Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 20:56, 18 November 2007 (UTC)[edit]
Conflict: Ambiguous Proteins (1)[edit]
Proteins without matches (14)[edit]
Proteins with a High Potential Match (5)[edit]
Redirected Proteins (5)[edit]
Manual Inspection (Page not found) (20)[edit]
Updated (5)[edit]
Protein Status Grid - Date: 20:56, 18 November 2007 (UTC)[edit]
Vebose Log - Date: 20:56, 18 November 2007 (UTC)[edit]
- INFO: Beginning work on AP2A1... {November 18, 2007 12:21:38 PM PST}
- SEARCH REDIRECT: Control Box Found: AP2A1 {November 18, 2007 12:22:31 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 12:22:33 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 12:22:33 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 12:22:33 PM PST}
- UPDATED: Updated protein page: AP2A1 {November 18, 2007 12:22:45 PM PST}
- INFO: Beginning work on CADM1... {November 18, 2007 12:45:34 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 12:46:50 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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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 = Cell adhesion molecule 1
| HGNCid = 5951
| Symbol = CADM1
| AltSymbols =; BL2; DKFZp686F1789; IGSF4; IGSF4A; MGC149785; MGC51880; NECL2; Necl-2; RA175; ST17; SYNCAM; TSLC1; sTSLC-1; synCAM1
| OMIM = 605686
| ECnumber =
| Homologene = 8641
| MGIid = 1889272
| GeneAtlas_image1 = PBB_GE_CADM1_209030_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CADM1_209032_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0008022 |text = protein C-terminus binding}} {{GNF_GO|id=GO:0030165 |text = PDZ domain binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005911 |text = intercellular junction}} {{GNF_GO|id=GO:0016323 |text = basolateral plasma membrane}}
| Process = {{GNF_GO|id=GO:0001913 |text = T cell mediated cytotoxicity}} {{GNF_GO|id=GO:0007156 |text = homophilic cell adhesion}} {{GNF_GO|id=GO:0007157 |text = heterophilic cell adhesion}} {{GNF_GO|id=GO:0008037 |text = cell recognition}} {{GNF_GO|id=GO:0016338 |text = calcium-independent cell-cell adhesion}} {{GNF_GO|id=GO:0042271 |text = susceptibility to natural killer cell mediated cytotoxicity}} {{GNF_GO|id=GO:0050715 |text = positive regulation of cytokine secretion}} {{GNF_GO|id=GO:0050798 |text = activated T cell proliferation}} {{GNF_GO|id=GO:0051606 |text = detection of stimulus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 23705
| Hs_Ensembl = ENSG00000182985
| Hs_RefseqProtein = NP_055148
| Hs_RefseqmRNA = NM_014333
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 114552404
| Hs_GenLoc_end = 114880322
| Hs_Uniprot =
| Mm_EntrezGene = 54725
| Mm_Ensembl = ENSMUSG00000032076
| Mm_RefseqmRNA = NM_001025600
| Mm_RefseqProtein = NP_001020771
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 47281368
| Mm_GenLoc_end = 47601384
| Mm_Uniprot =
}}
}}
'''Cell adhesion molecule 1''', also known as '''CADM1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CADM1 cell adhesion molecule 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23705| 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=Watabe K, Ito A, Koma YI, Kitamura Y |title=IGSF4: a new intercellular adhesion molecule that is called by three names, TSLC1, SgIGSF and SynCAM, by virtue of its diverse function. |journal=Histol. Histopathol. |volume=18 |issue= 4 |pages= 1321-9 |year= 2004 |pmid= 12973698 |doi= }}
*{{cite journal | author=Gomyo H, Arai Y, Tanigami A, ''et al.'' |title=A 2-Mb sequence-ready contig map and a novel immunoglobulin superfamily gene IGSF4 in the LOH region of chromosome 11q23.2. |journal=Genomics |volume=62 |issue= 2 |pages= 139-46 |year= 2000 |pmid= 10610705 |doi= 10.1006/geno.1999.6001 }}
*{{cite journal | author=Kuramochi M, Fukuhara H, Nobukuni T, ''et al.'' |title=TSLC1 is a tumor-suppressor gene in human non-small-cell lung cancer. |journal=Nat. Genet. |volume=27 |issue= 4 |pages= 427-30 |year= 2001 |pmid= 11279526 |doi= 10.1038/86934 }}
*{{cite journal | author=Masuda M, Yageta M, Fukuhara H, ''et al.'' |title=The tumor suppressor protein TSLC1 is involved in cell-cell adhesion. |journal=J. Biol. Chem. |volume=277 |issue= 34 |pages= 31014-9 |year= 2002 |pmid= 12050160 |doi= 10.1074/jbc.M203620200 }}
*{{cite journal | author=Fukuhara H, Kuramochi M, Fukami T, ''et al.'' |title=Promoter methylation of TSLC1 and tumor suppression by its gene product in human prostate cancer. |journal=Jpn. J. Cancer Res. |volume=93 |issue= 6 |pages= 605-9 |year= 2003 |pmid= 12079507 |doi= }}
*{{cite journal | author=Allinen M, Peri L, Kujala S, ''et al.'' |title=Analysis of 11q21-24 loss of heterozygosity candidate target genes in breast cancer: indications of TSLC1 promoter hypermethylation. |journal=Genes Chromosomes Cancer |volume=34 |issue= 4 |pages= 384-9 |year= 2002 |pmid= 12112527 |doi= 10.1002/gcc.10079 }}
*{{cite journal | author=Biederer T, Sara Y, Mozhayeva M, ''et al.'' |title=SynCAM, a synaptic adhesion molecule that drives synapse assembly. |journal=Science |volume=297 |issue= 5586 |pages= 1525-31 |year= 2002 |pmid= 12202822 |doi= 10.1126/science.1072356 }}
*{{cite journal | author=Yageta M, Kuramochi M, Masuda M, ''et al.'' |title=Direct association of TSLC1 and DAL-1, two distinct tumor suppressor proteins in lung cancer. |journal=Cancer Res. |volume=62 |issue= 18 |pages= 5129-33 |year= 2002 |pmid= 12234973 |doi= }}
*{{cite journal | author=Jansen M, Fukushima N, Rosty C, ''et al.'' |title=Aberrant methylation of the 5' CpG island of TSLC1 is common in pancreatic ductal adenocarcinoma and is first manifest in high-grade PanlNs. |journal=Cancer Biol. Ther. |volume=1 |issue= 3 |pages= 293-6 |year= 2003 |pmid= 12432281 |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=Honda T, Tamura G, Waki T, ''et al.'' |title=Hypermethylation of the TSLC1 gene promoter in primary gastric cancers and gastric cancer cell lines. |journal=Jpn. J. Cancer Res. |volume=93 |issue= 8 |pages= 857-60 |year= 2003 |pmid= 12716461 |doi= }}
*{{cite journal | author=Shingai T, Ikeda W, Kakunaga S, ''et al.'' |title=Implications of nectin-like molecule-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in cell-cell adhesion and transmembrane protein localization in epithelial cells. |journal=J. Biol. Chem. |volume=278 |issue= 37 |pages= 35421-7 |year= 2003 |pmid= 12826663 |doi= 10.1074/jbc.M305387200 }}
*{{cite journal | author=Ito A, Okada M, Uchino K, ''et al.'' |title=Expression of the TSLC1 adhesion molecule in pulmonary epithelium and its down-regulation in pulmonary adenocarcinoma other than bronchioloalveolar carcinoma. |journal=Lab. Invest. |volume=83 |issue= 8 |pages= 1175-83 |year= 2003 |pmid= 12920246 |doi= }}
*{{cite journal | author=Fukami T, Fukuhara H, Kuramochi M, ''et al.'' |title=Promoter methylation of the TSLC1 gene in advanced lung tumors and various cancer cell lines. |journal=Int. J. Cancer |volume=107 |issue= 1 |pages= 53-9 |year= 2003 |pmid= 12925956 |doi= 10.1002/ijc.11348 }}
*{{cite journal | author=Uchino K, Ito A, Wakayama T, ''et al.'' |title=Clinical implication and prognostic significance of the tumor suppressor TSLC1 gene detected in adenocarcinoma of the lung. |journal=Cancer |volume=98 |issue= 5 |pages= 1002-7 |year= 2003 |pmid= 12942568 |doi= 10.1002/cncr.11599 }}
*{{cite journal | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
*{{cite journal | author=Fukuhara H, Masuda M, Yageta M, ''et al.'' |title=Association of a lung tumor suppressor TSLC1 with MPP3, a human homologue of Drosophila tumor suppressor Dlg. |journal=Oncogene |volume=22 |issue= 40 |pages= 6160-5 |year= 2003 |pmid= 13679854 |doi= 10.1038/sj.onc.1206744 }}
*{{cite journal | author=Ito T, Shimada Y, Hashimoto Y, ''et al.'' |title=Involvement of TSLC1 in progression of esophageal squamous cell carcinoma. |journal=Cancer Res. |volume=63 |issue= 19 |pages= 6320-6 |year= 2003 |pmid= 14559819 |doi= }}
*{{cite journal | author=Mao X, Seidlitz E, Ghosh K, ''et al.'' |title=The cytoplasmic domain is critical to the tumor suppressor activity of TSLC1 in non-small cell lung cancer. |journal=Cancer Res. |volume=63 |issue= 22 |pages= 7979-85 |year= 2004 |pmid= 14633730 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CD1A... {November 18, 2007 12:25:19 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 12:26:07 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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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_CD1A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1onq.
| PDB = {{PDB2|1onq}}, {{PDB2|1xz0}}
| Name = CD1a molecule
| HGNCid = 1634
| Symbol = CD1A
| AltSymbols =; CD1; FCB6; HTA1; R4; T6
| OMIM = 188370
| ECnumber =
| Homologene = 74408
| MGIid =
| GeneAtlas_image1 = PBB_GE_CD1A_210325_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0042612 |text = MHC class I protein complex}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0019882 |text = antigen processing and presentation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 909
| Hs_Ensembl = ENSG00000158477
| Hs_RefseqProtein = NP_001754
| Hs_RefseqmRNA = NM_001763
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 156490551
| Hs_GenLoc_end = 156494683
| Hs_Uniprot = P06126
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''CD1a molecule''', also known as '''CD1A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CD1A CD1a molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=909| 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 CD1 family of transmembrane glycoproteins, which are structurally related to the major histocompatibility complex (MHC) proteins and form heterodimers with beta-2-microglobulin. The CD1 proteins mediate the presentation of primarily lipid and glycolipid antigens of self or microbial origin to T cells. The human genome contains five CD1 family genes organized in a cluster on chromosome 1. The CD1 family members are thought to differ in their cellular localization and specificity for particular lipid ligands. The protein encoded by this gene localizes to the plasma membrane and to recycling vesicles of the early endocytic system. Alternatively spliced transcript variants have been observed, but their biological validity has not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: CD1A CD1a molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=909| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Melián A, Beckman EM, Porcelli SA, Brenner MB |title=Antigen presentation by CD1 and MHC-encoded class I-like molecules. |journal=Curr. Opin. Immunol. |volume=8 |issue= 1 |pages= 82-8 |year= 1996 |pmid= 8729450 |doi= }}
*{{cite journal | author=Park SH, Bendelac A |title=CD1-restricted T-cell responses and microbial infection. |journal=Nature |volume=406 |issue= 6797 |pages= 788-92 |year= 2000 |pmid= 10963609 |doi= 10.1038/35021233 }}
*{{cite journal | author=Brigl M, Brenner MB |title=CD1: antigen presentation and T cell function. |journal=Annu. Rev. Immunol. |volume=22 |issue= |pages= 817-90 |year= 2004 |pmid= 15032598 |doi= 10.1146/annurev.immunol.22.012703.104608 }}
*{{cite journal | author=Coventry B, Heinzel S |title=CD1a in human cancers: a new role for an old molecule. |journal=Trends Immunol. |volume=25 |issue= 5 |pages= 242-8 |year= 2004 |pmid= 15099564 |doi= 10.1016/j.it.2004.03.002 }}
*{{cite journal | author=Moody DB, Zajonc DM, Wilson IA |title=Anatomy of CD1-lipid antigen complexes. |journal=Nat. Rev. Immunol. |volume=5 |issue= 5 |pages= 387-99 |year= 2005 |pmid= 15864273 |doi= 10.1038/nri1605 }}
*{{cite journal | author=Stove V, Verhasselt B |title=Modelling thymic HIV-1 Nef effects. |journal=Curr. HIV Res. |volume=4 |issue= 1 |pages= 57-64 |year= 2006 |pmid= 16454711 |doi= }}
*{{cite journal | author=Quaranta MG, Mattioli B, Giordani L, Viora M |title=The immunoregulatory effects of HIV-1 Nef on dendritic cells and the pathogenesis of AIDS. |journal=FASEB J. |volume=20 |issue= 13 |pages= 2198-208 |year= 2006 |pmid= 17077296 |doi= 10.1096/fj.06-6260rev }}
*{{cite journal | author=Oakey RJ, Watson ML, Seldin MF |title=Construction of a physical map on mouse and human chromosome 1: comparison of 13 Mb of mouse and 11 Mb of human DNA. |journal=Hum. Mol. Genet. |volume=1 |issue= 8 |pages= 613-20 |year= 1993 |pmid= 1301170 |doi= }}
*{{cite journal | author=Martin LH, Calabi F, Lefebvre FA, ''et al.'' |title=Structure and expression of the human thymocyte antigens CD1a, CD1b, and CD1c. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 24 |pages= 9189-93 |year= 1988 |pmid= 2447586 |doi= }}
*{{cite journal | author=Moseley WS, Watson ML, Kingsmore SF, Seldin MF |title=CD1 defines conserved linkage group border between human chromosomes 1 and mouse chromosomes 1 and 3. |journal=Immunogenetics |volume=30 |issue= 5 |pages= 378-82 |year= 1989 |pmid= 2478463 |doi= }}
*{{cite journal | author=Yu CY, Milstein C |title=A physical map linking the five CD1 human thymocyte differentiation antigen genes. |journal=EMBO J. |volume=8 |issue= 12 |pages= 3727-32 |year= 1990 |pmid= 2583117 |doi= }}
*{{cite journal | author=Aruffo A, Seed B |title=Expression of cDNA clones encoding the thymocyte antigens CD1a, b, c demonstrates a hierarchy of exclusion in fibroblasts. |journal=J. Immunol. |volume=143 |issue= 5 |pages= 1723-30 |year= 1989 |pmid= 2701945 |doi= }}
*{{cite journal | author=Longley J, Kraus J, Alonso M, Edelson R |title=Molecular cloning of CD1a (T6), a human epidermal dendritic cell marker related to class I MHC molecules. |journal=J. Invest. Dermatol. |volume=92 |issue= 4 |pages= 628-31 |year= 1989 |pmid= 2784820 |doi= }}
*{{cite journal | author=Albertson DG, Fishpool R, Sherrington P, ''et al.'' |title=Sensitive and high resolution in situ hybridization to human chromosomes using biotin labelled probes: assignment of the human thymocyte CD1 antigen genes to chromosome 1. |journal=EMBO J. |volume=7 |issue= 9 |pages= 2801-5 |year= 1988 |pmid= 3053166 |doi= }}
*{{cite journal | author=Calabi F, Milstein C |title=A novel family of human major histocompatibility complex-related genes not mapping to chromosome 6. |journal=Nature |volume=323 |issue= 6088 |pages= 540-3 |year= 1986 |pmid= 3093894 |doi= 10.1038/323540a0 }}
*{{cite journal | author=Martin LH, Calabi F, Milstein C |title=Isolation of CD1 genes: a family of major histocompatibility complex-related differentiation antigens. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 23 |pages= 9154-8 |year= 1987 |pmid= 3097645 |doi= }}
*{{cite journal | author=Woolfson A, Milstein C |title=Alternative splicing generates secretory isoforms of human CD1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 14 |pages= 6683-7 |year= 1994 |pmid= 7517559 |doi= }}
*{{cite journal | author=Han M, Hannick LI, DiBrino M, Robinson MA |title=Polymorphism of human CD1 genes. |journal=Tissue Antigens |volume=54 |issue= 2 |pages= 122-7 |year= 2000 |pmid= 10488738 |doi= }}
*{{cite journal | author=Sugita M, Grant EP, van Donselaar E, ''et al.'' |title=Separate pathways for antigen presentation by CD1 molecules. |journal=Immunity |volume=11 |issue= 6 |pages= 743-52 |year= 2000 |pmid= 10626896 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CD22... {November 18, 2007 12:26:57 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 12:28:36 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = CD22 molecule
| HGNCid = 1643
| Symbol = CD22
| AltSymbols =; MGC130020; SIGLEC-2; SIGLEC2
| OMIM = 107266
| ECnumber =
| Homologene = 31052
| MGIid = 88322
| GeneAtlas_image1 = PBB_GE_CD22_38521_at_tn.png
| GeneAtlas_image2 = PBB_GE_CD22_204581_at_tn.png
| GeneAtlas_image3 = PBB_GE_CD22_217422_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005529 |text = sugar binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0009897 |text = external side of plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0016337 |text = cell-cell adhesion}} {{GNF_GO|id=GO:0019735 |text = antimicrobial humoral response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 933
| Hs_Ensembl = ENSG00000012124
| Hs_RefseqProtein = NP_001762
| Hs_RefseqmRNA = NM_001771
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 40511944
| Hs_GenLoc_end = 40530098
| Hs_Uniprot = P20273
| Mm_EntrezGene = 12483
| Mm_Ensembl = ENSMUSG00000030577
| Mm_RefseqmRNA = NM_001043317
| Mm_RefseqProtein = NP_001036782
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 30574589
| Mm_GenLoc_end = 30589029
| Mm_Uniprot = Q3T9T5
}}
}}
'''CD22 molecule''', also known as '''CD22''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CD22 CD22 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=933| 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=Tedder TF, Tuscano J, Sato S, Kehrl JH |title=CD22, a B lymphocyte-specific adhesion molecule that regulates antigen receptor signaling. |journal=Annu. Rev. Immunol. |volume=15 |issue= |pages= 481-504 |year= 1997 |pmid= 9143697 |doi= 10.1146/annurev.immunol.15.1.481 }}
*{{cite journal | author=Blasioli J, Goodnow CC |title=Lyn/CD22/SHP-1 and their importance in autoimmunity. |journal=Curr. Dir. Autoimmun. |volume=5 |issue= |pages= 151-60 |year= 2002 |pmid= 11826756 |doi= }}
*{{cite journal | author=Torres RM, Law CL, Santos-Argumedo L, ''et al.'' |title=Identification and characterization of the murine homologue of CD22, a B lymphocyte-restricted adhesion molecule. |journal=J. Immunol. |volume=149 |issue= 8 |pages= 2641-9 |year= 1992 |pmid= 1401903 |doi= }}
*{{cite journal | author=Stamenkovic I, Seed B |title=The B-cell antigen CD22 mediates monocyte and erythrocyte adhesion. |journal=Nature |volume=345 |issue= 6270 |pages= 74-7 |year= 1990 |pmid= 1691828 |doi= 10.1038/345074a0 }}
*{{cite journal | author=Wilson GL, Fox CH, Fauci AS, Kehrl JH |title=cDNA cloning of the B cell membrane protein CD22: a mediator of B-B cell interactions. |journal=J. Exp. Med. |volume=173 |issue= 1 |pages= 137-46 |year= 1991 |pmid= 1985119 |doi= }}
*{{cite journal | author=Sgroi D, Koretzky GA, Stamenkovic I |title=Regulation of CD45 engagement by the B-cell receptor CD22. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 9 |pages= 4026-30 |year= 1995 |pmid= 7537381 |doi= }}
*{{cite journal | author=Doody GM, Justement LB, Delibrias CC, ''et al.'' |title=A role in B cell activation for CD22 and the protein tyrosine phosphatase SHP. |journal=Science |volume=269 |issue= 5221 |pages= 242-4 |year= 1995 |pmid= 7618087 |doi= }}
*{{cite journal | author=Crocker PR, Mucklow S, Bouckson V, ''et al.'' |title=Sialoadhesin, a macrophage sialic acid binding receptor for haemopoietic cells with 17 immunoglobulin-like domains. |journal=EMBO J. |volume=13 |issue= 19 |pages= 4490-503 |year= 1994 |pmid= 7925291 |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=Powell LD, Sgroi D, Sjoberg ER, ''et al.'' |title=Natural ligands of the B cell adhesion molecule CD22 beta carry N-linked oligosaccharides with alpha-2,6-linked sialic acids that are required for recognition. |journal=J. Biol. Chem. |volume=268 |issue= 10 |pages= 7019-27 |year= 1993 |pmid= 8463235 |doi= }}
*{{cite journal | author=Leprince C, Draves KE, Geahlen RL, ''et al.'' |title=CD22 associates with the human surface IgM-B-cell antigen receptor complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 8 |pages= 3236-40 |year= 1993 |pmid= 8475064 |doi= }}
*{{cite journal | author=Wilson GL, Najfeld V, Kozlow E, ''et al.'' |title=Genomic structure and chromosomal mapping of the human CD22 gene. |journal=J. Immunol. |volume=150 |issue= 11 |pages= 5013-24 |year= 1993 |pmid= 8496602 |doi= }}
*{{cite journal | author=Law CL, Sidorenko SP, Chandran KA, ''et al.'' |title=CD22 associates with protein tyrosine phosphatase 1C, Syk, and phospholipase C-gamma(1) upon B cell activation. |journal=J. Exp. Med. |volume=183 |issue= 2 |pages= 547-60 |year= 1996 |pmid= 8627166 |doi= }}
*{{cite journal | author=Tuscano JM, Engel P, Tedder TF, ''et al.'' |title=Involvement of p72syk kinase, p53/56lyn kinase and phosphatidyl inositol-3 kinase in signal transduction via the human B lymphocyte antigen CD22. |journal=Eur. J. Immunol. |volume=26 |issue= 6 |pages= 1246-52 |year= 1996 |pmid= 8647200 |doi= }}
*{{cite journal | author=Sgroi D, Nocks A, Stamenkovic I |title=A single N-linked glycosylation site is implicated in the regulation of ligand recognition by the I-type lectins CD22 and CD33. |journal=J. Biol. Chem. |volume=271 |issue= 31 |pages= 18803-9 |year= 1996 |pmid= 8702538 |doi= }}
*{{cite journal | author=Carter RH, Doody GM, Bolen JB, Fearon DT |title=Membrane IgM-induced tyrosine phosphorylation of CD19 requires a CD19 domain that mediates association with components of the B cell antigen receptor complex. |journal=J. Immunol. |volume=158 |issue= 7 |pages= 3062-9 |year= 1997 |pmid= 9120258 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Chan CH, Wang J, French RR, Glennie MJ |title=Internalization of the lymphocytic surface protein CD22 is controlled by a novel membrane proximal cytoplasmic motif. |journal=J. Biol. Chem. |volume=273 |issue= 43 |pages= 27809-15 |year= 1998 |pmid= 9774390 |doi= }}
*{{cite journal | author=Blasioli J, Paust S, Thomas ML |title=Definition of the sites of interaction between the protein tyrosine phosphatase SHP-1 and CD22. |journal=J. Biol. Chem. |volume=274 |issue= 4 |pages= 2303-7 |year= 1999 |pmid= 9890995 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CD5... {November 18, 2007 12:26:07 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 12:26:57 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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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_CD5_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2ja4.
