Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 23:42, 18 November 2007 (UTC)
[edit]Proteins without matches (3)
[edit]Proteins with a High Potential Match (2)
[edit]Redirected Proteins (5)
[edit]Manual Inspection (Page not found) (5)
[edit]
Protein Status Grid - Date: 23:42, 18 November 2007 (UTC)
[edit]Vebose Log - Date: 23:42, 18 November 2007 (UTC)
[edit]- INFO: Beginning work on ACP1... {November 18, 2007 3:22:36 PM PST}
- SEARCH REDIRECT: Control Box Found: ACP1 {November 18, 2007 3:23:30 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 3:23:31 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 3:23:31 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 3:23:31 PM PST}
- UPDATED: Updated protein page: ACP1 {November 18, 2007 3:23:44 PM PST}
- INFO: Beginning work on APTX... {November 18, 2007 3:33:48 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 3:34:57 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 = Aprataxin
| HGNCid = 15984
| Symbol = APTX
| AltSymbols =; AOA; AOA1; AXA1; EAOH; EOAHA; FHA-HIT; FLJ20157; MGC1072
| OMIM = 606350
| ECnumber =
| Homologene = 41634
| MGIid = 1913658
| GeneAtlas_image1 = PBB_GE_APTX_218527_at_tn.png
| Function = {{GNF_GO|id=GO:0003676 |text = nucleic acid binding}} {{GNF_GO|id=GO:0003684 |text = damaged DNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion 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:0000012 |text = single strand break repair}} {{GNF_GO|id=GO:0006284 |text = base-excision repair}} {{GNF_GO|id=GO:0008219 |text = cell death}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 54840
| Hs_Ensembl = ENSG00000137074
| Hs_RefseqProtein = NP_060162
| Hs_RefseqmRNA = NM_017692
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 32962609
| Hs_GenLoc_end = 33015110
| Hs_Uniprot = Q7Z2E3
| Mm_EntrezGene = 66408
| Mm_Ensembl = ENSMUSG00000028411
| Mm_RefseqmRNA = NM_001025445
| Mm_RefseqProtein = NP_001020616
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 40874906
| Mm_GenLoc_end = 40891858
| Mm_Uniprot = Q7TQC5
}}
}}
'''Aprataxin''', also known as '''APTX''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: APTX aprataxin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54840| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the histidine triad (HIT) superfamily, some of which have nucleotide-binding and diadenosine polyphosphate hydrolase activities. The encoded protein may play a role in single-stranded DNA repair. Mutations in this gene have been associated with ataxia-ocular apraxia. Multiple transcript variants encoding distinct isoforms have been identified for this gene, however, the full length nature of some variants has not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: APTX aprataxin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54840| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Aicardi J, Barbosa C, Andermann E, ''et al.'' |title=Ataxia-ocular motor apraxia: a syndrome mimicking ataxia-telangiectasia. |journal=Ann. Neurol. |volume=24 |issue= 4 |pages= 497-502 |year= 1989 |pmid= 3239952 |doi= 10.1002/ana.410240404 }}
*{{cite journal | author=Gascon GG, Abdo N, Sigut D, ''et al.'' |title=Ataxia-oculomotor apraxia syndrome. |journal=J. Child Neurol. |volume=10 |issue= 2 |pages= 118-22 |year= 1995 |pmid= 7782601 |doi= }}
*{{cite journal | author=Hannan MA, Sigut D, Waghray M, Gascon GG |title=Ataxia-ocular motor apraxia syndrome: an investigation of cellular radiosensitivity of patients and their families. |journal=J. Med. Genet. |volume=31 |issue= 12 |pages= 953-6 |year= 1995 |pmid= 7891378 |doi= }}
*{{cite journal | author=Moreira MC, Barbot C, Tachi N, ''et al.'' |title=Homozygosity mapping of Portuguese and Japanese forms of ataxia-oculomotor apraxia to 9p13, and evidence for genetic heterogeneity. |journal=Am. J. Hum. Genet. |volume=68 |issue= 2 |pages= 501-8 |year= 2001 |pmid= 11170899 |doi= }}
*{{cite journal | author=Date H, Onodera O, Tanaka H, ''et al.'' |title=Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is caused by mutations in a new HIT superfamily gene. |journal=Nat. Genet. |volume=29 |issue= 2 |pages= 184-8 |year= 2001 |pmid= 11586299 |doi= 10.1038/ng1001-184 }}
