Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 20:57, 19 November 2007 (UTC)
[edit]Proteins without matches (8)
[edit]Proteins with a High Potential Match (6)
[edit]Redirected Proteins (11)
[edit]Manual Inspection (Page not found) (14)
[edit]
Protein Status Grid - Date: 20:57, 19 November 2007 (UTC)
[edit]Vebose Log - Date: 20:57, 19 November 2007 (UTC)
[edit]- INFO: Beginning work on CBFB... {November 19, 2007 12:05:37 PM PST}
- SEARCH REDIRECT: Control Box Found: CBFB {November 19, 2007 12:06:02 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:06:04 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:06:04 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:06:04 PM PST}
- UPDATED: Updated protein page: CBFB {November 19, 2007 12:06:10 PM PST}
- INFO: Beginning work on CCKAR... {November 19, 2007 12:06:10 PM PST}
- SEARCH REDIRECT: Control Box Found: CCKAR {November 19, 2007 12:13:38 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:13:39 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:13:39 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:13:39 PM PST}
- UPDATED: Updated protein page: CCKAR {November 19, 2007 12:13:46 PM PST}
- INFO: Beginning work on CD53... {November 19, 2007 12:14:27 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:14:52 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = CD53 molecule
| HGNCid = 1686
| Symbol = CD53
| AltSymbols =; MOX44; TSPAN25
| OMIM = 151525
| ECnumber =
| Homologene = 20152
| MGIid = 88341
| GeneAtlas_image1 = PBB_GE_CD53_203416_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0019735 |text = antimicrobial humoral response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 963
| Hs_Ensembl = ENSG00000143119
| Hs_RefseqProtein = NP_000551
| Hs_RefseqmRNA = NM_000560
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 111217284
| Hs_GenLoc_end = 111244069
| Hs_Uniprot = P19397
| Mm_EntrezGene = 12508
| Mm_Ensembl = ENSMUSG00000040747
| Mm_RefseqmRNA = NM_007651
| Mm_RefseqProtein = NP_031677
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 106887989
| Mm_GenLoc_end = 106918108
| Mm_Uniprot = Q3TV80
}}
}}
'''CD53 molecule''', also known as '''CD53''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CD53 CD53 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=963| 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 transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. This encoded protein is a cell surface glycoprotein that is known to complex with integrins. It contributes to the transduction of CD2-generated signals in T cells and natural killer cells and has been suggested to play a role in growth regulation. Familial deficiency of this gene has been linked to an immunodeficiency associated with recurrent infectious diseases caused by bacteria, fungi and viruses. Alternative splicing results in multiple transcript variants encoding the same protein.<ref name="entrez">{{cite web | title = Entrez Gene: CD53 CD53 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=963| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Horejsí V, Vlcek C |title=Novel structurally distinct family of leucocyte surface glycoproteins including CD9, CD37, CD53 and CD63. |journal=FEBS Lett. |volume=288 |issue= 1-2 |pages= 1-4 |year= 1991 |pmid= 1879540 |doi= }}
*{{cite journal | author=Berditchevski F |title=Complexes of tetraspanins with integrins: more than meets the eye. |journal=J. Cell. Sci. |volume=114 |issue= Pt 23 |pages= 4143-51 |year= 2002 |pmid= 11739647 |doi= }}
*{{cite journal | author=Bell GM, Seaman WE, Niemi EC, Imboden JB |title=The OX-44 molecule couples to signaling pathways and is associated with CD2 on rat T lymphocytes and a natural killer cell line. |journal=J. Exp. Med. |volume=175 |issue= 2 |pages= 527-36 |year= 1992 |pmid= 1346273 |doi= }}
*{{cite journal | author=Angelisová P, Vlcek C, Stefanová I, ''et al.'' |title=The human leucocyte surface antigen CD53 is a protein structurally similar to the CD37 and MRC OX-44 antigens. |journal=Immunogenetics |volume=32 |issue= 4 |pages= 281-5 |year= 1990 |pmid= 1700763 |doi= }}
*{{cite journal | author=Amiot M |title=Identification and analysis of cDNA clones encoding CD53. A pan-leukocyte antigen related to membrane transport proteins. |journal=J. Immunol. |volume=145 |issue= 12 |pages= 4322-5 |year= 1991 |pmid= 2258620 |doi= }}
*{{cite journal | author=Dianzani U, Bragardo M, Buonfiglio D, ''et al.'' |title=Modulation of CD4 lateral interaction with lymphocyte surface molecules induced by HIV-1 gp120. |journal=Eur. J. Immunol. |volume=25 |issue= 5 |pages= 1306-11 |year= 1995 |pmid= 7539755 |doi= }}
*{{cite journal | author=Carmo AM, Wright MD |title=Association of the transmembrane 4 superfamily molecule CD53 with a tyrosine phosphatase activity. |journal=Eur. J. Immunol. |volume=25 |issue= 7 |pages= 2090-5 |year= 1995 |pmid= 7621882 |doi= }}
*{{cite journal | author=Rasmussen AM, Blomhoff HK, Stokke T, ''et al.'' |title=Cross-linking of CD53 promotes activation of resting human B lymphocytes. |journal=J. Immunol. |volume=153 |issue= 11 |pages= 4997-5007 |year= 1994 |pmid= 7963560 |doi= }}
*{{cite journal | author=Gonzalez ME, Pardo-Manuel de Villena F, Fernandez-Ruiz E, ''et al.'' |title=The human CD53 gene, coding for a four transmembrane domain protein, maps to chromosomal region 1p13. |journal=Genomics |volume=18 |issue= 3 |pages= 725-8 |year= 1994 |pmid= 8307585 |doi= }}
*{{cite journal | author=Korínek V, Horejsí V |title=Genomic structure of the human CD53 gene. |journal=Immunogenetics |volume=38 |issue= 4 |pages= 272-9 |year= 1993 |pmid= 8319976 |doi= }}
*{{cite journal | author=Olweus J, Lund-Johansen F, Horejsi V |title=CD53, a protein with four membrane-spanning domains, mediates signal transduction in human monocytes and B cells. |journal=J. Immunol. |volume=151 |issue= 2 |pages= 707-16 |year= 1993 |pmid= 8335905 |doi= }}
*{{cite journal | author=Taguchi T, Bellacosa A, Zhou JY, ''et al.'' |title=Chromosomal localization of the Ox-44 (CD53) leukocyte antigen gene in man and rodents. |journal=Cytogenet. Cell Genet. |volume=64 |issue= 3-4 |pages= 217-21 |year= 1993 |pmid= 8404042 |doi= }}
*{{cite journal | author=Virtaneva KI, Angelisová P, Baumruker T, ''et al.'' |title=The genes for CD37, CD53, and R2, all members of a novel gene family, are located on different chromosomes. |journal=Immunogenetics |volume=37 |issue= 6 |pages= 461-5 |year= 1993 |pmid= 8436422 |doi= }}
*{{cite journal | author=Wright MD, Rochelle JM, Tomlinson MG, ''et al.'' |title=Gene structure, chromosomal localization, and protein sequence of mouse CD53 (Cd53): evidence that the transmembrane 4 superfamily arose by gene duplication. |journal=Int. Immunol. |volume=5 |issue= 2 |pages= 209-16 |year= 1993 |pmid= 8452817 |doi= }}
*{{cite journal | author=Mannion BA, Berditchevski F, Kraeft SK, ''et al.'' |title=Transmembrane-4 superfamily proteins CD81 (TAPA-1), CD82, CD63, and CD53 specifically associated with integrin alpha 4 beta 1 (CD49d/CD29). |journal=J. Immunol. |volume=157 |issue= 5 |pages= 2039-47 |year= 1996 |pmid= 8757325 |doi= }}
*{{cite journal | author=Szöllósi J, Horejsí V, Bene L, ''et al.'' |title=Supramolecular complexes of MHC class I, MHC class II, CD20, and tetraspan molecules (CD53, CD81, and CD82) at the surface of a B cell line JY. |journal=J. Immunol. |volume=157 |issue= 7 |pages= 2939-46 |year= 1996 |pmid= 8816400 |doi= }}
*{{cite journal | author=Okochi H, Kato M, Nashiro K, ''et al.'' |title=Expression of tetra-spans transmembrane family (CD9, CD37, CD53, CD63, CD81 and CD82) in normal and neoplastic human keratinocytes: an association of CD9 with alpha 3 beta 1 integrin. |journal=Br. J. Dermatol. |volume=137 |issue= 6 |pages= 856-63 |year= 1998 |pmid= 9470900 |doi= }}
*{{cite journal | author=Nichols TC, Guthridge JM, Karp DR, ''et al.'' |title=Gamma-glutamyl transpeptidase, an ecto-enzyme regulator of intracellular redox potential, is a component of TM4 signal transduction complexes. |journal=Eur. J. Immunol. |volume=28 |issue= 12 |pages= 4123-9 |year= 1999 |pmid= 9862348 |doi= }}
*{{cite journal | author=Serru V, Le Naour F, Billard M, ''et al.'' |title=Selective tetraspan-integrin complexes (CD81/alpha4beta1, CD151/alpha3beta1, CD151/alpha6beta1) under conditions disrupting tetraspan interactions. |journal=Biochem. J. |volume=340 ( Pt 1) |issue= |pages= 103-11 |year= 1999 |pmid= 10229664 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CDT1... {November 19, 2007 12:49:50 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:50:19 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
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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 = Chromatin licensing and DNA replication factor 1
| HGNCid = 24576
| Symbol = CDT1
| AltSymbols =; DUP; RIS2
| OMIM = 605525
| ECnumber =
| Homologene = 32650
| MGIid = 1914427
| GeneAtlas_image1 = PBB_GE_CDT1_209832_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005657 |text = replication fork}}
| Process = {{GNF_GO|id=GO:0000076 |text = DNA replication checkpoint}} {{GNF_GO|id=GO:0006260 |text = DNA replication}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007090 |text = regulation of S phase of mitotic cell cycle}} {{GNF_GO|id=GO:0030174 |text = regulation of DNA replication initiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 81620
| Hs_Ensembl = ENSG00000167513
| Hs_RefseqProtein = NP_112190
| Hs_RefseqmRNA = NM_030928
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 87397687
| Hs_GenLoc_end = 87403166
| Hs_Uniprot = Q9H211
| Mm_EntrezGene = 67177
| Mm_Ensembl = ENSMUSG00000006585
| Mm_RefseqmRNA = NM_026014
| Mm_RefseqProtein = NP_080290
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 125454116
| Mm_GenLoc_end = 125459644
| Mm_Uniprot = Q8R4E9
}}
}}
'''Chromatin licensing and DNA replication factor 1''', also known as '''CDT1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CDT1 chromatin licensing and DNA replication factor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=81620| 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=Xouri G, Dimaki M, Bastiaens PI, Lygerou Z |title=Cdt1 interactions in the licensing process: a model for dynamic spatiotemporal control of licensing. |journal=Cell Cycle |volume=6 |issue= 13 |pages= 1549-52 |year= 2007 |pmid= 17598984 |doi= }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi= }}
*{{cite journal | author=Nishitani H, Lygerou Z, Nishimoto T, Nurse P |title=The Cdt1 protein is required to license DNA for replication in fission yeast. |journal=Nature |volume=404 |issue= 6778 |pages= 625-8 |year= 2000 |pmid= 10766248 |doi= 10.1038/35007110 }}
*{{cite journal | author=Whittaker AJ, Royzman I, Orr-Weaver TL |title=Drosophila double parked: a conserved, essential replication protein that colocalizes with the origin recognition complex and links DNA replication with mitosis and the down-regulation of S phase transcripts. |journal=Genes Dev. |volume=14 |issue= 14 |pages= 1765-76 |year= 2000 |pmid= 10898791 |doi= }}
*{{cite journal | author=Wohlschlegel JA, Dwyer BT, Dhar SK, ''et al.'' |title=Inhibition of eukaryotic DNA replication by geminin binding to Cdt1. |journal=Science |volume=290 |issue= 5500 |pages= 2309-12 |year= 2001 |pmid= 11125146 |doi= 10.1126/science.290.5500.2309 }}
*{{cite journal | author=Nishitani H, Taraviras S, Lygerou Z, Nishimoto T |title=The human licensing factor for DNA replication Cdt1 accumulates in G1 and is destabilized after initiation of S-phase. |journal=J. Biol. Chem. |volume=276 |issue= 48 |pages= 44905-11 |year= 2002 |pmid= 11555648 |doi= 10.1074/jbc.M105406200 }}
*{{cite journal | author=Rialland M, Sola F, Santocanale C |title=Essential role of human CDT1 in DNA replication and chromatin licensing. |journal=J. Cell. Sci. |volume=115 |issue= Pt 7 |pages= 1435-40 |year= 2002 |pmid= 11896191 |doi= }}
*{{cite journal | author=Yanagi K, Mizuno T, You Z, Hanaoka F |title=Mouse geminin inhibits not only Cdt1-MCM6 interactions but also a novel intrinsic Cdt1 DNA binding activity. |journal=J. Biol. Chem. |volume=277 |issue= 43 |pages= 40871-80 |year= 2002 |pmid= 12192004 |doi= 10.1074/jbc.M206202200 }}
*{{cite journal | author=Bermejo R, Vilaboa N, Calés C |title=Regulation of CDC6, geminin, and CDT1 in human cells that undergo polyploidization. |journal=Mol. Biol. Cell |volume=13 |issue= 11 |pages= 3989-4000 |year= 2003 |pmid= 12429841 |doi= 10.1091/mbc.E02-04-0217 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Li X, Zhao Q, Liao R, ''et al.'' |title=The SCF(Skp2) ubiquitin ligase complex interacts with the human replication licensing factor Cdt1 and regulates Cdt1 degradation. |journal=J. Biol. Chem. |volume=278 |issue= 33 |pages= 30854-8 |year= 2003 |pmid= 12840033 |doi= 10.1074/jbc.C300251200 }}
*{{cite journal | author=Cook JG, Chasse DA, Nevins JR |title=The regulated association of Cdt1 with minichromosome maintenance proteins and Cdc6 in mammalian cells. |journal=J. Biol. Chem. |volume=279 |issue= 10 |pages= 9625-33 |year= 2004 |pmid= 14672932 |doi= 10.1074/jbc.M311933200 }}
*{{cite journal | author=Sugimoto N, Tatsumi Y, Tsurumi T, ''et al.'' |title=Cdt1 phosphorylation by cyclin A-dependent kinases negatively regulates its function without affecting geminin binding. |journal=J. Biol. Chem. |volume=279 |issue= 19 |pages= 19691-7 |year= 2004 |pmid= 14993212 |doi= 10.1074/jbc.M313175200 }}
*{{cite journal | author=Liu E, Li X, Yan F, ''et al.'' |title=Cyclin-dependent kinases phosphorylate human Cdt1 and induce its degradation. |journal=J. Biol. Chem. |volume=279 |issue= 17 |pages= 17283-8 |year= 2004 |pmid= 15004027 |doi= 10.1074/jbc.C300549200 }}
*{{cite journal | author=Ramachandran N, Hainsworth E, Bhullar B, ''et al.'' |title=Self-assembling protein microarrays. |journal=Science |volume=305 |issue= 5680 |pages= 86-90 |year= 2004 |pmid= 15232106 |doi= 10.1126/science.1097639 }}
*{{cite journal | author=Ballabeni A, Melixetian M, Zamponi R, ''et al.'' |title=Human geminin promotes pre-RC formation and DNA replication by stabilizing CDT1 in mitosis. |journal=EMBO J. |volume=23 |issue= 15 |pages= 3122-32 |year= 2005 |pmid= 15257290 |doi= 10.1038/sj.emboj.7600314 }}
*{{cite journal | author=Saxena S, Yuan P, Dhar SK, ''et al.'' |title=A dimerized coiled-coil domain and an adjoining part of geminin interact with two sites on Cdt1 for replication inhibition. |journal=Mol. Cell |volume=15 |issue= 2 |pages= 245-58 |year= 2004 |pmid= 15260975 |doi= 10.1016/j.molcel.2004.06.045 }}
*{{cite journal | author=Kulartz M, Knippers R |title=The replicative regulator protein geminin on chromatin in the HeLa cell cycle. |journal=J. Biol. Chem. |volume=279 |issue= 40 |pages= 41686-94 |year= 2004 |pmid= 15284237 |doi= 10.1074/jbc.M405798200 }}
*{{cite journal | author=Beausoleil SA, Jedrychowski M, Schwartz D, ''et al.'' |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130-5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CES1... {November 19, 2007 12:14:52 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:15:35 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_CES1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1mx1.