| PDB = {{PDB2|2ja4}}, {{PDB2|2ott}}
| Name = CD5 molecule
| HGNCid = 1685
| Symbol = CD5
| AltSymbols =; T1; LEU1
| OMIM = 153340
| ECnumber =
| Homologene = 7260
| MGIid = 88340
| GeneAtlas_image1 = PBB_GE_CD5_206485_at_tn.png
| Function = {{GNF_GO|id=GO:0005044 |text = scavenger receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0009897 |text = external side of plasma membrane}}
| Process = {{GNF_GO|id=GO:0008037 |text = cell recognition}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008624 |text = induction of apoptosis by extracellular signals}} {{GNF_GO|id=GO:0031295 |text = T cell costimulation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 921
| Hs_Ensembl = ENSG00000110448
| Hs_RefseqProtein = NP_055022
| Hs_RefseqmRNA = NM_014207
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 60626543
| Hs_GenLoc_end = 60651895
| Hs_Uniprot = P06127
| Mm_EntrezGene = 12507
| Mm_Ensembl = ENSMUSG00000024669
| Mm_RefseqmRNA = NM_007650
| Mm_RefseqProtein = NP_031676
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 10785188
| Mm_GenLoc_end = 10806019
| Mm_Uniprot = Q3UP78
}}
}}
'''CD5 molecule''', also known as '''CD5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CD5 CD5 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=921| 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=Berland R, Wortis HH |title=Origins and functions of B-1 cells with notes on the role of CD5. |journal=Annu. Rev. Immunol. |volume=20 |issue= |pages= 253-300 |year= 2002 |pmid= 11861604 |doi= 10.1146/annurev.immunol.20.100301.064833 }}
*{{cite journal | author=Osman N, Ley SC, Crumpton MJ |title=Evidence for an association between the T cell receptor/CD3 antigen complex and the CD5 antigen in human T lymphocytes. |journal=Eur. J. Immunol. |volume=22 |issue= 11 |pages= 2995-3000 |year= 1992 |pmid= 1385158 |doi= }}
*{{cite journal | author=Van de Velde H, von Hoegen I, Luo W, ''et al.'' |title=The B-cell surface protein CD72/Lyb-2 is the ligand for CD5. |journal=Nature |volume=351 |issue= 6328 |pages= 662-5 |year= 1991 |pmid= 1711157 |doi= 10.1038/351662a0 }}
*{{cite journal | author=Jones NH, Clabby ML, Dialynas DP, ''et al.'' |title=Isolation of complementary DNA clones encoding the human lymphocyte glycoprotein T1/Leu-1. |journal=Nature |volume=323 |issue= 6086 |pages= 346-9 |year= 1986 |pmid= 3093892 |doi= 10.1038/323346a0 }}
*{{cite journal | author=Lankester AC, van Schijndel GM, Cordell JL, ''et al.'' |title=CD5 is associated with the human B cell antigen receptor complex. |journal=Eur. J. Immunol. |volume=24 |issue= 4 |pages= 812-6 |year= 1994 |pmid= 7512031 |doi= }}
*{{cite journal | author=Raab M, Yamamoto M, Rudd CE |title=The T-cell antigen CD5 acts as a receptor and substrate for the protein-tyrosine kinase p56lck. |journal=Mol. Cell. Biol. |volume=14 |issue= 5 |pages= 2862-70 |year= 1994 |pmid= 7513045 |doi= }}
*{{cite journal | author=Dianzani U, Bragardo M, Buonfiglio D, ''et al.'' |title=Modulation of CD4 lateral interaction with lymphocyte surface molecules induced by HIV-1 gp120. |journal=Eur. J. Immunol. |volume=25 |issue= 5 |pages= 1306-11 |year= 1995 |pmid= 7539755 |doi= }}
*{{cite journal | author=Van de Velde H, Thielemans K |title=Native soluble CD5 delivers a costimulatory signal to resting human B lymphocytes. |journal=Cell. Immunol. |volume=172 |issue= 1 |pages= 84-91 |year= 1996 |pmid= 8806810 |doi= 10.1006/cimm.1996.0218 }}
*{{cite journal | author=Dennehy KM, Broszeit R, Garnett D, ''et al.'' |title=Thymocyte activation induces the association of phosphatidylinositol 3-kinase and pp120 with CD5. |journal=Eur. J. Immunol. |volume=27 |issue= 3 |pages= 679-86 |year= 1997 |pmid= 9079809 |doi= }}
*{{cite journal | author=Gary-Gouy H, Lang V, Sarun S, ''et al.'' |title=In vivo association of CD5 with tyrosine-phosphorylated ZAP-70 and p21 phospho-zeta molecules in human CD3+ thymocytes. |journal=J. Immunol. |volume=159 |issue= 8 |pages= 3739-47 |year= 1997 |pmid= 9378960 |doi= }}
*{{cite journal | author=Dennehy KM, Broszeit R, Ferris WF, Beyers AD |title=Thymocyte activation induces the association of the proto-oncoprotein c-cbl and ras GTPase-activating protein with CD5. |journal=Eur. J. Immunol. |volume=28 |issue= 5 |pages= 1617-25 |year= 1998 |pmid= 9603468 |doi= }}
*{{cite journal | author=Bauch A, Campbell KS, Reth M |title=Interaction of the CD5 cytoplasmic domain with the Ca2+/calmodulin-dependent kinase IIdelta. |journal=Eur. J. Immunol. |volume=28 |issue= 7 |pages= 2167-77 |year= 1998 |pmid= 9692886 |doi= }}
*{{cite journal | author=Calvo J, Vildà JM, Places L, ''et al.'' |title=Human CD5 signaling and constitutive phosphorylation of C-terminal serine residues by casein kinase II. |journal=J. Immunol. |volume=161 |issue= 11 |pages= 6022-9 |year= 1998 |pmid= 9834084 |doi= }}
*{{cite journal | author=McAlister MS, Davis B, Pfuhl M, Driscoll PC |title=NMR analysis of the N-terminal SRCR domain of human CD5: engineering of a glycoprotein for superior characteristics in NMR experiments. |journal=Protein Eng. |volume=11 |issue= 10 |pages= 847-53 |year= 1999 |pmid= 9862202 |doi= }}
*{{cite journal | author=Perez-Villar JJ, Whitney GS, Bowen MA, ''et al.'' |title=CD5 negatively regulates the T-cell antigen receptor signal transduction pathway: involvement of SH2-containing phosphotyrosine phosphatase SHP-1. |journal=Mol. Cell. Biol. |volume=19 |issue= 4 |pages= 2903-12 |year= 1999 |pmid= 10082557 |doi= }}
*{{cite journal | author=Carmo AM, Castro MA, Arosa FA |title=CD2 and CD3 associate independently with CD5 and differentially regulate signaling through CD5 in Jurkat T cells. |journal=J. Immunol. |volume=163 |issue= 8 |pages= 4238-45 |year= 1999 |pmid= 10510361 |doi= }}
*{{cite journal | author=Vilà JM, Calvo J, Places L, ''et al.'' |title=Role of two conserved cytoplasmic threonine residues (T410 and T412) in CD5 signaling. |journal=J. Immunol. |volume=166 |issue= 1 |pages= 396-402 |year= 2001 |pmid= 11123317 |doi= }}
*{{cite journal | author=Vilà JM, Gimferrer I, Padilla O, ''et al.'' |title=Residues Y429 and Y463 of the human CD5 are targeted by protein tyrosine kinases. |journal=Eur. J. Immunol. |volume=31 |issue= 4 |pages= 1191-8 |year= 2001 |pmid= 11298344 |doi= }}
*{{cite journal | author=Kirchgessner H, Dietrich J, Scherer J, ''et al.'' |title=The transmembrane adaptor protein TRIM regulates T cell receptor (TCR) expression and TCR-mediated signaling via an association with the TCR zeta chain. |journal=J. Exp. Med. |volume=193 |issue= 11 |pages= 1269-84 |year= 2001 |pmid= 11390434 |doi= }}
*{{cite journal | author=Gary-Gouy H, Harriague J, Dalloul A, ''et al.'' |title=CD5-negative regulation of B cell receptor signaling pathways originates from tyrosine residue Y429 outside an immunoreceptor tyrosine-based inhibitory motif. |journal=J. Immunol. |volume=168 |issue= 1 |pages= 232-9 |year= 2002 |pmid= 11751967 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CDC73... {November 18, 2007 12:46:50 PM PST}
- SEARCH REDIRECT: Control Box Found: CDC73 {November 18, 2007 12:47:31 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 12:47:38 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 12:47:38 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 12:47:38 PM PST}
- UPDATED: Updated protein page: CDC73 {November 18, 2007 12:47:50 PM PST}
- INFO: Beginning work on COL6A1... {November 18, 2007 12:28:36 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 12:30:07 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Collagen, type VI, alpha 1
| HGNCid = 2211
| Symbol = COL6A1
| AltSymbols =; OPLL
| OMIM = 120220
| ECnumber =
| Homologene = 1391
| MGIid = 88459
| GeneAtlas_image1 = PBB_GE_COL6A1_212091_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_COL6A1_212937_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_COL6A1_212938_at_tn.png
| Function = {{GNF_GO|id=GO:0005201 |text = extracellular matrix structural constituent}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005581 |text = collagen}} {{GNF_GO|id=GO:0005589 |text = collagen type VI}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006817 |text = phosphate transport}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1291
| Hs_Ensembl = ENSG00000142156
| Hs_RefseqProtein = NP_001839
| Hs_RefseqmRNA = NM_001848
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 21
| Hs_GenLoc_start = 46226111
| Hs_GenLoc_end = 46248443
| Hs_Uniprot = P12109
| Mm_EntrezGene = 12833
| Mm_Ensembl = ENSMUSG00000001119
| Mm_RefseqmRNA = NM_009933
| Mm_RefseqProtein = NP_034063
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 76152508
| Mm_GenLoc_end = 76169760
| Mm_Uniprot = Q8C6Y0
}}
}}
'''Collagen, type VI, alpha 1''', also known as '''COL6A1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: COL6A1 collagen, type VI, alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1291| 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 collagens are a superfamily of proteins that play a role in maintaining the integrity of various tissues. Collagens are extracellular matrix proteins and have a triple-helical domain as their common structural element. Collagen VI is a major structural component of microfibrils. The basic structural unit of collagen VI is a heterotrimer of the alpha1(VI), alpha2(VI), and alpha3(VI) chains. The alpha2(VI) and alpha3(VI) chains are encoded by the COL6A2 and COL6A3 genes, respectively. The protein encoded by this gene is the alpha 1 subunit of type VI collagen (alpha1(VI) chain). Mutations in the genes that code for the collagen VI subunits result in the autosomal dominant disorder, Bethlem myopathy.<ref name="entrez">{{cite web | title = Entrez Gene: COL6A1 collagen, type VI, alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1291| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bertini E, Pepe G |title=Collagen type VI and related disorders: Bethlem myopathy and Ullrich scleroatonic muscular dystrophy. |journal=Eur. J. Paediatr. Neurol. |volume=6 |issue= 4 |pages= 193-8 |year= 2002 |pmid= 12374585 |doi= }}
*{{cite journal | author=Lampe AK, Bushby KM |title=Collagen VI related muscle disorders. |journal=J. Med. Genet. |volume=42 |issue= 9 |pages= 673-85 |year= 2006 |pmid= 16141002 |doi= 10.1136/jmg.2002.002311 }}
*{{cite journal | author=Bidanset DJ, Guidry C, Rosenberg LC, ''et al.'' |title=Binding of the proteoglycan decorin to collagen type VI. |journal=J. Biol. Chem. |volume=267 |issue= 8 |pages= 5250-6 |year= 1992 |pmid= 1544908 |doi= }}
*{{cite journal | author=Saitta B, Wang YM, Renkart L, ''et al.'' |title=The exon organization of the triple-helical coding regions of the human alpha 1(VI) and alpha 2(VI) collagen genes is highly similar. |journal=Genomics |volume=11 |issue= 1 |pages= 145-53 |year= 1992 |pmid= 1765372 |doi= }}
*{{cite journal | author=Chu ML, Pan TC, Conway D, ''et al.'' |title=Sequence analysis of alpha 1(VI) and alpha 2(VI) chains of human type VI collagen reveals internal triplication of globular domains similar to the A domains of von Willebrand factor and two alpha 2(VI) chain variants that differ in the carboxy terminus. |journal=EMBO J. |volume=8 |issue= 7 |pages= 1939-46 |year= 1989 |pmid= 2551668 |doi= }}
*{{cite journal | author=Chu ML, Conway D, Pan TC, ''et al.'' |title=Amino acid sequence of the triple-helical domain of human collagen type VI. |journal=J. Biol. Chem. |volume=263 |issue= 35 |pages= 18601-6 |year= 1989 |pmid= 3198591 |doi= }}
*{{cite journal | author=Weil D, Mattei MG, Passage E, ''et al.'' |title=Cloning and chromosomal localization of human genes encoding the three chains of type VI collagen. |journal=Am. J. Hum. Genet. |volume=42 |issue= 3 |pages= 435-45 |year= 1988 |pmid= 3348212 |doi= }}
*{{cite journal | author=Chu ML, Mann K, Deutzmann R, ''et al.'' |title=Characterization of three constituent chains of collagen type VI by peptide sequences and cDNA clones. |journal=Eur. J. Biochem. |volume=168 |issue= 2 |pages= 309-17 |year= 1987 |pmid= 3665927 |doi= }}
*{{cite journal | author=Jander R, Rauterberg J, Glanville RW |title=Further characterization of the three polypeptide chains of bovine and human short-chain collagen (intima collagen). |journal=Eur. J. Biochem. |volume=133 |issue= 1 |pages= 39-46 |year= 1983 |pmid= 6852033 |doi= }}
*{{cite journal | author=Tillet E, Wiedemann H, Golbik R, ''et al.'' |title=Recombinant expression and structural and binding properties of alpha 1(VI) and alpha 2(VI) chains of human collagen type VI. |journal=Eur. J. Biochem. |volume=221 |issue= 1 |pages= 177-85 |year= 1994 |pmid= 8168508 |doi= }}
*{{cite journal | author=Saitta B, Chu ML |title=Characterization of the human alpha 1(VI) collagen promoter and its comparison with human alpha 2(VI) promoters. |journal=Eur. J. Biochem. |volume=234 |issue= 2 |pages= 542-9 |year= 1996 |pmid= 8536701 |doi= }}
*{{cite journal | author=Jobsis GJ, Bolhuis PA, Boers JM, ''et al.'' |title=Genetic localization of Bethlem myopathy. |journal=Neurology |volume=46 |issue= 3 |pages= 779-82 |year= 1996 |pmid= 8618682 |doi= }}
*{{cite journal | author=Jöbsis GJ, Keizers H, Vreijling JP, ''et al.'' |title=Type VI collagen mutations in Bethlem myopathy, an autosomal dominant myopathy with contractures. |journal=Nat. Genet. |volume=14 |issue= 1 |pages= 113-5 |year= 1996 |pmid= 8782832 |doi= 10.1038/ng0996-113 }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Trikka D, Davis T, Lapenta V, ''et al.'' |title=Human COL6A1: genomic characterization of the globular domains, structural and evolutionary comparison with COL6A2. |journal=Mamm. Genome |volume=8 |issue= 5 |pages= 342-5 |year= 1997 |pmid= 9107679 |doi= }}
*{{cite journal | author=Kuo HJ, Maslen CL, Keene DR, Glanville RW |title=Type VI collagen anchors endothelial basement membranes by interacting with type IV collagen. |journal=J. Biol. Chem. |volume=272 |issue= 42 |pages= 26522-9 |year= 1997 |pmid= 9334230 |doi= }}
*{{cite journal | author=Sasaki T, Brakebusch C, Engel J, Timpl R |title=Mac-2 binding protein is a cell-adhesive protein of the extracellular matrix which self-assembles into ring-like structures and binds beta1 integrins, collagens and fibronectin. |journal=EMBO J. |volume=17 |issue= 6 |pages= 1606-13 |year= 1998 |pmid= 9501082 |doi= 10.1093/emboj/17.6.1606 }}
*{{cite journal | author=Lamandé SR, Bateman JF, Hutchison W, ''et al.'' |title=Reduced collagen VI causes Bethlem myopathy: a heterozygous COL6A1 nonsense mutation results in mRNA decay and functional haploinsufficiency. |journal=Hum. Mol. Genet. |volume=7 |issue= 6 |pages= 981-9 |year= 1998 |pmid= 9580662 |doi= }}
*{{cite journal | author=Pepe G, Giusti B, Bertini E, ''et al.'' |title=A heterozygous splice site mutation in COL6A1 leading to an in-frame deletion of the alpha1(VI) collagen chain in an italian family affected by bethlem myopathy. |journal=Biochem. Biophys. Res. Commun. |volume=258 |issue= 3 |pages= 802-7 |year= 1999 |pmid= 10329467 |doi= 10.1006/bbrc.1999.0680 }}
*{{cite journal | author=Merlini L, Villanova M, Sabatelli P, ''et al.'' |title=Decreased expression of laminin beta 1 in chromosome 21-linked Bethlem myopathy. |journal=Neuromuscul. Disord. |volume=9 |issue= 5 |pages= 326-9 |year= 1999 |pmid= 10407855 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CPT2... {November 18, 2007 12:30:07 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 12:30:52 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Carnitine palmitoyltransferase II
| HGNCid = 2330
| Symbol = CPT2
| AltSymbols =; CPT1; CPTASE
| OMIM = 600650
| ECnumber =
| Homologene = 77
| MGIid = 109176
| GeneAtlas_image1 = PBB_GE_CPT2_204264_at_tn.png
| GeneAtlas_image2 = PBB_GE_CPT2_204263_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004095 |text = carnitine O-palmitoyltransferase activity}} {{GNF_GO|id=GO:0008415 |text = acyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005743 |text = mitochondrial inner membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006631 |text = fatty acid metabolic process}} {{GNF_GO|id=GO:0006635 |text = fatty acid beta-oxidation}} {{GNF_GO|id=GO:0006810 |text = transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1376
| Hs_Ensembl = ENSG00000157184
| Hs_RefseqProtein = NP_000089
| Hs_RefseqmRNA = NM_000098
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 53434689
| Hs_GenLoc_end = 53626815
| Hs_Uniprot = P23786
| Mm_EntrezGene = 12896
| Mm_Ensembl = ENSMUSG00000028607
| Mm_RefseqmRNA = NM_009949
| Mm_RefseqProtein = NP_034079
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 107401912
| Mm_GenLoc_end = 107421466
| Mm_Uniprot = Q3TFS0
}}
}}
'''Carnitine palmitoyltransferase II''', also known as '''CPT2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CPT2 carnitine palmitoyltransferase II| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1376| 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 = Carnitine palmitoyltransferase II precursor (CPT2) is a nuclear protein which is transported to the mitochondrial inner membrane. CPT2 together with carnitine palmitoyltransferase I oxidizes long-chain fatty acids in the mitochondria. Defects in this gene are associated with mitochondrial long-chain fatty-acid (LCFA) oxidation disorders.<ref name="entrez">{{cite web | title = Entrez Gene: CPT2 carnitine palmitoyltransferase II| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1376| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bonnefont JP, Demaugre F, Prip-Buus C, ''et al.'' |title=Carnitine palmitoyltransferase deficiencies. |journal=Mol. Genet. Metab. |volume=68 |issue= 4 |pages= 424-40 |year= 2000 |pmid= 10607472 |doi= 10.1006/mgme.1999.2938 }}
*{{cite journal | author=van der Leij FR, Huijkman NC, Boomsma C, ''et al.'' |title=Genomics of the human carnitine acyltransferase genes. |journal=Mol. Genet. Metab. |volume=71 |issue= 1-2 |pages= 139-53 |year= 2000 |pmid= 11001805 |doi= 10.1006/mgme.2000.3055 }}
*{{cite journal | author=Sigauke E, Rakheja D, Kitson K, Bennett MJ |title=Carnitine palmitoyltransferase II deficiency: a clinical, biochemical, and molecular review. |journal=Lab. Invest. |volume=83 |issue= 11 |pages= 1543-54 |year= 2003 |pmid= 14615409 |doi= }}
*{{cite journal | author=Minoletti F, Colombo I, Martin AL, ''et al.'' |title=Localization of the human gene for carnitine palmitoyltransferase to 1p13-p11 by nonradioactive in situ hybridization. |journal=Genomics |volume=13 |issue= 4 |pages= 1372-4 |year= 1992 |pmid= 1339389 |doi= }}
