Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 01:22, 17 November 2007 (UTC)
[edit]Proteins without matches (7)
[edit]Proteins with a High Potential Match (7)
[edit]Redirected Proteins (11)
[edit]Manual Inspection (Page not found) (14)
[edit]
Protein Status Grid - Date: 01:22, 17 November 2007 (UTC)
[edit]Vebose Log - Date: 01:22, 17 November 2007 (UTC)
[edit]- INFO: Beginning work on AHSG... {November 16, 2007 5:01:27 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 5:01:56 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Alpha-2-HS-glycoprotein
| HGNCid = 349
| Symbol = AHSG
| AltSymbols =; A2HS; AHS; FETUA; HSGA
| OMIM = 138680
| ECnumber =
| Homologene = 1225
| MGIid = 107189
| GeneAtlas_image1 = PBB_GE_AHSG_204551_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_AHSG_210929_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004869 |text = cysteine protease inhibitor activity}} {{GNF_GO|id=GO:0019210 |text = kinase inhibitor activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0001503 |text = ossification}} {{GNF_GO|id=GO:0006907 |text = pinocytosis}} {{GNF_GO|id=GO:0006953 |text = acute-phase response}} {{GNF_GO|id=GO:0030502 |text = negative regulation of bone mineralization}} {{GNF_GO|id=GO:0046627 |text = negative regulation of insulin receptor signaling pathway}} {{GNF_GO|id=GO:0050727 |text = regulation of inflammatory response}} {{GNF_GO|id=GO:0050766 |text = positive regulation of phagocytosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 197
| Hs_Ensembl = ENSG00000145192
| Hs_RefseqProtein = NP_001613
| Hs_RefseqmRNA = NM_001622
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 187813549
| Hs_GenLoc_end = 187821786
| Hs_Uniprot = P02765
| Mm_EntrezGene = 11625
| Mm_Ensembl = ENSMUSG00000022868
| Mm_RefseqmRNA = NM_013465
| Mm_RefseqProtein = NP_038493
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 22807376
| Mm_GenLoc_end = 22814772
| Mm_Uniprot = O35399
}}
}}
'''Alpha-2-HS-glycoprotein''', also known as '''AHSG''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AHSG alpha-2-HS-glycoprotein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=197| 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 = Alpha2-HS glycoprotein (AHSG), a glycoprotein present in the serum, is synthesized by hepatocytes. The AHSG molecule consists of two polypeptide chains, which are both cleaved from a proprotein encoded from a single mRNA. It is involved in several functions, such as endocytosis, brain development and the formation of bone tissue. The protein is commonly present in the cortical plate of the immature cerebral cortex and bone marrow hemopoietic matrix, and it has therefore been postulated that it participates in the development of the tissues. However, its exact significance is still obscure.<ref name="entrez">{{cite web | title = Entrez Gene: AHSG alpha-2-HS-glycoprotein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=197| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ketteler M, Vermeer C, Wanner C, ''et al.'' |title=Novel insights into uremic vascular calcification: role of matrix Gla protein and alpha-2-Heremans Schmid glycoprotein/fetuin. |journal=Blood Purif. |volume=20 |issue= 5 |pages= 473-6 |year= 2003 |pmid= 12207096 |doi= }}
*{{cite journal | author=Ketteler M |title=Fetuin-A and extraosseous calcification in uremia. |journal=Curr. Opin. Nephrol. Hypertens. |volume=14 |issue= 4 |pages= 337-42 |year= 2005 |pmid= 15931001 |doi= }}
*{{cite journal | author=Yang F, Schwartz Z, Swain LD, ''et al.'' |title=Alpha 2-HS-glycoprotein: expression in chondrocytes and augmentation of alkaline phosphatase and phospholipase A2 activity. |journal=Bone |volume=12 |issue= 1 |pages= 7-15 |year= 1991 |pmid= 2054237 |doi= }}
*{{cite journal | author=Araki T, Yoshioka Y, Schmid K |title=The position of the disulfide bonds in human plasma alpha 2 HS-glycoprotein and the repeating double disulfide bonds in the domain structure. |journal=Biochim. Biophys. Acta |volume=994 |issue= 3 |pages= 195-9 |year= 1989 |pmid= 2645941 |doi= }}
*{{cite journal | author=Kellermann J, Haupt H, Auerswald EA, Müller-Ester W |title=The arrangement of disulfide loops in human alpha 2-HS glycoprotein. Similarity to the disulfide bridge structures of cystatins and kininogens. |journal=J. Biol. Chem. |volume=264 |issue= 24 |pages= 14121-8 |year= 1989 |pmid= 2760061 |doi= }}
*{{cite journal | author=Magnuson VL, McCombs JL, Lee CC, ''et al.'' |title=Human alpha 2-HS-glycoprotein localized to 3q27----q29 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=47 |issue= 1-2 |pages= 72-4 |year= 1988 |pmid= 3356172 |doi= }}
*{{cite journal | author=Lee CC, Bowman BH, Yang FM |title=Human alpha 2-HS-glycoprotein: the A and B chains with a connecting sequence are encoded by a single mRNA transcript. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 13 |pages= 4403-7 |year= 1987 |pmid= 3474608 |doi= }}
*{{cite journal | author=Keeley FW, Sitarz EE |title=Identification and quantitation of alpha 2-HS-glycoprotein in the mineralized matrix of calcified plaques of atherosclerotic human aorta. |journal=Atherosclerosis |volume=55 |issue= 1 |pages= 63-9 |year= 1985 |pmid= 3924066 |doi= }}
*{{cite journal | author=Yoshioka Y, Gejyo F, Marti T, ''et al.'' |title=The complete amino acid sequence of the A-chain of human plasma alpha 2HS-glycoprotein. |journal=J. Biol. Chem. |volume=261 |issue= 4 |pages= 1665-76 |year= 1986 |pmid= 3944104 |doi= }}
*{{cite journal | author=Matsushima K, Cheng M, Migita S |title=Purification and physicochemical characterization of human alpha 2-HS-glycoprotein. |journal=Biochim. Biophys. Acta |volume=701 |issue= 2 |pages= 200-5 |year= 1982 |pmid= 6803836 |doi= }}
*{{cite journal | author=Gejyo F, Chang JL, Bürgi W, ''et al.'' |title=Characterization of the B-chain of human plasma alpha 2HS-glycoprotein. The complete amino acid sequence and primary structure of its heteroglycan. |journal=J. Biol. Chem. |volume=258 |issue= 8 |pages= 4966-71 |year= 1983 |pmid= 6833285 |doi= }}
*{{cite journal | author=Rizzu P, Baldini A |title=Three members of the human cystatin gene superfamily, AHSG, HRG, and KNG, map within one megabase of genomic DNA at 3q27. |journal=Cytogenet. Cell Genet. |volume=70 |issue= 1-2 |pages= 26-8 |year= 1995 |pmid= 7736783 |doi= }}
*{{cite journal | author=Srinivas PR, Wagner AS, Reddy LV, ''et al.'' |title=Serum alpha 2-HS-glycoprotein is an inhibitor of the human insulin receptor at the tyrosine kinase level. |journal=Mol. Endocrinol. |volume=7 |issue= 11 |pages= 1445-55 |year= 1994 |pmid= 7906861 |doi= }}
*{{cite journal | author=Nawratil P, Lenzen S, Kellermann J, ''et al.'' |title=Limited proteolysis of human alpha2-HS glycoprotein/fetuin. Evidence that a chymotryptic activity can release the connecting peptide. |journal=J. Biol. Chem. |volume=271 |issue= 49 |pages= 31735-41 |year= 1997 |pmid= 8940198 |doi= }}
*{{cite journal | author=Osawa M, Umetsu K, Ohki T, ''et al.'' |title=Molecular evidence for human alpha 2-HS glycoprotein (AHSG) polymorphism. |journal=Hum. Genet. |volume=99 |issue= 1 |pages= 18-21 |year= 1997 |pmid= 9003486 |doi= }}
*{{cite journal | author=Osawa M, Umetsu K, Sato M, ''et al.'' |title=Structure of the gene encoding human alpha 2-HS glycoprotein (AHSG). |journal=Gene |volume=196 |issue= 1-2 |pages= 121-5 |year= 1997 |pmid= 9322749 |doi= }}
*{{cite journal | author=Umekawa T, Iguchi M, Konya E, ''et al.'' |title=Localization and inhibitory activity of alpha(2)HS-glycoprotein in the kidney. |journal=Urol. Res. |volume=27 |issue= 5 |pages= 315-8 |year= 2000 |pmid= 10550518 |doi= }}
*{{cite journal | author=Olivier E, Soury E, Ruminy P, ''et al.'' |title=Fetuin-B, a second member of the fetuin family in mammals. |journal=Biochem. J. |volume=350 Pt 2 |issue= |pages= 589-97 |year= 2001 |pmid= 10947975 |doi= }}
*{{cite journal | author=Osawa M, Yuasa I, Kitano T, ''et al.'' |title=Haplotype analysis of the human alpha2-HS glycoprotein (fetuin) gene. |journal=Ann. Hum. Genet. |volume=65 |issue= Pt 1 |pages= 27-34 |year= 2001 |pmid= 11415520 |doi= }}
*{{cite journal | author=Haglund AC, Ek B, Ek P |title=Phosphorylation of human plasma alpha2-Heremans-Schmid glycoprotein (human fetuin) in vivo. |journal=Biochem. J. |volume=357 |issue= Pt 2 |pages= 437-45 |year= 2001 |pmid= 11439093 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on APOC2... {November 16, 2007 5:01:56 PM PST}
- SEARCH REDIRECT: Control Box Found: APOC2 {November 16, 2007 5:02:15 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 5:02:16 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 5:02:16 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 5:02:16 PM PST}
- UPDATED: Updated protein page: APOC2 {November 16, 2007 5:02:23 PM PST}
- INFO: Beginning work on BMI1... {November 16, 2007 5:02:23 PM PST}
- SEARCH REDIRECT: Control Box Found: BMI1 {November 16, 2007 5:02:51 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 5:02:52 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 5:02:52 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 5:02:52 PM PST}
- UPDATED: Updated protein page: BMI1 {November 16, 2007 5:02:58 PM PST}
- INFO: Beginning work on CD79A... {November 16, 2007 5:02:58 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 5:03:25 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
}}
<!-- 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 = CD79a molecule, immunoglobulin-associated alpha
| HGNCid = 1698
| Symbol = CD79A
| AltSymbols =; IGA; MB-1
| OMIM = 112205
| ECnumber =
| Homologene = 31053
| MGIid = 101774
| GeneAtlas_image1 = PBB_GE_CD79A_205049_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004888 |text = transmembrane receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005771 |text = multivesicular body}} {{GNF_GO|id=GO:0009897 |text = external side of plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0019815 |text = B cell receptor complex}}
| Process = {{GNF_GO|id=GO:0006952 |text = defense response}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0050853 |text = B cell receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 973
| Hs_Ensembl = ENSG00000105369
| Hs_RefseqProtein = NP_001774
| Hs_RefseqmRNA = NM_001783
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 47073030
| Hs_GenLoc_end = 47077275
| Hs_Uniprot = P11912
| Mm_EntrezGene = 12518
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_989437
| Mm_RefseqProtein = XP_994531
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''CD79a molecule, immunoglobulin-associated alpha''', also known as '''CD79A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CD79A CD79a molecule, immunoglobulin-associated alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=973| 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 B lymphocyte antigen receptor is a multimeric complex that includes the antigen-specific component, surface immunoglobulin (Ig). Surface Ig non-covalently associates with two other proteins, Ig-alpha and Ig-beta, which are necessary for expression and function of the B-cell antigen receptor. This gene encodes the Ig-alpha protein of the B-cell antigen component. Alternatively spliced transcript variants encoding different isoforms have been described.<ref name="entrez">{{cite web | title = Entrez Gene: CD79A CD79a molecule, immunoglobulin-associated alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=973| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Reth M |title=Antigen receptors on B lymphocytes. |journal=Annu. Rev. Immunol. |volume=10 |issue= |pages= 97-121 |year= 1992 |pmid= 1591006 |doi= 10.1146/annurev.iy.10.040192.000525 }}
*{{cite journal | author=Herren B, Burrows PD |title=B cell-restricted human mb-1 gene: expression, function, and lineage infidelity. |journal=Immunol. Res. |volume=26 |issue= 1-3 |pages= 35-43 |year= 2003 |pmid= 12403343 |doi= }}
*{{cite journal | author=Bastian A, Kratzin H, Eckart K, Hilschmann N |title=Intra- and interchain disulfide bridges of the human J chain in secretory immunoglobulin A. |journal=Biol. Chem. Hoppe-Seyler |volume=373 |issue= 12 |pages= 1255-63 |year= 1993 |pmid= 1292512 |doi= }}
*{{cite journal | author=Leduc I, Preud'homme JL, Cogné M |title=Structure and expression of the mb-1 transcript in human lymphoid cells. |journal=Clin. Exp. Immunol. |volume=90 |issue= 1 |pages= 141-6 |year= 1992 |pmid= 1395095 |doi= }}
*{{cite journal | author=Kristensen T, Lopez R, Prydz H |title=An estimate of the sequencing error frequency in the DNA sequence databases. |journal=DNA Seq. |volume=2 |issue= 6 |pages= 343-6 |year= 1992 |pmid= 1446073 |doi= }}
*{{cite journal | author=Müller B, Cooper L, Terhorst C |title=Cloning and sequencing of the cDNA encoding the human homologue of the murine immunoglobulin-associated protein B29. |journal=Eur. J. Immunol. |volume=22 |issue= 6 |pages= 1621-5 |year= 1992 |pmid= 1534761 |doi= }}
*{{cite journal | author=Ha HJ, Kubagawa H, Burrows PD |title=Molecular cloning and expression pattern of a human gene homologous to the murine mb-1 gene. |journal=J. Immunol. |volume=148 |issue= 5 |pages= 1526-31 |year= 1992 |pmid= 1538135 |doi= }}
