Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 22:23, 17 November 2007 (UTC)[edit]
Proteins without matches (11)[edit]
Proteins with a High Potential Match (5)[edit]
Redirected Proteins (9)[edit]
Manual Inspection (Page not found) (16)[edit]
Updated (9)[edit]
Protein Status Grid - Date: 22:23, 17 November 2007 (UTC)[edit]
Vebose Log - Date: 22:23, 17 November 2007 (UTC)[edit]
- INFO: Beginning work on ADH1C... {November 17, 2007 1:56:03 PM PST}
- SEARCH REDIRECT: Control Box Found: ADH1C {November 17, 2007 1:56:22 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 1:56:24 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 1:56:24 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 1:56:24 PM PST}
- UPDATED: Updated protein page: ADH1C {November 17, 2007 1:56:30 PM PST}
- INFO: Beginning work on ADORA1... {November 17, 2007 1:56:30 PM PST}
- SEARCH REDIRECT: Control Box Found: ADORA1 {November 17, 2007 1:56:54 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 1:56:57 PM PST}
- SKIP SUMMARY: SKIPPING Summary, No Errors. {November 17, 2007 1:56:57 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 1:56:57 PM PST}
- UPDATED: Updated protein page: ADORA1 {November 17, 2007 1:57:03 PM PST}
- INFO: Beginning work on ALDOA... {November 17, 2007 1:57:03 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:57:39 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_ALDOA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ado.
| PDB = {{PDB2|1ado}}, {{PDB2|1ald}}, {{PDB2|1ewd}}, {{PDB2|1ewe}}, {{PDB2|1ewg}}, {{PDB2|1ex5}}, {{PDB2|1j4e}}, {{PDB2|1zah}}, {{PDB2|1zai}}, {{PDB2|1zaj}}, {{PDB2|1zal}}, {{PDB2|2ald}}, {{PDB2|2ot0}}, {{PDB2|2ot1}}, {{PDB2|4ald}}, {{PDB2|6ald}}
| Name = Aldolase A, fructose-bisphosphate
| HGNCid = 414
| Symbol = ALDOA
| AltSymbols =; ALDA; MGC10942; MGC17716; MGC17767
| OMIM = 103850
| ECnumber =
| Homologene = 68996
| MGIid = 87994
| GeneAtlas_image1 = PBB_GE_ALDOA_200966_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_ALDOA_214687_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004332 |text = fructose-bisphosphate aldolase activity}} {{GNF_GO|id=GO:0016829 |text = lyase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006000 |text = fructose metabolic process}} {{GNF_GO|id=GO:0006096 |text = glycolysis}} {{GNF_GO|id=GO:0006941 |text = striated muscle contraction}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 226
| Hs_Ensembl = ENSG00000149925
| Hs_RefseqProtein = NP_000025
| Hs_RefseqmRNA = NM_000034
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 29971973
| Hs_GenLoc_end = 29989235
| Hs_Uniprot = P04075
| Mm_EntrezGene = 11674
| Mm_Ensembl = ENSMUSG00000030695
| Mm_RefseqmRNA = NM_007438
| Mm_RefseqProtein = NP_031464
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 126586384
| Mm_GenLoc_end = 126590331
| Mm_Uniprot = Q5FWB7
}}
}}
'''Aldolase A, fructose-bisphosphate''', also known as '''ALDOA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ALDOA aldolase A, fructose-bisphosphate| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=226| 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 product, Aldolase A (fructose-bisphosphate aldolase) is a glycolytic enzyme that catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. Three aldolase isozymes (A, B, and C), encoded by three different genes, are differentially expressed during development. Aldolase A is found in the developing embryo and is produced in even greater amounts in adult muscle. Aldolase A expression is repressed in adult liver, kidney and intestine and similar to aldolase C levels in brain and other nervous tissue. Aldolase A deficiency has been associated with myopathy and hemolytic anemia. Alternative splicing of this gene results in multiple transcript variants which encode the same protein.<ref name="entrez">{{cite web | title = Entrez Gene: ALDOA aldolase A, fructose-bisphosphate| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=226| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Pfleiderer G, Thöner M, Wachsmuth ED |title=Histological examination of the aldolase monomer composition of cells from human kidney and hypernephroid carcinoma. |journal=Beiträge zur Pathologie |volume=156 |issue= 3 |pages= 266-79 |year= 1976 |pmid= 766744 |doi= }}