*{{cite journal | author=Taroni F, Verderio E, Fiorucci S, ''et al.'' |title=Molecular characterization of inherited carnitine palmitoyltransferase II deficiency. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 18 |pages= 8429-33 |year= 1992 |pmid= 1528846 |doi= }}
*{{cite journal | author=Finocchiaro G, Taroni F, Rocchi M, ''et al.'' |title=cDNA cloning, sequence analysis, and chromosomal localization of human carnitine palmitoyltransferase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 23 |pages= 10981 |year= 1992 |pmid= 1961767 |doi= }}
*{{cite journal | author=Finocchiaro G, Taroni F, Rocchi M, ''et al.'' |title=cDNA cloning, sequence analysis, and chromosomal localization of the gene for human carnitine palmitoyltransferase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 2 |pages= 661-5 |year= 1991 |pmid= 1988962 |doi= }}
*{{cite journal | author=Finocchiaro G, Colombo I, DiDonato S |title=Purification, characterization and partial amino acid sequences of carnitine palmitoyl-transferase from human liver. |journal=FEBS Lett. |volume=274 |issue= 1-2 |pages= 163-6 |year= 1991 |pmid= 2174799 |doi= }}
*{{cite journal | author=Verderio E, Cavadini P, Montermini L, ''et al.'' |title=Carnitine palmitoyltransferase II deficiency: structure of the gene and characterization of two novel disease-causing mutations. |journal=Hum. Mol. Genet. |volume=4 |issue= 1 |pages= 19-29 |year= 1995 |pmid= 7711730 |doi= }}
*{{cite journal | author=Britton CH, Schultz RA, Zhang B, ''et al.'' |title=Human liver mitochondrial carnitine palmitoyltransferase I: characterization of its cDNA and chromosomal localization and partial analysis of the gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 6 |pages= 1984-8 |year= 1995 |pmid= 7892212 |doi= }}
*{{cite journal | author=Gellera C, Verderio E, Floridia G, ''et al.'' |title=Assignment of the human carnitine palmitoyltransferase II gene (CPT1) to chromosome 1p32. |journal=Genomics |volume=24 |issue= 1 |pages= 195-7 |year= 1995 |pmid= 7896283 |doi= 10.1006/geno.1994.1605 }}
*{{cite journal | author=Montermini L, Wang H, Verderio E, ''et al.'' |title=Identification of 5' regulatory regions of the human carnitine palmitoyltransferase II gene. |journal=Biochim. Biophys. Acta |volume=1219 |issue= 1 |pages= 237-40 |year= 1994 |pmid= 8086471 |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=Taroni F, Verderio E, Dworzak F, ''et al.'' |title=Identification of a common mutation in the carnitine palmitoyltransferase II gene in familial recurrent myoglobinuria patients. |journal=Nat. Genet. |volume=4 |issue= 3 |pages= 314-20 |year= 1993 |pmid= 8358442 |doi= 10.1038/ng0793-314 }}
*{{cite journal | author=Verderio E, Cavadini P, Pandolfo M, ''et al.'' |title=Two novel sequence polymorphisms of the human carnitine palmitoyltransferase II (CPT1) gene. |journal=Hum. Mol. Genet. |volume=2 |issue= 3 |pages= 334 |year= 1993 |pmid= 8499929 |doi= }}
*{{cite journal | author=Bonnefont JP, Taroni F, Cavadini P, ''et al.'' |title=Molecular analysis of carnitine palmitoyltransferase II deficiency with hepatocardiomuscular expression. |journal=Am. J. Hum. Genet. |volume=58 |issue= 5 |pages= 971-8 |year= 1996 |pmid= 8651281 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Wataya K, Akanuma J, Cavadini P, ''et al.'' |title=Two CPT2 mutations in three Japanese patients with carnitine palmitoyltransferase II deficiency: functional analysis and association with polymorphic haplotypes and two clinical phenotypes. |journal=Hum. Mutat. |volume=11 |issue= 5 |pages= 377-86 |year= 1998 |pmid= 9600456 |doi= 10.1002/(SICI)1098-1004(1998)11:5<377::AID-HUMU5>3.0.CO;2-E }}
*{{cite journal | author=Yang BZ, Ding JH, Dewese T, ''et al.'' |title=Identification of four novel mutations in patients with carnitine palmitoyltransferase II (CPT II) deficiency. |journal=Mol. Genet. Metab. |volume=64 |issue= 4 |pages= 229-36 |year= 1998 |pmid= 9758712 |doi= 10.1006/mgme.1998.2711 }}
*{{cite journal | author=Taggart RT, Smail D, Apolito C, Vladutiu GD |title=Novel mutations associated with carnitine palmitoyltransferase II deficiency. |journal=Hum. Mutat. |volume=13 |issue= 3 |pages= 210-20 |year= 1999 |pmid= 10090476 |doi= 10.1002/(SICI)1098-1004(1999)13:3<210::AID-HUMU5>3.0.CO;2-0 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CSTB... {November 18, 2007 12:30:53 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 12:31:49 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CSTB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1stf.
| PDB = {{PDB2|1stf}}, {{PDB2|2oct}}
| Name = Cystatin B (stefin B)
| HGNCid = 2482
| Symbol = CSTB
| AltSymbols =; CST6; EPM1; PME; STFB
| OMIM = 601145
| ECnumber =
| Homologene = 79
| MGIid = 109514
| GeneAtlas_image1 = PBB_GE_CSTB_201201_at_tn.png
| Function = {{GNF_GO|id=GO:0004869 |text = cysteine protease inhibitor activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0008344 |text = adult locomotory behavior}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1476
| Hs_Ensembl = ENSG00000160213
| Hs_RefseqProtein = NP_000091
| Hs_RefseqmRNA = NM_000100
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 21
| Hs_GenLoc_start = 44016826
| Hs_GenLoc_end = 44020585
| Hs_Uniprot = P04080
| Mm_EntrezGene = 13014
| Mm_Ensembl = ENSMUSG00000005054
| Mm_RefseqmRNA = NM_007793
| Mm_RefseqProtein = NP_031819
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 77828799
| Mm_GenLoc_end = 77830755
| Mm_Uniprot = Q62426
}}
}}
'''Cystatin B (stefin B)''', also known as '''CSTB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CSTB cystatin B (stefin B)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1476| 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 cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and kininogens. This gene encodes a stefin that functions as an intracellular thiol protease inhibitor. The protein is able to form a dimer stabilized by noncovalent forces, inhibiting papain and cathepsins l, h and b. The protein is thought to play a role in protecting against the proteases leaking from lysosomes. Evidence indicates that mutations in this gene are responsible for the primary defects in patients with progressive myoclonic epilepsy (EPM1).<ref name="entrez">{{cite web | title = Entrez Gene: CSTB cystatin B (stefin B)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1476| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Turk V, Bode W |title=The cystatins: protein inhibitors of cysteine proteinases. |journal=FEBS Lett. |volume=285 |issue= 2 |pages= 213-9 |year= 1991 |pmid= 1855589 |doi= }}
*{{cite journal | author=Järvinen M, Rinne A, Hopsu-Havu VK |title=Human cystatins in normal and diseased tissues--a review. |journal=Acta Histochem. |volume=82 |issue= 1 |pages= 5-18 |year= 1988 |pmid= 3122506 |doi= }}
*{{cite journal | author=Brown WM, Dziegielewska KM |title=Friends and relations of the cystatin superfamily--new members and their evolution. |journal=Protein Sci. |volume=6 |issue= 1 |pages= 5-12 |year= 1997 |pmid= 9007972 |doi= }}
*{{cite journal | author=Kos J, Lah TT |title=Cysteine proteinases and their endogenous inhibitors: target proteins for prognosis, diagnosis and therapy in cancer (review). |journal=Oncol. Rep. |volume=5 |issue= 6 |pages= 1349-61 |year= 1998 |pmid= 9769367 |doi= }}
*{{cite journal | author=Stubbs MT, Laber B, Bode W, ''et al.'' |title=The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction. |journal=EMBO J. |volume=9 |issue= 6 |pages= 1939-47 |year= 1990 |pmid= 2347312 |doi= }}
*{{cite journal | author=Jerala R, Trstenjak M, Lenarcic B, Turk V |title=Cloning a synthetic gene for human stefin B and its expression in E. coli. |journal=FEBS Lett. |volume=239 |issue= 1 |pages= 41-4 |year= 1988 |pmid= 3053245 |doi= }}
*{{cite journal | author=Lenarcic B, Kos J, Dolenc I, ''et al.'' |title=Cathepsin D inactivates cysteine proteinase inhibitors, cystatins. |journal=Biochem. Biophys. Res. Commun. |volume=154 |issue= 2 |pages= 765-72 |year= 1988 |pmid= 3261170 |doi= }}
*{{cite journal | author=Ritonja A, Machleidt W, Barrett AJ |title=Amino acid sequence of the intracellular cysteine proteinase inhibitor cystatin B from human liver. |journal=Biochem. Biophys. Res. Commun. |volume=131 |issue= 3 |pages= 1187-92 |year= 1985 |pmid= 3902020 |doi= }}
*{{cite journal | author=Spiess E, Brüning A, Gack S, ''et al.'' |title=Cathepsin B activity in human lung tumor cell lines: ultrastructural localization, pH sensitivity, and inhibitor status at the cellular level. |journal=J. Histochem. Cytochem. |volume=42 |issue= 7 |pages= 917-29 |year= 1994 |pmid= 8014475 |doi= }}
*{{cite journal | author=Lehesjoki AE, Koskiniemi M, Norio R, ''et al.'' |title=Localization of the EPM1 gene for progressive myoclonus epilepsy on chromosome 21: linkage disequilibrium allows high resolution mapping. |journal=Hum. Mol. Genet. |volume=2 |issue= 8 |pages= 1229-34 |year= 1993 |pmid= 8104628 |doi= }}
*{{cite journal | author=Pennacchio LA, Lehesjoki AE, Stone NE, ''et al.'' |title=Mutations in the gene encoding cystatin B in progressive myoclonus epilepsy (EPM1) |journal=Science |volume=271 |issue= 5256 |pages= 1731-4 |year= 1996 |pmid= 8596935 |doi= }}
*{{cite journal | author=Pennacchio LA, Myers RM |title=Isolation and characterization of the mouse cystatin B gene. |journal=Genome Res. |volume=6 |issue= 11 |pages= 1103-9 |year= 1997 |pmid= 8938434 |doi= }}
*{{cite journal | author=Lalioti MD, Mirotsou M, Buresi C, ''et al.'' |title=Identification of mutations in cystatin B, the gene responsible for the Unverricht-Lundborg type of progressive myoclonus epilepsy (EPM1). |journal=Am. J. Hum. Genet. |volume=60 |issue= 2 |pages= 342-51 |year= 1997 |pmid= 9012407 |doi= }}
*{{cite journal | author=Lafrenière RG, Rochefort DL, Chrétien N, ''et al.'' |title=Unstable insertion in the 5' flanking region of the cystatin B gene is the most common mutation in progressive myoclonus epilepsy type 1, EPM1. |journal=Nat. Genet. |volume=15 |issue= 3 |pages= 298-302 |year= 1997 |pmid= 9054946 |doi= 10.1038/ng0397-298 }}
*{{cite journal | author=Virtaneva K, D'Amato E, Miao J, ''et al.'' |title=Unstable minisatellite expansion causing recessively inherited myoclonus epilepsy, EPM1. |journal=Nat. Genet. |volume=15 |issue= 4 |pages= 393-6 |year= 1997 |pmid= 9090386 |doi= 10.1038/ng0497-393 }}
*{{cite journal | author=Bespalova IN, Adkins S, Pranzatelli M, Burmeister M |title=Novel cystatin B mutation and diagnostic PCR assay in an Unverricht-Lundborg progressive myoclonus epilepsy patient. |journal=Am. J. Med. Genet. |volume=74 |issue= 5 |pages= 467-71 |year= 1997 |pmid= 9342192 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DAZL... {November 18, 2007 12:31:49 PM PST}
- SEARCH REDIRECT: Control Box Found: DAZL {November 18, 2007 12:32:41 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 12:32:48 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 12:32:48 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 12:32:48 PM PST}
- UPDATED: Updated protein page: DAZL {November 18, 2007 12:33:01 PM PST}
- INFO: Beginning work on DKC1... {November 18, 2007 12:33:01 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 12:33:58 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Dyskeratosis congenita 1, dyskerin
| HGNCid = 2890
| Symbol = DKC1
| AltSymbols =; DKC; NAP57; NOLA4; XAP101; dyskerin
| OMIM = 300126
| ECnumber =
| Homologene = 1045
| MGIid =
| GeneAtlas_image1 = PBB_GE_DKC1_201479_at_tn.png
| GeneAtlas_image2 = PBB_GE_DKC1_201478_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_DKC1_216212_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003720 |text = telomerase activity}} {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0016439 |text = tRNA-pseudouridine synthase activity}} {{GNF_GO|id=GO:0016853 |text = isomerase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005654 |text = nucleoplasm}} {{GNF_GO|id=GO:0005697 |text = telomerase holoenzyme complex}} {{GNF_GO|id=GO:0005730 |text = nucleolus}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006364 |text = rRNA processing}} {{GNF_GO|id=GO:0007004 |text = telomere maintenance via telomerase}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1736
| Hs_Ensembl = ENSG00000130826
| Hs_RefseqProtein = NP_001354
| Hs_RefseqmRNA = NM_001363
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 153644229
| Hs_GenLoc_end = 153659158
| Hs_Uniprot = O60832
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Dyskeratosis congenita 1, dyskerin''', also known as '''DKC1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DKC1 dyskeratosis congenita 1, dyskerin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1736| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is a member of the H/ACA snoRNPs (small nucleolar ribonucleoproteins) gene family. snoRNPs are involved in various aspects of rRNA processing and modification and have been classified into two families: C/D and H/ACA. The H/ACA snoRNPs also include the NOLA1, 2 and 3 proteins. The protein encoded by this gene and the three NOLA proteins localize to the dense fibrillar components of nucleoli and to coiled (Cajal) bodies in the nucleus. Both 18S rRNA production and rRNA pseudouridylation are impaired if any one of the four proteins is depleted. These four H/ACA snoRNP proteins are also components of the telomerase complex. The protein encoded by this gene is related to the Saccharomyces cerevisiae Cbf5p and Drosophila melanogaster Nop60B proteins. The gene lies in a tail-to-tail orientation with the palmitoylated erythrocyte membrane protein (MPP1) gene and is transcribed in a telomere to centromere direction. Both nucleotide substitutions and single trinucleotide repeat polymorphisms have been found in this gene. Mutations in this gene cause X-linked dyskeratosis congenita disease.<ref name="entrez">{{cite web | title = Entrez Gene: DKC1 dyskeratosis congenita 1, dyskerin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1736| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Marrone A, Dokal I |title=Dyskeratosis congenita: molecular insights into telomerase function, ageing and cancer. |journal=Expert reviews in molecular medicine |volume=6 |issue= 26 |pages= 1-23 |year= 2007 |pmid= 15613268 |doi= 10.1017/S1462399404008671 }}
*{{cite journal | author=Yamaguchi H |title=Mutations of telomerase complex genes linked to bone marrow failures. |journal=Journal of Nippon Medical School = Nihon Ika Daigaku zasshi |volume=74 |issue= 3 |pages= 202-9 |year= 2007 |pmid= 17625368 |doi= }}
*{{cite journal | author=Aalfs CM, van den Berg H, Barth PG, Hennekam RC |title=The Hoyeraal-Hreidarsson syndrome: the fourth case of a separate entity with prenatal growth retardation, progressive pancytopenia and cerebellar hypoplasia. |journal=Eur. J. Pediatr. |volume=154 |issue= 4 |pages= 304-8 |year= 1995 |pmid= 7607282 |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=Devriendt K, Matthijs G, Legius E, ''et al.'' |title=Skewed X-chromosome inactivation in female carriers of dyskeratosis congenita. |journal=Am. J. Hum. Genet. |volume=60 |issue= 3 |pages= 581-7 |year= 1997 |pmid= 9042917 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Heiss NS, Knight SW, Vulliamy TJ, ''et al.'' |title=X-linked dyskeratosis congenita is caused by mutations in a highly conserved gene with putative nucleolar functions. |journal=Nat. Genet. |volume=19 |issue= 1 |pages= 32-8 |year= 1998 |pmid= 9590285 |doi= 10.1038/ng0598-32 }}
*{{cite journal | author=Hassock S, Vetrie D, Giannelli F |title=Mapping and characterization of the X-linked dyskeratosis congenita (DKC) gene. |journal=Genomics |volume=55 |issue= 1 |pages= 21-7 |year= 1999 |pmid= 9888995 |doi= 10.1006/geno.1998.5600 }}
*{{cite journal | author=McGrath JA |title=Dyskeratosis congenita: new clinical and molecular insights into ribosome function. |journal=Lancet |volume=353 |issue= 9160 |pages= 1204-5 |year= 1999 |pmid= 10217077 |doi= }}
*{{cite journal | author=Knight SW, Heiss NS, Vulliamy TJ, ''et al.'' |title=X-linked dyskeratosis congenita is predominantly caused by missense mutations in the DKC1 gene. |journal=Am. J. Hum. Genet. |volume=65 |issue= 1 |pages= 50-8 |year= 1999 |pmid= 10364516 |doi= }}
*{{cite journal | author=Vulliamy TJ, Knight SW, Heiss NS, ''et al.'' |title=Dyskeratosis congenita caused by a 3' deletion: germline and somatic mosaicism in a female carrier. |journal=Blood |volume=94 |issue= 4 |pages= 1254-60 |year= 1999 |pmid= 10438713 |doi= }}
*{{cite journal | author=Heiss NS, Girod A, Salowsky R, ''et al.'' |title=Dyskerin localizes to the nucleolus and its mislocalization is unlikely to play a role in the pathogenesis of dyskeratosis congenita. |journal=Hum. Mol. Genet. |volume=8 |issue= 13 |pages= 2515-24 |year= 2000 |pmid= 10556300 |doi= }}
*{{cite journal | author=Knight SW, Heiss NS, Vulliamy TJ, ''et al.'' |title=Unexplained aplastic anaemia, immunodeficiency, and cerebellar hypoplasia (Hoyeraal-Hreidarsson syndrome) due to mutations in the dyskeratosis congenita gene, DKC1. |journal=Br. J. Haematol. |volume=107 |issue= 2 |pages= 335-9 |year= 2000 |pmid= 10583221 |doi= }}
*{{cite journal | author=Mitchell JR, Wood E, Collins K |title=A telomerase component is defective in the human disease dyskeratosis congenita. |journal=Nature |volume=402 |issue= 6761 |pages= 551-5 |year= 1999 |pmid= 10591218 |doi= 10.1038/990141 }}
*{{cite journal | author=Yaghmai R, Kimyai-Asadi A, Rostamiani K, ''et al.'' |title=Overlap of dyskeratosis congenita with the Hoyeraal-Hreidarsson syndrome. |journal=J. Pediatr. |volume=136 |issue= 3 |pages= 390-3 |year= 2000 |pmid= 10700698 |doi= 10.1067/mpd.2000.104295 }}
*{{cite journal | author=Heiss NS, Bächner D, Salowsky R, ''et al.'' |title=Gene structure and expression of the mouse dyskeratosis congenita gene, dkc1. |journal=Genomics |volume=67 |issue= 2 |pages= 153-63 |year= 2000 |pmid= 10903840 |doi= 10.1006/geno.2000.6227 }}
*{{cite journal | author=Pogacić V, Dragon F, Filipowicz W |title=Human H/ACA small nucleolar RNPs and telomerase share evolutionarily conserved proteins NHP2 and NOP10. |journal=Mol. Cell. Biol. |volume=20 |issue= 23 |pages= 9028-40 |year= 2000 |pmid= 11074001 |doi= }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