*{{cite journal | author=Moreira MC, Barbot C, Tachi N, ''et al.'' |title=The gene mutated in ataxia-ocular apraxia 1 encodes the new HIT/Zn-finger protein aprataxin. |journal=Nat. Genet. |volume=29 |issue= 2 |pages= 189-93 |year= 2001 |pmid= 11586300 |doi= 10.1038/ng1001-189 }}
*{{cite journal | author=Brenner C |title=Hint, Fhit, and GalT: function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases. |journal=Biochemistry |volume=41 |issue= 29 |pages= 9003-14 |year= 2002 |pmid= 12119013 |doi= }}
*{{cite journal | author=Shimazaki H, Takiyama Y, Sakoe K, ''et al.'' |title=Early-onset ataxia with ocular motor apraxia and hypoalbuminemia: the aprataxin gene mutations. |journal=Neurology |volume=59 |issue= 4 |pages= 590-5 |year= 2002 |pmid= 12196655 |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=Tranchant C, Fleury M, Moreira MC, ''et al.'' |title=Phenotypic variability of aprataxin gene mutations. |journal=Neurology |volume=60 |issue= 5 |pages= 868-70 |year= 2004 |pmid= 12629250 |doi= }}
*{{cite journal | author=Le Ber I, Moreira MC, Rivaud-Péchoux S, ''et al.'' |title=Cerebellar ataxia with oculomotor apraxia type 1: clinical and genetic studies. |journal=Brain |volume=126 |issue= Pt 12 |pages= 2761-72 |year= 2003 |pmid= 14506070 |doi= 10.1093/brain/awg283 }}
*{{cite journal | author=Sekijima Y, Hashimoto T, Onodera O, ''et al.'' |title=Severe generalized dystonia as a presentation of a patient with aprataxin gene mutation. |journal=Mov. Disord. |volume=18 |issue= 10 |pages= 1198-200 |year= 2004 |pmid= 14534929 |doi= 10.1002/mds.10526 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Sano Y, Date H, Igarashi S, ''et al.'' |title=Aprataxin, the causative protein for EAOH is a nuclear protein with a potential role as a DNA repair protein. |journal=Ann. Neurol. |volume=55 |issue= 2 |pages= 241-9 |year= 2004 |pmid= 14755728 |doi= 10.1002/ana.10808 }}
*{{cite journal | author=Gueven N, Becherel OJ, Kijas AW, ''et al.'' |title=Aprataxin, a novel protein that protects against genotoxic stress. |journal=Hum. Mol. Genet. |volume=13 |issue= 10 |pages= 1081-93 |year= 2004 |pmid= 15044383 |doi= 10.1093/hmg/ddh122 }}
*{{cite journal | author=Humphray SJ, Oliver K, Hunt AR, ''et al.'' |title=DNA sequence and analysis of human chromosome 9. |journal=Nature |volume=429 |issue= 6990 |pages= 369-74 |year= 2004 |pmid= 15164053 |doi= 10.1038/nature02465 }}
*{{cite journal | author=Habeck M, Zühlke C, Bentele KH, ''et al.'' |title=Aprataxin mutations are a rare cause of early onset ataxia in Germany. |journal=J. Neurol. |volume=251 |issue= 5 |pages= 591-4 |year= 2004 |pmid= 15164193 |doi= 10.1007/s00415-004-0374-7 }}
*{{cite journal | author=Hirano M, Nishiwaki T, Kariya S, ''et al.'' |title=Novel splice variants increase molecular diversity of aprataxin, the gene responsible for early-onset ataxia with ocular motor apraxia and hypoalbuminemia. |journal=Neurosci. Lett. |volume=366 |issue= 2 |pages= 120-5 |year= 2004 |pmid= 15276230 |doi= 10.1016/j.neulet.2004.05.034 }}
*{{cite journal | author=Amouri R, Moreira MC, Zouari M, ''et al.'' |title=Aprataxin gene mutations in Tunisian families. |journal=Neurology |volume=63 |issue= 5 |pages= 928-9 |year= 2005 |pmid= 15365154 |doi= }}
*{{cite journal | author=Clements PM, Breslin C, Deeks ED, ''et al.'' |title=The ataxia-oculomotor apraxia 1 gene product has a role distinct from ATM and interacts with the DNA strand break repair proteins XRCC1 and XRCC4. |journal=DNA Repair (Amst.) |volume=3 |issue= 11 |pages= 1493-502 |year= 2005 |pmid= 15380105 |doi= 10.1016/j.dnarep.2004.06.017 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ODC1... {November 18, 2007 3:23:44 PM PST}
- SEARCH REDIRECT: Control Box Found: ODC1 {November 18, 2007 3:24:25 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 3:24:26 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 3:24:26 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 3:24:26 PM PST}
- UPDATED: Updated protein page: ODC1 {November 18, 2007 3:24:38 PM PST}