| PDB = {{PDB2|1mx1}}, {{PDB2|1mx5}}, {{PDB2|1mx9}}, {{PDB2|1ya4}}, {{PDB2|1ya8}}, {{PDB2|1yah}}, {{PDB2|1yaj}}, {{PDB2|2dqy}}, {{PDB2|2dqz}}, {{PDB2|2dr0}}, {{PDB2|2h7c}}, {{PDB2|2hrq}}, {{PDB2|2hrr}}
| Name = Carboxylesterase 1 (monocyte/macrophage serine esterase 1)
| HGNCid = 1863
| Symbol = CES1
| AltSymbols =; ACAT; CEH; CES2; HMSE; HMSE1; MGC117365; PCE-1; SES1; TGH
| OMIM = 114835
| ECnumber =
| Homologene = 35606
| MGIid = 2148202
| Function = {{GNF_GO|id=GO:0004091 |text = carboxylesterase activity}} {{GNF_GO|id=GO:0004759 |text = carboxylesterase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}}
| Process = {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0009636 |text = response to toxin}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1066
| Hs_Ensembl =
| Hs_RefseqProtein = XP_001130190
| Hs_RefseqmRNA = XM_001130190
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 104158
| Mm_Ensembl = ENSMUSG00000056973
| Mm_RefseqmRNA = NM_053200
| Mm_RefseqProtein = NP_444430
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 96055196
| Mm_GenLoc_end = 96086907
| Mm_Uniprot = Q8VCT4
}}
}}
'''Carboxylesterase 1 (monocyte/macrophage serine esterase 1)''', also known as '''CES1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CES1 carboxylesterase 1 (monocyte/macrophage serine esterase 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1066| 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 = Carboxylesterase 1 is a member of a large multigene family. The enzymes encoded by these genes are responsible for the hydrolysis of ester- and amide-bond-containing drugs such as cocaine and heroin. They also hydrolize long-chain fatty acid esters and thioesters. This enzyme is known to hydrolyze aromatic and aliphatic esters and is necessary for cellular cholesterol esterification. It may also play a role in detoxification in the lung and/or protection of the central nervous system from ester or amide compounds. Carboxylesterase deficiency may be associated with non-Hodgkin lymphoma or B-cell lymphocytic leukemia. Three transcript variants encoding three different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: CES1 carboxylesterase 1 (monocyte/macrophage serine esterase 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1066| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Riddles PW, Richards LJ, Bowles MR, Pond SM |title=Cloning and analysis of a cDNA encoding a human liver carboxylesterase. |journal=Gene |volume=108 |issue= 2 |pages= 289-92 |year= 1992 |pmid= 1748313 |doi= }}
*{{cite journal | author=Munger JS, Shi GP, Mark EA, ''et al.'' |title=A serine esterase released by human alveolar macrophages is closely related to liver microsomal carboxylesterases. |journal=J. Biol. Chem. |volume=266 |issue= 28 |pages= 18832-8 |year= 1991 |pmid= 1918003 |doi= }}
*{{cite journal | author=Long RM, Calabrese MR, Martin BM, Pohl LR |title=Cloning and sequencing of a human liver carboxylesterase isoenzyme. |journal=Life Sci. |volume=48 |issue= 11 |pages= PL43-9 |year= 1991 |pmid= 1997784 |doi= }}
*{{cite journal | author=Zschunke F, Salmassi A, Kreipe H, ''et al.'' |title=cDNA cloning and characterization of human monocyte/macrophage serine esterase-1. |journal=Blood |volume=78 |issue= 2 |pages= 506-12 |year= 1991 |pmid= 2070086 |doi= }}
*{{cite journal | author=Ketterman AJ, Bowles MR, Pond SM |title=Purification and characterization of two human liver carboxylesterases. |journal=Int. J. Biochem. |volume=21 |issue= 12 |pages= 1303-12 |year= 1990 |pmid= 2612723 |doi= }}
*{{cite journal | author=Becker A, Böttcher A, Lackner KJ, ''et al.'' |title=Purification, cloning, and expression of a human enzyme with acyl coenzyme A: cholesterol acyltransferase activity, which is identical to liver carboxylesterase. |journal=Arterioscler. Thromb. |volume=14 |issue= 8 |pages= 1346-55 |year= 1994 |pmid= 8049197 |doi= }}
*{{cite journal | author=Kroetz DL, McBride OW, Gonzalez FJ |title=Glycosylation-dependent activity of baculovirus-expressed human liver carboxylesterases: cDNA cloning and characterization of two highly similar enzyme forms. |journal=Biochemistry |volume=32 |issue= 43 |pages= 11606-17 |year= 1993 |pmid= 8218228 |doi= }}
*{{cite journal | author=Shibata F, Takagi Y, Kitajima M, ''et al.'' |title=Molecular cloning and characterization of a human carboxylesterase gene. |journal=Genomics |volume=17 |issue= 1 |pages= 76-82 |year= 1993 |pmid= 8406473 |doi= 10.1006/geno.1993.1285 }}
*{{cite journal | author=Langmann T, Becker A, Aslanidis C, ''et al.'' |title=Structural organization and characterization of the promoter region of a human carboxylesterase gene. |journal=Biochim. Biophys. Acta |volume=1350 |issue= 1 |pages= 65-74 |year= 1997 |pmid= 9003459 |doi= }}
*{{cite journal | author=Brzezinski MR, Spink BJ, Dean RA, ''et al.'' |title=Human liver carboxylesterase hCE-1: binding specificity for cocaine, heroin, and their metabolites and analogs. |journal=Drug Metab. Dispos. |volume=25 |issue= 9 |pages= 1089-96 |year= 1997 |pmid= 9311626 |doi= }}
*{{cite journal | author=Yan B, Matoney L, Yang D |title=Human carboxylesterases in term placentae: enzymatic characterization, molecular cloning and evidence for the existence of multiple forms. |journal=Placenta |volume=20 |issue= 7 |pages= 599-607 |year= 1999 |pmid= 10452915 |doi= 10.1053/plac.1999.0407 }}
*{{cite journal | author=Mori M, Hosokawa M, Ogasawara Y, ''et al.'' |title=cDNA cloning, characterization and stable expression of novel human brain carboxylesterase. |journal=FEBS Lett. |volume=458 |issue= 1 |pages= 17-22 |year= 1999 |pmid= 10518925 |doi= }}
*{{cite journal | author=Islam MR, Waheed A, Shah GN, ''et al.'' |title=Human egasyn binds beta-glucuronidase but neither the esterase active site of egasyn nor the C terminus of beta-glucuronidase is involved in their interaction. |journal=Arch. Biochem. Biophys. |volume=372 |issue= 1 |pages= 53-61 |year= 1999 |pmid= 10562416 |doi= 10.1006/abbi.1999.1449 }}
*{{cite journal | author=Ghosh S |title=Cholesteryl ester hydrolase in human monocyte/macrophage: cloning, sequencing, and expression of full-length cDNA. |journal=Physiol. Genomics |volume=2 |issue= 1 |pages= 1-8 |year= 2001 |pmid= 11015575 |doi= }}
*{{cite journal | author=Ghosh S, Natarajan R |title=Cloning of the human cholesteryl ester hydrolase promoter: identification of functional peroxisomal proliferator-activated receptor responsive elements. |journal=Biochem. Biophys. Res. Commun. |volume=284 |issue= 4 |pages= 1065-70 |year= 2001 |pmid= 11409902 |doi= 10.1006/bbrc.2001.5078 }}
*{{cite journal | author=Alam M, Ho S, Vance DE, Lehner R |title=Heterologous expression, purification, and characterization of human triacylglycerol hydrolase. |journal=Protein Expr. Purif. |volume=24 |issue= 1 |pages= 33-42 |year= 2002 |pmid= 11812220 |doi= 10.1006/prep.2001.1553 }}
*{{cite journal | author=Satoh T, Taylor P, Bosron WF, ''et al.'' |title=Current progress on esterases: from molecular structure to function. |journal=Drug Metab. Dispos. |volume=30 |issue= 5 |pages= 488-93 |year= 2002 |pmid= 11950776 |doi= }}
*{{cite journal | author=Alam M, Vance DE, Lehner R |title=Structure-function analysis of human triacylglycerol hydrolase by site-directed mutagenesis: identification of the catalytic triad and a glycosylation site. |journal=Biochemistry |volume=41 |issue= 21 |pages= 6679-87 |year= 2002 |pmid= 12022871 |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=Bencharit S, Morton CL, Xue Y, ''et al.'' |title=Structural basis of heroin and cocaine metabolism by a promiscuous human drug-processing enzyme. |journal=Nat. Struct. Biol. |volume=10 |issue= 5 |pages= 349-56 |year= 2003 |pmid= 12679808 |doi= 10.1038/nsb919 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CHGB... {November 19, 2007 12:15:35 PM PST}
- SEARCH REDIRECT: Control Box Found: CHGB {November 19, 2007 12:15:58 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:16:00 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:16:00 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:16:00 PM PST}
- UPDATED: Updated protein page: CHGB {November 19, 2007 12:16:06 PM PST}
- INFO: Beginning work on CHRNE... {November 19, 2007 12:16:06 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:16:43 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
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| 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 = Cholinergic receptor, nicotinic, epsilon
| HGNCid = 1966
| Symbol = CHRNE
| AltSymbols =; CMS2A; FCCMS; SCCMS; CMS1D; ACHRE; CMS1E
| OMIM = 100725
| ECnumber =
| Homologene = 60
| MGIid = 87894
| GeneAtlas_image1 = PBB_GE_CHRNE_207274_at_tn.png
| Function = {{GNF_GO|id=GO:0004889 |text = nicotinic acetylcholine-activated cation-selective channel activity}} {{GNF_GO|id=GO:0005216 |text = ion channel activity}} {{GNF_GO|id=GO:0005230 |text = extracellular ligand-gated ion channel activity}} {{GNF_GO|id=GO:0008324 |text = cation transmembrane transporter activity}} {{GNF_GO|id=GO:0015464 |text = acetylcholine receptor activity}}
| Component = {{GNF_GO|id=GO:0005892 |text = nicotinic acetylcholine-gated receptor-channel complex}} {{GNF_GO|id=GO:0045211 |text = postsynaptic membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006936 |text = muscle contraction}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007271 |text = synaptic transmission, cholinergic}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1145
| Hs_Ensembl = ENSG00000108556
| Hs_RefseqProtein = NP_000071
| Hs_RefseqmRNA = NM_000080
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 4741840
| Hs_GenLoc_end = 4747148
| Hs_Uniprot = Q04844
| Mm_EntrezGene = 11448
| Mm_Ensembl = ENSMUSG00000014609
| Mm_RefseqmRNA = NM_009603
| Mm_RefseqProtein = NP_033733
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 70431078
| Mm_GenLoc_end = 70435389
| Mm_Uniprot = Q8K1N0
}}
}}
'''Cholinergic receptor, nicotinic, epsilon''', also known as '''CHRNE''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CHRNE cholinergic receptor, nicotinic, epsilon| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1145| 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 = Acetylcholine receptors at mature mammalian neuromuscular junctions are pentameric protein complexes composed of four subunits in the ratio of two alpha subunits to one beta, one epsilon, and one delta subunit. The achetylcholine receptor changes subunit composition shortly after birth when the epsilon subunit replaces the gamma subunit seen in embryonic receptors. Mutations in the epsilon subunit are associated with congenital myasthenic syndrome.<ref name="entrez">{{cite web | title = Entrez Gene: CHRNE cholinergic receptor, nicotinic, epsilon| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1145| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hantaï D, Richard P, Koenig J, Eymard B |title=Congenital myasthenic syndromes. |journal=Curr. Opin. Neurol. |volume=17 |issue= 5 |pages= 539-51 |year= 2005 |pmid= 15367858 |doi= }}
*{{cite journal | author=Yu XM, Hall ZW |title=Extracellular domains mediating epsilon subunit interactions of muscle acetylcholine receptor. |journal=Nature |volume=352 |issue= 6330 |pages= 64-7 |year= 1991 |pmid= 1712080 |doi= 10.1038/352064a0 }}
*{{cite journal | author=Ohno K, Hutchinson DO, Milone M, ''et al.'' |title=Congenital myasthenic syndrome caused by prolonged acetylcholine receptor channel openings due to a mutation in the M2 domain of the epsilon subunit. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 3 |pages= 758-62 |year= 1995 |pmid= 7531341 |doi= }}
*{{cite journal | author=Gomez CM, Gammack JT |title=A leucine-to-phenylalanine substitution in the acetylcholine receptor ion channel in a family with the slow-channel syndrome. |journal=Neurology |volume=45 |issue= 5 |pages= 982-5 |year= 1995 |pmid= 7538206 |doi= }}
*{{cite journal | author=Beeson D, Brydson M, Betty M, ''et al.'' |title=Primary structure of the human muscle acetylcholine receptor. cDNA cloning of the gamma and epsilon subunits. |journal=Eur. J. Biochem. |volume=215 |issue= 2 |pages= 229-38 |year= 1993 |pmid= 7688301 |doi= }}
*{{cite journal | author=Lobos EA |title=Five subunit genes of the human muscle nicotinic acetylcholine receptor are mapped to two linkage groups on chromosomes 2 and 17. |journal=Genomics |volume=17 |issue= 3 |pages= 642-50 |year= 1993 |pmid= 7902325 |doi= 10.1006/geno.1993.1384 }}
*{{cite journal | author=Brenner HR, Rotzler S, Kues WA, ''et al.'' |title=Nerve-dependent induction of AChR epsilon-subunit gene expression in muscle is independent of state of differentiation. |journal=Dev. Biol. |volume=165 |issue= 2 |pages= 527-36 |year= 1994 |pmid= 7958418 |doi= }}
*{{cite journal | author=Uchitel O, Engel AG, Walls TJ, ''et al.'' |title=Congenital myasthenic syndromes: II. Syndrome attributed to abnormal interaction of acetylcholine with its receptor. |journal=Muscle Nerve |volume=16 |issue= 12 |pages= 1293-301 |year= 1993 |pmid= 8232384 |doi= 10.1002/mus.880161205 }}
*{{cite journal | author=Ohno K, Wang HL, Milone M, ''et al.'' |title=Congenital myasthenic syndrome caused by decreased agonist binding affinity due to a mutation in the acetylcholine receptor epsilon subunit. |journal=Neuron |volume=17 |issue= 1 |pages= 157-70 |year= 1996 |pmid= 8755487 |doi= }}
*{{cite journal | author=Engel AG, Ohno K, Milone M, ''et al.'' |title=New mutations in acetylcholine receptor subunit genes reveal heterogeneity in the slow-channel congenital myasthenic syndrome. |journal=Hum. Mol. Genet. |volume=5 |issue= 9 |pages= 1217-27 |year= 1997 |pmid= 8872460 |doi= }}
*{{cite journal | author=Engel AG, Ohno K, Bouzat C, ''et al.'' |title=End-plate acetylcholine receptor deficiency due to nonsense mutations in the epsilon subunit. |journal=Ann. Neurol. |volume=40 |issue= 5 |pages= 810-7 |year= 1997 |pmid= 8957026 |doi= 10.1002/ana.410400521 }}
*{{cite journal | author=Ohno K, Quiram PA, Milone M, ''et al.'' |title=Congenital myasthenic syndromes due to heteroallelic nonsense/missense mutations in the acetylcholine receptor epsilon subunit gene: identification and functional characterization of six new mutations. |journal=Hum. Mol. Genet. |volume=6 |issue= 5 |pages= 753-66 |year= 1997 |pmid= 9158150 |doi= }}