*{{cite journal | author=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=Knight SW, Vulliamy TJ, Morgan B, ''et al.'' |title=Identification of novel DKC1 mutations in patients with dyskeratosis congenita: implications for pathophysiology and diagnosis. |journal=Hum. Genet. |volume=108 |issue= 4 |pages= 299-303 |year= 2001 |pmid= 11379875 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on EXT1... {November 18, 2007 12:33:59 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 12:35:18 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Exostoses (multiple) 1
| HGNCid = 3512
| Symbol = EXT1
| AltSymbols =; EXT; ttv
| OMIM = 608177
| ECnumber =
| Homologene = 30957
| MGIid = 894663
| GeneAtlas_image1 = PBB_GE_EXT1_201995_at_tn.png
| GeneAtlas_image2 = PBB_GE_EXT1_214985_at_tn.png
| Function = {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}} {{GNF_GO|id=GO:0050508 |text = glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity}} {{GNF_GO|id=GO:0050509 |text = N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005789 |text = endoplasmic reticulum membrane}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0030176 |text = integral to endoplasmic reticulum membrane}}
| Process = {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0006024 |text = glycosaminoglycan biosynthetic process}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007369 |text = gastrulation}} {{GNF_GO|id=GO:0007492 |text = endoderm development}} {{GNF_GO|id=GO:0007498 |text = mesoderm development}} {{GNF_GO|id=GO:0015012 |text = heparan sulfate proteoglycan biosynthetic process}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2131
| Hs_Ensembl = ENSG00000182197
| Hs_RefseqProtein = NP_000118
| Hs_RefseqmRNA = NM_000127
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 118875910
| Hs_GenLoc_end = 119193119
| Hs_Uniprot = Q16394
| Mm_EntrezGene = 14042
| Mm_Ensembl = ENSMUSG00000061731
| Mm_RefseqmRNA = NM_010162
| Mm_RefseqProtein = NP_034292
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 52898747
| Mm_GenLoc_end = 53175446
| Mm_Uniprot = Q3V1P4
}}
}}
'''Exostoses (multiple) 1''', also known as '''EXT1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EXT1 exostoses (multiple) 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2131| 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 an endoplasmic reticulum-resident type II transmembrane glycosyltransferase involved in the chain elongation step of heparan sulfate biosynthesis. Mutations in this gene cause the type I form of multiple exostoses.<ref name="entrez">{{cite web | title = Entrez Gene: EXT1 exostoses (multiple) 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2131| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wuyts W, Van Hul W |title=Molecular basis of multiple exostoses: mutations in the EXT1 and EXT2 genes. |journal=Hum. Mutat. |volume=15 |issue= 3 |pages= 220-7 |year= 2000 |pmid= 10679937 |doi= 10.1002/(SICI)1098-1004(200003)15:3<220::AID-HUMU2>3.0.CO;2-K }}
*{{cite journal | author=Duncan G, McCormick C, Tufaro F |title=The link between heparan sulfate and hereditary bone disease: finding a function for the EXT family of putative tumor suppressor proteins. |journal=J. Clin. Invest. |volume=108 |issue= 4 |pages= 511-6 |year= 2001 |pmid= 11518722 |doi= }}
*{{cite journal | author=Ogle RF, Dalzell P, Turner G, ''et al.'' |title=Multiple exostoses in a patient with t(8;11)(q24.11;p15.5). |journal=J. Med. Genet. |volume=28 |issue= 12 |pages= 881-3 |year= 1992 |pmid= 1757967 |doi= }}
*{{cite journal | author=Ahn J, Lüdecke HJ, Lindow S, ''et al.'' |title=Cloning of the putative tumour suppressor gene for hereditary multiple exostoses (EXT1). |journal=Nat. Genet. |volume=11 |issue= 2 |pages= 137-43 |year= 1995 |pmid= 7550340 |doi= 10.1038/ng1095-137 }}
*{{cite journal | author=Cook A, Raskind W, Blanton SH, ''et al.'' |title=Genetic heterogeneity in families with hereditary multiple exostoses. |journal=Am. J. Hum. Genet. |volume=53 |issue= 1 |pages= 71-9 |year= 1993 |pmid= 8317501 |doi= }}
*{{cite journal | author=Hou J, Parrish J, Lüdecke HJ, ''et al.'' |title=A 4-megabase YAC contig that spans the Langer-Giedion syndrome region on human chromosome 8q24.1: use in refining the location of the trichorhinophalangeal syndrome and multiple exostoses genes (TRPS1 and EXT1). |journal=Genomics |volume=29 |issue= 1 |pages= 87-97 |year= 1996 |pmid= 8530105 |doi= }}
*{{cite journal | author=Hecht JT, Hogue D, Wang Y, ''et al.'' |title=Hereditary multiple exostoses (EXT): mutational studies of familial EXT1 cases and EXT-associated malignancies. |journal=Am. J. Hum. Genet. |volume=60 |issue= 1 |pages= 80-6 |year= 1997 |pmid= 8981950 |doi= }}
*{{cite journal | author=Lüdecke HJ, Ahn J, Lin X, ''et al.'' |title=Genomic organization and promoter structure of the human EXT1 gene. |journal=Genomics |volume=40 |issue= 2 |pages= 351-4 |year= 1997 |pmid= 9119404 |doi= 10.1006/geno.1996.4577 }}
*{{cite journal | author=Philippe C, Porter DE, Emerton ME, ''et al.'' |title=Mutation screening of the EXT1 and EXT2 genes in patients with hereditary multiple exostoses. |journal=Am. J. Hum. Genet. |volume=61 |issue= 3 |pages= 520-8 |year= 1997 |pmid= 9326317 |doi= }}
*{{cite journal | author=Wuyts W, Van Hul W, De Boulle K, ''et al.'' |title=Mutations in the EXT1 and EXT2 genes in hereditary multiple exostoses. |journal=Am. J. Hum. Genet. |volume=62 |issue= 2 |pages= 346-54 |year= 1998 |pmid= 9463333 |doi= }}
*{{cite journal | author=Raskind WH, Conrad EU, Matsushita M, ''et al.'' |title=Evaluation of locus heterogeneity and EXT1 mutations in 34 families with hereditary multiple exostoses. |journal=Hum. Mutat. |volume=11 |issue= 3 |pages= 231-9 |year= 1998 |pmid= 9521425 |doi= 10.1002/(SICI)1098-1004(1998)11:3<231::AID-HUMU8>3.0.CO;2-K }}
*{{cite journal | author=McCormick C, Leduc Y, Martindale D, ''et al.'' |title=The putative tumour suppressor EXT1 alters the expression of cell-surface heparan sulfate. |journal=Nat. Genet. |volume=19 |issue= 2 |pages= 158-61 |year= 1998 |pmid= 9620772 |doi= 10.1038/514 }}
*{{cite journal | author=Lin X, Gan L, Klein WH, Wells D |title=Expression and functional analysis of mouse EXT1, a homolog of the human multiple exostoses type 1 gene. |journal=Biochem. Biophys. Res. Commun. |volume=248 |issue= 3 |pages= 738-43 |year= 1998 |pmid= 9703997 |doi= 10.1006/bbrc.1998.9050 }}
*{{cite journal | author=Lind T, Tufaro F, McCormick C, ''et al.'' |title=The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate. |journal=J. Biol. Chem. |volume=273 |issue= 41 |pages= 26265-8 |year= 1998 |pmid= 9756849 |doi= }}
*{{cite journal | author=Bovée JV, Cleton-Jansen AM, Wuyts W, ''et al.'' |title=EXT-mutation analysis and loss of heterozygosity in sporadic and hereditary osteochondromas and secondary chondrosarcomas. |journal=Am. J. Hum. Genet. |volume=65 |issue= 3 |pages= 689-98 |year= 1999 |pmid= 10441575 |doi= }}
*{{cite journal | author=Xu L, Xia J, Jiang H, ''et al.'' |title=Mutation analysis of hereditary multiple exostoses in the Chinese. |journal=Hum. Genet. |volume=105 |issue= 1-2 |pages= 45-50 |year= 1999 |pmid= 10480354 |doi= }}
*{{cite journal | author=Simmons AD, Musy MM, Lopes CS, ''et al.'' |title=A direct interaction between EXT proteins and glycosyltransferases is defective in hereditary multiple exostoses. |journal=Hum. Mol. Genet. |volume=8 |issue= 12 |pages= 2155-64 |year= 1999 |pmid= 10545594 |doi= }}
*{{cite journal | author=McCormick C, Duncan G, Goutsos KT, Tufaro F |title=The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 2 |pages= 668-73 |year= 2000 |pmid= 10639137 |doi= }}
*{{cite journal | author=Kobayashi S, Morimoto K, Shimizu T, ''et al.'' |title=Association of EXT1 and EXT2, hereditary multiple exostoses gene products, in Golgi apparatus. |journal=Biochem. Biophys. Res. Commun. |volume=268 |issue= 3 |pages= 860-7 |year= 2000 |pmid= 10679296 |doi= 10.1006/bbrc.2000.2219 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FMO3... {November 18, 2007 12:35:18 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 12:36:08 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Flavin containing monooxygenase 3
| HGNCid = 3771
| Symbol = FMO3
| AltSymbols =; FMOII; MGC34400; dJ127D3.1
| OMIM = 136132
| ECnumber =
| Homologene = 68130
| MGIid = 1100496
| GeneAtlas_image1 = PBB_GE_FMO3_40665_at_tn.png
| GeneAtlas_image2 = PBB_GE_FMO3_206496_at_tn.png
| Function = {{GNF_GO|id=GO:0004497 |text = monooxygenase activity}} {{GNF_GO|id=GO:0004499 |text = flavin-containing monooxygenase activity}} {{GNF_GO|id=GO:0015036 |text = disulfide oxidoreductase activity}} {{GNF_GO|id=GO:0050660 |text = FAD binding}} {{GNF_GO|id=GO:0050661 |text = NADP binding}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0031227 |text = intrinsic to endoplasmic reticulum membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2328
| Hs_Ensembl = ENSG00000007933
| Hs_RefseqProtein = NP_001002294
| Hs_RefseqmRNA = NM_001002294
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 169326642
| Hs_GenLoc_end = 169353583
| Hs_Uniprot = P31513
| Mm_EntrezGene = 14262
| Mm_Ensembl = ENSMUSG00000026691
| Mm_RefseqmRNA = NM_008030
| Mm_RefseqProtein = NP_032056
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 164790475
| Mm_GenLoc_end = 164821205
| Mm_Uniprot = Q3UEN4
}}
}}
'''Flavin containing monooxygenase 3''', also known as '''FMO3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FMO3 flavin containing monooxygenase 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2328| 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=Cashman JR, Park SB, Berkman CE, Cashman LE |title=Role of hepatic flavin-containing monooxygenase 3 in drug and chemical metabolism in adult humans. |journal=Chem. Biol. Interact. |volume=96 |issue= 1 |pages= 33-46 |year= 1995 |pmid= 7720103 |doi= }}
*{{cite journal | author=Cashman JR |title=The implications of polymorphisms in mammalian flavin-containing monooxygenases in drug discovery and development. |journal=Drug Discov. Today |volume=9 |issue= 13 |pages= 574-81 |year= 2004 |pmid= 15203093 |doi= 10.1016/S1359-6446(04)03136-8 }}
*{{cite journal | author=Zhou J, Shephard EA |title=Mutation, polymorphism and perspectives for the future of human flavin-containing monooxygenase 3. |journal=Mutat. Res. |volume=612 |issue= 3 |pages= 165-71 |year= 2006 |pmid= 16481213 |doi= 10.1016/j.mrrev.2005.09.001 }}
*{{cite journal | author=Lomri N, Gu Q, Cashman JR |title=Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 5 |pages= 1685-9 |year= 1992 |pmid= 1542660 |doi= }}
*{{cite journal | author=Humbert JA, Hammond KB, Hathaway WE |title=Trimethylaminuria: the fish-odour syndrome. |journal=Lancet |volume=2 |issue= 7676 |pages= 770-1 |year= 1970 |pmid= 4195988 |doi= }}
*{{cite journal | author=Higgins T, Chaykin S, Hammond KB, Humbert JR |title=Trimethylamine N-oxide synthesis: a human variant. |journal=Biochemical medicine |volume=6 |issue= 4 |pages= 392-6 |year= 1972 |pmid= 5048998 |doi= }}
*{{cite journal | author=Lomri N, Gu Q, Cashman JR |title=Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 21 |pages= 9910 |year= 1995 |pmid= 7568243 |doi= }}
*{{cite journal | author=Bhamre S, Bhagwat SV, Shankar SK, ''et al.'' |title=Flavin-containing monooxygenase mediated metabolism of psychoactive drugs by human brain microsomes. |journal=Brain Res. |volume=672 |issue= 1-2 |pages= 276-80 |year= 1995 |pmid= 7749747 |doi= }}
*{{cite journal | author=Cashman JR, Park SB, Yang ZC, ''et al.'' |title=Chemical, enzymatic, and human enantioselective S-oxygenation of cimetidine. |journal=Drug Metab. Dispos. |volume=21 |issue= 4 |pages= 587-97 |year= 1993 |pmid= 8104117 |doi= }}
*{{cite journal | author=Park SB, Jacob P, Benowitz NL, Cashman JR |title=Stereoselective metabolism of (S)-(-)-nicotine in humans: formation of trans-(S)-(-)-nicotine N-1'-oxide. |journal=Chem. Res. Toxicol. |volume=6 |issue= 6 |pages= 880-8 |year= 1994 |pmid= 8117928 |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=Shephard EA, Dolphin CT, Fox MF, ''et al.'' |title=Localization of genes encoding three distinct flavin-containing monooxygenases to human chromosome 1q. |journal=Genomics |volume=16 |issue= 1 |pages= 85-9 |year= 1993 |pmid= 8486388 |doi= 10.1006/geno.1993.1144 }}
*{{cite journal | author=Dolphin CT, Cullingford TE, Shephard EA, ''et al.'' |title=Differential developmental and tissue-specific regulation of expression of the genes encoding three members of the flavin-containing monooxygenase family of man, FMO1, FMO3 and FM04. |journal=Eur. J. Biochem. |volume=235 |issue= 3 |pages= 683-9 |year= 1996 |pmid= 8654418 |doi= }}
*{{cite journal | author=Chung WG, Cha YN |title=Oxidation of caffeine to theobromine and theophylline is catalyzed primarily by flavin-containing monooxygenase in liver microsomes. |journal=Biochem. Biophys. Res. Commun. |volume=235 |issue= 3 |pages= 685-8 |year= 1997 |pmid= 9207220 |doi= 10.1006/bbrc.1997.6866 }}
*{{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=Dolphin CT, Janmohamed A, Smith RL, ''et al.'' |title=Missense mutation in flavin-containing mono-oxygenase 3 gene, FMO3, underlies fish-odour syndrome. |journal=Nat. Genet. |volume=17 |issue= 4 |pages= 491-4 |year= 1997 |pmid= 9398858 |doi= 10.1038/ng1297-491 }}
*{{cite journal | author=Dolphin CT, Riley JH, Smith RL, ''et al.'' |title=Structural organization of the human flavin-containing monooxygenase 3 gene (FMO3), the favored candidate for fish-odor syndrome, determined directly from genomic DNA. |journal=Genomics |volume=46 |issue= 2 |pages= 260-7 |year= 1998 |pmid= 9417913 |doi= 10.1006/geno.1997.5031 }}
*{{cite journal | author=Treacy EP, Akerman BR, Chow LM, ''et al.'' |title=Mutations of the flavin-containing monooxygenase gene (FMO3) cause trimethylaminuria, a defect in detoxication. |journal=Hum. Mol. Genet. |volume=7 |issue= 5 |pages= 839-45 |year= 1998 |pmid= 9536088 |doi= }}
*{{cite journal | author=Akerman BR, Forrest S, Chow L, ''et al.'' |title=Two novel mutations of the FMO3 gene in a proband with trimethylaminuria. |journal=Hum. Mutat. |volume=13 |issue= 5 |pages= 376-9 |year= 1999 |pmid= 10338091 |doi= 10.1002/(SICI)1098-1004(1999)13:5<376::AID-HUMU5>3.0.CO;2-A }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GGCX... {November 18, 2007 12:36:09 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 12:37:04 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Gamma-glutamyl carboxylase
| HGNCid = 4247
| Symbol = GGCX
| AltSymbols =; FLJ26629; VKCFD1
| OMIM = 137167
| ECnumber =
| Homologene = 639
| MGIid = 1927655
| GeneAtlas_image1 = PBB_GE_GGCX_205351_at_tn.png
| GeneAtlas_image2 = PBB_GE_GGCX_214006_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008488 |text = gamma-glutamyl carboxylase activity}} {{GNF_GO|id=GO:0016874 |text = ligase activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006464 |text = protein modification process}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}} {{GNF_GO|id=GO:0017187 |text = peptidyl-glutamic acid carboxylation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2677
| Hs_Ensembl = ENSG00000115486
| Hs_RefseqProtein = NP_000812
| Hs_RefseqmRNA = NM_000821
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 85629718
| Hs_GenLoc_end = 85642090
| Hs_Uniprot = P38435
| Mm_EntrezGene = 56316
| Mm_Ensembl = ENSMUSG00000053460
| Mm_RefseqmRNA = NM_019802
| Mm_RefseqProtein = NP_062776
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 72343843
| Mm_GenLoc_end = 72360221
| Mm_Uniprot = Q3TME3
}}
}}
'''Gamma-glutamyl carboxylase''', also known as '''GGCX''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GGCX gamma-glutamyl carboxylase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2677| 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=Zhang L, Jhingan A, Castellino FJ |title=Role of individual gamma-carboxyglutamic acid residues of activated human protein C in defining its in vitro anticoagulant activity. |journal=Blood |volume=80 |issue= 4 |pages= 942-52 |year= 1992 |pmid= 1498334 |doi= }}
*{{cite journal | author=Wu SM, Cheung WF, Frazier D, Stafford DW |title=Cloning and expression of the cDNA for human gamma-glutamyl carboxylase. |journal=Science |volume=254 |issue= 5038 |pages= 1634-6 |year= 1992 |pmid= 1749935 |doi= }}
*{{cite journal | author=Brenner B, Tavori S, Zivelin A, ''et al.'' |title=Hereditary deficiency of all vitamin K-dependent procoagulants and anticoagulants. |journal=Br. J. Haematol. |volume=75 |issue= 4 |pages= 537-42 |year= 1990 |pmid= 2145029 |doi= }}
*{{cite journal | author=Borowski M, Furie BC, Furie B |title=Distribution of gamma-carboxyglutamic acid residues in partially carboxylated human prothrombins. |journal=J. Biol. Chem. |volume=261 |issue= 4 |pages= 1624-8 |year= 1986 |pmid= 3944102 |doi= }}
*{{cite journal | author=Kuo WL, Stafford DW, Cruces J, ''et al.'' |title=Chromosomal localization of the gamma-glutamyl carboxylase gene at 2p12. |journal=Genomics |volume=25 |issue= 3 |pages= 746-8 |year= 1995 |pmid= 7759116 |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=Persson E, Nielsen LS |title=Site-directed mutagenesis but not gamma-carboxylation of Glu-35 in factor VIIa affects the association with tissue factor. |journal=FEBS Lett. |volume=385 |issue= 3 |pages= 241-3 |year= 1996 |pmid= 8647260 |doi= }}
*{{cite journal | author=Liu Y, Nelson AN, Lipsky JJ |title=Vitamin K-dependent carboxylase: mRNA distribution and effects of vitamin K-deficiency and warfarin treatment. |journal=Biochem. Biophys. Res. Commun. |volume=224 |issue= 2 |pages= 549-54 |year= 1996 |pmid= 8702425 |doi= 10.1006/bbrc.1996.1063 }}
*{{cite journal | author=Wu SM, Stafford DW, Frazier LD, ''et al.'' |title=Genomic sequence and transcription start site for the human gamma-glutamyl carboxylase. |journal=Blood |volume=89 |issue= 11 |pages= 4058-62 |year= 1997 |pmid= 9166845 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Larson PJ, Camire RM, Wong D, ''et al.'' |title=Structure/function analyses of recombinant variants of human factor Xa: factor Xa incorporation into prothrombinase on the thrombin-activated platelet surface is not mimicked by synthetic phospholipid vesicles. |journal=Biochemistry |volume=37 |issue= 14 |pages= 5029-38 |year= 1998 |pmid= 9538022 |doi= 10.1021/bi972428p }}
*{{cite journal | author=Brenner B, Sánchez-Vega B, Wu SM, ''et al.'' |title=A missense mutation in gamma-glutamyl carboxylase gene causes combined deficiency of all vitamin K-dependent blood coagulation factors. |journal=Blood |volume=92 |issue= 12 |pages= 4554-9 |year= 1999 |pmid= 9845520 |doi= }}