- INFO: Beginning work on PDK1... {November 18, 2007 3:25:37 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 3:26:23 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Pyruvate dehydrogenase kinase, isozyme 1
| HGNCid = 8809
| Symbol = PDK1
| AltSymbols =;
| OMIM = 602524
| ECnumber =
| Homologene = 20576
| MGIid = 1926119
| GeneAtlas_image1 = PBB_GE_PDK1_206686_at_tn.png
| Function = {{GNF_GO|id=GO:0004673 |text = protein histidine kinase activity}} {{GNF_GO|id=GO:0004740 |text = [pyruvate dehydrogenase (lipoamide)] kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016301 |text = kinase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}}
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006006 |text = glucose metabolic process}} {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}} {{GNF_GO|id=GO:0018106 |text = peptidyl-histidine phosphorylation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5163
| Hs_Ensembl = ENSG00000152256
| Hs_RefseqProtein = NP_002601
| Hs_RefseqmRNA = NM_002610
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 173129025
| Hs_GenLoc_end = 173172108
| Hs_Uniprot = Q15118
| Mm_EntrezGene = 228026
| Mm_Ensembl = ENSMUSG00000006494
| Mm_RefseqmRNA = NM_172665
| Mm_RefseqProtein = NP_766253
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 71674063
| Mm_GenLoc_end = 71702840
| Mm_Uniprot = Q3U5E5
}}
}}
'''Pyruvate dehydrogenase kinase, isozyme 1''', also known as '''PDK1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PDK1 pyruvate dehydrogenase kinase, isozyme 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5163| 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 = Pyruvate dehydrogenase (PDH) is a mitochondrial multienzyme complex that catalyzes the oxidative decarboxylation of pyruvate and is one of the major enzymes responsible for the regulation of homeostasis of carbohydrate fuels in mammals. The enzymatic activity is regulated by a phosphorylation/dephosphorylation cycle. Phosphorylation of PDH by a specific pyruvate dehydrogenase kinase (PDK) results in inactivation.<ref name="entrez">{{cite web | title = Entrez Gene: PDK1 pyruvate dehydrogenase kinase, isozyme 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5163| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Sugden MC, Holness MJ |title=Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKs. |journal=Am. J. Physiol. Endocrinol. Metab. |volume=284 |issue= 5 |pages= E855-62 |year= 2003 |pmid= 12676647 |doi= 10.1152/ajpendo.00526.2002 }}
*{{cite journal | author=Gudi R, Bowker-Kinley MM, Kedishvili NY, ''et al.'' |title=Diversity of the pyruvate dehydrogenase kinase gene family in humans. |journal=J. Biol. Chem. |volume=270 |issue= 48 |pages= 28989-94 |year= 1996 |pmid= 7499431 |doi= }}
*{{cite journal | author=Liu S, Baker JC, Andrews PC, Roche TE |title=Recombinant expression and evaluation of the lipoyl domains of the dihydrolipoyl acetyltransferase component of the human pyruvate dehydrogenase complex. |journal=Arch. Biochem. Biophys. |volume=316 |issue= 2 |pages= 926-40 |year= 1995 |pmid= 7864652 |doi= }}
*{{cite journal | author=Pullen N, Dennis PB, Andjelkovic M, ''et al.'' |title=Phosphorylation and activation of p70s6k by PDK1. |journal=Science |volume=279 |issue= 5351 |pages= 707-10 |year= 1998 |pmid= 9445476 |doi= }}
*{{cite journal | author=Walker KS, Deak M, Paterson A, ''et al.'' |title=Activation of protein kinase B beta and gamma isoforms by insulin in vivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro: comparison with protein kinase B alpha. |journal=Biochem. J. |volume=331 ( Pt 1) |issue= |pages= 299-308 |year= 1998 |pmid= 9512493 |doi= }}
*{{cite journal | author=Cheng X, Ma Y, Moore M, ''et al.'' |title=Phosphorylation and activation of cAMP-dependent protein kinase by phosphoinositide-dependent protein kinase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 17 |pages= 9849-54 |year= 1998 |pmid= 9707564 |doi= }}
*{{cite journal | author=Le Good JA, Ziegler WH, Parekh DB, ''et al.'' |title=Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1. |journal=Science |volume=281 |issue= 5385 |pages= 2042-5 |year= 1998 |pmid= 9748166 |doi= }}
