-44 |year= 1999 |pmid= 10207129 |doi= }}
*{{cite journal | author=Wilkinson DG |title=Eph receptors and ephrins: regulators of guidance and assembly. |journal=Int. Rev. Cytol. |volume=196 |issue= |pages= 177-244 |year= 2000 |pmid= 10730216 |doi= }}
*{{cite journal | author=Xu Q, Mellitzer G, Wilkinson DG |title=Roles of Eph receptors and ephrins in segmental patterning. |journal=Philos. Trans. R. Soc. Lond., B, Biol. Sci. |volume=355 |issue= 1399 |pages= 993-1002 |year= 2001 |pmid= 11128993 |doi= 10.1098/rstb.2000.0635 }}
*{{cite journal | author=Wilkinson DG |title=Multiple roles of EPH receptors and ephrins in neural development. |journal=Nat. Rev. Neurosci. |volume=2 |issue= 3 |pages= 155-64 |year= 2001 |pmid= 11256076 |doi= }}
*{{cite journal | author=Holzman LB, Marks RM, Dixit VM |title=A novel immediate-early response gene of endothelium is induced by cytokines and encodes a secreted protein. |journal=Mol. Cell. Biol. |volume=10 |issue= 11 |pages= 5830-8 |year= 1990 |pmid= 2233719 |doi= }}
*{{cite journal | author=Mahadevan D, Thanki N, Singh J, ''et al.'' |title=Structural studies on the PH domains of Db1, Sos1, IRS-1, and beta ARK1 and their differential binding to G beta gamma subunits. |journal=Biochemistry |volume=34 |issue= 28 |pages= 9111-7 |year= 1995 |pmid= 7619809 |doi= }}
*{{cite journal | author=Kozlosky CJ, Maraskovsky E, McGrew JT, ''et al.'' |title=Ligands for the receptor tyrosine kinases hek and elk: isolation of cDNAs encoding a family of proteins. |journal=Oncogene |volume=10 |issue= 2 |pages= 299-306 |year= 1995 |pmid= 7838529 |doi= }}
*{{cite journal | author=Davis S, Gale NW, Aldrich TH, ''et al.'' |title=Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity. |journal=Science |volume=266 |issue= 5186 |pages= 816-9 |year= 1994 |pmid= 7973638 |doi= }}
*{{cite journal | author=Beckmann MP, Cerretti DP, Baum P, ''et al.'' |title=Molecular characterization of a family of ligands for eph-related tyrosine kinase receptors. |journal=EMBO J. |volume=13 |issue= 16 |pages= 3757-62 |year= 1994 |pmid= 8070404 |doi= }}
*{{cite journal | author=Cerretti DP, Lyman SD, Kozlosky CJ, ''et al.'' |title=The genes encoding the eph-related receptor tyrosine kinase ligands LERK-1 (EPLG1, Epl1), LERK-3 (EPLG3, Epl3), and LERK-4 (EPLG4, Epl4) are clustered on human chromosome 1 and mouse chromosome 3. |journal=Genomics |volume=33 |issue= 2 |pages= 277-82 |year= 1997 |pmid= 8660976 |doi= 10.1006/geno.1996.0192 }}
*{{cite journal | author=Gale NW, Holland SJ, Valenzuela DM, ''et al.'' |title=Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis. |journal=Neuron |volume=17 |issue= 1 |pages= 9-19 |year= 1996 |pmid= 8755474 |doi= }}
*{{cite journal | author= |title=Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee. |journal=Cell |volume=90 |issue= 3 |pages= 403-4 |year= 1997 |pmid= 9267020 |doi= }}
*{{cite journal | author=Nagel W, Schilcher P, Zeitlmann L, Kolanus W |title=The PH domain and the polybasic c domain of cytohesin-1 cooperate specifically in plasma membrane association and cellular function. |journal=Mol. Biol. Cell |volume=9 |issue= 8 |pages= 1981-94 |year= 1998 |pmid= 9693361 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ETS2... {November 18, 2007 10:42:42 AM PST}
- SEARCH REDIRECT: Control Box Found: ETS2 {November 18, 2007 10:43:08 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:43:09 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:43:09 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:43:09 AM PST}
- UPDATED: Updated protein page: ETS2 {November 18, 2007 10:43:16 AM PST}
- INFO: Beginning work on GAD2... {November 18, 2007 10:43:16 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:43:57 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_GAD2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2okk.
| PDB = {{PDB2|2okk}}
| Name = Glutamate decarboxylase 2 (pancreatic islets and brain, 65kDa)
| HGNCid = 4093
| Symbol = GAD2
| AltSymbols =; GAD65; MGC161605; MGC161607
| OMIM = 138275
| ECnumber =
| Homologene = 20223
| MGIid = 95634
| GeneAtlas_image1 = PBB_GE_GAD2_206780_at_tn.png
| GeneAtlas_image2 = PBB_GE_GAD2_211264_at_tn.png
| GeneAtlas_image3 = PBB_GE_GAD2_216651_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004351 |text = glutamate decarboxylase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016829 |text = lyase activity}} {{GNF_GO|id=GO:0016831 |text = carboxy-lyase activity}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0030424 |text = axon}} {{GNF_GO|id=GO:0045202 |text = synapse}}
| Process = {{GNF_GO|id=GO:0006540 |text = glutamate decarboxylation to succinate}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0019752 |text = carboxylic acid metabolic process}} {{GNF_GO|id=GO:0042136 |text = neurotransmitter biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2572
| Hs_Ensembl = ENSG00000136750
| Hs_RefseqProtein = NP_000809
| Hs_RefseqmRNA = NM_000818
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 26545242
| Hs_GenLoc_end = 26633493
| Hs_Uniprot = Q05329
| Mm_EntrezGene = 14417
| Mm_Ensembl = ENSMUSG00000026787
| Mm_RefseqmRNA = NM_008078
| Mm_RefseqProtein = NP_032104
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 22473965
| Mm_GenLoc_end = 22542637
| Mm_Uniprot = Q3URJ3
}}
}}
'''Glutamate decarboxylase 2 (pancreatic islets and brain, 65kDa)''', also known as '''GAD2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GAD2 glutamate decarboxylase 2 (pancreatic islets and brain, 65kDa)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2572| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes one of several forms of glutamic acid decarboxylase, identified as a major autoantigen in insulin-dependent diabetes. The enzyme encoded is responsible for catalyzing the production of gamma-aminobutyric acid from L-glutamic acid. A pathogenic role for this enzyme has been identified in the human pancreas since it has been identified as an autoantibody and an autoreactive T cell target in insulin-dependent diabetes. This gene may also play a role in the stiff man syndrome.<ref name="entrez">{{cite web | title = Entrez Gene: GAD2 glutamate decarboxylase 2 (pancreatic islets and brain, 65kDa)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2572| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bu DF, Erlander MG, Hitz BC, ''et al.'' |title=Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 6 |pages= 2115-9 |year= 1992 |pmid= 1549570 |doi= }}
*{{cite journal | author=Karlsen AE, Hagopian WA, Grubin CE, ''et al.'' |title=Cloning and primary structure of a human islet isoform of glutamic acid decarboxylase from chromosome 10. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 19 |pages= 8337-41 |year= 1991 |pmid= 1924293 |doi= }}
*{{cite journal | author=Cram DS, Barnett LD, Joseph JL, Harrison LC |title=Cloning and partial nucleotide sequence of human glutamic acid decarboxylase cDNA from brain and pancreatic islets. |journal=Biochem. Biophys. Res. Commun. |volume=176 |issue= 3 |pages= 1239-44 |year= 1991 |pmid= 2039509 |doi= }}
*{{cite journal | author=Mauch L, Abney CC, Berg H, ''et al.'' |title=Characterization of a linear epitope within the human pancreatic 64-kDa glutamic acid decarboxylase and its autoimmune recognition by sera from insulin-dependent diabetes mellitus patients. |journal=Eur. J. Biochem. |volume=212 |issue= 2 |pages= 597-603 |year= 1993 |pmid= 7680313 |doi= }}
*{{cite journal | author=Dirkx R, Thomas A, Li L, ''et al.'' |title=Targeting of the 67-kDa isoform of glutamic acid decarboxylase to intracellular organelles is mediated by its interaction with the NH2-terminal region of the 65-kDa isoform of glutamic acid decarboxylase. |journal=J. Biol. Chem. |volume=270 |issue= 5 |pages= 2241-6 |year= 1995 |pmid= 7836456 |doi= }}
*{{cite journal | author=Bu DF, Tobin AJ |title=The exon-intron organization of the genes (GAD1 and GAD2) encoding two human glutamate decarboxylases (GAD67 and GAD65) suggests that they derive from a common ancestral GAD. |journal=Genomics |volume=21 |issue= 1 |pages= 222-8 |year= 1994 |pmid= 8088791 |doi= 10.1006/geno.1994.1246 }}
