Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 00:52, 16 November 2007 (UTC)
[edit]Proteins without matches (16)
[edit]Proteins with a High Potential Match (5)
[edit]Redirected Proteins (4)
[edit]Manual Inspection (Page not found) (21)
[edit]
Protein Status Grid - Date: 00:52, 16 November 2007 (UTC)
[edit]Vebose Log - Date: 00:52, 16 November 2007 (UTC)
[edit]- INFO: Beginning work on ARRB1... {November 15, 2007 4:25:20 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 4:27:36 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| 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_ARRB1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1g4m.
| PDB = {{PDB2|1g4m}}, {{PDB2|1g4r}}, {{PDB2|1jsy}}, {{PDB2|1zsh}}
| Name = Arrestin, beta 1
| HGNCid = 711
| Symbol = ARRB1
| AltSymbols =; ARB1; ARR1
| OMIM = 107940
| ECnumber =
| Homologene = 2981
| MGIid = 99473
| GeneAtlas_image1 = PBB_GE_ARRB1_218832_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004857 |text = enzyme inhibitor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005834 |text = heterotrimeric G-protein complex}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007600 |text = sensory perception}} {{GNF_GO|id=GO:0008277 |text = regulation of G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 408
| Hs_Ensembl = ENSG00000137486
| Hs_RefseqProtein = NP_004032
| Hs_RefseqmRNA = NM_004041
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 74654130
| Hs_GenLoc_end = 74740521
| Hs_Uniprot = P49407
| Mm_EntrezGene = 109689
| Mm_Ensembl = ENSMUSG00000018909
| Mm_RefseqmRNA = NM_177231
| Mm_RefseqProtein = NP_796205
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 99409569
| Mm_GenLoc_end = 99480854
| Mm_Uniprot = Q8BWG8
}}
}}
'''Arrestin, beta 1''', also known as '''ARRB1''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: ARRB1 arrestin, beta 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=408| 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 arrestin/beta-arrestin protein family are thought to participate in agonist-mediated desensitization of G-protein-coupled receptors and cause specific dampening of cellular responses to stimuli such as hormones, neurotransmitters, or sensory signals. Arrestin beta 1 is a cytosolic protein and acts as a cofactor in the beta-adrenergic receptor kinase (BARK) mediated desensitization of beta-adrenergic receptors. Besides the central nervous system, it is expressed at high levels in peripheral blood leukocytes, and thus the BARK/beta-arrestin system is believed to play a major role in regulating receptor-mediated immune functions. Alternatively spliced transcripts encoding different isoforms of arrestin beta 1 have been described, however, their exact functions are not known.<ref>{{cite web | title = Entrez Gene: ARRB1 arrestin, beta 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=408| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lefkowitz RJ |title=G protein-coupled receptors. III. New roles for receptor kinases and beta-arrestins in receptor signaling and desensitization. |journal=J. Biol. Chem. |volume=273 |issue= 30 |pages= 18677-80 |year= 1998 |pmid= 9668034 |doi= }}
*{{cite journal | author=Lohse MJ, Benovic JL, Codina J, ''et al.'' |title=beta-Arrestin: a protein that regulates beta-adrenergic receptor function. |journal=Science |volume=248 |issue= 4962 |pages= 1547-50 |year= 1990 |pmid= 2163110 |doi= }}
*{{cite journal | author=Calabrese G, Sallese M, Stornaiuolo A, ''et al.'' |title=Assignment of the beta-arrestin 1 gene (ARRB1) to human chromosome 11q13. |journal=Genomics |volume=24 |issue= 1 |pages= 169-71 |year= 1995 |pmid= 7896272 |doi= 10.1006/geno.1994.1594 }}
*{{cite journal | author=Parruti G, Peracchia F, Sallese M, ''et al.'' |title=Molecular analysis of human beta-arrestin-1: cloning, tissue distribution, and regulation of expression. Identification of two isoforms generated by alternative splicing. |journal=J. Biol. Chem. |volume=268 |issue= 13 |pages= 9753-61 |year= 1993 |pmid= 8486659 |doi= }}
*{{cite journal | author=Iacovelli L, Franchetti R, Masini M, De Blasi A |title=GRK2 and beta-arrestin 1 as negative regulators of thyrotropin receptor-stimulated response. |journal=Mol. Endocrinol. |volume=10 |issue= 9 |pages= 1138-46 |year= 1997 |pmid= 8885248 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Goodman OB, Krupnick JG, Gurevich VV, ''et al.'' |title=Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain. |journal=J. Biol. Chem. |volume=272 |issue= 23 |pages= 15017-22 |year= 1997 |pmid= 9169477 |doi= }}
*{{cite journal | author=Lin FT, Krueger KM, Kendall HE, ''et al.'' |title=Clathrin-mediated endocytosis of the beta-adrenergic receptor is regulated by phosphorylation/dephosphorylation of beta-arrestin1. |journal=J. Biol. Chem. |volume=272 |issue= 49 |pages= 31051-7 |year= 1998 |pmid= 9388255 |doi= }}
*{{cite journal | author=Aragay AM, Mellado M, Frade JM, ''et al.'' |title=Monocyte chemoattractant protein-1-induced CCR2B receptor desensitization mediated by the G protein-coupled receptor kinase 2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 6 |pages= 2985-90 |year= 1998 |pmid= 9501202 |doi= }}
*{{cite journal | author=ter Haar E, Musacchio A, Harrison SC, Kirchhausen T |title=Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker. |journal=Cell |volume=95 |issue= 4 |pages= 563-73 |year= 1998 |pmid= 9827808 |doi= }}
*{{cite journal | author=Luttrell LM, Ferguson SS, Daaka Y, ''et al.'' |title=Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes. |journal=Science |volume=283 |issue= 5402 |pages= 655-61 |year= 1999 |pmid= 9924018 |doi= }}
*{{cite journal | author=McDonald PH, Cote NL, Lin FT, ''et al.'' |title=Identification of NSF as a beta-arrestin1-binding protein. Implications for beta2-adrenergic receptor regulation. |journal=J. Biol. Chem. |volume=274 |issue= 16 |pages= 10677-80 |year= 1999 |pmid= 10196135 |doi= }}
*{{cite journal | author=Lin FT, Miller WE, Luttrell LM, Lefkowitz RJ |title=Feedback regulation of beta-arrestin1 function by extracellular signal-regulated kinases. |journal=J. Biol. Chem. |volume=274 |issue= 23 |pages= 15971-4 |year= 1999 |pmid= 10347142 |doi= }}
*{{cite journal | author=McConalogue K, Déry O, Lovett M, ''et al.'' |title=Substance P-induced trafficking of beta-arrestins. The role of beta-arrestins in endocytosis of the neurokinin-1 receptor. |journal=J. Biol. Chem. |volume=274 |issue= 23 |pages= 16257-68 |year= 1999 |pmid= 10347182 |doi= }}
*{{cite journal | author=Miller WE, Maudsley S, Ahn S, ''et al.'' |title=beta-arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of beta-arrestin1-dependent targeting of c-SRC in receptor endocytosis. |journal=J. Biol. Chem. |volume=275 |issue= 15 |pages= 11312-9 |year= 2000 |pmid= 10753943 |doi= }}
*{{cite journal | author=Laporte SA, Oakley RH, Holt JA, ''et al.'' |title=The interaction of beta-arrestin with the AP-2 adaptor is required for the clustering of beta 2-adrenergic receptor into clathrin-coated pits. |journal=J. Biol. Chem. |volume=275 |issue= 30 |pages= 23120-6 |year= 2000 |pmid= 10770944 |doi= 10.1074/jbc.M002581200 }}
*{{cite journal | author=Bennett TA, Maestas DC, Prossnitz ER |title=Arrestin binding to the G protein-coupled N-formyl peptide receptor is regulated by the conserved "DRY" sequence. |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24590-4 |year= 2000 |pmid= 10823817 |doi= 10.1074/jbc.C000314200 }}
*{{cite journal | author=Shiina T, Kawasaki A, Nagao T, Kurose H |title=Interaction with beta-arrestin determines the difference in internalization behavor between beta1- and beta2-adrenergic receptors. |journal=J. Biol. Chem. |volume=275 |issue= 37 |pages= 29082-90 |year= 2000 |pmid= 10862778 |doi= 10.1074/jbc.M909757199 }}
*{{cite journal | author=Barlic J, Andrews JD, Kelvin AA, ''et al.'' |title=Regulation of tyrosine kinase activation and granule release through beta-arrestin by CXCRI. |journal=Nat. Immunol. |volume=1 |issue= 3 |pages= 227-33 |year= 2001 |pmid= 10973280 |doi= 10.1038/79767 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ATXN3... {November 15, 2007 4:35:21 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 4:36:22 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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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_ATXN3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1yzb.
| PDB = {{PDB2|1yzb}}, {{PDB2|2aga}}, {{PDB2|2dos}}
| Name = Ataxin 3
| HGNCid = 7106
| Symbol = ATXN3
| AltSymbols =; AT3; ATX3; JOS; MJD; MJD1; SCA3
| OMIM = 607047
| ECnumber =
| Homologene = 3658
| MGIid = 1099442
| GeneAtlas_image1 = PBB_GE_ATXN3_205415_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ATXN3_205416_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005654 |text = nucleoplasm}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006289 |text = nucleotide-excision repair}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0008219 |text = cell death}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4287
| Hs_Ensembl = ENSG00000066427
| Hs_RefseqProtein = NP_001019802
| Hs_RefseqmRNA = NM_001024631
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 91598887
| Hs_GenLoc_end = 91642707
| Hs_Uniprot =
| Mm_EntrezGene = 110616
| Mm_Ensembl = ENSMUSG00000021189
| Mm_RefseqmRNA = NM_029705
| Mm_RefseqProtein = NP_083981
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 102320604
| Mm_GenLoc_end = 102359232
| Mm_Uniprot = Q546X9
}}
}}
'''Ataxin 3''', also known as '''ATXN3''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: ATXN3 ataxin 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4287| 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 = Machado-Joseph disease, also known as spinocerebellar ataxia-3, is an autosomal dominant neurologic disorder. The protein encoded by this gene contains (CAG)n repeats in the coding region, and the expansion of these repeats from the normal 13-36 to 68-79 is the cause of Machado-Joseph disease. There is a negative correlation between the age of onset and CAG repeat numbers. Alternatively spliced transcript variants encoding different isoforms have been described for this gene.<ref>{{cite web | title = Entrez Gene: ATXN3 ataxin 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4287| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Goto J, Watanabe M, Ichikawa Y, ''et al.'' |title=Machado-Joseph disease gene products carrying different carboxyl termini. |journal=Neurosci. Res. |volume=28 |issue= 4 |pages= 373-7 |year= 1997 |pmid= 9274833 |doi= }}
*{{cite journal | author=Schöls L, Vieira-Saecker AM, Schöls S, ''et al.'' |title=Trinucleotide expansion within the MJD1 gene presents clinically as spinocerebellar ataxia and occurs most frequently in German SCA patients. |journal=Hum. Mol. Genet. |volume=4 |issue= 6 |pages= 1001-5 |year= 1995 |pmid= 7655453 |doi= }}
*{{cite journal | author=Stevanin G, Cancel G, Dürr A, ''et al.'' |title=The gene for spinal cerebellar ataxia 3 (SCA3) is located in a region of approximately 3 cM on chromosome 14q24.3-q32.2. |journal=Am. J. Hum. Genet. |volume=56 |issue= 1 |pages= 193-201 |year= 1995 |pmid= 7825578 |doi= }}
*{{cite journal | author=Kawaguchi Y, Okamoto T, Taniwaki M, ''et al.'' |title=CAG expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1. |journal=Nat. Genet. |volume=8 |issue= 3 |pages= 221-8 |year= 1995 |pmid= 7874163 |doi= 10.1038/ng1194-221 }}
*{{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=Takiyama Y, Nishizawa M, Tanaka H, ''et al.'' |title=The gene for Machado-Joseph disease maps to human chromosome 14q. |journal=Nat. Genet. |volume=4 |issue= 3 |pages= 300-4 |year= 1993 |pmid= 8358439 |doi= 10.1038/ng0793-300 }}
*{{cite journal | author=Ikeda H, Yamaguchi M, Sugai S, ''et al.'' |title=Expanded polyglutamine in the Machado-Joseph disease protein induces cell death in vitro and in vivo. |journal=Nat. Genet. |volume=13 |issue= 2 |pages= 196-202 |year= 1996 |pmid= 8640226 |doi= 10.1038/ng0696-196 }}
*{{cite journal | author=Paulson HL, Das SS, Crino PB, ''et al.'' |title=Machado-Joseph disease gene product is a cytoplasmic protein widely expressed in brain. |journal=Ann. Neurol. |volume=41 |issue= 4 |pages= 453-62 |year= 1997 |pmid= 9124802 |doi= 10.1002/ana.410410408 }}
*{{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=Wellington CL, Ellerby LM, Hackam AS, ''et al.'' |title=Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract. |journal=J. Biol. Chem. |volume=273 |issue= 15 |pages= 9158-67 |year= 1998 |pmid= 9535906 |doi= }}
*{{cite journal | author=Tait D, Riccio M, Sittler A, ''et al.'' |title=Ataxin-3 is transported into the nucleus and associates with the nuclear matrix. |journal=Hum. Mol. Genet. |volume=7 |issue= 6 |pages= 991-7 |year= 1998 |pmid= 9580663 |doi= }}
*{{cite journal | author=Wang G, Sawai N, Kotliarova S, ''et al.'' |title=Ataxin-3, the MJD1 gene product, interacts with the two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B. |journal=Hum. Mol. Genet. |volume=9 |issue= 12 |pages= 1795-803 |year= 2000 |pmid= 10915768 |doi= }}
*{{cite journal | author=Ichikawa Y, Goto J, Hattori M, ''et al.'' |title=The genomic structure and expression of MJD, the Machado-Joseph disease gene. |journal=J. Hum. Genet. |volume=46 |issue= 7 |pages= 413-22 |year= 2001 |pmid= 11450850 |doi= }}
*{{cite journal | author=Chai Y, Shao J, Miller VM, ''et al.'' |title=Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 14 |pages= 9310-5 |year= 2002 |pmid= 12084819 |doi= 10.1073/pnas.152101299 }}
*{{cite journal | author=Yoshida H, Yoshizawa T, Shibasaki F, ''et al.'' |title=Chemical chaperones reduce aggregate formation and cell death caused by the truncated Machado-Joseph disease gene product with an expanded polyglutamine stretch. |journal=Neurobiol. Dis. |volume=10 |issue= 2 |pages= 88-99 |year= 2002 |pmid= 12127147 |doi= }}
*{{cite journal | author=Li F, Macfarlan T, Pittman RN, Chakravarti D |title=Ataxin-3 is a histone-binding protein with two independent transcriptional corepressor activities. |journal=J. Biol. Chem. |volume=277 |issue= 47 |pages= 45004-12 |year= 2003 |pmid= 12297501 |doi= 10.1074/jbc.M205259200 }}
*{{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=Albrecht M, Hoffmann D, Evert BO, ''et al.'' |title=Structural modeling of ataxin-3 reveals distant homology to adaptins. |journal=Proteins |volume=50 |issue= 2 |pages= 355-70 |year= 2003 |pmid= 12486728 |doi= 10.1002/prot.10280 }}
*{{cite journal | author=Marchal S, Shehi E, Harricane MC, ''et al.'' |title=Structural instability and fibrillar aggregation of non-expanded human ataxin-3 revealed under high pressure and temperature. |journal=J. Biol. Chem. |volume=278 |issue= 34 |pages= 31554-63 |year= 2003 |pmid= 12766160 |doi= 10.1074/jbc.M304205200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on BIRC3... {November 15, 2007 4:24:04 PM PST}
- SEARCH REDIRECT: Control Box Found: BIRC3 {November 15, 2007 4:25:12 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 4:25:13 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 4:25:13 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 4:25:13 PM PST}
- UPDATED: Updated protein page: BIRC3 {November 15, 2007 4:25:20 PM PST}
- INFO: Beginning work on CD1D... {November 15, 2007 4:27:36 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 4:28:10 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_CD1D_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1zt4.
| PDB = {{PDB2|1zt4}}
| Name = CD1d molecule
| HGNCid = 1637
| Symbol = CD1D
| AltSymbols =; CD1A; MGC34622; R3
| OMIM = 188410
| ECnumber =
| Homologene = 1337
| MGIid = 107674
| GeneAtlas_image1 = PBB_GE_CD1D_205789_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0030881 |text = beta-2-microglobulin binding}} {{GNF_GO|id=GO:0030884 |text = exogenous lipid antigen binding}} {{GNF_GO|id=GO:0046982 |text = protein heterodimerization activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0016045 |text = detection of bacterium}} {{GNF_GO|id=GO:0045058 |text = T cell selection}} {{GNF_GO|id=GO:0045089 |text = positive regulation of innate immune response}} {{GNF_GO|id=GO:0048006 |text = antigen processing and presentation, endogenous lipid antigen via MHC class Ib}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 912
| Hs_Ensembl = ENSG00000158473
| Hs_RefseqProtein = NP_001757
| Hs_RefseqmRNA = NM_001766
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 156416361
| Hs_GenLoc_end = 156421310
| Hs_Uniprot = P15813
| Mm_EntrezGene = 12479
| Mm_Ensembl = ENSMUSG00000028076
| Mm_RefseqmRNA = NM_007639
| Mm_RefseqProtein = NP_031665
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 87081765
| Mm_GenLoc_end = 87085264
| Mm_Uniprot = Q91XK9
}}
}}
'''CD1d molecule''', also known as '''CD1D''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: CD1D CD1d molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=912| 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 divergent 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 late endosomes and lysosomes via a tyrosine-based motif in the cytoplasmic tail.<ref>{{cite web | title = Entrez Gene: CD1D CD1d molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=912| 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=Joyce S |title=CD1d and natural T cells: how their properties jump-start the immune system. |journal=Cell. Mol. Life Sci. |volume=58 |issue= 3 |pages= 442-69 |year= 2001 |pmid= 11315191 |doi= }}
*{{cite journal | author=Sköld M, Behar SM |title=Role of CD1d-restricted NKT cells in microbial immunity. |journal=Infect. Immun. |volume=71 |issue= 10 |pages= 5447-55 |year= 2003 |pmid= 14500461 |doi= }}
*{{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=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=Brutkiewicz RR |title=CD1d ligands: the good, the bad, and the ugly. |journal=J. Immunol. |volume=177 |issue= 2 |pages= 769-75 |year= 2006 |pmid= 16818729 |doi= }}
*{{cite journal | author=Blumberg RS, Terhorst C, Bleicher P, ''et al.'' |title=Expression of a nonpolymorphic MHC class I-like molecule, CD1D, by human intestinal epithelial cells. |journal=J. Immunol. |volume=147 |issue= 8 |pages= 2518-24 |year= 1991 |pmid= 1717564 |doi= }}
*{{cite journal | author=Balk SP, Bleicher PA, Terhorst C |title=Isolation and characterization of a cDNA and gene coding for a fourth CD1 molecule. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 1 |pages= 252-6 |year= 1989 |pmid= 2463622 |doi= }}
*{{cite journal | author=Calabi F, Jarvis JM, Martin L, Milstein C |title=Two classes of CD1 genes. |journal=Eur. J. Immunol. |volume=19 |issue= 2 |pages= 285-92 |year= 1989 |pmid= 2467814 |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=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=Balk SP, Burke S, Polischuk JE, ''et al.'' |title=Beta 2-microglobulin-independent MHC class Ib molecule expressed by human intestinal epithelium. |journal=Science |volume=265 |issue= 5169 |pages= 259-62 |year= 1994 |pmid= 7517575 |doi= }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Kawano T, Cui J, Koezuka Y, ''et al.'' |title=CD1d-restricted and TCR-mediated activation of valpha14 NKT cells by glycosylceramides. |journal=Science |volume=278 |issue= 5343 |pages= 1626-9 |year= 1997 |pmid= 9374463 |doi= }}
*{{cite journal | author=Katabami S, Matsuura A, Chen HZ, ''et al.'' |title=Structural organization of rat CD1 typifies evolutionarily conserved CD1D class genes. |journal=Immunogenetics |volume=48 |issue= 1 |pages= 22-31 |year= 1998 |pmid= 9601940 |doi= }}
*{{cite journal | author=Somnay-Wadgaonkar K, Nusrat A, Kim HS, ''et al.'' |title=Immunolocalization of CD1d in human intestinal epithelial cells and identification of a beta2-microglobulin-associated form. |journal=Int. Immunol. |volume=11 |issue= 3 |pages= 383-92 |year= 1999 |pmid= 10221650 |doi= }}
*{{cite journal | author=Campbell NA, Kim HS, Blumberg RS, Mayer L |title=The nonclassical class I molecule CD1d associates with the novel CD8 ligand gp180 on intestinal epithelial cells. |journal=J. Biol. Chem. |volume=274 |issue= 37 |pages= 26259-65 |year= 1999 |pmid= 10473580 |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= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CD3E... {November 15, 2007 4:28:10 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 4:28:47 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_CD3E_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1xiw.