*{{cite journal | author=Park J, Leong ML, Buse P, ''et al.'' |title=Serum and glucocorticoid-inducible kinase (SGK) is a target of the PI 3-kinase-stimulated signaling pathway. |journal=EMBO J. |volume=18 |issue= 11 |pages= 3024-33 |year= 1999 |pmid= 10357815 |doi= 10.1093/emboj/18.11.3024 }}
*{{cite journal | author=Jensen CJ, Buch MB, Krag TO, ''et al.'' |title=90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1. |journal=J. Biol. Chem. |volume=274 |issue= 38 |pages= 27168-76 |year= 1999 |pmid= 10480933 |doi= }}
*{{cite journal | author=King CC, Zenke FT, Dawson PE, ''et al.'' |title=Sphingosine is a novel activator of 3-phosphoinositide-dependent kinase 1. |journal=J. Biol. Chem. |volume=275 |issue= 24 |pages= 18108-13 |year= 2000 |pmid= 10748151 |doi= 10.1074/jbc.M909663199 }}
*{{cite journal | author=Flynn P, Mellor H, Casamassima A, Parker PJ |title=Rho GTPase control of protein kinase C-related protein kinase activation by 3-phosphoinositide-dependent protein kinase. |journal=J. Biol. Chem. |volume=275 |issue= 15 |pages= 11064-70 |year= 2000 |pmid= 10753910 |doi= }}
*{{cite journal | author=Kirk RI, Sanderson MR, Lerea KM |title=Threonine phosphorylation of the beta 3 integrin cytoplasmic tail, at a site recognized by PDK1 and Akt/PKB in vitro, regulates Shc binding. |journal=J. Biol. Chem. |volume=275 |issue= 40 |pages= 30901-6 |year= 2000 |pmid= 10896934 |doi= 10.1074/jbc.M001908200 }}
*{{cite journal | author=King CC, Gardiner EM, Zenke FT, ''et al.'' |title=p21-activated kinase (PAK1) is phosphorylated and activated by 3-phosphoinositide-dependent kinase-1 (PDK1). |journal=J. Biol. Chem. |volume=275 |issue= 52 |pages= 41201-9 |year= 2001 |pmid= 10995762 |doi= 10.1074/jbc.M006553200 }}
*{{cite journal | author=Rafty LA, Khachigian LM |title=Sp1 phosphorylation regulates inducible expression of platelet-derived growth factor B-chain gene via atypical protein kinase C-zeta. |journal=Nucleic Acids Res. |volume=29 |issue= 5 |pages= 1027-33 |year= 2001 |pmid= 11222751 |doi= }}
*{{cite journal | author=Matsumoto M, Ogawa W, Hino Y, ''et al.'' |title=Inhibition of insulin-induced activation of Akt by a kinase-deficient mutant of the epsilon isozyme of protein kinase C. |journal=J. Biol. Chem. |volume=276 |issue= 17 |pages= 14400-6 |year= 2001 |pmid= 11278835 |doi= 10.1074/jbc.M011093200 }}
*{{cite journal | author=Persad S, Attwell S, Gray V, ''et al.'' |title=Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: critical roles for kinase activity and amino acids arginine 211 and serine 343. |journal=J. Biol. Chem. |volume=276 |issue= 29 |pages= 27462-9 |year= 2001 |pmid= 11313365 |doi= 10.1074/jbc.M102940200 }}
*{{cite journal | author=Kolobova E, Tuganova A, Boulatnikov I, Popov KM |title=Regulation of pyruvate dehydrogenase activity through phosphorylation at multiple sites. |journal=Biochem. J. |volume=358 |issue= Pt 1 |pages= 69-77 |year= 2001 |pmid= 11485553 |doi= }}
*{{cite journal | author=Korotchkina LG, Patel MS |title=Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenase. |journal=J. Biol. Chem. |volume=276 |issue= 40 |pages= 37223-9 |year= 2001 |pmid= 11486000 |doi= 10.1074/jbc.M103069200 }}
*{{cite journal | author=Hodgkinson CP, Sale GJ |title=Regulation of both PDK1 and the phosphorylation of PKC-zeta and -delta by a C-terminal PRK2 fragment. |journal=Biochemistry |volume=41 |issue= 2 |pages= 561-9 |year= 2002 |pmid= 11781095 |doi= }}
*{{cite journal | author=Tuganova A, Boulatnikov I, Popov KM |title=Interaction between the individual isoenzymes of pyruvate dehydrogenase kinase and the inner lipoyl-bearing domain of transacetylase component of pyruvate dehydrogenase complex. |journal=Biochem. J. |volume=366 |issue= Pt 1 |pages= 129-36 |year= 2002 |pmid= 11978179 |doi= 10.1042/BJ20020301 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PEBP1... {November 18, 2007 3:24:38 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 3:25:37 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_PEBP1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a44.