*{{cite journal | author=Houben RJ, Jin D, Stafford DW, ''et al.'' |title=Osteocalcin binds tightly to the gamma-glutamylcarboxylase at a site distinct from that of the other known vitamin K-dependent proteins. |journal=Biochem. J. |volume=341 ( Pt 2) |issue= |pages= 265-9 |year= 1999 |pmid= 10393081 |doi= }}
*{{cite journal | author=Uehara S, Gotoh K, Handa H, ''et al.'' |title=Process of carboxylation of glutamic acid residues in the gla domain of human des-gamma-carboxyprothrombin. |journal=Clin. Chim. Acta |volume=289 |issue= 1-2 |pages= 33-44 |year= 2000 |pmid= 10556651 |doi= }}
*{{cite journal | author=Tie J, Wu SM, Jin D, ''et al.'' |title=A topological study of the human gamma-glutamyl carboxylase. |journal=Blood |volume=96 |issue= 3 |pages= 973-8 |year= 2000 |pmid= 10910912 |doi= }}
*{{cite journal | author=Mutucumarana VP, Stafford DW, Stanley TB, ''et al.'' |title=Expression and characterization of the naturally occurring mutation L394R in human gamma-glutamyl carboxylase. |journal=J. Biol. Chem. |volume=275 |issue= 42 |pages= 32572-7 |year= 2000 |pmid= 10934213 |doi= 10.1074/jbc.M006808200 }}
*{{cite journal | author=Spronk HM, Farah RA, Buchanan GR, ''et al.'' |title=Novel mutation in the gamma-glutamyl carboxylase gene resulting in congenital combined deficiency of all vitamin K-dependent blood coagulation factors. |journal=Blood |volume=96 |issue= 10 |pages= 3650-2 |year= 2001 |pmid= 11071668 |doi= }}
*{{cite journal | author=Pudota BN, Miyagi M, Hallgren KW, ''et al.'' |title=Identification of the vitamin K-dependent carboxylase active site: Cys-99 and Cys-450 are required for both epoxidation and carboxylation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 24 |pages= 13033-8 |year= 2001 |pmid= 11087858 |doi= 10.1073/pnas.97.24.13033 }}
*{{cite journal | author=Arruda VR, Hagstrom JN, Deitch J, ''et al.'' |title=Posttranslational modifications of recombinant myotube-synthesized human factor IX. |journal=Blood |volume=97 |issue= 1 |pages= 130-8 |year= 2001 |pmid= 11133752 |doi= }}
*{{cite journal | author=Presnell SR, Tripathy A, Lentz BR, ''et al.'' |title=A novel fluorescence assay to study propeptide interaction with gamma-glutamyl carboxylase. |journal=Biochemistry |volume=40 |issue= 39 |pages= 11723-33 |year= 2001 |pmid= 11570873 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KLF4... {November 18, 2007 12:43:23 PM PST}
- SEARCH REDIRECT: Control Box Found: KLF4 {November 18, 2007 12:44:20 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 12:44:27 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 12:44:27 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 12:44:27 PM PST}
- UPDATED: Updated protein page: KLF4 {November 18, 2007 12:44:40 PM PST}
- INFO: Beginning work on KRIT1... {November 18, 2007 12:23:49 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 12:25:19 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
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| 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 = KRIT1, ankyrin repeat containing
| HGNCid = 1573
| Symbol = KRIT1
| AltSymbols =; CAM; CCM1
| OMIM = 604214
| ECnumber =
| Homologene = 12746
| MGIid = 1930618
| GeneAtlas_image1 = PBB_GE_KRIT1_216713_at_tn.png
| Function = {{GNF_GO|id=GO:0005083 |text = small GTPase regulator activity}} {{GNF_GO|id=GO:0005488 |text = binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}}
| Process = {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 889
| Hs_Ensembl = ENSG00000001631
| Hs_RefseqProtein = NP_001013424
| Hs_RefseqmRNA = NM_001013406
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 91666219
| Hs_GenLoc_end = 91713350
| Hs_Uniprot = O00522
| Mm_EntrezGene = 79264
| Mm_Ensembl = ENSMUSG00000000600
| Mm_RefseqmRNA = NM_030675
| Mm_RefseqProtein = NP_109600
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 3809195
| Mm_GenLoc_end = 3847363
| Mm_Uniprot = Q5U463
}}
}}
'''KRIT1, ankyrin repeat containing''', also known as '''KRIT1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KRIT1 KRIT1, ankyrin repeat containing| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=889| 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=Verlaan DJ, Davenport WJ, Stefan H, ''et al.'' |title=Cerebral cavernous malformations: mutations in Krit1. |journal=Neurology |volume=58 |issue= 6 |pages= 853-7 |year= 2002 |pmid= 11914398 |doi= }}
*{{cite journal | author=Günel M, Awad IA, Anson J, Lifton RP |title=Mapping a gene causing cerebral cavernous malformation to 7q11.2-q21. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 14 |pages= 6620-4 |year= 1995 |pmid= 7604043 |doi= }}
*{{cite journal | author=Marchuk DA, Gallione CJ, Morrison LA, ''et al.'' |title=A locus for cerebral cavernous malformations maps to chromosome 7q in two families. |journal=Genomics |volume=28 |issue= 2 |pages= 311-4 |year= 1996 |pmid= 8530042 |doi= }}
*{{cite journal | author=Serebriiskii I, Estojak J, Sonoda G, ''et al.'' |title=Association of Krev-1/rap1a with Krit1, a novel ankyrin repeat-containing protein encoded by a gene mapping to 7q21-22. |journal=Oncogene |volume=15 |issue= 9 |pages= 1043-9 |year= 1997 |pmid= 9285558 |doi= 10.1038/sj.onc.1201268 }}
*{{cite journal | author=Deloulme JC, Prichard L, Delattre O, Storm DR |title=The prooncoprotein EWS binds calmodulin and is phosphorylated by protein kinase C through an IQ domain. |journal=J. Biol. Chem. |volume=272 |issue= 43 |pages= 27369-77 |year= 1997 |pmid= 9341188 |doi= }}
*{{cite journal | author=Laberge-le Couteulx S, Jung HH, Labauge P, ''et al.'' |title=Truncating mutations in CCM1, encoding KRIT1, cause hereditary cavernous angiomas. |journal=Nat. Genet. |volume=23 |issue= 2 |pages= 189-93 |year= 1999 |pmid= 10508515 |doi= 10.1038/13815 }}
*{{cite journal | author=Sahoo T, Johnson EW, Thomas JW, ''et al.'' |title=Mutations in the gene encoding KRIT1, a Krev-1/rap1a binding protein, cause cerebral cavernous malformations (CCM1). |journal=Hum. Mol. Genet. |volume=8 |issue= 12 |pages= 2325-33 |year= 1999 |pmid= 10545614 |doi= }}
*{{cite journal | author=Eerola I, Plate KH, Spiegel R, ''et al.'' |title=KRIT1 is mutated in hyperkeratotic cutaneous capillary-venous malformation associated with cerebral capillary malformation. |journal=Hum. Mol. Genet. |volume=9 |issue= 9 |pages= 1351-5 |year= 2000 |pmid= 10814716 |doi= }}
*{{cite journal | author=Zhang J, Clatterbuck RE, Rigamonti D, Dietz HC |title=Cloning of the murine Krit1 cDNA reveals novel mammalian 5' coding exons. |journal=Genomics |volume=70 |issue= 3 |pages= 392-5 |year= 2001 |pmid= 11161791 |doi= 10.1006/geno.2000.6410 }}
*{{cite journal | author=Sahoo T, Goenaga-Diaz E, Serebriiskii IG, ''et al.'' |title=Computational and experimental analyses reveal previously undetected coding exons of the KRIT1 (CCM1) gene. |journal=Genomics |volume=71 |issue= 1 |pages= 123-6 |year= 2001 |pmid= 11161805 |doi= 10.1006/geno.2000.6426 }}
*{{cite journal | author=Eerola I, McIntyre B, Vikkula M |title=Identification of eight novel 5'-exons in cerebral capillary malformation gene-1 (CCM1) encoding KRIT1. |journal=Biochim. Biophys. Acta |volume=1517 |issue= 3 |pages= 464-7 |year= 2001 |pmid= 11342228 |doi= }}
*{{cite journal | author=Zhang J, Clatterbuck RE, Rigamonti D, ''et al.'' |title=Interaction between krit1 and icap1alpha infers perturbation of integrin beta1-mediated angiogenesis in the pathogenesis of cerebral cavernous malformation. |journal=Hum. Mol. Genet. |volume=10 |issue= 25 |pages= 2953-60 |year= 2002 |pmid= 11741838 |doi= }}
*{{cite journal | author=Couteulx SL, Brézin AP, Fontaine B, ''et al.'' |title=A novel KRIT1/CCM1 truncating mutation in a patient with cerebral and retinal cavernous angiomas. |journal=Arch. Ophthalmol. |volume=120 |issue= 2 |pages= 217-8 |year= 2002 |pmid= 11831930 |doi= }}
*{{cite journal | author=Zawistowski JS, Serebriiskii IG, Lee MF, ''et al.'' |title=KRIT1 association with the integrin-binding protein ICAP-1: a new direction in the elucidation of cerebral cavernous malformations (CCM1) pathogenesis. |journal=Hum. Mol. Genet. |volume=11 |issue= 4 |pages= 389-96 |year= 2002 |pmid= 11854171 |doi= }}
*{{cite journal | author=Verlaan DJ, Siegel AM, Rouleau GA |title=Krit1 missense mutations lead to splicing errors in cerebral cavernous malformation. |journal=Am. J. Hum. Genet. |volume=70 |issue= 6 |pages= 1564-7 |year= 2002 |pmid= 11941540 |doi= }}
*{{cite journal | author=Gunel M, Laurans MS, Shin D, ''et al.'' |title=KRIT1, a gene mutated in cerebral cavernous malformation, encodes a microtubule-associated protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 16 |pages= 10677-82 |year= 2002 |pmid= 12140362 |doi= 10.1073/pnas.122354499 }}
*{{cite journal | author=Kehrer-Sawatzki H, Wilda M, Braun VM, ''et al.'' |title=Mutation and expression analysis of the KRIT1 gene associated with cerebral cavernous malformations (CCM1). |journal=Acta Neuropathol. |volume=104 |issue= 3 |pages= 231-40 |year= 2002 |pmid= 12172908 |doi= 10.1007/s00401-002-0552-6 }}
*{{cite journal | author=Denier C, Gasc JM, Chapon F, ''et al.'' |title=Krit1/cerebral cavernous malformation 1 mRNA is preferentially expressed in neurons and epithelial cells in embryo and adult. |journal=Mech. Dev. |volume=117 |issue= 1-2 |pages= 363-7 |year= 2003 |pmid= 12204286 |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 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NR1I3... {November 18, 2007 12:44:41 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 12:45:34 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_NR1I3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1xv9.
| PDB = {{PDB2|1xv9}}, {{PDB2|1xvp}}
| Name = Nuclear receptor subfamily 1, group I, member 3
| HGNCid = 7969
| Symbol = NR1I3
| AltSymbols =; CAR; CAR1; MB67; MGC150433; MGC97144; MGC97209
| OMIM = 603881
| ECnumber =
| Homologene = 3759
| MGIid = 1346307
| GeneAtlas_image1 = PBB_GE_NR1I3_207007_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003707 |text = steroid hormone receptor activity}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004879 |text = ligand-dependent nuclear receptor activity}} {{GNF_GO|id=GO:0004882 |text = androgen receptor activity}} {{GNF_GO|id=GO:0004887 |text = thyroid hormone receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0016481 |text = negative regulation of transcription}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 9970
| Hs_Ensembl = ENSG00000143257
| Hs_RefseqProtein = NP_001070937
| Hs_RefseqmRNA = NM_001077469
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 159466079
| Hs_GenLoc_end = 159474590
| Hs_Uniprot = Q14994
| Mm_EntrezGene = 12355
| Mm_Ensembl = ENSMUSG00000005677
| Mm_RefseqmRNA = NM_009803
| Mm_RefseqProtein = NP_033933
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 173050645
| Mm_GenLoc_end = 173055519
| Mm_Uniprot = Q3UEP1
}}
}}
'''Nuclear receptor subfamily 1, group I, member 3''', also known as '''NR1I3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NR1I3 nuclear receptor subfamily 1, group I, member 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9970| 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 nuclear receptor superfamily, and is a key regulator of xenobiotic and endobiotic metabolism. The protein binds to DNA as a monomer or a heterodimer with the retinoid X receptor and regulates the transcription of target genes involved in drug metabolism and bilirubin clearance, such as cytochrome P450 family members. Unlike most nuclear receptors, this transcriptional regulator is constitutively active in the absence of ligand but is regulated by both agonists and inverse agonists. Ligand binding results in translocation of this protein to the nucleus, where it activates or represses target gene transcription. These ligands include bilirubin, a variety of foreign compounds, steroid hormones, and prescription drugs. Multiple transcript variants encoding different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: NR1I3 nuclear receptor subfamily 1, group I, member 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9970| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Masuno M, Shimozawa N, Suzuki Y, ''et al.'' |title=Assignment of the human peroxisome assembly factor-1 gene (PXMP3) responsible for Zellweger syndrome to chromosome 8q21.1 by fluorescence in situ hybridization. |journal=Genomics |volume=20 |issue= 1 |pages= 141-2 |year= 1994 |pmid= 8020947 |doi= 10.1006/geno.1994.1144 }}
*{{cite journal | author=Baes M, Gulick T, Choi HS, ''et al.'' |title=A new orphan member of the nuclear hormone receptor superfamily that interacts with a subset of retinoic acid response elements. |journal=Mol. Cell. Biol. |volume=14 |issue= 3 |pages= 1544-52 |year= 1994 |pmid= 8114692 |doi= }}
*{{cite journal | author=Choi HS, Seol W, Moore DD |title=A component of the 26S proteasome binds on orphan member of the nuclear hormone receptor superfamily. |journal=J. Steroid Biochem. Mol. Biol. |volume=56 |issue= 1-6 Spec No |pages= 23-30 |year= 1996 |pmid= 8603043 |doi= }}
*{{cite journal | author=Seol W, Choi HS, Moore DD |title=An orphan nuclear hormone receptor that lacks a DNA binding domain and heterodimerizes with other receptors. |journal=Science |volume=272 |issue= 5266 |pages= 1336-9 |year= 1996 |pmid= 8650544 |doi= }}
*{{cite journal | author=Choi HS, Chung M, Tzameli I, ''et al.'' |title=Differential transactivation by two isoforms of the orphan nuclear hormone receptor CAR. |journal=J. Biol. Chem. |volume=272 |issue= 38 |pages= 23565-71 |year= 1997 |pmid= 9295294 |doi= }}
*{{cite journal | author=Seol W, Hanstein B, Brown M, Moore DD |title=Inhibition of estrogen receptor action by the orphan receptor SHP (short heterodimer partner). |journal=Mol. Endocrinol. |volume=12 |issue= 10 |pages= 1551-7 |year= 1998 |pmid= 9773978 |doi= }}
*{{cite journal | author=Forman BM, Tzameli I, Choi HS, ''et al.'' |title=Androstane metabolites bind to and deactivate the nuclear receptor CAR-beta. |journal=Nature |volume=395 |issue= 6702 |pages= 612-5 |year= 1998 |pmid= 9783588 |doi= 10.1038/26996 }}
*{{cite journal | author=Gonzalez MM, Carlberg C |title=Cross-repression, a functional consequence of the physical interaction of non-liganded nuclear receptors and POU domain transcription factors. |journal=J. Biol. Chem. |volume=277 |issue= 21 |pages= 18501-9 |year= 2002 |pmid= 11891224 |doi= 10.1074/jbc.M200205200 }}
*{{cite journal | author=Min G, Kim H, Bae Y, ''et al.'' |title=Inhibitory cross-talk between estrogen receptor (ER) and constitutively activated androstane receptor (CAR). CAR inhibits ER-mediated signaling pathway by squelching p160 coactivators. |journal=J. Biol. Chem. |volume=277 |issue= 37 |pages= 34626-33 |year= 2002 |pmid= 12114525 |doi= 10.1074/jbc.M205239200 }}
*{{cite journal | author=Goodwin B, Hodgson E, D'Costa DJ, ''et al.'' |title=Transcriptional regulation of the human CYP3A4 gene by the constitutive androstane receptor. |journal=Mol. Pharmacol. |volume=62 |issue= 2 |pages= 359-65 |year= 2002 |pmid= 12130689 |doi= }}
*{{cite journal | author=Ferguson SS, LeCluyse EL, Negishi M, Goldstein JA |title=Regulation of human CYP2C9 by the constitutive androstane receptor: discovery of a new distal binding site. |journal=Mol. Pharmacol. |volume=62 |issue= 3 |pages= 737-46 |year= 2002 |pmid= 12181452 |doi= }}
*{{cite journal | author=Zhang J, Huang W, Chua SS, ''et al.'' |title=Modulation of acetaminophen-induced hepatotoxicity by the xenobiotic receptor CAR. |journal=Science |volume=298 |issue= 5592 |pages= 422-4 |year= 2002 |pmid= 12376703 |doi= 10.1126/science.1073502 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Chang TK, Bandiera SM, Chen J |title=Constitutive androstane receptor and pregnane X receptor gene expression in human liver: interindividual variability and correlation with CYP2B6 mRNA levels. |journal=Drug Metab. Dispos. |volume=31 |issue= 1 |pages= 7-10 |year= 2003 |pmid= 12485946 |doi= }}
*{{cite journal | author=Pascussi JM, Busson-Le Coniat M, Maurel P, Vilarem MJ |title=Transcriptional analysis of the orphan nuclear receptor constitutive androstane receptor (NR1I3) gene promoter: identification of a distal glucocorticoid response element. |journal=Mol. Endocrinol. |volume=17 |issue= 1 |pages= 42-55 |year= 2003 |pmid= 12511605 |doi= }}
*{{cite journal | author=Shiraki T, Sakai N, Kanaya E, Jingami H |title=Activation of orphan nuclear constitutive androstane receptor requires subnuclear targeting by peroxisome proliferator-activated receptor gamma coactivator-1 alpha. A possible link between xenobiotic response and nutritional state. |journal=J. Biol. Chem. |volume=278 |issue= 13 |pages= 11344-50 |year= 2003 |pmid= 12551939 |doi= 10.1074/jbc.M212859200 }}
*{{cite journal | author=Maglich JM, Parks DJ, Moore LB, ''et al.'' |title=Identification of a novel human constitutive androstane receptor (CAR) agonist and its use in the identification of CAR target genes. |journal=J. Biol. Chem. |volume=278 |issue= 19 |pages= 17277-83 |year= 2003 |pmid= 12611900 |doi= 10.1074/jbc.M300138200 }}
*{{cite journal | author=Xie W, Yeuh MF, Radominska-Pandya A, ''et al.'' |title=Control of steroid, heme, and carcinogen metabolism by nuclear pregnane X receptor and constitutive androstane receptor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 7 |pages= 4150-5 |year= 2003 |pmid= 12644700 |doi= 10.1073/pnas.0438010100 }}
*{{cite journal | author=Huang W, Zhang J, Chua SS, ''et al.'' |title=Induction of bilirubin clearance by the constitutive androstane receptor (CAR). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 7 |pages= 4156-61 |year= 2003 |pmid= 12644704 |doi= 10.1073/pnas.0630614100 }}
*{{cite journal | author=Auerbach SS, Ramsden R, Stoner MA, ''et al.'' |title=Alternatively spliced isoforms of the human constitutive androstane receptor. |journal=Nucleic Acids Res. |volume=31 |issue= 12 |pages= 3194-207 |year= 2003 |pmid= 12799447 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RAB11A... {November 18, 2007 12:41:39 PM PST}
- SEARCH: Multiple Conflicting Pages. Need Resolution. {November 18, 2007 12:42:24 PM PST}
- AMBIGUITY: More than one potential page found for updating, RAB11A RAB11A {November 18, 2007 12:42:24 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_RAB11A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1oiv.