| PDB = {{PDB2|1xiw}}
| Name = CD3e molecule, epsilon (CD3-TCR complex)
| HGNCid = 1674
| Symbol = CD3E
| AltSymbols =; T3E; TCRE
| OMIM = 186830
| ECnumber =
| Homologene = 586
| MGIid = 88332
| GeneAtlas_image1 = PBB_GE_CD3E_205456_at_tn.png
| Function = {{GNF_GO|id=GO:0004888 |text = transmembrane receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0017124 |text = SH3 domain binding}} {{GNF_GO|id=GO:0019901 |text = protein kinase binding}} {{GNF_GO|id=GO:0030159 |text = receptor signaling complex scaffold activity}} {{GNF_GO|id=GO:0042608 |text = T cell receptor binding}} {{GNF_GO|id=GO:0046982 |text = protein heterodimerization activity}}
| 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}} {{GNF_GO|id=GO:0042105 |text = alpha-beta T cell receptor complex}}
| Process = {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0007172 |text = signal complex assembly}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0042102 |text = positive regulation of T cell proliferation}} {{GNF_GO|id=GO:0042110 |text = T cell activation}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}} {{GNF_GO|id=GO:0045060 |text = negative thymic T cell selection}} {{GNF_GO|id=GO:0050731 |text = positive regulation of peptidyl-tyrosine phosphorylation}} {{GNF_GO|id=GO:0050850 |text = positive regulation of calcium-mediated signaling}} {{GNF_GO|id=GO:0050852 |text = T cell receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 916
| Hs_Ensembl = ENSG00000198851
| Hs_RefseqProtein = NP_000724
| Hs_RefseqmRNA = NM_000733
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 117680662
| Hs_GenLoc_end = 117692096
| Hs_Uniprot = P07766
| Mm_EntrezGene = 12501
| Mm_Ensembl = ENSMUSG00000032093
| Mm_RefseqmRNA = NM_007648
| Mm_RefseqProtein = NP_031674
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 44749738
| Mm_GenLoc_end = 44760585
| Mm_Uniprot = P22646
}}
}}
'''CD3e molecule, epsilon (CD3-TCR complex)''', also known as '''CD3E''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: CD3E CD3e molecule, epsilon (CD3-TCR complex)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=916| 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=Li CJ |title=Therapeutic biology: checkpoint pathway activation therapy, HIV Tat, and transkingdom RNA interference. |journal=J. Cell. Physiol. |volume=209 |issue= 3 |pages= 695-700 |year= 2007 |pmid= 17001685 |doi= 10.1002/jcp.20817 }}
*{{cite journal | author=Thoenes G, Soudais C, le Deist F, ''et al.'' |title=Structural analysis of low TCR-CD3 complex expression in T cells of an immunodeficient patient. |journal=J. Biol. Chem. |volume=267 |issue= 1 |pages= 487-93 |year= 1992 |pmid= 1370449 |doi= }}
*{{cite journal | author=Luzzati AL, Giacomini E, Giordani L, ''et al.'' |title=The antigen-specific induction of normal human lymphocytes in vitro is down-regulated by a conserved HIV p24 epitope. |journal=Immunol. Lett. |volume=33 |issue= 3 |pages= 307-14 |year= 1992 |pmid= 1385321 |doi= }}
*{{cite journal | author=Lanier LL, Chang C, Spits H, Phillips JH |title=Expression of cytoplasmic CD3 epsilon proteins in activated human adult natural killer (NK) cells and CD3 gamma, delta, epsilon complexes in fetal NK cells. Implications for the relationship of NK and T lymphocytes. |journal=J. Immunol. |volume=149 |issue= 6 |pages= 1876-80 |year= 1992 |pmid= 1387664 |doi= }}
*{{cite journal | author=Wong S, Moore S, Orisio S, ''et al.'' |title=Susceptibility to type I diabetes in women is associated with the CD3 epsilon locus on chromosome 11. |journal=Clin. Exp. Immunol. |volume=83 |issue= 1 |pages= 69-73 |year= 1991 |pmid= 1671006 |doi= }}
*{{cite journal | author=Ruegg CL, Strand M |title=A synthetic peptide with sequence identity to the transmembrane protein GP41 of HIV-1 inhibits distinct lymphocyte activation pathways dependent on protein kinase C and intracellular calcium influx. |journal=Cell. Immunol. |volume=137 |issue= 1 |pages= 1-13 |year= 1991 |pmid= 1832084 |doi= }}
*{{cite journal | author=Cefai D, Debre P, Kaczorek M, ''et al.'' |title=Human immunodeficiency virus-1 glycoproteins gp120 and gp160 specifically inhibit the CD3/T cell-antigen receptor phosphoinositide transduction pathway. |journal=J. Clin. Invest. |volume=86 |issue= 6 |pages= 2117-24 |year= 1991 |pmid= 1979339 |doi= }}
*{{cite journal | author=Luzzati AL, Pugliese O, Giacomini E, ''et al.'' |title=Immunoregulatory effect of a synthetic peptide corresponding to a region of protein p24 of HIV. |journal=Folia Biol. (Praha) |volume=36 |issue= 1 |pages= 71-7 |year= 1990 |pmid= 2111780 |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=van den Elsen P, Shepley BA, Cho M, Terhorst C |title=Isolation and characterization of a cDNA clone encoding the murine homologue of the human 20K T3/T-cell receptor glycoprotein. |journal=Nature |volume=314 |issue= 6011 |pages= 542-4 |year= 1985 |pmid= 2859526 |doi= }}
*{{cite journal | author=Gold DP, Puck JM, Pettey CL, ''et al.'' |title=Isolation of cDNA clones encoding the 20K non-glycosylated polypeptide chain of the human T-cell receptor/T3 complex. |journal=Nature |volume=321 |issue= 6068 |pages= 431-4 |year= 1986 |pmid= 3012357 |doi= 10.1038/321431a0 }}
*{{cite journal | author=Clevers HC, Dunlap S, Wileman TE, Terhorst C |title=Human CD3-epsilon gene contains three miniexons and is transcribed from a non-TATA promoter. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 21 |pages= 8156-60 |year= 1988 |pmid= 3267235 |doi= }}
*{{cite journal | author=Gold DP, Clevers H, Alarcon B, ''et al.'' |title=Evolutionary relationship between the T3 chains of the T-cell receptor complex and the immunoglobulin supergene family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 21 |pages= 7649-53 |year= 1987 |pmid= 3478717 |doi= }}
*{{cite journal | author=DeNofrio D, Radcliff G, Weinhold KJ, Denning SM |title=CD3 delta and epsilon gene expression in CD3-CD16+ natural killer cell clones derived from thymic precursors. |journal=Hum. Immunol. |volume=43 |issue= 4 |pages= 283-94 |year= 1996 |pmid= 7499176 |doi= }}
*{{cite journal | author=Kishimoto H, Kubo RT, Yorifuji H, ''et al.'' |title=Physical dissociation of the TCR-CD3 complex accompanies receptor ligation. |journal=J. Exp. Med. |volume=182 |issue= 6 |pages= 1997-2006 |year= 1996 |pmid= 7500045 |doi= }}
*{{cite journal | author=Oravecz T, Norcross MA |title=Costimulatory properties of the human CD4 molecule: enhancement of CD3-induced T cell activation by human immunodeficiency virus type 1 through viral envelope glycoprotein gp120. |journal=AIDS Res. Hum. Retroviruses |volume=9 |issue= 10 |pages= 945-55 |year= 1994 |pmid= 7506554 |doi= }}
*{{cite journal | author=Beecher MS, Baiocchi RA, Linett ML, ''et al.'' |title=Expression of the zeta protein subunit in CD3- NK effectors derived from human thymus. |journal=Cell. Immunol. |volume=155 |issue= 2 |pages= 508-16 |year= 1994 |pmid= 7514106 |doi= 10.1006/cimm.1994.1143 }}
*{{cite journal | author=Luzzati AL, Giacomini E, Giordani L, ''et al.'' |title=An HIV p24 heptapeptide down-regulates antigen-specific responses in vitro interfering at the level of the T3-Ti complex. |journal=Cell. Immunol. |volume=156 |issue= 2 |pages= 286-95 |year= 1994 |pmid= 7517794 |doi= 10.1006/cimm.1994.1175 }}
*{{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=Müller B, Cooper L, Terhorst C |title=Interplay between the human TCR/CD3 epsilon and the B-cell antigen receptor associated Ig-beta (B29). |journal=Immunol. Lett. |volume=44 |issue= 2-3 |pages= 97-103 |year= 1995 |pmid= 7541024 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on COL4A1... {November 15, 2007 4:28:47 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 4:29:23 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
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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_COL4A1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1li1.
| PDB = {{PDB2|1li1}}, {{PDB2|1m3d}}, {{PDB2|1t60}}, {{PDB2|1t61}}
| Name = Collagen, type IV, alpha 1
| HGNCid = 2202
| Symbol = COL4A1
| AltSymbols =; arresten
| OMIM = 120130
| ECnumber =
| Homologene = 20437
| MGIid = 88454
| GeneAtlas_image1 = PBB_GE_COL4A1_211980_at_tn.png
| GeneAtlas_image2 = PBB_GE_COL4A1_211981_at_tn.png
| Function = {{GNF_GO|id=GO:0005201 |text = extracellular matrix structural constituent}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005581 |text = collagen}} {{GNF_GO|id=GO:0005587 |text = collagen type IV}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006817 |text = phosphate transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1282
| Hs_Ensembl = ENSG00000187498
| Hs_RefseqProtein = NP_001836
| Hs_RefseqmRNA = NM_001845
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 13
| Hs_GenLoc_start = 109599311
| Hs_GenLoc_end = 109757505
| Hs_Uniprot = P02462
| Mm_EntrezGene = 12826
| Mm_Ensembl = ENSMUSG00000031502
| Mm_RefseqmRNA = NM_009931
| Mm_RefseqProtein = NP_034061
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 11198403
| Mm_GenLoc_end = 11312702
| Mm_Uniprot = Q3UHJ4
}}
}}
'''Collagen, type IV, alpha 1''', also known as '''COL4A1''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: COL4A1 collagen, type IV, alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1282| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes the major type IV alpha collagen chain of basement membranes. Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another type IV collagen gene so that each gene pair shares a common promoter.<ref>{{cite web | title = Entrez Gene: COL4A1 collagen, type IV, alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1282| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tryggvason K, Soininen R, Hostikka SL, ''et al.'' |title=Structure of the human type IV collagen genes. |journal=Ann. N. Y. Acad. Sci. |volume=580 |issue= |pages= 97-111 |year= 1990 |pmid= 2186699 |doi= }}
*{{cite journal | author=Hinek A |title=Nature and the multiple functions of the 67-kD elastin-/laminin binding protein. |journal=Cell Adhes. Commun. |volume=2 |issue= 3 |pages= 185-93 |year= 1995 |pmid= 7827955 |doi= }}
*{{cite journal | author=Ständer M, Naumann U, Wick W, Weller M |title=Transforming growth factor-beta and p-21: multiple molecular targets of decorin-mediated suppression of neoplastic growth. |journal=Cell Tissue Res. |volume=296 |issue= 2 |pages= 221-7 |year= 1999 |pmid= 10382266 |doi= }}
*{{cite journal | author=Kurpakus Wheater M, Kernacki KA, Hazlett LD |title=Corneal cell proteins and ocular surface pathology. |journal=Biotechnic & histochemistry : official publication of the Biological Stain Commission |volume=74 |issue= 3 |pages= 146-59 |year= 1999 |pmid= 10416788 |doi= }}
*{{cite journal | author=Ghebrehiwet B, Peerschke EI, Hong Y, ''et al.'' |title=Short amino acid sequences derived from C1q receptor (C1q-R) show homology with the alpha chains of fibronectin and vitronectin receptors and collagen type IV. |journal=J. Leukoc. Biol. |volume=51 |issue= 6 |pages= 546-56 |year= 1992 |pmid= 1377218 |doi= }}
*{{cite journal | author=Gupta S, Batchu RB, Datta K |title=Purification, partial characterization of rat kidney hyaluronic acid binding protein and its localization on the cell surface. |journal=Eur. J. Cell Biol. |volume=56 |issue= 1 |pages= 58-67 |year= 1992 |pmid= 1724753 |doi= }}
*{{cite journal | author=Paralkar VM, Nandedkar AK, Pointer RH, ''et al.'' |title=Interaction of osteogenin, a heparin binding bone morphogenetic protein, with type IV collagen. |journal=J. Biol. Chem. |volume=265 |issue= 28 |pages= 17281-4 |year= 1990 |pmid= 2211625 |doi= }}
*{{cite journal | author=Hernandez MR, Igoe F, Neufeld AH |title=Extracellular matrix of the human optic nerve head. |journal=Am. J. Ophthalmol. |volume=102 |issue= 2 |pages= 139-48 |year= 1986 |pmid= 2426947 |doi= }}
*{{cite journal | author=Aumailley M, Wiedemann H, Mann K, Timpl R |title=Binding of nidogen and the laminin-nidogen complex to basement membrane collagen type IV. |journal=Eur. J. Biochem. |volume=184 |issue= 1 |pages= 241-8 |year= 1989 |pmid= 2506015 |doi= }}
*{{cite journal | author=Pihlajaniemi T, Tryggvason K, Myers JC, ''et al.'' |title=cDNA clones coding for the pro-alpha1(IV) chain of human type IV procollagen reveal an unusual homology of amino acid sequences in two halves of the carboxyl-terminal domain. |journal=J. Biol. Chem. |volume=260 |issue= 12 |pages= 7681-7 |year= 1985 |pmid= 2581969 |doi= }}
*{{cite journal | author=Brinker JM, Gudas LJ, Loidl HR, ''et al.'' |title=Restricted homology between human alpha 1 type IV and other procollagen chains. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 11 |pages= 3649-53 |year= 1985 |pmid= 2582422 |doi= }}
*{{cite journal | author=Soininen R, Huotari M, Ganguly A, ''et al.'' |title=Structural organization of the gene for the alpha 1 chain of human type IV collagen. |journal=J. Biol. Chem. |volume=264 |issue= 23 |pages= 13565-71 |year= 1989 |pmid= 2701944 |doi= }}
*{{cite journal | author=Siebold B, Deutzmann R, Kühn K |title=The arrangement of intra- and intermolecular disulfide bonds in the carboxyterminal, non-collagenous aggregation and cross-linking domain of basement-membrane type IV collagen. |journal=Eur. J. Biochem. |volume=176 |issue= 3 |pages= 617-24 |year= 1988 |pmid= 2844531 |doi= }}
*{{cite journal | author=Pöschl E, Pollner R, Kühn K |title=The genes for the alpha 1(IV) and alpha 2(IV) chains of human basement membrane collagen type IV are arranged head-to-head and separated by a bidirectional promoter of unique structure. |journal=EMBO J. |volume=7 |issue= 9 |pages= 2687-95 |year= 1988 |pmid= 2846280 |doi= }}
*{{cite journal | author=Bowcock AM, Hebert JM, Christiano AM, ''et al.'' |title=The pro alpha 1 (IV) collagen gene is linked to the D13S3 locus at the distal end of human chromosome 13q. |journal=Cytogenet. Cell Genet. |volume=45 |issue= 3-4 |pages= 234-6 |year= 1988 |pmid= 2891465 |doi= }}
*{{cite journal | author=Solomon E, Hiorns LR, Spurr N, ''et al.'' |title=Chromosomal assignments of the genes coding for human types II, III, and IV collagen: a dispersed gene family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 10 |pages= 3330-4 |year= 1985 |pmid= 2987919 |doi= }}
*{{cite journal | author=Soininen R, Huotari M, Hostikka SL, ''et al.'' |title=The structural genes for alpha 1 and alpha 2 chains of human type IV collagen are divergently encoded on opposite DNA strands and have an overlapping promoter region. |journal=J. Biol. Chem. |volume=263 |issue= 33 |pages= 17217-20 |year= 1988 |pmid= 3182844 |doi= }}
*{{cite journal | author=Brazel D, Oberbäumer I, Dieringer H, ''et al.'' |title=Completion of the amino acid sequence of the alpha 1 chain of human basement membrane collagen (type IV) reveals 21 non-triplet interruptions located within the collagenous domain. |journal=Eur. J. Biochem. |volume=168 |issue= 3 |pages= 529-36 |year= 1987 |pmid= 3311751 |doi= }}
*{{cite journal | author=Soininen R, Haka-Risku T, Prockop DJ, Tryggvason K |title=Complete primary structure of the alpha 1-chain of human basement membrane (type IV) collagen. |journal=FEBS Lett. |volume=225 |issue= 1-2 |pages= 188-94 |year= 1988 |pmid= 3691802 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on COL4A3... {November 15, 2007 4:29:23 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 4:30:04 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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| 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 = Collagen, type IV, alpha 3 (Goodpasture antigen)