| PDB = {{PDB2|1a44}}, {{PDB2|1b7a}}, {{PDB2|1bd9}}, {{PDB2|1beh}}
| Name = Phosphatidylethanolamine binding protein 1
| HGNCid = 8630
| Symbol = PEBP1
| AltSymbols =; PBP; HCNP; PEBP; RKIP
| OMIM = 604591
| ECnumber =
| Homologene = 37637
| MGIid = 1344408
| GeneAtlas_image1 = PBB_GE_PEBP1_210825_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PEBP1_211941_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_PEBP1_205353_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004867 |text = serine-type endopeptidase inhibitor activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008289 |text = lipid binding}} {{GNF_GO|id=GO:0008429 |text = phosphatidylethanolamine binding}}
| Component =
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5037
| Hs_Ensembl = ENSG00000089220
| Hs_RefseqProtein = NP_002558
| Hs_RefseqmRNA = NM_002567
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 117058253
| Hs_GenLoc_end = 117067770
| Hs_Uniprot = P30086
| Mm_EntrezGene = 23980
| Mm_Ensembl = ENSMUSG00000032959
| Mm_RefseqmRNA = NM_018858
| Mm_RefseqProtein = NP_061346
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 117543684
| Mm_GenLoc_end = 117548617
| Mm_Uniprot = Q3TGC5
}}
}}
'''Phosphatidylethanolamine binding protein 1''', also known as '''PEBP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PEBP1 phosphatidylethanolamine binding protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5037| 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=Schoentgen F, Jollès P |title=From structure to function: possible biological roles of a new widespread protein family binding hydrophobic ligands and displaying a nucleotide binding site. |journal=FEBS Lett. |volume=369 |issue= 1 |pages= 22-6 |year= 1995 |pmid= 7641877 |doi= }}
*{{cite journal | author=Ojika K, Mitake S, Tohdoh N, ''et al.'' |title=Hippocampal cholinergic neurostimulating peptides (HCNP). |journal=Prog. Neurobiol. |volume=60 |issue= 1 |pages= 37-83 |year= 2000 |pmid= 10622376 |doi= }}
*{{cite journal | author=Odabaei G, Chatterjee D, Jazirehi AR, ''et al.'' |title=Raf-1 kinase inhibitor protein: structure, function, regulation of cell signaling, and pivotal role in apoptosis. |journal=Adv. Cancer Res. |volume=91 |issue= |pages= 169-200 |year= 2004 |pmid= 15327891 |doi= 10.1016/S0065-230X(04)91005-6 }}
*{{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=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi= }}
*{{cite journal | author=Tohdoh N, Tojo S, Agui H, Ojika K |title=Sequence homology of rat and human HCNP precursor proteins, bovine phosphatidylethanolamine-binding protein and rat 23-kDa protein associated with the opioid-binding protein. |journal=Brain Res. Mol. Brain Res. |volume=30 |issue= 2 |pages= 381-4 |year= 1995 |pmid= 7637590 |doi= }}
*{{cite journal | author=Seddiqi N, Bollengier F, Alliel PM, ''et al.'' |title=Amino acid sequence of the Homo sapiens brain 21-23-kDa protein (neuropolypeptide h3), comparison with its counterparts from Rattus norvegicus and Bos taurus species, and expression of its mRNA in different tissues. |journal=J. Mol. Evol. |volume=39 |issue= 6 |pages= 655-60 |year= 1995 |pmid= 7807553 |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=Hori N, Chae KS, Murakawa K, ''et al.'' |title=A human cDNA sequence homologue of bovine phosphatidylethanolamine-binding protein. |journal=Gene |volume=140 |issue= 2 |pages= 293-4 |year= 1994 |pmid= 8144042 |doi= }}
*{{cite journal | author=Moore C, Perry AC, Love S, Hall L |title=Sequence analysis and immunolocalisation of phosphatidylethanolamine binding protein (PBP) in human brain tissue. |journal=Brain Res. Mol. Brain Res. |volume=37 |issue= 1-2 |pages= 74-8 |year= 1996 |pmid= 8738137 |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=Banfield MJ, Barker JJ, Perry AC, Brady RL |title=Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction. |journal=Structure |volume=6 |issue= 10 |pages= 1245-54 |year= 1998 |pmid= 9782050 |doi= }}
*{{cite journal | author=Yeung K, Seitz T, Li S, ''et al.'' |title=Suppression of Raf-1 kinase activity and MAP kinase signalling by RKIP. |journal=Nature |volume=401 |issue= 6749 |pages= 173-7 |year= 1999 |pmid= 10490027 |doi= 10.1038/43686 }}
*{{cite journal | author=Yeung K, Janosch P, McFerran B, ''et al.'' |title=Mechanism of suppression of the Raf/MEK/extracellular signal-regulated kinase pathway by the raf kinase inhibitor protein. |journal=Mol. Cell. Biol. |volume=20 |issue= 9 |pages= 3079-85 |year= 2000 |pmid= 10757792 |doi= }}
*{{cite journal | author=Hengst U, Albrecht H, Hess D, Monard D |title=The phosphatidylethanolamine-binding protein is the prototype of a novel family of serine protease inhibitors. |journal=J. Biol. Chem. |volume=276 |issue= 1 |pages= 535-40 |year= 2001 |pmid= 11034991 |doi= 10.1074/jbc.M002524200 }}