*{{cite journal | author=Rehbein-Thöner M, Pfleiderer G |title=The changes in aldolase isoenzyme pattern during development of the human kidney and small intestine--demonstrated in organ extracts and tissue sections. |journal=Hoppe-Seyler's Z. Physiol. Chem. |volume=358 |issue= 2 |pages= 169-80 |year= 1977 |pmid= 844801 |doi= }}
*{{cite journal | author=Wachsmuth ED |title=Differentiation of epithelial cells in human jejunum: localization and quantification of aminopeptidase, alkaline phosphatase and aldolase isozymes in tissue sections. |journal=Histochemistry |volume=48 |issue= 2 |pages= 101-9 |year= 1976 |pmid= 955981 |doi= }}
*{{cite journal | author=Lee KN, Maxwell MD, Patterson MK, ''et al.'' |title=Identification of transglutaminase substrates in HT29 colon cancer cells: use of 5-(biotinamido)pentylamine as a transglutaminase-specific probe. |journal=Biochim. Biophys. Acta |volume=1136 |issue= 1 |pages= 12-6 |year= 1992 |pmid= 1353685 |doi= }}
*{{cite journal | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi= }}
*{{cite journal | author=Mukai T, Arai Y, Yatsuki H, ''et al.'' |title=An additional promoter functions in the human aldolase A gene, but not in rat. |journal=Eur. J. Biochem. |volume=195 |issue= 3 |pages= 781-7 |year= 1991 |pmid= 1999195 |doi= }}
*{{cite journal | author=Gamblin SJ, Davies GJ, Grimes JM, ''et al.'' |title=Activity and specificity of human aldolases. |journal=J. Mol. Biol. |volume=219 |issue= 4 |pages= 573-6 |year= 1991 |pmid= 2056525 |doi= }}
*{{cite journal | author=Vértessy BG, Orosz F, Ovádi J |title=Modulation of the interaction between aldolase and glycerol-phosphate dehydrogenase by fructose phosphates. |journal=Biochim. Biophys. Acta |volume=1078 |issue= 2 |pages= 236-42 |year= 1991 |pmid= 2065091 |doi= }}
*{{cite journal | author=Takasaki Y, Takahashi I, Mukai T, Hori K |title=Human aldolase A of a hemolytic anemia patient with Asp-128----Gly substitution: characteristics of an enzyme generated in E. coli transfected with the expression plasmid pHAAD128G. |journal=J. Biochem. |volume=108 |issue= 2 |pages= 153-7 |year= 1990 |pmid= 2229018 |doi= }}
*{{cite journal | author=Gamblin SJ, Cooper B, Millar JR, ''et al.'' |title=The crystal structure of human muscle aldolase at 3.0 A resolution. |journal=FEBS Lett. |volume=262 |issue= 2 |pages= 282-6 |year= 1990 |pmid= 2335208 |doi= }}
*{{cite journal | author=Kishi H, Mukai T, Hirono A, ''et al.'' |title=Human aldolase A deficiency associated with a hemolytic anemia: thermolabile aldolase due to a single base mutation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 23 |pages= 8623-7 |year= 1988 |pmid= 2825199 |doi= }}
*{{cite journal | author=Izzo P, Costanzo P, Lupo A, ''et al.'' |title=A new human species of aldolase A mRNA from fibroblasts. |journal=Eur. J. Biochem. |volume=164 |issue= 1 |pages= 9-13 |year= 1987 |pmid= 3030757 |doi= }}
*{{cite journal | author=Inagaki H, Haimoto H, Hosoda S, Kato K |title=Aldolase C is localized in neuroendocrine cells. |journal=Experientia |volume=44 |issue= 9 |pages= 749-51 |year= 1988 |pmid= 3046960 |doi= }}
*{{cite journal | author=Freemont PS, Dunbar B, Fothergill-Gilmore LA |title=The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase. |journal=Biochem. J. |volume=249 |issue= 3 |pages= 779-88 |year= 1988 |pmid= 3355497 |doi= }}