*{{cite journal | author=Nichols P, Croxen R, Vincent A, ''et al.'' |title=Mutation of the acetylcholine receptor epsilon-subunit promoter in congenital myasthenic syndrome. |journal=Ann. Neurol. |volume=45 |issue= 4 |pages= 439-43 |year= 1999 |pmid= 10211467 |doi= }}
*{{cite journal | author=Croxen R, Newland C, Betty M, ''et al.'' |title=Novel functional epsilon-subunit polypeptide generated by a single nucleotide deletion in acetylcholine receptor deficiency congenital myasthenic syndrome. |journal=Ann. Neurol. |volume=46 |issue= 4 |pages= 639-47 |year= 1999 |pmid= 10514102 |doi= }}
*{{cite journal | author=Abicht A, Stucka R, Karcagi V, ''et al.'' |title=A common mutation (epsilon1267delG) in congenital myasthenic patients of Gypsy ethnic origin. |journal=Neurology |volume=53 |issue= 7 |pages= 1564-9 |year= 1999 |pmid= 10534268 |doi= }}
*{{cite journal | author=Kindler CH, Verotta D, Gray AT, ''et al.'' |title=Additive inhibition of nicotinic acetylcholine receptors by corticosteroids and the neuromuscular blocking drug vecuronium. |journal=Anesthesiology |volume=92 |issue= 3 |pages= 821-32 |year= 2000 |pmid= 10719961 |doi= }}
*{{cite journal | author=Wang HL, Ohno K, Milone M, ''et al.'' |title=Fundamental gating mechanism of nicotinic receptor channel revealed by mutation causing a congenital myasthenic syndrome. |journal=J. Gen. Physiol. |volume=116 |issue= 3 |pages= 449-62 |year= 2000 |pmid= 10962020 |doi= }}
*{{cite journal | author=Sieb JP, Kraner S, Rauch M, Steinlein OK |title=Immature end-plates and utrophin deficiency in congenital myasthenic syndrome caused by epsilon-AChR subunit truncating mutations. |journal=Hum. Genet. |volume=107 |issue= 2 |pages= 160-4 |year= 2000 |pmid= 11030414 |doi= }}
*{{cite journal | author=Dan I, Watanabe NM, Kajikawa E, ''et al.'' |title=Overlapping of MINK and CHRNE gene loci in the course of mammalian evolution. |journal=Nucleic Acids Res. |volume=30 |issue= 13 |pages= 2906-10 |year= 2002 |pmid= 12087176 |doi= }}
*{{cite journal | author=Croxen R, Hatton C, Shelley C, ''et al.'' |title=Recessive inheritance and variable penetrance of slow-channel congenital myasthenic syndromes. |journal=Neurology |volume=59 |issue= 2 |pages= 162-8 |year= 2002 |pmid= 12141316 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DNAJA3... {November 19, 2007 12:31:55 PM PST}
- SEARCH REDIRECT: Control Box Found: DNAJA3 {November 19, 2007 12:33:11 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:33:12 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:33:12 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:33:12 PM PST}
- UPDATED: Updated protein page: DNAJA3 {November 19, 2007 12:33:18 PM PST}
- INFO: Beginning work on ENTPD1... {November 19, 2007 12:13:46 PM PST}
- SEARCH REDIRECT: Control Box Found: ENTPD1 {November 19, 2007 12:14:18 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:14:21 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:14:21 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:14:21 PM PST}
- UPDATED: Updated protein page: ENTPD1 {November 19, 2007 12:14:27 PM PST}
- INFO: Beginning work on GDF5... {November 19, 2007 12:26:57 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:27:32 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_GDF5_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1waq.
| PDB = {{PDB2|1waq}}, {{PDB2|2bhk}}
| Name = Growth differentiation factor 5 (cartilage-derived morphogenetic protein-1)
| HGNCid = 4220
| Symbol = GDF5
| AltSymbols =; CDMP1; LAP4; SYNS2
| OMIM = 601146
| ECnumber =
| Homologene = 468
| MGIid = 95688
| GeneAtlas_image1 = PBB_GE_GDF5_206614_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0007179 |text = transforming growth factor beta receptor signaling pathway}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0030326 |text = embryonic limb morphogenesis}} {{GNF_GO|id=GO:0040007 |text = growth}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8200
| Hs_Ensembl = ENSG00000125965
| Hs_RefseqProtein = NP_000548
| Hs_RefseqmRNA = NM_000557
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 33484559
| Hs_GenLoc_end = 33505982
| Hs_Uniprot = P43026
| Mm_EntrezGene = 14563
| Mm_Ensembl = ENSMUSG00000038259
| Mm_RefseqmRNA = NM_008109
| Mm_RefseqProtein = NP_032135
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 155632468
| Mm_GenLoc_end = 155636808
| Mm_Uniprot = Q8BRW9
}}
}}
'''Growth differentiation factor 5 (cartilage-derived morphogenetic protein-1)''', also known as '''GDF5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GDF5 growth differentiation factor 5 (cartilage-derived morphogenetic protein-1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8200| 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 bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. Mutations in this gene are associated with acromesomelic dysplasia, Hunter-Thompson type; brachydactyly, type C; and chondrodysplasia, Grebe type. These associations confirm that the gene product plays a role in skeletal development.<ref name="entrez">{{cite web | title = Entrez Gene: GDF5 growth differentiation factor 5 (cartilage-derived morphogenetic protein-1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8200| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Reddi AH |title=Cartilage morphogenesis: role of bone and cartilage morphogenetic proteins, homeobox genes and extracellular matrix. |journal=Matrix Biol. |volume=14 |issue= 8 |pages= 599-606 |year= 1997 |pmid= 9057810 |doi= }}
*{{cite journal | author=Luyten FP |title=Cartilage-derived morphogenetic protein-1. |journal=Int. J. Biochem. Cell Biol. |volume=29 |issue= 11 |pages= 1241-4 |year= 1998 |pmid= 9451821 |doi= }}
*{{cite journal | author=Ducy P, Karsenty G |title=The family of bone morphogenetic proteins. |journal=Kidney Int. |volume=57 |issue= 6 |pages= 2207-14 |year= 2000 |pmid= 10844590 |doi= 10.1046/j.1523-1755.2000.00081.x }}
*{{cite journal | author=Faiyaz-Ul-Haque M, Ahmad W, Wahab A, ''et al.'' |title=Frameshift mutation in the cartilage-derived morphogenetic protein 1 (CDMP1) gene and severe acromesomelic chondrodysplasia resembling Grebe-type chondrodysplasia. |journal=Am. J. Med. Genet. |volume=111 |issue= 1 |pages= 31-7 |year= 2003 |pmid= 12124730 |doi= 10.1002/ajmg.10501 }}
*{{cite journal | author=Chang SC, Hoang B, Thomas JT, ''et al.'' |title=Cartilage-derived morphogenetic proteins. New members of the transforming growth factor-beta superfamily predominantly expressed in long bones during human embryonic development. |journal=J. Biol. Chem. |volume=269 |issue= 45 |pages= 28227-34 |year= 1994 |pmid= 7961761 |doi= }}
*{{cite journal | author=Hötten G, Neidhardt H, Jacobowsky B, Pohl J |title=Cloning and expression of recombinant human growth/differentiation factor 5. |journal=Biochem. Biophys. Res. Commun. |volume=204 |issue= 2 |pages= 646-52 |year= 1994 |pmid= 7980526 |doi= 10.1006/bbrc.1994.2508 }}
*{{cite journal | author=Thomas JT, Lin K, Nandedkar M, ''et al.'' |title=A human chondrodysplasia due to a mutation in a TGF-beta superfamily member. |journal=Nat. Genet. |volume=12 |issue= 3 |pages= 315-7 |year= 1996 |pmid= 8589725 |doi= 10.1038/ng0396-315 }}
*{{cite journal | author=Lin K, Thomas JT, McBride OW, Luyten FP |title=Assignment of a new TGF-beta superfamily member, human cartilage-derived morphogenetic protein-1, to chromosome 20q11.2. |journal=Genomics |volume=34 |issue= 1 |pages= 150-1 |year= 1996 |pmid= 8661040 |doi= 10.1006/geno.1996.0257 }}
*{{cite journal | author=Nishitoh H, Ichijo H, Kimura M, ''et al.'' |title=Identification of type I and type II serine/threonine kinase receptors for growth/differentiation factor-5. |journal=J. Biol. Chem. |volume=271 |issue= 35 |pages= 21345-52 |year= 1996 |pmid= 8702914 |doi= }}
*{{cite journal | author=Polinkovsky A, Robin NH, Thomas JT, ''et al.'' |title=Mutations in CDMP1 cause autosomal dominant brachydactyly type C. |journal=Nat. Genet. |volume=17 |issue= 1 |pages= 18-9 |year= 1997 |pmid= 9288091 |doi= 10.1038/ng0997-18 }}
*{{cite journal | author=Thomas JT, Kilpatrick MW, Lin K, ''et al.'' |title=Disruption of human limb morphogenesis by a dominant negative mutation in CDMP1. |journal=Nat. Genet. |volume=17 |issue= 1 |pages= 58-64 |year= 1997 |pmid= 9288098 |doi= 10.1038/ng0997-58 }}
*{{cite journal | author=Erlacher L, McCartney J, Piek E, ''et al.'' |title=Cartilage-derived morphogenetic proteins and osteogenic protein-1 differentially regulate osteogenesis. |journal=J. Bone Miner. Res. |volume=13 |issue= 3 |pages= 383-92 |year= 1998 |pmid= 9525338 |doi= }}
*{{cite journal | author=Sugiura T, Hötten G, Kawai S |title=Minimal promoter components of the human growth/differentiation factor-5 gene. |journal=Biochem. Biophys. Res. Commun. |volume=263 |issue= 3 |pages= 707-13 |year= 1999 |pmid= 10512744 |doi= 10.1006/bbrc.1999.1445 }}
*{{cite journal | author=Aoki H, Fujii M, Imamura T, ''et al.'' |title=Synergistic effects of different bone morphogenetic protein type I receptors on alkaline phosphatase induction. |journal=J. Cell. Sci. |volume=114 |issue= Pt 8 |pages= 1483-9 |year= 2001 |pmid= 11282024 |doi= }}
*{{cite journal | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
*{{cite journal | author=Faiyaz-Ul-Haque M, Ahmad W, Zaidi SH, ''et al.'' |title=Mutation in the cartilage-derived morphogenetic protein-1 (CDMP1) gene in a kindred affected with fibular hypoplasia and complex brachydactyly (DuPan syndrome). |journal=Clin. Genet. |volume=61 |issue= 6 |pages= 454-8 |year= 2003 |pmid= 12121354 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IER3... {November 19, 2007 12:31:09 PM PST}
- SEARCH REDIRECT: Control Box Found: IER3 {November 19, 2007 12:31:46 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:31:49 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:31:49 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:31:49 PM PST}
- UPDATED: Updated protein page: IER3 {November 19, 2007 12:31:55 PM PST}
- INFO: Beginning work on IL1RL1... {November 19, 2007 12:33:18 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:34:08 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| 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 = Interleukin 1 receptor-like 1
| HGNCid = 5998
| Symbol = IL1RL1
| AltSymbols =; T1; ST2; DER4; FIT-1; MGC32623; ST2L; ST2V
| OMIM = 601203
| ECnumber =
| Homologene = 2862
| MGIid = 98427
| GeneAtlas_image1 = PBB_GE_IL1RL1_207526_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004888 |text = transmembrane receptor activity}} {{GNF_GO|id=GO:0004908 |text = interleukin-1 receptor activity}} {{GNF_GO|id=GO:0005057 |text = receptor signaling protein activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 9173
| Hs_Ensembl = ENSG00000115602
| Hs_RefseqProtein = NP_003847
| Hs_RefseqmRNA = NM_003856
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 102294394
| Hs_GenLoc_end = 102334929
| Hs_Uniprot = Q01638
| Mm_EntrezGene = 17082
| Mm_Ensembl = ENSMUSG00000026069
| Mm_RefseqmRNA = NM_001025602
| Mm_RefseqProtein = NP_001020773
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 40374143
| Mm_GenLoc_end = 40409958
| Mm_Uniprot = Q3UM53
}}
}}
'''Interleukin 1 receptor-like 1''', also known as '''IL1RL1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IL1RL1 interleukin 1 receptor-like 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9173| 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 interleukin 1 receptor family. Studies of the similar gene in mouse suggested that this receptor can be induced by proinflammatory stimuli, and may be involved in the function of helper T cells. This gene, interleukin 1 receptor, type I (IL1R1), interleukin 1 receptor, type II (IL1R2) and interleukin 1 receptor-like 2 (IL1RL2) form a cytokine receptor gene cluster in a region mapped to chromosome 2q12. Alternative splicing of this gene results in multiple transcript variants.<ref name="entrez">{{cite web | title = Entrez Gene: IL1RL1 interleukin 1 receptor-like 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9173| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tominaga S, Yokota T, Yanagisawa K, ''et al.'' |title=Nucleotide sequence of a complementary DNA for human ST2. |journal=Biochim. Biophys. Acta |volume=1171 |issue= 2 |pages= 215-8 |year= 1993 |pmid= 1482686 |doi= }}
*{{cite journal | author=Gayle MA, Slack JL, Bonnert TP, ''et al.'' |title=Cloning of a putative ligand for the T1/ST2 receptor. |journal=J. Biol. Chem. |volume=271 |issue= 10 |pages= 5784-9 |year= 1996 |pmid= 8621446 |doi= }}
*{{cite journal | author=Yanagisawa K, Naito Y, Kuroiwa K, ''et al.'' |title=The expression of ST2 gene in helper T cells and the binding of ST2 protein to myeloma-derived RPMI8226 cells. |journal=J. Biochem. |volume=121 |issue= 1 |pages= 95-103 |year= 1997 |pmid= 9058198 |doi= }}
*{{cite journal | author=Kumar S, Tzimas MN, Griswold DE, Young PR |title=Expression of ST2, an interleukin-1 receptor homologue, is induced by proinflammatory stimuli. |journal=Biochem. Biophys. Res. Commun. |volume=235 |issue= 3 |pages= 474-8 |year= 1997 |pmid= 9207179 |doi= 10.1006/bbrc.1997.6810 }}
*{{cite journal | author=Löhning M, Stroehmann A, Coyle AJ, ''et al.'' |title=T1/ST2 is preferentially expressed on murine Th2 cells, independent of interleukin 4, interleukin 5, and interleukin 10, and important for Th2 effector function. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 12 |pages= 6930-5 |year= 1998 |pmid= 9618516 |doi= }}
*{{cite journal | author=Moritz DR, Rodewald HR, Gheyselinck J, Klemenz R |title=The IL-1 receptor-related T1 antigen is expressed on immature and mature mast cells and on fetal blood mast cell progenitors. |journal=J. Immunol. |volume=161 |issue= 9 |pages= 4866-74 |year= 1998 |pmid= 9794420 |doi= }}
*{{cite journal | author=Saccani S, Polentarutti N, Penton-Rol G, ''et al.'' |title=Divergent effects of LPS on expression of IL-1 receptor family members in mononuclear phagocytes in vitro and in vivo. |journal=Cytokine |volume=10 |issue= 10 |pages= 773-80 |year= 1999 |pmid= 9811530 |doi= 10.1006/cyto.1998.0359 }}