*{{cite journal | author=Hutchcroft JE, Harrison ML, Geahlen RL |title=Association of the 72-kDa protein-tyrosine kinase PTK72 with the B cell antigen receptor. |journal=J. Biol. Chem. |volume=267 |issue= 12 |pages= 8613-9 |year= 1992 |pmid= 1569106 |doi= }}
*{{cite journal | author=Flaswinkel H, Reth M |title=Molecular cloning of the Ig-alpha subunit of the human B-cell antigen receptor complex. |journal=Immunogenetics |volume=36 |issue= 4 |pages= 266-9 |year= 1992 |pmid= 1639443 |doi= }}
*{{cite journal | author=Yu LM, Chang TW |title=Human mb-1 gene: complete cDNA sequence and its expression in B cells bearing membrane Ig of various isotypes. |journal=J. Immunol. |volume=148 |issue= 2 |pages= 633-7 |year= 1992 |pmid= 1729378 |doi= }}
*{{cite journal | author=Venkitaraman AR, Williams GT, Dariavach P, Neuberger MS |title=The B-cell antigen receptor of the five immunoglobulin classes. |journal=Nature |volume=352 |issue= 6338 |pages= 777-81 |year= 1991 |pmid= 1881434 |doi= 10.1038/352777a0 }}
*{{cite journal | author=Bakos MA, Kurosky A, Goldblum RM |title=Characterization of a critical binding site for human polymeric Ig on secretory component. |journal=J. Immunol. |volume=147 |issue= 10 |pages= 3419-26 |year= 1991 |pmid= 1940346 |doi= }}
*{{cite journal | author=Sakaguchi N, Kashiwamura S, Kimoto M, ''et al.'' |title=B lymphocyte lineage-restricted expression of mb-1, a gene with CD3-like structural properties. |journal=EMBO J. |volume=7 |issue= 11 |pages= 3457-64 |year= 1989 |pmid= 2463161 |doi= }}
*{{cite journal | author=Grubb AO, López C, Tejler L, Mendez E |title=Isolation of human complex-forming glycoprotein, heterogeneous in charge (protein HC), and its IgA complex from plasma. Physiochemical and immunochemical properties, normal plasma concentration. |journal=J. Biol. Chem. |volume=258 |issue= 23 |pages= 14698-707 |year= 1984 |pmid= 6196366 |doi= }}
*{{cite journal | author=Kurosaki T, Johnson SA, Pao L, ''et al.'' |title=Role of the Syk autophosphorylation site and SH2 domains in B cell antigen receptor signaling. |journal=J. Exp. Med. |volume=182 |issue= 6 |pages= 1815-23 |year= 1996 |pmid= 7500027 |doi= }}
*{{cite journal | author=Lankester AC, van Schijndel GM, Cordell JL, ''et al.'' |title=CD5 is associated with the human B cell antigen receptor complex. |journal=Eur. J. Immunol. |volume=24 |issue= 4 |pages= 812-6 |year= 1994 |pmid= 7512031 |doi= }}
*{{cite journal | author=Vasile S, Coligan JE, Yoshida M, Seon BK |title=Isolation and chemical characterization of the human B29 and mb-1 proteins of the B cell antigen receptor complex. |journal=Mol. Immunol. |volume=31 |issue= 6 |pages= 419-27 |year= 1994 |pmid= 7514267 |doi= }}
*{{cite journal | author=Brown VK, Ogle EW, Burkhardt AL, ''et al.'' |title=Multiple components of the B cell antigen receptor complex associate with the protein tyrosine phosphatase, CD45. |journal=J. Biol. Chem. |volume=269 |issue= 25 |pages= 17238-44 |year= 1994 |pmid= 7516335 |doi= }}
*{{cite journal | author=Pani G, Kozlowski M, Cambier JC, ''et al.'' |title=Identification of the tyrosine phosphatase PTP1C as a B cell antigen receptor-associated protein involved in the regulation of B cell signaling. |journal=J. Exp. Med. |volume=181 |issue= 6 |pages= 2077-84 |year= 1995 |pmid= 7539038 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CLN3... {November 16, 2007 5:03:25 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 5:04:17 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 = Ceroid-lipofuscinosis, neuronal 3, juvenile (Batten, Spielmeyer-Vogt disease)
| HGNCid = 2074
| Symbol = CLN3
| AltSymbols =; BTS; MGC102840
| OMIM = 607042
| ECnumber =
| Homologene = 37259
| MGIid = 107537
| GeneAtlas_image1 = PBB_GE_CLN3_209275_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CLN3_210859_x_at_tn.png
| Function = {{GNF_GO|id=GO:0051082 |text = unfolded protein binding}}
| Component = {{GNF_GO|id=GO:0000139 |text = Golgi membrane}} {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0005769 |text = early endosome}} {{GNF_GO|id=GO:0005770 |text = late endosome}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0005795 |text = Golgi stack}} {{GNF_GO|id=GO:0005802 |text = trans-Golgi network}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005901 |text = caveola}} {{GNF_GO|id=GO:0008021 |text = synaptic vesicle}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0030176 |text = integral to endoplasmic reticulum membrane}} {{GNF_GO|id=GO:0043005 |text = neuron projection}} {{GNF_GO|id=GO:0045121 |text = lipid raft}}
| Process = {{GNF_GO|id=GO:0001508 |text = regulation of action potential}} {{GNF_GO|id=GO:0001575 |text = globoside metabolic process}} {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0006520 |text = amino acid metabolic process}} {{GNF_GO|id=GO:0006678 |text = glucosylceramide metabolic process}} {{GNF_GO|id=GO:0006681 |text = galactosylceramide metabolic process}} {{GNF_GO|id=GO:0006684 |text = sphingomyelin metabolic process}} {{GNF_GO|id=GO:0006865 |text = amino acid transport}} {{GNF_GO|id=GO:0006898 |text = receptor-mediated endocytosis}} {{GNF_GO|id=GO:0007042 |text = lysosomal lumen acidification}} {{GNF_GO|id=GO:0008306 |text = associative learning}} {{GNF_GO|id=GO:0015809 |text = arginine transport}} {{GNF_GO|id=GO:0016044 |text = membrane organization and biogenesis}} {{GNF_GO|id=GO:0016236 |text = macroautophagy}} {{GNF_GO|id=GO:0016485 |text = protein processing}} {{GNF_GO|id=GO:0030163 |text = protein catabolic process}} {{GNF_GO|id=GO:0035235 |text = ionotropic glutamate receptor signaling pathway}} {{GNF_GO|id=GO:0042133 |text = neurotransmitter metabolic process}} {{GNF_GO|id=GO:0042987 |text = amyloid precursor protein catabolic process}} {{GNF_GO|id=GO:0043066 |text = negative regulation of apoptosis}} {{GNF_GO|id=GO:0045861 |text = negative regulation of proteolysis}} {{GNF_GO|id=GO:0050885 |text = regulation of balance}} {{GNF_GO|id=GO:0051453 |text = regulation of cellular pH}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1201
| Hs_Ensembl = ENSG00000188603
| Hs_RefseqProtein = NP_000077
| Hs_RefseqmRNA = NM_000086
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 28396102
| Hs_GenLoc_end = 28413398
| Hs_Uniprot = Q13286
| Mm_EntrezGene = 12752
| Mm_Ensembl = ENSMUSG00000030720
| Mm_RefseqmRNA = XM_993441
| Mm_RefseqProtein = XP_998535
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 126362548
| Mm_GenLoc_end = 126374526
| Mm_Uniprot = O35934
}}
}}
'''Ceroid-lipofuscinosis, neuronal 3, juvenile (Batten, Spielmeyer-Vogt disease)''', also known as '''CLN3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CLN3 ceroid-lipofuscinosis, neuronal 3, juvenile (Batten, Spielmeyer-Vogt disease)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1201| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a protein that is involved in lysosomal function. Mutations in this, as well as other neuronal ceroid-lipofuscinosis (CLN) genes, cause neurodegenerative diseases commonly known as Batten disease or collectively known as neuronal ceroid lipofuscinoses (NCLs). Many alternatively spliced transcript variants have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: CLN3 ceroid-lipofuscinosis, neuronal 3, juvenile (Batten, Spielmeyer-Vogt disease)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1201| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Dawson G, Cho S |title=Batten's disease: clues to neuronal protein catabolism in lysosomes. |journal=J. Neurosci. Res. |volume=60 |issue= 2 |pages= 133-40 |year= 2000 |pmid= 10740217 |doi= }}
*{{cite journal | author=Vesa J, Peltonen L |title=Mutated genes in juvenile and variant late infantile neuronal ceroid lipofuscinoses encode lysosomal proteins. |journal=Curr. Mol. Med. |volume=2 |issue= 5 |pages= 439-44 |year= 2003 |pmid= 12125809 |doi= }}
*{{cite journal | author=Phillips SN, Benedict JW, Weimer JM, Pearce DA |title=CLN3, the protein associated with batten disease: structure, function and localization. |journal=J. Neurosci. Res. |volume=79 |issue= 5 |pages= 573-83 |year= 2005 |pmid= 15657902 |doi= 10.1002/jnr.20367 }}
*{{cite journal | author= |title=Isolation of a novel gene underlying Batten disease, CLN3. The International Batten Disease Consortium. |journal=Cell |volume=82 |issue= 6 |pages= 949-57 |year= 1995 |pmid= 7553855 |doi= }}
*{{cite journal | author=Taschner PE, de Vos N, Thompson AD, ''et al.'' |title=Chromosome 16 microdeletion in a patient with juvenile neuronal ceroid lipofuscinosis (Batten disease). |journal=Am. J. Hum. Genet. |volume=56 |issue= 3 |pages= 663-8 |year= 1995 |pmid= 7887420 |doi= }}
*{{cite journal | author=Janes RW, Munroe PB, Mitchison HM, ''et al.'' |title=A model for Batten disease protein CLN3: functional implications from homology and mutations. |journal=FEBS Lett. |volume=399 |issue= 1-2 |pages= 75-7 |year= 1997 |pmid= 8980123 |doi= }}
*{{cite journal | author=Järvelä I, Mitchison HM, Munroe PB, ''et al.'' |title=Rapid diagnostic test for the major mutation underlying Batten disease. |journal=J. Med. Genet. |volume=33 |issue= 12 |pages= 1041-2 |year= 1997 |pmid= 9004140 |doi= }}
*{{cite journal | author=Mitchison HM, Munroe PB, O'Rawe AM, ''et al.'' |title=Genomic structure and complete nucleotide sequence of the Batten disease gene, CLN3. |journal=Genomics |volume=40 |issue= 2 |pages= 346-50 |year= 1997 |pmid= 9119403 |doi= 10.1006/geno.1996.4576 }}
*{{cite journal | author=Munroe PB, Mitchison HM, O'Rawe AM, ''et al.'' |title=Spectrum of mutations in the Batten disease gene, CLN3. |journal=Am. J. Hum. Genet. |volume=61 |issue= 2 |pages= 310-6 |year= 1997 |pmid= 9311735 |doi= }}
*{{cite journal | author=Järvelä I, Sainio M, Rantamäki T, ''et al.'' |title=Biosynthesis and intracellular targeting of the CLN3 protein defective in Batten disease. |journal=Hum. Mol. Genet. |volume=7 |issue= 1 |pages= 85-90 |year= 1998 |pmid= 9384607 |doi= }}
*{{cite journal | author=Wisniewski KE, Zhong N, Kaczmarski W, ''et al.'' |title=Compound heterozygous genotype is associated with protracted juvenile neuronal ceroid lipofuscinosis. |journal=Ann. Neurol. |volume=43 |issue= 1 |pages= 106-10 |year= 1998 |pmid= 9450775 |doi= 10.1002/ana.410430118 }}
*{{cite journal | author=Zhong N, Wisniewski KE, Kaczmarski AL, ''et al.'' |title=Molecular screening of Batten disease: identification of a missense mutation (E295K) in the CLN3 gene. |journal=Hum. Genet. |volume=102 |issue= 1 |pages= 57-62 |year= 1998 |pmid= 9490299 |doi= }}
*{{cite journal | author=Kremmidiotis G, Lensink IL, Bilton RL, ''et al.'' |title=The Batten disease gene product (CLN3p) is a Golgi integral membrane protein. |journal=Hum. Mol. Genet. |volume=8 |issue= 3 |pages= 523-31 |year= 1999 |pmid= 9949212 |doi= }}
*{{cite journal | author=Haskell RE, Derksen TA, Davidson BL |title=Intracellular trafficking of the JNCL protein CLN3. |journal=Mol. Genet. Metab. |volume=66 |issue= 4 |pages= 253-60 |year= 1999 |pmid= 10191111 |doi= 10.1006/mgme.1999.2802 }}
*{{cite journal | author=Kaczmarski W, Wisniewski KE, Golabek A, ''et al.'' |title=Studies of membrane association of CLN3 protein. |journal=Mol. Genet. Metab. |volume=66 |issue= 4 |pages= 261-4 |year= 1999 |pmid= 10191112 |doi= 10.1006/mgme.1999.2833 }}
*{{cite journal | author=Golabek AA, Kaczmarski W, Kida E, ''et al.'' |title=Expression studies of CLN3 protein (battenin) in fusion with the green fluorescent protein in mammalian cells in vitro. |journal=Mol. Genet. Metab. |volume=66 |issue= 4 |pages= 277-82 |year= 1999 |pmid= 10191115 |doi= 10.1006/mgme.1999.2836 }}
*{{cite journal | author=Margraf LR, Boriack RL, Routheut AA, ''et al.'' |title=Tissue expression and subcellular localization of CLN3, the Batten disease protein. |journal=Mol. Genet. Metab. |volume=66 |issue= 4 |pages= 283-9 |year= 1999 |pmid= 10191116 |doi= 10.1006/mgme.1999.2830 }}
*{{cite journal | author=Järvelä I, Lehtovirta M, Tikkanen R, ''et al.'' |title=Defective intracellular transport of CLN3 is the molecular basis of Batten disease (JNCL) |journal=Hum. Mol. Genet. |volume=8 |issue= 6 |pages= 1091-8 |year= 1999 |pmid= 10332042 |doi= }}
*{{cite journal | author=Loftus BJ, Kim UJ, Sneddon VP, ''et al.'' |title=Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q. |journal=Genomics |volume=60 |issue= 3 |pages= 295-308 |year= 1999 |pmid= 10493829 |doi= 10.1006/geno.1999.5927 }}
*{{cite journal | author=Pane MA, Puranam KL, Boustany RM |title=Expression of cln3 in human NT2 neuronal precursor cells and neonatal rat brain. |journal=Pediatr. Res. |volume=46 |issue= 4 |pages= 367-74 |year= 2004 |pmid= 10509355 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CREM... {November 16, 2007 5:04:17 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 5:05:03 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
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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_CREM_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dh3.