*{{cite journal | author=Izzo P, Costanzo P, Lupo A, ''et al.'' |title=Human aldolase A gene. Structural organization and tissue-specific expression by multiple promoters and alternate mRNA processing. |journal=Eur. J. Biochem. |volume=174 |issue= 4 |pages= 569-78 |year= 1988 |pmid= 3391172 |doi= }}
*{{cite journal | author=Maire P, Gautron S, Hakim V, ''et al.'' |title=Characterization of three optional promoters in the 5' region of the human aldolase A gene. |journal=J. Mol. Biol. |volume=197 |issue= 3 |pages= 425-38 |year= 1988 |pmid= 3441006 |doi= }}
*{{cite journal | author=Kukita A, Yoshida MC, Fukushige S, ''et al.'' |title=Molecular gene mapping of human aldolase A (ALDOA) gene to chromosome 16. |journal=Hum. Genet. |volume=76 |issue= 1 |pages= 20-6 |year= 1987 |pmid= 3570299 |doi= }}
*{{cite journal | author=Tolan DR, Niclas J, Bruce BD, Lebo RV |title=Evolutionary implications of the human aldolase-A, -B, -C, and -pseudogene chromosome locations. |journal=Am. J. Hum. Genet. |volume=41 |issue= 5 |pages= 907-24 |year= 1987 |pmid= 3674018 |doi= }}
*{{cite journal | author=Sakakibara M, Mukai T, Hori K |title=Nucleotide sequence of a cDNA clone for human aldolase: a messenger RNA in the liver. |journal=Biochem. Biophys. Res. Commun. |volume=131 |issue= 1 |pages= 413-20 |year= 1985 |pmid= 3840020 |doi= }}
*{{cite journal | author=Ovádi J, Mohamed Osman IR, Batke J |title=Interaction of the dissociable glycerol-3-phosphate dehydrogenase and fructose-1,6-bisphosphate aldolase. Quantitative analysis by an extrinsic fluorescence probe. |journal=Eur. J. Biochem. |volume=133 |issue= 2 |pages= 433-7 |year= 1983 |pmid= 6406231 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ANK1... {November 17, 2007 1:57:39 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 1:58:14 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 = PBB_Protein_ANK1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1n11.
| PDB = {{PDB2|1n11}}
| Name = Ankyrin 1, erythrocytic
| HGNCid = 492
| Symbol = ANK1
| AltSymbols =; ANK; SPH1; SPH2
| OMIM = 182900
| ECnumber =
| Homologene = 55427
| MGIid = 88024
| GeneAtlas_image1 = PBB_GE_ANK1_205389_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ANK1_205390_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_ANK1_205391_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0008093 |text = cytoskeletal adaptor activity}} {{GNF_GO|id=GO:0019899 |text = enzyme binding}} {{GNF_GO|id=GO:0030507 |text = spectrin binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}} {{GNF_GO|id=GO:0016323 |text = basolateral plasma membrane}}
| Process = {{GNF_GO|id=GO:0006887 |text = exocytosis}} {{GNF_GO|id=GO:0007010 |text = cytoskeleton organization and biogenesis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0045199 |text = maintenance of epithelial cell polarity}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 286
| Hs_Ensembl = ENSG00000029534
| Hs_RefseqProtein = NP_000028
| Hs_RefseqmRNA = NM_000037
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 41629902
| Hs_GenLoc_end = 41873437
| Hs_Uniprot = P16157
| Mm_EntrezGene = 11733
| Mm_Ensembl = ENSMUSG00000031543
| Mm_RefseqmRNA = XM_981917
| Mm_RefseqProtein = XP_987011
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 24440681
| Mm_GenLoc_end = 24616041
| Mm_Uniprot = Q0VGY9
}}
}}