*{{cite journal | author=Kim J, Richter W, Aanstoot HJ, ''et al.'' |title=Differential expression of GAD65 and GAD67 in human, rat, and mouse pancreatic islets. |journal=Diabetes |volume=42 |issue= 12 |pages= 1799-808 |year= 1993 |pmid= 8243826 |doi= }}
*{{cite journal | author=Asada H, Kawamura Y, Maruyama K, ''et al.'' |title=Mice lacking the 65 kDa isoform of glutamic acid decarboxylase (GAD65) maintain normal levels of GAD67 and GABA in their brains but are susceptible to seizures. |journal=Biochem. Biophys. Res. Commun. |volume=229 |issue= 3 |pages= 891-5 |year= 1997 |pmid= 8954991 |doi= }}
*{{cite journal | author=Namchuk M, Lindsay L, Turck CW, ''et al.'' |title=Phosphorylation of serine residues 3, 6, 10, and 13 distinguishes membrane anchored from soluble glutamic acid decarboxylase 65 and is restricted to glutamic acid decarboxylase 65alpha. |journal=J. Biol. Chem. |volume=272 |issue= 3 |pages= 1548-57 |year= 1997 |pmid= 8999827 |doi= }}
*{{cite journal | author=Chessler SD, Lernmark A |title=Alternative splicing of GAD67 results in the synthesis of a third form of glutamic-acid decarboxylase in human islets and other non-neural tissues. |journal=J. Biol. Chem. |volume=275 |issue= 7 |pages= 5188-92 |year= 2000 |pmid= 10671565 |doi= }}
*{{cite journal | author=Santos J, Antón EA, Buslje CM, ''et al.'' |title=Replacement of methionine-161 with threonine eliminates a major by-product of human glutamate decarboxylase 65-kDa variant expression in Escherichia coli. |journal=Biotechnol. Appl. Biochem. |volume=31 ( Pt 3) |issue= |pages= 205-12 |year= 2000 |pmid= 10814590 |doi= }}
*{{cite journal | author=Roep BO, Hiemstra HS, Schloot NC, ''et al.'' |title=Molecular mimicry in type 1 diabetes: immune cross-reactivity between islet autoantigen and human cytomegalovirus but not Coxsackie virus. |journal=Ann. N. Y. Acad. Sci. |volume=958 |issue= |pages= 163-5 |year= 2002 |pmid= 12021098 |doi= }}
*{{cite journal | author=Tong JC, Myers MA, Mackay IR, ''et al.'' |title=The PEVKEK region of the pyridoxal phosphate binding domain of GAD65 expresses a dominant B cell epitope for type 1 diabetes sera. |journal=Ann. N. Y. Acad. Sci. |volume=958 |issue= |pages= 182-9 |year= 2002 |pmid= 12021103 |doi= }}
*{{cite journal | author=Jaume JC, Parry SL, Madec AM, ''et al.'' |title=Suppressive effect of glutamic acid decarboxylase 65-specific autoimmune B lymphocytes on processing of T cell determinants located within the antibody epitope. |journal=J. Immunol. |volume=169 |issue= 2 |pages= 665-72 |year= 2002 |pmid= 12097368 |doi= }}
*{{cite journal | author=Johnson GC, Payne F, Nutland S, ''et al.'' |title=A comprehensive, statistically powered analysis of GAD2 in type 1 diabetes. |journal=Diabetes |volume=51 |issue= 9 |pages= 2866-70 |year= 2002 |pmid= 12196483 |doi= }}
*{{cite journal | author=Costa M, Saiz A, Casamitjana R, ''et al.'' |title=T-cell reactivity to glutamic acid decarboxylase in stiff-man syndrome and cerebellar ataxia associated with polyendocrine autoimmunity. |journal=Clin. Exp. Immunol. |volume=129 |issue= 3 |pages= 471-8 |year= 2002 |pmid= 12197888 |doi= }}
*{{cite journal | author=Al-Bukhari TA, Radford PM, Bouras G, ''et al.'' |title=Distinct antigenic features of linear epitopes at the N-terminus and C-terminus of 65 kDa glutamic acid decarboxylase (GAD65): implications for autoantigen modification during pathogenesis. |journal=Clin. Exp. Immunol. |volume=130 |issue= 1 |pages= 131-9 |year= 2002 |pmid= 12296864 |doi= }}
*{{cite journal | author=Kanaani J, el-Husseini Ael-D, Aguilera-Moreno A, ''et al.'' |title=A combination of three distinct trafficking signals mediates axonal targeting and presynaptic clustering of GAD65. |journal=J. Cell Biol. |volume=158 |issue= 7 |pages= 1229-38 |year= 2002 |pmid= 12356867 |doi= }}
*{{cite journal | author=Luo J, Kaplitt MG, Fitzsimons HL, ''et al.'' |title=Subthalamic GAD gene therapy in a Parkinson's disease rat model. |journal=Science |volume=298 |issue= 5592 |pages= 425-9 |year= 2002 |pmid= 12376704 |doi= 10.1126/science.1074549 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GDI1... {November 18, 2007 10:43:57 AM PST}
- SEARCH REDIRECT: Control Box Found: GDI1 {November 18, 2007 10:44:43 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:44:45 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:44:45 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:44:45 AM PST}
- UPDATED: Updated protein page: GDI1 {November 18, 2007 10:44:53 AM PST}
- INFO: Beginning work on MALT1... {November 18, 2007 10:51:26 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:52:15 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_MALT1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2g7r.
| PDB = {{PDB2|2g7r}}
| Name = Mucosa associated lymphoid tissue lymphoma translocation gene 1
| HGNCid = 6819
| Symbol = MALT1
| AltSymbols =; DKFZp434L132; MLT; MLT1
| OMIM = 604860
| ECnumber =
| Homologene = 4938
| MGIid = 2445027
| GeneAtlas_image1 = PBB_GE_MALT1_210017_at_tn.png
| GeneAtlas_image2 = PBB_GE_MALT1_208309_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_MALT1_210018_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004842 |text = ubiquitin-protein ligase activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}} {{GNF_GO|id=GO:0019209 |text = kinase activator activity}} {{GNF_GO|id=GO:0030693 |text = caspase activity}} {{GNF_GO|id=GO:0043621 |text = protein self-association}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0032449 |text = CBM complex}}
| Process = {{GNF_GO|id=GO:0002726 |text = positive regulation of T cell cytokine production}} {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0006952 |text = defense response}} {{GNF_GO|id=GO:0007250 |text = activation of NF-kappaB-inducing kinase}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}} {{GNF_GO|id=GO:0050852 |text = T cell receptor signaling pathway}} {{GNF_GO|id=GO:0050870 |text = positive regulation of T cell activation}} {{GNF_GO|id=GO:0051168 |text = nuclear export}} {{GNF_GO|id=GO:0051259 |text = protein oligomerization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10892
| Hs_Ensembl = ENSG00000172175
| Hs_RefseqProtein = NP_006776
| Hs_RefseqmRNA = NM_006785
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 18
| Hs_GenLoc_start = 54489598
| Hs_GenLoc_end = 54568350
| Hs_Uniprot = Q9UDY8
| Mm_EntrezGene = 240354
| Mm_Ensembl = ENSMUSG00000032688
| Mm_RefseqmRNA = NM_172833
| Mm_RefseqProtein = NP_766421
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 18
| Mm_GenLoc_start = 65556332
| Mm_GenLoc_end = 65604192
| Mm_Uniprot = Q8BRB5
}}
}}
'''Mucosa associated lymphoid tissue lymphoma translocation gene 1''', also known as '''MALT1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MALT1 mucosa associated lymphoid tissue lymphoma translocation gene 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10892| 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 has been found to be recurrently rearranged in chromosomal translocation with two other genes - baculoviral IAP repeat-containing protein 3 (also known as apoptosis inhibitor 2) and immunoglobulin heavy chain locus - in mucosa-associated lymphoid tissue lymphomas. The protein encoded by this gene may play a role in NF-kappaB activation. Two alternatively spliced transcript variants encoding different isoforms have been described for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: MALT1 mucosa associated lymphoid tissue lymphoma translocation gene 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10892| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bertoni F, Cavalli F, Cotter FE, Zucca E |title=Genetic alterations underlying the pathogenesis of MALT lymphoma. |journal=Hematol. J. |volume=3 |issue= 1 |pages= 10-3 |year= 2003 |pmid= 11960389 |doi= 10.1038/sj/thj/6200146 }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi= }}
*{{cite journal | author=Dierlamm J, Baens M, Wlodarska I, ''et al.'' |title=The apoptosis inhibitor gene API2 and a novel 18q gene, MLT, are recurrently rearranged in the t(11;18)(q21;q21) associated with mucosa-associated lymphoid tissue lymphomas. |journal=Blood |volume=93 |issue= 11 |pages= 3601-9 |year= 1999 |pmid= 10339464 |doi= }}