| PDB = {{PDB2|1dh3}}
| Name = CAMP responsive element modulator
| HGNCid = 2352
| Symbol = CREM
| AltSymbols =; ICER; MGC111110; MGC17881; MGC41893; hCREM-2
| OMIM = 123812
| ECnumber =
| Homologene = 84591
| MGIid =
| GeneAtlas_image1 = PBB_GE_CREM_207630_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CREM_209967_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_CREM_210171_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008140 |text = cAMP response element binding protein binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046983 |text = protein dimerization activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1390
| Hs_Ensembl = ENSG00000095794
| Hs_RefseqProtein = NP_001872
| Hs_RefseqmRNA = NM_001881
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 35455807
| Hs_GenLoc_end = 35541892
| Hs_Uniprot = Q03060
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''CAMP responsive element modulator''', also known as '''CREM''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CREM cAMP responsive element modulator| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1390| 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 bZIP transcription factor that binds to the cAMP responsive element found in many viral and cellular promoters. It is an important component of cAMP-mediated signal transduction during the spermatogenetic cycle, as well as other complex processes. Alternative promoter and translation initiation site usage allows this gene to exert spatial and temporal specificity to cAMP responsiveness. Multiple alternatively spliced transcript variants encoding several different isoforms have been found for this gene, with some of them functioning as activators and some as repressors of transcription.<ref name="entrez">{{cite web | title = Entrez Gene: CREM cAMP responsive element modulator| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1390| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Don J, Stelzer G |title=The expanding family of CREB/CREM transcription factors that are involved with spermatogenesis. |journal=Mol. Cell. Endocrinol. |volume=187 |issue= 1-2 |pages= 115-24 |year= 2003 |pmid= 11988318 |doi= }}
*{{cite journal | author=Yan C, Miller CL, Abe J |title=Regulation of phosphodiesterase 3 and inducible cAMP early repressor in the heart. |journal=Circ. Res. |volume=100 |issue= 4 |pages= 489-501 |year= 2007 |pmid= 17332439 |doi= 10.1161/01.RES.0000258451.44949.d7 }}
*{{cite journal | author=Meyer TE, Habener JF |title=Cyclic AMP response element binding protein CREB and modulator protein CREM are products of distinct genes. |journal=Nucleic Acids Res. |volume=20 |issue= 22 |pages= 6106 |year= 1993 |pmid= 1461747 |doi= }}
*{{cite journal | author=Pongubala JM, Atchison ML |title=Activating transcription factor 1 and cyclic AMP response element modulator can modulate the activity of the immunoglobulin kappa 3' enhancer. |journal=J. Biol. Chem. |volume=270 |issue= 17 |pages= 10304-13 |year= 1995 |pmid= 7730336 |doi= }}
*{{cite journal | author=Walker WH, Sanborn BM, Habener JF |title=An isoform of transcription factor CREM expressed during spermatogenesis lacks the phosphorylation domain and represses cAMP-induced transcription. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 26 |pages= 12423-7 |year= 1995 |pmid= 7809053 |doi= }}
*{{cite journal | author=Masquilier D, Foulkes NS, Mattei MG, Sassone-Corsi P |title=Human CREM gene: evolutionary conservation, chromosomal localization, and inducibility of the transcript. |journal=Cell Growth Differ. |volume=4 |issue= 11 |pages= 931-7 |year= 1994 |pmid= 7916662 |doi= }}
*{{cite journal | author=Fujimoto T, Fujisawa J, Yoshida M |title=Novel isoforms of human cyclic AMP-responsive element modulator (hCREM) mRNA. |journal=J. Biochem. |volume=115 |issue= 2 |pages= 298-303 |year= 1994 |pmid= 8206879 |doi= }}
*{{cite journal | author=de Groot RP, den Hertog J, Vandenheede JR, ''et al.'' |title=Multiple and cooperative phosphorylation events regulate the CREM activator function. |journal=EMBO J. |volume=12 |issue= 10 |pages= 3903-11 |year= 1993 |pmid= 8404858 |doi= }}
*{{cite journal | author=Bodor J, Walker W, Flemington E, ''et al.'' |title=Modulation of Tax and PKA-mediated expression of HTLV-I promoter via cAMP response element binding and modulator proteins CREB and CREM. |journal=FEBS Lett. |volume=377 |issue= 3 |pages= 413-8 |year= 1996 |pmid= 8549766 |doi= 10.1016/0014-5793(95)01299-0 }}
*{{cite journal | author=Nantel F, Monaco L, Foulkes NS, ''et al.'' |title=Spermiogenesis deficiency and germ-cell apoptosis in CREM-mutant mice. |journal=Nature |volume=380 |issue= 6570 |pages= 159-62 |year= 1996 |pmid= 8600390 |doi= 10.1038/380159a0 }}
*{{cite journal | author=Blendy JA, Kaestner KH, Weinbauer GF, ''et al.'' |title=Severe impairment of spermatogenesis in mice lacking the CREM gene. |journal=Nature |volume=380 |issue= 6570 |pages= 162-5 |year= 1996 |pmid= 8600391 |doi= 10.1038/380162a0 }}
*{{cite journal | author=Bodor J, Spetz AL, Strominger JL, Habener JF |title=cAMP inducibility of transcriptional repressor ICER in developing and mature human T lymphocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 8 |pages= 3536-41 |year= 1996 |pmid= 8622971 |doi= }}
*{{cite journal | author=Gellersen B, Kempf R, Telgmann R |title=Human endometrial stromal cells express novel isoforms of the transcriptional modulator CREM and up-regulate ICER in the course of decidualization. |journal=Mol. Endocrinol. |volume=11 |issue= 1 |pages= 97-113 |year= 1997 |pmid= 8994192 |doi= }}
*{{cite journal | author=Laurance ME, Kwok RP, Huang MS, ''et al.'' |title=Differential activation of viral and cellular promoters by human T-cell lymphotropic virus-1 tax and cAMP-responsive element modulator isoforms. |journal=J. Biol. Chem. |volume=272 |issue= 5 |pages= 2646-51 |year= 1997 |pmid= 9006899 |doi= }}
*{{cite journal | author=Bonny C, Cooker LA, Goldberg E |title=Deoxyribonucleic acid-protein interactions and expression of the human testis-specific lactate dehydrogenase promoter: transcription factor Sp1 plays a major role. |journal=Biol. Reprod. |volume=58 |issue= 3 |pages= 754-9 |year= 1998 |pmid= 9510963 |doi= }}
*{{cite journal | author=Müller FU, Bokník P, Knapp J, ''et al.'' |title=Identification and expression of a novel isoform of cAMP response element modulator in the human heart. |journal=FASEB J. |volume=12 |issue= 12 |pages= 1191-9 |year= 1998 |pmid= 9737722 |doi= }}
*{{cite journal | author=Fimia GM, De Cesare D, Sassone-Corsi P |title=CBP-independent activation of CREM and CREB by the LIM-only protein ACT. |journal=Nature |volume=398 |issue= 6723 |pages= 165-9 |year= 1999 |pmid= 10086359 |doi= 10.1038/18237 }}
*{{cite journal | author=Pati D, Meistrich ML, Plon SE |title=Human Cdc34 and Rad6B ubiquitin-conjugating enzymes target repressors of cyclic AMP-induced transcription for proteolysis. |journal=Mol. Cell. Biol. |volume=19 |issue= 7 |pages= 5001-13 |year= 1999 |pmid= 10373550 |doi= }}
*{{cite journal | author=Inada A, Someya Y, Yamada Y, ''et al.'' |title=The cyclic AMP response element modulator family regulates the insulin gene transcription by interacting with transcription factor IID. |journal=J. Biol. Chem. |volume=274 |issue= 30 |pages= 21095-103 |year= 1999 |pmid= 10409662 |doi= }}
*{{cite journal | author=Zauli G, Secchiero P, Rodella L, ''et al.'' |title=HIV-1 Tat-mediated inhibition of the tyrosine hydroxylase gene expression in dopaminergic neuronal cells. |journal=J. Biol. Chem. |volume=275 |issue= 6 |pages= 4159-65 |year= 2000 |pmid= 10660577 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on EPS15... {November 16, 2007 5:05:03 PM PST}
- SEARCH REDIRECT: Control Box Found: EPS15 {November 16, 2007 5:05:32 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 5:05:34 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 5:05:34 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 5:05:34 PM PST}
- UPDATED: Updated protein page: EPS15 {November 16, 2007 5:05:40 PM PST}
- INFO: Beginning work on F12... {November 16, 2007 5:05:40 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 5:06:03 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Coagulation factor XII (Hageman factor)
| HGNCid = 3530
| Symbol = F12
| AltSymbols =; HAF
| OMIM = 234000
| ECnumber =
| Homologene = 425
| MGIid = 1891012
| GeneAtlas_image1 = PBB_GE_F12_205774_at_tn.png
| Function = {{GNF_GO|id=GO:0003805 |text = coagulation factor XIa activity}} {{GNF_GO|id=GO:0003806 |text = coagulation factor XIIa activity}} {{GNF_GO|id=GO:0004252 |text = serine-type endopeptidase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}} {{GNF_GO|id=GO:0042730 |text = fibrinolysis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2161
| Hs_Ensembl = ENSG00000131187
| Hs_RefseqProtein = NP_000496
| Hs_RefseqmRNA = NM_000505
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 176761747
| Hs_GenLoc_end = 176769183
| Hs_Uniprot = P00748
| Mm_EntrezGene = 58992
| Mm_Ensembl = ENSMUSG00000021492
| Mm_RefseqmRNA = NM_021489
| Mm_RefseqProtein = NP_067464
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 55427588
| Mm_GenLoc_end = 55436415
| Mm_Uniprot =
}}
}}
'''Coagulation factor XII (Hageman factor)''', also known as '''F12''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: F12 coagulation factor XII (Hageman factor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2161| 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 coagulation factor XII which circulates in blood as a zymogen. This single chain zymogen is converted to a two-chain serine protease with an heavy chain (alpha-factor XIIa) and a light chain. The heavy chain contains two fibronectin-type domains, two epidermal growth factor (EGF)-like domains, a kringle domain and a proline-rich domain, whereas the light chain contains only a catalytic domain. On activation, further cleavages takes place in the heavy chain, resulting in the production of beta-factor XIIa light chain and the alpha-factor XIIa light chain becomes beta-factor XIIa heavy chain. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then to beta-factor XIIa. The active factor XIIa participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. It activates coagulation factors VII and XI. Defects in this gene do not cause any clinical symptoms and the sole effect is that whole-blood clotting time is prolonged.<ref name="entrez">{{cite web | title = Entrez Gene: F12 coagulation factor XII (Hageman factor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2161| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Girolami A, Randi ML, Gavasso S, ''et al.'' |title=The occasional venous thromboses seen in patients with severe (homozygous) FXII deficiency are probably due to associated risk factors: a study of prevalence in 21 patients and review of the literature. |journal=J. Thromb. Thrombolysis |volume=17 |issue= 2 |pages= 139-43 |year= 2005 |pmid= 15306750 |doi= 10.1023/B:THRO.0000037670.42776.cd }}
*{{cite journal | author=Renné T, Gailani D |title=Role of Factor XII in hemostasis and thrombosis: clinical implications. |journal=Expert review of cardiovascular therapy |volume=5 |issue= 4 |pages= 733-41 |year= 2007 |pmid= 17605651 |doi= 10.1586/14779072.5.4.733 }}
*{{cite journal | author=Harris RJ, Ling VT, Spellman MW |title=O-linked fucose is present in the first epidermal growth factor domain of factor XII but not protein C. |journal=J. Biol. Chem. |volume=267 |issue= 8 |pages= 5102-7 |year= 1992 |pmid= 1544894 |doi= }}
*{{cite journal | author=McMullen BA, Fujikawa K, Davie EW |title=Location of the disulfide bonds in human plasma prekallikrein: the presence of four novel apple domains in the amino-terminal portion of the molecule. |journal=Biochemistry |volume=30 |issue= 8 |pages= 2050-6 |year= 1991 |pmid= 1998666 |doi= }}
*{{cite journal | author=Miyata T, Kawabata S, Iwanaga S, ''et al.'' |title=Coagulation factor XII (Hageman factor) Washington D.C.: inactive factor XIIa results from Cys-571----Ser substitution. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 21 |pages= 8319-22 |year= 1989 |pmid= 2510163 |doi= }}
*{{cite journal | author=Bernardi F, Marchetti G, Patracchini P, ''et al.'' |title=Factor XII gene alteration in Hageman trait detected by TaqI restriction enzyme. |journal=Blood |volume=69 |issue= 5 |pages= 1421-4 |year= 1987 |pmid= 2882793 |doi= }}
*{{cite journal | author=Cool DE, MacGillivray RT |title=Characterization of the human blood coagulation factor XII gene. Intron/exon gene organization and analysis of the 5'-flanking region. |journal=J. Biol. Chem. |volume=262 |issue= 28 |pages= 13662-73 |year= 1987 |pmid= 2888762 |doi= }}
*{{cite journal | author=Que BG, Davie EW |title=Characterization of a cDNA coding for human factor XII (Hageman factor). |journal=Biochemistry |volume=25 |issue= 7 |pages= 1525-8 |year= 1986 |pmid= 3011063 |doi= }}
*{{cite journal | author=Royle NJ, Nigli M, Cool D, ''et al.'' |title=Structural gene encoding human factor XII is located at 5q33-qter. |journal=Somat. Cell Mol. Genet. |volume=14 |issue= 2 |pages= 217-21 |year= 1988 |pmid= 3162339 |doi= }}
*{{cite journal | author=Citarella F, Tripodi M, Fantoni A, ''et al.'' |title=Assignment of human coagulation factor XII (fXII) to chromosome 5 by cDNA hybridization to DNA from somatic cell hybrids. |journal=Hum. Genet. |volume=80 |issue= 4 |pages= 397-8 |year= 1989 |pmid= 3198120 |doi= }}
*{{cite journal | author=Henry ML, Everson B, Ratnoff OD |title=Inhibition of the activation of Hageman factor (factor XII) by beta 2-glycoprotein I. |journal=J. Lab. Clin. Med. |volume=111 |issue= 5 |pages= 519-23 |year= 1988 |pmid= 3361230 |doi= }}
*{{cite journal | author=Chung DW, Fujikawa K, McMullen BA, Davie EW |title=Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats. |journal=Biochemistry |volume=25 |issue= 9 |pages= 2410-7 |year= 1986 |pmid= 3521732 |doi= }}
*{{cite journal | author=Tripodi M, Citarella F, Guida S, ''et al.'' |title=cDNA sequence coding for human coagulation factor XII (Hageman). |journal=Nucleic Acids Res. |volume=14 |issue= 7 |pages= 3146 |year= 1986 |pmid= 3754331 |doi= }}
*{{cite journal | author=Cool DE, Edgell CJ, Louie GV, ''et al.'' |title=Characterization of human blood coagulation factor XII cDNA. Prediction of the primary structure of factor XII and the tertiary structure of beta-factor XIIa. |journal=J. Biol. Chem. |volume=260 |issue= 25 |pages= 13666-76 |year= 1985 |pmid= 3877053 |doi= }}
*{{cite journal | author=McMullen BA, Fujikawa K |title=Amino acid sequence of the heavy chain of human alpha-factor XIIa (activated Hageman factor). |journal=J. Biol. Chem. |volume=260 |issue= 9 |pages= 5328-41 |year= 1985 |pmid= 3886654 |doi= }}
*{{cite journal | author=de Grouchy J, Turleau C |title=Tentative localization of a Hageman (Factor XII) locus on 7q, probably the 7q35 band. |journal=Humangenetik |volume=24 |issue= 3 |pages= 197-200 |year= 1975 |pmid= 4140832 |doi= }}