| HGNCid = 2204
| Symbol = COL4A3
| AltSymbols =;
| OMIM = 120070
| ECnumber =
| Homologene = 68033
| MGIid = 104688
| GeneAtlas_image1 = PBB_GE_COL4A3_214641_at_tn.png
| GeneAtlas_image2 = PBB_GE_COL4A3_216893_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_COL4A3_222073_at_tn.png
| Function = {{GNF_GO|id=GO:0005178 |text = integrin binding}} {{GNF_GO|id=GO:0005201 |text = extracellular matrix structural constituent}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008191 |text = metalloendopeptidase inhibitor activity}}
| Component = {{GNF_GO|id=GO:0005581 |text = collagen}} {{GNF_GO|id=GO:0005587 |text = collagen type IV}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006817 |text = phosphate transport}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0006919 |text = caspase activation}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0008015 |text = circulation}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0016525 |text = negative regulation of angiogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1285
| Hs_Ensembl = ENSG00000169031
| Hs_RefseqProtein = NP_000082
| Hs_RefseqmRNA = NM_000091
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 227810928
| Hs_GenLoc_end = 227884953
| Hs_Uniprot = Q01955
| Mm_EntrezGene = 12828
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_007734
| Mm_RefseqProtein = NP_031760
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Collagen, type IV, alpha 3 (Goodpasture antigen)''', also known as '''COL4A3''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: COL4A3 collagen, type IV, alpha 3 (Goodpasture antigen)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1285| 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 = Type IV collagen, the major structural component of basement membranes, is a multimeric protein composed of 3 alpha subunits. These subunits are encoded by 6 different genes, alpha 1 through alpha 6, each of which can form a triple helix structure with 2 other subunits to form type IV collagen. This gene encodes alpha 3. In the Goodpasture syndrome, autoantibodies bind to the collagen molecules in the basement membranes of alveoli and glomeruli. The epitopes that elicit these autoantibodies are localized largely to the non-collagenous C-terminal domain of the protein. A specific kinase phosphorylates amino acids in this same C-terminal region and the expression of this kinase is upregulated during pathogenesis. There are multiple alternate transcripts that appear to be unique to this human alpha 3 gene and alternate splicing is restricted to the six exons that encode this C-terminal domain. This gene is also linked to an autosomal recessive form of Alport syndrome. The mutations contributing to this syndrome are also located within the exons that encode this C-terminal region. Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another type IV collagen gene so that each gene pair shares a common promoter. Some exons of this gene are interspersed with exons of an uncharacterized gene which is on the opposite strand.<ref>{{cite web | title = Entrez Gene: COL4A3 collagen, type IV, alpha 3 (Goodpasture antigen)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1285| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hinek A |title=Nature and the multiple functions of the 67-kD elastin-/laminin binding protein. |journal=Cell Adhes. Commun. |volume=2 |issue= 3 |pages= 185-93 |year= 1995 |pmid= 7827955 |doi= }}
*{{cite journal | author=Ständer M, Naumann U, Wick W, Weller M |title=Transforming growth factor-beta and p-21: multiple molecular targets of decorin-mediated suppression of neoplastic growth. |journal=Cell Tissue Res. |volume=296 |issue= 2 |pages= 221-7 |year= 1999 |pmid= 10382266 |doi= }}
*{{cite journal | author=Kurpakus Wheater M, Kernacki KA, Hazlett LD |title=Corneal cell proteins and ocular surface pathology. |journal=Biotechnic & histochemistry : official publication of the Biological Stain Commission |volume=74 |issue= 3 |pages= 146-59 |year= 1999 |pmid= 10416788 |doi= }}
*{{cite journal | author=Pescucci C, Longo I, Bruttini M, ''et al.'' |title=Type-IV collagen related diseases. |journal=J. Nephrol. |volume=16 |issue= 2 |pages= 314-6 |year= 2003 |pmid= 12768082 |doi= }}
*{{cite journal | author=Torra R, Tazón-Vega B, Ars E, Ballarín J |title=Collagen type IV (alpha3-alpha4) nephropathy: from isolated haematuria to renal failure. |journal=Nephrol. Dial. Transplant. |volume=19 |issue= 10 |pages= 2429-32 |year= 2005 |pmid= 15280517 |doi= 10.1093/ndt/gfh435 }}
*{{cite journal | author=Rana K, Wang YY, Buzza M, ''et al.'' |title=The genetics of thin basement membrane nephropathy. |journal=Semin. Nephrol. |volume=25 |issue= 3 |pages= 163-70 |year= 2005 |pmid= 15880327 |doi= }}
*{{cite journal | author=Maziers N, Dahan K, Pirson Y |title=[From Alport syndrome to benign familial hematuria: clinical and genetic aspect] |journal=Nephrol. Ther. |volume=1 |issue= 2 |pages= 90-100 |year= 2006 |pmid= 16895672 |doi= 10.1016/j.nephro.2005.03.005 }}
*{{cite journal | author=Ghebrehiwet B, Peerschke EI, Hong Y, ''et al.'' |title=Short amino acid sequences derived from C1q receptor (C1q-R) show homology with the alpha chains of fibronectin and vitronectin receptors and collagen type IV. |journal=J. Leukoc. Biol. |volume=51 |issue= 6 |pages= 546-56 |year= 1992 |pmid= 1377218 |doi= }}
*{{cite journal | author=Quinones S, Bernal D, García-Sogo M, ''et al.'' |title=Exon/intron structure of the human alpha 3(IV) gene encompassing the Goodpasture antigen (alpha 3(IV)NC1). Identification of a potentially antigenic region at the triple helix/NC1 domain junction. |journal=J. Biol. Chem. |volume=267 |issue= 28 |pages= 19780-4 |year= 1992 |pmid= 1400291 |doi= }}
*{{cite journal | author=Gupta S, Batchu RB, Datta K |title=Purification, partial characterization of rat kidney hyaluronic acid binding protein and its localization on the cell surface. |journal=Eur. J. Cell Biol. |volume=56 |issue= 1 |pages= 58-67 |year= 1992 |pmid= 1724753 |doi= }}
*{{cite journal | author=Turner N, Mason PJ, Brown R, ''et al.'' |title=Molecular cloning of the human Goodpasture antigen demonstrates it to be the alpha 3 chain of type IV collagen. |journal=J. Clin. Invest. |volume=89 |issue= 2 |pages= 592-601 |year= 1992 |pmid= 1737849 |doi= }}
*{{cite journal | author=Morrison KE, Mariyama M, Yang-Feng TL, Reeders ST |title=Sequence and localization of a partial cDNA encoding the human alpha 3 chain of type IV collagen. |journal=Am. J. Hum. Genet. |volume=49 |issue= 3 |pages= 545-54 |year= 1991 |pmid= 1882840 |doi= }}
*{{cite journal | author=Hernandez MR, Igoe F, Neufeld AH |title=Extracellular matrix of the human optic nerve head. |journal=Am. J. Ophthalmol. |volume=102 |issue= 2 |pages= 139-48 |year= 1986 |pmid= 2426947 |doi= }}
*{{cite journal | author=Griffin CA, Emanuel BS, Hansen JR, ''et al.'' |title=Human collagen genes encoding basement membrane alpha 1 (IV) and alpha 2 (IV) chains map to the distal long arm of chromosome 13. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 2 |pages= 512-6 |year= 1987 |pmid= 3025878 |doi= }}
*{{cite journal | author=Murata K, Motayama T, Kotake C |title=Collagen types in various layers of the human aorta and their changes with the atherosclerotic process. |journal=Atherosclerosis |volume=60 |issue= 3 |pages= 251-62 |year= 1986 |pmid= 3089234 |doi= }}
*{{cite journal | author=Glant TT, Hadházy C, Mikecz K, Sipos A |title=Appearance and persistence of fibronectin in cartilage. Specific interaction of fibronectin with collagen type II. |journal=Histochemistry |volume=82 |issue= 2 |pages= 149-58 |year= 1985 |pmid= 3997552 |doi= }}
*{{cite journal | author=Uscanga L, Kennedy RH, Stocker S, ''et al.'' |title=Immunolocalization of collagen types, laminin and fibronectin in the normal human pancreas. |journal=Digestion |volume=30 |issue= 3 |pages= 158-64 |year= 1984 |pmid= 6389236 |doi= }}
*{{cite journal | author=Sundarraj N, Willson J |title=Monoclonal antibody to human basement membrane collagen type IV. |journal=Immunology |volume=47 |issue= 1 |pages= 133-40 |year= 1982 |pmid= 6811420 |doi= }}
*{{cite journal | author=Hahn E, Wick G, Pencev D, Timpl R |title=Distribution of basement membrane proteins in normal and fibrotic human liver: collagen type IV, laminin, and fibronectin. |journal=Gut |volume=21 |issue= 1 |pages= 63-71 |year= 1980 |pmid= 6988303 |doi= }}
*{{cite journal | author=Singhal PC, Sharma P, Garg P |title=HIV-1 gp160 protein-macrophage interactions modulate mesangial cell proliferation and matrix synthesis. |journal=Am. J. Pathol. |volume=147 |issue= 6 |pages= 1780-9 |year= 1996 |pmid= 7495302 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on COX2... {November 15, 2007 4:38:01 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 4:38:31 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Cytochrome c oxidase subunit II
| HGNCid = 7421
| Symbol = COX2
| AltSymbols =; MTCO2
| OMIM =
| ECnumber =
| Homologene = 5017
| MGIid = 102503
| Function = {{GNF_GO|id=GO:0004129 |text = cytochrome-c oxidase activity}} {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005746 |text = mitochondrial respiratory chain}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006123 |text = mitochondrial electron transport, cytochrome c to oxygen}} {{GNF_GO|id=GO:0006810 |text = transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4513
| Hs_Ensembl = ENSG00000198712
| Hs_RefseqProtein = NP_536846
| Hs_RefseqmRNA =
| Hs_GenLoc_db =
| Hs_GenLoc_chr = MT
| Hs_GenLoc_start = 7587
| Hs_GenLoc_end = 8270
| Hs_Uniprot = P00403
| Mm_EntrezGene = 17709
| Mm_Ensembl = ENSMUSG00000064354
| Mm_RefseqmRNA =
| Mm_RefseqProtein = NP_904331
| Mm_GenLoc_db =
| Mm_GenLoc_chr = MT
| Mm_GenLoc_start = 7013
| Mm_GenLoc_end = 7696
| Mm_Uniprot = Q7JCZ1
}}
}}
'''Cytochrome c oxidase subunit II''', also known as '''COX2''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: COX2 cytochrome c oxidase subunit II| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4513| 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=Torroni A, Achilli A, Macaulay V, ''et al.'' |title=Harvesting the fruit of the human mtDNA tree. |journal=Trends Genet. |volume=22 |issue= 6 |pages= 339-45 |year= 2006 |pmid= 16678300 |doi= 10.1016/j.tig.2006.04.001 }}
*{{cite journal | author=Barrell BG, Bankier AT, Drouin J |title=A different genetic code in human mitochondria. |journal=Nature |volume=282 |issue= 5735 |pages= 189-94 |year= 1979 |pmid= 226894 |doi= }}
*{{cite journal | author=Bodenteich A, Mitchell LG, Polymeropoulos MH, Merril CR |title=Dinucleotide repeat in the human mitochondrial D-loop. |journal=Hum. Mol. Genet. |volume=1 |issue= 2 |pages= 140 |year= 1993 |pmid= 1301157 |doi= }}
*{{cite journal | author=Lu X, Walker T, MacManus JP, Seligy VL |title=Differentiation of HT-29 human colonic adenocarcinoma cells correlates with increased expression of mitochondrial RNA: effects of trehalose on cell growth and maturation. |journal=Cancer Res. |volume=52 |issue= 13 |pages= 3718-25 |year= 1992 |pmid= 1377597 |doi= }}
*{{cite journal | author=Marzuki S, Noer AS, Lertrit P, ''et al.'' |title=Normal variants of human mitochondrial DNA and translation products: the building of a reference data base. |journal=Hum. Genet. |volume=88 |issue= 2 |pages= 139-45 |year= 1992 |pmid= 1757091 |doi= }}
*{{cite journal | author=Moraes CT, Andreetta F, Bonilla E, ''et al.'' |title=Replication-competent human mitochondrial DNA lacking the heavy-strand promoter region. |journal=Mol. Cell. Biol. |volume=11 |issue= 3 |pages= 1631-7 |year= 1991 |pmid= 1996112 |doi= }}
*{{cite journal | author=Power MD, Kiefer MC, Barr PJ, Reeves R |title=Nucleotide sequence of human mitochondrial cytochrome c oxidase II cDNA. |journal=Nucleic Acids Res. |volume=17 |issue= 16 |pages= 6734 |year= 1989 |pmid= 2550900 |doi= }}
*{{cite journal | author=Attardi G, Chomyn A, Doolittle RF, ''et al.'' |title=Seven unidentified reading frames of human mitochondrial DNA encode subunits of the respiratory chain NADH dehydrogenase. |journal=Cold Spring Harb. Symp. Quant. Biol. |volume=51 Pt 1 |issue= |pages= 103-14 |year= 1987 |pmid= 3472707 |doi= }}
*{{cite journal | author=Chomyn A, Cleeter MW, Ragan CI, ''et al.'' |title=URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit. |journal=Science |volume=234 |issue= 4776 |pages= 614-8 |year= 1986 |pmid= 3764430 |doi= }}
*{{cite journal | author=Chomyn A, Mariottini P, Cleeter MW, ''et al.'' |title=Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase. |journal=Nature |volume=314 |issue= 6012 |pages= 592-7 |year= 1985 |pmid= 3921850 |doi= }}
*{{cite journal | author=Anderson S, Bankier AT, Barrell BG, ''et al.'' |title=Sequence and organization of the human mitochondrial genome. |journal=Nature |volume=290 |issue= 5806 |pages= 457-65 |year= 1981 |pmid= 7219534 |doi= }}
*{{cite journal | author=Montoya J, Ojala D, Attardi G |title=Distinctive features of the 5'-terminal sequences of the human mitochondrial mRNAs. |journal=Nature |volume=290 |issue= 5806 |pages= 465-70 |year= 1981 |pmid= 7219535 |doi= }}
*{{cite journal | author=Horai S, Hayasaka K, Kondo R, ''et al.'' |title=Recent African origin of modern humans revealed by complete sequences of hominoid mitochondrial DNAs. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 2 |pages= 532-6 |year= 1995 |pmid= 7530363 |doi= }}
*{{cite journal | author=Ruvolo M, Zehr S, von Dornum M, ''et al.'' |title=Mitochondrial COII sequences and modern human origins. |journal=Mol. Biol. Evol. |volume=10 |issue= 6 |pages= 1115-35 |year= 1994 |pmid= 8277847 |doi= }}
*{{cite journal | author=Polyak K, Li Y, Zhu H, ''et al.'' |title=Somatic mutations of the mitochondrial genome in human colorectal tumours. |journal=Nat. Genet. |volume=20 |issue= 3 |pages= 291-3 |year= 1998 |pmid= 9806551 |doi= 10.1038/3108 }}
*{{cite journal | author=Kato MV |title=The mechanisms of death of an erythroleukemic cell line by p53: involvement of the microtubule and mitochondria. |journal=Leuk. Lymphoma |volume=33 |issue= 1-2 |pages= 181-6 |year= 1999 |pmid= 10194136 |doi= }}
*{{cite journal | author=Andrews RM, Kubacka I, Chinnery PF, ''et al.'' |title=Reanalysis and revision of the Cambridge reference sequence for human mitochondrial DNA. |journal=Nat. Genet. |volume=23 |issue= 2 |pages= 147 |year= 1999 |pmid= 10508508 |doi= 10.1038/13779 }}
*{{cite journal | author=Ingman M, Kaessmann H, Pääbo S, Gyllensten U |title=Mitochondrial genome variation and the origin of modern humans. |journal=Nature |volume=408 |issue= 6813 |pages= 708-13 |year= 2001 |pmid= 11130070 |doi= 10.1038/35047064 }}
*{{cite journal | author=Finnilä S, Lehtonen MS, Majamaa K |title=Phylogenetic network for European mtDNA. |journal=Am. J. Hum. Genet. |volume=68 |issue= 6 |pages= 1475-84 |year= 2001 |pmid= 11349229 |doi= }}
*{{cite journal | author=Maca-Meyer N, González AM, Larruga JM, ''et al.'' |title=Major genomic mitochondrial lineages delineate early human expansions. |journal=BMC Genet. |volume=2 |issue= |pages= 13 |year= 2003 |pmid= 11553319 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CYP1A2... {November 15, 2007 4:30:04 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 4:30:36 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
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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_CYP1A2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2hi4.