*{{cite journal | author=Hosaka S, Akamatsu T, Nakamura S, ''et al.'' |title=Mucosa-associated lymphoid tissue (MALT) lymphoma of the rectum with chromosomal translocation of the t(11;18)(q21;q21) and an additional aberration of trisomy 3. |journal=Am. J. Gastroenterol. |volume=94 |issue= 7 |pages= 1951-4 |year= 1999 |pmid= 10406266 |doi= }}
*{{cite journal | author=Akagi T, Motegi M, Tamura A, ''et al.'' |title=A novel gene, MALT1 at 18q21, is involved in t(11;18) (q21;q21) found in low-grade B-cell lymphoma of mucosa-associated lymphoid tissue. |journal=Oncogene |volume=18 |issue= 42 |pages= 5785-94 |year= 1999 |pmid= 10523859 |doi= }}
*{{cite journal | author=Suzuki H, Motegi M, Akagi T, ''et al.'' |title=API1-MALT1-MLT is involved in mucosa-associated lymphoid tissue lymphoma with t(11;18)(q21;q21) |journal=Blood |volume=94 |issue= 9 |pages= 3270-1 |year= 1999 |pmid= 10610122 |doi= }}
*{{cite journal | author=Morgan JA, Yin Y, Borowsky AD, ''et al.'' |title=Breakpoints of the t(11;18)(q21;q21) in mucosa-associated lymphoid tissue (MALT) lymphoma lie within or near the previously undescribed gene MALT1 in chromosome 18. |journal=Cancer Res. |volume=59 |issue= 24 |pages= 6205-13 |year= 2000 |pmid= 10626814 |doi= }}
*{{cite journal | author=Motegi M, Yonezumi M, Suzuki H, ''et al.'' |title=API2-MALT1 chimeric transcripts involved in mucosa-associated lymphoid tissue type lymphoma predict heterogeneous products. |journal=Am. J. Pathol. |volume=156 |issue= 3 |pages= 807-12 |year= 2000 |pmid= 10702396 |doi= }}
*{{cite journal | author=Uren AG, O'Rourke K, Aravind LA, ''et al.'' |title=Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma. |journal=Mol. Cell |volume=6 |issue= 4 |pages= 961-7 |year= 2000 |pmid= 11090634 |doi= }}
*{{cite journal | author=Stoffel A, Le Beau MM |title=The API2/MALT1 fusion product may lead to germinal center B cell lymphomas by suppression of apoptosis. |journal=Hum. Hered. |volume=51 |issue= 1-2 |pages= 1-7 |year= 2001 |pmid= 11096264 |doi= }}
*{{cite journal | author=Sato Y, Akiyama Y, Tanizawa T, ''et al.'' |title=Molecular characterization of the genomic breakpoint junction in the t(11;18) (q21;q21) translocation of a gastric MALT lymphoma. |journal=Biochem. Biophys. Res. Commun. |volume=280 |issue= 1 |pages= 301-6 |year= 2001 |pmid= 11162514 |doi= 10.1006/bbrc.2000.4124 }}
*{{cite journal | author=Lucas PC, Yonezumi M, Inohara N, ''et al.'' |title=Bcl10 and MALT1, independent targets of chromosomal translocation in malt lymphoma, cooperate in a novel NF-kappa B signaling pathway. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 19012-9 |year= 2001 |pmid= 11262391 |doi= 10.1074/jbc.M009984200 }}
*{{cite journal | author=Vega F, Medeiros LJ |title=Marginal-zone B-cell lymphoma of extranodal mucosa-associated lymphoid tissue type: molecular genetics provides new insights into pathogenesis. |journal=Advances in anatomic pathology |volume=8 |issue= 6 |pages= 313-26 |year= 2002 |pmid= 11707622 |doi= }}
*{{cite journal | author=Streubel B, Lamprecht A, Dierlamm J, ''et al.'' |title=T(14;18)(q32;q21) involving IGH and MALT1 is a frequent chromosomal aberration in MALT lymphoma. |journal=Blood |volume=101 |issue= 6 |pages= 2335-9 |year= 2003 |pmid= 12406890 |doi= 10.1182/blood-2002-09-2963 }}
*{{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=Okabe M, Inagaki H, Ohshima K, ''et al.'' |title=API2-MALT1 fusion defines a distinctive clinicopathologic subtype in pulmonary extranodal marginal zone B-cell lymphoma of mucosa-associated lymphoid tissue. |journal=Am. J. Pathol. |volume=162 |issue= 4 |pages= 1113-22 |year= 2003 |pmid= 12651604 |doi= }}
*{{cite journal | author=Matsuda A, Suzuki Y, Honda G, ''et al.'' |title=Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. |journal=Oncogene |volume=22 |issue= 21 |pages= 3307-18 |year= 2003 |pmid= 12761501 |doi= 10.1038/sj.onc.1206406 }}
*{{cite journal | author=Reed JC, Doctor K, Rojas A, ''et al.'' |title=Comparative analysis of apoptosis and inflammation genes of mice and humans. |journal=Genome Res. |volume=13 |issue= 6B |pages= 1376-88 |year= 2003 |pmid= 12819136 |doi= 10.1101/gr.1053803 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NEDD4L... {November 18, 2007 10:52:15 AM PST}
- SEARCH REDIRECT: Control Box Found: NEDD4L {November 18, 2007 10:52:42 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:52:43 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:52:43 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:52:43 AM PST}
- UPDATED: Updated protein page: NEDD4L {November 18, 2007 10:52:49 AM PST}
- INFO: Beginning work on OGT... {November 18, 2007 10:48:22 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:49:06 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_OGT_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1w3b.
| PDB = {{PDB2|1w3b}}
| Name = O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase)
| HGNCid = 8127
| Symbol = OGT
| AltSymbols =; FLJ23071; HRNT1; MGC22921; O-GLCNAC
| OMIM = 300255
| ECnumber =
| Homologene = 9675
| MGIid = 1339639
| GeneAtlas_image1 = PBB_GE_OGT_207563_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_OGT_207564_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_OGT_209240_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008375 |text = acetylglucosaminyltransferase activity}} {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006493 |text = protein amino acid O-linked glycosylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007584 |text = response to nutrient}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8473
| Hs_Ensembl = ENSG00000147162
| Hs_RefseqProtein = NP_858058
| Hs_RefseqmRNA = NM_181672
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 70669658
| Hs_GenLoc_end = 70712472
| Hs_Uniprot = O15294
| Mm_EntrezGene = 108155
| Mm_Ensembl = ENSMUSG00000034160
| Mm_RefseqmRNA = NM_139144
| Mm_RefseqProtein = NP_631883
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 97842783
| Mm_GenLoc_end = 97887068
| Mm_Uniprot =
}}
}}
'''O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase)''', also known as '''OGT''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: OGT O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8473| 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 = O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) catalyzes the addition of a single N-acetylglucosamine in O-glycosidic linkage to serine or threonine residues. Since both phosphorylation and glycosylation compete for similar serine or threonine residues, the two processes may compete for sites, or they may alter the substrate specificity of nearby sites by steric or electrostatic effects. The protein contains nine tetratricopeptide repeats and a putative bipartite nuclear localization signal. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: OGT O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8473| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Konrad RJ, Kudlow JE |title=The role of O-linked protein glycosylation in beta-cell dysfunction. |journal=Int. J. Mol. Med. |volume=10 |issue= 5 |pages= 535-9 |year= 2002 |pmid= 12373287 |doi= }}
*{{cite journal | author=Reason AJ, Morris HR, Panico M, ''et al.'' |title=Localization of O-GlcNAc modification on the serum response transcription factor. |journal=J. Biol. Chem. |volume=267 |issue= 24 |pages= 16911-21 |year= 1992 |pmid= 1512232 |doi= }}
*{{cite journal | author=Haltiwanger RS, Blomberg MA, Hart GW |title=Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase. |journal=J. Biol. Chem. |volume=267 |issue= 13 |pages= 9005-13 |year= 1992 |pmid= 1533623 |doi= }}
*{{cite journal | author=Roquemore EP, Dell A, Morris HR, ''et al.'' |title=Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine. |journal=J. Biol. Chem. |volume=267 |issue= 1 |pages= 555-63 |year= 1992 |pmid= 1730617 |doi= }}
*{{cite journal | author=Chou TY, Hart GW, Dang CV |title=c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas. |journal=J. Biol. Chem. |volume=270 |issue= 32 |pages= 18961-5 |year= 1995 |pmid= 7642555 |doi= }}