*{{cite journal | author=Fujikawa K, McMullen BA |title=Amino acid sequence of human beta-factor XIIa. |journal=J. Biol. Chem. |volume=258 |issue= 18 |pages= 10924-33 |year= 1983 |pmid= 6604055 |doi= }}
*{{cite journal | author=Hovinga JK, Schaller J, Stricker H, ''et al.'' |title=Coagulation factor XII Locarno: the functional defect is caused by the amino acid substitution Arg 353-->Pro leading to loss of a kallikrein cleavage site. |journal=Blood |volume=84 |issue= 4 |pages= 1173-81 |year= 1994 |pmid= 8049433 |doi= }}
*{{cite journal | author=Schloesser M, Hofferbert S, Bartz U, ''et al.'' |title=The novel acceptor splice site mutation 11396(G-->A) in the factor XII gene causes a truncated transcript in cross-reacting material negative patients. |journal=Hum. Mol. Genet. |volume=4 |issue= 7 |pages= 1235-7 |year= 1996 |pmid= 8528215 |doi= }}
*{{cite journal | author=Hofferbert S, Müller J, Köstering H, ''et al.'' |title=A novel 5'-upstream mutation in the factor XII gene is associated with a TaqI restriction site in an Alu repeat in factor XII-deficient patients. |journal=Hum. Genet. |volume=97 |issue= 6 |pages= 838-41 |year= 1996 |pmid= 8641707 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FPR1... {November 16, 2007 5:06:03 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 5:06:33 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- 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 = Formyl peptide receptor 1
| HGNCid = 3826
| Symbol = FPR1
| AltSymbols =; FMLP; FPR
| OMIM = 136537
| ECnumber =
| Homologene = 20466
| MGIid = 107443
| GeneAtlas_image1 = PBB_GE_FPR1_205119_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_FPR1_205118_at_tn.png
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004982 |text = N-formyl peptide receptor activity}}
| Component = {{GNF_GO|id=GO:0005768 |text = endosome}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0000187 |text = activation of MAPK activity}} {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007188 |text = G-protein signaling, coupled to cAMP nucleotide second messenger}} {{GNF_GO|id=GO:0007263 |text = nitric oxide mediated signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2357
| Hs_Ensembl = ENSG00000171051
| Hs_RefseqProtein = NP_002020
| Hs_RefseqmRNA = NM_002029
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 56940237
| Hs_GenLoc_end = 56946912
| Hs_Uniprot = P21462
| Mm_EntrezGene = 14293
| Mm_Ensembl = ENSMUSG00000045551
| Mm_RefseqmRNA = NM_013521
| Mm_RefseqProtein = NP_038549
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 17581087
| Mm_GenLoc_end = 17588557
| Mm_Uniprot = Q3UV01
}}
}}
'''Formyl peptide receptor 1''', also known as '''FPR1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FPR1 formyl peptide receptor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2357| 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=Graves V, Gabig T, McCarthy L, ''et al.'' |title=Simultaneous mobilization of Mac-1 (CD11b/CD18) and formyl peptide chemoattractant receptors in human neutrophils. |journal=Blood |volume=80 |issue= 3 |pages= 776-87 |year= 1992 |pmid= 1322204 |doi= }}
*{{cite journal | author=Murphy PM, Ozçelik T, Kenney RT, ''et al.'' |title=A structural homologue of the N-formyl peptide receptor. Characterization and chromosome mapping of a peptide chemoattractant receptor family. |journal=J. Biol. Chem. |volume=267 |issue= 11 |pages= 7637-43 |year= 1992 |pmid= 1373134 |doi= }}
*{{cite journal | author=Perez HD, Holmes R, Kelly E, ''et al.'' |title=Cloning of the gene coding for a human receptor for formyl peptides. Characterization of a promoter region and evidence for polymorphic expression. |journal=Biochemistry |volume=31 |issue= 46 |pages= 11595-9 |year= 1992 |pmid= 1445895 |doi= }}
*{{cite journal | author=Bao L, Gerard NP, Eddy RL, ''et al.'' |title=Mapping of genes for the human C5a receptor (C5AR), human FMLP receptor (FPR), and two FMLP receptor homologue orphan receptors (FPRH1, FPRH2) to chromosome 19. |journal=Genomics |volume=13 |issue= 2 |pages= 437-40 |year= 1992 |pmid= 1612600 |doi= }}
*{{cite journal | author=Murphy PM, McDermott D |title=Functional expression of the human formyl peptide receptor in Xenopus oocytes requires a complementary human factor. |journal=J. Biol. Chem. |volume=266 |issue= 19 |pages= 12560-7 |year= 1991 |pmid= 1712023 |doi= }}
*{{cite journal | author=Boulay F, Tardif M, Brouchon L, Vignais P |title=Synthesis and use of a novel N-formyl peptide derivative to isolate a human N-formyl peptide receptor cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=168 |issue= 3 |pages= 1103-9 |year= 1990 |pmid= 2161213 |doi= }}
*{{cite journal | author=Boulay F, Tardif M, Brouchon L, Vignais P |title=The human N-formylpeptide receptor. Characterization of two cDNA isolates and evidence for a new subfamily of G-protein-coupled receptors. |journal=Biochemistry |volume=29 |issue= 50 |pages= 11123-33 |year= 1991 |pmid= 2176894 |doi= }}
*{{cite journal | author=Wahl SM, Allen JB, Gartner S, ''et al.'' |title=HIV-1 and its envelope glycoprotein down-regulate chemotactic ligand receptors and chemotactic function of peripheral blood monocytes. |journal=J. Immunol. |volume=142 |issue= 10 |pages= 3553-9 |year= 1989 |pmid= 2541200 |doi= }}
*{{cite journal | author=Jesaitis AJ, Naemura JR, Painter RG, ''et al.'' |title=Intracellular localization of N-formyl chemotactic receptor and Mg2+ dependent ATPase in human granulocytes. |journal=Biochim. Biophys. Acta |volume=719 |issue= 3 |pages= 556-68 |year= 1983 |pmid= 6129903 |doi= }}
*{{cite journal | author=Prossnitz ER, Kim CM, Benovic JL, Ye RD |title=Phosphorylation of the N-formyl peptide receptor carboxyl terminus by the G protein-coupled receptor kinase, GRK2. |journal=J. Biol. Chem. |volume=270 |issue= 3 |pages= 1130-7 |year= 1995 |pmid= 7836371 |doi= }}
*{{cite journal | author=Klotz KN, Jesaitis AJ |title=Physical coupling of N-formyl peptide chemoattractant receptors to G protein is unaffected by desensitization. |journal=Biochem. Pharmacol. |volume=48 |issue= 6 |pages= 1297-300 |year= 1994 |pmid= 7945424 |doi= }}
*{{cite journal | author=Bommakanti RK, Dratz EA, Siemsen DW, Jesaitis AJ |title=Characterization of complex formation between Gi2 and octyl glucoside solubilized neutrophil N-formyl peptide chemoattractant receptor by sedimentation velocity. |journal=Biochim. Biophys. Acta |volume=1209 |issue= 1 |pages= 69-76 |year= 1994 |pmid= 7947984 |doi= }}
*{{cite journal | author=Murphy PM, Tiffany HL, McDermott D, Ahuja SK |title=Sequence and organization of the human N-formyl peptide receptor-encoding gene. |journal=Gene |volume=133 |issue= 2 |pages= 285-90 |year= 1993 |pmid= 8224916 |doi= }}
*{{cite journal | author=Jesaitis AJ, Erickson RW, Klotz KN, ''et al.'' |title=Functional molecular complexes of human N-formyl chemoattractant receptors and actin. |journal=J. Immunol. |volume=151 |issue= 10 |pages= 5653-65 |year= 1993 |pmid= 8228254 |doi= }}
*{{cite journal | author=Särndahl E, Bokoch GM, Boulay F, ''et al.'' |title=Direct or C5a-induced activation of heterotrimeric Gi2 proteins in human neutrophils is associated with interaction between formyl peptide receptors and the cytoskeleton. |journal=J. Biol. Chem. |volume=271 |issue= 25 |pages= 15267-71 |year= 1996 |pmid= 8663057 |doi= }}
*{{cite journal | author=Maestes DC, Potter RM, Prossnitz ER |title=Differential phosphorylation paradigms dictate desensitization and internalization of the N-formyl peptide receptor. |journal=J. Biol. Chem. |volume=274 |issue= 42 |pages= 29791-5 |year= 1999 |pmid= 10514456 |doi= }}
*{{cite journal | author=Liang TS, Wang JM, Murphy PM, Gao JL |title=Serum amyloid A is a chemotactic agonist at FPR2, a low-affinity N-formylpeptide receptor on mouse neutrophils. |journal=Biochem. Biophys. Res. Commun. |volume=270 |issue= 2 |pages= 331-5 |year= 2000 |pmid= 10753626 |doi= 10.1006/bbrc.2000.2416 }}
*{{cite journal | author=Luu NT, Rainger GE, Nash GB |title=Differential ability of exogenous chemotactic agents to disrupt transendothelial migration of flowing neutrophils. |journal=J. Immunol. |volume=164 |issue= 11 |pages= 5961-9 |year= 2000 |pmid= 10820279 |doi= }}
*{{cite journal | author=Bennett TA, Maestas DC, Prossnitz ER |title=Arrestin binding to the G protein-coupled N-formyl peptide receptor is regulated by the conserved "DRY" sequence. |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24590-4 |year= 2000 |pmid= 10823817 |doi= 10.1074/jbc.C000314200 }}
*{{cite journal | author=Ayala JM, Goyal S, Liverton NJ, ''et al.'' |title=Serum-induced monocyte differentiation and monocyte chemotaxis are regulated by the p38 MAP kinase signal transduction pathway. |journal=J. Leukoc. Biol. |volume=67 |issue= 6 |pages= 869-75 |year= 2000 |pmid= 10857861 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HLA-F... {November 16, 2007 5:06:33 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 5:07:14 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 = Major histocompatibility complex, class I, F
| HGNCid = 4963
| Symbol = HLA-F
| AltSymbols =; HLA-5.4; HLA-CDA12; HLAF
| OMIM = 143110
| ECnumber =
| Homologene = 85957
| MGIid = 95931
| GeneAtlas_image1 = PBB_GE_HLA-F_204806_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_HLA-F_221875_x_at_tn.png
| Function = {{GNF_GO|id=GO:0032393 |text = MHC class I receptor activity}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0042612 |text = MHC class I protein complex}}
| Process = {{GNF_GO|id=GO:0002474 |text = antigen processing and presentation of peptide antigen via MHC class I}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0019882 |text = antigen processing and presentation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3134
| Hs_Ensembl = ENSG00000137403
| Hs_RefseqProtein = NP_061823
| Hs_RefseqmRNA = NM_018950
| Hs_GenLoc_db =
| Hs_GenLoc_chr = c6_COX
| Hs_GenLoc_start = 29832424
| Hs_GenLoc_end = 29836307
| Hs_Uniprot = P30511
| Mm_EntrezGene = 15013
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_010392
| Mm_RefseqProtein = NP_034522
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Major histocompatibility complex, class I, F''', also known as '''HLA-F''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HLA-F major histocompatibility complex, class I, F| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3134| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = HLA-F belongs to the HLA class I heavy chain paralogues. This class I molecule is a heterodimer consisting of a heavy chain and a light chain (beta-2 microglobulin). The heavy chain is anchored in the membrane. HLA-F binds a restricted subset of peptides derived from the leader peptides of other class I molecules. The heavy chain is approximately 42 kDa and its gene contains 8 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the alpha1 and alpha2 domains, which both bind the peptide, exon 4 encodes the alpha3 domain, exon 5 encodes the transmembrane region and exons 6 and 7 encode the cytoplasmic tail. The HLA-F gene exhibits few polymorphisms.<ref name="entrez">{{cite web | title = Entrez Gene: HLA-F major histocompatibility complex, class I, F| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3134| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Geyer M, Fackler OT, Peterlin BM |title=Structure--function relationships in HIV-1 Nef. |journal=EMBO Rep. |volume=2 |issue= 7 |pages= 580-5 |year= 2001 |pmid= 11463741 |doi= 10.1093/embo-reports/kve141 }}
*{{cite journal | author=Greenway AL, Holloway G, McPhee DA, ''et al.'' |title=HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication. |journal=J. Biosci. |volume=28 |issue= 3 |pages= 323-35 |year= 2004 |pmid= 12734410 |doi= }}
*{{cite journal | author=Bénichou S, Benmerah A |title=[The HIV nef and the Kaposi-sarcoma-associated virus K3/K5 proteins: "parasites"of the endocytosis pathway] |journal=Med Sci (Paris) |volume=19 |issue= 1 |pages= 100-6 |year= 2003 |pmid= 12836198 |doi= }}
*{{cite journal | author=Leavitt SA, SchOn A, Klein JC, ''et al.'' |title=Interactions of HIV-1 proteins gp120 and Nef with cellular partners define a novel allosteric paradigm. |journal=Curr. Protein Pept. Sci. |volume=5 |issue= 1 |pages= 1-8 |year= 2004 |pmid= 14965316 |doi= }}
*{{cite journal | author=Tolstrup M, Ostergaard L, Laursen AL, ''et al.'' |title=HIV/SIV escape from immune surveillance: focus on Nef. |journal=Curr. HIV Res. |volume=2 |issue= 2 |pages= 141-51 |year= 2004 |pmid= 15078178 |doi= }}
*{{cite journal | author=Joseph AM, Kumar M, Mitra D |title=Nef: "necessary and enforcing factor" in HIV infection. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 87-94 |year= 2005 |pmid= 15638726 |doi= }}
*{{cite journal | author=Anderson JL, Hope TJ |title=HIV accessory proteins and surviving the host cell. |journal=Current HIV/AIDS reports |volume=1 |issue= 1 |pages= 47-53 |year= 2005 |pmid= 16091223 |doi= }}
*{{cite journal | author=Kozlowski S, Corr M, Takeshita T, ''et al.'' |title=Serum angiotensin-1 converting enzyme activity processes a human immunodeficiency virus 1 gp160 peptide for presentation by major histocompatibility complex class I molecules. |journal=J. Exp. Med. |volume=175 |issue= 6 |pages= 1417-22 |year= 1992 |pmid= 1316930 |doi= }}
*{{cite journal | author=Geraghty DE, Wei XH, Orr HT, Koller BH |title=Human leukocyte antigen F (HLA-F). An expressed HLA gene composed of a class I coding sequence linked to a novel transcribed repetitive element. |journal=J. Exp. Med. |volume=171 |issue= 1 |pages= 1-18 |year= 1990 |pmid= 1688605 |doi= }}
*{{cite journal | author=Lury D, Epstein H, Holmes N |title=The human class I MHC gene HLA-F is expressed in lymphocytes. |journal=Int. Immunol. |volume=2 |issue= 6 |pages= 531-7 |year= 1991 |pmid= 1707659 |doi= }}
*{{cite journal | author=Takahashi H, Merli S, Putney SD, ''et al.'' |title=A single amino acid interchange yields reciprocal CTL specificities for HIV-1 gp160. |journal=Science |volume=246 |issue= 4926 |pages= 118-21 |year= 1989 |pmid= 2789433 |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=Howcroft TK, Palmer LA, Brown J, ''et al.'' |title=HIV Tat represses transcription through Sp1-like elements in the basal promoter. |journal=Immunity |volume=3 |issue= 1 |pages= 127-38 |year= 1995 |pmid= 7621073 |doi= }}
*{{cite journal | author=Chen YH, Böck G, Vornhagen R, ''et al.'' |title=HIV-1 gp41 enhances major histocompatibility complex class I and ICAM-1 expression on H9 and U937 cells. |journal=Int. Arch. Allergy Immunol. |volume=104 |issue= 3 |pages= 227-31 |year= 1994 |pmid= 7913356 |doi= }}