| PDB = {{PDB2|2hi4}}
| Name = Cytochrome P450, family 1, subfamily A, polypeptide 2
| HGNCid = 2596
| Symbol = CYP1A2
| AltSymbols =; CP12; P3-450; P450(PA)
| OMIM = 124060
| ECnumber =
| Homologene = 68082
| MGIid = 88589
| GeneAtlas_image1 = PBB_GE_CYP1A2_207609_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CYP1A2_207608_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0009055 |text = electron carrier activity}} {{GNF_GO|id=GO:0019825 |text = oxygen binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0050381 |text = unspecific monooxygenase activity}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1544
| Hs_Ensembl = ENSG00000140505
| Hs_RefseqProtein = NP_000752
| Hs_RefseqmRNA = NM_000761
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 72828237
| Hs_GenLoc_end = 72835994
| Hs_Uniprot = P05177
| Mm_EntrezGene = 13077
| Mm_Ensembl = ENSMUSG00000032310
| Mm_RefseqmRNA = NM_009993
| Mm_RefseqProtein = NP_034123
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 57475074
| Mm_GenLoc_end = 57481792
| Mm_Uniprot = P00186
}}
}}
'''Cytochrome P450, family 1, subfamily A, polypeptide 2''', also known as '''CYP1A2''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: CYP1A2 cytochrome P450, family 1, subfamily A, polypeptide 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1544| 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 cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. The protein encoded by this gene localizes to the endoplasmic reticulum and its expression is induced by some polycyclic aromatic hydrocarbons (PAHs), some of which are found in cigarette smoke. The enzyme's endogenous substrate is unknown; however, it is able to metabolize some PAHs to carcinogenic intermediates. Other xenobiotic substrates for this enzyme include caffeine, aflatoxin B1, and acetaminophen. The transcript from this gene contains four Alu sequences flanked by direct repeats in the 3' untranslated region.<ref>{{cite web | title = Entrez Gene: CYP1A2 cytochrome P450, family 1, subfamily A, polypeptide 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1544| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Smith G, Stubbins MJ, Harries LW, Wolf CR |title=Molecular genetics of the human cytochrome P450 monooxygenase superfamily. |journal=Xenobiotica |volume=28 |issue= 12 |pages= 1129-65 |year= 1999 |pmid= 9890157 |doi= }}
*{{cite journal | author=Landi MT, Sinha R, Lang NP, Kadlubar FF |title=Human cytochrome P4501A2. |journal=IARC Sci. Publ. |volume= |issue= 148 |pages= 173-95 |year= 1999 |pmid= 10493258 |doi= }}
*{{cite journal | author=Nelson DR, Zeldin DC, Hoffman SM, ''et al.'' |title=Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants. |journal=Pharmacogenetics |volume=14 |issue= 1 |pages= 1-18 |year= 2004 |pmid= 15128046 |doi= }}
*{{cite journal | author=Ikeya K, Jaiswal AK, Owens RA, ''et al.'' |title=Human CYP1A2: sequence, gene structure, comparison with the mouse and rat orthologous gene, and differences in liver 1A2 mRNA expression. |journal=Mol. Endocrinol. |volume=3 |issue= 9 |pages= 1399-408 |year= 1990 |pmid= 2575218 |doi= }}
*{{cite journal | author=Butler MA, Iwasaki M, Guengerich FP, Kadlubar FF |title=Human cytochrome P-450PA (P-450IA2), the phenacetin O-deethylase, is primarily responsible for the hepatic 3-demethylation of caffeine and N-oxidation of carcinogenic arylamines. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 20 |pages= 7696-700 |year= 1989 |pmid= 2813353 |doi= }}
*{{cite journal | author=Quattrochi LC, Okino ST, Pendurthi UR, Tukey RH |title=Cloning and isolation of human cytochrome P-450 cDNAs homologous to dioxin-inducible rabbit mRNAs encoding P-450 4 and P-450 6. |journal=DNA |volume=4 |issue= 5 |pages= 395-400 |year= 1986 |pmid= 3000715 |doi= }}
*{{cite journal | author=Quattrochi LC, Pendurthi UR, Okino ST, ''et al.'' |title=Human cytochrome P-450 4 mRNA and gene: part of a multigene family that contains Alu sequences in its mRNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 18 |pages= 6731-5 |year= 1986 |pmid= 3462722 |doi= }}
*{{cite journal | author=Wrighton SA, Campanile C, Thomas PE, ''et al.'' |title=Identification of a human liver cytochrome P-450 homologous to the major isosafrole-inducible cytochrome P-450 in the rat. |journal=Mol. Pharmacol. |volume=29 |issue= 4 |pages= 405-10 |year= 1986 |pmid= 3517618 |doi= }}
*{{cite journal | author=Jaiswal AK, Nebert DW, McBride OW, Gonzalez FJ |title=Human P(3)450: cDNA and complete protein sequence, repetitive Alu sequences in the 3' nontranslated region, and localization of gene to chromosome 15. |journal=J. Exp. Pathol. |volume=3 |issue= 1 |pages= 1-17 |year= 1988 |pmid= 3681487 |doi= }}
*{{cite journal | author=Jaiswal AK, Nebert DW, Gonzalez FJ |title=Human P3(450): cDNA and complete amino acid sequence. |journal=Nucleic Acids Res. |volume=14 |issue= 16 |pages= 6773-4 |year= 1986 |pmid= 3755823 |doi= }}
*{{cite journal | author=Eugster HP, Probst M, Würgler FE, Sengstag C |title=Caffeine, estradiol, and progesterone interact with human CYP1A1 and CYP1A2. Evidence from cDNA-directed expression in Saccharomyces cerevisiae. |journal=Drug Metab. Dispos. |volume=21 |issue= 1 |pages= 43-9 |year= 1993 |pmid= 8095225 |doi= }}
*{{cite journal | author=Schweikl H, Taylor JA, Kitareewan S, ''et al.'' |title=Expression of CYP1A1 and CYP1A2 genes in human liver. |journal=Pharmacogenetics |volume=3 |issue= 5 |pages= 239-49 |year= 1994 |pmid= 8287062 |doi= }}
*{{cite journal | author=Yamazaki H, Inoue K, Mimura M, ''et al.'' |title=7-Ethoxycoumarin O-deethylation catalyzed by cytochromes P450 1A2 and 2E1 in human liver microsomes. |journal=Biochem. Pharmacol. |volume=51 |issue= 3 |pages= 313-9 |year= 1996 |pmid= 8573198 |doi= }}
*{{cite journal | author=Hakkola J, Raunio H, Purkunen R, ''et al.'' |title=Detection of cytochrome P450 gene expression in human placenta in first trimester of pregnancy. |journal=Biochem. Pharmacol. |volume=52 |issue= 2 |pages= 379-83 |year= 1996 |pmid= 8694864 |doi= }}
*{{cite journal | author=Guengerich FP, Johnson WW |title=Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: rapid reduction in the absence of substrate and variations among cytochrome P450 systems. |journal=Biochemistry |volume=36 |issue= 48 |pages= 14741-50 |year= 1998 |pmid= 9398194 |doi= 10.1021/bi9719399 }}
*{{cite journal | author=Wacke R, Kirchner A, Prall F, ''et al.'' |title=Up-regulation of cytochrome P450 1A2, 2C9, and 2E1 in chronic pancreatitis. |journal=Pancreas |volume=16 |issue= 4 |pages= 521-8 |year= 1998 |pmid= 9598815 |doi= }}
*{{cite journal | author=Macé K, Bowman ED, Vautravers P, ''et al.'' |title=Characterisation of xenobiotic-metabolising enzyme expression in human bronchial mucosa and peripheral lung tissues. |journal=Eur. J. Cancer |volume=34 |issue= 6 |pages= 914-20 |year= 1998 |pmid= 9797707 |doi= }}
*{{cite journal | author=Huang JD, Guo WC, Lai MD, ''et al.'' |title=Detection of a novel cytochrome P-450 1A2 polymorphism (F21L) in Chinese. |journal=Drug Metab. Dispos. |volume=27 |issue= 1 |pages= 98-101 |year= 1999 |pmid= 9884316 |doi= }}
*{{cite journal | author=Tatemichi M, Nomura S, Ogura T, ''et al.'' |title=Mutagenic activation of environmental carcinogens by microsomes of gastric mucosa with intestinal metaplasia. |journal=Cancer Res. |volume=59 |issue= 16 |pages= 3893-8 |year= 1999 |pmid= 10463577 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CYP2C19... {November 15, 2007 4:30:36 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 4:31:40 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| 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_CYP2C19_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1r9o.
| PDB = {{PDB2|1r9o}}
| Name = Cytochrome P450, family 2, subfamily C, polypeptide 19
| HGNCid = 2621
| Symbol = CYP2C19
| AltSymbols =; CPCJ; CYP 2C; CYP2C; P450C2C; P450IIC19
| OMIM = 124020
| ECnumber =
| Homologene = 86659
| MGIid = 1306818
| GeneAtlas_image1 = PBB_GE_CYP2C19_216058_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004497 |text = monooxygenase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0016712 |text = oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen}} {{GNF_GO|id=GO:0018675 |text = (S)-limonene 6-monooxygenase activity}} {{GNF_GO|id=GO:0018676 |text = (S)-limonene 7-monooxygenase activity}} {{GNF_GO|id=GO:0019825 |text = oxygen binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1557
| Hs_Ensembl = ENSG00000165841
| Hs_RefseqProtein = NP_000760
| Hs_RefseqmRNA = NM_000769
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 96512371
| Hs_GenLoc_end = 96603007
| Hs_Uniprot = P33261
| Mm_EntrezGene = 13098
| Mm_Ensembl = ENSMUSG00000025003
| Mm_RefseqmRNA = NM_010003
| Mm_RefseqProtein = NP_034133
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 39564182
| Mm_GenLoc_end = 39621840
| Mm_Uniprot = Q6PER7
}}
}}
'''Cytochrome P450, family 2, subfamily C, polypeptide 19''', also known as '''CYP2C19''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: CYP2C19 cytochrome P450, family 2, subfamily C, polypeptide 19| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1557| 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 cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum and is known to metabolize many xenobiotics, including the anticonvulsive drug mephenytoin, omeprazole, diazepam and some barbiturates. Polymorphism within this gene is associated with variable ability to metabolize mephenytoin, known as the poor metabolizer and extensive metabolizer phenotypes. The gene is located within a cluster of cytochrome P450 genes on chromosome 10q24.<ref>{{cite web | title = Entrez Gene: CYP2C19 cytochrome P450, family 2, subfamily C, polypeptide 19| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1557| accessdate = }}</ref>
}}
==References==
{{reflist}}
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DIABLO... {November 15, 2007 4:44:44 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 4:45:34 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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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_DIABLO_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1few.
| PDB = {{PDB2|1few}}, {{PDB2|1g73}}
| Name = Diablo homolog (Drosophila)
| HGNCid = 21528
| Symbol = DIABLO
| AltSymbols =; DIABLO-S; FLJ10537; FLJ25049; SMAC; SMAC3
| OMIM = 605219
| ECnumber =
| Homologene = 10532
| MGIid = 1913843
| GeneAtlas_image1 = PBB_GE_DIABLO_219350_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}}
| Process = {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0008625 |text = induction of apoptosis via death domain receptors}} {{GNF_GO|id=GO:0008631 |text = induction of apoptosis by oxidative stress}} {{GNF_GO|id=GO:0008635 |text = caspase activation via cytochrome c}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 56616
| Hs_Ensembl = ENSG00000184047
| Hs_RefseqProtein = NP_063940
| Hs_RefseqmRNA = NM_019887
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 121258163
| Hs_GenLoc_end = 121277973
| Hs_Uniprot = Q9NR28
| Mm_EntrezGene = 66593
| Mm_Ensembl = ENSMUSG00000029433
| Mm_RefseqmRNA = NM_023232
| Mm_RefseqProtein = NP_075721
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 123773129
| Mm_GenLoc_end = 123784782
| Mm_Uniprot = Q542V8
}}
}}
'''Diablo homolog (Drosophila)''', also known as '''DIABLO''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: DIABLO diablo homolog (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=56616| 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 inhibitor of apoptosis protein (IAP)-binding protein. The encoded mitochondrial protein enters the cytosol when cells undergo apoptosis, and it moderates the caspase inhibition of IAPs. Multiple polyadenylation sites have been found for this gene. Several alternatively spliced transcript variants that encode distinct isoforms have been described for this gene but the validity of some transcripts, and their predicted ORFs, has not been determined conclusively.<ref>{{cite web | title = Entrez Gene: DIABLO diablo homolog (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=56616| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Shi Y |title=A structural view of mitochondria-mediated apoptosis. |journal=Nat. Struct. Biol. |volume=8 |issue= 5 |pages= 394-401 |year= 2001 |pmid= 11323712 |doi= 10.1038/87548 }}
*{{cite journal | author=Anguiano-Hernandez YM, Chartier A, Huerta S |title=Smac/DIABLO and colon cancer. |journal=Anti-cancer agents in medicinal chemistry |volume=7 |issue= 4 |pages= 467-73 |year= 2007 |pmid= 17630921 |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=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=Hillier LD, Lennon G, Becker M, ''et al.'' |title=Generation and analysis of 280,000 human expressed sequence tags. |journal=Genome Res. |volume=6 |issue= 9 |pages= 807-28 |year= 1997 |pmid= 8889549 |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=Du C, Fang M, Li Y, ''et al.'' |title=Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. |journal=Cell |volume=102 |issue= 1 |pages= 33-42 |year= 2000 |pmid= 10929711 |doi= }}
*{{cite journal | author=Verhagen AM, Ekert PG, Pakusch M, ''et al.'' |title=Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. |journal=Cell |volume=102 |issue= 1 |pages= 43-53 |year= 2000 |pmid= 10929712 |doi= }}
*{{cite journal | author=Srinivasula SM, Datta P, Fan XJ, ''et al.'' |title=Molecular determinants of the caspase-promoting activity of Smac/DIABLO and its role in the death receptor pathway. |journal=J. Biol. Chem. |volume=275 |issue= 46 |pages= 36152-7 |year= 2000 |pmid= 10950947 |doi= 10.1074/jbc.C000533200 }}
*{{cite journal | author=Chai J, Du C, Wu JW, ''et al.'' |title=Structural and biochemical basis of apoptotic activation by Smac/DIABLO. |journal=Nature |volume=406 |issue= 6798 |pages= 855-62 |year= 2000 |pmid= 10972280 |doi= 10.1038/35022514 }}
*{{cite journal | author=Liu Z, Sun C, Olejniczak ET, ''et al.'' |title=Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain. |journal=Nature |volume=408 |issue= 6815 |pages= 1004-8 |year= 2001 |pmid= 11140637 |doi= 10.1038/35050006 }}
*{{cite journal | author=Wu G, Chai J, Suber TL, ''et al.'' |title=Structural basis of IAP recognition by Smac/DIABLO. |journal=Nature |volume=408 |issue= 6815 |pages= 1008-12 |year= 2001 |pmid= 11140638 |doi= 10.1038/35050012 }}
*{{cite journal | author=Srinivasula SM, Hegde R, Saleh A, ''et al.'' |title=A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis. |journal=Nature |volume=410 |issue= 6824 |pages= 112-6 |year= 2001 |pmid= 11242052 |doi= 10.1038/35065125 }}
*{{cite journal | author=Huang Y, Park YC, Rich RL, ''et al.'' |title=Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain. |journal=Cell |volume=104 |issue= 5 |pages= 781-90 |year= 2001 |pmid= 11257231 |doi= }}
*{{cite journal | author=Roberts DL, Merrison W, MacFarlane M, Cohen GM |title=The inhibitor of apoptosis protein-binding domain of Smac is not essential for its proapoptotic activity. |journal=J. Cell Biol. |volume=153 |issue= 1 |pages= 221-8 |year= 2001 |pmid= 11285287 |doi= }}
*{{cite journal | author=Verhagen AM, Silke J, Ekert PG, ''et al.'' |title=HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins. |journal=J. Biol. Chem. |volume=277 |issue= 1 |pages= 445-54 |year= 2002 |pmid= 11604410 |doi= 10.1074/jbc.M109891200 }}
*{{cite journal | author=Adrain C, Creagh EM, Martin SJ |title=Apoptosis-associated release of Smac/DIABLO from mitochondria requires active caspases and is blocked by Bcl-2. |journal=EMBO J. |volume=20 |issue= 23 |pages= 6627-36 |year= 2002 |pmid= 11726499 |doi= 10.1093/emboj/20.23.6627 }}
*{{cite journal | author=Sun XM, Bratton SB, Butterworth M, ''et al.'' |title=Bcl-2 and Bcl-xL inhibit CD95-mediated apoptosis by preventing mitochondrial release of Smac/DIABLO and subsequent inactivation of X-linked inhibitor-of-apoptosis protein. |journal=J. Biol. Chem. |volume=277 |issue= 13 |pages= 11345-51 |year= 2002 |pmid= 11801595 |doi= 10.1074/jbc.M109893200 }}
*{{cite journal | author=Vucic D, Deshayes K, Ackerly H, ''et al.'' |title=SMAC negatively regulates the anti-apoptotic activity of melanoma inhibitor of apoptosis (ML-IAP). |journal=J. Biol. Chem. |volume=277 |issue= 14 |pages= 12275-9 |year= 2002 |pmid= 11801603 |doi= 10.1074/jbc.M112045200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DMPK... {November 15, 2007 4:31:40 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 4:33:34 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
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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_DMPK_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1wt6.
| PDB = {{PDB2|1wt6}}
| Name = Dystrophia myotonica-protein kinase
| HGNCid = 2933
| Symbol = DMPK
| AltSymbols =; DM; DM1; DM1PK; DMK; MDPK; MT-PK
| OMIM = 605377
| ECnumber =
| Homologene = 3247
| MGIid = 94906
| GeneAtlas_image1 = PBB_GE_DMPK_37996_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_DMPK_217066_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_DMPK_217661_x_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:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component =
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006936 |text = muscle contraction}} {{GNF_GO|id=GO:0008016 |text = regulation of heart contraction}} {{GNF_GO|id=GO:0051056 |text = regulation of small GTPase mediated signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1760
| Hs_Ensembl = ENSG00000104936
| Hs_RefseqProtein = NP_001075029
| Hs_RefseqmRNA = NM_001081560
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 50965579
| Hs_GenLoc_end = 50977469
| Hs_Uniprot = Q09013
| Mm_EntrezGene = 13400
| Mm_Ensembl = ENSMUSG00000030409
| Mm_RefseqmRNA = XM_986224
| Mm_RefseqProtein = XP_991318
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 18242463
| Mm_GenLoc_end = 18252340
| Mm_Uniprot = Q05CL1
}}
}}
'''Dystrophia myotonica-protein kinase''', also known as '''DMPK''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: DMPK dystrophia myotonica-protein kinase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1760| 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 serine-threonine kinase that is closely related to other kinases that interact with members of the Rho family of small GTPases. Substrates for this enzyme include myogenin, the beta-subunit of the L-type calcium channels, and phospholemman. The 3' untranslated region of this gene contains 5-37 copies of a CTG trinucleotide repeat. Expansion of this unstable motif to 50-5,000 copies causes myotonic dystrophy type I, which increases in severity with increasing repeat element copy number. Repeat expansion is associated with condensation of local chromatin structure that disrupts the expression of genes in this region. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined.<ref>{{cite web | title = Entrez Gene: DMPK dystrophia myotonica-protein kinase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1760| accessdate = }}</ref>
}}
==References==
{{reflist}}
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on EPHA2... {November 15, 2007 4:33:34 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 4:34:10 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 = PBB_Protein_EPHA2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1mqb.
| PDB = {{PDB2|1mqb}}
| Name = EPH receptor A2
| HGNCid = 3386
| Symbol = EPHA2
| AltSymbols =; ECK
| OMIM = 176946
| ECnumber =
| Homologene = 20929
| MGIid = 95278
| GeneAtlas_image1 = PBB_GE_EPHA2_203499_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine kinase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005003 |text = ephrin receptor activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0030182 |text = neuron differentiation}} {{GNF_GO|id=GO:0048013 |text = ephrin receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1969
| Hs_Ensembl = ENSG00000142627
| Hs_RefseqProtein = NP_004422
| Hs_RefseqmRNA = NM_004431
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 16323419
| Hs_GenLoc_end = 16355169
| Hs_Uniprot = P29317
| Mm_EntrezGene = 13836
| Mm_Ensembl = ENSMUSG00000006445
| Mm_RefseqmRNA = XM_982454
| Mm_RefseqProtein = XP_987548
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 140573316
| Mm_GenLoc_end = 140601454
| Mm_Uniprot = Q3UNI2
}}
}}
'''EPH receptor A2''', also known as '''EPHA2''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: EPHA2 EPH receptor A2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1969| 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 belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. This gene encodes a protein that binds ephrin-A ligands.<ref>{{cite web | title = Entrez Gene: EPHA2 EPH receptor A2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1969| accessdate = }}</ref>
}}
==References==
{{reflist}}
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HLA-DRB5... {November 15, 2007 4:34:52 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 4:35:20 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 = PBB_Protein_HLA-DRB5_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aqd.