*{{cite journal | author=Murphy JE, Hanover JA, Froehlich M, ''et al.'' |title=Clathrin assembly protein AP-3 is phosphorylated and glycosylated on the 50-kDa structural domain. |journal=J. Biol. Chem. |volume=269 |issue= 33 |pages= 21346-52 |year= 1994 |pmid= 8063760 |doi= }}
*{{cite journal | author=Matoba R, Okubo K, Hori N, ''et al.'' |title=The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression. |journal=Gene |volume=146 |issue= 2 |pages= 199-207 |year= 1994 |pmid= 8076819 |doi= }}
*{{cite journal | author=Dong DL, Xu ZS, Chevrier MR, ''et al.'' |title=Glycosylation of mammalian neurofilaments. Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. |journal=J. Biol. Chem. |volume=268 |issue= 22 |pages= 16679-87 |year= 1993 |pmid= 8344946 |doi= }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal | author=Roquemore EP, Chevrier MR, Cotter RJ, Hart GW |title=Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin. |journal=Biochemistry |volume=35 |issue= 11 |pages= 3578-86 |year= 1996 |pmid= 8639509 |doi= 10.1021/bi951918j }}
*{{cite journal | author=Dong DL, Xu ZS, Hart GW, Cleveland DW |title=Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H. |journal=J. Biol. Chem. |volume=271 |issue= 34 |pages= 20845-52 |year= 1996 |pmid= 8702840 |doi= }}
*{{cite journal | author=Arnold CS, Johnson GV, Cole RN, ''et al.'' |title=The microtubule-associated protein tau is extensively modified with O-linked N-acetylglucosamine. |journal=J. Biol. Chem. |volume=271 |issue= 46 |pages= 28741-4 |year= 1997 |pmid= 8910513 |doi= }}
*{{cite journal | author=Kreppel LK, Blomberg MA, Hart GW |title=Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats. |journal=J. Biol. Chem. |volume=272 |issue= 14 |pages= 9308-15 |year= 1997 |pmid= 9083067 |doi= }}
*{{cite journal | author=Lubas WA, Frank DW, Krause M, Hanover JA |title=O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats. |journal=J. Biol. Chem. |volume=272 |issue= 14 |pages= 9316-24 |year= 1997 |pmid= 9083068 |doi= }}
*{{cite journal | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi= }}
*{{cite journal | author=Roos MD, Su K, Baker JR, Kudlow JE |title=O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions. |journal=Mol. Cell. Biol. |volume=17 |issue= 11 |pages= 6472-80 |year= 1997 |pmid= 9343410 |doi= }}
*{{cite journal | author=Medina L, Grove K, Haltiwanger RS |title=SV40 large T antigen is modified with O-linked N-acetylglucosamine but not with other forms of glycosylation. |journal=Glycobiology |volume=8 |issue= 4 |pages= 383-91 |year= 1998 |pmid= 9499386 |doi= }}
*{{cite journal | author=Cole RN, Hart GW |title=Glycosylation sites flank phosphorylation sites on synapsin I: O-linked N-acetylglucosamine residues are localized within domains mediating synapsin I interactions. |journal=J. Neurochem. |volume=73 |issue= 1 |pages= 418-28 |year= 1999 |pmid= 10386995 |doi= }}
*{{cite journal | author=Akimoto Y, Kreppel LK, Hirano H, Hart GW |title=Localization of the O-linked N-acetylglucosamine transferase in rat pancreas. |journal=Diabetes |volume=48 |issue= 12 |pages= 2407-13 |year= 1999 |pmid= 10580430 |doi= }}
*{{cite journal | author=Lubas WA, Hanover JA |title=Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity. |journal=J. Biol. Chem. |volume=275 |issue= 15 |pages= 10983-8 |year= 2000 |pmid= 10753899 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PLA2G7... {November 18, 2007 10:47:56 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:48:22 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Phospholipase A2, group VII (platelet-activating factor acetylhydrolase, plasma)
| HGNCid = 9040
| Symbol = PLA2G7
| AltSymbols =; PAFAH; LDL-PLA2
| OMIM = 601690
| ECnumber =
| Homologene = 3725
| MGIid = 1351327
| GeneAtlas_image1 = PBB_GE_PLA2G7_206214_at_tn.png
| Function = {{GNF_GO|id=GO:0003847 |text = 1-alkyl-2-acetylglycerophosphocholine esterase activity}} {{GNF_GO|id=GO:0005543 |text = phospholipid binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0008247 |text = 2-acetyl-1-alkylglycerophosphocholine esterase complex}}
| Process = {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0016042 |text = lipid catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7941
| Hs_Ensembl = ENSG00000146070
| Hs_RefseqProtein = NP_005075
| Hs_RefseqmRNA = NM_005084
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 46779897
| Hs_GenLoc_end = 46811389
| Hs_Uniprot = Q13093
| Mm_EntrezGene = 27226
| Mm_Ensembl = ENSMUSG00000023913
| Mm_RefseqmRNA = XM_001003905
| Mm_RefseqProtein = XP_001003905
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 43031500
| Mm_GenLoc_end = 43075242
| Mm_Uniprot = Q3U1V7
}}
}}
'''Phospholipase A2, group VII (platelet-activating factor acetylhydrolase, plasma)''', also known as '''PLA2G7''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PLA2G7 phospholipase A2, group VII (platelet-activating factor acetylhydrolase, plasma)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7941| 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 PLA2G7 gene encodes platelet-activating factor (PAF) acetylhydrolase (EC 3.1.1.47), a secreted enzyme that catalyzes the degradation of PAF to inactive products by hydrolysis of the acetyl group at the sn-2 position, producing the biologically inactive products LYSO-PAF and acetate.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: PLA2G7 phospholipase A2, group VII (platelet-activating factor acetylhydrolase, plasma)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7941| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schröder HC, Perovic S, Kavsan V, ''et al.'' |title=Mechanisms of prionSc- and HIV-1 gp120 induced neuronal cell death. |journal=Neurotoxicology |volume=19 |issue= 4-5 |pages= 683-8 |year= 1998 |pmid= 9745929 |doi= }}
*{{cite journal | author=Feng Y, Walsh CA |title=Protein-protein interactions, cytoskeletal regulation and neuronal migration. |journal=Nat. Rev. Neurosci. |volume=2 |issue= 6 |pages= 408-16 |year= 2001 |pmid= 11389474 |doi= 10.1038/35077559 }}
*{{cite journal | author=Tjoelker LW, Eberhardt C, Unger J, ''et al.'' |title=Plasma platelet-activating factor acetylhydrolase is a secreted phospholipase A2 with a catalytic triad. |journal=J. Biol. Chem. |volume=270 |issue= 43 |pages= 25481-7 |year= 1995 |pmid= 7592717 |doi= }}
*{{cite journal | author=Tjoelker LW, Wilder C, Eberhardt C, ''et al.'' |title=Anti-inflammatory properties of a platelet-activating factor acetylhydrolase. |journal=Nature |volume=374 |issue= 6522 |pages= 549-53 |year= 1995 |pmid= 7700381 |doi= 10.1038/374549a0 }}
*{{cite journal | author=Tew DG, Southan C, Rice SQ, ''et al.'' |title=Purification, properties, sequencing, and cloning of a lipoprotein-associated, serine-dependent phospholipase involved in the oxidative modification of low-density lipoproteins. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=16 |issue= 4 |pages= 591-9 |year= 1996 |pmid= 8624782 |doi= }}
*{{cite journal | author=Stafforini DM, Satoh K, Atkinson DL, ''et al.'' |title=Platelet-activating factor acetylhydrolase deficiency. A missense mutation near the active site of an anti-inflammatory phospholipase. |journal=J. Clin. Invest. |volume=97 |issue= 12 |pages= 2784-91 |year= 1996 |pmid= 8675689 |doi= }}
*{{cite journal | author=Yamada Y, Yokota M |title=Loss of activity of plasma platelet-activating factor acetylhydrolase due to a novel Gln281-->Arg mutation. |journal=Biochem. Biophys. Res. Commun. |volume=236 |issue= 3 |pages= 772-5 |year= 1997 |pmid= 9245731 |doi= 10.1006/bbrc.1997.7047 }}
*{{cite journal | author=Mavoungou E, Georges-Courbot MC, Poaty-Mavoungou V, ''et al.'' |title=HIV and SIV envelope glycoproteins induce phospholipase A2 activation in human and macaque lymphocytes. |journal=J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. |volume=16 |issue= 1 |pages= 1-9 |year= 1997 |pmid= 9377118 |doi= }}
*{{cite journal | author=Sapir T, Elbaum M, Reiner O |title=Reduction of microtubule catastrophe events by LIS1, platelet-activating factor acetylhydrolase subunit. |journal=EMBO J. |volume=16 |issue= 23 |pages= 6977-84 |year= 1998 |pmid= 9384577 |doi= 10.1093/emboj/16.23.6977 }}