| PDB = {{PDB2|1oiv}}, {{PDB2|1oiw}}, {{PDB2|1oix}}, {{PDB2|1yzk}}, {{PDB2|2d7c}}, {{PDB2|2f9l}}, {{PDB2|2f9m}}, {{PDB2|2gzd}}, {{PDB2|2gzh}}, {{PDB2|2hv8}}
| Name = RAB11A, member RAS oncogene family
| HGNCid = 9760
| Symbol = RAB11A
| AltSymbols =; MGC1490; YL8
| OMIM = 605570
| ECnumber =
| Homologene = 37903
| MGIid = 1858202
| GeneAtlas_image1 = PBB_GE_RAB11A_200863_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_RAB11A_200864_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}} {{GNF_GO|id=GO:0019905 |text = syntaxin binding}}
| Component = {{GNF_GO|id=GO:0005802 |text = trans-Golgi network}}
| Process = {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}} {{GNF_GO|id=GO:0015031 |text = protein transport}} {{GNF_GO|id=GO:0048227 |text = plasma membrane to endosome transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8766
| Hs_Ensembl = ENSG00000103769
| Hs_RefseqProtein = NP_004654
| Hs_RefseqmRNA = NM_004663
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 63948850
| Hs_GenLoc_end = 63968846
| Hs_Uniprot = P62491
| Mm_EntrezGene = 53869
| Mm_Ensembl = ENSMUSG00000004771
| Mm_RefseqmRNA = NM_017382
| Mm_RefseqProtein = NP_059078
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 64513391
| Mm_GenLoc_end = 64535665
| Mm_Uniprot = P97345
}}
}}
'''RAB11A, member RAS oncogene family''', also known as '''RAB11A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RAB11A RAB11A, member RAS oncogene family| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8766| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene belongs to the small GTPase superfamily, Rab family. It is associated with both constitutive and regulated secretory pathways, and may be involved in protein transport.<ref name="entrez">{{cite web | title = Entrez Gene: RAB11A RAB11A, member RAS oncogene family| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8766| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Drivas GT, Shih A, Coutavas EE, ''et al.'' |title=Identification and characterization of a human homolog of the Schizosaccharomyces pombe ras-like gene YPT-3. |journal=Oncogene |volume=6 |issue= 1 |pages= 3-9 |year= 1991 |pmid= 1704119 |doi= }}
*{{cite journal | author=Sakurada K, Uchida K, Yamaguchi K, ''et al.'' |title=Molecular cloning and characterization of a ras p21-like GTP-binding protein (24KG) from rat liver. |journal=Biochem. Biophys. Res. Commun. |volume=177 |issue= 3 |pages= 1224-32 |year= 1991 |pmid= 1711847 |doi= }}
*{{cite journal | author=Gromov PS, Celis JE, Hansen C, ''et al.'' |title=Human rab11a: transcription, chromosome mapping and effect on the expression levels of host GTP-binding proteins. |journal=FEBS Lett. |volume=429 |issue= 3 |pages= 359-64 |year= 1998 |pmid= 9662449 |doi= }}
*{{cite journal | author=Gromov P, Celis JE |title=Rab11a is modified in vivo by isoprenoid geranylgeranyl. |journal=Electrophoresis |volume=19 |issue= 10 |pages= 1803-7 |year= 1998 |pmid= 9719562 |doi= 10.1002/elps.1150191043 }}
*{{cite journal | author=Zeng J, Ren M, Gravotta D, ''et al.'' |title=Identification of a putative effector protein for rab11 that participates in transferrin recycling. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 6 |pages= 2840-5 |year= 1999 |pmid= 10077598 |doi= }}
*{{cite journal | author=Dumanchin C, Czech C, Campion D, ''et al.'' |title=Presenilins interact with Rab11, a small GTPase involved in the regulation of vesicular transport. |journal=Hum. Mol. Genet. |volume=8 |issue= 7 |pages= 1263-9 |year= 1999 |pmid= 10369872 |doi= }}
*{{cite journal | author=Mammoto A, Ohtsuka T, Hotta I, ''et al.'' |title=Rab11BP/Rabphilin-11, a downstream target of rab11 small G protein implicated in vesicle recycling. |journal=J. Biol. Chem. |volume=274 |issue= 36 |pages= 25517-24 |year= 1999 |pmid= 10464283 |doi= }}
*{{cite journal | author=Shisheva A, Chinni SR, DeMarco C |title=General role of GDP dissociation inhibitor 2 in membrane release of Rab proteins: modulations of its functional interactions by in vitro and in vivo structural modifications. |journal=Biochemistry |volume=38 |issue= 36 |pages= 11711-21 |year= 1999 |pmid= 10512627 |doi= }}
*{{cite journal | author=Prekeris R, Klumperman J, Scheller RH |title=A Rab11/Rip11 protein complex regulates apical membrane trafficking via recycling endosomes. |journal=Mol. Cell |volume=6 |issue= 6 |pages= 1437-48 |year= 2001 |pmid= 11163216 |doi= }}
*{{cite journal | author=Lapierre LA, Kumar R, Hales CM, ''et al.'' |title=Myosin vb is associated with plasma membrane recycling systems. |journal=Mol. Biol. Cell |volume=12 |issue= 6 |pages= 1843-57 |year= 2001 |pmid= 11408590 |doi= }}
*{{cite journal | author=Prekeris R, Davies JM, Scheller RH |title=Identification of a novel Rab11/25 binding domain present in Eferin and Rip proteins. |journal=J. Biol. Chem. |volume=276 |issue= 42 |pages= 38966-70 |year= 2001 |pmid= 11481332 |doi= 10.1074/jbc.M106133200 }}
*{{cite journal | author=Hales CM, Griner R, Hobdy-Henderson KC, ''et al.'' |title=Identification and characterization of a family of Rab11-interacting proteins. |journal=J. Biol. Chem. |volume=276 |issue= 42 |pages= 39067-75 |year= 2001 |pmid= 11495908 |doi= 10.1074/jbc.M104831200 }}
*{{cite journal | author=Lindsay AJ, Hendrick AG, Cantalupo G, ''et al.'' |title=Rab coupling protein (RCP), a novel Rab4 and Rab11 effector protein. |journal=J. Biol. Chem. |volume=277 |issue= 14 |pages= 12190-9 |year= 2002 |pmid= 11786538 |doi= 10.1074/jbc.M108665200 }}
*{{cite journal | author=Lindsay AJ, McCaffrey MW |title=Rab11-FIP2 functions in transferrin recycling and associates with endosomal membranes via its COOH-terminal domain. |journal=J. Biol. Chem. |volume=277 |issue= 30 |pages= 27193-9 |year= 2002 |pmid= 11994279 |doi= 10.1074/jbc.M200757200 }}
*{{cite journal | author=Scales SJ, Hesser BA, Masuda ES, Scheller RH |title=Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex assembly. |journal=J. Biol. Chem. |volume=277 |issue= 31 |pages= 28271-9 |year= 2002 |pmid= 12145319 |doi= 10.1074/jbc.M204929200 }}
*{{cite journal | author=Band AM, Ali H, Vartiainen MK, ''et al.'' |title=Endogenous plasma membrane t-SNARE syntaxin 4 is present in rab11 positive endosomal membranes and associates with cortical actin cytoskeleton. |journal=FEBS Lett. |volume=531 |issue= 3 |pages= 513-9 |year= 2002 |pmid= 12435603 |doi= }}
*{{cite journal | author=Wallace DM, Lindsay AJ, Hendrick AG, McCaffrey MW |title=Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its overexpression condenses the Rab11 positive compartment in HeLa cells. |journal=Biochem. Biophys. Res. Commun. |volume=299 |issue= 5 |pages= 770-9 |year= 2003 |pmid= 12470645 |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=Roosterman D, Schmidlin F, Bunnett NW |title=Rab5a and rab11a mediate agonist-induced trafficking of protease-activated receptor 2. |journal=Am. J. Physiol., Cell Physiol. |volume=284 |issue= 5 |pages= C1319-29 |year= 2003 |pmid= 12540381 |doi= 10.1152/ajpcell.00540.2002 }}
*{{cite journal | author=Tani K, Shibata M, Kawase K, ''et al.'' |title=Mapping of functional domains of gamma-SNAP. |journal=J. Biol. Chem. |volume=278 |issue= 15 |pages= 13531-8 |year= 2003 |pmid= 12554740 |doi= 10.1074/jbc.M213205200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RPS6KA5... {November 18, 2007 12:42:24 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 12:43:23 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_RPS6KA5_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1vzo.
| PDB = {{PDB2|1vzo}}
| Name = Ribosomal protein S6 kinase, 90kDa, polypeptide 5
| HGNCid = 10434
| Symbol = RPS6KA5
| AltSymbols =; MGC1911; MSK1; MSPK1; RLPK
| OMIM = 603607
| ECnumber =
| Homologene = 48302
| MGIid = 1920336
| GeneAtlas_image1 = PBB_GE_RPS6KA5_204635_at_tn.png
| GeneAtlas_image2 = PBB_GE_RPS6KA5_204633_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0003824 |text = catalytic activity}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008237 |text = metallopeptidase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006950 |text = response to stress}} {{GNF_GO|id=GO:0007173 |text = epidermal growth factor receptor signaling pathway}} {{GNF_GO|id=GO:0007243 |text = protein kinase cascade}} {{GNF_GO|id=GO:0009605 |text = response to external stimulus}} {{GNF_GO|id=GO:0016572 |text = histone phosphorylation}} {{GNF_GO|id=GO:0042221 |text = response to chemical stimulus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 9252
| Hs_Ensembl = ENSG00000100784
| Hs_RefseqProtein = NP_004746
| Hs_RefseqmRNA = NM_004755
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 90406925
| Hs_GenLoc_end = 90596746
| Hs_Uniprot = O75582
| Mm_EntrezGene = 73086
| Mm_Ensembl = ENSMUSG00000021180
| Mm_RefseqmRNA = NM_153587
| Mm_RefseqProtein = NP_705815
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 100950828
| Mm_GenLoc_end = 101126078
| Mm_Uniprot = Q8C050
}}
}}
'''Ribosomal protein S6 kinase, 90kDa, polypeptide 5''', also known as '''RPS6KA5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RPS6KA5 ribosomal protein S6 kinase, 90kDa, polypeptide 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9252| 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=Chung J, Uchida E, Grammer TC, Blenis J |title=STAT3 serine phosphorylation by ERK-dependent and -independent pathways negatively modulates its tyrosine phosphorylation. |journal=Mol. Cell. Biol. |volume=17 |issue= 11 |pages= 6508-16 |year= 1997 |pmid= 9343414 |doi= }}
*{{cite journal | author=Deak M, Clifton AD, Lucocq LM, Alessi DR |title=Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB. |journal=EMBO J. |volume=17 |issue= 15 |pages= 4426-41 |year= 1998 |pmid= 9687510 |doi= 10.1093/emboj/17.15.4426 }}
*{{cite journal | author=Jain N, Zhang T, Fong SL, ''et al.'' |title=Repression of Stat3 activity by activation of mitogen-activated protein kinase (MAPK). |journal=Oncogene |volume=17 |issue= 24 |pages= 3157-67 |year= 1999 |pmid= 9872331 |doi= 10.1038/sj.onc.1202238 }}
*{{cite journal | author=New L, Zhao M, Li Y, ''et al.'' |title=Cloning and characterization of RLPK, a novel RSK-related protein kinase. |journal=J. Biol. Chem. |volume=274 |issue= 2 |pages= 1026-32 |year= 1999 |pmid= 9873047 |doi= }}
*{{cite journal | author=Thomson S, Clayton AL, Hazzalin CA, ''et al.'' |title=The nucleosomal response associated with immediate-early gene induction is mediated via alternative MAP kinase cascades: MSK1 as a potential histone H3/HMG-14 kinase. |journal=EMBO J. |volume=18 |issue= 17 |pages= 4779-93 |year= 1999 |pmid= 10469656 |doi= 10.1093/emboj/18.17.4779 }}
*{{cite journal | author=Lim CP, Cao X |title=Serine phosphorylation and negative regulation of Stat3 by JNK. |journal=J. Biol. Chem. |volume=274 |issue= 43 |pages= 31055-61 |year= 1999 |pmid= 10521505 |doi= }}
*{{cite journal | author=Buck M, Poli V, van der Geer P, ''et al.'' |title=Phosphorylation of rat serine 105 or mouse threonine 217 in C/EBP beta is required for hepatocyte proliferation induced by TGF alpha. |journal=Mol. Cell |volume=4 |issue= 6 |pages= 1087-92 |year= 2000 |pmid= 10635333 |doi= }}
*{{cite journal | author=Jiang C, Yu L, Tu Q, ''et al.'' |title=Assignment of a member of the ribosomal protein S6 kinase family, RPS6KA5, to human chromosome 14q31-->q32.1 by radiation hybrid mapping. |journal=Cytogenet. Cell Genet. |volume=87 |issue= 3-4 |pages= 261-2 |year= 2000 |pmid= 10702687 |doi= }}
*{{cite journal | author=Lizcano JM, Morrice N, Cohen P |title=Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser155. |journal=Biochem. J. |volume=349 |issue= Pt 2 |pages= 547-57 |year= 2001 |pmid= 10880354 |doi= }}
*{{cite journal | author=Hefner Y, Borsch-Haubold AG, Murakami M, ''et al.'' |title=Serine 727 phosphorylation and activation of cytosolic phospholipase A2 by MNK1-related protein kinases. |journal=J. Biol. Chem. |volume=275 |issue= 48 |pages= 37542-51 |year= 2001 |pmid= 10978317 |doi= 10.1074/jbc.M003395200 }}
*{{cite journal | author=Arthur JS, Cohen P |title=MSK1 is required for CREB phosphorylation in response to mitogens in mouse embryonic stem cells. |journal=FEBS Lett. |volume=482 |issue= 1-2 |pages= 44-8 |year= 2000 |pmid= 11018520 |doi= }}
*{{cite journal | author=Sapkota GP, Kieloch A, Lizcano JM, ''et al.'' |title=Phosphorylation of the protein kinase mutated in Peutz-Jeghers cancer syndrome, LKB1/STK11, at Ser431 by p90(RSK) and cAMP-dependent protein kinase, but not its farnesylation at Cys(433), is essential for LKB1 to suppress cell vrowth. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 19469-82 |year= 2001 |pmid= 11297520 |doi= 10.1074/jbc.M009953200 }}
*{{cite journal | author=Deb A, Zamanian-Daryoush M, Xu Z, ''et al.'' |title=Protein kinase PKR is required for platelet-derived growth factor signaling of c-fos gene expression via Erks and Stat3. |journal=EMBO J. |volume=20 |issue= 10 |pages= 2487-96 |year= 2001 |pmid= 11350938 |doi= 10.1093/emboj/20.10.2487 }}
*{{cite journal | author=Liu G, Zhang Y, Bode AM, ''et al.'' |title=Phosphorylation of 4E-BP1 is mediated by the p38/MSK1 pathway in response to UVB irradiation. |journal=J. Biol. Chem. |volume=277 |issue= 11 |pages= 8810-6 |year= 2002 |pmid= 11777913 |doi= 10.1074/jbc.M110477200 }}
*{{cite journal | author=Wiggin GR, Soloaga A, Foster JM, ''et al.'' |title=MSK1 and MSK2 are required for the mitogen- and stress-induced phosphorylation of CREB and ATF1 in fibroblasts. |journal=Mol. Cell. Biol. |volume=22 |issue= 8 |pages= 2871-81 |year= 2002 |pmid= 11909979 |doi= }}
*{{cite journal | author=Markou T, Lazou A |title=Phosphorylation and activation of mitogen- and stress-activated protein kinase-1 in adult rat cardiac myocytes by G-protein-coupled receptor agonists requires both extracellular-signal-regulated kinase and p38 mitogen-activated protein kinase. |journal=Biochem. J. |volume=365 |issue= Pt 3 |pages= 757-63 |year= 2002 |pmid= 11994045 |doi= 10.1042/BJ20011828 }}
*{{cite journal | author=Toska K, Kleppe R, Armstrong CG, ''et al.'' |title=Regulation of tyrosine hydroxylase by stress-activated protein kinases. |journal=J. Neurochem. |volume=83 |issue= 4 |pages= 775-83 |year= 2002 |pmid= 12421349 |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=Janknecht R |title=Regulation of the ER81 transcription factor and its coactivators by mitogen- and stress-activated protein kinase 1 (MSK1). |journal=Oncogene |volume=22 |issue= 5 |pages= 746-55 |year= 2003 |pmid= 12569367 |doi= 10.1038/sj.onc.1206185 }}
*{{cite journal | author=Dolled-Filhart M, Camp RL, Kowalski DP, ''et al.'' |title=Tissue microarray analysis of signal transducers and activators of transcription 3 (Stat3) and phospho-Stat3 (Tyr705) in node-negative breast cancer shows nuclear localization is associated with a better prognosis. |journal=Clin. Cancer Res. |volume=9 |issue= 2 |pages= 594-600 |year= 2003 |pmid= 12576423 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SERPINH1... {November 18, 2007 12:22:45 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 12:23:49 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Serpin peptidase inhibitor, clade H (heat shock protein 47), member 1, (collagen binding protein 1)