| PDB = {{PDB2|1aqd}}, {{PDB2|1d5m}}, {{PDB2|1dlh}}, {{PDB2|1fv1}}, {{PDB2|1fyt}}, {{PDB2|1h15}}, {{PDB2|1hqr}}, {{PDB2|1hxy}}, {{PDB2|1j8h}}, {{PDB2|1jwm}}, {{PDB2|1jws}}, {{PDB2|1jwu}}, {{PDB2|1kg0}}, {{PDB2|1klg}}, {{PDB2|1klu}}, {{PDB2|1lo5}}, {{PDB2|1pyw}}, {{PDB2|1r5i}}, {{PDB2|1seb}}, {{PDB2|1sje}}, {{PDB2|1sjh}}, {{PDB2|1t5w}}, {{PDB2|1t5x}}, {{PDB2|1zgl}}, {{PDB2|2g9h}}, {{PDB2|2iam}}, {{PDB2|2ian}}, {{PDB2|2icw}}, {{PDB2|2ipk}}, {{PDB2|2oje}}
| Name = Major histocompatibility complex, class II, DR beta 5
| HGNCid = 4953
| Symbol = HLA-DRB5
| AltSymbols =;
| OMIM = 604776
| ECnumber =
| Homologene = 88657
| MGIid =
| Function = {{GNF_GO|id=GO:0032395 |text = MHC class II receptor activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0042613 |text = MHC class II protein complex}}
| Process = {{GNF_GO|id=GO:0002504 |text = antigen processing and presentation of peptide or polysaccharide antigen via MHC class II}} {{GNF_GO|id=GO:0006955 |text = immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3127
| Hs_Ensembl =
| Hs_RefseqProtein = NP_002116
| Hs_RefseqmRNA = NM_002125
| 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 =
}}
}}
'''Major histocompatibility complex, class II, DR beta 5''', also known as '''HLA-DRB5''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: HLA-DRB5 major histocompatibility complex, class II, DR beta 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3127| 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 = HLA-DRB5 belongs to the HLA class II beta chain paralogues. This class II molecule is a heterodimer consisting of an alpha (DRA) and a beta (DRB) chain, both anchored in the membrane. It plays a central role in the immune system by presenting peptides derived from extracellular proteins. Class II molecules are expressed in antigen presenting cells (APC: B lymphocytes, dendritic cells, macrophages). The beta chain is approximately 26-28 kDa and its gene contains 6 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, exon 4 encodes the transmembrane domain and exon 5 encodes the cytoplasmic tail. Within the DR molecule the beta chain contains all the polymorphisms specifying the peptide binding specificities. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. DRB1 is expressed at a level five times higher than its paralogues DRB3, DRB4 and DRB5. The presence of DRB5 is linked with allelic variants of DRB1, otherwise it is omitted. There are 4 related pseudogenes: DRB2, DRB6, DRB7, DRB8 and DRB9.<ref>{{cite web | title = Entrez Gene: HLA-DRB5 major histocompatibility complex, class II, DR beta 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3127| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lau M, Terasaki PI, Park MS |title=International Cell Exchange, 1994. |journal=Clinical transplants |volume= |issue= |pages= 467-88 |year= 1995 |pmid= 7547576 |doi= }}
*{{cite journal | author=Dong RP, Kimura A, Sasazuki T |title=Sequence analysis of three novel DRw14-DRB1 alleles. |journal=Immunogenetics |volume=36 |issue= 2 |pages= 130-3 |year= 1992 |pmid= 1612646 |doi= }}
*{{cite journal | author=Piatier-Tonneau D, Gastinel LN, Amblard F, ''et al.'' |title=Interaction of CD4 with HLA class II antigens and HIV gp120. |journal=Immunogenetics |volume=34 |issue= 2 |pages= 121-8 |year= 1991 |pmid= 1869305 |doi= }}
*{{cite journal | author=Nong Y, Kandil O, Tobin EH, ''et al.'' |title=The HIV core protein p24 inhibits interferon-gamma-induced increase of HLA-DR and cytochrome b heavy chain mRNA levels in the human monocyte-like cell line THP1. |journal=Cell. Immunol. |volume=132 |issue= 1 |pages= 10-6 |year= 1991 |pmid= 1905983 |doi= }}
*{{cite journal | author=Rosenstein Y, Burakoff SJ, Herrmann SH |title=HIV-gp120 can block CD4-class II MHC-mediated adhesion. |journal=J. Immunol. |volume=144 |issue= 2 |pages= 526-31 |year= 1990 |pmid= 1967269 |doi= }}
*{{cite journal | author=Callahan KM, Fort MM, Obah EA, ''et al.'' |title=Genetic variability in HIV-1 gp120 affects interactions with HLA molecules and T cell receptor. |journal=J. Immunol. |volume=144 |issue= 9 |pages= 3341-6 |year= 1990 |pmid= 1970352 |doi= }}
*{{cite journal | author=Petersdorf EW, Griffith RL, Erlich HA, ''et al.'' |title=Unique sequences for two HLA-DRB1 genes expressed on distinct DRw6 haplotypes. |journal=Immunogenetics |volume=32 |issue= 2 |pages= 96-103 |year= 1990 |pmid= 1975801 |doi= }}
*{{cite journal | author=Bowman MR, MacFerrin KD, Schreiber SL, Burakoff SJ |title=Identification and structural analysis of residues in the V1 region of CD4 involved in interaction with human immunodeficiency virus envelope glycoprotein gp120 and class II major histocompatibility complex molecules. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 22 |pages= 9052-6 |year= 1991 |pmid= 1978941 |doi= }}
*{{cite journal | author=Gyllensten UB, Sundvall M, Erlich HA |title=Allelic diversity is generated by intraexon sequence exchange at the DRB1 locus of primates. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 9 |pages= 3686-90 |year= 1991 |pmid= 2023919 |doi= }}
*{{cite journal | author=Lee KW, Johnson AH, Hurley CK |title=Two divergent routes of evolution gave rise to the DRw13 haplotypes. |journal=J. Immunol. |volume=145 |issue= 9 |pages= 3119-25 |year= 1990 |pmid= 2212675 |doi= }}
*{{cite journal | author=Gorski J |title=HLA-DR beta-chain polymorphism. Second domain polymorphism reflects evolutionary relatedness of alleles and may explain public serologic epitopes. |journal=J. Immunol. |volume=143 |issue= 1 |pages= 329-33 |year= 1989 |pmid= 2471740 |doi= }}
*{{cite journal | author=Clayton LK, Sieh M, Pious DA, Reinherz EL |title=Identification of human CD4 residues affecting class II MHC versus HIV-1 gp120 binding. |journal=Nature |volume=339 |issue= 6225 |pages= 548-51 |year= 1989 |pmid= 2543930 |doi= 10.1038/339548a0 }}
*{{cite journal | author=Hurley CK, Gregersen PK, Gorski J, ''et al.'' |title=The DR3(w18),DQw4 haplotype differs from DR3(w17),DQw2 haplotypes at multiple class II loci. |journal=Hum. Immunol. |volume=25 |issue= 1 |pages= 37-50 |year= 1989 |pmid= 2565895 |doi= }}
*{{cite journal | author=Diamond DC, Sleckman BP, Gregory T, ''et al.'' |title=Inhibition of CD4+ T cell function by the HIV envelope protein, gp120. |journal=J. Immunol. |volume=141 |issue= 11 |pages= 3715-7 |year= 1988 |pmid= 2846691 |doi= }}
*{{cite journal | author=Freeman SM, Saunders TL, Madden M, ''et al.'' |title=Comparison of DR beta 1 alleles from diabetic and normal individuals. |journal=Hum. Immunol. |volume=19 |issue= 1 |pages= 1-6 |year= 1987 |pmid= 2884201 |doi= }}
*{{cite journal | author=Lee BS, Rust NA, McMichael AJ, McDevitt HO |title=HLA-DR2 subtypes form an additional supertypic family of DR beta alleles. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 13 |pages= 4591-5 |year= 1987 |pmid= 2885840 |doi= }}
*{{cite journal | author=Owerbach D, Rich C, Taneja K |title=Characterization of three HLA-DR beta genes isolated from an HLA-DR 3/4 insulin-dependent diabetic patient. |journal=Immunogenetics |volume=24 |issue= 1 |pages= 41-6 |year= 1986 |pmid= 3015788 |doi= }}
*{{cite journal | author=Wu S, Saunders TL, Bach FH |title=Polymorphism of human Ia antigens generated by reciprocal intergenic exchange between two DR beta loci. |journal=Nature |volume=324 |issue= 6098 |pages= 676-9 |year= 1987 |pmid= 3099214 |doi= 10.1038/324676a0 }}
*{{cite journal | author=Liu CP, Bach FH, Wu SK |title=Molecular studies of a rare DR2/LD-5a/DQw3 HLA class II haplotype. Multiple genetic mechanisms in the generation of polymorphic HLA class II genes. |journal=J. Immunol. |volume=140 |issue= 10 |pages= 3631-9 |year= 1988 |pmid= 3129499 |doi= }}
*{{cite journal | author=Steimle V, Hinkkanen A, Schlesier M, Epplen JT |title=A novel HLA-DR beta I sequence from the DRw11 haplotype. |journal=Immunogenetics |volume=28 |issue= 3 |pages= 208-10 |year= 1988 |pmid= 3137159 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MMP13... {November 15, 2007 4:36:22 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 4:36:56 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_MMP13_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cxv.
| PDB = {{PDB2|1cxv}}, {{PDB2|1eub}}, {{PDB2|1fls}}, {{PDB2|1fm1}}, {{PDB2|1pex}}, {{PDB2|1xuc}}, {{PDB2|1xud}}, {{PDB2|1xur}}, {{PDB2|1you}}, {{PDB2|1ztq}}, {{PDB2|2d1n}}, {{PDB2|2e2d}}, {{PDB2|2ow9}}, {{PDB2|456c}}, {{PDB2|830c}}
| Name = Matrix metallopeptidase 13 (collagenase 3)
| HGNCid = 7159
| Symbol = MMP13
| AltSymbols =; CLG3
| OMIM = 600108
| ECnumber =
| Homologene = 20548
| MGIid = 1340026
| GeneAtlas_image1 = PBB_GE_MMP13_205959_at_tn.png
| Function = {{GNF_GO|id=GO:0004222 |text = metalloendopeptidase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0008133 |text = collagenase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0000270 |text = peptidoglycan metabolic process}} {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0030574 |text = collagen catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4322
| Hs_Ensembl = ENSG00000137745
| Hs_RefseqProtein = NP_002418
| Hs_RefseqmRNA = NM_002427
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 102318937
| Hs_GenLoc_end = 102331672
| Hs_Uniprot = P45452
| Mm_EntrezGene = 17386
| Mm_Ensembl = ENSMUSG00000050578
| Mm_RefseqmRNA = NM_008607
| Mm_RefseqProtein = NP_032633
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 7272545
| Mm_GenLoc_end = 7283333
| Mm_Uniprot = Q3U2N6
}}
}}
'''Matrix metallopeptidase 13 (collagenase 3)''', also known as '''MMP13''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: MMP13 matrix metallopeptidase 13 (collagenase 3)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4322| 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 = Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The protein encoded by this gene cleaves type II collagen more efficiently than types I and III. It may be involved in articular cartilage turnover and cartilage pathophysiology associated with osteoarthritis. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.<ref>{{cite web | title = Entrez Gene: MMP13 matrix metallopeptidase 13 (collagenase 3)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4322| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nagase H, Woessner JF |title=Matrix metalloproteinases. |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21491-4 |year= 1999 |pmid= 10419448 |doi= }}
*{{cite journal | author=Leeman MF, Curran S, Murray GI |title=The structure, regulation, and function of human matrix metalloproteinase-13. |journal=Crit. Rev. Biochem. Mol. Biol. |volume=37 |issue= 3 |pages= 149-66 |year= 2003 |pmid= 12139441 |doi= }}
*{{cite journal | author=Pendás AM, Matilla T, Estivill X, López-Otín C |title=The human collagenase-3 (CLG3) gene is located on chromosome 11q22.3 clustered to other members of the matrix metalloproteinase gene family. |journal=Genomics |volume=26 |issue= 3 |pages= 615-8 |year= 1995 |pmid= 7607691 |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=Freije JM, Díez-Itza I, Balbín M, ''et al.'' |title=Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas. |journal=J. Biol. Chem. |volume=269 |issue= 24 |pages= 16766-73 |year= 1994 |pmid= 8207000 |doi= }}
*{{cite journal | author=Mitchell PG, Magna HA, Reeves LM, ''et al.'' |title=Cloning, expression, and type II collagenolytic activity of matrix metalloproteinase-13 from human osteoarthritic cartilage. |journal=J. Clin. Invest. |volume=97 |issue= 3 |pages= 761-8 |year= 1996 |pmid= 8609233 |doi= }}
*{{cite journal | author=Knäuper V, Will H, López-Otin C, ''et al.'' |title=Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme. |journal=J. Biol. Chem. |volume=271 |issue= 29 |pages= 17124-31 |year= 1996 |pmid= 8663255 |doi= }}
*{{cite journal | author=Gomis-Rüth FX, Gohlke U, Betz M, ''et al.'' |title=The helping hand of collagenase-3 (MMP-13): 2.7 A crystal structure of its C-terminal haemopexin-like domain. |journal=J. Mol. Biol. |volume=264 |issue= 3 |pages= 556-66 |year= 1997 |pmid= 8969305 |doi= 10.1006/jmbi.1996.0661 }}
*{{cite journal | author=Knäuper V, Cowell S, Smith B, ''et al.'' |title=The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction. |journal=J. Biol. Chem. |volume=272 |issue= 12 |pages= 7608-16 |year= 1997 |pmid= 9065415 |doi= }}
*{{cite journal | author=Pendás AM, Balbín M, Llano E, ''et al.'' |title=Structural analysis and promoter characterization of the human collagenase-3 gene (MMP13). |journal=Genomics |volume=40 |issue= 2 |pages= 222-33 |year= 1997 |pmid= 9119388 |doi= 10.1006/geno.1996.4554 }}
*{{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=Willmroth F, Peter HH, Conca W |title=A matrix metalloproteinase gene expressed in human T lymphocytes is identical with collagenase 3 from breast carcinomas. |journal=Immunobiology |volume=198 |issue= 4 |pages= 375-84 |year= 1998 |pmid= 9562863 |doi= }}
*{{cite journal | author=Lovejoy B, Welch AR, Carr S, ''et al.'' |title=Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors. |journal=Nat. Struct. Biol. |volume=6 |issue= 3 |pages= 217-21 |year= 1999 |pmid= 10074939 |doi= 10.1038/6657 }}
*{{cite journal | author=Barmina OY, Walling HW, Fiacco GJ, ''et al.'' |title=Collagenase-3 binds to a specific receptor and requires the low density lipoprotein receptor-related protein for internalization. |journal=J. Biol. Chem. |volume=274 |issue= 42 |pages= 30087-93 |year= 1999 |pmid= 10514495 |doi= }}
*{{cite journal | author=Lauer-Fields JL, Tuzinski KA, Shimokawa K, ''et al.'' |title=Hydrolysis of triple-helical collagen peptide models by matrix metalloproteinases. |journal=J. Biol. Chem. |volume=275 |issue= 18 |pages= 13282-90 |year= 2000 |pmid= 10788434 |doi= }}
*{{cite journal | author=Hiller O, Lichte A, Oberpichler A, ''et al.'' |title=Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII. |journal=J. Biol. Chem. |volume=275 |issue= 42 |pages= 33008-13 |year= 2000 |pmid= 10930399 |doi= 10.1074/jbc.M001836200 }}
*{{cite journal | author=McQuibban GA, Gong JH, Tam EM, ''et al.'' |title=Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3. |journal=Science |volume=289 |issue= 5482 |pages= 1202-6 |year= 2000 |pmid= 10947989 |doi= }}
*{{cite journal | author=Terp GE, Christensen IT, Jørgensen FS |title=Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes. |journal=J. Biomol. Struct. Dyn. |volume=17 |issue= 6 |pages= 933-46 |year= 2000 |pmid= 10949161 |doi= }}
*{{cite journal | author=Nakamura H, Fujii Y, Inoki I, ''et al.'' |title=Brevican is degraded by matrix metalloproteinases and aggrecanase-1 (ADAMTS4) at different sites. |journal=J. Biol. Chem. |volume=275 |issue= 49 |pages= 38885-90 |year= 2001 |pmid= 10986281 |doi= 10.1074/jbc.M003875200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MRE11A... {November 15, 2007 4:36:56 PM PST}
- SEARCH REDIRECT: Control Box Found: MRE11A {November 15, 2007 4:37:52 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 4:37:54 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 4:37:54 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 4:37:54 PM PST}
- UPDATED: Updated protein page: MRE11A {November 15, 2007 4:38:01 PM PST}
- INFO: Beginning work on POLR2D... {November 15, 2007 4:38:31 PM PST}
- SEARCH REDIRECT: Control Box Found: POLR2D {November 15, 2007 4:39:10 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 4:39:11 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 4:39:11 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 4:39:11 PM PST}
- UPDATED: Updated protein page: POLR2D {November 15, 2007 4:39:17 PM PST}
- INFO: Beginning work on POU1F1... {November 15, 2007 4:39:17 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 4:39:54 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_POU1F1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1au7.