'''Ankyrin 1, erythrocytic''', also known as '''ANK1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ANK1 ankyrin 1, erythrocytic| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=286| 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 = Ankyrins are a family of proteins that are believed to link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of ankyrin 1 have been described, however, the precise functions of the various isoforms are not known. Alternative polyadenylation accounting for the different sized erythrocytic ankyrin 1 mRNAs, has also been reported. Truncated muscle-specific isoforms of ankyrin 1 resulting from usage of an alternate promoter have also been identified.<ref name="entrez">{{cite web | title = Entrez Gene: ANK1 ankyrin 1, erythrocytic| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=286| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bennett V, Baines AJ |title=Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues. |journal=Physiol. Rev. |volume=81 |issue= 3 |pages= 1353-92 |year= 2001 |pmid= 11427698 |doi= }}
*{{cite journal | author=Bennett V |title=Immunoreactive forms of human erythrocyte ankyrin are present in diverse cells and tissues. |journal=Nature |volume=281 |issue= 5732 |pages= 597-9 |year= 1979 |pmid= 492324 |doi= }}
*{{cite journal | author=Lambert S, Yu H, Prchal JT, ''et al.'' |title=cDNA sequence for human erythrocyte ankyrin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 5 |pages= 1730-4 |year= 1990 |pmid= 1689849 |doi= }}
*{{cite journal | author=Fujimoto T, Lee K, Miwa S, Ogawa K |title=Immunocytochemical localization of fodrin and ankyrin in bovine chromaffin cells in vitro. |journal=J. Histochem. Cytochem. |volume=39 |issue= 11 |pages= 1485-93 |year= 1991 |pmid= 1833445 |doi= }}
*{{cite journal | author=Lux SE, John KM, Bennett V |title=Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins. |journal=Nature |volume=344 |issue= 6261 |pages= 36-42 |year= 1990 |pmid= 2137557 |doi= 10.1038/344036a0 }}
*{{cite journal | author=Davis LH, Bennett V |title=Mapping the binding sites of human erythrocyte ankyrin for the anion exchanger and spectrin. |journal=J. Biol. Chem. |volume=265 |issue= 18 |pages= 10589-96 |year= 1990 |pmid= 2141335 |doi= }}
*{{cite journal | author=Korsgren C, Cohen CM |title=Associations of human erythrocyte band 4.2. Binding to ankyrin and to the cytoplasmic domain of band 3. |journal=J. Biol. Chem. |volume=263 |issue= 21 |pages= 10212-8 |year= 1988 |pmid= 2968981 |doi= }}
*{{cite journal | author=Cianci CD, Giorgi M, Morrow JS |title=Phosphorylation of ankyrin down-regulates its cooperative interaction with spectrin and protein 3. |journal=J. Cell. Biochem. |volume=37 |issue= 3 |pages= 301-15 |year= 1988 |pmid= 2970468 |doi= 10.1002/jcb.240370305 }}
*{{cite journal | author=Steiner JP, Bennett V |title=Ankyrin-independent membrane protein-binding sites for brain and erythrocyte spectrin. |journal=J. Biol. Chem. |volume=263 |issue= 28 |pages= 14417-25 |year= 1988 |pmid= 2971657 |doi= }}
*{{cite journal | author=Hargreaves WR, Giedd KN, Verkleij A, Branton D |title=Reassociation of ankyrin with band 3 in erythrocyte membranes and in lipid vesicles. |journal=J. Biol. Chem. |volume=255 |issue= 24 |pages= 11965-72 |year= 1981 |pmid= 6449514 |doi= }}
*{{cite journal | author=Bourguignon LY, Lokeshwar VB, Chen X, Kerrick WG |title=Hyaluronic acid-induced lymphocyte signal transduction and HA receptor (GP85/CD44)-cytoskeleton interaction. |journal=J. Immunol. |volume=151 |issue= 12 |pages= 6634-44 |year= 1994 |pmid= 7505012 |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=Morgans CW, Kopito RR |title=Association of the brain anion exchanger, AE3, with the repeat domain of ankyrin. |journal=J. Cell. Sci. |volume=105 ( Pt 4) |issue= |pages= 1137-42 |year= 1993 |pmid= 8227202 |doi= }}
*{{cite journal | author=Bourguignon LY, Jin H, Iida N, ''et al.'' |title=The involvement of ankyrin in the regulation of inositol 1,4,5-trisphosphate receptor-mediated internal Ca2+ release from Ca2+ storage vesicles in mouse T-lymphoma cells. |journal=J. Biol. Chem. |volume=268 |issue= 10 |pages= 7290-7 |year= 1993 |pmid= 8385102 |doi= }}
*{{cite journal | author=Eber SW, Gonzalez JM, Lux ML, ''et al.'' |title=Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis. |journal=Nat. Genet. |volume=13 |issue= 2 |pages= 214-8 |year= 1996 |pmid= 8640229 |doi= 10.1038/ng0696-214 }}