*{{cite journal | author=Hiramoto M, Yoshida H, Imaizumi T, ''et al.'' |title=A mutation in plasma platelet-activating factor acetylhydrolase (Val279-->Phe) is a genetic risk factor for stroke. |journal=Stroke |volume=28 |issue= 12 |pages= 2417-20 |year= 1998 |pmid= 9412624 |doi= }}
*{{cite journal | author=Yamada Y, Ichihara S, Fujimura T, Yokota M |title=Identification of the G994--> T missense in exon 9 of the plasma platelet-activating factor acetylhydrolase gene as an independent risk factor for coronary artery disease in Japanese men. |journal=Metab. Clin. Exp. |volume=47 |issue= 2 |pages= 177-81 |year= 1998 |pmid= 9472966 |doi= }}
*{{cite journal | author=Yoshida H, Imaizumi T, Fujimoto K, ''et al.'' |title=A mutation in plasma platelet-activating factor acetylhydrolase (Val279Phe) is a genetic risk factor for cerebral hemorrhage but not for hypertension. |journal=Thromb. Haemost. |volume=80 |issue= 3 |pages= 372-5 |year= 1998 |pmid= 9759612 |doi= }}
*{{cite journal | author=Lecointe N, Meerabux J, Ebihara M, ''et al.'' |title=Molecular analysis of an unstable genomic region at chromosome band 11q23 reveals a disruption of the gene encoding the alpha2 subunit of platelet-activating factor acetylhydrolase (Pafah1a2) in human lymphoma. |journal=Oncogene |volume=18 |issue= 18 |pages= 2852-9 |year= 1999 |pmid= 10362256 |doi= 10.1038/sj.onc.1202645 }}
*{{cite journal | author=Kruse S, Mao XQ, Heinzmann A, ''et al.'' |title=The Ile198Thr and Ala379Val variants of plasmatic PAF-acetylhydrolase impair catalytical activities and are associated with atopy and asthma. |journal=Am. J. Hum. Genet. |volume=66 |issue= 5 |pages= 1522-30 |year= 2000 |pmid= 10733466 |doi= }}
*{{cite journal | author=Howard KM, Olson MS |title=The expression and localization of plasma platelet-activating factor acetylhydrolase in endotoxemic rats. |journal=J. Biol. Chem. |volume=275 |issue= 26 |pages= 19891-6 |year= 2000 |pmid= 10748027 |doi= 10.1074/jbc.M001462200 }}
*{{cite journal | author=Min JH, Wilder C, Aoki J, ''et al.'' |title=Platelet-activating factor acetylhydrolases: broad substrate specificity and lipoprotein binding does not modulate the catalytic properties of the plasma enzyme. |journal=Biochemistry |volume=40 |issue= 15 |pages= 4539-49 |year= 2001 |pmid= 11294621 |doi= }}
*{{cite journal | author=Quarck R, De Geest B, Stengel D, ''et al.'' |title=Adenovirus-mediated gene transfer of human platelet-activating factor-acetylhydrolase prevents injury-induced neointima formation and reduces spontaneous atherosclerosis in apolipoprotein E-deficient mice. |journal=Circulation |volume=103 |issue= 20 |pages= 2495-500 |year= 2001 |pmid= 11369691 |doi= }}
*{{cite journal | author=Unno N, Nakamura T, Mitsuoka H, ''et al.'' |title=Association of a G994 -->T missense mutation in the plasma platelet-activating factor acetylhydrolase gene with risk of abdominal aortic aneurysm in Japanese. |journal=Ann. Surg. |volume=235 |issue= 2 |pages= 297-302 |year= 2002 |pmid= 11807372 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PSMF1... {November 18, 2007 10:50:44 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:51:25 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Proteasome (prosome, macropain) inhibitor subunit 1 (PI31)
| HGNCid = 9571
| Symbol = PSMF1
| AltSymbols =; PI31
| OMIM =
| ECnumber =
| Homologene = 38231
| MGIid = 1346072
| GeneAtlas_image1 = PBB_GE_PSMF1_201052_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PSMF1_201053_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008539 |text = proteasome inhibitor activity}}
| Component = {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005839 |text = proteasome core complex (sensu Eukaryota)}}
| Process = {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 9491
| Hs_Ensembl = ENSG00000125818
| Hs_RefseqProtein = NP_006805
| Hs_RefseqmRNA = NM_006814
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 1041939
| Hs_GenLoc_end = 1097022
| Hs_Uniprot = Q92530
| Mm_EntrezGene = 228769
| Mm_Ensembl = ENSMUSG00000032869
| Mm_RefseqmRNA = NM_144889
| Mm_RefseqProtein = NP_659138
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 151407256
| Mm_GenLoc_end = 151432734
| Mm_Uniprot = Q8BHL8
}}
}}
'''Proteasome (prosome, macropain) inhibitor subunit 1 (PI31)''', also known as '''PSMF1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMF1 proteasome (prosome, macropain) inhibitor subunit 1 (PI31)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9491| 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 a protein that inhibits the activation of the proteasome by the 11S and 19S regulators. Alternative transcript variants have been identified for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: PSMF1 proteasome (prosome, macropain) inhibitor subunit 1 (PI31)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9491| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tanahashi N, Kawahara H, Murakami Y, Tanaka K |title=The proteasome-dependent proteolytic system. |journal=Mol. Biol. Rep. |volume=26 |issue= 1-2 |pages= 3-9 |year= 1999 |pmid= 10363639 |doi= }}
*{{cite journal | author=Goff SP |title=Death by deamination: a novel host restriction system for HIV-1. |journal=Cell |volume=114 |issue= 3 |pages= 281-3 |year= 2003 |pmid= 12914693 |doi= }}
*{{cite journal | author=Minghetti L, Visentin S, Patrizio M, ''et al.'' |title=Multiple actions of the human immunodeficiency virus type-1 Tat protein on microglial cell functions. |journal=Neurochem. Res. |volume=29 |issue= 5 |pages= 965-78 |year= 2004 |pmid= 15139295 |doi= }}
*{{cite journal | author=Liou LY, Herrmann CH, Rice AP |title=HIV-1 infection and regulation of Tat function in macrophages. |journal=Int. J. Biochem. Cell Biol. |volume=36 |issue= 9 |pages= 1767-75 |year= 2005 |pmid= 15183343 |doi= 10.1016/j.biocel.2004.02.018 }}
*{{cite journal | author=Bannwarth S, Gatignol A |title=HIV-1 TAR RNA: the target of molecular interactions between the virus and its host. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 61-71 |year= 2005 |pmid= 15638724 |doi= }}
*{{cite journal | author=Gibellini D, Vitone F, Schiavone P, Re MC |title=HIV-1 tat protein and cell proliferation and survival: a brief review. |journal=New Microbiol. |volume=28 |issue= 2 |pages= 95-109 |year= 2005 |pmid= 16035254 |doi= }}
*{{cite journal | author=Hetzer C, Dormeyer W, Schnölzer M, Ott M |title=Decoding Tat: the biology of HIV Tat posttranslational modifications. |journal=Microbes Infect. |volume=7 |issue= 13 |pages= 1364-9 |year= 2006 |pmid= 16046164 |doi= 10.1016/j.micinf.2005.06.003 }}
*{{cite journal | author=Peruzzi F |title=The multiple functions of HIV-1 Tat: proliferation versus apoptosis. |journal=Front. Biosci. |volume=11 |issue= |pages= 708-17 |year= 2006 |pmid= 16146763 |doi= }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{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=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |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=McCutchen-Maloney SL, Matsuda K, Shimbara N, ''et al.'' |title=cDNA cloning, expression, and functional characterization of PI31, a proline-rich inhibitor of the proteasome. |journal=J. Biol. Chem. |volume=275 |issue= 24 |pages= 18557-65 |year= 2000 |pmid= 10764772 |doi= 10.1074/jbc.M001697200 }}
*{{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=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
*{{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=Zaiss DM, Standera S, Kloetzel PM, Sijts AJ |title=PI31 is a modulator of proteasome formation and antigen processing. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 22 |pages= 14344-9 |year= 2002 |pmid= 12374861 |doi= 10.1073/pnas.212257299 }}
*{{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= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TAF9... {November 18, 2007 10:44:53 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:45:55 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_TAF9_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1rkb.