*{{cite journal | author=Dale M, Nicklin MJ |title=Interleukin-1 receptor cluster: gene organization of IL1R2, IL1R1, IL1RL2 (IL-1Rrp2), IL1RL1 (T1/ST2), and IL18R1 (IL-1Rrp) on human chromosome 2q. |journal=Genomics |volume=57 |issue= 1 |pages= 177-9 |year= 1999 |pmid= 10191101 |doi= 10.1006/geno.1999.5767 }}
*{{cite journal | author=Iwahana H, Yanagisawa K, Ito-Kosaka A, ''et al.'' |title=Different promoter usage and multiple transcription initiation sites of the interleukin-1 receptor-related human ST2 gene in UT-7 and TM12 cells. |journal=Eur. J. Biochem. |volume=264 |issue= 2 |pages= 397-406 |year= 1999 |pmid= 10491084 |doi= }}
*{{cite journal | author=Tominaga S, Kuroiwa K, Tago K, ''et al.'' |title=Presence and expression of a novel variant form of ST2 gene product in human leukemic cell line UT-7/GM. |journal=Biochem. Biophys. Res. Commun. |volume=264 |issue= 1 |pages= 14-8 |year= 1999 |pmid= 10527832 |doi= 10.1006/bbrc.1999.1469 }}
*{{cite journal | author=Li H, Tago K, Io K, ''et al.'' |title=The cloning and nucleotide sequence of human ST2L cDNA. |journal=Genomics |volume=67 |issue= 3 |pages= 284-90 |year= 2000 |pmid= 10936050 |doi= 10.1006/geno.2000.6269 }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
*{{cite journal | author=Sweet MJ, Leung BP, Kang D, ''et al.'' |title=A novel pathway regulating lipopolysaccharide-induced shock by ST2/T1 via inhibition of Toll-like receptor 4 expression. |journal=J. Immunol. |volume=166 |issue= 11 |pages= 6633-9 |year= 2001 |pmid= 11359817 |doi= }}
*{{cite journal | author=Tago K, Noda T, Hayakawa M, ''et al.'' |title=Tissue distribution and subcellular localization of a variant form of the human ST2 gene product, ST2V. |journal=Biochem. Biophys. Res. Commun. |volume=285 |issue= 5 |pages= 1377-83 |year= 2001 |pmid= 11478810 |doi= 10.1006/bbrc.2001.5306 }}
*{{cite journal | author=Lécart S, Lecointe N, Subramaniam A, ''et al.'' |title=Activated, but not resting human Th2 cells, in contrast to Th1 and T regulatory cells, produce soluble ST2 and express low levels of ST2L at the cell surface. |journal=Eur. J. Immunol. |volume=32 |issue= 10 |pages= 2979-87 |year= 2002 |pmid= 12355452 |doi= 10.1002/1521-4141(2002010)32:10<2979::AID-IMMU2979>3.0.CO;2-5 }}
*{{cite journal | author=Brint EK, Fitzgerald KA, Smith P, ''et al.'' |title=Characterization of signaling pathways activated by the interleukin 1 (IL-1) receptor homologue T1/ST2. A role for Jun N-terminal kinase in IL-4 induction. |journal=J. Biol. Chem. |volume=277 |issue= 51 |pages= 49205-11 |year= 2003 |pmid= 12368275 |doi= 10.1074/jbc.M209685200 }}
*{{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=Haga Y, Yanagisawa K, Ohto-Ozaki H, ''et al.'' |title=The effect of ST2 gene product on anchorage-independent growth of a glioblastoma cell line, T98G. |journal=Eur. J. Biochem. |volume=270 |issue= 1 |pages= 163-70 |year= 2003 |pmid= 12492487 |doi= }}
*{{cite journal | author=Weinberg EO, Shimpo M, Hurwitz S, ''et al.'' |title=Identification of serum soluble ST2 receptor as a novel heart failure biomarker. |journal=Circulation |volume=107 |issue= 5 |pages= 721-6 |year= 2003 |pmid= 12578875 |doi= }}
*{{cite journal | author=Gevaert K, Goethals M, Martens L, ''et al.'' |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566-9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LRP8... {November 19, 2007 12:26:25 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:26:57 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| 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 = Low density lipoprotein receptor-related protein 8, apolipoprotein e receptor
| HGNCid = 6700
| Symbol = LRP8
| AltSymbols =; APOER2; HSZ75190
| OMIM = 602600
| ECnumber =
| Homologene = 31250
| MGIid = 1340044
| GeneAtlas_image1 = PBB_GE_LRP8_205282_at_tn.png
| GeneAtlas_image2 = PBB_GE_LRP8_208433_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004888 |text = transmembrane receptor activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0008034 |text = lipoprotein binding}} {{GNF_GO|id=GO:0030227 |text = apolipoprotein E receptor activity}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006897 |text = endocytosis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0019221 |text = cytokine and chemokine mediated signaling pathway}} {{GNF_GO|id=GO:0045860 |text = positive regulation of protein kinase activity}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7804
| Hs_Ensembl = ENSG00000157193
| Hs_RefseqProtein = NP_001018064
| Hs_RefseqmRNA = NM_001018054
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 53483800
| Hs_GenLoc_end = 53566409
| Hs_Uniprot = Q14114
| Mm_EntrezGene = 16975
| Mm_Ensembl = ENSMUSG00000028613
| Mm_RefseqmRNA = NM_001080926
| Mm_RefseqProtein = NP_001074395
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 107300193
| Mm_GenLoc_end = 107372099
| Mm_Uniprot = Q924X6
}}
}}
'''Low density lipoprotein receptor-related protein 8, apolipoprotein e receptor''', also known as '''LRP8''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LRP8 low density lipoprotein receptor-related protein 8, apolipoprotein e receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7804| 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 apolipoprotein E receptor, a member of the low density lipoprotein receptor (LDLR) family. Apolipoprotein E is a small lipophilic plasma protein and a component of lipoproteins such as chylomicron remnants, very low density lipoprotein (VLDL), and high density lipoprotein (HDL). The apolipoprotein E receptor is involved in cellular recognition and internalization of these lipoproteins. Alternative splicing generates multiple transcript variants encoding distinct isoforms for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: LRP8 low density lipoprotein receptor-related protein 8, apolipoprotein e receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7804| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kim DH, Iijima H, Goto K, ''et al.'' |title=Human apolipoprotein E receptor 2. A novel lipoprotein receptor of the low density lipoprotein receptor family predominantly expressed in brain. |journal=J. Biol. Chem. |volume=271 |issue= 14 |pages= 8373-80 |year= 1996 |pmid= 8626535 |doi= }}
*{{cite journal | author=Kim DH, Magoori K, Inoue TR, ''et al.'' |title=Exon/intron organization, chromosome localization, alternative splicing, and transcription units of the human apolipoprotein E receptor 2 gene. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8498-504 |year= 1997 |pmid= 9079678 |doi= }}
*{{cite journal | author=Clatworthy AE, Stockinger W, Christie RH, ''et al.'' |title=Expression and alternate splicing of apolipoprotein E receptor 2 in brain. |journal=Neuroscience |volume=90 |issue= 3 |pages= 903-11 |year= 1999 |pmid= 10218790 |doi= }}
*{{cite journal | author=Sun XM, Soutar AK |title=Expression in vitro of alternatively spliced variants of the messenger RNA for human apolipoprotein E receptor-2 identified in human tissues by ribonuclease protection assays. |journal=Eur. J. Biochem. |volume=262 |issue= 1 |pages= 230-9 |year= 1999 |pmid= 10231386 |doi= }}
*{{cite journal | author=Trommsdorff M, Gotthardt M, Hiesberger T, ''et al.'' |title=Reeler/Disabled-like disruption of neuronal migration in knockout mice lacking the VLDL receptor and ApoE receptor 2. |journal=Cell |volume=97 |issue= 6 |pages= 689-701 |year= 1999 |pmid= 10380922 |doi= }}
*{{cite journal | author=Riddell DR, Vinogradov DV, Stannard AK, ''et al.'' |title=Identification and characterization of LRP8 (apoER2) in human blood platelets. |journal=J. Lipid Res. |volume=40 |issue= 10 |pages= 1925-30 |year= 1999 |pmid= 10508213 |doi= }}
*{{cite journal | author=D'Arcangelo G, Homayouni R, Keshvara L, ''et al.'' |title=Reelin is a ligand for lipoprotein receptors. |journal=Neuron |volume=24 |issue= 2 |pages= 471-9 |year= 1999 |pmid= 10571240 |doi= }}
*{{cite journal | author=Korschineck I, Ziegler S, Breuss J, ''et al.'' |title=Identification of a novel exon in apolipoprotein E receptor 2 leading to alternatively spliced mRNAs found in cells of the vascular wall but not in neuronal tissue. |journal=J. Biol. Chem. |volume=276 |issue= 16 |pages= 13192-7 |year= 2001 |pmid= 11152697 |doi= 10.1074/jbc.M011795200 }}
*{{cite journal | author=Riddell DR, Sun XM, Stannard AK, ''et al.'' |title=Localization of apolipoprotein E receptor 2 to caveolae in the plasma membrane. |journal=J. Lipid Res. |volume=42 |issue= 6 |pages= 998-1002 |year= 2001 |pmid= 11369809 |doi= }}
*{{cite journal | author=Weeber EJ, Beffert U, Jones C, ''et al.'' |title=Reelin and ApoE receptors cooperate to enhance hippocampal synaptic plasticity and learning. |journal=J. Biol. Chem. |volume=277 |issue= 42 |pages= 39944-52 |year= 2002 |pmid= 12167620 |doi= 10.1074/jbc.M205147200 }}
*{{cite journal | author=Stockinger W, Sailler B, Strasser V, ''et al.'' |title=The PX-domain protein SNX17 interacts with members of the LDL receptor family and modulates endocytosis of the LDL receptor. |journal=EMBO J. |volume=21 |issue= 16 |pages= 4259-67 |year= 2002 |pmid= 12169628 |doi= }}
*{{cite journal | author=Ma SL, Ng HK, Baum L, ''et al.'' |title=Low-density lipoprotein receptor-related protein 8 (apolipoprotein E receptor 2) gene polymorphisms in Alzheimer's disease. |journal=Neurosci. Lett. |volume=332 |issue= 3 |pages= 216-8 |year= 2003 |pmid= 12399018 |doi= }}
*{{cite journal | author=Koch S, Strasser V, Hauser C, ''et al.'' |title=A secreted soluble form of ApoE receptor 2 acts as a dominant-negative receptor and inhibits Reelin signaling. |journal=EMBO J. |volume=21 |issue= 22 |pages= 5996-6004 |year= 2003 |pmid= 12426372 |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=Sun XM, Soutar AK |title=The transmembrane domain and PXXP motifs of ApoE receptor 2 exclude it from carrying out clathrin-mediated endocytosis. |journal=J. Biol. Chem. |volume=278 |issue= 22 |pages= 19926-32 |year= 2003 |pmid= 12621059 |doi= 10.1074/jbc.M302047200 }}
*{{cite journal | author=Benhayon D, Magdaleno S, Curran T |title=Binding of purified Reelin to ApoER2 and VLDLR mediates tyrosine phosphorylation of Disabled-1. |journal=Brain Res. Mol. Brain Res. |volume=112 |issue= 1-2 |pages= 33-45 |year= 2003 |pmid= 12670700 |doi= }}
*{{cite journal | author=Sacre SM, Stannard AK, Owen JS |title=Apolipoprotein E (apoE) isoforms differentially induce nitric oxide production in endothelial cells. |journal=FEBS Lett. |volume=540 |issue= 1-3 |pages= 181-7 |year= 2003 |pmid= 12681505 |doi= }}
*{{cite journal | author=Lutters BC, Derksen RH, Tekelenburg WL, ''et al.'' |title=Dimers of beta 2-glycoprotein I increase platelet deposition to collagen via interaction with phospholipids and the apolipoprotein E receptor 2'. |journal=J. Biol. Chem. |volume=278 |issue= 36 |pages= 33831-8 |year= 2003 |pmid= 12807892 |doi= 10.1074/jbc.M212655200 }}
*{{cite journal | author=Bajari TM, Strasser V, Nimpf J, Schneider WJ |title=A model for modulation of leptin activity by association with clusterin. |journal=FASEB J. |volume=17 |issue= 11 |pages= 1505-7 |year= 2003 |pmid= 12824284 |doi= 10.1096/fj.02-1106fje }}
*{{cite journal | author=May P, Bock HH, Nimpf J, Herz J |title=Differential glycosylation regulates processing of lipoprotein receptors by gamma-secretase. |journal=J. Biol. Chem. |volume=278 |issue= 39 |pages= 37386-92 |year= 2003 |pmid= 12871934 |doi= 10.1074/jbc.M305858200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NMT2... {November 19, 2007 12:34:08 PM PST}
- SEARCH REDIRECT: Control Box Found: NMT2 {November 19, 2007 12:34:29 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:34:32 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:34:32 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:34:32 PM PST}
- UPDATED: Updated protein page: NMT2 {November 19, 2007 12:34:39 PM PST}
- INFO: Beginning work on NRP2... {November 19, 2007 12:30:16 PM PST}
- SEARCH REDIRECT: Control Box Found: NRP2 {November 19, 2007 12:31:01 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:31:04 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:31:04 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:31:04 PM PST}
- UPDATED: Updated protein page: NRP2 {November 19, 2007 12:31:09 PM PST}
- INFO: Beginning work on NUMB... {November 19, 2007 12:28:57 PM PST}
- SEARCH REDIRECT: Control Box Found: NUMB {November 19, 2007 12:29:27 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:29:28 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:29:28 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:29:28 PM PST}
- UPDATED: Updated protein page: NUMB {November 19, 2007 12:29:34 PM PST}
- INFO: Beginning work on PDCD6... {November 19, 2007 12:40:27 PM PST}
- SEARCH REDIRECT: Control Box Found: PDCD6 {November 19, 2007 12:48:10 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:48:12 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:48:12 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:48:12 PM PST}
- UPDATED: Updated protein page: PDCD6 {November 19, 2007 12:48:18 PM PST}
- INFO: Beginning work on SMARCA5... {November 19, 2007 12:28:19 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:28:57 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5
| HGNCid = 11101
| Symbol = SMARCA5
| AltSymbols =; ISWI; SNF2H; WCRF135; hISWI; hSNF2H
| OMIM = 603375
| ECnumber =
| Homologene = 55764
| MGIid = 1935129
| GeneAtlas_image1 = PBB_GE_SMARCA5_213251_at_tn.png
| GeneAtlas_image2 = PBB_GE_SMARCA5_202303_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_SMARCA5_213859_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003702 |text = RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0004386 |text = helicase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016887 |text = ATPase activity}} {{GNF_GO|id=GO:0042393 |text = histone binding}}
| Component = {{GNF_GO|id=GO:0000793 |text = condensed chromosome}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005654 |text = nucleoplasm}} {{GNF_GO|id=GO:0031213 |text = RSF complex}}
| Process = {{GNF_GO|id=GO:0006334 |text = nucleosome assembly}} {{GNF_GO|id=GO:0006338 |text = chromatin remodeling}} {{GNF_GO|id=GO:0006352 |text = transcription initiation}} {{GNF_GO|id=GO:0006357 |text = regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0016584 |text = nucleosome positioning}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8467