*{{cite journal | author=Lanfranchi G, Muraro T, Caldara F, ''et al.'' |title=Identification of 4370 expressed sequence tags from a 3'-end-specific cDNA library of human skeletal muscle by DNA sequencing and filter hybridization. |journal=Genome Res. |volume=6 |issue= 1 |pages= 35-42 |year= 1996 |pmid= 8681137 |doi= }}
*{{cite journal | author=del Giudice EM, Hayette S, Bozon M, ''et al.'' |title=Ankyrin Napoli: a de novo deletional frameshift mutation in exon 16 of ankyrin gene (ANK1) associated with spherocytosis. |journal=Br. J. Haematol. |volume=93 |issue= 4 |pages= 828-34 |year= 1996 |pmid= 8703812 |doi= }}
*{{cite journal | author=Zhou D, Birkenmeier CS, Williams MW, ''et al.'' |title=Small, membrane-bound, alternatively spliced forms of ankyrin 1 associated with the sarcoplasmic reticulum of mammalian skeletal muscle. |journal=J. Cell Biol. |volume=136 |issue= 3 |pages= 621-31 |year= 1997 |pmid= 9024692 |doi= }}
*{{cite journal | author=Gallagher PG, Tse WT, Scarpa AL, ''et al.'' |title=Structure and organization of the human ankyrin-1 gene. Basis for complexity of pre-mRNA processing. |journal=J. Biol. Chem. |volume=272 |issue= 31 |pages= 19220-8 |year= 1997 |pmid= 9235914 |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= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on APOC1... {November 17, 2007 1:58:14 PM PST}
- SEARCH REDIRECT: Control Box Found: APOC1 {November 17, 2007 1:58:33 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 2:03:25 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 2:03:25 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 2:03:25 PM PST}
- UPDATED: Updated protein page: APOC1 {November 17, 2007 2:03:31 PM PST}
- INFO: Beginning work on ATP2B4... {November 17, 2007 2:03:31 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 2:04:21 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 = ATPase, Ca++ transporting, plasma membrane 4
| HGNCid = 817
| Symbol = ATP2B4
| AltSymbols =; ATP2B2; DKFZp686G08106; DKFZp686M088; MXRA1; PMCA4
| OMIM = 108732
| ECnumber =
| Homologene = 48034
| MGIid = 88111
| GeneAtlas_image1 = PBB_GE_ATP2B4_205410_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ATP2B4_212136_at_tn.png
| GeneAtlas_image3 = PBB_GE_ATP2B4_212135_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:0005388 |text = calcium-transporting ATPase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016820 |text = hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0006812 |text = cation transport}} {{GNF_GO|id=GO:0006816 |text = calcium ion transport}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 493
| Hs_Ensembl = ENSG00000058668
| Hs_RefseqProtein = NP_001001396
| Hs_RefseqmRNA = NM_001001396
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 201862312
| Hs_GenLoc_end = 201979832
| Hs_Uniprot = P23634
| Mm_EntrezGene = 381290
| Mm_Ensembl = ENSMUSG00000026463
| Mm_RefseqmRNA = XM_981196
| Mm_RefseqProtein = XP_986290
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 135523057
| Mm_GenLoc_end = 135569692
| Mm_Uniprot =
}}
}}
'''ATPase, Ca++ transporting, plasma membrane 4''', also known as '''ATP2B4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATP2B4 ATPase, Ca++ transporting, plasma membrane 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=493| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene belongs to the family of P-type primary ion transport ATPases characterized by the formation of an aspartyl phosphate intermediate during the reaction cycle. These enzymes remove bivalent calcium ions from eukaryotic cells against very large concentration gradients and play a critical role in intracellular calcium homeostasis. The mammalian plasma membrane calcium ATPase isoforms