*{{cite journal | author=Chen YH, Böck G, Vornhagen R, ''et al.'' |title=HIV-1 gp41 binding proteins and antibodies to gp41 could inhibit enhancement of human Raji cell MHC class I and II expression by gp41. |journal=Mol. Immunol. |volume=31 |issue= 13 |pages= 977-82 |year= 1994 |pmid= 8084338 |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=Howcroft TK, Strebel K, Martin MA, Singer DS |title=Repression of MHC class I gene promoter activity by two-exon Tat of HIV. |journal=Science |volume=260 |issue= 5112 |pages= 1320-2 |year= 1993 |pmid= 8493575 |doi= }}
*{{cite journal | author=Gasparini P, Borgato L, Piperno A, ''et al.'' |title=Linkage analysis of 6p21 polymorphic markers and the hereditary hemochromatosis: localization of the gene centromeric to HLA-F. |journal=Hum. Mol. Genet. |volume=2 |issue= 5 |pages= 571-6 |year= 1993 |pmid= 8518796 |doi= }}
*{{cite journal | author=Schwartz O, Maréchal V, Le Gall S, ''et al.'' |title=Endocytosis of major histocompatibility complex class I molecules is induced by the HIV-1 Nef protein. |journal=Nat. Med. |volume=2 |issue= 3 |pages= 338-42 |year= 1996 |pmid= 8612235 |doi= }}
*{{cite journal | author=Alexander-Miller MA, Parker KC, Tsukui T, ''et al.'' |title=Molecular analysis of presentation by HLA-A2.1 of a promiscuously binding V3 loop peptide from the HIV-envelope protein to human cytotoxic T lymphocytes. |journal=Int. Immunol. |volume=8 |issue= 5 |pages= 641-9 |year= 1997 |pmid= 8671651 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HSPA1A... {November 16, 2007 5:07:14 PM PST}
- SEARCH REDIRECT: Control Box Found: HSPA1A {November 16, 2007 5:07:43 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 5:07:44 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 5:07:44 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 5:07:44 PM PST}
- UPDATED: Updated protein page: HSPA1A {November 16, 2007 5:07:51 PM PST}
- INFO: Beginning work on IL3... {November 16, 2007 5:07:51 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 5:08:25 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
}}
<!-- 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 3 (colony-stimulating factor, multiple)
| HGNCid = 6011
| Symbol = IL3
| AltSymbols =; IL-3; MCGF; MGC79398; MGC79399; MULTI-CSF
| OMIM = 147740
| ECnumber =
| Homologene = 47938
| MGIid =
| GeneAtlas_image1 = PBB_GE_IL3_207906_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005135 |text = interleukin-3 receptor binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0045885 |text = positive regulation of survival gene product activity}} {{GNF_GO|id=GO:0050731 |text = positive regulation of peptidyl-tyrosine phosphorylation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3562
| Hs_Ensembl = ENSG00000164399
| Hs_RefseqProtein = NP_000579
| Hs_RefseqmRNA = NM_000588
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 131424121
| Hs_GenLoc_end = 131426796
| Hs_Uniprot = P08700
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Interleukin 3 (colony-stimulating factor, multiple)''', also known as '''IL3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IL3 interleukin 3 (colony-stimulating factor, multiple)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3562| 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 potent growth promoting cytokine. This cytokine is capable of supporting the proliferation of a broad range of hematopoietic cell types. It is involved in a variety of cell activities such as cell growth, differentiation and apoptosis. This cytokine has been shown to also possess neurotrophic activity, and it may be associated with neurologic disorders.<ref name="entrez">{{cite web | title = Entrez Gene: IL3 interleukin 3 (colony-stimulating factor, multiple)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3562| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wagemaker G, Burger H, van Gils FC, ''et al.'' |title=Interleukin-3. |journal=Biotherapy (Dordrecht, Netherlands) |volume=2 |issue= 4 |pages= 337-45 |year= 1991 |pmid= 2268499 |doi= }}
*{{cite journal | author=Martinez-Moczygemba M, Huston DP |title=Biology of common beta receptor-signaling cytokines: IL-3, IL-5, and GM-CSF. |journal=J. Allergy Clin. Immunol. |volume=112 |issue= 4 |pages= 653-65; quiz 666 |year= 2003 |pmid= 14564341 |doi= 10.1016/S0091 }}
*{{cite journal | author=Mroczko B, Szmitkowski M |title=Hematopoietic cytokines as tumor markers. |journal=Clin. Chem. Lab. Med. |volume=42 |issue= 12 |pages= 1347-54 |year= 2005 |pmid= 15576295 |doi= 10.1515/CCLM.2004.253 }}
*{{cite journal | author=Kitamura T, Sato N, Arai K, Miyajima A |title=Expression cloning of the human IL-3 receptor cDNA reveals a shared beta subunit for the human IL-3 and GM-CSF receptors. |journal=Cell |volume=66 |issue= 6 |pages= 1165-74 |year= 1991 |pmid= 1833064 |doi= }}
*{{cite journal | author=Urdal DL, Price V, Sassenfeld HM, ''et al.'' |title=Molecular characterization of colony-stimulating factors and their receptors: human interleukin-3. |journal=Ann. N. Y. Acad. Sci. |volume=554 |issue= |pages= 167-76 |year= 1989 |pmid= 2544122 |doi= }}
*{{cite journal | author=Otsuka T, Miyajima A, Brown N, ''et al.'' |title=Isolation and characterization of an expressible cDNA encoding human IL-3. Induction of IL-3 mRNA in human T cell clones. |journal=J. Immunol. |volume=140 |issue= 7 |pages= 2288-95 |year= 1988 |pmid= 3127463 |doi= }}
*{{cite journal | author=Yang YC, Ciarletta AB, Temple PA, ''et al.'' |title=Human IL-3 (multi-CSF): identification by expression cloning of a novel hematopoietic growth factor related to murine IL-3. |journal=Cell |volume=47 |issue= 1 |pages= 3-10 |year= 1986 |pmid= 3489530 |doi= }}
*{{cite journal | author=Le Beau MM, Epstein ND, O'Brien SJ, ''et al.'' |title=The interleukin 3 gene is located on human chromosome 5 and is deleted in myeloid leukemias with a deletion of 5q. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 16 |pages= 5913-7 |year= 1987 |pmid= 3497400 |doi= }}
*{{cite journal | author=Dorssers L, Burger H, Bot F, ''et al.'' |title=Characterization of a human multilineage-colony-stimulating factor cDNA clone identified by a conserved noncoding sequence in mouse interleukin-3. |journal=Gene |volume=55 |issue= 1 |pages= 115-24 |year= 1987 |pmid= 3497843 |doi= }}
*{{cite journal | author=Chirmule N, Goonewardena H, Pahwa S, ''et al.'' |title=HIV-1 envelope glycoproteins induce activation of activated protein-1 in CD4+ T cells. |journal=J. Biol. Chem. |volume=270 |issue= 33 |pages= 19364-9 |year= 1995 |pmid= 7642615 |doi= }}
*{{cite journal | author=Than S, Oyaizu N, Pahwa RN, ''et al.'' |title=Effect of human immunodeficiency virus type-1 envelope glycoprotein gp160 on cytokine production from cord-blood T cells. |journal=Blood |volume=84 |issue= 1 |pages= 184-8 |year= 1994 |pmid= 8018916 |doi= }}
*{{cite journal | author=Le Beau MM, Espinosa R, Neuman WL, ''et al.'' |title=Cytogenetic and molecular delineation of the smallest commonly deleted region of chromosome 5 in malignant myeloid diseases. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 12 |pages= 5484-8 |year= 1993 |pmid= 8516290 |doi= }}
*{{cite journal | author=Stomski FC, Sun Q, Bagley CJ, ''et al.'' |title=Human interleukin-3 (IL-3) induces disulfide-linked IL-3 receptor alpha- and beta-chain heterodimerization, which is required for receptor activation but not high-affinity binding. |journal=Mol. Cell. Biol. |volume=16 |issue= 6 |pages= 3035-46 |year= 1996 |pmid= 8649415 |doi= }}
*{{cite journal | author=Feng Y, Klein BK, McWherter CA |title=Three-dimensional solution structure and backbone dynamics of a variant of human interleukin-3. |journal=J. Mol. Biol. |volume=259 |issue= 3 |pages= 524-41 |year= 1996 |pmid= 8676386 |doi= 10.1006/jmbi.1996.0337 }}
*{{cite journal | author=Vanhaesebroeck B, Welham MJ, Kotani K, ''et al.'' |title=P110delta, a novel phosphoinositide 3-kinase in leukocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 9 |pages= 4330-5 |year= 1997 |pmid= 9113989 |doi= }}
*{{cite journal | author=Klein BK, Feng Y, McWherter CA, ''et al.'' |title=The receptor binding site of human interleukin-3 defined by mutagenesis and molecular modeling. |journal=J. Biol. Chem. |volume=272 |issue= 36 |pages= 22630-41 |year= 1997 |pmid= 9278420 |doi= }}
*{{cite journal | author=Sanchez X, Suetomi K, Cousins-Hodges B, ''et al.'' |title=CXC chemokines suppress proliferation of myeloid progenitor cells by activation of the CXC chemokine receptor 2. |journal=J. Immunol. |volume=160 |issue= 2 |pages= 906-10 |year= 1998 |pmid= 9551928 |doi= }}
*{{cite journal | author=Tabira T, Chui DH, Fan JP, ''et al.'' |title=Interleukin-3 and interleukin-3 receptors in the brain. |journal=Ann. N. Y. Acad. Sci. |volume=840 |issue= |pages= 107-16 |year= 1998 |pmid= 9629242 |doi= }}
*{{cite journal | author=Nilsen EM, Johansen FE, Jahnsen FL, ''et al.'' |title=Cytokine profiles of cultured microvascular endothelial cells from the human intestine. |journal=Gut |volume=42 |issue= 5 |pages= 635-42 |year= 1998 |pmid= 9659156 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KCNE1... {November 16, 2007 5:08:25 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 5:09:04 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
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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 = Potassium voltage-gated channel, Isk-related family, member 1
| HGNCid = 6240
| Symbol = KCNE1
| AltSymbols =; ISK; JLNS; JLNS2; LQT5; MGC33114; MinK
| OMIM = 176261
| ECnumber =
| Homologene = 185
| MGIid = 96673
| GeneAtlas_image1 = PBB_GE_KCNE1_208514_at_tn.png
| Function = {{GNF_GO|id=GO:0005251 |text = delayed rectifier potassium channel activity}} {{GNF_GO|id=GO:0015459 |text = potassium channel regulator activity}} {{GNF_GO|id=GO:0030955 |text = potassium ion binding}}
| Component = {{GNF_GO|id=GO:0008076 |text = voltage-gated potassium channel complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0016324 |text = apical plasma membrane}}
| Process = {{GNF_GO|id=GO:0002070 |text = epithelial cell maturation}} {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006813 |text = potassium ion transport}} {{GNF_GO|id=GO:0006936 |text = muscle contraction}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0008016 |text = regulation of heart contraction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3753
| Hs_Ensembl = ENSG00000180509
| Hs_RefseqProtein = NP_000210
| Hs_RefseqmRNA = NM_000219
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 21
| Hs_GenLoc_start = 34740858
| Hs_GenLoc_end = 34806443
| Hs_Uniprot = P15382
| Mm_EntrezGene = 16509
| Mm_Ensembl = ENSMUSG00000039639
| Mm_RefseqmRNA = XM_983408
| Mm_RefseqProtein = XP_988502
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 92234860
| Mm_GenLoc_end = 92248327
| Mm_Uniprot = Q545H6
}}
}}
'''Potassium voltage-gated channel, Isk-related family, member 1''', also known as '''KCNE1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KCNE1 potassium voltage-gated channel, Isk-related family, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3753| 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 = KCNE1 together with KCNQ1 encode the two subunits of the K+ channel responsible for the delayed-rectifier K+ current in cardiac myocytes (referred to as IsK).<ref name="entrez">{{cite web | title = Entrez Gene: KCNE1 potassium voltage-gated channel, Isk-related family, member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3753| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Murai T, Kakizuka A, Takumi T, ''et al.'' |title=Molecular cloning and sequence analysis of human genomic DNA encoding a novel membrane protein which exhibits a slowly activating potassium channel activity. |journal=Biochem. Biophys. Res. Commun. |volume=161 |issue= 1 |pages= 176-81 |year= 1989 |pmid= 2730656 |doi= }}
*{{cite journal | author=Malo MS, Srivastava K, Ingram VM |title=Gene assignment by polymerase chain reaction: localization of the human potassium channel IsK gene to the Down's syndrome region of chromosome 21q22.1-q22.2. |journal=Gene |volume=159 |issue= 2 |pages= 273-5 |year= 1995 |pmid= 7622063 |doi= }}
*{{cite journal | author=Lai LP, Deng CL, Moss AJ, ''et al.'' |title=Polymorphism of the gene encoding a human minimal potassium ion channel (minK). |journal=Gene |volume=151 |issue= 1-2 |pages= 339-40 |year= 1995 |pmid= 7828904 |doi= }}
*{{cite journal | author=Chevillard C, Attali B, Lesage F, ''et al.'' |title=Localization of a potassium channel gene (KCNE1) to 21q22.1-q22.2 by in situ hybridization and somatic cell hybridization. |journal=Genomics |volume=15 |issue= 1 |pages= 243-5 |year= 1993 |pmid= 8432548 |doi= 10.1006/geno.1993.1051 }}
*{{cite journal | author=Tesson F, Donger C, Denjoy I, ''et al.'' |title=Exclusion of KCNE1 (IsK) as a candidate gene for Jervell and Lange-Nielsen syndrome. |journal=J. Mol. Cell. Cardiol. |volume=28 |issue= 9 |pages= 2051-5 |year= 1997 |pmid= 8899564 |doi= }}
*{{cite journal | author=Sanguinetti MC, Curran ME, Zou A, ''et al.'' |title=Coassembly of K(V)LQT1 and minK (IsK) proteins to form cardiac I(Ks) potassium channel. |journal=Nature |volume=384 |issue= 6604 |pages= 80-3 |year= 1996 |pmid= 8900283 |doi= 10.1038/384080a0 }}
*{{cite journal | author=Neyroud N, Tesson F, Denjoy I, ''et al.'' |title=A novel mutation in the potassium channel gene KVLQT1 causes the Jervell and Lange-Nielsen cardioauditory syndrome. |journal=Nat. Genet. |volume=15 |issue= 2 |pages= 186-9 |year= 1997 |pmid= 9020846 |doi= 10.1038/ng0297-186 }}
*{{cite journal | author=McDonald TV, Yu Z, Ming Z, ''et al.'' |title=A minK-HERG complex regulates the cardiac potassium current I(Kr). |journal=Nature |volume=388 |issue= 6639 |pages= 289-92 |year= 1997 |pmid= 9230439 |doi= 10.1038/40882 }}
*{{cite journal | author=Chouabe C, Neyroud N, Guicheney P, ''et al.'' |title=Properties of KvLQT1 K+ channel mutations in Romano-Ward and Jervell and Lange-Nielsen inherited cardiac arrhythmias. |journal=EMBO J. |volume=16 |issue= 17 |pages= 5472-9 |year= 1997 |pmid= 9312006 |doi= 10.1093/emboj/16.17.5472 }}
*{{cite journal | author=Tyson J, Tranebjaerg L, Bellman S, ''et al.'' |title=IsK and KvLQT1: mutation in either of the two subunits of the slow component of the delayed rectifier potassium channel can cause Jervell and Lange-Nielsen syndrome. |journal=Hum. Mol. Genet. |volume=6 |issue= 12 |pages= 2179-85 |year= 1997 |pmid= 9328483 |doi= }}
*{{cite journal | author=Schulze-Bahr E, Wang Q, Wedekind H, ''et al.'' |title=KCNE1 mutations cause jervell and Lange-Nielsen syndrome. |journal=Nat. Genet. |volume=17 |issue= 3 |pages= 267-8 |year= 1997 |pmid= 9354783 |doi= 10.1038/ng1197-267 }}
*{{cite journal | author=Splawski I, Tristani-Firouzi M, Lehmann MH, ''et al.'' |title=Mutations in the hminK gene cause long QT syndrome and suppress IKs function. |journal=Nat. Genet. |volume=17 |issue= 3 |pages= 338-40 |year= 1997 |pmid= 9354802 |doi= 10.1038/ng1197-338 }}
*{{cite journal | author=Duggal P, Vesely MR, Wattanasirichaigoon D, ''et al.'' |title=Mutation of the gene for IsK associated with both Jervell and Lange-Nielsen and Romano-Ward forms of Long-QT syndrome. |journal=Circulation |volume=97 |issue= 2 |pages= 142-6 |year= 1998 |pmid= 9445165 |doi= }}