| Hs_Ensembl = ENSG00000153147
| Hs_RefseqProtein = NP_003592
| Hs_RefseqmRNA = NM_003601
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 144654066
| Hs_GenLoc_end = 144694016
| Hs_Uniprot = O60264
| Mm_EntrezGene = 93762
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_053124
| Mm_RefseqProtein = NP_444354
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5''', also known as '''SMARCA5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SMARCA5 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8467| 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 SWI/SNF family of proteins. Members of this family have helicase and ATPase activities and are thought to regulate transcription of certain genes by altering the chromatin structure around those genes. The protein encoded by this gene is a component of the chromatin remodeling and spacing factor RSF, a facilitator of the transcription of class II genes by RNA polymerase II. The encoded protein is similar in sequence to the Drosophila ISWI chromatin remodeling protein.<ref name="entrez">{{cite web | title = Entrez Gene: SMARCA5 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8467| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Dirscherl SS, Krebs JE |title=Functional diversity of ISWI complexes. |journal=Biochem. Cell Biol. |volume=82 |issue= 4 |pages= 482-9 |year= 2005 |pmid= 15284901 |doi= 10.1139/o04-044 }}
*{{cite journal | author=Aihara T, Miyoshi Y, Koyama K, ''et al.'' |title=Cloning and mapping of SMARCA5 encoding hSNF2H, a novel human homologue of Drosophila ISWI. |journal=Cytogenet. Cell Genet. |volume=81 |issue= 3-4 |pages= 191-3 |year= 1998 |pmid= 9730600 |doi= }}
*{{cite journal | author=LeRoy G, Orphanides G, Lane WS, Reinberg D |title=Requirement of RSF and FACT for transcription of chromatin templates in vitro. |journal=Science |volume=282 |issue= 5395 |pages= 1900-4 |year= 1998 |pmid= 9836642 |doi= }}
*{{cite journal | author=Bochar DA, Savard J, Wang W, ''et al.'' |title=A family of chromatin remodeling factors related to Williams syndrome transcription factor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 3 |pages= 1038-43 |year= 2000 |pmid= 10655480 |doi= }}
*{{cite journal | author=Poot RA, Dellaire G, Hülsmann BB, ''et al.'' |title=HuCHRAC, a human ISWI chromatin remodelling complex contains hACF1 and two novel histone-fold proteins. |journal=EMBO J. |volume=19 |issue= 13 |pages= 3377-87 |year= 2000 |pmid= 10880450 |doi= 10.1093/emboj/19.13.3377 }}
*{{cite journal | author=Stopka T, Zakova D, Fuchs O, ''et al.'' |title=Chromatin remodeling gene SMARCA5 is dysregulated in primitive hematopoietic cells of acute leukemia. |journal=Leukemia |volume=14 |issue= 7 |pages= 1247-52 |year= 2000 |pmid= 10914549 |doi= }}
*{{cite journal | author=Aalfs JD, Narlikar GJ, Kingston RE |title=Functional differences between the human ATP-dependent nucleosome remodeling proteins BRG1 and SNF2H. |journal=J. Biol. Chem. |volume=276 |issue= 36 |pages= 34270-8 |year= 2001 |pmid= 11435432 |doi= 10.1074/jbc.M104163200 }}
*{{cite journal | author=Strohner R, Nemeth A, Jansa P, ''et al.'' |title=NoRC--a novel member of mammalian ISWI-containing chromatin remodeling machines. |journal=EMBO J. |volume=20 |issue= 17 |pages= 4892-900 |year= 2001 |pmid= 11532953 |doi= 10.1093/emboj/20.17.4892 }}
*{{cite journal | author=Bozhenok L, Wade PA, Varga-Weisz P |title=WSTF-ISWI chromatin remodeling complex targets heterochromatic replication foci. |journal=EMBO J. |volume=21 |issue= 9 |pages= 2231-41 |year= 2002 |pmid= 11980720 |doi= 10.1093/emboj/21.9.2231 }}
*{{cite journal | author=Levine SS, Weiss A, Erdjument-Bromage H, ''et al.'' |title=The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans. |journal=Mol. Cell. Biol. |volume=22 |issue= 17 |pages= 6070-8 |year= 2002 |pmid= 12167701 |doi= }}
*{{cite journal | author=Hakimi MA, Bochar DA, Schmiesing JA, ''et al.'' |title=A chromatin remodelling complex that loads cohesin onto human chromosomes. |journal=Nature |volume=418 |issue= 6901 |pages= 994-8 |year= 2002 |pmid= 12198550 |doi= 10.1038/nature01024 }}
*{{cite journal | author=Yasui D, Miyano M, Cai S, ''et al.'' |title=SATB1 targets chromatin remodelling to regulate genes over long distances. |journal=Nature |volume=419 |issue= 6907 |pages= 641-5 |year= 2002 |pmid= 12374985 |doi= 10.1038/nature01084 }}
*{{cite journal | author=Collins N, Poot RA, Kukimoto I, ''et al.'' |title=An ACF1-ISWI chromatin-remodeling complex is required for DNA replication through heterochromatin. |journal=Nat. Genet. |volume=32 |issue= 4 |pages= 627-32 |year= 2003 |pmid= 12434153 |doi= 10.1038/ng1046 }}
*{{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=Loyola A, Huang JY, LeRoy G, ''et al.'' |title=Functional analysis of the subunits of the chromatin assembly factor RSF. |journal=Mol. Cell. Biol. |volume=23 |issue= 19 |pages= 6759-68 |year= 2003 |pmid= 12972596 |doi= }}
*{{cite journal | author=Shu H, Chen S, Bi Q, ''et al.'' |title=Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line. |journal=Mol. Cell Proteomics |volume=3 |issue= 3 |pages= 279-86 |year= 2004 |pmid= 14729942 |doi= 10.1074/mcp.D300003-MCP200 }}
*{{cite journal | author=Obuse C, Yang H, Nozaki N, ''et al.'' |title=Proteomics analysis of the centromere complex from HeLa interphase cells: UV-damaged DNA binding protein 1 (DDB-1) is a component of the CEN-complex, while BMI-1 is transiently co-localized with the centromeric region in interphase. |journal=Genes Cells |volume=9 |issue= 2 |pages= 105-20 |year= 2004 |pmid= 15009096 |doi= }}
*{{cite journal | author=Geiman TM, Sankpal UT, Robertson AK, ''et al.'' |title=DNMT3B interacts with hSNF2H chromatin remodeling enzyme, HDACs 1 and 2, and components of the histone methylation system. |journal=Biochem. Biophys. Res. Commun. |volume=318 |issue= 2 |pages= 544-55 |year= 2004 |pmid= 15120635 |doi= 10.1016/j.bbrc.2004.04.058 }}
*{{cite journal | author=Geiman TM, Sankpal UT, Robertson AK, ''et al.'' |title=Isolation and characterization of a novel DNA methyltransferase complex linking DNMT3B with components of the mitotic chromosome condensation machinery. |journal=Nucleic Acids Res. |volume=32 |issue= 9 |pages= 2716-29 |year= 2004 |pmid= 15148359 |doi= 10.1093/nar/gkh589 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TNFRSF14... {November 19, 2007 12:29:34 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:30:16 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_TNFRSF14_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1jma.
| PDB = {{PDB2|1jma}}, {{PDB2|2aw2}}
| Name = Tumor necrosis factor receptor superfamily, member 14 (herpesvirus entry mediator)
| HGNCid = 11912
| Symbol = TNFRSF14
| AltSymbols =; TR2; ATAR; HVEA; HVEM; LIGHTR
| OMIM = 602746
| ECnumber =
| Homologene = 2833
| MGIid = 2675303
| GeneAtlas_image1 = PBB_GE_TNFRSF14_209354_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004888 |text = transmembrane receptor activity}} {{GNF_GO|id=GO:0005031 |text = tumor necrosis factor receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0018108 |text = peptidyl-tyrosine phosphorylation}} {{GNF_GO|id=GO:0050798 |text = activated T cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8764
| Hs_Ensembl = ENSG00000157873
| Hs_RefseqProtein = NP_003811
| Hs_RefseqmRNA = NM_003820
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 2479150
| Hs_GenLoc_end = 2486613
| Hs_Uniprot = Q92956
| Mm_EntrezGene = 230979
| Mm_Ensembl = ENSMUSG00000042333
| Mm_RefseqmRNA = NM_178931
| Mm_RefseqProtein = NP_849262
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 153766010
| Mm_GenLoc_end = 153771877
| Mm_Uniprot =
}}
}}
'''Tumor necrosis factor receptor superfamily, member 14 (herpesvirus entry mediator)''', also known as '''TNFRSF14''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TNFRSF14 tumor necrosis factor receptor superfamily, member 14 (herpesvirus entry mediator)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8764| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor was identified as a cellular mediator of herpes simplex virus (HSV) entry. Binding of HSV viral envelope glycoprotein D (gD) to this receptor protein has been shown to be part of the viral entry mechanism. The cytoplasmic region of this receptor was found to bind to several TRAF family members, which may mediate the signal transduction pathways that activate the immune response.<ref name="entrez">{{cite web | title = Entrez Gene: TNFRSF14 tumor necrosis factor receptor superfamily, member 14 (herpesvirus entry mediator)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8764| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Montgomery RI, Warner MS, Lum BJ, Spear PG |title=Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family. |journal=Cell |volume=87 |issue= 3 |pages= 427-36 |year= 1996 |pmid= 8898196 |doi= }}
*{{cite journal | author=Hsu H, Solovyev I, Colombero A, ''et al.'' |title=ATAR, a novel tumor necrosis factor receptor family member, signals through TRAF2 and TRAF5. |journal=J. Biol. Chem. |volume=272 |issue= 21 |pages= 13471-4 |year= 1997 |pmid= 9153189 |doi= }}
*{{cite journal | author=Marsters SA, Ayres TM, Skubatch M, ''et al.'' |title=Herpesvirus entry mediator, a member of the tumor necrosis factor receptor (TNFR) family, interacts with members of the TNFR-associated factor family and activates the transcription factors NF-kappaB and AP-1. |journal=J. Biol. Chem. |volume=272 |issue= 22 |pages= 14029-32 |year= 1997 |pmid= 9162022 |doi= }}
*{{cite journal | author=Kwon BS, Tan KB, Ni J, ''et al.'' |title=A newly identified member of the tumor necrosis factor receptor superfamily with a wide tissue distribution and involvement in lymphocyte activation. |journal=J. Biol. Chem. |volume=272 |issue= 22 |pages= 14272-6 |year= 1997 |pmid= 9162061 |doi= }}
*{{cite journal | author=Mauri DN, Ebner R, Montgomery RI, ''et al.'' |title=LIGHT, a new member of the TNF superfamily, and lymphotoxin alpha are ligands for herpesvirus entry mediator. |journal=Immunity |volume=8 |issue= 1 |pages= 21-30 |year= 1998 |pmid= 9462508 |doi= }}
*{{cite journal | author=Lee CH, Chinpaisal C, Wei LN |title=Cloning and characterization of mouse RIP140, a corepressor for nuclear orphan receptor TR2. |journal=Mol. Cell. Biol. |volume=18 |issue= 11 |pages= 6745-55 |year= 1998 |pmid= 9774688 |doi= }}
*{{cite journal | author=Kelly K, Manos E, Jensen G, ''et al.'' |title=APRIL/TRDL-1, a tumor necrosis factor-like ligand, stimulates cell death. |journal=Cancer Res. |volume=60 |issue= 4 |pages= 1021-7 |year= 2000 |pmid= 10706119 |doi= }}
*{{cite journal | author=Zhang J, Salcedo TW, Wan X, ''et al.'' |title=Modulation of T-cell responses to alloantigens by TR6/DcR3. |journal=J. Clin. Invest. |volume=107 |issue= 11 |pages= 1459-68 |year= 2001 |pmid= 11390428 |doi= }}
*{{cite journal | author=Franco PJ, Farooqui M, Seto E, Wei LN |title=The orphan nuclear receptor TR2 interacts directly with both class I and class II histone deacetylases. |journal=Mol. Endocrinol. |volume=15 |issue= 8 |pages= 1318-28 |year= 2001 |pmid= 11463856 |doi= }}
*{{cite journal | author=Carfí A, Willis SH, Whitbeck JC, ''et al.'' |title=Herpes simplex virus glycoprotein D bound to the human receptor HveA. |journal=Mol. Cell |volume=8 |issue= 1 |pages= 169-79 |year= 2001 |pmid= 11511370 |doi= }}
*{{cite journal | author=Bobik A, Kalinina N |title=Tumor necrosis factor receptor and ligand superfamily family members TNFRSF14 and LIGHT: new players in human atherogenesis. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=21 |issue= 12 |pages= 1873-5 |year= 2002 |pmid= 11742858 |doi= }}
*{{cite journal | author=Struyf F, Posavad CM, Keyaerts E, ''et al.'' |title=Search for polymorphisms in the genes for herpesvirus entry mediator, nectin-1, and nectin-2 in immune seronegative individuals. |journal=J. Infect. Dis. |volume=185 |issue= 1 |pages= 36-44 |year= 2002 |pmid= 11756979 |doi= }}
*{{cite journal | author=Carfí A, Gong H, Lou H, ''et al.'' |title=Crystallization and preliminary diffraction studies of the ectodomain of the envelope glycoprotein D from herpes simplex virus 1 alone and in complex with the ectodomain of the human receptor HveA. |journal=Acta Crystallogr. D Biol. Crystallogr. |volume=58 |issue= Pt 5 |pages= 836-8 |year= 2002 |pmid= 11976496 |doi= }}
*{{cite journal | author=Hu YC, Shyr CR, Che W, ''et al.'' |title=Suppression of estrogen receptor-mediated transcription and cell growth by interaction with TR2 orphan receptor. |journal=J. Biol. Chem. |volume=277 |issue= 37 |pages= 33571-9 |year= 2002 |pmid= 12093804 |doi= 10.1074/jbc.M203531200 }}
*{{cite journal | author=Gill RM, Ni J, Hunt JS |title=Differential expression of LIGHT and its receptors in human placental villi and amniochorion membranes. |journal=Am. J. Pathol. |volume=161 |issue= 6 |pages= 2011-7 |year= 2003 |pmid= 12466117 |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=Bender FC, Whitbeck JC, Ponce de Leon M, ''et al.'' |title=Specific association of glycoprotein B with lipid rafts during herpes simplex virus entry. |journal=J. Virol. |volume=77 |issue= 17 |pages= 9542-52 |year= 2003 |pmid= 12915568 |doi= }}
*{{cite journal | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
*{{cite journal | author=Jung HW, La SJ, Kim JY, ''et al.'' |title=High levels of soluble herpes virus entry mediator in sera of patients with allergic and autoimmune diseases. |journal=Exp. Mol. Med. |volume=35 |issue= 6 |pages= 501-8 |year= 2004 |pmid= 14749527 |doi= }}
*{{cite journal | author=Krummenacher C, Baribaud F, Ponce de Leon M, ''et al.'' |title=Comparative usage of herpesvirus entry mediator A and nectin-1 by laboratory strains and clinical isolates of herpes simplex virus. |journal=Virology |volume=322 |issue= 2 |pages= 286-99 |year= 2004 |pmid= 15110526 |doi= 10.1016/j.virol.2004.02.005 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TPT1... {November 19, 2007 12:16:43 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:17:26 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_TPT1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1yz1.