| PDB = {{PDB2|1rkb}}
| Name = TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa
| HGNCid = 11542
| Symbol = TAF9
| AltSymbols =; AD-004; AK6; CGI-137; CINAP; CIP; MGC1603; MGC3647; MGC5067; MGC:1603; MGC:3647; MGC:5067; TAF2G; TAFII31; TAFII32; TAFIID32
| OMIM = 600822
| ECnumber =
| Homologene = 39986
| MGIid = 1888697
| GeneAtlas_image1 = PBB_GE_TAF9_203893_at_tn.png
| GeneAtlas_image2 = PBB_GE_TAF9_202168_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0004017 |text = adenylate kinase activity}} {{GNF_GO|id=GO:0004765 |text = shikimate kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008022 |text = protein C-terminus binding}} {{GNF_GO|id=GO:0016251 |text = general RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0019201 |text = nucleotide kinase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005669 |text = transcription factor TFIID complex}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006352 |text = transcription initiation}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0008652 |text = amino acid biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6880
| Hs_Ensembl = ENSG00000085231
| Hs_RefseqProtein = NP_001015891
| Hs_RefseqmRNA = NM_001015891
| Hs_GenLoc_db =
| Hs_GenLoc_chr = c5_H2
| Hs_GenLoc_start = 69107684
| Hs_GenLoc_end = 69125972
| Hs_Uniprot = Q9Y3D8
| Mm_EntrezGene = 108143
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_001015889
| Mm_RefseqProtein = NP_001015889
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa''', also known as '''TAF9''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TAF9 TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6880| 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 = Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein that coordinates these activities is transcription factor IID (TFIID), which binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes one of the smaller subunits of TFIID that binds to the basal transcription factor GTF2B as well as to several transcriptional activators such as p53 and VP16. A similar but distinct gene (TAF9L) has been found on the X chromosome and a pseudogene has been identified on chromosome 19. Alternative splicing results in multiple transcript variants encoding different isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: TAF9 TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6880| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Klemm RD, Goodrich JA, Zhou S, Tjian R |title=Molecular cloning and expression of the 32-kDa subunit of human TFIID reveals interactions with VP16 and TFIIB that mediate transcriptional activation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 13 |pages= 5788-92 |year= 1995 |pmid= 7597030 |doi= }}
*{{cite journal | author=Hisatake K, Ohta T, Takada R, ''et al.'' |title=Evolutionary conservation of human TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and with general transcription factors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 18 |pages= 8195-9 |year= 1995 |pmid= 7667268 |doi= }}
*{{cite journal | author=Lu H, Levine AJ |title=Human TAFII31 protein is a transcriptional coactivator of the p53 protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 11 |pages= 5154-8 |year= 1995 |pmid= 7761466 |doi= }}
*{{cite journal | author=Thut CJ, Chen JL, Klemm R, Tjian R |title=p53 transcriptional activation mediated by coactivators TAFII40 and TAFII60. |journal=Science |volume=267 |issue= 5194 |pages= 100-4 |year= 1995 |pmid= 7809597 |doi= }}
*{{cite journal | author=Zhou Q, Sharp PA |title=Novel mechanism and factor for regulation by HIV-1 Tat. |journal=EMBO J. |volume=14 |issue= 2 |pages= 321-8 |year= 1995 |pmid= 7835343 |doi= }}
*{{cite journal | author=Parada CA, Yoon JB, Roeder RG |title=A novel LBP-1-mediated restriction of HIV-1 transcription at the level of elongation in vitro. |journal=J. Biol. Chem. |volume=270 |issue= 5 |pages= 2274-83 |year= 1995 |pmid= 7836461 |doi= }}
*{{cite journal | author=Ou SH, Garcia-Martínez LF, Paulssen EJ, Gaynor RB |title=Role of flanking E box motifs in human immunodeficiency virus type 1 TATA element function. |journal=J. Virol. |volume=68 |issue= 11 |pages= 7188-99 |year= 1994 |pmid= 7933101 |doi= }}
*{{cite journal | author=Kashanchi F, Piras G, Radonovich MF, ''et al.'' |title=Direct interaction of human TFIID with the HIV-1 transactivator tat. |journal=Nature |volume=367 |issue= 6460 |pages= 295-9 |year= 1994 |pmid= 8121496 |doi= 10.1038/367295a0 }}
*{{cite journal | author=Adams MD, Soares MB, Kerlavage AR, ''et al.'' |title=Rapid cDNA sequencing (expressed sequence tags) from a directionally cloned human infant brain cDNA library. |journal=Nat. Genet. |volume=4 |issue= 4 |pages= 373-80 |year= 1993 |pmid= 8401585 |doi= 10.1038/ng0893-373 }}
*{{cite journal | author=Wang Z, Morris GF, Rice AP, ''et al.'' |title=Wild-type and transactivation-defective mutants of human immunodeficiency virus type 1 Tat protein bind human TATA-binding protein in vitro. |journal=J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. |volume=12 |issue= 2 |pages= 128-38 |year= 1996 |pmid= 8680883 |doi= }}
*{{cite journal | author=Pendergrast PS, Morrison D, Tansey WP, Hernandez N |title=Mutations in the carboxy-terminal domain of TBP affect the synthesis of human immunodeficiency virus type 1 full-length and short transcripts similarly. |journal=J. Virol. |volume=70 |issue= 8 |pages= 5025-34 |year= 1996 |pmid= 8764009 |doi= }}
*{{cite journal | author=Kashanchi F, Khleif SN, Duvall JF, ''et al.'' |title=Interaction of human immunodeficiency virus type 1 Tat with a unique site of TFIID inhibits negative cofactor Dr1 and stabilizes the TFIID-TFIIA complex. |journal=J. Virol. |volume=70 |issue= 8 |pages= 5503-10 |year= 1996 |pmid= 8764062 |doi= }}
*{{cite journal | author=Zhou Q, Sharp PA |title=Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. |journal=Science |volume=274 |issue= 5287 |pages= 605-10 |year= 1996 |pmid= 8849451 |doi= }}
*{{cite journal | author=Tao Y, Guermah M, Martinez E, ''et al.'' |title=Specific interactions and potential functions of human TAFII100. |journal=J. Biol. Chem. |volume=272 |issue= 10 |pages= 6714-21 |year= 1997 |pmid= 9045704 |doi= }}
*{{cite journal | author=García-Martínez LF, Ivanov D, Gaynor RB |title=Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes. |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 6951-8 |year= 1997 |pmid= 9054383 |doi= }}
*{{cite journal | author=Ogryzko VV, Kotani T, Zhang X, ''et al.'' |title=Histone-like TAFs within the PCAF histone acetylase complex. |journal=Cell |volume=94 |issue= 1 |pages= 35-44 |year= 1998 |pmid= 9674425 |doi= }}
*{{cite journal | author=Vassilev A, Yamauchi J, Kotani T, ''et al.'' |title=The 400 kDa subunit of the PCAF histone acetylase complex belongs to the ATM superfamily. |journal=Mol. Cell |volume=2 |issue= 6 |pages= 869-75 |year= 1999 |pmid= 9885574 |doi= }}
*{{cite journal | author=Evans SC, Foster CJ, El-Naggar AK, Lozano G |title=Mapping and mutational analysis of the human TAF2G gene encoding a p53 cofactor. |journal=Genomics |volume=57 |issue= 1 |pages= 182-3 |year= 1999 |pmid= 10191103 |doi= 10.1006/geno.1999.5745 }}
*{{cite journal | author=Lai CH, Chou CY, Ch'ang LY, ''et al.'' |title=Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. |journal=Genome Res. |volume=10 |issue= 5 |pages= 703-13 |year= 2000 |pmid= 10810093 |doi= }}
*{{cite journal | author=Choi Y, Asada S, Uesugi M |title=Divergent hTAFII31-binding motifs hidden in activation domains. |journal=J. Biol. Chem. |volume=275 |issue= 21 |pages= 15912-6 |year= 2000 |pmid= 10821850 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TLN1... {November 18, 2007 10:45:55 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:46:30 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_TLN1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1mix.