are encoded by at least four separate genes and the diversity of these enzymes is further increased by alternative splicing of transcripts. The expression of different isoforms and splice variants is regulated in a developmental, tissue- and cell type-specific manner, suggesting that these pumps are functionally adapted to the physiological needs of particular cells and tissues. This gene encodes the plasma membrane calcium ATPase isoform 4. Alternatively spliced transcript variants encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: ATP2B4 ATPase, Ca++ transporting, plasma membrane 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=493| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Møller JV, Juul B, le Maire M |title=Structural organization, ion transport, and energy transduction of P-type ATPases. |journal=Biochim. Biophys. Acta |volume=1286 |issue= 1 |pages= 1-51 |year= 1996 |pmid= 8634322 |doi= }}
*{{cite journal | author=Strehler EE, Zacharias DA |title=Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps. |journal=Physiol. Rev. |volume=81 |issue= 1 |pages= 21-50 |year= 2001 |pmid= 11152753 |doi= }}
*{{cite journal | author=Strehler EE, Treiman M |title=Calcium pumps of plasma membrane and cell interior. |journal=Curr. Mol. Med. |volume=4 |issue= 3 |pages= 323-35 |year= 2004 |pmid= 15101689 |doi= }}
*{{cite journal | author=Heim R, Hug M, Iwata T, ''et al.'' |title=Microdiversity of human-plasma-membrane calcium-pump isoform 2 generated by alternative RNA splicing in the N-terminal coding region. |journal=Eur. J. Biochem. |volume=205 |issue= 1 |pages= 333-40 |year= 1992 |pmid= 1313367 |doi= }}
*{{cite journal | author=Brandt P, Neve RL, Kammesheidt A, ''et al.'' |title=Analysis of the tissue-specific distribution of mRNAs encoding the plasma membrane calcium-pumping ATPases and characterization of an alternately spliced form of PMCA4 at the cDNA and genomic levels. |journal=J. Biol. Chem. |volume=267 |issue= 7 |pages= 4376-85 |year= 1992 |pmid= 1531651 |doi= }}
*{{cite journal | author=Olson S, Wang MG, Carafoli E, ''et al.'' |title=Localization of two genes encoding plasma membrane Ca2(+)-transporting ATPases to human chromosomes 1q25-32 and 12q21-23. |journal=Genomics |volume=9 |issue= 4 |pages= 629-41 |year= 1991 |pmid= 1674727 |doi= }}
*{{cite journal | author=Strehler EE, James P, Fischer R, ''et al.'' |title=Peptide sequence analysis and molecular cloning reveal two calcium pump isoforms in the human erythrocyte membrane. |journal=J. Biol. Chem. |volume=265 |issue= 5 |pages= 2835-42 |year= 1990 |pmid= 2137451 |doi= }}
*{{cite journal | author=James P, Maeda M, Fischer R, ''et al.'' |title=Identification and primary structure of a calmodulin binding domain of the Ca2+ pump of human erythrocytes. |journal=J. Biol. Chem. |volume=263 |issue= 6 |pages= 2905-10 |year= 1988 |pmid= 2963820 |doi= }}
*{{cite journal | author=Brandt P, Zurini M, Neve RL, ''et al.'' |title=A C-terminal, calmodulin-like regulatory domain from the plasma membrane Ca2+-pumping ATPase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 9 |pages= 2914-8 |year= 1988 |pmid= 2966397 |doi= }}
*{{cite journal | author=Howard A, Barley NF, Legon S, Walters JR |title=Plasma-membrane calcium-pump isoforms in human and rat liver. |journal=Biochem. J. |volume=303 ( Pt 1) |issue= |pages= 275-9 |year= 1994 |pmid= 7945253 |doi= }}
*{{cite journal | author=Stauffer TP, Hilfiker H, Carafoli E, Strehler EE |title=Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes. |journal=J. Biol. Chem. |volume=269 |issue= 50 |pages= 32022 |year= 1995 |pmid= 7989379 |doi= }}
*{{cite journal | author=Stauffer TP, Hilfiker H, Carafoli E, Strehler EE |title=Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes. |journal=J. Biol. Chem. |volume=268 |issue= 34 |pages= 25993-6003 |year= 1994 |pmid= 8245032 |doi= }}