| PDB = {{PDB2|1yz1}}, {{PDB2|2hr9}}
| Name = Tumor protein, translationally-controlled 1
| HGNCid = 12022
| Symbol = TPT1
| AltSymbols =; FLJ27337; HRF; TCTP; p02
| OMIM = 600763
| ECnumber =
| Homologene = 55730
| MGIid = 104890
| GeneAtlas_image1 = PBB_GE_TPT1_216520_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_TPT1_207783_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_TPT1_211943_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005771 |text = multivesicular body}} {{GNF_GO|id=GO:0045298 |text = tubulin complex}}
| Process = {{GNF_GO|id=GO:0006816 |text = calcium ion transport}} {{GNF_GO|id=GO:0006874 |text = cellular calcium ion homeostasis}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7178
| Hs_Ensembl = ENSG00000133112
| Hs_RefseqProtein = NP_003286
| Hs_RefseqmRNA = NM_003295
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 13
| Hs_GenLoc_start = 44809008
| Hs_GenLoc_end = 44813505
| Hs_Uniprot = P13693
| Mm_EntrezGene = 22070
| Mm_Ensembl = ENSMUSG00000060126
| Mm_RefseqmRNA = NM_009429
| Mm_RefseqProtein = NP_033455
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 74579584
| Mm_GenLoc_end = 74581515
| Mm_Uniprot = P63028
}}
}}
'''Tumor protein, translationally-controlled 1''', also known as '''TPT1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TPT1 tumor protein, translationally-controlled 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7178| 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=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=Hochstrasser DF, Frutiger S, Paquet N, ''et al.'' |title=Human liver protein map: a reference database established by microsequencing and gel comparison. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 992-1001 |year= 1993 |pmid= 1286669 |doi= }}
*{{cite journal | author=Gross B, Gaestel M, Böhm H, Bielka H |title=cDNA sequence coding for a translationally controlled human tumor protein. |journal=Nucleic Acids Res. |volume=17 |issue= 20 |pages= 8367 |year= 1989 |pmid= 2813067 |doi= }}
*{{cite journal | author=MacDonald SM, Rafnar T, Langdon J, Lichtenstein LM |title=Molecular identification of an IgE-dependent histamine-releasing factor. |journal=Science |volume=269 |issue= 5224 |pages= 688-90 |year= 1995 |pmid= 7542803 |doi= }}
*{{cite journal | author=Sanchez JC, Schaller D, Ravier F, ''et al.'' |title=Translationally controlled tumor protein: a protein identified in several nontumoral cells including erythrocytes. |journal=Electrophoresis |volume=18 |issue= 1 |pages= 150-5 |year= 1997 |pmid= 9059837 |doi= 10.1002/elps.1150180127 }}
*{{cite journal | author=Rasmussen RK, Ji H, Eddes JS, ''et al.'' |title=Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2. |journal=Electrophoresis |volume=18 |issue= 3-4 |pages= 588-98 |year= 1997 |pmid= 9150946 |doi= 10.1002/elps.1150180342 }}
*{{cite journal | author=MacDonald SM, Paznekas WA, Jabs EW |title=Chromosomal localization of tumor protein, translationally-controlled 1 (TPT1) encoding the human histamine releasing factor (HRF) to 13q12-->q14. |journal=Cytogenet. Cell Genet. |volume=84 |issue= 1-2 |pages= 128-9 |year= 1999 |pmid= 10343127 |doi= }}
*{{cite journal | author=Yoon T, Jung J, Kim M, ''et al.'' |title=Identification of the self-interaction of rat TCTP/IgE-dependent histamine-releasing factor using yeast two-hybrid system. |journal=Arch. Biochem. Biophys. |volume=384 |issue= 2 |pages= 379-82 |year= 2001 |pmid= 11368327 |doi= 10.1006/abbi.2000.2108 }}
*{{cite journal | author=Li F, Zhang D, Fujise K |title=Characterization of fortilin, a novel antiapoptotic protein. |journal=J. Biol. Chem. |volume=276 |issue= 50 |pages= 47542-9 |year= 2002 |pmid= 11598139 |doi= 10.1074/jbc.M108954200 }}
*{{cite journal | author=Andersen JS, Lyon CE, Fox AH, ''et al.'' |title=Directed proteomic analysis of the human nucleolus. |journal=Curr. Biol. |volume=12 |issue= 1 |pages= 1-11 |year= 2002 |pmid= 11790298 |doi= }}
*{{cite journal | author=Bommer UA, Borovjagin AV, Greagg MA, ''et al.'' |title=The mRNA of the translationally controlled tumor protein P23/TCTP is a highly structured RNA, which activates the dsRNA-dependent protein kinase PKR. |journal=RNA |volume=8 |issue= 4 |pages= 478-96 |year= 2002 |pmid= 11991642 |doi= }}
*{{cite journal | author=Zhang D, Li F, Weidner D, ''et al.'' |title=Physical and functional interaction between myeloid cell leukemia 1 protein (MCL1) and Fortilin. The potential role of MCL1 as a fortilin chaperone. |journal=J. Biol. Chem. |volume=277 |issue= 40 |pages= 37430-8 |year= 2002 |pmid= 12149273 |doi= 10.1074/jbc.M207413200 }}
*{{cite journal | author=Yarm FR |title=Plk phosphorylation regulates the microtubule-stabilizing protein TCTP. |journal=Mol. Cell. Biol. |volume=22 |issue= 17 |pages= 6209-21 |year= 2002 |pmid= 12167714 |doi= }}
*{{cite journal | author=Tuynder M, Susini L, Prieur S, ''et al.'' |title=Biological models and genes of tumor reversion: cellular reprogramming through tpt1/TCTP and SIAH-1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 23 |pages= 14976-81 |year= 2003 |pmid= 12399545 |doi= 10.1073/pnas.222470799 }}
*{{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=Budde IK, Lopuhaa CE, de Heer PG, ''et al.'' |title=Lack of correlation between bronchial late allergic reaction to Dermatophagoides pteronyssinus and in vitro immunoglobulin E reactivity to histamine-releasing factor derived from mononuclear cells. |journal=Ann. Allergy Asthma Immunol. |volume=89 |issue= 6 |pages= 606-12 |year= 2003 |pmid= 12487227 |doi= }}
*{{cite journal | author=Asero R, Tedeschi A, Lorini M, ''et al.'' |title=Sera from patients with multiple drug allergy syndrome contain circulating histamine-releasing factors. |journal=Int. Arch. Allergy Immunol. |volume=131 |issue= 3 |pages= 195-200 |year= 2003 |pmid= 12876410 |doi= 10.1159/000071486 }}
*{{cite journal | author=Yoneda K, Rokutan K, Nakamura Y, ''et al.'' |title=Stimulation of human bronchial epithelial cells by IgE-dependent histamine-releasing factor. |journal=Am. J. Physiol. Lung Cell Mol. Physiol. |volume=286 |issue= 1 |pages= L174-81 |year= 2004 |pmid= 12948934 |doi= 10.1152/ajplung.00118.2003 }}
*{{cite journal | author=Reuter TY, Medhurst AL, Waisfisz Q, ''et al.'' |title=Yeast two-hybrid screens imply involvement of Fanconi anemia proteins in transcription regulation, cell signaling, oxidative metabolism, and cellular transport. |journal=Exp. Cell Res. |volume=289 |issue= 2 |pages= 211-21 |year= 2003 |pmid= 14499622 |doi= }}
*{{cite journal | author=Vonakis BM, Sora R, Langdon JM, ''et al.'' |title=Inhibition of cytokine gene transcription by the human recombinant histamine-releasing factor in human T lymphocytes. |journal=J. Immunol. |volume=171 |issue= 7 |pages= 3742-50 |year= 2004 |pmid= 14500674 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TRRAP... {November 19, 2007 12:27:32 PM PST}
- SEARCH REDIRECT: Control Box Found: TRRAP {November 19, 2007 12:28:09 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 19, 2007 12:28:12 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 19, 2007 12:28:12 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 19, 2007 12:28:12 PM PST}
- UPDATED: Updated protein page: TRRAP {November 19, 2007 12:28:19 PM PST}
- INFO: Beginning work on TUBA1B... {November 19, 2007 12:48:18 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:49:07 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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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_TUBA1B_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ffx.