| HGNCid = 1546
| Symbol = SERPINH1
| AltSymbols =; AsTP3; CBP1; CBP2; HSP47; PIG14; RA-A47; SERPINH2; gp46
| OMIM = 600943
| ECnumber =
| Homologene = 20331
| MGIid = 88283
| GeneAtlas_image1 = PBB_GE_SERPINH1_207714_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004867 |text = serine-type endopeptidase inhibitor activity}} {{GNF_GO|id=GO:0005518 |text = collagen binding}} {{GNF_GO|id=GO:0051082 |text = unfolded protein binding}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005793 |text = ER-Golgi intermediate compartment}}
| Process = {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0006986 |text = response to unfolded protein}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 871
| Hs_Ensembl = ENSG00000149257
| Hs_RefseqProtein = NP_001226
| Hs_RefseqmRNA = NM_001235
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 74955043
| Hs_GenLoc_end = 74961473
| Hs_Uniprot = P50454
| Mm_EntrezGene = 12406
| Mm_Ensembl = ENSMUSG00000070436
| Mm_RefseqmRNA = XM_988921
| Mm_RefseqProtein = XP_994015
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 99219453
| Mm_GenLoc_end = 99227197
| Mm_Uniprot = Q3TJK3
}}
}}
'''Serpin peptidase inhibitor, clade H (heat shock protein 47), member 1, (collagen binding protein 1)''', also known as '''SERPINH1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SERPINH1 serpin peptidase inhibitor, clade H (heat shock protein 47), member 1, (collagen binding protein 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=871| 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 serpin superfamily of serine proteinase inhibitors. Its expression is induced by heat shock. The protein localizes to the endoplasmic reticulum lumen and binds collagen; thus it is thought to be a molecular chaperone involved in the maturation of collagen molecules. Autoantibodies to this protein have been found in patients with rheumatoid arthritis.<ref name="entrez">{{cite web | title = Entrez Gene: SERPINH1 serpin peptidase inhibitor, clade H (heat shock protein 47), member 1, (collagen binding protein 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=871| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Razzaque MS, Taguchi T |title=The possible role of colligin/HSP47, a collagen-binding protein, in the pathogenesis of human and experimental fibrotic diseases. |journal=Histol. Histopathol. |volume=14 |issue= 4 |pages= 1199-212 |year= 1999 |pmid= 10506936 |doi= }}
*{{cite journal | author=Gettins PG |title=Serpin structure, mechanism, and function. |journal=Chem. Rev. |volume=102 |issue= 12 |pages= 4751-804 |year= 2003 |pmid= 12475206 |doi= }}
*{{cite journal | author=Clarke EP, Sanwal BD |title=Cloning of a human collagen-binding protein, and its homology with rat gp46, chick hsp47 and mouse J6 proteins. |journal=Biochim. Biophys. Acta |volume=1129 |issue= 2 |pages= 246-8 |year= 1992 |pmid= 1309665 |doi= }}
*{{cite journal | author=Ikegawa S, Sudo K, Okui K, Nakamura Y |title=Isolation, characterization and chromosomal assignment of human colligin-2 gene (CBP2). |journal=Cytogenet. Cell Genet. |volume=71 |issue= 2 |pages= 182-6 |year= 1995 |pmid= 7656593 |doi= }}
*{{cite journal | author=Ikegawa S, Nakamura Y |title=Structure of the gene encoding human colligin-2 (CBP2). |journal=Gene |volume=194 |issue= 2 |pages= 301-3 |year= 1997 |pmid= 9272875 |doi= }}
*{{cite journal | author=Bekri S, Adélaïde J, Merscher S, ''et al.'' |title=Detailed map of a region commonly amplified at 11q13-->q14 in human breast carcinoma. |journal=Cytogenet. Cell Genet. |volume=79 |issue= 1-2 |pages= 125-31 |year= 1998 |pmid= 9533029 |doi= }}
*{{cite journal | author=Hattori T, Fujisawa T, Sasaki K, ''et al.'' |title=Isolation and characterization of a rheumatoid arthritis-specific antigen (RA-A47) from a human chondrocytic cell line (HCS-2/8). |journal=Biochem. Biophys. Res. Commun. |volume=245 |issue= 3 |pages= 679-83 |year= 1998 |pmid= 9588174 |doi= 10.1006/bbrc.1998.8505 }}
*{{cite journal | author=Nagai N, Tetuya Y, Hosokawa N, Nagata K |title=The human genome has only one functional hsp47 gene (CBP2) and a pseudogene (pshsp47). |journal=Gene |volume=227 |issue= 2 |pages= 241-8 |year= 1999 |pmid= 10023073 |doi= }}
*{{cite journal | author=Hebert C, Norris K, Della Coletta R, ''et al.'' |title=Cell surface colligin/Hsp47 associates with tetraspanin protein CD9 in epidermoid carcinoma cell lines. |journal=J. Cell. Biochem. |volume=73 |issue= 2 |pages= 248-58 |year= 1999 |pmid= 10227388 |doi= }}
*{{cite journal | author=Koide T, Aso A, Yorihuzi T, Nagata K |title=Conformational requirements of collagenous peptides for recognition by the chaperone protein HSP47. |journal=J. Biol. Chem. |volume=275 |issue= 36 |pages= 27957-63 |year= 2000 |pmid= 10862616 |doi= 10.1074/jbc.M003026200 }}
*{{cite journal | author=Hattori T, Takahash K, Yutani Y, ''et al.'' |title=Rheumatoid arthritis-related antigen 47kDa (RA-A47) is a product of colligin-2 and acts as a human HSP47. |journal=J. Bone Miner. Metab. |volume=18 |issue= 6 |pages= 328-34 |year= 2001 |pmid= 11052465 |doi= }}
*{{cite journal | author=Pelletier G, Stefanovsky VY, Faubladier M, ''et al.'' |title=Competitive recruitment of CBP and Rb-HDAC regulates UBF acetylation and ribosomal transcription. |journal=Mol. Cell |volume=6 |issue= 5 |pages= 1059-66 |year= 2002 |pmid= 11106745 |doi= }}
*{{cite journal | author=Matsuda M, Koide T, Yorihuzi T, ''et al.'' |title=Molecular cloning of a novel ubiquitin-like protein, UBIN, that binds to ER targeting signal sequences. |journal=Biochem. Biophys. Res. Commun. |volume=280 |issue= 2 |pages= 535-40 |year= 2001 |pmid= 11162551 |doi= 10.1006/bbrc.2000.4149 }}
*{{cite journal | author=Zhou M, Nekhai S, Bharucha DC, ''et al.'' |title=TFIIH inhibits CDK9 phosphorylation during human immunodeficiency virus type 1 transcription. |journal=J. Biol. Chem. |volume=276 |issue= 48 |pages= 44633-40 |year= 2002 |pmid= 11572868 |doi= 10.1074/jbc.M107466200 }}
*{{cite journal | author=Song CZ, Keller K, Murata K, ''et al.'' |title=Functional interaction between coactivators CBP/p300, PCAF, and transcription factor FKLF2. |journal=J. Biol. Chem. |volume=277 |issue= 9 |pages= 7029-36 |year= 2002 |pmid= 11748222 |doi= 10.1074/jbc.M108826200 }}
*{{cite journal | author=Sasaki H, Sato T, Yamauchi N, ''et al.'' |title=Induction of heat shock protein 47 synthesis by TGF-beta and IL-1 beta via enhancement of the heat shock element binding activity of heat shock transcription factor 1. |journal=J. Immunol. |volume=168 |issue= 10 |pages= 5178-83 |year= 2002 |pmid= 11994473 |doi= }}
*{{cite journal | author=Razzaque MS, Ahmed AR |title=Collagens, collagen-binding heat shock protein 47 and transforming growth factor-beta 1 are induced in cicatricial pemphigoid: possible role(s) in dermal fibrosis. |journal=Cytokine |volume=17 |issue= 6 |pages= 311-6 |year= 2002 |pmid= 12061838 |doi= 10.1006/cyto.2002.1020 }}
*{{cite journal | author=Sato K, Yomogida K, Wada T, ''et al.'' |title=Type XXVI collagen, a new member of the collagen family, is specifically expressed in the testis and ovary. |journal=J. Biol. Chem. |volume=277 |issue= 40 |pages= 37678-84 |year= 2002 |pmid= 12145293 |doi= 10.1074/jbc.M205347200 }}
*{{cite journal | author=Rocnik EF, van der Veer E, Cao H, ''et al.'' |title=Functional linkage between the endoplasmic reticulum protein Hsp47 and procollagen expression in human vascular smooth muscle cells. |journal=J. Biol. Chem. |volume=277 |issue= 41 |pages= 38571-8 |year= 2002 |pmid= 12163502 |doi= 10.1074/jbc.M206689200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TEC... {November 18, 2007 12:37:59 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 12:38:46 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
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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_TEC_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1gl5.
| PDB = {{PDB2|1gl5}}
| Name = Tec protein tyrosine kinase
| HGNCid = 11719
| Symbol = TEC
| AltSymbols =; MGC126760; MGC126762; PSCTK4
| OMIM = 600583
| ECnumber =
| Homologene = 1302
| MGIid = 98662
| GeneAtlas_image1 = PBB_GE_TEC_206301_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004715 |text = non-membrane spanning protein tyrosine kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component =
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007243 |text = protein kinase cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7006
| Hs_Ensembl = ENSG00000135605
| Hs_RefseqProtein = NP_003206
| Hs_RefseqmRNA = NM_003215
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 47832557
| Hs_GenLoc_end = 47966638
| Hs_Uniprot = P42680
| Mm_EntrezGene = 21682
| Mm_Ensembl = ENSMUSG00000029217
| Mm_RefseqmRNA = NM_013689
| Mm_RefseqProtein = NP_038717
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 73034869
| Mm_GenLoc_end = 73147618
| Mm_Uniprot = Q3U436
}}
}}
'''Tec protein tyrosine kinase''', also known as '''TEC''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TEC tec protein tyrosine kinase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7006| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene belongs to the Tec family of non-receptor protein-tyrosine kinases containing a pleckstrin homology domain. Tec family kinases are involved in the intracellular signaling mechanisms of cytokine receptors, lymphocyte surface antigens, heterotrimeric G-protein coupled receptors, and integrin molecules. They are also key players in the regulation of the immune functions. Tec kinase is an integral component of T cell signaling and has a distinct role in T cell activation. This gene may be associated with myelodysplastic syndrome.<ref name="entrez">{{cite web | title = Entrez Gene: TEC tec protein tyrosine kinase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7006| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Mano H |title=Tec family of protein-tyrosine kinases: an overview of their structure and function. |journal=Cytokine Growth Factor Rev. |volume=10 |issue= 3-4 |pages= 267-80 |year= 2000 |pmid= 10647781 |doi= }}
*{{cite journal | author=Yang WC, Collette Y, Nunès JA, Olive D |title=Tec kinases: a family with multiple roles in immunity. |journal=Immunity |volume=12 |issue= 4 |pages= 373-82 |year= 2000 |pmid= 10795735 |doi= }}
*{{cite journal | author=Mano H, Ishikawa F, Nishida J, ''et al.'' |title=A novel protein-tyrosine kinase, tec, is preferentially expressed in liver. |journal=Oncogene |volume=5 |issue= 12 |pages= 1781-6 |year= 1991 |pmid= 2284097 |doi= }}
*{{cite journal | author=Tang B, Mano H, Yi T, Ihle JN |title=Tec kinase associates with c-kit and is tyrosine phosphorylated and activated following stem cell factor binding. |journal=Mol. Cell. Biol. |volume=14 |issue= 12 |pages= 8432-7 |year= 1994 |pmid= 7526158 |doi= }}
*{{cite journal | author=Machide M, Mano H, Todokoro K |title=Interleukin 3 and erythropoietin induce association of Vav with Tec kinase through Tec homology domain. |journal=Oncogene |volume=11 |issue= 4 |pages= 619-25 |year= 1995 |pmid= 7651724 |doi= }}
*{{cite journal | author=Sato K, Mano H, Ariyama T, ''et al.'' |title=Molecular cloning and analysis of the human Tec protein-tyrosine kinase. |journal=Leukemia |volume=8 |issue= 10 |pages= 1663-72 |year= 1994 |pmid= 7934162 |doi= }}
*{{cite journal | author=Mano H, Yamashita Y, Miyazato A, ''et al.'' |title=Tec protein-tyrosine kinase is an effector molecule of Lyn protein-tyrosine kinase. |journal=FASEB J. |volume=10 |issue= 5 |pages= 637-42 |year= 1996 |pmid= 8621063 |doi= }}
*{{cite journal | author=Rawlings DJ, Scharenberg AM, Park H, ''et al.'' |title=Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases. |journal=Science |volume=271 |issue= 5250 |pages= 822-5 |year= 1996 |pmid= 8629002 |doi= }}
*{{cite journal | author=Park H, Wahl MI, Afar DE, ''et al.'' |title=Regulation of Btk function by a major autophosphorylation site within the SH3 domain. |journal=Immunity |volume=4 |issue= 5 |pages= 515-25 |year= 1996 |pmid= 8630736 |doi= }}
*{{cite journal | author=Ohta Y, Haire RN, Amemiya CT, ''et al.'' |title=Human Txk: genomic organization, structure and contiguous physical linkage with the Tec gene. |journal=Oncogene |volume=12 |issue= 4 |pages= 937-42 |year= 1996 |pmid= 8632917 |doi= }}
*{{cite journal | author=Cory GO, MacCarthy-Morrogh L, Banin S, ''et al.'' |title=Evidence that the Wiskott-Aldrich syndrome protein may be involved in lymphoid cell signaling pathways. |journal=J. Immunol. |volume=157 |issue= 9 |pages= 3791-5 |year= 1996 |pmid= 8892607 |doi= }}
*{{cite journal | author=Takahashi-Tezuka M, Hibi M, Fujitani Y, ''et al.'' |title=Tec tyrosine kinase links the cytokine receptors to PI-3 kinase probably through JAK. |journal=Oncogene |volume=14 |issue= 19 |pages= 2273-82 |year= 1997 |pmid= 9178903 |doi= 10.1038/sj.onc.1201071 }}
*{{cite journal | author=Laffargue M, Monnereau L, Tuech J, ''et al.'' |title=Integrin-dependent tyrosine phoshorylation and cytoskeletal translocation of Tec in thrombin-activated platelets. |journal=Biochem. Biophys. Res. Commun. |volume=238 |issue= 1 |pages= 247-51 |year= 1997 |pmid= 9299487 |doi= 10.1006/bbrc.1997.7269 }}
*{{cite journal | author=Ohya K, Kajigaya S, Yamashita Y, ''et al.'' |title=SOCS-1/JAB/SSI-1 can bind to and suppress Tec protein-tyrosine kinase. |journal=J. Biol. Chem. |volume=272 |issue= 43 |pages= 27178-82 |year= 1997 |pmid= 9341160 |doi= }}
*{{cite journal | author=Kitanaka A, Mano H, Conley ME, Campana D |title=Expression and activation of the nonreceptor tyrosine kinase Tec in human B cells. |journal=Blood |volume=91 |issue= 3 |pages= 940-8 |year= 1998 |pmid= 9446655 |doi= }}
*{{cite journal | author=Yamashita Y, Watanabe S, Miyazato A, ''et al.'' |title=Tec and Jak2 kinases cooperate to mediate cytokine-driven activation of c-fos transcription. |journal=Blood |volume=91 |issue= 5 |pages= 1496-507 |year= 1998 |pmid= 9473212 |doi= }}
*{{cite journal | author=Yang WC, Ghiotto M, Barbarat B, Olive D |title=The role of Tec protein-tyrosine kinase in T cell signaling. |journal=J. Biol. Chem. |volume=274 |issue= 2 |pages= 607-17 |year= 1999 |pmid= 9872994 |doi= }}
*{{cite journal | author=Yang WC, Olive D |title=Tec kinase is involved in transcriptional regulation of IL-2 and IL-4 in the CD28 pathway. |journal=Eur. J. Immunol. |volume=29 |issue= 6 |pages= 1842-9 |year= 1999 |pmid= 10382746 |doi= }}
*{{cite journal | author=Ohya K, Kajigaya S, Kitanaka A, ''et al.'' |title=Molecular cloning of a docking protein, BRDG1, that acts downstream of the Tec tyrosine kinase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 21 |pages= 11976-81 |year= 1999 |pmid= 10518561 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TFF3... {November 18, 2007 12:38:46 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 12:39:53 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_TFF3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1e9t.