| PDB = {{PDB2|1au7}}
| Name = POU domain, class 1, transcription factor 1 (Pit1, growth hormone factor 1)
| HGNCid = 9210
| Symbol = POU1F1
| AltSymbols =; GHF-1; PIT1; Pit-1; Pit-1 beta
| OMIM = 173110
| ECnumber =
| Homologene = 259
| MGIid = 97588
| GeneAtlas_image1 = PBB_GE_POU1F1_207846_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5449
| Hs_Ensembl = ENSG00000064835
| Hs_RefseqProtein = NP_000297
| Hs_RefseqmRNA = NM_000306
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 87391473
| Hs_GenLoc_end = 87408427
| Hs_Uniprot = P28069
| Mm_EntrezGene = 18736
| Mm_Ensembl = ENSMUSG00000004842
| Mm_RefseqmRNA = NM_008849
| Mm_RefseqProtein = NP_032875
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 65438862
| Mm_GenLoc_end = 65453881
| Mm_Uniprot = Q62089
}}
}}
'''POU domain, class 1, transcription factor 1 (Pit1, growth hormone factor 1)''', also known as '''POU1F1''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: POU1F1 POU domain, class 1, transcription factor 1 (Pit1, growth hormone factor 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5449| 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 = PIT1 is a pituitary-specific transcription factor responsible for pituitary development and hormone expression in mammals and is a member of the POU family of transcription factors that regulate mammalian development. The POU family is so named because the first 3 members identified were PIT1 and OCT1 (MIM 164175) of mammals, and Unc-86 of C. elegans (Herr et al., 1988). PIT1 contains 2 protein domains, termed POU-specific and POU-homeo, which are both necessary for high affinity DNA binding on genes encoding growth hormone (GH; MIM 139250) and prolactin (PRL; MIM 176760). PIT1 is also important for regulation of the genes encoding prolactin and thyroid-stimulating hormone beta subunit (TSHB; MIM 188540) by thyrotropin-releasing hormone (TRH; MIM 257120) and cyclic AMP.[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: POU1F1 POU domain, class 1, transcription factor 1 (Pit1, growth hormone factor 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5449| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Parks JS, Brown MR |title=Transcription factors regulating pituitary development. |journal=Growth Horm. IGF Res. |volume=9 Suppl B |issue= |pages= 2-8; discussion 8-11 |year= 1999 |pmid= 10549299 |doi= }}
*{{cite journal | author=Rodriguez R, Andersen B |title=Cellular determination in the anterior pituitary gland: PIT-1 and PROP-1 mutations as causes of human combined pituitary hormone deficiency. |journal=Minerva Endocrinol. |volume=28 |issue= 2 |pages= 123-33 |year= 2003 |pmid= 12717343 |doi= }}
*{{cite journal | author=Quentien MH, Barlier A, Franc JL, ''et al.'' |title=Pituitary transcription factors: from congenital deficiencies to gene therapy. |journal=J. Neuroendocrinol. |volume=18 |issue= 9 |pages= 633-42 |year= 2006 |pmid= 16879162 |doi= 10.1111/j.1365-2826.2006.01461.x }}
*{{cite journal | author=Cattini PA, Yang X, Jin Y, Detillieux KA |title=Regulation of the human growth hormone gene family: possible role for Pit-1 in early stages of pituitary-specific expression and repression. |journal=Neuroendocrinology |volume=83 |issue= 3-4 |pages= 145-53 |year= 2006 |pmid= 17047377 |doi= 10.1159/000095522 }}
*{{cite journal | author=Li X, Giachelli CM |title=Sodium-dependent phosphate cotransporters and vascular calcification. |journal=Curr. Opin. Nephrol. Hypertens. |volume=16 |issue= 4 |pages= 325-8 |year= 2007 |pmid= 17565274 |doi= 10.1097/MNH.0b013e3281c55ef1 }}
*{{cite journal | author=Tatsumi K, Miyai K, Notomi T, ''et al.'' |title=Cretinism with combined hormone deficiency caused by a mutation in the PIT1 gene. |journal=Nat. Genet. |volume=1 |issue= 1 |pages= 56-8 |year= 1993 |pmid= 1302000 |doi= 10.1038/ng0492-56 }}
*{{cite journal | author=Tatsumi K, Notomi T, Amino N, Miyai K |title=Nucleotide sequence of the complementary DNA for human Pit-1/GHF-1. |journal=Biochim. Biophys. Acta |volume=1129 |issue= 2 |pages= 231-4 |year= 1992 |pmid= 1370379 |doi= }}
*{{cite journal | author=Ohta K, Nobukuni Y, Mitsubuchi H, ''et al.'' |title=Mutations in the Pit-1 gene in children with combined pituitary hormone deficiency. |journal=Biochem. Biophys. Res. Commun. |volume=189 |issue= 2 |pages= 851-5 |year= 1993 |pmid= 1472057 |doi= }}
*{{cite journal | author=Ohta K, Nobukuni Y, Mitsubuchi H, ''et al.'' |title=Characterization of the gene encoding human pituitary-specific transcription factor, Pit-1. |journal=Gene |volume=122 |issue= 2 |pages= 387-8 |year= 1993 |pmid= 1487156 |doi= }}
*{{cite journal | author=Radovick S, Nations M, Du Y, ''et al.'' |title=A mutation in the POU-homeodomain of Pit-1 responsible for combined pituitary hormone deficiency. |journal=Science |volume=257 |issue= 5073 |pages= 1115-8 |year= 1992 |pmid= 1509262 |doi= }}
*{{cite journal | author=Pfäffle RW, DiMattia GE, Parks JS, ''et al.'' |title=Mutation of the POU-specific domain of Pit-1 and hypopituitarism without pituitary hypoplasia. |journal=Science |volume=257 |issue= 5073 |pages= 1118-21 |year= 1992 |pmid= 1509263 |doi= }}
*{{cite journal | author=Lew AM, Elsholtz HP |title=Cloning of the human cDNA for transcription factor Pit-1. |journal=Nucleic Acids Res. |volume=19 |issue= 22 |pages= 6329 |year= 1991 |pmid= 1956794 |doi= }}
*{{cite journal | author=He X, Treacy MN, Simmons DM, ''et al.'' |title=Expression of a large family of POU-domain regulatory genes in mammalian brain development. |journal=Nature |volume=340 |issue= 6228 |pages= 35-41 |year= 1989 |pmid= 2739723 |doi= 10.1038/340035a0 }}
*{{cite journal | author=Bodner M, Castrillo JL, Theill LE, ''et al.'' |title=The pituitary-specific transcription factor GHF-1 is a homeobox-containing protein. |journal=Cell |volume=55 |issue= 3 |pages= 505-18 |year= 1988 |pmid= 2902927 |doi= }}
*{{cite journal | author=Herr W, Sturm RA, Clerc RG, ''et al.'' |title=The POU domain: a large conserved region in the mammalian pit-1, oct-1, oct-2, and Caenorhabditis elegans unc-86 gene products. |journal=Genes Dev. |volume=2 |issue= 12A |pages= 1513-6 |year= 1989 |pmid= 3215510 |doi= }}
*{{cite journal | author=de Zegher F, Pernasetti F, Vanhole C, ''et al.'' |title=The prenatal role of thyroid hormone evidenced by fetomaternal Pit-1 deficiency. |journal=J. Clin. Endocrinol. Metab. |volume=80 |issue= 11 |pages= 3127-30 |year= 1995 |pmid= 7593413 |doi= }}
*{{cite journal | author=Bamberger AM, Bamberger CM, Pu LP, ''et al.'' |title=Expression of pit-1 messenger ribonucleic acid and protein in the human placenta. |journal=J. Clin. Endocrinol. Metab. |volume=80 |issue= 7 |pages= 2021-6 |year= 1995 |pmid= 7608249 |doi= }}
*{{cite journal | author=Irie Y, Tatsumi K, Ogawa M, ''et al.'' |title=A novel E250X mutation of the PIT1 gene in a patient with combined pituitary hormone deficiency. |journal=Endocr. J. |volume=42 |issue= 3 |pages= 351-4 |year= 1995 |pmid= 7670563 |doi= }}
*{{cite journal | author=Delhase M, Vila V, Hooghe-Peters EL, Castrillo JL |title=A novel pituitary transcription factor is produced by alternative splicing of the human GHF-1/PIT-1 gene. |journal=Gene |volume=155 |issue= 2 |pages= 273-5 |year= 1995 |pmid= 7721104 |doi= }}
*{{cite journal | author=Okamoto N, Wada Y, Ida S, ''et al.'' |title=Monoallelic expression of normal mRNA in the PIT1 mutation heterozygotes with normal phenotype and biallelic expression in the abnormal phenotype. |journal=Hum. Mol. Genet. |volume=3 |issue= 9 |pages= 1565-8 |year= 1995 |pmid= 7833912 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PPP1CA... {November 15, 2007 4:39:54 PM PST}
- SEARCH REDIRECT: Control Box Found: PPP1CA {November 15, 2007 4:40:34 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 4:40:35 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 4:40:35 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 4:40:35 PM PST}
- UPDATED: Updated protein page: PPP1CA {November 15, 2007 4:40:41 PM PST}
- INFO: Beginning work on RBL1... {November 15, 2007 4:40:41 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 4:41:25 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_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 = Retinoblastoma-like 1 (p107)
| HGNCid = 9893
| Symbol = RBL1
| AltSymbols =; PRB1; CP107; MGC40006; p107
| OMIM = 116957
| ECnumber =
| Homologene = 2172
| MGIid = 103300
| GeneAtlas_image1 = PBB_GE_RBL1_205296_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005667 |text = transcription factor complex}}
| Process = {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0043550 |text = regulation of lipid kinase activity}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5933
| Hs_Ensembl = ENSG00000080839
| Hs_RefseqProtein = NP_002886
| Hs_RefseqmRNA = NM_002895
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 35058166
| Hs_GenLoc_end = 35157824
| Hs_Uniprot = P28749
| Mm_EntrezGene = 19650
| Mm_Ensembl = ENSMUSG00000027641
| Mm_RefseqmRNA = NM_011249
| Mm_RefseqProtein = NP_035379
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 156837339
| Mm_GenLoc_end = 156895960
| Mm_Uniprot = Q3U1D4
}}
}}
'''Retinoblastoma-like 1 (p107)''', also known as '''RBL1''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: RBL1 retinoblastoma-like 1 (p107)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5933| 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 similar in sequence and possibly function to the product of the retinoblastoma 1 (RB1) gene. The RB1 gene product is a tumor suppressor protein that appears to be involved in cell cycle regulation, as it is phosphorylated in the S to M phase transition and is dephosphorylated in the G1 phase of the cell cycle. Both the RB1 protein and the product of this gene can form a complex with adenovirus E1A protein and SV40 large T-antigen, with the SV40 large T-antigen binding only to the unphosphorylated form of each protein. In addition, both proteins can inhibit the transcription of cell cycle genes containing E2F binding sites in their promoters. Due to the sequence and biochemical similarities with the RB1 protein, it is thought that the protein encoded by this gene may also be a tumor suppressor. Two transcript variants encoding different isoforms have been found for this gene.<ref>{{cite web | title = Entrez Gene: RBL1 retinoblastoma-like 1 (p107)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5933| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Faha B, Ewen ME, Tsai LH, ''et al.'' |title=Interaction between human cyclin A and adenovirus E1A-associated p107 protein. |journal=Science |volume=255 |issue= 5040 |pages= 87-90 |year= 1992 |pmid= 1532458 |doi= }}
*{{cite journal | author=Ewen ME, Xing YG, Lawrence JB, Livingston DM |title=Molecular cloning, chromosomal mapping, and expression of the cDNA for p107, a retinoblastoma gene product-related protein. |journal=Cell |volume=66 |issue= 6 |pages= 1155-64 |year= 1991 |pmid= 1833063 |doi= }}
*{{cite journal | author=Datta PK, Raychaudhuri P, Bagchi S |title=Association of p107 with Sp1: genetically separable regions of p107 are involved in regulation of E2F- and Sp1-dependent transcription. |journal=Mol. Cell. Biol. |volume=15 |issue= 10 |pages= 5444-52 |year= 1995 |pmid= 7565695 |doi= }}
*{{cite journal | author=Zhu L, Zhu L, Xie E, Chang LS |title=Differential roles of two tandem E2F sites in repression of the human p107 promoter by retinoblastoma and p107 proteins. |journal=Mol. Cell. Biol. |volume=15 |issue= 7 |pages= 3552-62 |year= 1995 |pmid= 7791762 |doi= }}
*{{cite journal | author=Sardet C, Vidal M, Cobrinik D, ''et al.'' |title=E2F-4 and E2F-5, two members of the E2F family, are expressed in the early phases of the cell cycle. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 6 |pages= 2403-7 |year= 1995 |pmid= 7892279 |doi= }}
*{{cite journal | author=Kim YW, Otterson GA, Kratzke RA, ''et al.'' |title=Differential specificity for binding of retinoblastoma binding protein 2 to RB, p107, and TATA-binding protein. |journal=Mol. Cell. Biol. |volume=14 |issue= 11 |pages= 7256-64 |year= 1994 |pmid= 7935440 |doi= }}
*{{cite journal | author=Ginsberg D, Vairo G, Chittenden T, ''et al.'' |title=E2F-4, a new member of the E2F transcription factor family, interacts with p107. |journal=Genes Dev. |volume=8 |issue= 22 |pages= 2665-79 |year= 1994 |pmid= 7958924 |doi= }}
*{{cite journal | author=Beijersbergen RL, Kerkhoven RM, Zhu L, ''et al.'' |title=E2F-4, a new member of the E2F gene family, has oncogenic activity and associates with p107 in vivo. |journal=Genes Dev. |volume=8 |issue= 22 |pages= 2680-90 |year= 1994 |pmid= 7958925 |doi= }}
*{{cite journal | author=Beijersbergen RL, Hijmans EM, Zhu L, Bernards R |title=Interaction of c-Myc with the pRb-related protein p107 results in inhibition of c-Myc-mediated transactivation. |journal=EMBO J. |volume=13 |issue= 17 |pages= 4080-6 |year= 1994 |pmid= 8076603 |doi= }}
*{{cite journal | author=Dyson N, Dembski M, Fattaey A, ''et al.'' |title=Analysis of p107-associated proteins: p107 associates with a form of E2F that differs from pRB-associated E2F-1. |journal=J. Virol. |volume=67 |issue= 12 |pages= 7641-7 |year= 1993 |pmid= 8230483 |doi= }}
*{{cite journal | author=Zhu L, van den Heuvel S, Helin K, ''et al.'' |title=Inhibition of cell proliferation by p107, a relative of the retinoblastoma protein. |journal=Genes Dev. |volume=7 |issue= 7A |pages= 1111-25 |year= 1993 |pmid= 8319904 |doi= }}
*{{cite journal | author=Ikeda MA, Jakoi L, Nevins JR |title=A unique role for the Rb protein in controlling E2F accumulation during cell growth and differentiation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 8 |pages= 3215-20 |year= 1996 |pmid= 8622916 |doi= }}
*{{cite journal | author=Xiao ZX, Ginsberg D, Ewen M, Livingston DM |title=Regulation of the retinoblastoma protein-related protein p107 by G1 cyclin-associated kinases. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 10 |pages= 4633-7 |year= 1996 |pmid= 8643455 |doi= }}
*{{cite journal | author=Vidal M, Brachmann RK, Fattaey A, ''et al.'' |title=Reverse two-hybrid and one-hybrid systems to detect dissociation of protein-protein and DNA-protein interactions. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 19 |pages= 10315-20 |year= 1996 |pmid= 8816797 |doi= }}
*{{cite journal | author=Shao Z, Siegert JL, Ruppert S, Robbins PD |title=Rb interacts with TAF(II)250/TFIID through multiple domains. |journal=Oncogene |volume=15 |issue= 4 |pages= 385-92 |year= 1997 |pmid= 9242374 |doi= 10.1038/sj.onc.1201204 }}
*{{cite journal | author=Verona R, Moberg K, Estes S, ''et al.'' |title=E2F activity is regulated by cell cycle-dependent changes in subcellular localization. |journal=Mol. Cell. Biol. |volume=17 |issue= 12 |pages= 7268-82 |year= 1997 |pmid= 9372959 |doi= }}
*{{cite journal | author=Trimarchi JM, Fairchild B, Verona R, ''et al.'' |title=E2F-6, a member of the E2F family that can behave as a transcriptional repressor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 6 |pages= 2850-5 |year= 1998 |pmid= 9501179 |doi= }}
*{{cite journal | author=Sterner JM, Dew-Knight S, Musahl C, ''et al.'' |title=Negative regulation of DNA replication by the retinoblastoma protein is mediated by its association with MCM7. |journal=Mol. Cell. Biol. |volume=18 |issue= 5 |pages= 2748-57 |year= 1998 |pmid= 9566894 |doi= }}
*{{cite journal | author=Woitach JT, Zhang M, Niu CH, Thorgeirsson SS |title=A retinoblastoma-binding protein that affects cell-cycle control and confers transforming ability. |journal=Nat. Genet. |volume=19 |issue= 4 |pages= 371-4 |year= 1998 |pmid= 9697699 |doi= 10.1038/1258 }}
*{{cite journal | author=Veal E, Eisenstein M, Tseng ZH, Gill G |title=A cellular repressor of E1A-stimulated genes that inhibits activation by E2F. |journal=Mol. Cell. Biol. |volume=18 |issue= 9 |pages= 5032-41 |year= 1998 |pmid= 9710587 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RPGR... {November 15, 2007 4:41:25 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 4:42:12 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 = Retinitis pigmentosa GTPase regulator
| HGNCid = 10295
| Symbol = RPGR
| AltSymbols =; CRD; COD1; CORDX1; PCDX; RP15; RP3; XLRP3; orf15
| OMIM = 312610
| ECnumber =
| Homologene = 55455
| MGIid = 1344037
| GeneAtlas_image1 = PBB_GE_RPGR_207624_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005085 |text = guanyl-nucleotide exchange factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}}
| Process = {{GNF_GO|id=GO:0006886 |text = intracellular protein transport}} {{GNF_GO|id=GO:0007601 |text = visual perception}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6103
| Hs_Ensembl = ENSG00000156313
| Hs_RefseqProtein = NP_000319
| Hs_RefseqmRNA = NM_000328
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 38013368
| Hs_GenLoc_end = 38071732
| Hs_Uniprot = Q92834
| Mm_EntrezGene = 19893
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_011285
| Mm_RefseqProtein = NP_035415
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Retinitis pigmentosa GTPase regulator''', also known as '''RPGR''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: RPGR retinitis pigmentosa GTPase regulator| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6103| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a protein with a series of six RCC1-like domains (RLDs), characteristic of the highly conserved guanine nucleotide exchange factors. Mutations in this gene have been associated with X-linked retinitis pigmentosa (XLRP). Multiple alternatively spliced transcript variants that encode different isoforms of this gene have been reported, but the full-length natures of only some have been determined.<ref>{{cite web | title = Entrez Gene: RPGR retinitis pigmentosa GTPase regulator| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6103| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Jin ZB, Hayakawa M, Murakami A, Nao-i N |title=RCC1-like domain and ORF15: essentials in RPGR gene. |journal=Adv. Exp. Med. Biol. |volume=572 |issue= |pages= 29-33 |year= 2007 |pmid= 17249551 |doi= }}
*{{cite journal | author=Ott J, Bhattacharya S, Chen JD, ''et al.'' |title=Localizing multiple X chromosome-linked retinitis pigmentosa loci using multilocus homogeneity tests. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 2 |pages= 701-4 |year= 1990 |pmid= 2300556 |doi= }}
*{{cite journal | author=McGuire RE, Sullivan LS, Blanton SH, ''et al.'' |title=X-linked dominant cone-rod degeneration: linkage mapping of a new locus for retinitis pigmentosa (RP 15) to Xp22.13-p22.11. |journal=Am. J. Hum. Genet. |volume=57 |issue= 1 |pages= 87-94 |year= 1995 |pmid= 7611300 |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=Meindl A, Dry K, Herrmann K, ''et al.'' |title=A gene (RPGR) with homology to the RCC1 guanine nucleotide exchange factor is mutated in X-linked retinitis pigmentosa (RP3). |journal=Nat. Genet. |volume=13 |issue= 1 |pages= 35-42 |year= 1996 |pmid= 8673101 |doi= 10.1038/ng0596-35 }}
*{{cite journal | author=Roepman R, van Duijnhoven G, Rosenberg T, ''et al.'' |title=Positional cloning of the gene for X-linked retinitis pigmentosa 3: homology with the guanine-nucleotide-exchange factor RCC1. |journal=Hum. Mol. Genet. |volume=5 |issue= 7 |pages= 1035-41 |year= 1997 |pmid= 8817343 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Fujita R, Buraczynska M, Gieser L, ''et al.'' |title=Analysis of the RPGR gene in 11 pedigrees with the retinitis pigmentosa type 3 genotype: paucity of mutations in the coding region but splice defects in two families. |journal=Am. J. Hum. Genet. |volume=61 |issue= 3 |pages= 571-80 |year= 1997 |pmid= 9326322 |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=Buraczynska M, Wu W, Fujita R, ''et al.'' |title=Spectrum of mutations in the RPGR gene that are identified in 20% of families with X-linked retinitis pigmentosa. |journal=Am. J. Hum. Genet. |volume=61 |issue= 6 |pages= 1287-92 |year= 1998 |pmid= 9399904 |doi= }}
*{{cite journal | author=Hardcastle AJ, David-Gray ZK, Jay M, ''et al.'' |title=Localization of CSNBX (CSNB4) between the retinitis pigmentosa loci RP2 and RP3 on proximal Xp. |journal=Invest. Ophthalmol. Vis. Sci. |volume=38 |issue= 13 |pages= 2750-5 |year= 1998 |pmid= 9418727 |doi= }}
*{{cite journal | author=Yan D, Swain PK, Breuer D, ''et al.'' |title=Biochemical characterization and subcellular localization of the mouse retinitis pigmentosa GTPase regulator (mRpgr). |journal=J. Biol. Chem. |volume=273 |issue= 31 |pages= 19656-63 |year= 1998 |pmid= 9677393 |doi= }}
*{{cite journal | author=Fishman GA, Grover S, Jacobson SG, ''et al.'' |title=X-linked retinitis pigmentosa in two families with a missense mutation in the RPGR gene and putative change of glycine to valine at codon 60. |journal=Ophthalmology |volume=105 |issue= 12 |pages= 2286-96 |year= 1998 |pmid= 9855162 |doi= 10.1016/S0161-6420(98)91231-3 }}
*{{cite journal | author=Linari M, Ueffing M, Manson F, ''et al.'' |title=The retinitis pigmentosa GTPase regulator, RPGR, interacts with the delta subunit of rod cyclic GMP phosphodiesterase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 4 |pages= 1315-20 |year= 1999 |pmid= 9990021 |doi= }}
*{{cite journal | author=Dry KL, Manson FD, Lennon A, ''et al.'' |title=Identification of a 5' splice site mutation in the RPGR gene in a family with X-linked retinitis pigmentosa (RP3). |journal=Hum. Mutat. |volume=13 |issue= 2 |pages= 141-5 |year= 1999 |pmid= 10094550 |doi= 10.1002/(SICI)1098-1004(1999)13:2<141::AID-HUMU6>3.0.CO;2-Q }}
*{{cite journal | author=Kirschner R, Rosenberg T, Schultz-Heienbrok R, ''et al.'' |title=RPGR transcription studies in mouse and human tissues reveal a retina-specific isoform that is disrupted in a patient with X-linked retinitis pigmentosa. |journal=Hum. Mol. Genet. |volume=8 |issue= 8 |pages= 1571-8 |year= 1999 |pmid= 10401007 |doi= }}
*{{cite journal | author=Zito I, Thiselton DL, Gorin MB, ''et al.'' |title=Identification of novel RPGR (retinitis pigmentosa GTPase regulator) mutations in a subset of X-linked retinitis pigmentosa families segregating with the RP3 locus. |journal=Hum. Genet. |volume=105 |issue= 1-2 |pages= 57-62 |year= 1999 |pmid= 10480356 |doi= }}
*{{cite journal | author=Miano MG, Testa F, Strazzullo M, ''et al.'' |title=Mutation analysis of the RPGR gene reveals novel mutations in south European patients with X-linked retinitis pigmentosa. |journal=Eur. J. Hum. Genet. |volume=7 |issue= 6 |pages= 687-94 |year= 1999 |pmid= 10482958 |doi= 10.1038/sj.ejhg.5200352 }}
*{{cite journal | author=Hong DH, Pawlyk BS, Shang J, ''et al.'' |title=A retinitis pigmentosa GTPase regulator (RPGR)-deficient mouse model for X-linked retinitis pigmentosa (RP3). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3649-54 |year= 2000 |pmid= 10725384 |doi= 10.1073/pnas.060037497 }}
*{{cite journal | author=Zito I, Gorin MB, Plant C, ''et al.'' |title=Novel mutations of the RPGR gene in RP3 families. |journal=Hum. Mutat. |volume=15 |issue= 4 |pages= 386 |year= 2000 |pmid= 10737996 |doi= 10.1002/(SICI)1098-1004(200004)15:4<386::AID-HUMU23>3.0.CO;2-4 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on S100A8... {November 15, 2007 4:42:12 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 4:43:03 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_S100A8_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1mr8.