| PDB = {{PDB2|1ffx}}, {{PDB2|1ia0}}, {{PDB2|1jff}}, {{PDB2|1sa0}}, {{PDB2|1sa1}}, {{PDB2|1tub}}, {{PDB2|1tvk}}, {{PDB2|1z2b}}, {{PDB2|2hxf}}, {{PDB2|2hxh}}
| Name = Tubulin, alpha 1b
| HGNCid = 18809
| Symbol = TUBA1B
| AltSymbols =; K-ALPHA-1
| OMIM = 602530
| ECnumber =
| Homologene = 81745
| MGIid = 107804
| GeneAtlas_image1 = PBB_GE_TUBA1B_201090_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_TUBA1B_209251_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_TUBA1B_211058_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0005874 |text = microtubule}} {{GNF_GO|id=GO:0043234 |text = protein complex}}
| Process = {{GNF_GO|id=GO:0007018 |text = microtubule-based movement}} {{GNF_GO|id=GO:0051258 |text = protein polymerization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10376
| Hs_Ensembl = ENSG00000123416
| Hs_RefseqProtein = NP_006073
| Hs_RefseqmRNA = NM_006082
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 47807836
| Hs_GenLoc_end = 47811571
| Hs_Uniprot = P68363
| Mm_EntrezGene = 22143
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_011654
| Mm_RefseqProtein = NP_035784
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Tubulin, alpha 1b''', also known as '''TUBA1B''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TUBA1B tubulin, alpha 1b| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10376| 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=Venter JC |title=Identification of new human receptor and transporter genes by high throughput cDNA (EST) sequencing. |journal=J. Pharm. Pharmacol. |volume=45 Suppl 1 |issue= |pages= 355-60 |year= 1993 |pmid= 8098743 |doi= }}
*{{cite journal | author=Lopez-Fanarraga M, Avila J, Guasch A, ''et al.'' |title=Review: postchaperonin tubulin folding cofactors and their role in microtubule dynamics. |journal=J. Struct. Biol. |volume=135 |issue= 2 |pages= 219-29 |year= 2002 |pmid= 11580271 |doi= 10.1006/jsbi.2001.4386 }}
*{{cite journal | author=Cowan NJ, Dobner PR, Fuchs EV, Cleveland DW |title=Expression of human alpha-tubulin genes: interspecies conservation of 3' untranslated regions. |journal=Mol. Cell. Biol. |volume=3 |issue= 10 |pages= 1738-45 |year= 1984 |pmid= 6646120 |doi= }}
*{{cite journal | author=Kapeller R, Toker A, Cantley LC, Carpenter CL |title=Phosphoinositide 3-kinase binds constitutively to alpha/beta-tubulin and binds to gamma-tubulin in response to insulin. |journal=J. Biol. Chem. |volume=270 |issue= 43 |pages= 25985-91 |year= 1995 |pmid= 7592789 |doi= }}
*{{cite journal | author=Alexandrova N, Niklinski J, Bliskovsky V, ''et al.'' |title=The N-terminal domain of c-Myc associates with alpha-tubulin and microtubules in vivo and in vitro. |journal=Mol. Cell. Biol. |volume=15 |issue= 9 |pages= 5188-95 |year= 1995 |pmid= 7651436 |doi= }}
*{{cite journal | author=Szasz J, Yaffe MB, Sternlicht H |title=Site-directed mutagenesis of alpha-tubulin. Reductive methylation studies of the Lys 394 region. |journal=Biophys. J. |volume=64 |issue= 3 |pages= 792-802 |year= 1993 |pmid= 8097117 |doi= }}
*{{cite journal | author=Baumann MH, Wisniewski T, Levy E, ''et al.'' |title=C-terminal fragments of alpha- and beta-tubulin form amyloid fibrils in vitro and associate with amyloid deposits of familial cerebral amyloid angiopathy, British type. |journal=Biochem. Biophys. Res. Commun. |volume=219 |issue= 1 |pages= 238-42 |year= 1996 |pmid= 8619814 |doi= 10.1006/bbrc.1996.0211 }}
*{{cite journal | author=Gress TM, Müller-Pillasch F, Geng M, ''et al.'' |title=A pancreatic cancer-specific expression profile. |journal=Oncogene |volume=13 |issue= 8 |pages= 1819-30 |year= 1996 |pmid= 8895530 |doi= }}
*{{cite journal | author=Crépieux P, Kwon H, Leclerc N, ''et al.'' |title=I kappaB alpha physically interacts with a cytoskeleton-associated protein through its signal response domain. |journal=Mol. Cell. Biol. |volume=17 |issue= 12 |pages= 7375-85 |year= 1997 |pmid= 9372968 |doi= }}
*{{cite journal | author=Herreros L, Rodríguez-Fernandez JL, Brown MC, ''et al.'' |title=Paxillin localizes to the lymphocyte microtubule organizing center and associates with the microtubule cytoskeleton. |journal=J. Biol. Chem. |volume=275 |issue= 34 |pages= 26436-40 |year= 2000 |pmid= 10840040 |doi= 10.1074/jbc.M003970200 }}
*{{cite journal | author=Watts NR, Sackett DL, Ward RD, ''et al.'' |title=HIV-1 rev depolymerizes microtubules to form stable bilayered rings. |journal=J. Cell Biol. |volume=150 |issue= 2 |pages= 349-60 |year= 2000 |pmid= 10908577 |doi= }}
*{{cite journal | author=Takeoka A, Shimizu M, Horio T |title=Identification of an alpha-tubulin mutant of fission yeast from gamma-tubulin-interacting protein screening: genetic evidence for alpha-/gamma-tubulin interaction. |journal=J. Cell. Sci. |volume=113 Pt 24 |issue= |pages= 4557-62 |year= 2001 |pmid= 11082048 |doi= }}
*{{cite journal | author=Germani A, Bruzzoni-Giovanelli H, Fellous A, ''et al.'' |title=SIAH-1 interacts with alpha-tubulin and degrades the kinesin Kid by the proteasome pathway during mitosis. |journal=Oncogene |volume=19 |issue= 52 |pages= 5997-6006 |year= 2001 |pmid= 11146551 |doi= 10.1038/sj.onc.1204002 }}
*{{cite journal | author=Yokota S, Yanagi H, Yura T, Kubota H |title=Cytosolic chaperonin-containing t-complex polypeptide 1 changes the content of a particular subunit species concomitant with substrate binding and folding activities during the cell cycle. |journal=Eur. J. Biochem. |volume=268 |issue= 17 |pages= 4664-73 |year= 2001 |pmid= 11532003 |doi= }}
*{{cite journal | author=Rommelaere H, De Neve M, Neirynck K, ''et al.'' |title=Prefoldin recognition motifs in the nonhomologous proteins of the actin and tubulin families. |journal=J. Biol. Chem. |volume=276 |issue= 44 |pages= 41023-8 |year= 2001 |pmid= 11535601 |doi= 10.1074/jbc.M106591200 }}
*{{cite journal | author=Klein C, Kramer EM, Cardine AM, ''et al.'' |title=Process outgrowth of oligodendrocytes is promoted by interaction of fyn kinase with the cytoskeletal protein tau. |journal=J. Neurosci. |volume=22 |issue= 3 |pages= 698-707 |year= 2002 |pmid= 11826099 |doi= }}
*{{cite journal | author=Saugstad JA, Yang S, Pohl J, ''et al.'' |title=Interaction between metabotropic glutamate receptor 7 and alpha tubulin. |journal=J. Neurochem. |volume=80 |issue= 6 |pages= 980-8 |year= 2002 |pmid= 11953448 |doi= }}
*{{cite journal | author=Banerjee A |title=Increased levels of tyrosinated alpha-, beta(III)-, and beta(IV)-tubulin isotypes in paclitaxel-resistant MCF-7 breast cancer cells. |journal=Biochem. Biophys. Res. Commun. |volume=293 |issue= 1 |pages= 598-601 |year= 2002 |pmid= 12054644 |doi= 10.1016/S0006-291X(02)00269-3 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on UROD... {November 19, 2007 12:17:26 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:26:25 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| 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_UROD_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1jph.
| PDB = {{PDB2|1jph}}, {{PDB2|1jpi}}, {{PDB2|1jpk}}, {{PDB2|1r3q}}, {{PDB2|1r3r}}, {{PDB2|1r3s}}, {{PDB2|1r3t}}, {{PDB2|1r3v}}, {{PDB2|1r3w}}, {{PDB2|1r3y}}, {{PDB2|1uro}}
| Name = Uroporphyrinogen decarboxylase
| HGNCid = 12591
| Symbol = UROD
| AltSymbols =; PCT
| OMIM = 176100
| ECnumber =
| Homologene = 320
| MGIid = 98916
| GeneAtlas_image1 = PBB_GE_UROD_208970_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_UROD_208971_at_tn.png
| Function = {{GNF_GO|id=GO:0004853 |text = uroporphyrinogen decarboxylase activity}} {{GNF_GO|id=GO:0016829 |text = lyase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006779 |text = porphyrin biosynthetic process}} {{GNF_GO|id=GO:0006783 |text = heme biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7389
| Hs_Ensembl = ENSG00000126088
| Hs_RefseqProtein = NP_000365
| Hs_RefseqmRNA = NM_000374
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 45250417
| Hs_GenLoc_end = 45253928
| Hs_Uniprot = P06132
| Mm_EntrezGene = 22275
| Mm_Ensembl = ENSMUSG00000028684
| Mm_RefseqmRNA = NM_009478
| Mm_RefseqProtein = NP_033504
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 116488150
| Mm_GenLoc_end = 116492307
| Mm_Uniprot = Q91VW4
}}
}}
'''Uroporphyrinogen decarboxylase''', also known as '''UROD''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: UROD uroporphyrinogen decarboxylase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7389| 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 fifth enzyme of the heme biosynthetic pathway. This enzyme is responsible for catalyzing the conversion of uroporphyrinogen to coproporphyrinogen through the removal of four carboxymethyl side chains. Mutations and deficiency in this enzyme are known to cause familial porphyria cutanea tarda and hepatoerythropoetic porphyria.<ref name="entrez">{{cite web | title = Entrez Gene: UROD uroporphyrinogen decarboxylase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7389| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Elder GH, Lee GB, Tovey JA |title=Decreased activity of hepatic uroporphyrinogen decarboxylase in sporadic porphyria cutanea tarda. |journal=N. Engl. J. Med. |volume=299 |issue= 6 |pages= 274-8 |year= 1978 |pmid= 661926 |doi= }}
*{{cite journal | author=de Verneuil H, Bourgeois F, de Rooij F, ''et al.'' |title=Characterization of a new mutation (R292G) and a deletion at the human uroporphyrinogen decarboxylase locus in two patients with hepatoerythropoietic porphyria. |journal=Hum. Genet. |volume=89 |issue= 5 |pages= 548-52 |year= 1992 |pmid= 1634232 |doi= }}
*{{cite journal | author=Romana M, Grandchamp B, Dubart A, ''et al.'' |title=Identification of a new mutation responsible for hepatoerythropoietic porphyria. |journal=Eur. J. Clin. Invest. |volume=21 |issue= 2 |pages= 225-9 |year= 1991 |pmid= 1905636 |doi= }}
*{{cite journal | author=Garey JR, Harrison LM, Franklin KF, ''et al.'' |title=Uroporphyrinogen decarboxylase: a splice site mutation causes the deletion of exon 6 in multiple families with porphyria cutanea tarda. |journal=J. Clin. Invest. |volume=86 |issue= 5 |pages= 1416-22 |year= 1990 |pmid= 2243121 |doi= }}
*{{cite journal | author=Garey JR, Hansen JL, Harrison LM, ''et al.'' |title=A point mutation in the coding region of uroporphyrinogen decarboxylase associated with familial porphyria cutanea tarda. |journal=Blood |volume=73 |issue= 4 |pages= 892-5 |year= 1989 |pmid= 2920211 |doi= }}
*{{cite journal | author=Roméo PH, Raich N, Dubart A, ''et al.'' |title=Molecular cloning and nucleotide sequence of a complete human uroporphyrinogen decarboxylase cDNA. |journal=J. Biol. Chem. |volume=261 |issue= 21 |pages= 9825-31 |year= 1986 |pmid= 3015909 |doi= }}
*{{cite journal | author=Dubart A, Mattei MG, Raich N, ''et al.'' |title=Assignment of human uroporphyrinogen decarboxylase (URO-D) to the p34 band of chromosome 1. |journal=Hum. Genet. |volume=73 |issue= 3 |pages= 277-9 |year= 1986 |pmid= 3460962 |doi= }}
*{{cite journal | author=Romana M, Dubart A, Beaupain D, ''et al.'' |title=Structure of the gene for human uroporphyrinogen decarboxylase. |journal=Nucleic Acids Res. |volume=15 |issue= 18 |pages= 7343-56 |year= 1987 |pmid= 3658695 |doi= }}
*{{cite journal | author=de Verneuil H, Grandchamp B, Beaumont C, ''et al.'' |title=Uroporphyrinogen decarboxylase structural mutant (Gly281----Glu) in a case of porphyria. |journal=Science |volume=234 |issue= 4777 |pages= 732-4 |year= 1986 |pmid= 3775362 |doi= }}
*{{cite journal | author=Roberts AG, Elder GH, De Salamanca RE, ''et al.'' |title=A mutation (G281E) of the human uroporphyrinogen decarboxylase gene causes both hepatoerythropoietic porphyria and overt familial porphyria cutanea tarda: biochemical and genetic studies on Spanish patients. |journal=J. Invest. Dermatol. |volume=104 |issue= 4 |pages= 500-2 |year= 1995 |pmid= 7706766 |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=Meguro K, Fujita H, Ishida N, ''et al.'' |title=Molecular defects of uroporphyrinogen decarboxylase in a patient with mild hepatoerythropoietic porphyria. |journal=J. Invest. Dermatol. |volume=102 |issue= 5 |pages= 681-5 |year= 1994 |pmid= 8176248 |doi= }}
*{{cite journal | author=Moran-Jimenez MJ, Ged C, Romana M, ''et al.'' |title=Uroporphyrinogen decarboxylase: complete human gene sequence and molecular study of three families with hepatoerythropoietic porphyria. |journal=Am. J. Hum. Genet. |volume=58 |issue= 4 |pages= 712-21 |year= 1996 |pmid= 8644733 |doi= }}
*{{cite journal | author=McManus JF, Begley CG, Sassa S, Ratnaike S |title=Five new mutations in the uroporphyrinogen decarboxylase gene identified in families with cutaneous porphyria. |journal=Blood |volume=88 |issue= 9 |pages= 3589-600 |year= 1996 |pmid= 8896428 |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=Whitby FG, Phillips JD, Kushner JP, Hill CP |title=Crystal structure of human uroporphyrinogen decarboxylase. |journal=EMBO J. |volume=17 |issue= 9 |pages= 2463-71 |year= 1998 |pmid= 9564029 |doi= 10.1093/emboj/17.9.2463 }}
*{{cite journal | author=Mendez M, Sorkin L, Rossetti MV, ''et al.'' |title=Familial porphyria cutanea tarda: characterization of seven novel uroporphyrinogen decarboxylase mutations and frequency of common hemochromatosis alleles. |journal=Am. J. Hum. Genet. |volume=63 |issue= 5 |pages= 1363-75 |year= 1998 |pmid= 9792863 |doi= }}
*{{cite journal | author=Wang H, Long Q, Marty SD, ''et al.'' |title=A zebrafish model for hepatoerythropoietic porphyria. |journal=Nat. Genet. |volume=20 |issue= 3 |pages= 239-43 |year= 1998 |pmid= 9806541 |doi= 10.1038/3041 }}
*{{cite journal | author=McManus JF, Begley CG, Sassa S, Ratnaike S |title=Three new mutations in the uroporphyrinogen decarboxylase gene in familial porphyria cutanea tarda. Mutation in brief no. 237. Online. |journal=Hum. Mutat. |volume=13 |issue= 5 |pages= 412 |year= 1999 |pmid= 10338097 |doi= 10.1002/(SICI)1098-1004(1999)13:5<412::AID-HUMU13>3.0.CO;2-N }}
*{{cite journal | author=Christiansen L, Ged C, Hombrados I, ''et al.'' |title=Screening for mutations in the uroporphyrinogen decarboxylase gene using denaturing gradient gel electrophoresis. Identification and characterization of six novel mutations associated with familial PCT. |journal=Hum. Mutat. |volume=14 |issue= 3 |pages= 222-32 |year= 1999 |pmid= 10477430 |doi= 10.1002/(SICI)1098-1004(1999)14:3<222::AID-HUMU5>3.0.CO;2-V }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on VKORC1... {November 19, 2007 12:49:07 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:49:50 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Vitamin K epoxide reductase complex, subunit 1
| HGNCid = 23663
| Symbol = VKORC1
| AltSymbols =; EDTP308; FLJ00289; IMAGE3455200; MGC2694; MST134; MST576; VKCFD2; VKOR
| OMIM = 608547
| ECnumber =
| Homologene = 11416
| MGIid = 106442
| GeneAtlas_image1 = PBB_GE_VKORC1_217949_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004252 |text = serine-type endopeptidase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0047057 |text = vitamin-K-epoxide reductase (warfarin-sensitive) activity}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0042373 |text = vitamin K metabolic process}} {{GNF_GO|id=GO:0050820 |text = positive regulation of coagulation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 79001