| PDB = {{PDB2|1e9t}}, {{PDB2|1pe3}}
| Name = Trefoil factor 3 (intestinal)
| HGNCid = 11757
| Symbol = TFF3
| AltSymbols =; HITF; ITF; TFI; hP1.B
| OMIM = 600633
| ECnumber =
| Homologene = 2427
| MGIid = 104638
| GeneAtlas_image1 = PBB_GE_TFF3_204623_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0030141 |text = secretory granule}}
| Process = {{GNF_GO|id=GO:0006952 |text = defense response}} {{GNF_GO|id=GO:0007586 |text = digestion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7033
| Hs_Ensembl = ENSG00000160180
| Hs_RefseqProtein = NP_003217
| Hs_RefseqmRNA = NM_003226
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 21
| Hs_GenLoc_start = 42599751
| Hs_GenLoc_end = 42608775
| Hs_Uniprot = Q07654
| Mm_EntrezGene = 21786
| Mm_Ensembl = ENSMUSG00000024029
| Mm_RefseqmRNA = NM_011575
| Mm_RefseqProtein = NP_035705
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 30852327
| Mm_GenLoc_end = 30856623
| Mm_Uniprot = Q62395
}}
}}
'''Trefoil factor 3 (intestinal)''', also known as '''TFF3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TFF3 trefoil factor 3 (intestinal)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7033| 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 = Members of the trefoil family are characterized by having at least one copy of the trefoil motif, a 40-amino acid domain that contains three conserved disulfides. They are stable secretory proteins expressed in gastrointestinal mucosa. Their functions are not defined, but they may protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium. This gene is expressed in goblet cells of the intestines and colon. This gene and two other related trefoil family member genes are found in a cluster on chromosome 21.<ref name="entrez">{{cite web | title = Entrez Gene: TFF3 trefoil factor 3 (intestinal)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7033| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hoffmann W, Jagla W, Wiede A |title=Molecular medicine of TFF-peptides: from gut to brain. |journal=Histol. Histopathol. |volume=16 |issue= 1 |pages= 319-34 |year= 2001 |pmid= 11193208 |doi= }}
*{{cite journal | author=Hoffmann W, Jagla W |title=Cell type specific expression of secretory TFF peptides: colocalization with mucins and synthesis in the brain. |journal=Int. Rev. Cytol. |volume=213 |issue= |pages= 147-81 |year= 2002 |pmid= 11837892 |doi= }}
*{{cite journal | author=Langer G, Jagla W, Behrens-Baumann W, ''et al.'' |title=Ocular TFF-peptides: new mucus-associated secretory products of conjunctival goblet cells. |journal=Adv. Exp. Med. Biol. |volume=506 |issue= Pt A |pages= 313-6 |year= 2003 |pmid= 12613926 |doi= }}
*{{cite journal | author=Seib T, Dooley S, Welter C |title=Characterization of the genomic structure and the promoter region of the human intestinal trefoil factor. |journal=Biochem. Biophys. Res. Commun. |volume=214 |issue= 1 |pages= 195-9 |year= 1995 |pmid= 7669039 |doi= 10.1006/bbrc.1995.2274 }}
*{{cite journal | author=Thim L, Wöldike HF, Nielsen PF, ''et al.'' |title=Characterization of human and rat intestinal trefoil factor produced in yeast. |journal=Biochemistry |volume=34 |issue= 14 |pages= 4757-64 |year= 1995 |pmid= 7718582 |doi= }}
*{{cite journal | author=Hauser F, Poulsom R, Chinery R, ''et al.'' |title=hP1.B, a human P-domain peptide homologous with rat intestinal trefoil factor, is expressed also in the ulcer-associated cell lineage and the uterus. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 15 |pages= 6961-5 |year= 1993 |pmid= 8346203 |doi= }}
*{{cite journal | author=Podolsky DK, Lynch-Devaney K, Stow JL, ''et al.'' |title=Identification of human intestinal trefoil factor. Goblet cell-specific expression of a peptide targeted for apical secretion. |journal=J. Biol. Chem. |volume=268 |issue= 9 |pages= 6694-702 |year= 1993 |pmid= 8454642 |doi= }}
*{{cite journal | author=Schmitt H, Wundrack I, Beck S, ''et al.'' |title=A third P-domain peptide gene (TFF3), human intestinal trefoil factor, maps to 21q22.3. |journal=Cytogenet. Cell Genet. |volume=72 |issue= 4 |pages= 299-302 |year= 1996 |pmid= 8641134 |doi= }}
*{{cite journal | author=Chinery R, Williamson J, Poulsom R |title=The gene encoding human intestinal trefoil factor (TFF3) is located on chromosome 21q22.3 clustered with other members of the trefoil peptide family. |journal=Genomics |volume=32 |issue= 2 |pages= 281-4 |year= 1997 |pmid= 8833157 |doi= 10.1006/geno.1996.0117 }}
*{{cite journal | author=Probst JC, Zetzsche T, Weber M, ''et al.'' |title=Human intestinal trefoil factor is expressed in human hypothalamus and pituitary: evidence for a novel neuropeptide. |journal=FASEB J. |volume=10 |issue= 13 |pages= 1518-23 |year= 1997 |pmid= 8940297 |doi= }}
*{{cite journal | author=Gött P, Beck S, Machado JC, ''et al.'' |title=Human trefoil peptides: genomic structure in 21q22.3 and coordinated expression. |journal=Eur. J. Hum. Genet. |volume=4 |issue= 6 |pages= 308-15 |year= 1997 |pmid= 9043862 |doi= }}
*{{cite journal | author=Seib T, Blin N, Hilgert K, ''et al.'' |title=The three human trefoil genes TFF1, TFF2, and TFF3 are located within a region of 55 kb on chromosome 21q22.3. |journal=Genomics |volume=40 |issue= 1 |pages= 200-2 |year= 1997 |pmid= 9070946 |doi= 10.1006/geno.1996.4511 }}
*{{cite journal | author=Tan XD, Liu QP, Hsueh W, ''et al.'' |title=Intestinal trefoil factor binds to intestinal epithelial cells and induces nitric oxide production: priming and enhancing effects of mucin. |journal=Biochem. J. |volume=338 ( Pt 3) |issue= |pages= 745-51 |year= 1999 |pmid= 10051448 |doi= }}
*{{cite journal | author=Hattori M, Fujiyama A, Taylor TD, ''et al.'' |title=The DNA sequence of human chromosome 21. |journal=Nature |volume=405 |issue= 6784 |pages= 311-9 |year= 2000 |pmid= 10830953 |doi= 10.1038/35012518 }}
*{{cite journal | author=Berry A, Scott HS, Kudoh J, ''et al.'' |title=Refined localization of autosomal recessive nonsyndromic deafness DFNB10 locus using 34 novel microsatellite markers, genomic structure, and exclusion of six known genes in the region. |journal=Genomics |volume=68 |issue= 1 |pages= 22-9 |year= 2001 |pmid= 10950923 |doi= 10.1006/geno.2000.6253 }}
*{{cite journal | author=Wiede A, Hinz M, Canzler E, ''et al.'' |title=Synthesis and localization of the mucin-associated TFF-peptides in the human uterus. |journal=Cell Tissue Res. |volume=303 |issue= 1 |pages= 109-15 |year= 2001 |pmid= 11235998 |doi= }}
*{{cite journal | author=Yamachika T, Werther JL, Bodian C, ''et al.'' |title=Intestinal trefoil factor: a marker of poor prognosis in gastric carcinoma. |journal=Clin. Cancer Res. |volume=8 |issue= 5 |pages= 1092-9 |year= 2002 |pmid= 12006524 |doi= }}
*{{cite journal | author=Kimura Y, Leung PS, Kenny TP, ''et al.'' |title=Differential expression of intestinal trefoil factor in biliary epithelial cells of primary biliary cirrhosis. |journal=Hepatology |volume=36 |issue= 5 |pages= 1227-35 |year= 2002 |pmid= 12395334 |doi= 10.1053/jhep.2002.36157 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TFR2... {November 18, 2007 12:39:53 PM PST}
- SEARCH REDIRECT: Control Box Found: TFR2 {November 18, 2007 12:41:17 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 12:41:25 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 12:41:25 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 12:41:25 PM PST}
- UPDATED: Updated protein page: TFR2 {November 18, 2007 12:41:38 PM PST}
- INFO: Beginning work on TRA@... {November 18, 2007 12:37:05 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 12:37:59 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = T cell receptor alpha locus
| HGNCid = 12027
| Symbol = TRA@
| AltSymbols =; FLJ22602; MGC117436; MGC22624; MGC23964; MGC71411; TCRA; TCRD; TRA; TRDD3
| OMIM = 186880
| ECnumber =
| Homologene =
| MGIid =
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0042287 |text = MHC protein binding}} {{GNF_GO|id=GO:0042605 |text = peptide antigen binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006968 |text = cellular defense response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6955
| Hs_Ensembl =
| Hs_RefseqProtein =
| Hs_RefseqmRNA =
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''T cell receptor alpha locus''', also known as '''TRA@''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TRA@ T cell receptor alpha locus| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6955| 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=Kenwrick S, Levinson B, Taylor S, ''et al.'' |title=Isolation and sequence of two genes associated with a CpG island 5' of the factor VIII gene. |journal=Hum. Mol. Genet. |volume=1 |issue= 3 |pages= 179-86 |year= 1993 |pmid= 1303175 |doi= }}
*{{cite journal | author=Suzuki CK, Bonifacino JS, Lin AY, ''et al.'' |title=Regulating the retention of T-cell receptor alpha chain variants within the endoplasmic reticulum: Ca(2+)-dependent association with BiP. |journal=J. Cell Biol. |volume=114 |issue= 2 |pages= 189-205 |year= 1991 |pmid= 1649196 |doi= }}
*{{cite journal | author=Travis A, Amsterdam A, Belanger C, Grosschedl R |title=LEF-1, a gene encoding a lymphoid-specific protein with an HMG domain, regulates T-cell receptor alpha enhancer function [corrected] |journal=Genes Dev. |volume=5 |issue= 5 |pages= 880-94 |year= 1991 |pmid= 1827423 |doi= }}
*{{cite journal | author=Koning F, Maloy WL, Coligan JE |title=The implications of subunit interactions for the structure of the T cell receptor-CD3 complex. |journal=Eur. J. Immunol. |volume=20 |issue= 2 |pages= 299-305 |year= 1990 |pmid= 2138083 |doi= }}
*{{cite journal | author=Dyer MJ |title=T-cell receptor delta/alpha rearrangements in lymphoid neoplasms. |journal=Blood |volume=74 |issue= 3 |pages= 1073-83 |year= 1989 |pmid= 2546634 |doi= }}
*{{cite journal | author=Chilson OP, Kelly-Chilson AE |title=Mitogenic lectins bind to the antigen receptor on human lymphocytes. |journal=Eur. J. Immunol. |volume=19 |issue= 2 |pages= 389-96 |year= 1989 |pmid= 2703017 |doi= }}
*{{cite journal | author=Yanagi Y, Chan A, Chin B, ''et al.'' |title=Analysis of cDNA clones specific for human T cells and the alpha and beta chains of the T-cell receptor heterodimer from a human T-cell line. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 10 |pages= 3430-4 |year= 1985 |pmid= 3873654 |doi= }}
*{{cite journal | author=Erikson J, Williams DL, Finan J, ''et al.'' |title=Locus of the alpha-chain of the T-cell receptor is split by chromosome translocation in T-cell leukemias. |journal=Science |volume=229 |issue= 4715 |pages= 784-6 |year= 1985 |pmid= 3875152 |doi= }}
*{{cite journal | author=Rabbitts TH, Lefranc MP, Stinson MA, ''et al.'' |title=The chromosomal location of T-cell receptor genes and a T cell rearranging gene: possible correlation with specific translocations in human T cell leukaemia. |journal=EMBO J. |volume=4 |issue= 6 |pages= 1461-5 |year= 1985 |pmid= 3875483 |doi= }}
*{{cite journal | author=Sim GK, Yagüe J, Nelson J, ''et al.'' |title=Primary structure of human T-cell receptor alpha-chain. |journal=Nature |volume=312 |issue= 5996 |pages= 771-5 |year= 1985 |pmid= 6440030 |doi= }}
*{{cite journal | author=Kearse KP, Roberts JL, Singer A |title=TCR alpha-CD3 delta epsilon association is the initial step in alpha beta dimer formation in murine T cells and is limiting in immature CD4+ CD8+ thymocytes. |journal=Immunity |volume=2 |issue= 4 |pages= 391-9 |year= 1995 |pmid= 7719941 |doi= }}
*{{cite journal | author=Manolios N, Kemp O, Li ZG |title=The T cell antigen receptor alpha and beta chains interact via distinct regions with CD3 chains. |journal=Eur. J. Immunol. |volume=24 |issue= 1 |pages= 84-92 |year= 1994 |pmid= 8020575 |doi= }}
*{{cite journal | author=Bagga R, Emerson BM |title=An HMG I/Y-containing repressor complex and supercoiled DNA topology are critical for long-range enhancer-dependent transcription in vitro. |journal=Genes Dev. |volume=11 |issue= 5 |pages= 629-39 |year= 1997 |pmid= 9119227 |doi= }}
*{{cite journal | author=San José E, Sahuquillo AG, Bragado R, Alarcón B |title=Assembly of the TCR/CD3 complex: CD3 epsilon/delta and CD3 epsilon/gamma dimers associate indistinctly with both TCR alpha and TCR beta chains. Evidence for a double TCR heterodimer model. |journal=Eur. J. Immunol. |volume=28 |issue= 1 |pages= 12-21 |year= 1998 |pmid= 9485181 |doi= }}
*{{cite journal | author=Ding YH, Smith KJ, Garboczi DN, ''et al.'' |title=Two human T cell receptors bind in a similar diagonal mode to the HLA-A2/Tax peptide complex using different TCR amino acids. |journal=Immunity |volume=8 |issue= 4 |pages= 403-11 |year= 1998 |pmid= 9586631 |doi= }}
*{{cite journal | author=Kirchgessner H, Dietrich J, Scherer J, ''et al.'' |title=The transmembrane adaptor protein TRIM regulates T cell receptor (TCR) expression and TCR-mediated signaling via an association with the TCR zeta chain. |journal=J. Exp. Med. |volume=193 |issue= 11 |pages= 1269-84 |year= 2001 |pmid= 11390434 |doi= }}
*{{cite journal | author=Shelton JG, Gülland S, Nicolson K, ''et al.'' |title=Importance of the T cell receptor alpha-chain transmembrane distal region for assembly with cognate subunits. |journal=Mol. Immunol. |volume=38 |issue= 4 |pages= 259-65 |year= 2001 |pmid= 11566319 |doi= }}
*{{cite journal | author=Pietra G, Romagnani C, Falco M, ''et al.'' |title=The analysis of the natural killer-like activity of human cytolytic T lymphocytes revealed HLA-E as a novel target for TCR alpha/beta-mediated recognition. |journal=Eur. J. Immunol. |volume=31 |issue= 12 |pages= 3687-93 |year= 2002 |pmid= 11745389 |doi= }}
*{{cite journal | author=Hennecke J, Wiley DC |title=Structure of a complex of the human alpha/beta T cell receptor (TCR) HA1.7, influenza hemagglutinin peptide, and major histocompatibility complex class II molecule, HLA-DR4 (DRA*0101 and DRB1*0401): insight into TCR cross-restriction and alloreactivity. |journal=J. Exp. Med. |volume=195 |issue= 5 |pages= 571-81 |year= 2002 |pmid= 11877480 |doi= }}
*{{cite journal | author=García P, Llano M, de Heredia AB, ''et al.'' |title=Human T cell receptor-mediated recognition of HLA-E. |journal=Eur. J. Immunol. |volume=32 |issue= 4 |pages= 936-44 |year= 2002 |pmid= 11920559 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TRIM5... {November 18, 2007 12:47:50 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 12:48:49 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Tripartite motif-containing 5
| HGNCid = 16276
| Symbol = TRIM5
| AltSymbols =; RNF88; TRIM5alpha
| OMIM = 608487
| ECnumber =
| Homologene = 75345
| MGIid = 2441735
| GeneAtlas_image1 = PBB_GE_TRIM5_210705_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016874 |text = ligase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}}
| Process = {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0009615 |text = response to virus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 85363
| Hs_Ensembl = ENSG00000132256
| Hs_RefseqProtein = NP_149023
| Hs_RefseqmRNA = NM_033034
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 5641363
| Hs_GenLoc_end = 5850164
| Hs_Uniprot = Q9C035
| Mm_EntrezGene = 319236
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_175677
| Mm_RefseqProtein = NP_783608
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Tripartite motif-containing 5''', also known as '''TRIM5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TRIM5 tripartite motif-containing 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=85363| 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 tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes to cytoplasmic bodies. Its function has not been identified. Five alternatively spliced transcript variants for this gene have been described. However, the full length nature of two of the variants has not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: TRIM5 tripartite motif-containing 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=85363| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Luban J |title=Cyclophilin A, TRIM5, and resistance to human immunodeficiency virus type 1 infection. |journal=J. Virol. |volume=81 |issue= 3 |pages= 1054-61 |year= 2007 |pmid= 16956947 |doi= 10.1128/JVI.01519-06 }}
*{{cite journal | author=Freed EO, Mouland AJ |title=The cell biology of HIV-1 and other retroviruses. |journal=Retrovirology |volume=3 |issue= |pages= 77 |year= 2006 |pmid= 17083721 |doi= 10.1186/1742-4690-3-77 }}
*{{cite journal | author=Reymond A, Meroni G, Fantozzi A, ''et al.'' |title=The tripartite motif family identifies cell compartments. |journal=EMBO J. |volume=20 |issue= 9 |pages= 2140-51 |year= 2001 |pmid= 11331580 |doi= 10.1093/emboj/20.9.2140 }}
*{{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=Xu L, Yang L, Moitra PK, ''et al.'' |title=BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta. |journal=Exp. Cell Res. |volume=288 |issue= 1 |pages= 84-93 |year= 2003 |pmid= 12878161 |doi= }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Stremlau M, Owens CM, Perron MJ, ''et al.'' |title=The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys. |journal=Nature |volume=427 |issue= 6977 |pages= 848-53 |year= 2004 |pmid= 14985764 |doi= 10.1038/nature02343 }}
*{{cite journal | author=Hatziioannou T, Perez-Caballero D, Yang A, ''et al.'' |title=Retrovirus resistance factors Ref1 and Lv1 are species-specific variants of TRIM5alpha. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 29 |pages= 10774-9 |year= 2004 |pmid= 15249685 |doi= 10.1073/pnas.0402361101 }}
*{{cite journal | author=Keckesova Z, Ylinen LM, Towers GJ |title=The human and African green monkey TRIM5alpha genes encode Ref1 and Lv1 retroviral restriction factor activities. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 29 |pages= 10780-5 |year= 2004 |pmid= 15249687 |doi= 10.1073/pnas.0402474101 }}
*{{cite journal | author=Yap MW, Nisole S, Lynch C, Stoye JP |title=Trim5alpha protein restricts both HIV-1 and murine leukemia virus. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 29 |pages= 10786-91 |year= 2004 |pmid= 15249690 |doi= 10.1073/pnas.0402876101 }}
*{{cite journal | author=Perron MJ, Stremlau M, Song B, ''et al.'' |title=TRIM5alpha mediates the postentry block to N-tropic murine leukemia viruses in human cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 32 |pages= 11827-32 |year= 2004 |pmid= 15280539 |doi= 10.1073/pnas.0403364101 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal | author=Yap MW, Nisole S, Stoye JP |title=A single amino acid change in the SPRY domain of human Trim5alpha leads to HIV-1 restriction. |journal=Curr. Biol. |volume=15 |issue= 1 |pages= 73-8 |year= 2005 |pmid= 15649369 |doi= 10.1016/j.cub.2004.12.042 }}
*{{cite journal | author=Stremlau M, Perron M, Welikala S, Sodroski J |title=Species-specific variation in the B30.2(SPRY) domain of TRIM5alpha determines the potency of human immunodeficiency virus restriction. |journal=J. Virol. |volume=79 |issue= 5 |pages= 3139-45 |year= 2005 |pmid= 15709033 |doi= 10.1128/JVI.79.5.3139-3145.2005 }}
*{{cite journal | author=Song B, Javanbakht H, Perron M, ''et al.'' |title=Retrovirus restriction by TRIM5alpha variants from Old World and New World primates. |journal=J. Virol. |volume=79 |issue= 7 |pages= 3930-7 |year= 2005 |pmid= 15767395 |doi= 10.1128/JVI.79.7.3930-3937.2005 }}
*{{cite journal | author=Berthoux L, Sebastian S, Sayah DM, Luban J |title=Disruption of human TRIM5alpha antiviral activity by nonhuman primate orthologues. |journal=J. Virol. |volume=79 |issue= 12 |pages= 7883-8 |year= 2005 |pmid= 15919943 |doi= 10.1128/JVI.79.12.7883-7888.2005 }}
*{{cite journal | author=Sebastian S, Luban J |title=TRIM5alpha selectively binds a restriction-sensitive retroviral capsid. |journal=Retrovirology |volume=2 |issue= |pages= 40 |year= 2005 |pmid= 15967037 |doi= 10.1186/1742-4690-2-40 }}
*{{cite journal | author=Perez-Caballero D, Hatziioannou T, Yang A, ''et al.'' |title=Human tripartite motif 5alpha domains responsible for retrovirus restriction activity and specificity. |journal=J. Virol. |volume=79 |issue= 14 |pages= 8969-78 |year= 2005 |pmid= 15994791 |doi= 10.1128/JVI.79.14.8969-8978.2005 }}
*{{cite journal | author=Liu HL, Wang YQ, Liao CH, ''et al.'' |title=Adaptive evolution of primate TRIM5alpha, a gene restricting HIV-1 infection. |journal=Gene |volume=362 |issue= |pages= 109-16 |year= 2006 |pmid= 16226405 |doi= 10.1016/j.gene.2005.06.045 }}
*{{cite journal | author=Mische CC, Javanbakht H, Song B, ''et al.'' |title=Retroviral restriction factor TRIM5alpha is a trimer. |journal=J. Virol. |volume=79 |issue= 22 |pages= 14446-50 |year= 2006 |pmid= 16254380 |doi= 10.1128/JVI.79.22.14446-14450.2005 }}
}}
{{refend}}
{{protein-stub}}
end log.