*{{cite journal | author=Bianchi L, Shen Z, Dennis AT, ''et al.'' |title=Cellular dysfunction of LQT5-minK mutants: abnormalities of IKs, IKr and trafficking in long QT syndrome. |journal=Hum. Mol. Genet. |volume=8 |issue= 8 |pages= 1499-507 |year= 1999 |pmid= 10400998 |doi= }}
*{{cite journal | author=Piccini M, Vitelli F, Seri M, ''et al.'' |title=KCNE1-like gene is deleted in AMME contiguous gene syndrome: identification and characterization of the human and mouse homologs. |journal=Genomics |volume=60 |issue= 3 |pages= 251-7 |year= 1999 |pmid= 10493825 |doi= 10.1006/geno.1999.5904 }}
*{{cite journal | author=Hattori M, Fujiyama A, Taylor TD, ''et al.'' |title=The DNA sequence of human chromosome 21. |journal=Nature |volume=405 |issue= 6784 |pages= 311-9 |year= 2000 |pmid= 10830953 |doi= 10.1038/35012518 }}
*{{cite journal | author=Splawski I, Shen J, Timothy KW, ''et al.'' |title=Spectrum of mutations in long-QT syndrome genes. KVLQT1, HERG, SCN5A, KCNE1, and KCNE2. |journal=Circulation |volume=102 |issue= 10 |pages= 1178-85 |year= 2000 |pmid= 10973849 |doi= }}
*{{cite journal | author=Melman YF, Domènech A, de la Luna S, McDonald TV |title=Structural determinants of KvLQT1 control by the KCNE family of proteins. |journal=J. Biol. Chem. |volume=276 |issue= 9 |pages= 6439-44 |year= 2001 |pmid= 11104781 |doi= 10.1074/jbc.M010713200 }}
*{{cite journal | author=Schulze-Bahr E, Schwarz M, Hauenschild S, ''et al.'' |title=A novel long-QT 5 gene mutation in the C-terminus (V109I) is associated with a mild phenotype. |journal=J. Mol. Med. |volume=79 |issue= 9 |pages= 504-9 |year= 2002 |pmid= 11692163 |doi= 10.1007/s001090100249 }}
*{{cite journal | author=Furukawa T, Ono Y, Tsuchiya H, ''et al.'' |title=Specific interaction of the potassium channel beta-subunit minK with the sarcomeric protein T-cap suggests a T-tubule-myofibril linking system. |journal=J. Mol. Biol. |volume=313 |issue= 4 |pages= 775-84 |year= 2001 |pmid= 11697903 |doi= 10.1006/jmbi.2001.5053 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KPNA4... {November 16, 2007 5:09:04 PM PST}
- SEARCH REDIRECT: Control Box Found: KPNA4 {November 16, 2007 5:09:40 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 5:09:43 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 5:09:43 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 5:09:43 PM PST}
- UPDATED: Updated protein page: KPNA4 {November 16, 2007 5:09:49 PM PST}
- INFO: Beginning work on LAMA5... {November 16, 2007 5:09:49 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 5:10:12 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Laminin, alpha 5
| HGNCid = 6485
| Symbol = LAMA5
| AltSymbols =; KIAA1907
| OMIM = 601033
| ECnumber =
| Homologene = 4060
| MGIid = 105382
| GeneAtlas_image1 = PBB_GE_LAMA5_210150_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0005605 |text = basal lamina}} {{GNF_GO|id=GO:0005606 |text = laminin-1 complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0030155 |text = regulation of cell adhesion}} {{GNF_GO|id=GO:0030334 |text = regulation of cell migration}} {{GNF_GO|id=GO:0045995 |text = regulation of embryonic development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3911
| Hs_Ensembl = ENSG00000130702
| Hs_RefseqProtein = NP_005551
| Hs_RefseqmRNA = NM_005560
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 60317510
| Hs_GenLoc_end = 60375763
| Hs_Uniprot = O15230
| Mm_EntrezGene = 16776
| Mm_Ensembl = ENSMUSG00000015647
| Mm_RefseqmRNA = XM_203796
| Mm_RefseqProtein = XP_203796
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 180105782
| Mm_GenLoc_end = 180155210
| Mm_Uniprot = Q3TZ05
}}
}}
'''Laminin, alpha 5''', also known as '''LAMA5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LAMA5 laminin, alpha 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3911| 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 = Components of the extracellular matrix exert myriad effects on tissues throughout the body. In particular, the laminins, a family of heterotrimeric extracellular glycoproteins, affect tissue development and integrity in such diverse organs as the kidney, lung, skin, and nervous system. It is thought that laminins mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Laminins function as heterotrimeric complexes of alpha, beta, and gamma chains, with each chain type representing a different subfamily of proteins. The protein encoded by this gene belongs to the alpha subfamily of laminin chains and is a major component of basement membranes. Two transcript variants encoding different isoforms have been found for this gene, but the full-length nature of one of them has not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: LAMA5 laminin, alpha 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3911| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Utani A, Nomizu M, Yamada Y |title=Fibulin-2 binds to the short arms of laminin-5 and laminin-1 via conserved amino acid sequences. |journal=J. Biol. Chem. |volume=272 |issue= 5 |pages= 2814-20 |year= 1997 |pmid= 9006922 |doi= }}
*{{cite journal | author=Rousselle P, Keene DR, Ruggiero F, ''et al.'' |title=Laminin 5 binds the NC-1 domain of type VII collagen. |journal=J. Cell Biol. |volume=138 |issue= 3 |pages= 719-28 |year= 1997 |pmid= 9245798 |doi= }}
*{{cite journal | author=Durkin ME, Loechel F, Mattei MG, ''et al.'' |title=Tissue-specific expression of the human laminin alpha5-chain, and mapping of the gene to human chromosome 20q13.2-13.3 and to distal mouse chromosome 2 near the locus for the ragged (Ra) mutation. |journal=FEBS Lett. |volume=411 |issue= 2-3 |pages= 296-300 |year= 1997 |pmid= 9271224 |doi= }}
*{{cite journal | author=Tiger CF, Champliaud MF, Pedrosa-Domellof F, ''et al.'' |title=Presence of laminin alpha5 chain and lack of laminin alpha1 chain during human muscle development and in muscular dystrophies. |journal=J. Biol. Chem. |volume=272 |issue= 45 |pages= 28590-5 |year= 1997 |pmid= 9353324 |doi= }}
*{{cite journal | author=Mrowiec T, Melchar C, Górski A |title=HIV-protein-mediated alterations in T cell interactions with the extracellular matrix proteins and endothelium. |journal=Arch. Immunol. Ther. Exp. (Warsz.) |volume=45 |issue= 2-3 |pages= 255-9 |year= 1998 |pmid= 9597096 |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=Shimizu H, Hosokawa H, Ninomiya H, ''et al.'' |title=Adhesion of cultured bovine aortic endothelial cells to laminin-1 mediated by dystroglycan. |journal=J. Biol. Chem. |volume=274 |issue= 17 |pages= 11995-2000 |year= 1999 |pmid= 10207021 |doi= }}
*{{cite journal | author=Son YJ, Scranton TW, Sunderland WJ, ''et al.'' |title=The synaptic vesicle protein SV2 is complexed with an alpha5-containing laminin on the nerve terminal surface. |journal=J. Biol. Chem. |volume=275 |issue= 1 |pages= 451-60 |year= 2000 |pmid= 10617638 |doi= }}
*{{cite journal | author=Köhler D, Kruse M, Stöcker W, Sterchi EE |title=Heterologously overexpressed, affinity-purified human meprin alpha is functionally active and cleaves components of the basement membrane in vitro. |journal=FEBS Lett. |volume=465 |issue= 1 |pages= 2-7 |year= 2000 |pmid= 10620696 |doi= }}
*{{cite journal | author=Kikkawa Y, Sanzen N, Fujiwara H, ''et al.'' |title=Integrin binding specificity of laminin-10/11: laminin-10/11 are recognized by alpha 3 beta 1, alpha 6 beta 1 and alpha 6 beta 4 integrins. |journal=J. Cell. Sci. |volume=113 ( Pt 5) |issue= |pages= 869-76 |year= 2000 |pmid= 10671376 |doi= }}
*{{cite journal | author=Champliaud MF, Virtanen I, Tiger CF, ''et al.'' |title=Posttranslational modifications and beta/gamma chain associations of human laminin alpha1 and laminin alpha5 chains: purification of laminin-3 from placenta. |journal=Exp. Cell Res. |volume=259 |issue= 2 |pages= 326-35 |year= 2000 |pmid= 10964500 |doi= 10.1006/excr.2000.4980 }}
*{{cite journal | author=Libby RT, Champliaud MF, Claudepierre T, ''et al.'' |title=Laminin expression in adult and developing retinae: evidence of two novel CNS laminins. |journal=J. Neurosci. |volume=20 |issue= 17 |pages= 6517-28 |year= 2000 |pmid= 10964957 |doi= }}
*{{cite journal | author=Pierce RA, Griffin GL, Miner JH, Senior RM |title=Expression patterns of laminin alpha1 and alpha5 in human lung during development. |journal=Am. J. Respir. Cell Mol. Biol. |volume=23 |issue= 6 |pages= 742-7 |year= 2001 |pmid= 11104726 |doi= }}
*{{cite journal | author=Parsons SF, Lee G, Spring FA, ''et al.'' |title=Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity. |journal=Blood |volume=97 |issue= 1 |pages= 312-20 |year= 2001 |pmid= 11133776 |doi= }}
*{{cite journal | author=Saghizadeh M, Brown DJ, Castellon R, ''et al.'' |title=Overexpression of matrix metalloproteinase-10 and matrix metalloproteinase-3 in human diabetic corneas: a possible mechanism of basement membrane and integrin alterations. |journal=Am. J. Pathol. |volume=158 |issue= 2 |pages= 723-34 |year= 2001 |pmid= 11159210 |doi= }}
*{{cite journal | author=McArthur CP, Wang Y, Heruth D, Gustafson S |title=Amplification of extracellular matrix and oncogenes in tat-transfected human salivary gland cell lines with expression of laminin, fibronectin, collagens I, III, IV, c-myc and p53. |journal=Arch. Oral Biol. |volume=46 |issue= 6 |pages= 545-55 |year= 2001 |pmid= 11311202 |doi= }}
*{{cite journal | author=Gagnoux-Palacios L, Allegra M, Spirito F, ''et al.'' |title=The short arm of the laminin gamma2 chain plays a pivotal role in the incorporation of laminin 5 into the extracellular matrix and in cell adhesion. |journal=J. Cell Biol. |volume=153 |issue= 4 |pages= 835-50 |year= 2001 |pmid= 11352943 |doi= }}
*{{cite journal | author=Nagase T, Kikuno R, Ohara O |title=Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins. |journal=DNA Res. |volume=8 |issue= 4 |pages= 179-87 |year= 2002 |pmid= 11572484 |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=Doi M, Thyboll J, Kortesmaa J, ''et al.'' |title=Recombinant human laminin-10 (alpha5beta1gamma1). Production, purification, and migration-promoting activity on vascular endothelial cells. |journal=J. Biol. Chem. |volume=277 |issue= 15 |pages= 12741-8 |year= 2002 |pmid= 11821406 |doi= 10.1074/jbc.M111228200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LYZ... {November 16, 2007 5:10:12 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 5:10:31 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_LYZ_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 133l.
| PDB = {{PDB2|133l}}, {{PDB2|134l}}, {{PDB2|1b5u}}, {{PDB2|1b5v}}, {{PDB2|1b5w}}, {{PDB2|1b5x}}, {{PDB2|1b5y}}, {{PDB2|1b5z}}, {{PDB2|1b7l}}, {{PDB2|1b7m}}, {{PDB2|1b7n}}, {{PDB2|1b7o}}, {{PDB2|1b7p}}, {{PDB2|1b7q}}, {{PDB2|1b7r}}, {{PDB2|1b7s}}, {{PDB2|1bb3}}, {{PDB2|1bb4}}, {{PDB2|1bb5}}, {{PDB2|1c43}}, {{PDB2|1c45}}, {{PDB2|1c46}}, {{PDB2|1c7p}}, {{PDB2|1cj6}}, {{PDB2|1cj7}}, {{PDB2|1cj8}}, {{PDB2|1cj9}}, {{PDB2|1ckc}}, {{PDB2|1ckd}}, {{PDB2|1ckf}}, {{PDB2|1ckg}}, {{PDB2|1ckh}}, {{PDB2|1d6p}}, {{PDB2|1d6q}}, {{PDB2|1di3}}, {{PDB2|1di4}}, {{PDB2|1di5}}, {{PDB2|1eq4}}, {{PDB2|1eq5}}, {{PDB2|1eqe}}, {{PDB2|1gay}}, {{PDB2|1gaz}}, {{PDB2|1gb0}}, {{PDB2|1gb2}}, {{PDB2|1gb3}}, {{PDB2|1gb5}}, {{PDB2|1gb6}}, {{PDB2|1gb7}}, {{PDB2|1gb8}}, {{PDB2|1gb9}}, {{PDB2|1gbo}}, {{PDB2|1gbw}}, {{PDB2|1gbx}}, {{PDB2|1gby}}, {{PDB2|1gbz}}, {{PDB2|1gdw}}, {{PDB2|1gdx}}, {{PDB2|1ge0}}, {{PDB2|1ge1}}, {{PDB2|1ge2}}, {{PDB2|1ge3}}, {{PDB2|1ge4}}, {{PDB2|1gev}}, {{PDB2|1gez}}, {{PDB2|1gf0}}, {{PDB2|1gf3}}, {{PDB2|1gf4}}, {{PDB2|1gf5}}, {{PDB2|1gf6}}, {{PDB2|1gf7}}, {{PDB2|1gf8}}, {{PDB2|1gf9}}, {{PDB2|1gfa}}, {{PDB2|1gfe}}, {{PDB2|1gfg}}, {{PDB2|1gfh}}, {{PDB2|1gfj}}, {{PDB2|1gfk}}, {{PDB2|1gfr}}, {{PDB2|1gft}}, {{PDB2|1gfu}}, {{PDB2|1gfv}}, {{PDB2|1hnl}}, {{PDB2|1i1z}}, {{PDB2|1i20}}, {{PDB2|1i22}}, {{PDB2|1inu}}, {{PDB2|1ioc}}, {{PDB2|1ip1}}, {{PDB2|1ip2}}, {{PDB2|1ip3}}, {{PDB2|1ip4}}, {{PDB2|1ip5}}, {{PDB2|1ip6}}, {{PDB2|1ip7}}, {{PDB2|1iwt}}, {{PDB2|1iwu}}, {{PDB2|1iwv}}, {{PDB2|1iww}}, {{PDB2|1iwx}}, {{PDB2|1iwy}}, {{PDB2|1iwz}}, {{PDB2|1ix0}}, {{PDB2|1iy3}}, {{PDB2|1iy4}}, {{PDB2|1jka}}, {{PDB2|1jkb}}, {{PDB2|1jkc}}, {{PDB2|1jkd}}, {{PDB2|1jsf}}, {{PDB2|1jwr}}, {{PDB2|1laa}}, {{PDB2|1lhh}}, {{PDB2|1lhi}}, {{PDB2|1lhj}}, {{PDB2|1lhk}}, {{PDB2|1lhl}}, {{PDB2|1lhm}}, {{PDB2|1lmt}}, {{PDB2|1loz}}, {{PDB2|1lyy}}, {{PDB2|1lz1}}, {{PDB2|1lz4}}, {{PDB2|1lz5}}, {{PDB2|1lz6}}, {{PDB2|1lzr}}, {{PDB2|1lzs}}, {{PDB2|1op9}}, {{PDB2|1oua}}, {{PDB2|1oub}}, {{PDB2|1ouc}}, {{PDB2|1oud}}, {{PDB2|1oue}}, {{PDB2|1ouf}}, {{PDB2|1oug}}, {{PDB2|1ouh}}, {{PDB2|1oui}}, {{PDB2|1ouj}}, {{PDB2|1qsw}}, {{PDB2|1re2}}, {{PDB2|1rem}}, {{PDB2|1rex}}, {{PDB2|1rey}}, {{PDB2|1rez}}, {{PDB2|1tay}}, {{PDB2|1tby}}, {{PDB2|1tcy}}, {{PDB2|1tdy}}, {{PDB2|1ubz}}, {{PDB2|1w08}}, {{PDB2|1wqm}}, {{PDB2|1wqn}}, {{PDB2|1wqo}}, {{PDB2|1wqp}}, {{PDB2|1wqq}}, {{PDB2|1wqr}}, {{PDB2|1yam}}, {{PDB2|1yan}}, {{PDB2|1yao}}, {{PDB2|1yap}}, {{PDB2|1yaq}}, {{PDB2|207l}}, {{PDB2|208l}}, {{PDB2|2bqa}}, {{PDB2|2bqb}}, {{PDB2|2bqc}}, {{PDB2|2bqd}}, {{PDB2|2bqe}}, {{PDB2|2bqf}}, {{PDB2|2bqg}}, {{PDB2|2bqh}}, {{PDB2|2bqi}}, {{PDB2|2bqj}}, {{PDB2|2bqk}}, {{PDB2|2bql}}, {{PDB2|2bqm}}, {{PDB2|2bqn}}, {{PDB2|2bqo}}, {{PDB2|2hea}}, {{PDB2|2heb}}, {{PDB2|2hec}}, {{PDB2|2hed}}, {{PDB2|2hee}}, {{PDB2|2hef}}, {{PDB2|2lhm}}, {{PDB2|2mea}}, {{PDB2|2meb}}, {{PDB2|2mec}}, {{PDB2|2med}}, {{PDB2|2mee}}, {{PDB2|2mef}}, {{PDB2|2meg}}, {{PDB2|2meh}}, {{PDB2|2mei}}, {{PDB2|2nwd}}, {{PDB2|3lhm}}
| Name = Lysozyme (renal amyloidosis)
| HGNCid = 6740
| Symbol = LYZ
| AltSymbols =;
| OMIM = 153450
| ECnumber =
| Homologene = 37278
| MGIid = 96897
| GeneAtlas_image1 = PBB_GE_LYZ_213975_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003796 |text = lysozyme activity}} {{GNF_GO|id=GO:0016798 |text = hydrolase activity, acting on glycosyl bonds}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0016998 |text = cell wall catabolic process}} {{GNF_GO|id=GO:0019835 |text = cytolysis}} {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4069
| Hs_Ensembl = ENSG00000090382
| Hs_RefseqProtein = NP_000230
| Hs_RefseqmRNA = NM_000239
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 68028401
| Hs_GenLoc_end = 68034280
| Hs_Uniprot = P61626
| Mm_EntrezGene = 17105
| Mm_Ensembl = ENSMUSG00000069516
| Mm_RefseqmRNA = NM_017372
| Mm_RefseqProtein = NP_059068
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 116681441
| Mm_GenLoc_end = 116686397
| Mm_Uniprot = Q3TXG2
}}
}}