| PDB = {{PDB2|1mr8}}, {{PDB2|1xk4}}
| Name = S100 calcium binding protein A8
| HGNCid = 10498
| Symbol = S100A8
| AltSymbols =; MIF; 60B8AG; CAGA; CFAG; CGLA; CP-10; L1Ag; MA387; MRP8; NIF; P8
| OMIM = 123885
| ECnumber =
| Homologene = 2225
| MGIid = 88244
| GeneAtlas_image1 = PBB_GE_S100A8_202917_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006954 |text = inflammatory response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6279
| Hs_Ensembl = ENSG00000143546
| Hs_RefseqProtein = NP_002955
| Hs_RefseqmRNA = NM_002964
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 151629132
| Hs_GenLoc_end = 151630288
| Hs_Uniprot = P05109
| Mm_EntrezGene = 20201
| Mm_Ensembl = ENSMUSG00000056054
| Mm_RefseqmRNA = NM_013650
| Mm_RefseqProtein = NP_038678
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 90755012
| Mm_GenLoc_end = 90755961
| Mm_Uniprot = Q53X15
}}
}}
'''S100 calcium binding protein A8''', also known as '''S100A8''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: S100A8 S100 calcium binding protein A8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6279| 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 S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein may function in the inhibition of casein kinase and as a cytokine. Altered expression of this protein is associated with the disease cystic fibrosis.<ref>{{cite web | title = Entrez Gene: S100A8 S100 calcium binding protein A8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6279| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schäfer BW, Heizmann CW |title=The S100 family of EF-hand calcium-binding proteins: functions and pathology. |journal=Trends Biochem. Sci. |volume=21 |issue= 4 |pages= 134-40 |year= 1996 |pmid= 8701470 |doi= }}
*{{cite journal | author=Kerkhoff C, Klempt M, Sorg C |title=Novel insights into structure and function of MRP8 (S100A8) and MRP14 (S100A9). |journal=Biochim. Biophys. Acta |volume=1448 |issue= 2 |pages= 200-11 |year= 1999 |pmid= 9920411 |doi= }}
*{{cite journal | author=Nacken W, Roth J, Sorg C, Kerkhoff C |title=S100A9/S100A8: Myeloid representatives of the S100 protein family as prominent players in innate immunity. |journal=Microsc. Res. Tech. |volume=60 |issue= 6 |pages= 569-80 |year= 2003 |pmid= 12645005 |doi= 10.1002/jemt.10299 }}
*{{cite journal | author=Roth J, Vogl T, Sorg C, Sunderkötter C |title=Phagocyte-specific S100 proteins: a novel group of proinflammatory molecules. |journal=Trends Immunol. |volume=24 |issue= 4 |pages= 155-8 |year= 2004 |pmid= 12697438 |doi= }}
*{{cite journal | author=Rasmussen HH, van Damme J, Puype M, ''et al.'' |title=Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 960-9 |year= 1993 |pmid= 1286667 |doi= }}
*{{cite journal | author=Lemarchand P, Vaglio M, Mauël J, Markert M |title=Translocation of a small cytosolic calcium-binding protein (MRP-8) to plasma membrane correlates with human neutrophil activation. |journal=J. Biol. Chem. |volume=267 |issue= 27 |pages= 19379-82 |year= 1992 |pmid= 1326551 |doi= }}
*{{cite journal | author=Schäfer T, Sachse GE, Gassen HG |title=The calcium-binding protein MRP-8 is produced by human pulmonary tumor cells. |journal=Biol. Chem. Hoppe-Seyler |volume=372 |issue= 1 |pages= 1-4 |year= 1991 |pmid= 2039599 |doi= }}
*{{cite journal | author=Dorin JR, Emslie E, van Heyningen V |title=Related calcium-binding proteins map to the same subregion of chromosome 1q and to an extended region of synteny on mouse chromosome 3. |journal=Genomics |volume=8 |issue= 3 |pages= 420-6 |year= 1991 |pmid= 2149559 |doi= }}
*{{cite journal | author=Wilkinson MM, Busuttil A, Hayward C, ''et al.'' |title=Expression pattern of two related cystic fibrosis-associated calcium-binding proteins in normal and abnormal tissues. |journal=J. Cell. Sci. |volume=91 ( Pt 2) |issue= |pages= 221-30 |year= 1989 |pmid= 3267695 |doi= }}
*{{cite journal | author=Odink K, Cerletti N, Brüggen J, ''et al.'' |title=Two calcium-binding proteins in infiltrate macrophages of rheumatoid arthritis. |journal=Nature |volume=330 |issue= 6143 |pages= 80-2 |year= 1987 |pmid= 3313057 |doi= 10.1038/330080a0 }}
*{{cite journal | author=Lagasse E, Clerc RG |title=Cloning and expression of two human genes encoding calcium-binding proteins that are regulated during myeloid differentiation. |journal=Mol. Cell. Biol. |volume=8 |issue= 6 |pages= 2402-10 |year= 1988 |pmid= 3405210 |doi= }}
*{{cite journal | author=Dorin JR, Novak M, Hill RE, ''et al.'' |title=A clue to the basic defect in cystic fibrosis from cloning the CF antigen gene. |journal=Nature |volume=326 |issue= 6113 |pages= 614-7 |year= 1987 |pmid= 3561500 |doi= 10.1038/326614a0 }}
*{{cite journal | author=Schäfer BW, Wicki R, Engelkamp D, ''et al.'' |title=Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21: rationale for a new nomenclature of the S100 calcium-binding protein family. |journal=Genomics |volume=25 |issue= 3 |pages= 638-43 |year= 1995 |pmid= 7759097 |doi= }}
*{{cite journal | author=Umekawa T, Kurita T |title=Calprotectin-like protein is related to soluble organic matrix in calcium oxalate urinary stone. |journal=Biochem. Mol. Biol. Int. |volume=34 |issue= 2 |pages= 309-13 |year= 1995 |pmid= 7849642 |doi= }}
*{{cite journal | author=Engelkamp D, Schäfer BW, Mattei MG, ''et al.'' |title=Six S100 genes are clustered on human chromosome 1q21: identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 14 |pages= 6547-51 |year= 1993 |pmid= 8341667 |doi= }}
*{{cite journal | author=Roth J, Burwinkel F, van den Bos C, ''et al.'' |title=MRP8 and MRP14, S-100-like proteins associated with myeloid differentiation, are translocated to plasma membrane and intermediate filaments in a calcium-dependent manner. |journal=Blood |volume=82 |issue= 6 |pages= 1875-83 |year= 1993 |pmid= 8400238 |doi= }}
*{{cite journal | author=Miyasaki KT, Bodeau AL, Murthy AR, Lehrer RI |title=In vitro antimicrobial activity of the human neutrophil cytosolic S-100 protein complex, calprotectin, against Capnocytophaga sputigena. |journal=J. Dent. Res. |volume=72 |issue= 2 |pages= 517-23 |year= 1993 |pmid= 8423249 |doi= }}
*{{cite journal | author=Marti T, Erttmann KD, Gallin MY |title=Host-parasite interaction in human onchocerciasis: identification and sequence analysis of a novel human calgranulin. |journal=Biochem. Biophys. Res. Commun. |volume=221 |issue= 2 |pages= 454-8 |year= 1996 |pmid= 8619876 |doi= 10.1006/bbrc.1996.0616 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SFN... {November 15, 2007 4:34:10 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 4:34:52 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
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}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_SFN_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ywt.
| PDB = {{PDB2|1ywt}}, {{PDB2|1yz5}}
| Name = Stratifin
| HGNCid = 10773
| Symbol = SFN
| AltSymbols =; YWHAS
| OMIM = 601290
| ECnumber =
| Homologene = 4475
| MGIid = 1891831
| GeneAtlas_image1 = PBB_GE_SFN_33322_i_at_tn.png
| GeneAtlas_image2 = PBB_GE_SFN_33323_r_at_tn.png
| GeneAtlas_image3 = PBB_GE_SFN_209260_at_tn.png
| Function = {{GNF_GO|id=GO:0008426 |text = protein kinase C inhibitor activity}} {{GNF_GO|id=GO:0019904 |text = protein domain specific binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0000079 |text = regulation of cyclin-dependent protein kinase activity}} {{GNF_GO|id=GO:0006469 |text = negative regulation of protein kinase activity}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0030216 |text = keratinocyte differentiation}} {{GNF_GO|id=GO:0043588 |text = skin development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2810
| Hs_Ensembl = ENSG00000175793
| Hs_RefseqProtein = NP_006133
| Hs_RefseqmRNA = NM_006142
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 27062216
| Hs_GenLoc_end = 27063535
| Hs_Uniprot = P31947
| Mm_EntrezGene = 55948
| Mm_Ensembl = ENSMUSG00000047281
| Mm_RefseqmRNA = NM_018754
| Mm_RefseqProtein = NP_061224
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 132873099
| Mm_GenLoc_end = 132873845
| Mm_Uniprot = Q3TEZ1
}}
}}
'''Stratifin''', also known as '''SFN''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: SFN stratifin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2810| 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=Hermeking H |title=Extracellular 14-3-3sigma protein: a potential mediator of epithelial-mesenchymal interactions. |journal=J. Invest. Dermatol. |volume=124 |issue= 1 |pages= ix-x |year= 2005 |pmid= 15654940 |doi= 10.1111/j.0022-202X.2004.23534.x }}
*{{cite journal | author=Mhawech P |title=14-3-3 proteins--an update. |journal=Cell Res. |volume=15 |issue= 4 |pages= 228-36 |year= 2005 |pmid= 15857577 |doi= 10.1038/sj.cr.7290291 }}
*{{cite journal | author=Lodygin D, Hermeking H |title=The role of epigenetic inactivation of 14-3-3sigma in human cancer. |journal=Cell Res. |volume=15 |issue= 4 |pages= 237-46 |year= 2005 |pmid= 15857578 |doi= 10.1038/sj.cr.7290292 }}
*{{cite journal | author=Rasmussen HH, van Damme J, Puype M, ''et al.'' |title=Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 960-9 |year= 1993 |pmid= 1286667 |doi= }}
*{{cite journal | author=Prasad GL, Valverius EM, McDuffie E, Cooper HL |title=Complementary DNA cloning of a novel epithelial cell marker protein, HME1, that may be down-regulated in neoplastic mammary cells. |journal=Cell Growth Differ. |volume=3 |issue= 8 |pages= 507-13 |year= 1992 |pmid= 1390337 |doi= }}
*{{cite journal | author=Leffers H, Madsen P, Rasmussen HH, ''et al.'' |title=Molecular cloning and expression of the transformation sensitive epithelial marker stratifin. A member of a protein family that has been involved in the protein kinase C signalling pathway. |journal=J. Mol. Biol. |volume=231 |issue= 4 |pages= 982-98 |year= 1993 |pmid= 8515476 |doi= 10.1006/jmbi.1993.1346 }}
*{{cite journal | author=Hermeking H, Lengauer C, Polyak K, ''et al.'' |title=14-3-3 sigma is a p53-regulated inhibitor of G2/M progression. |journal=Mol. Cell |volume=1 |issue= 1 |pages= 3-11 |year= 1998 |pmid= 9659898 |doi= }}
*{{cite journal | author=Chan TA, Hermeking H, Lengauer C, ''et al.'' |title=14-3-3Sigma is required to prevent mitotic catastrophe after DNA damage. |journal=Nature |volume=401 |issue= 6753 |pages= 616-20 |year= 1999 |pmid= 10524633 |doi= 10.1038/44188 }}
*{{cite journal | author=Laronga C, Yang HY, Neal C, Lee MH |title=Association of the cyclin-dependent kinases and 14-3-3 sigma negatively regulates cell cycle progression. |journal=J. Biol. Chem. |volume=275 |issue= 30 |pages= 23106-12 |year= 2000 |pmid= 10767298 |doi= 10.1074/jbc.M905616199 }}
*{{cite journal | author=Samuel T, Weber HO, Rauch P, ''et al.'' |title=The G2/M regulator 14-3-3sigma prevents apoptosis through sequestration of Bax. |journal=J. Biol. Chem. |volume=276 |issue= 48 |pages= 45201-6 |year= 2002 |pmid= 11574543 |doi= 10.1074/jbc.M106427200 }}
*{{cite journal | author=Johnson BA, Stehn JR, Yaffe MB, Blackwell TK |title=Cytoplasmic localization of tristetraprolin involves 14-3-3-dependent and -independent mechanisms. |journal=J. Biol. Chem. |volume=277 |issue= 20 |pages= 18029-36 |year= 2002 |pmid= 11886850 |doi= 10.1074/jbc.M110465200 }}
*{{cite journal | author=Tian H, Faje AT, Lee SL, Jorgensen TJ |title=Radiation-induced phosphorylation of Chk1 at S345 is associated with p53-dependent cell cycle arrest pathways. |journal=Neoplasia |volume=4 |issue= 2 |pages= 171-80 |year= 2002 |pmid= 11896572 |doi= 10.1038/sj/neo/7900219 }}
*{{cite journal | author=Ku NO, Michie S, Resurreccion EZ, ''et al.'' |title=Keratin binding to 14-3-3 proteins modulates keratin filaments and hepatocyte mitotic progression. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 7 |pages= 4373-8 |year= 2002 |pmid= 11917136 |doi= 10.1073/pnas.072624299 }}
*{{cite journal | author=Urano T, Saito T, Tsukui T, ''et al.'' |title=Efp targets 14-3-3 sigma for proteolysis and promotes breast tumour growth. |journal=Nature |volume=417 |issue= 6891 |pages= 871-5 |year= 2002 |pmid= 12075357 |doi= 10.1038/nature00826 }}
*{{cite journal | author=Liu MY, Cai S, Espejo A, ''et al.'' |title=14-3-3 interacts with the tumor suppressor tuberin at Akt phosphorylation site(s). |journal=Cancer Res. |volume=62 |issue= 22 |pages= 6475-80 |year= 2002 |pmid= 12438239 |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=Bhatia K, Siraj AK, Hussain A, ''et al.'' |title=The tumor suppressor gene 14-3-3 sigma is commonly methylated in normal and malignant lymphoid cells. |journal=Cancer Epidemiol. Biomarkers Prev. |volume=12 |issue= 2 |pages= 165-9 |year= 2003 |pmid= 12582028 |doi= }}
*{{cite journal | author=Kino T, Souvatzoglou E, De Martino MU, ''et al.'' |title=Protein 14-3-3sigma interacts with and favors cytoplasmic subcellular localization of the glucocorticoid receptor, acting as a negative regulator of the glucocorticoid signaling pathway. |journal=J. Biol. Chem. |volume=278 |issue= 28 |pages= 25651-6 |year= 2003 |pmid= 12730237 |doi= 10.1074/jbc.M302818200 }}
*{{cite journal | author=Nakajima T, Shimooka H, Weixa P, ''et al.'' |title=Immunohistochemical demonstration of 14-3-3 sigma protein in normal human tissues and lung cancers, and the preponderance of its strong expression in epithelial cells of squamous cell lineage. |journal=Pathol. Int. |volume=53 |issue= 6 |pages= 353-60 |year= 2004 |pmid= 12787309 |doi= }}
*{{cite journal | author=Rishi AK, Zhang L, Boyanapalli M, ''et al.'' |title=Identification and characterization of a cell cycle and apoptosis regulatory protein-1 as a novel mediator of apoptosis signaling by retinoid CD437. |journal=J. Biol. Chem. |volume=278 |issue= 35 |pages= 33422-35 |year= 2003 |pmid= 12816952 |doi= 10.1074/jbc.M303173200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TGFB2... {November 15, 2007 4:43:03 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 4:43:43 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_TGFB2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1tfg.