*{{cite journal | author=Váradi A, Molnár E, Ashcroft SJ |title=A unique combination of plasma membrane Ca2+-ATPase isoforms is expressed in islets of Langerhans and pancreatic beta-cell lines. |journal=Biochem. J. |volume=314 ( Pt 2) |issue= |pages= 663-9 |year= 1996 |pmid= 8670083 |doi= }}
*{{cite journal | author=Santiago-García J, Mas-Oliva J, Saavedra D, Zarain-Herzberg A |title=Analysis of mRNA expression and cloning of a novel plasma membrane Ca(2+)-ATPase splice variant in human heart. |journal=Mol. Cell. Biochem. |volume=155 |issue= 2 |pages= 173-82 |year= 1996 |pmid= 8700162 |doi= }}
*{{cite journal | author=Zacharias DA, DeMarco SJ, Strehler EE |title=mRNA expression of the four isoforms of the human plasma membrane Ca(2+)-ATPase in the human hippocampus. |journal=Brain Res. Mol. Brain Res. |volume=45 |issue= 1 |pages= 173-6 |year= 1997 |pmid= 9105688 |doi= }}
*{{cite journal | author=Dean WL, Chen D, Brandt PC, Vanaman TC |title=Regulation of platelet plasma membrane Ca2+-ATPase by cAMP-dependent and tyrosine phosphorylation. |journal=J. Biol. Chem. |volume=272 |issue= 24 |pages= 15113-9 |year= 1997 |pmid= 9182531 |doi= }}
*{{cite journal | author=Kim E, DeMarco SJ, Marfatia SM, ''et al.'' |title=Plasma membrane Ca2+ ATPase isoform 4b binds to membrane-associated guanylate kinase (MAGUK) proteins via their PDZ (PSD-95/Dlg/ZO-1) domains. |journal=J. Biol. Chem. |volume=273 |issue= 3 |pages= 1591-5 |year= 1998 |pmid= 9430700 |doi= }}
*{{cite journal | author=Guerini D, García-Martin E, Gerber A, ''et al.'' |title=The expression of plasma membrane Ca2+ pump isoforms in cerebellar granule neurons is modulated by Ca2+. |journal=J. Biol. Chem. |volume=274 |issue= 3 |pages= 1667-76 |year= 1999 |pmid= 9880546 |doi= }}
*{{cite journal | author=Rosado JA, Sage SO |title=Regulation of plasma membrane Ca2+-ATPase by small GTPases and phosphoinositides in human platelets. |journal=J. Biol. Chem. |volume=275 |issue= 26 |pages= 19529-35 |year= 2000 |pmid= 10748016 |doi= 10.1074/jbc.M001319200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CUTL1... {November 17, 2007 2:05:00 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 2:05:36 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Cut-like 1, CCAAT displacement protein (Drosophila)
| HGNCid = 2557
| Symbol = CUTL1
| AltSymbols =; CASP; CDP; COY1; CUX; Nbla10317; p100; p110; p200; p75
| OMIM = 116896
| ECnumber =
| Homologene = 22551
| MGIid = 88568
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003702 |text = RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1523
| Hs_Ensembl = ENSG00000160967
| Hs_RefseqProtein = NP_001904
| Hs_RefseqmRNA = NM_001913
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 101246011
| Hs_GenLoc_end = 101713969
| Hs_Uniprot = P39880
| Mm_EntrezGene = 13047
| Mm_Ensembl = ENSMUSG00000029705
| Mm_RefseqmRNA = NM_009986
| Mm_RefseqProtein = NP_034116
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 136532763
| Mm_GenLoc_end = 136851889
| Mm_Uniprot = P70381
}}
}}
'''Cut-like 1, CCAAT displacement protein (Drosophila)''', also known as '''CUTL1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CUTL1 cut-like 1, CCAAT displacement protein (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1523| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the homeodomain family of DNA binding proteins. It may regulate gene expression, morphogenesis, and differentiation and it may also play a role in the cell cycle progession. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: CUTL1 cut-like 1, CCAAT displacement protein (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1523| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ottolenghi S, Mantovani R, Nicolis S, ''et al.'' |title=DNA sequences regulating human globin gene transcription in nondeletional hereditary persistence of fetal hemoglobin. |journal=Hemoglobin |volume=13 |issue= 6 |pages= 523-41 |year= 1990 |pmid= 2481658 |doi= }}