*{{cite journal | author=Yeung KC, Rose DW, Dhillon AS, ''et al.'' |title=Raf kinase inhibitor protein interacts with NF-kappaB-inducing kinase and TAK1 and inhibits NF-kappaB activation. |journal=Mol. Cell. Biol. |volume=21 |issue= 21 |pages= 7207-17 |year= 2001 |pmid= 11585904 |doi= 10.1128/MCB.21.21.7207-7217.2001 }}
*{{cite journal | author=Maki M, Matsukawa N, Yuasa H, ''et al.'' |title=Decreased expression of hippocampal cholinergic neurostimulating peptide precursor protein mRNA in the hippocampus in Alzheimer disease. |journal=J. Neuropathol. Exp. Neurol. |volume=61 |issue= 2 |pages= 176-85 |year= 2002 |pmid= 11853019 |doi= }}
*{{cite journal | author=Nakayama M, Kikuno R, Ohara O |title=Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs. |journal=Genome Res. |volume=12 |issue= 11 |pages= 1773-84 |year= 2003 |pmid= 12421765 |doi= 10.1101/gr.406902 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PPP2R2B... {November 18, 2007 3:26:23 PM PST}
- SEARCH REDIRECT: Control Box Found: PPP2R2B {November 18, 2007 3:28:12 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 3:28:20 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 3:28:20 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 3:28:20 PM PST}
- UPDATED: Updated protein page: PPP2R2B {November 18, 2007 3:28:33 PM PST}
- INFO: Beginning work on PSMB10... {November 18, 2007 3:28:33 PM PST}
- SEARCH REDIRECT: Control Box Found: PSMB10 {November 18, 2007 3:29:24 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 3:29:31 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 3:29:31 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 3:29:31 PM PST}
- UPDATED: Updated protein page: PSMB10 {November 18, 2007 3:29:46 PM PST}
- INFO: Beginning work on PSMD11... {November 18, 2007 3:29:46 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 3:30:54 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Proteasome (prosome, macropain) 26S subunit, non-ATPase, 11
| HGNCid = 9556
| Symbol = PSMD11
| AltSymbols =; MGC3844; S9; p44.5
| OMIM = 604449
| ECnumber =
| Homologene = 2108
| MGIid = 1916327
| GeneAtlas_image1 = PBB_GE_PSMD11_208777_s_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0000502 |text = proteasome complex (sensu Eukaryota)}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5717
| Hs_Ensembl = ENSG00000108671
| Hs_RefseqProtein = NP_002806
| Hs_RefseqmRNA = NM_002815
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 27795615
| Hs_GenLoc_end = 27832154
| Hs_Uniprot = O00231
| Mm_EntrezGene = 69077
| Mm_Ensembl = ENSMUSG00000017428
| Mm_RefseqmRNA = NM_178616
| Mm_RefseqProtein = NP_848731
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 80244860
| Mm_GenLoc_end = 80287789
| Mm_Uniprot = Q3THG2
}}
}}
'''Proteasome (prosome, macropain) 26S subunit, non-ATPase, 11''', also known as '''PSMD11''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMD11 proteasome (prosome, macropain) 26S subunit, non-ATPase, 11| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5717| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a non-ATPase subunit of the 19S regulator.<ref name="entrez">{{cite web | title = Entrez Gene: PSMD11 proteasome (prosome, macropain) 26S subunit, non-ATPase, 11| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5717| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Coux O, Tanaka K, Goldberg AL |title=Structure and functions of the 20S and 26S proteasomes. |journal=Annu. Rev. Biochem. |volume=65 |issue= |pages= 801-47 |year= 1996 |pmid= 8811196 |doi= 10.1146/annurev.bi.65.070196.004101 }}
*{{cite journal | author=Goff SP |title=Death by deamination: a novel host restriction system for HIV-1. |journal=Cell |volume=114 |issue= 3 |pages= 281-3 |year= 2003 |pmid= 12914693 |doi= }}
*{{cite journal | author=Kanayama HO, Tamura T, Ugai S, ''et al.'' |title=Demonstration that a human 26S proteolytic complex consists of a proteasome and multiple associated protein components and hydrolyzes ATP and ubiquitin-ligated proteins by closely linked mechanisms. |journal=Eur. J. Biochem. |volume=206 |issue= 2 |pages= 567-78 |year= 1992 |pmid= 1317798 |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=Seeger M, Ferrell K, Frank R, Dubiel W |title=HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8145-8 |year= 1997 |pmid= 9079628 |doi= }}
*{{cite journal | author=Hoffman L, Rechsteiner M |title=Molecular cloning and expression of subunit 9 of the 26S proteasome. |journal=FEBS Lett. |volume=404 |issue= 2-3 |pages= 179-84 |year= 1997 |pmid= 9119060 |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=Saito A, Watanabe TK, Shimada Y, ''et al.'' |title=cDNA cloning and functional analysis of p44.5 and p55, two regulatory subunits of the 26S proteasome. |journal=Gene |volume=203 |issue= 2 |pages= 241-50 |year= 1998 |pmid= 9426256 |doi= }}