| PDB = {{PDB2|1mix}}, {{PDB2|1miz}}, {{PDB2|1mk7}}, {{PDB2|1mk9}}, {{PDB2|1sj7}}, {{PDB2|1sj8}}, {{PDB2|1u89}}, {{PDB2|1y19}}, {{PDB2|2b0h}}, {{PDB2|2g35}}, {{PDB2|2h7d}}, {{PDB2|2h7e}}
| Name = Talin 1
| HGNCid = 11845
| Symbol = TLN1
| AltSymbols =; ILWEQ; TLN; KIAA1027
| OMIM = 186745
| ECnumber =
| Homologene = 21267
| MGIid = 1099832
| GeneAtlas_image1 = PBB_GE_TLN1_203254_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005488 |text = binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0017166 |text = vinculin binding}} {{GNF_GO|id=GO:0030274 |text = LIM domain binding}}
| Component = {{GNF_GO|id=GO:0001726 |text = ruffle}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005911 |text = intercellular junction}} {{GNF_GO|id=GO:0005925 |text = focal adhesion}}
| Process = {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0007016 |text = cytoskeletal anchoring}} {{GNF_GO|id=GO:0007043 |text = intercellular junction assembly}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7094
| Hs_Ensembl = ENSG00000137076
| Hs_RefseqProtein = NP_006280
| Hs_RefseqmRNA = NM_006289
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 35687336
| Hs_GenLoc_end = 35722369
| Hs_Uniprot = Q9Y490
| Mm_EntrezGene = 21894
| Mm_Ensembl = ENSMUSG00000028465
| Mm_RefseqmRNA = NM_011602
| Mm_RefseqProtein = NP_035732
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 43552618
| Mm_GenLoc_end = 43583522
| Mm_Uniprot = Q0V930
}}
}}
'''Talin 1''', also known as '''TLN1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TLN1 talin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7094| 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 cytoskeletal protein which is concentrated in areas of cell-substratum and cell-cell contacts. This protein plays a significant role in the assembly of actin filaments and in spreading and migration of various cell types, including fibroblasts and osteoclasts. It codistributes with integrins in the cell surface membrane in order to assist in the attachment of adherent cells to extracellular matrices and of lymphocytes to other cells. The N-terminus of this protein contains elements for localization to cell-extracellular matrix junctions. The C-terminus contains binding sites for proteins such as beta-1-integrin, actin, and vinculin.<ref name="entrez">{{cite web | title = Entrez Gene: TLN1 talin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7094| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Luna EJ, Hitt AL |title=Cytoskeleton--plasma membrane interactions. |journal=Science |volume=258 |issue= 5084 |pages= 955-64 |year= 1992 |pmid= 1439807 |doi= }}
*{{cite journal | author=Nakajima D, Okazaki N, Yamakawa H, ''et al.'' |title=Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. |journal=DNA Res. |volume=9 |issue= 3 |pages= 99-106 |year= 2003 |pmid= 12168954 |doi= }}
*{{cite journal | author=Critchley DR |title=Cytoskeletal proteins talin and vinculin in integrin-mediated adhesion. |journal=Biochem. Soc. Trans. |volume=32 |issue= Pt 5 |pages= 831-6 |year= 2005 |pmid= 15494027 |doi= 10.1042/BST0320831 }}
*{{cite journal | author=Kupfer A, Burn P, Singer SJ |title=The PMA-induced specific association of LFA-1 and talin in intact cloned T helper cells. |journal=J. Mol. Cell. Immunol. |volume=4 |issue= 6 |pages= 317-25 |year= 1991 |pmid= 2150484 |doi= }}
*{{cite journal | author=Salgia R, Li JL, Lo SH, ''et al.'' |title=Molecular cloning of human paxillin, a focal adhesion protein phosphorylated by P210BCR/ABL. |journal=J. Biol. Chem. |volume=270 |issue= 10 |pages= 5039-47 |year= 1995 |pmid= 7534286 |doi= }}
*{{cite journal | author=Chen HC, Appeddu PA, Parsons JT, ''et al.'' |title=Interaction of focal adhesion kinase with cytoskeletal protein talin. |journal=J. Biol. Chem. |volume=270 |issue= 28 |pages= 16995-9 |year= 1995 |pmid= 7622520 |doi= }}
*{{cite journal | author=Gilmore AP, Ohanian V, Spurr NK, Critchley DR |title=Localisation of the human gene encoding the cytoskeletal protein talin to chromosome 9p. |journal=Hum. Genet. |volume=96 |issue= 2 |pages= 221-4 |year= 1995 |pmid= 7635475 |doi= }}
*{{cite journal | author=Genini M, Schwalbe P, Scholl FA, Schäfer BW |title=Isolation of genes differentially expressed in human primary myoblasts and embryonal rhabdomyosarcoma. |journal=Int. J. Cancer |volume=66 |issue= 4 |pages= 571-7 |year= 1996 |pmid= 8635876 |doi= 10.1002/(SICI)1097-0215(19960516)66:4<571::AID-IJC24>3.0.CO;2-9 }}
*{{cite journal | author=Salgia R, Sattler M, Pisick E, ''et al.'' |title=p210BCR/ABL induces formation of complexes containing focal adhesion proteins and the protooncogene product p120c-Cbl. |journal=Exp. Hematol. |volume=24 |issue= 2 |pages= 310-3 |year= 1996 |pmid= 8641358 |doi= }}
*{{cite journal | author=Knezevic I, Leisner TM, Lam SC |title=Direct binding of the platelet integrin alphaIIbbeta3 (GPIIb-IIIa) to talin. Evidence that interaction is mediated through the cytoplasmic domains of both alphaIIb and beta3. |journal=J. Biol. Chem. |volume=271 |issue= 27 |pages= 16416-21 |year= 1996 |pmid= 8663236 |doi= }}
*{{cite journal | author=Zheng C, Xing Z, Bian ZC, ''et al.'' |title=Differential regulation of Pyk2 and focal adhesion kinase (FAK). The C-terminal domain of FAK confers response to cell adhesion. |journal=J. Biol. Chem. |volume=273 |issue= 4 |pages= 2384-9 |year= 1998 |pmid= 9442086 |doi= }}
*{{cite journal | author=Luo G, Herrera AH, Horowits R |title=Molecular interactions of N-RAP, a nebulin-related protein of striated muscle myotendon junctions and intercalated disks. |journal=Biochemistry |volume=38 |issue= 19 |pages= 6135-43 |year= 1999 |pmid= 10320340 |doi= 10.1021/bi982395t }}
*{{cite journal | author=Bass MD, Smith BJ, Prigent SA, Critchley DR |title=Talin contains three similar vinculin-binding sites predicted to form an amphipathic helix. |journal=Biochem. J. |volume=341 ( Pt 2) |issue= |pages= 257-63 |year= 1999 |pmid= 10393080 |doi= }}
*{{cite journal | author=Kikuno R, Nagase T, Ishikawa K, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=6 |issue= 3 |pages= 197-205 |year= 1999 |pmid= 10470851 |doi= }}
*{{cite journal | author=Patil S, Jedsadayanmata A, Wencel-Drake JD, ''et al.'' |title=Identification of a talin-binding site in the integrin beta(3) subunit distinct from the NPLY regulatory motif of post-ligand binding functions. The talin n-terminal head domain interacts with the membrane-proximal region of the beta(3) cytoplasmic tail. |journal=J. Biol. Chem. |volume=274 |issue= 40 |pages= 28575-83 |year= 1999 |pmid= 10497223 |doi= }}
*{{cite journal | author=McCann RO, Craig SW |title=Functional genomic analysis reveals the utility of the I/LWEQ module as a predictor of protein:actin interaction. |journal=Biochem. Biophys. Res. Commun. |volume=266 |issue= 1 |pages= 135-40 |year= 2000 |pmid= 10581178 |doi= 10.1006/bbrc.1999.1776 }}
*{{cite journal | author=Ben-Yosef T, Francomano CA |title=Characterization of the human talin (TLN) gene: genomic structure, chromosomal localization, and expression pattern. |journal=Genomics |volume=62 |issue= 2 |pages= 316-9 |year= 2000 |pmid= 10610730 |doi= 10.1006/geno.1999.6019 }}
*{{cite journal | author=Martel V, Vignoud L, Dupé S, ''et al.'' |title=Talin controls the exit of the integrin alpha 5 beta 1 from an early compartment of the secretory pathway. |journal=J. Cell. Sci. |volume=113 ( Pt 11) |issue= |pages= 1951-61 |year= 2000 |pmid= 10806106 |doi= }}
*{{cite journal | author=Gotthardt M, Trommsdorff M, Nevitt MF, ''et al.'' |title=Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction. |journal=J. Biol. Chem. |volume=275 |issue= 33 |pages= 25616-24 |year= 2000 |pmid= 10827173 |doi= 10.1074/jbc.M000955200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TPSAB1... {November 18, 2007 10:46:30 AM PST}
- SEARCH REDIRECT: Control Box Found: TPSAB1 {November 18, 2007 10:47:16 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:47:17 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:47:17 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:47:17 AM PST}
- UPDATED: Updated protein page: TPSAB1 {November 18, 2007 10:47:24 AM PST}
- INFO: Beginning work on TXNRD1... {November 18, 2007 10:47:24 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:47:56 AM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_TXNRD1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1h6v.