'''Lysozyme (renal amyloidosis)''', also known as '''LYZ''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LYZ lysozyme (renal amyloidosis)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4069| 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 = LYZ encodes human lysozyme, whose natural substrate is the bacterial cell wall peptidoglycan (cleaving the beta[1-4]glycosidic linkages between N-acetylmuramic acid and N-acetylglucosamine). Lysozyme is one of the anti-microbial agents found in human milk, and is also present in spleen, lung, kidney, white blood cells, plasma, aliva, and tears. Missense mutations in LYZ have been identified in heritable renal anyloidosis.<ref name="entrez">{{cite web | title = Entrez Gene: LYZ lysozyme (renal amyloidosis)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4069| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Reitamo S, Klockars M, Adinolfi M, Osserman EF |title=Human lysozyme (origin and distribution in health and disease). |journal=La Ricerca in clinica e in laboratorio |volume=8 |issue= 4 |pages= 211-31 |year= 1979 |pmid= 366724 |doi= }}
*{{cite journal | author=McKenzie HA |title=alpha-Lactalbumins and lysozymes. |journal=EXS |volume=75 |issue= |pages= 365-409 |year= 1996 |pmid= 8765309 |doi= }}
*{{cite journal | author=Ohkubo T, Taniyama Y, Kikuchi M |title=1H and 15N NMR study of human lysozyme. |journal=J. Biochem. |volume=110 |issue= 6 |pages= 1022-9 |year= 1992 |pmid= 1794972 |doi= }}
*{{cite journal | author=Inaka K, Taniyama Y, Kikuchi M, ''et al.'' |title=The crystal structure of a mutant human lysozyme C77/95A with increased secretion efficiency in yeast. |journal=J. Biol. Chem. |volume=266 |issue= 19 |pages= 12599-603 |year= 1991 |pmid= 2061330 |doi= }}
*{{cite journal | author=Redfield C, Dobson CM |title=1H NMR studies of human lysozyme: spectral assignment and comparison with hen lysozyme. |journal=Biochemistry |volume=29 |issue= 31 |pages= 7201-14 |year= 1990 |pmid= 2207098 |doi= }}
*{{cite journal | author=Peters CW, Kruse U, Pollwein R, ''et al.'' |title=The human lysozyme gene. Sequence organization and chromosomal localization. |journal=Eur. J. Biochem. |volume=182 |issue= 3 |pages= 507-16 |year= 1989 |pmid= 2546758 |doi= }}
*{{cite journal | author=Yoshimura K, Toibana A, Nakahama K |title=Human lysozyme: sequencing of a cDNA, and expression and secretion by Saccharomyces cerevisiae. |journal=Biochem. Biophys. Res. Commun. |volume=150 |issue= 2 |pages= 794-801 |year= 1988 |pmid= 2829884 |doi= }}
*{{cite journal | author=Castañón MJ, Spevak W, Adolf GR, ''et al.'' |title=Cloning of human lysozyme gene and expression in the yeast Saccharomyces cerevisiae. |journal=Gene |volume=66 |issue= 2 |pages= 223-34 |year= 1988 |pmid= 2971592 |doi= }}
*{{cite journal | author=Chung LP, Keshav S, Gordon S |title=Cloning the human lysozyme cDNA: inverted Alu repeat in the mRNA and in situ hybridization for macrophages and Paneth cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 17 |pages= 6227-31 |year= 1988 |pmid= 3413092 |doi= }}
*{{cite journal | author=Jollés J, Jollés P |title=Human milk lysozyme: unpublished data concerning the establishment of the complete primary structure; comparison with lysozymes of various origins. |journal=Helv. Chim. Acta |volume=54 |issue= 8 |pages= 2668-75 |year= 1972 |pmid= 5168859 |doi= 10.1002/hlca.19710540830 }}
*{{cite journal | author=Canfield RE, Kammerman S, Sobel JH, Morgan FJ |title=Primary structure of lysozymes from man and goose. |journal=Nature New Biol. |volume=232 |issue= 27 |pages= 16-7 |year= 1971 |pmid= 5284421 |doi= }}
*{{cite journal | author=Blake CC, Pulford WC, Artymiuk PJ |title=X-ray studies of water in crystals of lysozyme. |journal=J. Mol. Biol. |volume=167 |issue= 3 |pages= 693-723 |year= 1983 |pmid= 6876162 |doi= }}
*{{cite journal | author=Artymiuk PJ, Blake CC |title=Refinement of human lysozyme at 1.5 A resolution analysis of non-bonded and hydrogen-bond interactions. |journal=J. Mol. Biol. |volume=152 |issue= 4 |pages= 737-62 |year= 1982 |pmid= 7334520 |doi= }}
*{{cite journal | author=Pepys MB, Hawkins PN, Booth DR, ''et al.'' |title=Human lysozyme gene mutations cause hereditary systemic amyloidosis. |journal=Nature |volume=362 |issue= 6420 |pages= 553-7 |year= 1993 |pmid= 8464497 |doi= 10.1038/362553a0 }}
*{{cite journal | author=Kanaya E, Ishihara K, Tsunasawa S, ''et al.'' |title=Indication of possible post-translational formation of disulphide bonds in the beta-sheet domain of human lysozyme. |journal=Biochem. J. |volume=292 ( Pt 2) |issue= |pages= 469-76 |year= 1993 |pmid= 8503881 |doi= }}
*{{cite journal | author=Harrison RF, Hawkins PN, Roche WR, ''et al.'' |title='Fragile' liver and massive hepatic haemorrhage due to hereditary amyloidosis. |journal=Gut |volume=38 |issue= 1 |pages= 151-2 |year= 1996 |pmid= 8566845 |doi= }}
*{{cite journal | author=van Berkel PH, Geerts ME, van Veen HA, ''et al.'' |title=N-terminal stretch Arg2, Arg3, Arg4 and Arg5 of human lactoferrin is essential for binding to heparin, bacterial lipopolysaccharide, human lysozyme and DNA. |journal=Biochem. J. |volume=328 ( Pt 1) |issue= |pages= 145-51 |year= 1998 |pmid= 9359845 |doi= }}
*{{cite journal | author=Shteyngart B, Chaiwiriyakul S, Wong J, Cantor JO |title=Preferential binding of lysozyme to elastic fibres in pulmonary emphysema. |journal=Thorax |volume=53 |issue= 3 |pages= 193-6 |year= 1998 |pmid= 9659355 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MAPK7... {November 16, 2007 5:11:00 PM PST}
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- UPDATED: Updated protein page: PSMA3 {November 16, 2007 5:12:14 PM PST}
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- UPDATED: Updated protein page: RNASEL {November 16, 2007 5:12:52 PM PST}
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- UPDATED: Updated protein page: SIAH1 {November 16, 2007 5:13:27 PM PST}
- INFO: Beginning work on SPHK1... {November 16, 2007 5:14:50 PM PST}
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<!-- 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 = Sphingosine kinase 1
| HGNCid = 11240
| Symbol = SPHK1
| AltSymbols =; SPHK
| OMIM = 603730
| ECnumber =
| Homologene = 40294
| MGIid = 1316649
| GeneAtlas_image1 = PBB_GE_SPHK1_219257_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0004143 |text = diacylglycerol kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008481 |text = sphinganine kinase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0017050 |text = D-erythro-sphingosine kinase activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0001568 |text = blood vessel development}} {{GNF_GO|id=GO:0006670 |text = sphingosine metabolic process}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007205 |text = protein kinase C activation}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0007420 |text = brain development}} {{GNF_GO|id=GO:0019722 |text = calcium-mediated signaling}} {{GNF_GO|id=GO:0030307 |text = positive regulation of cell growth}} {{GNF_GO|id=GO:0030335 |text = positive regulation of cell migration}} {{GNF_GO|id=GO:0045766 |text = positive regulation of angiogenesis}} {{GNF_GO|id=GO:0045931 |text = positive regulation of progression through mitotic cell cycle}} {{GNF_GO|id=GO:0045987 |text = positive regulation of smooth muscle contraction}} {{GNF_GO|id=GO:0046521 |text = sphingoid catabolic process}} {{GNF_GO|id=GO:0048146 |text = positive regulation of fibroblast proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8877
| Hs_Ensembl = ENSG00000176170
| Hs_RefseqProtein = NP_068807
| Hs_RefseqmRNA = NM_021972
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 71892326
| Hs_GenLoc_end = 71895530
| Hs_Uniprot = Q9NYA1
| Mm_EntrezGene = 20698
| Mm_Ensembl = ENSMUSG00000061878
| Mm_RefseqmRNA = NM_011451
| Mm_RefseqProtein = NP_035581
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 116348001
| Mm_GenLoc_end = 116352758
| Mm_Uniprot =
}}
}}
'''Sphingosine kinase 1''', also known as '''SPHK1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SPHK1 sphingosine kinase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8877| 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 = Sphingosine-1-phosphate (SPP) is a novel lipid messenger with both intracellular and extracellular functions. Intracellularly, it regulates proliferation and survival, and extracellularly, it is a ligand for EDG1 (MIM 601974). Various stimuli increase cellular levels of SPP by activation of sphingosine kinase (SPHK), the enzyme that catalyzes the phosphorylation of sphingosine. Competitive inhibitors of SPHK block formation of SPP and selectively inhibit cellular proliferation induced by a variety of factors, including platelet-derived growth factor (e.g., MIM 173430) and serum.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: SPHK1 sphingosine kinase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8877| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tsukahara T, Mizuno H, Igarashi Y |title=[Molecular diversity of sphingosine kinase] |journal=Tanpakushitsu Kakusan Koso |volume=47 |issue= 4 Suppl |pages= 509-13 |year= 2002 |pmid= 11915350 |doi= }}
*{{cite journal | author=Sudo K, Chinen K, Nakamura Y |title=2058 expressed sequence tags (ESTs) from a human fetal lung cDNA library. |journal=Genomics |volume=24 |issue= 2 |pages= 276-9 |year= 1995 |pmid= 7698749 |doi= 10.1006/geno.1994.1616 }}
*{{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=Hillier LD, Lennon G, Becker M, ''et al.'' |title=Generation and analysis of 280,000 human expressed sequence tags. |journal=Genome Res. |volume=6 |issue= 9 |pages= 807-28 |year= 1997 |pmid= 8889549 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Kohama T, Olivera A, Edsall L, ''et al.'' |title=Molecular cloning and functional characterization of murine sphingosine kinase. |journal=J. Biol. Chem. |volume=273 |issue= 37 |pages= 23722-8 |year= 1998 |pmid= 9726979 |doi= }}
*{{cite journal | author=Liu H, Sugiura M, Nava VE, ''et al.'' |title=Molecular cloning and functional characterization of a novel mammalian sphingosine kinase type 2 isoform. |journal=J. Biol. Chem. |volume=275 |issue= 26 |pages= 19513-20 |year= 2000 |pmid= 10751414 |doi= 10.1074/jbc.M002759200 }}
*{{cite journal | author=Nava VE, Lacana E, Poulton S, ''et al.'' |title=Functional characterization of human sphingosine kinase-1. |journal=FEBS Lett. |volume=473 |issue= 1 |pages= 81-4 |year= 2000 |pmid= 10802064 |doi= }}
*{{cite journal | author=Melendez AJ, Carlos-Dias E, Gosink M, ''et al.'' |title=Human sphingosine kinase: molecular cloning, functional characterization and tissue distribution. |journal=Gene |volume=251 |issue= 1 |pages= 19-26 |year= 2000 |pmid= 10863092 |doi= }}
*{{cite journal | author=Pitson SM, D'andrea RJ, Vandeleur L, ''et al.'' |title=Human sphingosine kinase: purification, molecular cloning and characterization of the native and recombinant enzymes. |journal=Biochem. J. |volume=350 Pt 2 |issue= |pages= 429-41 |year= 2001 |pmid= 10947957 |doi= }}
*{{cite journal | author=Xia P, Wang L, Moretti PA, ''et al.'' |title=Sphingosine kinase interacts with TRAF2 and dissects tumor necrosis factor-alpha signaling. |journal=J. Biol. Chem. |volume=277 |issue= 10 |pages= 7996-8003 |year= 2002 |pmid= 11777919 |doi= 10.1074/jbc.M111423200 }}
*{{cite journal | author=Melendez AJ, Khaw AK |title=Dichotomy of Ca2+ signals triggered by different phospholipid pathways in antigen stimulation of human mast cells. |journal=J. Biol. Chem. |volume=277 |issue= 19 |pages= 17255-62 |year= 2002 |pmid= 11856736 |doi= 10.1074/jbc.M110944200 }}
*{{cite journal | author=Hayashi S, Okada T, Igarashi N, ''et al.'' |title=Identification and characterization of RPK118, a novel sphingosine kinase-1-binding protein. |journal=J. Biol. Chem. |volume=277 |issue= 36 |pages= 33319-24 |year= 2002 |pmid= 12077123 |doi= 10.1074/jbc.M201442200 }}
*{{cite journal | author=Lacaná E, Maceyka M, Milstien S, Spiegel S |title=Cloning and characterization of a protein kinase A anchoring protein (AKAP)-related protein that interacts with and regulates sphingosine kinase 1 activity. |journal=J. Biol. Chem. |volume=277 |issue= 36 |pages= 32947-53 |year= 2002 |pmid= 12080051 |doi= 10.1074/jbc.M202841200 }}
*{{cite journal | author=Johnson KR, Becker KP, Facchinetti MM, ''et al.'' |title=PKC-dependent activation of sphingosine kinase 1 and translocation to the plasma membrane. Extracellular release of sphingosine-1-phosphate induced by phorbol 12-myristate 13-acetate (PMA). |journal=J. Biol. Chem. |volume=277 |issue= 38 |pages= 35257-62 |year= 2002 |pmid= 12124383 |doi= 10.1074/jbc.M203033200 }}
*{{cite journal | author=Pitson SM, Moretti PA, Zebol JR, ''et al.'' |title=The nucleotide-binding site of human sphingosine kinase 1. |journal=J. Biol. Chem. |volume=277 |issue= 51 |pages= 49545-53 |year= 2003 |pmid= 12393916 |doi= 10.1074/jbc.M206687200 }}
*{{cite journal | author=Nava VE, Hobson JP, Murthy S, ''et al.'' |title=Sphingosine kinase type 1 promotes estrogen-dependent tumorigenesis of breast cancer MCF-7 cells. |journal=Exp. Cell Res. |volume=281 |issue= 1 |pages= 115-27 |year= 2002 |pmid= 12441135 |doi= }}
*{{cite journal | author=MacKinnon AC, Buckley A, Chilvers ER, ''et al.'' |title=Sphingosine kinase: a point of convergence in the action of diverse neutrophil priming agents. |journal=J. Immunol. |volume=169 |issue= 11 |pages= 6394-400 |year= 2002 |pmid= 12444147 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SRD5A2... {November 16, 2007 5:13:27 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 5:13:52 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| 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 = Steroid-5-alpha-reductase, alpha polypeptide 2 (3-oxo-5 alpha-steroid delta 4-dehydrogenase alpha 2)
| HGNCid = 11285
| Symbol = SRD5A2
| AltSymbols =; MGC138457
| OMIM = 607306
| ECnumber =
| Homologene = 37292
| MGIid = 2150380
| GeneAtlas_image1 = PBB_GE_SRD5A2_206938_at_tn.png
| Function = {{GNF_GO|id=GO:0003865 |text = 3-oxo-5-alpha-steroid 4-dehydrogenase activity}} {{GNF_GO|id=GO:0009917 |text = sterol 5-alpha reductase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006702 |text = androgen biosynthetic process}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007530 |text = sex determination}} {{GNF_GO|id=GO:0007548 |text = sex differentiation}} {{GNF_GO|id=GO:0008584 |text = male gonad development}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0030539 |text = male genitalia development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6716
| Hs_Ensembl = ENSG00000049319
| Hs_RefseqProtein = NP_000339
| Hs_RefseqmRNA = NM_000348
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 31603160
| Hs_GenLoc_end = 31659473
| Hs_Uniprot = P31213
| Mm_EntrezGene = 94224
| Mm_Ensembl = ENSMUSG00000038541
| Mm_RefseqmRNA = NM_053188
| Mm_RefseqProtein = NP_444418
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 73922606
| Mm_GenLoc_end = 73952814
| Mm_Uniprot = Q3UTZ9
}}
}}