| Hs_Ensembl = ENSG00000167397
| Hs_RefseqProtein = NP_076869
| Hs_RefseqmRNA = NM_024006
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 31009956
| Hs_GenLoc_end = 31013551
| Hs_Uniprot = Q9BQB6
| Mm_EntrezGene = 27973
| Mm_Ensembl = ENSMUSG00000030804
| Mm_RefseqmRNA = NM_178600
| Mm_RefseqProtein = NP_848715
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 127684211
| Mm_GenLoc_end = 127686765
| Mm_Uniprot = Q9CRC0
}}
}}
'''Vitamin K epoxide reductase complex, subunit 1''', also known as '''VKORC1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: VKORC1 vitamin K epoxide reductase complex, subunit 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=79001| 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 = Vitamin K is essential for blood clotting but must be enzymatically activated. This enzymatically activated form of vitamin K is a reduced form required for the carboxylation of glutamic acid residues in some blood-clotting proteins. The product of this gene encodes the enzyme that is responsible for reducing vitamin K 2,3-epoxide to the enzymatically activated form. Fatal bleeding can be caused by vitamin K deficiency and by the vitamin K antagonist warfarin, and it is the product of this gene that is sensitive to warfarin. In humans, mutations in this gene can be associated with deficiencies in vitamin-K-dependent clotting factors and, in humans and rats, with warfarin resistance. Two pseudogenes have been identified on chromosome 1 and the X chromosome. Two alternatively spliced transcripts encoding different isoforms have been described.<ref name="entrez">{{cite web | title = Entrez Gene: VKORC1 vitamin K epoxide reductase complex, subunit 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=79001| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Oldenburg J, Bevans CG, Müller CR, Watzka M |title=Vitamin K epoxide reductase complex subunit 1 (VKORC1): the key protein of the vitamin K cycle. |journal=Antioxid. Redox Signal. |volume=8 |issue= 3-4 |pages= 347-53 |year= 2006 |pmid= 16677080 |doi= 10.1089/ars.2006.8.347 }}
*{{cite journal | author=Oldenburg J, Bevans CG, Fregin A, ''et al.'' |title=Current pharmacogenetic developments in oral anticoagulation therapy: the influence of variant VKORC1 and CYP2C9 alleles. |journal=Thromb. Haemost. |volume=98 |issue= 3 |pages= 570-8 |year= 2007 |pmid= 17849045 |doi= }}
*{{cite journal | author=Oldenburg J, von Brederlow B, Fregin A, ''et al.'' |title=Congenital deficiency of vitamin K dependent coagulation factors in two families presents as a genetic defect of the vitamin K-epoxide-reductase-complex. |journal=Thromb. Haemost. |volume=84 |issue= 6 |pages= 937-41 |year= 2001 |pmid= 11154138 |doi= }}
*{{cite journal | author=Fregin A, Rost S, Wolz W, ''et al.'' |title=Homozygosity mapping of a second gene locus for hereditary combined deficiency of vitamin K-dependent clotting factors to the centromeric region of chromosome 16. |journal=Blood |volume=100 |issue= 9 |pages= 3229-32 |year= 2002 |pmid= 12384421 |doi= 10.1182/blood-2002-03-0698 }}
*{{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=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
*{{cite journal | author=Rost S, Fregin A, Ivaskevicius V, ''et al.'' |title=Mutations in VKORC1 cause warfarin resistance and multiple coagulation factor deficiency type 2. |journal=Nature |volume=427 |issue= 6974 |pages= 537-41 |year= 2004 |pmid= 14765194 |doi= 10.1038/nature02214 }}
*{{cite journal | author=Li T, Chang CY, Jin DY, ''et al.'' |title=Identification of the gene for vitamin K epoxide reductase. |journal=Nature |volume=427 |issue= 6974 |pages= 541-4 |year= 2004 |pmid= 14765195 |doi= 10.1038/nature02254 }}
*{{cite journal | author=Goodstadt L, Ponting CP |title=Vitamin K epoxide reductase: homology, active site and catalytic mechanism. |journal=Trends Biochem. Sci. |volume=29 |issue= 6 |pages= 289-92 |year= 2004 |pmid= 15276181 |doi= 10.1016/j.tibs.2004.04.004 }}
*{{cite journal | author=D'Andrea G, D'Ambrosio RL, Di Perna P, ''et al.'' |title=A polymorphism in the VKORC1 gene is associated with an interindividual variability in the dose-anticoagulant effect of warfarin. |journal=Blood |volume=105 |issue= 2 |pages= 645-9 |year= 2005 |pmid= 15358623 |doi= 10.1182/blood-2004-06-2111 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal | author=Harrington DJ, Underwood S, Morse C, ''et al.'' |title=Pharmacodynamic resistance to warfarin associated with a Val66Met substitution in vitamin K epoxide reductase complex subunit 1. |journal=Thromb. Haemost. |volume=93 |issue= 1 |pages= 23-6 |year= 2005 |pmid= 15630486 |doi= 10.1267/THRO05010023 }}
*{{cite journal | author=Tie JK, Nicchitta C, von Heijne G, Stafford DW |title=Membrane topology mapping of vitamin K epoxide reductase by in vitro translation/cotranslocation. |journal=J. Biol. Chem. |volume=280 |issue= 16 |pages= 16410-6 |year= 2005 |pmid= 15716279 |doi= 10.1074/jbc.M500765200 }}
*{{cite journal | author=Bodin L, Verstuyft C, Tregouet DA, ''et al.'' |title=Cytochrome P450 2C9 (CYP2C9) and vitamin K epoxide reductase (VKORC1) genotypes as determinants of acenocoumarol sensitivity. |journal=Blood |volume=106 |issue= 1 |pages= 135-40 |year= 2005 |pmid= 15790782 |doi= 10.1182/blood-2005-01-0341 }}
*{{cite journal | author=Wadelius M, Chen LY, Downes K, ''et al.'' |title=Common VKORC1 and GGCX polymorphisms associated with warfarin dose. |journal=Pharmacogenomics J. |volume=5 |issue= 4 |pages= 262-70 |year= 2005 |pmid= 15883587 |doi= 10.1038/sj.tpj.6500313 }}
*{{cite journal | author=Rieder MJ, Reiner AP, Gage BF, ''et al.'' |title=Effect of VKORC1 haplotypes on transcriptional regulation and warfarin dose. |journal=N. Engl. J. Med. |volume=352 |issue= 22 |pages= 2285-93 |year= 2005 |pmid= 15930419 |doi= 10.1056/NEJMoa044503 }}
*{{cite journal | author=Sconce EA, Khan TI, Wynne HA, ''et al.'' |title=The impact of CYP2C9 and VKORC1 genetic polymorphism and patient characteristics upon warfarin dose requirements: proposal for a new dosing regimen. |journal=Blood |volume=106 |issue= 7 |pages= 2329-33 |year= 2005 |pmid= 15947090 |doi= 10.1182/blood-2005-03-1108 }}
*{{cite journal | author=Wang Y, Zhen Y, Shi Y, ''et al.'' |title=Vitamin k epoxide reductase: a protein involved in angiogenesis. |journal=Mol. Cancer Res. |volume=3 |issue= 6 |pages= 317-23 |year= 2005 |pmid= 15972850 |doi= 10.1158/1541-7786.MCR-04-0221 }}
*{{cite journal | author=Bodin L, Horellou MH, Flaujac C, ''et al.'' |title=A vitamin K epoxide reductase complex subunit-1 (VKORC1) mutation in a patient with vitamin K antagonist resistance. |journal=J. Thromb. Haemost. |volume=3 |issue= 7 |pages= 1533-5 |year= 2005 |pmid= 15978113 |doi= 10.1111/j.1538-7836.2005.01449.x }}
*{{cite journal | author=Wajih N, Hutson SM, Owen J, Wallin R |title=Increased production of functional recombinant human clotting factor IX by baby hamster kidney cells engineered to overexpress VKORC1, the vitamin K 2,3-epoxide-reducing enzyme of the vitamin K cycle. |journal=J. Biol. Chem. |volume=280 |issue= 36 |pages= 31603-7 |year= 2005 |pmid= 16030016 |doi= 10.1074/jbc.M505373200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ZEB2... {November 19, 2007 12:34:39 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 19, 2007 12:40:26 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_ZEB2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2da7.
| PDB = {{PDB2|2da7}}
| Name = Zinc finger E-box binding homeobox 2
| HGNCid = 14881
| Symbol = ZEB2
| AltSymbols =; SIP1; SIP-1; KIAA0569; SMADIP1; ZFHX1B
| OMIM = 605802
| ECnumber =
| Homologene = 8868
| MGIid = 1344407
| GeneAtlas_image1 = PBB_GE_ZEB2_203603_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003676 |text = nucleic acid binding}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016564 |text = transcription repressor activity}} {{GNF_GO|id=GO:0019208 |text = phosphatase regulator activity}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046332 |text = SMAD binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0001755 |text = neural crest cell migration}} {{GNF_GO|id=GO:0001756 |text = somitogenesis}} {{GNF_GO|id=GO:0001843 |text = neural tube closure}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007417 |text = central nervous system development}} {{GNF_GO|id=GO:0016481 |text = negative regulation of transcription}} {{GNF_GO|id=GO:0048598 |text = embryonic morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 9839
| Hs_Ensembl = ENSG00000169554
| Hs_RefseqProtein = NP_055610
| Hs_RefseqmRNA = NM_014795
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 144862055
| Hs_GenLoc_end = 144994386
| Hs_Uniprot = O60315
| Mm_EntrezGene = 24136
| Mm_Ensembl = ENSMUSG00000026872
| Mm_RefseqmRNA = NM_001033635
| Mm_RefseqProtein = NP_001028807
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 44809127
| Mm_GenLoc_end = 44935233
| Mm_Uniprot = Q3URW5
}}
}}
'''Zinc finger E-box binding homeobox 2''', also known as '''ZEB2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ZEB2 zinc finger E-box binding homeobox 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9839| 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 SMADIP1 gene (also known as SIP1) is a member of the delta-EF1 (TCF8; MIM 189909)/Zfh1 family of 2-handed zinc finger/homeodomain proteins. SMADIP1 interacts with receptor-mediated, activated full-length SMADs (see MIM 605568).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: ZEB2 zinc finger E-box binding homeobox 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9839| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Mowat DR, Wilson MJ, Goossens M |title=Mowat-Wilson syndrome. |journal=J. Med. Genet. |volume=40 |issue= 5 |pages= 305-10 |year= 2003 |pmid= 12746390 |doi= }}
*{{cite journal | author=Nagase T, Ishikawa K, Miyajima N, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. |journal=DNA Res. |volume=5 |issue= 1 |pages= 31-9 |year= 1998 |pmid= 9628581 |doi= }}
*{{cite journal | author=Ueki N, Oda T, Kondo M, ''et al.'' |title=Selection system for genes encoding nuclear-targeted proteins. |journal=Nat. Biotechnol. |volume=16 |issue= 13 |pages= 1338-42 |year= 1999 |pmid= 9853615 |doi= 10.1038/4315 }}
*{{cite journal | author=Verschueren K, Remacle JE, Collart C, ''et al.'' |title=SIP1, a novel zinc finger/homeodomain repressor, interacts with Smad proteins and binds to 5'-CACCT sequences in candidate target genes. |journal=J. Biol. Chem. |volume=274 |issue= 29 |pages= 20489-98 |year= 1999 |pmid= 10400677 |doi= }}
*{{cite journal | author=Wakamatsu N, Yamada Y, Yamada K, ''et al.'' |title=Mutations in SIP1, encoding Smad interacting protein-1, cause a form of Hirschsprung disease. |journal=Nat. Genet. |volume=27 |issue= 4 |pages= 369-70 |year= 2001 |pmid= 11279515 |doi= 10.1038/86860 }}
*{{cite journal | author=Comijn J, Berx G, Vermassen P, ''et al.'' |title=The two-handed E box binding zinc finger protein SIP1 downregulates E-cadherin and induces invasion. |journal=Mol. Cell |volume=7 |issue= 6 |pages= 1267-78 |year= 2001 |pmid= 11430829 |doi= }}
*{{cite journal | author=Cacheux V, Dastot-Le Moal F, Kääriäinen H, ''et al.'' |title=Loss-of-function mutations in SIP1 Smad interacting protein 1 result in a syndromic Hirschsprung disease. |journal=Hum. Mol. Genet. |volume=10 |issue= 14 |pages= 1503-10 |year= 2001 |pmid= 11448942 |doi= }}
*{{cite journal | author=Tylzanowski P, Verschueren K, Huylebroeck D, Luyten FP |title=Smad-interacting protein 1 is a repressor of liver/bone/kidney alkaline phosphatase transcription in bone morphogenetic protein-induced osteogenic differentiation of C2C12 cells. |journal=J. Biol. Chem. |volume=276 |issue= 43 |pages= 40001-7 |year= 2001 |pmid= 11477103 |doi= 10.1074/jbc.M104112200 }}
*{{cite journal | author=Yamada K, Yamada Y, Nomura N, ''et al.'' |title=Nonsense and frameshift mutations in ZFHX1B, encoding Smad-interacting protein 1, cause a complex developmental disorder with a great variety of clinical features. |journal=Am. J. Hum. Genet. |volume=69 |issue= 6 |pages= 1178-85 |year= 2002 |pmid= 11592033 |doi= }}
*{{cite journal | author=Amiel J, Espinosa-Parrilla Y, Steffann J, ''et al.'' |title=Large-scale deletions and SMADIP1 truncating mutations in syndromic Hirschsprung disease with involvement of midline structures. |journal=Am. J. Hum. Genet. |volume=69 |issue= 6 |pages= 1370-7 |year= 2002 |pmid= 11595972 |doi= }}
*{{cite journal | author=Zweier C, Albrecht B, Mitulla B, ''et al.'' |title="Mowat-Wilson" syndrome with and without Hirschsprung disease is a distinct, recognizable multiple congenital anomalies-mental retardation syndrome caused by mutations in the zinc finger homeo box 1B gene. |journal=Am. J. Med. Genet. |volume=108 |issue= 3 |pages= 177-81 |year= 2002 |pmid= 11891681 |doi= }}
*{{cite journal | author=Nagaya M, Kato J, Niimi N, ''et al.'' |title=Clinical features of a form of Hirschsprung's disease caused by a novel genetic abnormality. |journal=J. Pediatr. Surg. |volume=37 |issue= 8 |pages= 1117-22 |year= 2002 |pmid= 12149685 |doi= }}
*{{cite journal | author=Guaita S, Puig I, Franci C, ''et al.'' |title=Snail induction of epithelial to mesenchymal transition in tumor cells is accompanied by MUC1 repression and ZEB1 expression. |journal=J. Biol. Chem. |volume=277 |issue= 42 |pages= 39209-16 |year= 2002 |pmid= 12161443 |doi= 10.1074/jbc.M206400200 }}
*{{cite journal | author=Espinosa-Parrilla Y, Amiel J, Augé J, ''et al.'' |title=Expression of the SMADIP1 gene during early human development. |journal=Mech. Dev. |volume=114 |issue= 1-2 |pages= 187-91 |year= 2003 |pmid= 12175509 |doi= }}
*{{cite journal | author=Yoneda M, Fujita T, Yamada Y, ''et al.'' |title=Late infantile Hirschsprung disease-mental retardation syndrome with a 3-bp deletion in ZFHX1B. |journal=Neurology |volume=59 |issue= 10 |pages= 1637-40 |year= 2002 |pmid= 12451214 |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=Postigo AA |title=Opposing functions of ZEB proteins in the regulation of the TGFbeta/BMP signaling pathway. |journal=EMBO J. |volume=22 |issue= 10 |pages= 2443-52 |year= 2003 |pmid= 12743038 |doi= 10.1093/emboj/cdg225 }}
*{{cite journal | author=Postigo AA, Depp JL, Taylor JJ, Kroll KL |title=Regulation of Smad signaling through a differential recruitment of coactivators and corepressors by ZEB proteins. |journal=EMBO J. |volume=22 |issue= 10 |pages= 2453-62 |year= 2003 |pmid= 12743039 |doi= 10.1093/emboj/cdg226 }}
*{{cite journal | author=Zweier C, Temple IK, Beemer F, ''et al.'' |title=Characterisation of deletions of the ZFHX1B region and genotype-phenotype analysis in Mowat-Wilson syndrome. |journal=J. Med. Genet. |volume=40 |issue= 8 |pages= 601-5 |year= 2003 |pmid= 12920073 |doi= }}
}}
{{refend}}
{{protein-stub}}
end log.