*{{cite journal | author=Madani N, Kabat D |title=An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. |journal=J. Virol. |volume=72 |issue= 12 |pages= 10251-5 |year= 1998 |pmid= 9811770 |doi= }}
*{{cite journal | author=Simon JH, Gaddis NC, Fouchier RA, Malim MH |title=Evidence for a newly discovered cellular anti-HIV-1 phenotype. |journal=Nat. Med. |volume=4 |issue= 12 |pages= 1397-400 |year= 1998 |pmid= 9846577 |doi= 10.1038/3987 }}
*{{cite journal | author=Mulder LC, Muesing MA |title=Degradation of HIV-1 integrase by the N-end rule pathway. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29749-53 |year= 2000 |pmid= 10893419 |doi= 10.1074/jbc.M004670200 }}
*{{cite journal | author=Sheehy AM, Gaddis NC, Choi JD, Malim MH |title=Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. |journal=Nature |volume=418 |issue= 6898 |pages= 646-50 |year= 2002 |pmid= 12167863 |doi= 10.1038/nature00939 }}
*{{cite journal | author=Fong A, Zhang M, Neely J, Sun SC |title=S9, a 19 S proteasome subunit interacting with ubiquitinated NF-kappaB2/p100. |journal=J. Biol. Chem. |volume=277 |issue= 43 |pages= 40697-702 |year= 2002 |pmid= 12185077 |doi= 10.1074/jbc.M205330200 }}
*{{cite journal | author=Huang X, Seifert U, Salzmann U, ''et al.'' |title=The RTP site shared by the HIV-1 Tat protein and the 11S regulator subunit alpha is crucial for their effects on proteasome function including antigen processing. |journal=J. Mol. Biol. |volume=323 |issue= 4 |pages= 771-82 |year= 2002 |pmid= 12419264 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=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 }}
*{{cite journal | author=Gaddis NC, Chertova E, Sheehy AM, ''et al.'' |title=Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions. |journal=J. Virol. |volume=77 |issue= 10 |pages= 5810-20 |year= 2003 |pmid= 12719574 |doi= }}
*{{cite journal | author=Lecossier D, Bouchonnet F, Clavel F, Hance AJ |title=Hypermutation of HIV-1 DNA in the absence of the Vif protein. |journal=Science |volume=300 |issue= 5622 |pages= 1112 |year= 2003 |pmid= 12750511 |doi= 10.1126/science.1083338 }}
*{{cite journal | author=Zhang H, Yang B, Pomerantz RJ, ''et al.'' |title=The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. |journal=Nature |volume=424 |issue= 6944 |pages= 94-8 |year= 2003 |pmid= 12808465 |doi= 10.1038/nature01707 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PTX3... {November 18, 2007 3:30:54 PM PST}
- SEARCH REDIRECT: Control Box Found: PTX3 {November 18, 2007 3:31:43 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 3:31:51 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 3:31:51 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 3:31:51 PM PST}
- UPDATED: Updated protein page: PTX3 {November 18, 2007 3:32:06 PM PST}
- INFO: Beginning work on PVR... {November 18, 2007 3:32:06 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 3:33:48 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_PVR_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dgi.
| PDB = {{PDB2|1dgi}}, {{PDB2|1nn8}}
| Name = Poliovirus receptor
| HGNCid = 9705
| Symbol = PVR
| AltSymbols =; CD155; HVED; NECL5; Necl-5; PVS; TAGE4
| OMIM = 173850
| ECnumber =
| Homologene = 9672
| MGIid =
| GeneAtlas_image1 = PBB_GE_PVR_214443_at_tn.png
| GeneAtlas_image2 = PBB_GE_PVR_212662_at_tn.png
| GeneAtlas_image3 = PBB_GE_PVR_214444_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0016337 |text = cell-cell adhesion}} {{GNF_GO|id=GO:0016477 |text = cell migration}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5817
| Hs_Ensembl = ENSG00000073008
| Hs_RefseqProtein = NP_006496
| Hs_RefseqmRNA = NM_006505
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 49839066
| Hs_GenLoc_end = 49858689
| Hs_Uniprot = P15151
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Poliovirus receptor''', also known as '''PVR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PVR poliovirus receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5817| 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=Zibert A, Wimmer E |title=N glycosylation of the virus binding domain is not essential for function of the human poliovirus receptor. |journal=J. Virol. |volume=66 |issue= 12 |pages= 7368-73 |year= 1992 |pmid= 1331527 |doi= }}
*{{cite journal | author=Schonk D, van Dijk P, Riegmann P, ''et al.'' |title=Assignment of seven genes to distinct intervals on the midportion of human chromosome 19q surrounding the myotonic dystrophy gene region. |journal=Cytogenet. Cell Genet. |volume=54 |issue= 1-2 |pages= 15-9 |year= 1991 |pmid= 1701111 |doi= }}
*{{cite journal | author=Koike S, Ise I, Nomoto A |title=Functional domains of the poliovirus receptor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 10 |pages= 4104-8 |year= 1991 |pmid= 1851992 |doi= }}