'''Steroid-5-alpha-reductase, alpha polypeptide 2 (3-oxo-5 alpha-steroid delta 4-dehydrogenase alpha 2)''', also known as '''SRD5A2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SRD5A2 steroid-5-alpha-reductase, alpha polypeptide 2 (3-oxo-5 alpha-steroid delta 4-dehydrogenase alpha 2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6716| 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 microsomal protein expressed at high levels in androgen-sensitive tissues such as the prostate. The encoded protein is active at acidic pH and is sensitive to the 4-azasteroid inhibitor finasteride. Deficiencies in this gene can result in male pseudohermaphroditism, specifically pseudovaginal perineoscrotal hypospadias (PPSH).<ref name="entrez">{{cite web | title = Entrez Gene: SRD5A2 steroid-5-alpha-reductase, alpha polypeptide 2 (3-oxo-5 alpha-steroid delta 4-dehydrogenase alpha 2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6716| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Thigpen AE, Davis DL, Gautier T, ''et al.'' |title=Brief report: the molecular basis of steroid 5 alpha-reductase deficiency in a large Dominican kindred. |journal=N. Engl. J. Med. |volume=327 |issue= 17 |pages= 1216-9 |year= 1992 |pmid= 1406794 |doi= }}
*{{cite journal | author=Labrie F, Sugimoto Y, Luu-The V, ''et al.'' |title=Structure of human type II 5 alpha-reductase gene. |journal=Endocrinology |volume=131 |issue= 3 |pages= 1571-3 |year= 1992 |pmid= 1505484 |doi= }}
*{{cite journal | author=Thigpen AE, Davis DL, Milatovich A, ''et al.'' |title=Molecular genetics of steroid 5 alpha-reductase 2 deficiency. |journal=J. Clin. Invest. |volume=90 |issue= 3 |pages= 799-809 |year= 1992 |pmid= 1522235 |doi= }}
*{{cite journal | author=Andersson S, Berman DM, Jenkins EP, Russell DW |title=Deletion of steroid 5 alpha-reductase 2 gene in male pseudohermaphroditism. |journal=Nature |volume=354 |issue= 6349 |pages= 159-61 |year= 1991 |pmid= 1944596 |doi= 10.1038/354159a0 }}
*{{cite journal | author=Boudon C, Lobaccaro JM, Lumbroso S, ''et al.'' |title=A new deletion of the 5 alpha-reductase type 2 gene in a Turkish family with 5 alpha-reductase deficiency. |journal=Clin. Endocrinol. (Oxf) |volume=43 |issue= 2 |pages= 183-8 |year= 1995 |pmid= 7554313 |doi= }}
*{{cite journal | author=Thigpen AE, Silver RI, Guileyardo JM, ''et al.'' |title=Tissue distribution and ontogeny of steroid 5 alpha-reductase isozyme expression. |journal=J. Clin. Invest. |volume=92 |issue= 2 |pages= 903-10 |year= 1993 |pmid= 7688765 |doi= }}
*{{cite journal | author=Cai LQ, Zhu YS, Katz MD, ''et al.'' |title=5 alpha-reductase-2 gene mutations in the Dominican Republic. |journal=J. Clin. Endocrinol. Metab. |volume=81 |issue= 5 |pages= 1730-5 |year= 1996 |pmid= 8626825 |doi= }}
*{{cite journal | author=Hochberg Z, Chayen R, Reiss N, ''et al.'' |title=Clinical, biochemical, and genetic findings in a large pedigree of male and female patients with 5 alpha-reductase 2 deficiency. |journal=J. Clin. Endocrinol. Metab. |volume=81 |issue= 8 |pages= 2821-7 |year= 1996 |pmid= 8768837 |doi= }}
*{{cite journal | author=Vilchis F, Canto P, Chávez B, ''et al.'' |title=Molecular analysis of the 5 alpha-steroid reductase type 2 gene in a family with deficiency of the enzyme. |journal=Am. J. Med. Genet. |volume=69 |issue= 1 |pages= 69-72 |year= 1997 |pmid= 9066886 |doi= }}
*{{cite journal | author=Anwar R, Gilbey SG, New JP, Markham AF |title=Male pseudohermaphroditism resulting from a novel mutation in the human steroid 5 alpha-reductase type 2 gene (SRD5A2). |journal=MP, Mol. Pathol. |volume=50 |issue= 1 |pages= 51-2 |year= 1997 |pmid= 9208814 |doi= }}
*{{cite journal | author=Can S, Zhu YS, Cai LQ, ''et al.'' |title=The identification of 5 alpha-reductase-2 and 17 beta-hydroxysteroid dehydrogenase-3 gene defects in male pseudohermaphrodites from a Turkish kindred. |journal=J. Clin. Endocrinol. Metab. |volume=83 |issue= 2 |pages= 560-9 |year= 1998 |pmid= 9467575 |doi= }}
*{{cite journal | author=Nordenskjöld A, Ivarsson SA |title=Molecular characterization of 5 alpha-reductase type 2 deficiency and fertility in a Swedish family. |journal=J. Clin. Endocrinol. Metab. |volume=83 |issue= 9 |pages= 3236-8 |year= 1998 |pmid= 9745434 |doi= }}
*{{cite journal | author=Nordenskjöld A, Magnus O, Aagenaes O, Knudtzon J |title=Homozygous mutation (A228T) in the 5alpha-reductase type 2 gene in a boy with 5alpha-reductase deficiency: genotype-phenotype correlations. |journal=Am. J. Med. Genet. |volume=80 |issue= 3 |pages= 269-72 |year= 1999 |pmid= 9843052 |doi= }}
*{{cite journal | author=Nnane IP, Kato K, Liu Y, ''et al.'' |title=Inhibition of androgen synthesis in human testicular and prostatic microsomes and in male rats by novel steroidal compounds. |journal=Endocrinology |volume=140 |issue= 6 |pages= 2891-7 |year= 1999 |pmid= 10342882 |doi= }}
*{{cite journal | author=Makridakis NM, Ross RK, Pike MC, ''et al.'' |title=Association of mis-sense substitution in SRD5A2 gene with prostate cancer in African-American and Hispanic men in Los Angeles, USA. |journal=Lancet |volume=354 |issue= 9183 |pages= 975-8 |year= 1999 |pmid= 10501358 |doi= }}
*{{cite journal | author=Vilchis F, Méndez JP, Canto P, ''et al.'' |title=Identification of missense mutations in the SRD5A2 gene from patients with steroid 5alpha-reductase 2 deficiency. |journal=Clin. Endocrinol. (Oxf) |volume=52 |issue= 3 |pages= 383-7 |year= 2000 |pmid= 10718838 |doi= }}
*{{cite journal | author=Hellwinkel OJ, Müller A, Struve D, Hiort O |title=Influence of androgens and age on androgen receptor and 5 alpha-reductase II transcription. |journal=Eur. J. Endocrinol. |volume=143 |issue= 2 |pages= 217-25 |year= 2000 |pmid= 10913941 |doi= }}
*{{cite journal | author=Chávez B, Valdez E, Vilchis F |title=Uniparental disomy in steroid 5alpha-reductase 2 deficiency. |journal=J. Clin. Endocrinol. Metab. |volume=85 |issue= 9 |pages= 3147-50 |year= 2000 |pmid= 10999800 |doi= }}
*{{cite journal | author=Kim KS, Liu W, Cunha GR, ''et al.'' |title=Expression of the androgen receptor and 5 alpha-reductase type 2 in the developing human fetal penis and urethra. |journal=Cell Tissue Res. |volume=307 |issue= 2 |pages= 145-53 |year= 2002 |pmid= 11845321 |doi= 10.1007/s004410100464 }}
*{{cite journal | author=Hiort O, Schütt SM, Bals-Pratsch M, ''et al.'' |title=A novel homozygous disruptive mutation in the SRD5A2-gene in a partially virilized patient with 5alpha-reductase deficiency. |journal=Int. J. Androl. |volume=25 |issue= 1 |pages= 55-8 |year= 2002 |pmid= 11869378 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TERF2... {November 16, 2007 5:13:52 PM PST}
- SEARCH REDIRECT: Control Box Found: TERF2 {November 16, 2007 5:14:18 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 5:14:19 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 5:14:19 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 5:14:19 PM PST}
- UPDATED: Updated protein page: TERF2 {November 16, 2007 5:14:25 PM PST}
- INFO: Beginning work on UCHL1... {November 16, 2007 5:14:25 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 5:14:50 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 = PBB_Protein_UCHL1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2etl.
| PDB = {{PDB2|2etl}}
| Name = Ubiquitin carboxyl-terminal esterase L1 (ubiquitin thiolesterase)
| HGNCid = 12513
| Symbol = UCHL1
| AltSymbols =; PARK5; PGP9.5; Uch-L1
| OMIM = 191342
| ECnumber =
| Homologene = 37894
| MGIid = 103149
| GeneAtlas_image1 = PBB_GE_UCHL1_201387_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004197 |text = cysteine-type endopeptidase activity}} {{GNF_GO|id=GO:0004221 |text = ubiquitin thiolesterase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008242 |text = omega peptidase activity}} {{GNF_GO|id=GO:0016874 |text = ligase activity}} {{GNF_GO|id=GO:0043130 |text = ubiquitin binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0030424 |text = axon}} {{GNF_GO|id=GO:0043025 |text = cell soma}}
| Process = {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}} {{GNF_GO|id=GO:0006950 |text = response to stress}} {{GNF_GO|id=GO:0007412 |text = axon target recognition}} {{GNF_GO|id=GO:0007628 |text = adult walking behavior}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0016579 |text = protein deubiquitination}} {{GNF_GO|id=GO:0019896 |text = axon transport of mitochondrion}} {{GNF_GO|id=GO:0042755 |text = eating behavior}} {{GNF_GO|id=GO:0050905 |text = neuromuscular process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7345
| Hs_Ensembl = ENSG00000154277
| Hs_RefseqProtein = NP_004172
| Hs_RefseqmRNA = NM_004181
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 40953607
| Hs_GenLoc_end = 40965203
| Hs_Uniprot = P09936
| Mm_EntrezGene = 22223
| Mm_Ensembl = ENSMUSG00000029223
| Mm_RefseqmRNA = NM_011670
| Mm_RefseqProtein = NP_035800
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 66955376
| Mm_GenLoc_end = 66966364
| Mm_Uniprot = Q3TCH2
}}
}}
'''Ubiquitin carboxyl-terminal esterase L1 (ubiquitin thiolesterase)''', also known as '''UCHL1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: UCHL1 ubiquitin carboxyl-terminal esterase L1 (ubiquitin thiolesterase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7345| 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 = UCHL1 is a member of a gene family whose products hydrolyze small C-terminal adducts of ubiquitin to generate the ubiquitin monomer. Expression of UCHL1 is highly specific to neurons and to cells of the diffuse neuroendocrine system and their tumors. It is present in all neurons (Doran et al., 1983).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: UCHL1 ubiquitin carboxyl-terminal esterase L1 (ubiquitin thiolesterase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7345| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Healy DG, Abou-Sleiman PM, Wood NW |title=Genetic causes of Parkinson's disease: UCHL-1. |journal=Cell Tissue Res. |volume=318 |issue= 1 |pages= 189-94 |year= 2005 |pmid= 15221445 |doi= 10.1007/s00441-004-0917-3 }}
*{{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=Edwards YH, Fox MF, Povey S, ''et al.'' |title=The gene for human neurone specific ubiquitin C-terminal hydrolase (UCHL1, PGP9.5) maps to chromosome 4p14. |journal=Ann. Hum. Genet. |volume=55 |issue= Pt 4 |pages= 273-8 |year= 1992 |pmid= 1840236 |doi= }}
*{{cite journal | author=Honoré B, Rasmussen HH, Vandekerckhove J, Celis JE |title=Neuronal protein gene product 9.5 (IEF SSP 6104) is expressed in cultured human MRC-5 fibroblasts of normal origin and is strongly down-regulated in their SV40 transformed counterparts. |journal=FEBS Lett. |volume=280 |issue= 2 |pages= 235-40 |year= 1991 |pmid= 1849484 |doi= }}
*{{cite journal | author=Day IN, Hinks LJ, Thompson RJ |title=The structure of the human gene encoding protein gene product 9.5 (PGP9.5), a neuron-specific ubiquitin C-terminal hydrolase. |journal=Biochem. J. |volume=268 |issue= 2 |pages= 521-4 |year= 1990 |pmid= 2163617 |doi= }}
*{{cite journal | author=Day IN, Thompson RJ |title=Molecular cloning of cDNA coding for human PGP 9.5 protein. A novel cytoplasmic marker for neurones and neuroendocrine cells. |journal=FEBS Lett. |volume=210 |issue= 2 |pages= 157-60 |year= 1987 |pmid= 2947814 |doi= }}
*{{cite journal | author=Doran JF, Jackson P, Kynoch PA, Thompson RJ |title=Isolation of PGP 9.5, a new human neurone-specific protein detected by high-resolution two-dimensional electrophoresis. |journal=J. Neurochem. |volume=40 |issue= 6 |pages= 1542-7 |year= 1983 |pmid= 6343558 |doi= }}
*{{cite journal | author=Onno M, Nakamura T, Mariage-Samson R, ''et al.'' |title=Human TRE17 oncogene is generated from a family of homologous polymorphic sequences by single-base changes. |journal=DNA Cell Biol. |volume=12 |issue= 2 |pages= 107-18 |year= 1993 |pmid= 8471161 |doi= }}
*{{cite journal | author=Larsen CN, Price JS, Wilkinson KD |title=Substrate binding and catalysis by ubiquitin C-terminal hydrolases: identification of two active site residues. |journal=Biochemistry |volume=35 |issue= 21 |pages= 6735-44 |year= 1996 |pmid= 8639624 |doi= 10.1021/bi960099f }}
*{{cite journal | author=Best CL, Pudney J, Welch WR, ''et al.'' |title=Localization and characterization of white blood cell populations within the human ovary throughout the menstrual cycle and menopause. |journal=Hum. Reprod. |volume=11 |issue= 4 |pages= 790-7 |year= 1996 |pmid= 8671330 |doi= }}
*{{cite journal | author=D'Andrea V, Malinovsky L, Berni A, ''et al.'' |title=The immunolocalization of PGP 9.5 in normal human kidney and renal cell carcinoma. |journal=Il Giornale di chirurgia |volume=18 |issue= 10 |pages= 521-4 |year= 1998 |pmid= 9435142 |doi= }}
*{{cite journal | author=Larsen CN, Krantz BA, Wilkinson KD |title=Substrate specificity of deubiquitinating enzymes: ubiquitin C-terminal hydrolases. |journal=Biochemistry |volume=37 |issue= 10 |pages= 3358-68 |year= 1998 |pmid= 9521656 |doi= 10.1021/bi972274d }}
*{{cite journal | author=Leroy E, Boyer R, Auburger G, ''et al.'' |title=The ubiquitin pathway in Parkinson's disease. |journal=Nature |volume=395 |issue= 6701 |pages= 451-2 |year= 1998 |pmid= 9774100 |doi= 10.1038/26652 }}
*{{cite journal | author=Wada H, Kito K, Caskey LS, ''et al.'' |title=Cleavage of the C-terminus of NEDD8 by UCH-L3. |journal=Biochem. Biophys. Res. Commun. |volume=251 |issue= 3 |pages= 688-92 |year= 1998 |pmid= 9790970 |doi= 10.1006/bbrc.1998.9532 }}
*{{cite journal | author=Leroy E, Boyer R, Polymeropoulos MH |title=Intron-exon structure of ubiquitin c-terminal hydrolase-L1. |journal=DNA Res. |volume=5 |issue= 6 |pages= 397-400 |year= 1999 |pmid= 10048490 |doi= }}
*{{cite journal | author=Lincoln S, Vaughan J, Wood N, ''et al.'' |title=Low frequency of pathogenic mutations in the ubiquitin carboxy-terminal hydrolase gene in familial Parkinson's disease. |journal=Neuroreport |volume=10 |issue= 2 |pages= 427-9 |year= 1999 |pmid= 10203348 |doi= }}
*{{cite journal | author=Harhangi BS, Farrer MJ, Lincoln S, ''et al.'' |title=The Ile93Met mutation in the ubiquitin carboxy-terminal-hydrolase-L1 gene is not observed in European cases with familial Parkinson's disease. |journal=Neurosci. Lett. |volume=270 |issue= 1 |pages= 1-4 |year= 1999 |pmid= 10454131 |doi= }}
*{{cite journal | author=Saigoh K, Wang YL, Suh JG, ''et al.'' |title=Intragenic deletion in the gene encoding ubiquitin carboxy-terminal hydrolase in gad mice. |journal=Nat. Genet. |volume=23 |issue= 1 |pages= 47-51 |year= 1999 |pmid= 10471497 |doi= 10.1038/12647 }}
*{{cite journal | author=Mellick GD, Silburn PA |title=The ubiquitin carboxy-terminal hydrolase-L1 gene S18Y polymorphism does not confer protection against idiopathic Parkinson's disease. |journal=Neurosci. Lett. |volume=293 |issue= 2 |pages= 127-30 |year= 2000 |pmid= 11027850 |doi= }}
*{{cite journal | author=Sharma N, McLean PJ, Kawamata H, ''et al.'' |title=Alpha-synuclein has an altered conformation and shows a tight intermolecular interaction with ubiquitin in Lewy bodies. |journal=Acta Neuropathol. |volume=102 |issue= 4 |pages= 329-34 |year= 2002 |pmid= 11603807 |doi= }}
}}
{{refend}}
{{protein-stub}}
end log.