| PDB = {{PDB2|1tfg}}, {{PDB2|2tgi}}
| Name = Transforming growth factor, beta 2
| HGNCid = 11768
| Symbol = TGFB2
| AltSymbols =; MGC116892; TGF-beta2
| OMIM = 190220
| ECnumber =
| Homologene = 2432
| MGIid = 98726
| GeneAtlas_image1 = PBB_GE_TGFB2_209908_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_TGFB2_209909_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_TGFB2_220407_s_at_tn.png
| Function = {{GNF_GO|id=GO:0001540 |text = beta-amyloid binding}} {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005160 |text = transforming growth factor beta receptor binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0046982 |text = protein heterodimerization activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0030424 |text = axon}} {{GNF_GO|id=GO:0043025 |text = cell soma}}
| Process = {{GNF_GO|id=GO:0000902 |text = cell morphogenesis}} {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0001654 |text = eye development}} {{GNF_GO|id=GO:0001707 |text = mesoderm formation}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0008219 |text = cell death}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0009790 |text = embryonic development}} {{GNF_GO|id=GO:0010002 |text = cardioblast differentiation}} {{GNF_GO|id=GO:0016049 |text = cell growth}} {{GNF_GO|id=GO:0030097 |text = hemopoiesis}} {{GNF_GO|id=GO:0030307 |text = positive regulation of cell growth}} {{GNF_GO|id=GO:0030593 |text = neutrophil chemotaxis}} {{GNF_GO|id=GO:0031069 |text = hair follicle morphogenesis}} {{GNF_GO|id=GO:0042060 |text = wound healing}} {{GNF_GO|id=GO:0042416 |text = dopamine biosynthetic process}} {{GNF_GO|id=GO:0042637 |text = catagen}} {{GNF_GO|id=GO:0043525 |text = positive regulation of neuron apoptosis}} {{GNF_GO|id=GO:0045617 |text = negative regulation of keratinocyte differentiation}} {{GNF_GO|id=GO:0045787 |text = positive regulation of progression through cell cycle}} {{GNF_GO|id=GO:0045823 |text = positive regulation of heart contraction}} {{GNF_GO|id=GO:0048103 |text = somatic stem cell division}} {{GNF_GO|id=GO:0048666 |text = neuron development}} {{GNF_GO|id=GO:0048699 |text = generation of neurons}} {{GNF_GO|id=GO:0050777 |text = negative regulation of immune response}} {{GNF_GO|id=GO:0050778 |text = positive regulation of immune response}} {{GNF_GO|id=GO:0051795 |text = positive regulation of catagen}} {{GNF_GO|id=GO:0051891 |text = positive regulation of cardioblast differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7042
| Hs_Ensembl = ENSG00000092969
| Hs_RefseqProtein = NP_003229
| Hs_RefseqmRNA = NM_003238
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 216586200
| Hs_GenLoc_end = 216684584
| Hs_Uniprot = P61812
| Mm_EntrezGene = 21808
| Mm_Ensembl = ENSMUSG00000039239
| Mm_RefseqmRNA = NM_009367
| Mm_RefseqProtein = NP_033393
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 188324430
| Mm_GenLoc_end = 188406777
| Mm_Uniprot = Q3TWH5
}}
}}
'''Transforming growth factor, beta 2''', also known as '''TGFB2''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: TGFB2 transforming growth factor, beta 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7042| 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=Clark DA, Coker R |title=Transforming growth factor-beta (TGF-beta). |journal=Int. J. Biochem. Cell Biol. |volume=30 |issue= 3 |pages= 293-8 |year= 1998 |pmid= 9611771 |doi= }}
*{{cite journal | author=Wick W, Platten M, Weller M |title=Glioma cell invasion: regulation of metalloproteinase activity by TGF-beta. |journal=J. Neurooncol. |volume=53 |issue= 2 |pages= 177-85 |year= 2002 |pmid= 11716069 |doi= }}
*{{cite journal | author=Bissell DM |title=Chronic liver injury, TGF-beta, and cancer. |journal=Exp. Mol. Med. |volume=33 |issue= 4 |pages= 179-90 |year= 2002 |pmid= 11795478 |doi= }}
*{{cite journal | author=Kalluri R, Neilson EG |title=Epithelial-mesenchymal transition and its implications for fibrosis. |journal=J. Clin. Invest. |volume=112 |issue= 12 |pages= 1776-84 |year= 2004 |pmid= 14679171 |doi= 10.1172/JCI200320530 }}
*{{cite journal | author=Daopin S, Piez KA, Ogawa Y, Davies DR |title=Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily. |journal=Science |volume=257 |issue= 5068 |pages= 369-73 |year= 1992 |pmid= 1631557 |doi= }}
*{{cite journal | author=Schlunegger MP, Grütter MG |title=An unusual feature revealed by the crystal structure at 2.2 A resolution of human transforming growth factor-beta 2. |journal=Nature |volume=358 |issue= 6385 |pages= 430-4 |year= 1992 |pmid= 1641027 |doi= 10.1038/358430a0 }}
*{{cite journal | author=Noma T, Glick AB, Geiser AG, ''et al.'' |title=Molecular cloning and structure of the human transforming growth factor-beta 2 gene promoter. |journal=Growth Factors |volume=4 |issue= 4 |pages= 247-55 |year= 1992 |pmid= 1764261 |doi= }}
*{{cite journal | author=Bodmer S, Podlisny MB, Selkoe DJ, ''et al.'' |title=Transforming growth factor-beta bound to soluble derivatives of the beta amyloid precursor protein of Alzheimer's disease. |journal=Biochem. Biophys. Res. Commun. |volume=171 |issue= 2 |pages= 890-7 |year= 1990 |pmid= 2119582 |doi= }}
*{{cite journal | author=Webb NR, Madisen L, Rose TM, Purchio AF |title=Structural and sequence analysis of TGF-beta 2 cDNA clones predicts two different precursor proteins produced by alternative mRNA splicing. |journal=DNA |volume=7 |issue= 7 |pages= 493-7 |year= 1989 |pmid= 2850146 |doi= }}
*{{cite journal | author=Madisen L, Webb NR, Rose TM, ''et al.'' |title=Transforming growth factor-beta 2: cDNA cloning and sequence analysis. |journal=DNA |volume=7 |issue= 1 |pages= 1-8 |year= 1988 |pmid= 3162414 |doi= }}
*{{cite journal | author=Barton DE, Foellmer BE, Du J, ''et al.'' |title=Chromosomal mapping of genes for transforming growth factors beta 2 and beta 3 in man and mouse: dispersion of TGF-beta gene family. |journal=Oncogene Res. |volume=3 |issue= 4 |pages= 323-31 |year= 1989 |pmid= 3226728 |doi= }}
*{{cite journal | author=de Martin R, Haendler B, Hofer-Warbinek R, ''et al.'' |title=Complementary DNA for human glioblastoma-derived T cell suppressor factor, a novel member of the transforming growth factor-beta gene family. |journal=EMBO J. |volume=6 |issue= 12 |pages= 3673-7 |year= 1988 |pmid= 3322813 |doi= }}
*{{cite journal | author=Marquardt H, Lioubin MN, Ikeda T |title=Complete amino acid sequence of human transforming growth factor type beta 2. |journal=J. Biol. Chem. |volume=262 |issue= 25 |pages= 12127-31 |year= 1987 |pmid= 3476488 |doi= }}
*{{cite journal | author=Philip A, Bostedt L, Stigbrand T, O'Connor-McCourt MD |title=Binding of transforming growth factor-beta (TGF-beta) to pregnancy zone protein (PZP). Comparison to the TGF-beta-alpha 2-macroglobulin interaction. |journal=Eur. J. Biochem. |volume=221 |issue= 2 |pages= 687-93 |year= 1994 |pmid= 7513640 |doi= }}
*{{cite journal | author=Lin HY, Moustakas A, Knaus P, ''et al.'' |title=The soluble exoplasmic domain of the type II transforming growth factor (TGF)-beta receptor. A heterogeneously glycosylated protein with high affinity and selectivity for TGF-beta ligands. |journal=J. Biol. Chem. |volume=270 |issue= 6 |pages= 2747-54 |year= 1995 |pmid= 7852346 |doi= }}
*{{cite journal | author=Hildebrand A, Romarís M, Rasmussen LM, ''et al.'' |title=Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta. |journal=Biochem. J. |volume=302 ( Pt 2) |issue= |pages= 527-34 |year= 1994 |pmid= 8093006 |doi= }}
*{{cite journal | author=López-Casillas F, Payne HM, Andres JL, Massagué J |title=Betaglycan can act as a dual modulator of TGF-beta access to signaling receptors: mapping of ligand binding and GAG attachment sites. |journal=J. Cell Biol. |volume=124 |issue= 4 |pages= 557-68 |year= 1994 |pmid= 8106553 |doi= }}
*{{cite journal | author=Fromigué O, Marie PJ, Lomri A |title=Bone morphogenetic protein-2 and transforming growth factor-beta2 interact to modulate human bone marrow stromal cell proliferation and differentiation. |journal=J. Cell. Biochem. |volume=68 |issue= 4 |pages= 411-26 |year= 1998 |pmid= 9493905 |doi= }}
*{{cite journal | author=Mori T, Kawara S, Shinozaki M, ''et al.'' |title=Role and interaction of connective tissue growth factor with transforming growth factor-beta in persistent fibrosis: A mouse fibrosis model. |journal=J. Cell. Physiol. |volume=181 |issue= 1 |pages= 153-9 |year= 1999 |pmid= 10457363 |doi= 10.1002/(SICI)1097-4652(199910)181:1<153::AID-JCP16>3.0.CO;2-K }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on VCP... {November 15, 2007 4:43:43 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 4:44:44 PM PST}
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{{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_VCP_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1e32.
| PDB = {{PDB2|1e32}}, {{PDB2|1oz4}}, {{PDB2|1r7r}}, {{PDB2|1s3s}}, {{PDB2|1ypw}}, {{PDB2|1yq0}}, {{PDB2|1yqi}}, {{PDB2|2pjh}}
| Name = Valosin-containing protein
| HGNCid = 12666
| Symbol = VCP
| AltSymbols =; p97; IBMPFD; MGC131997; MGC148092; MGC8560; TERA
| OMIM = 601023
| ECnumber =
| Homologene = 5168
| MGIid = 99919
| GeneAtlas_image1 = PBB_GE_VCP_208649_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_VCP_208648_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008289 |text = lipid binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016887 |text = ATPase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006302 |text = double-strand break repair}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006919 |text = caspase activation}} {{GNF_GO|id=GO:0016567 |text = protein ubiquitination}} {{GNF_GO|id=GO:0030433 |text = ER-associated protein catabolic process}} {{GNF_GO|id=GO:0030968 |text = unfolded protein response}} {{GNF_GO|id=GO:0030970 |text = retrograde protein transport, ER to cytosol}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}} {{GNF_GO|id=GO:0045184 |text = establishment of protein localization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7415
| Hs_Ensembl = ENSG00000165280
| Hs_RefseqProtein = NP_009057
| Hs_RefseqmRNA = NM_007126
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 35046061
| Hs_GenLoc_end = 35063246
| Hs_Uniprot = P55072
| Mm_EntrezGene = 269523
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_009503
| Mm_RefseqProtein = NP_033529
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Valosin-containing protein''', also known as '''VCP''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: VCP valosin-containing protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7415| 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 = Valosin-containing protein (VCP) is a member of a family that includes putative ATP-binding proteins involved in vesicle transport and fusion, 26S proteasome function, and assembly of peroxisomes. VCP, as a structural protein, is associated with clathrin, and heat-shock protein Hsc70, to form a complex. VCP has been implicated in a number of cellular events that are regulated during mitosis, including homotypic membrane fusion, spindle pole body function, and ubiquitin-dependent protein degradation.<ref>{{cite web | title = Entrez Gene: VCP valosin-containing protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7415| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi= }}
*{{cite journal | author=Rabouille C, Levine TP, Peters JM, Warren G |title=An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic Golgi fragments. |journal=Cell |volume=82 |issue= 6 |pages= 905-14 |year= 1995 |pmid= 7553851 |doi= }}
*{{cite journal | author=Pleasure IT, Black MM, Keen JH |title=Valosin-containing protein, VCP, is a ubiquitous clathrin-binding protein. |journal=Nature |volume=365 |issue= 6445 |pages= 459-62 |year= 1993 |pmid= 8413590 |doi= 10.1038/365459a0 }}
*{{cite journal | author=Druck T, Gu Y, Prabhala G, ''et al.'' |title=Chromosome localization of human genes for clathrin adaptor polypeptides AP2 beta and AP50 and the clathrin-binding protein, VCP. |journal=Genomics |volume=30 |issue= 1 |pages= 94-7 |year= 1996 |pmid= 8595912 |doi= 10.1006/geno.1995.0016 }}
*{{cite journal | author=Germain-Lee EL, Obie C, Valle D |title=NVL: a new member of the AAA family of ATPases localized to the nucleus. |journal=Genomics |volume=44 |issue= 1 |pages= 22-34 |year= 1997 |pmid= 9286697 |doi= 10.1006/geno.1997.4856 }}
*{{cite journal | author=Hoyle J, Tan KH, Fisher EM |title=Mapping the valosin-containing protein (VCP) gene on human chromosome 9 and mouse chromosome 4, and a likely pseudogene on the mouse X chromosome. |journal=Mamm. Genome |volume=8 |issue= 10 |pages= 778-80 |year= 1997 |pmid= 9321476 |doi= }}
*{{cite journal | author=Dai RM, Chen E, Longo DL, ''et al.'' |title=Involvement of valosin-containing protein, an ATPase Co-purified with IkappaBalpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalpha. |journal=J. Biol. Chem. |volume=273 |issue= 6 |pages= 3562-73 |year= 1998 |pmid= 9452483 |doi= }}
*{{cite journal | author=Rabouille C, Kondo H, Newman R, ''et al.'' |title=Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro. |journal=Cell |volume=92 |issue= 5 |pages= 603-10 |year= 1998 |pmid= 9506515 |doi= }}
*{{cite journal | author=Zhang SH, Liu J, Kobayashi R, Tonks NK |title=Identification of the cell cycle regulator VCP (p97/CDC48) as a substrate of the band 4.1-related protein-tyrosine phosphatase PTPH1. |journal=J. Biol. Chem. |volume=274 |issue= 25 |pages= 17806-12 |year= 1999 |pmid= 10364224 |doi= }}
*{{cite journal | author=Zhang H, Wang Q, Kajino K, Greene MI |title=VCP, a weak ATPase involved in multiple cellular events, interacts physically with BRCA1 in the nucleus of living cells. |journal=DNA Cell Biol. |volume=19 |issue= 5 |pages= 253-63 |year= 2000 |pmid= 10855792 |doi= 10.1089/10445490050021168 }}
*{{cite journal | author=Hu RM, Han ZG, Song HD, ''et al.'' |title=Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 17 |pages= 9543-8 |year= 2000 |pmid= 10931946 |doi= 10.1073/pnas.160270997 }}
*{{cite journal | author=Lavoie C, Chevet E, Roy L, ''et al.'' |title=Tyrosine phosphorylation of p97 regulates transitional endoplasmic reticulum assembly in vitro. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 25 |pages= 13637-42 |year= 2001 |pmid= 11087817 |doi= 10.1073/pnas.240278097 }}
*{{cite journal | author=Kimonis VE, Kovach MJ, Waggoner B, ''et al.'' |title=Clinical and molecular studies in a unique family with autosomal dominant limb-girdle muscular dystrophy and Paget disease of bone. |journal=Genet. Med. |volume=2 |issue= 4 |pages= 232-41 |year= 2001 |pmid= 11252708 |doi= }}
*{{cite journal | author=Seigneurin-Berny D, Verdel A, Curtet S, ''et al.'' |title=Identification of components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathways. |journal=Mol. Cell. Biol. |volume=21 |issue= 23 |pages= 8035-44 |year= 2001 |pmid= 11689694 |doi= 10.1128/MCB.21.23.8035-8044.2001 }}
*{{cite journal | author=Yang CS, Weiner H |title=Yeast two-hybrid screening identifies binding partners of human Tom34 that have ATPase activity and form a complex with Tom34 in the cytosol. |journal=Arch. Biochem. Biophys. |volume=400 |issue= 1 |pages= 105-10 |year= 2002 |pmid= 11913976 |doi= 10.1006/abbi.2002.2778 }}
*{{cite journal | author=Asai T, Tomita Y, Nakatsuka S, ''et al.'' |title=VCP (p97) regulates NFkappaB signaling pathway, which is important for metastasis of osteosarcoma cell line. |journal=Jpn. J. Cancer Res. |volume=93 |issue= 3 |pages= 296-304 |year= 2002 |pmid= 11927012 |doi= }}
*{{cite journal | author=Kobayashi T, Tanaka K, Inoue K, Kakizuka A |title=Functional ATPase activity of p97/valosin-containing protein (VCP) is required for the quality control of endoplasmic reticulum in neuronally differentiated mammalian PC12 cells. |journal=J. Biol. Chem. |volume=277 |issue= 49 |pages= 47358-65 |year= 2003 |pmid= 12351637 |doi= 10.1074/jbc.M207783200 }}
*{{cite journal | author=Uchiyama K, Jokitalo E, Kano F, ''et al.'' |title=VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo. |journal=J. Cell Biol. |volume=159 |issue= 5 |pages= 855-66 |year= 2003 |pmid= 12473691 |doi= 10.1083/jcb.200208112 }}
*{{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=Kaneko C, Hatakeyama S, Matsumoto M, ''et al.'' |title=Characterization of the mouse gene for the U-box-type ubiquitin ligase UFD2a. |journal=Biochem. Biophys. Res. Commun. |volume=300 |issue= 2 |pages= 297-304 |year= 2003 |pmid= 12504083 |doi= }}
}}
{{refend}}
{{protein-stub}}
end log.