*{{cite journal | author=Koike S, Horie H, Ise I, ''et al.'' |title=The poliovirus receptor protein is produced both as membrane-bound and secreted forms. |journal=EMBO J. |volume=9 |issue= 10 |pages= 3217-24 |year= 1990 |pmid= 2170108 |doi= }}
*{{cite journal | author=Mendelsohn CL, Wimmer E, Racaniello VR |title=Cellular receptor for poliovirus: molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily. |journal=Cell |volume=56 |issue= 5 |pages= 855-65 |year= 1989 |pmid= 2538245 |doi= }}
*{{cite journal | author=Bernhardt G, Harber J, Zibert A, ''et al.'' |title=The poliovirus receptor: identification of domains and amino acid residues critical for virus binding. |journal=Virology |volume=203 |issue= 2 |pages= 344-56 |year= 1994 |pmid= 7914388 |doi= 10.1006/viro.1994.1493 }}
*{{cite journal | author=He Y, Bowman VD, Mueller S, ''et al.'' |title=Interaction of the poliovirus receptor with poliovirus. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 1 |pages= 79-84 |year= 2000 |pmid= 10618374 |doi= }}
*{{cite journal | author=Gromeier M, Lachmann S, Rosenfeld MR, ''et al.'' |title=Intergeneric poliovirus recombinants for the treatment of malignant glioma. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 12 |pages= 6803-8 |year= 2000 |pmid= 10841575 |doi= }}
*{{cite journal | author=Lange R, Peng X, Wimmer E, ''et al.'' |title=The poliovirus receptor CD155 mediates cell-to-matrix contacts by specifically binding to vitronectin. |journal=Virology |volume=285 |issue= 2 |pages= 218-27 |year= 2001 |pmid= 11437656 |doi= 10.1006/viro.2001.0943 }}
*{{cite journal | author=Ohka S, Ohno H, Tohyama K, Nomoto A |title=Basolateral sorting of human poliovirus receptor alpha involves an interaction with the mu1B subunit of the clathrin adaptor complex in polarized epithelial cells. |journal=Biochem. Biophys. Res. Commun. |volume=287 |issue= 4 |pages= 941-8 |year= 2001 |pmid= 11573956 |doi= 10.1006/bbrc.2001.5660 }}
*{{cite journal | author=Mueller S, Cao X, Welker R, Wimmer E |title=Interaction of the poliovirus receptor CD155 with the dynein light chain Tctex-1 and its implication for poliovirus pathogenesis. |journal=J. Biol. Chem. |volume=277 |issue= 10 |pages= 7897-904 |year= 2002 |pmid= 11751937 |doi= 10.1074/jbc.M111937200 }}
*{{cite journal | author=Solecki DJ, Gromeier M, Mueller S, ''et al.'' |title=Expression of the human poliovirus receptor/CD155 gene is activated by sonic hedgehog. |journal=J. Biol. Chem. |volume=277 |issue= 28 |pages= 25697-702 |year= 2002 |pmid= 11983699 |doi= 10.1074/jbc.M201378200 }}
*{{cite journal | author=Fabre S, Reymond N, Cocchi F, ''et al.'' |title=Prominent role of the Ig-like V domain in trans-interactions of nectins. Nectin3 and nectin 4 bind to the predicted C-C'-C"-D beta-strands of the nectin1 V domain. |journal=J. Biol. Chem. |volume=277 |issue= 30 |pages= 27006-13 |year= 2002 |pmid= 12011057 |doi= 10.1074/jbc.M203228200 }}
*{{cite journal | author=Iwasaki A, Welker R, Mueller S, ''et al.'' |title=Immunofluorescence analysis of poliovirus receptor expression in Peyer's patches of humans, primates, and CD155 transgenic mice: implications for poliovirus infection. |journal=J. Infect. Dis. |volume=186 |issue= 5 |pages= 585-92 |year= 2002 |pmid= 12195344 |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=He Y, Mueller S, Chipman PR, ''et al.'' |title=Complexes of poliovirus serotypes with their common cellular receptor, CD155. |journal=J. Virol. |volume=77 |issue= 8 |pages= 4827-35 |year= 2003 |pmid= 12663789 |doi= }}
*{{cite journal | author=Mueller S, Wimmer E |title=Recruitment of nectin-3 to cell-cell junctions through trans-heterophilic interaction with CD155, a vitronectin and poliovirus receptor that localizes to alpha(v)beta3 integrin-containing membrane microdomains. |journal=J. Biol. Chem. |volume=278 |issue= 33 |pages= 31251-60 |year= 2003 |pmid= 12759359 |doi= 10.1074/jbc.M304166200 }}
*{{cite journal | author=Bottino C, Castriconi R, Pende D, ''et al.'' |title=Identification of PVR (CD155) and Nectin-2 (CD112) as cell surface ligands for the human DNAM-1 (CD226) activating molecule. |journal=J. Exp. Med. |volume=198 |issue= 4 |pages= 557-67 |year= 2003 |pmid= 12913096 |doi= 10.1084/jem.20030788 }}
*{{cite journal | author=Baury B, Masson D, McDermott BM, ''et al.'' |title=Identification of secreted CD155 isoforms. |journal=Biochem. Biophys. Res. Commun. |volume=309 |issue= 1 |pages= 175-82 |year= 2003 |pmid= 12943679 |doi= }}
*{{cite journal | author=Ravens I, Seth S, Förster R, Bernhardt G |title=Characterization and identification of Tage4 as the murine orthologue of human poliovirus receptor/CD155. |journal=Biochem. Biophys. Res. Commun. |volume=312 |issue= 4 |pages= 1364-71 |year= 2004 |pmid= 14652024 |doi= }}
}}
{{refend}}
{{protein-stub}}
end log.