| PDB = {{PDB2|1h6v}}, {{PDB2|2cfy}}
| Name = Thioredoxin reductase 1
| HGNCid = 12437
| Symbol = TXNRD1
| AltSymbols =; TR; TR1; GRIM-12; MGC9145; TRXR1; TXNR
| OMIM = 601112
| ECnumber =
| Homologene = 55733
| MGIid = 1354175
| Function = {{GNF_GO|id=GO:0004791 |text = thioredoxin-disulfide reductase activity}} {{GNF_GO|id=GO:0008430 |text = selenium binding}} {{GNF_GO|id=GO:0015036 |text = disulfide oxidoreductase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0016654 |text = oxidoreductase activity, acting on NADH or NADPH, disulfide as acceptor}} {{GNF_GO|id=GO:0050660 |text = FAD binding}} {{GNF_GO|id=GO:0050661 |text = NADP binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0045454 |text = cell redox homeostasis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7296
| Hs_Ensembl =
| Hs_RefseqProtein = NP_003321
| Hs_RefseqmRNA = NM_003330
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 50493
| Mm_Ensembl = ENSMUSG00000020250
| Mm_RefseqmRNA = NM_001042513
| Mm_RefseqProtein = NP_001035978
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 82304448
| Mm_GenLoc_end = 82325844
| Mm_Uniprot = Q3UEB7
}}
}}
'''Thioredoxin reductase 1''', also known as '''TXNRD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TXNRD1 thioredoxin reductase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7296| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the family of pyridine nucleotide oxidoreductases. This protein reduces thioredoxins as well as other substrates, and plays a role in selenium metabolism and protection against oxidative stress. The functional enzyme is thought to be a homodimer which uses FAD as a cofactor. Each subunit contains a selenocysteine (Sec) residue which is required for catalytic activity. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenocysteine-containing genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Alternative splicing results in several transcript variants encoding the same or different isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: TXNRD1 thioredoxin reductase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7296| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schallreuter KU, Grebe T, Pittelkow MR, Wood JM |title=[3H]-13-cis-retinoic acid covalently binds to thioredoxin reductase in human keratinocytes. |journal=Skin Pharmacol. |volume=4 |issue= 1 |pages= 14-20 |year= 1991 |pmid= 2064786 |doi= }}
*{{cite journal | author=Gasdaska PY, Gasdaska JR, Cochran S, Powis G |title=Cloning and sequencing of a human thioredoxin reductase. |journal=FEBS Lett. |volume=373 |issue= 1 |pages= 5-9 |year= 1995 |pmid= 7589432 |doi= }}
*{{cite journal | author=Cha MK, Kim IH |title=Thioredoxin-linked peroxidase from human red blood cell: evidence for the existence of thioredoxin and thioredoxin reductase in human red blood cell. |journal=Biochem. Biophys. Res. Commun. |volume=217 |issue= 3 |pages= 900-7 |year= 1996 |pmid= 8554614 |doi= 10.1006/bbrc.1995.2856 }}
*{{cite journal | author=Tamura T, Stadtman TC |title=A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 3 |pages= 1006-11 |year= 1996 |pmid= 8577704 |doi= }}
*{{cite journal | author=Gladyshev VN, Jeang KT, Stadtman TC |title=Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 12 |pages= 6146-51 |year= 1996 |pmid= 8650234 |doi= }}
*{{cite journal | author=Gasdaska JR, Gasdaska PY, Gallegos A, Powis G |title=Human thioredoxin reductase gene localization to chromosomal position 12q23-q24.1 and mRNA distribution in human tissue. |journal=Genomics |volume=37 |issue= 2 |pages= 257-9 |year= 1997 |pmid= 8921404 |doi= 10.1006/geno.1996.0554 }}
*{{cite journal | author=Koishi R, Kawashima I, Yoshimura C, ''et al.'' |title=Cloning and characterization of a novel oxidoreductase KDRF from a human bone marrow-derived stromal cell line KM-102. |journal=J. Biol. Chem. |volume=272 |issue= 4 |pages= 2570-7 |year= 1997 |pmid= 8999974 |doi= }}
*{{cite journal | author=Liu SY, Stadtman TC |title=Heparin-binding properties of selenium-containing thioredoxin reductase from HeLa cells and human lung adenocarcinoma cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 12 |pages= 6138-41 |year= 1997 |pmid= 9177183 |doi= }}
*{{cite journal | author=Bennett RA, Wilson DM, Wong D, Demple B |title=Interaction of human apurinic endonuclease and DNA polymerase beta in the base excision repair pathway. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 14 |pages= 7166-9 |year= 1997 |pmid= 9207062 |doi= }}
*{{cite journal | author=Gorlatov SN, Stadtman TC |title=Human thioredoxin reductase from HeLa cells: selective alkylation of selenocysteine in the protein inhibits enzyme activity and reduction with NADPH influences affinity to heparin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 15 |pages= 8520-5 |year= 1998 |pmid= 9671710 |doi= }}
*{{cite journal | author=Hofmann ER, Boyanapalli M, Lindner DJ, ''et al.'' |title=Thioredoxin reductase mediates cell death effects of the combination of beta interferon and retinoic acid. |journal=Mol. Cell. Biol. |volume=18 |issue= 11 |pages= 6493-504 |year= 1998 |pmid= 9774665 |doi= }}
*{{cite journal | author=Anema SM, Walker SW, Howie AF, ''et al.'' |title=Thioredoxin reductase is the major selenoprotein expressed in human umbilical-vein endothelial cells and is regulated by protein kinase C. |journal=Biochem. J. |volume=342 ( Pt 1) |issue= |pages= 111-7 |year= 1999 |pmid= 10432307 |doi= }}
*{{cite journal | author=Söderberg A, Sahaf B, Rosén A |title=Thioredoxin reductase, a redox-active selenoprotein, is secreted by normal and neoplastic cells: presence in human plasma. |journal=Cancer Res. |volume=60 |issue= 8 |pages= 2281-9 |year= 2000 |pmid= 10786696 |doi= }}
*{{cite journal | author=Rundlöf AK, Carlsten M, Arnér ES |title=The core promoter of human thioredoxin reductase 1: cloning, transcriptional activity, and Oct-1, Sp1, and Sp3 binding reveal a housekeeping-type promoter for the AU-rich element-regulated gene. |journal=J. Biol. Chem. |volume=276 |issue= 32 |pages= 30542-51 |year= 2001 |pmid= 11375392 |doi= 10.1074/jbc.M101452200 }}
*{{cite journal | author=Lewin MH, Hume R, Howie AF, ''et al.'' |title=Thioredoxin reductase and cytoplasmic glutathione peroxidase activity in human foetal and neonatal liver. |journal=Biochim. Biophys. Acta |volume=1526 |issue= 3 |pages= 237-41 |year= 2001 |pmid= 11410332 |doi= }}
*{{cite journal | author=Osborne SA, Tonissen KF |title=Genomic organisation and alternative splicing of mouse and human thioredoxin reductase 1 genes. |journal=BMC Genomics |volume=2 |issue= 1 |pages= 10 |year= 2003 |pmid= 11737861 |doi= }}
*{{cite journal | author=Gromer S, Gross JH |title=Methylseleninate is a substrate rather than an inhibitor of mammalian thioredoxin reductase. Implications for the antitumor effects of selenium. |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 9701-6 |year= 2002 |pmid= 11782468 |doi= 10.1074/jbc.M109234200 }}
*{{cite journal | author=Ma X, Hu J, Lindner DJ, Kalvakolanu DV |title=Mutational analysis of human thioredoxin reductase 1. Effects on p53-mediated gene expression and interferon and retinoic acid-induced cell death. |journal=J. Biol. Chem. |volume=277 |issue= 25 |pages= 22460-8 |year= 2002 |pmid= 11953436 |doi= 10.1074/jbc.M202286200 }}
*{{cite journal | author=Karimpour S, Lou J, Lin LL, ''et al.'' |title=Thioredoxin reductase regulates AP-1 activity as well as thioredoxin nuclear localization via active cysteines in response to ionizing radiation. |journal=Oncogene |volume=21 |issue= 41 |pages= 6317-27 |year= 2002 |pmid= 12214272 |doi= 10.1038/sj.onc.1205749 }}
*{{cite journal | author=Xia L, Nordman T, Olsson JM, ''et al.'' |title=The mammalian cytosolic selenoenzyme thioredoxin reductase reduces ubiquinone. A novel mechanism for defense against oxidative stress. |journal=J. Biol. Chem. |volume=278 |issue= 4 |pages= 2141-6 |year= 2003 |pmid= 12435734 |doi= 10.1074/jbc.M210456200 }}
}}
{{refend}}
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end log.