*{{cite journal | author=Nepveu A |title=Role of the multifunctional CDP/Cut/Cux homeodomain transcription factor in regulating differentiation, cell growth and development. |journal=Gene |volume=270 |issue= 1-2 |pages= 1-15 |year= 2001 |pmid= 11403998 |doi= }}
*{{cite journal | author=Neufeld EJ, Skalnik DG, Lievens PM, Orkin SH |title=Human CCAAT displacement protein is homologous to the Drosophila homeoprotein, cut. |journal=Nat. Genet. |volume=1 |issue= 1 |pages= 50-5 |year= 1993 |pmid= 1301999 |doi= 10.1038/ng0492-50 }}
*{{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=Scherer SW, Neufeld EJ, Lievens PM, ''et al.'' |title=Regional localization of the CCAAT displacement protein gene (CUTL1) to 7q22 by analysis of somatic cell hybrids. |journal=Genomics |volume=15 |issue= 3 |pages= 695-6 |year= 1993 |pmid= 8468066 |doi= 10.1006/geno.1993.1130 }}
*{{cite journal | author=Chernousov MA, Stahl RC, Carey DJ |title=Schwann cells secrete a novel collagen-like adhesive protein that binds N-syndecan. |journal=J. Biol. Chem. |volume=271 |issue= 23 |pages= 13844-53 |year= 1996 |pmid= 8662884 |doi= }}
*{{cite journal | author=Lievens PM, Tufarelli C, Donady JJ, ''et al.'' |title=CASP, a novel, highly conserved alternative-splicing product of the CDP/cut/cux gene, lacks cut-repeat and homeo DNA-binding domains, and interacts with full-length CDP in vitro. |journal=Gene |volume=197 |issue= 1-2 |pages= 73-81 |year= 1997 |pmid= 9332351 |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=Chattopadhyay S, Whitehurst CE, Chen J |title=A nuclear matrix attachment region upstream of the T cell receptor beta gene enhancer binds Cux/CDP and SATB1 and modulates enhancer-dependent reporter gene expression but not endogenous gene expression. |journal=J. Biol. Chem. |volume=273 |issue= 45 |pages= 29838-46 |year= 1998 |pmid= 9792700 |doi= }}
*{{cite journal | author=Glöckner G, Scherer S, Schattevoy R, ''et al.'' |title=Large-scale sequencing of two regions in human chromosome 7q22: analysis of 650 kb of genomic sequence around the EPO and CUTL1 loci reveals 17 genes. |journal=Genome Res. |volume=8 |issue= 10 |pages= 1060-73 |year= 1998 |pmid= 9799793 |doi= }}
*{{cite journal | author=Liu J, Barnett A, Neufeld EJ, Dudley JP |title=Homeoproteins CDP and SATB1 interact: potential for tissue-specific regulation. |journal=Mol. Cell. Biol. |volume=19 |issue= 7 |pages= 4918-26 |year= 1999 |pmid= 10373541 |doi= }}
*{{cite journal | author=Rong Zeng W, Soucie E, Sung Moon N, ''et al.'' |title=Exon/intron structure and alternative transcripts of the CUTL1 gene. |journal=Gene |volume=241 |issue= 1 |pages= 75-85 |year= 2000 |pmid= 10607901 |doi= }}
*{{cite journal | author=Martin-Soudant N, Drachman JG, Kaushansky K, Nepveu A |title=CDP/Cut DNA binding activity is down-modulated in granulocytes, macrophages and erythrocytes but remains elevated in differentiating megakaryocytes. |journal=Leukemia |volume=14 |issue= 5 |pages= 863-73 |year= 2000 |pmid= 10803519 |doi= }}
*{{cite journal | author=Li S, Aufiero B, Schiltz RL, Walsh MJ |title=Regulation of the homeodomain CCAAT displacement/cut protein function by histone acetyltransferases p300/CREB-binding protein (CBP)-associated factor and CBP. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 13 |pages= 7166-71 |year= 2000 |pmid= 10852958 |doi= 10.1073/pnas.130028697 }}
*{{cite journal | author=Nirodi C, Hart J, Dhawan P, ''et al.'' |title=The role of CDP in the negative regulation of CXCL1 gene expression. |journal=J. Biol. Chem. |volume=276 |issue= 28 |pages= 26122-31 |year= 2001 |pmid= 11371564 |doi= 10.1074/jbc.M102872200 }}
*{{cite journal | author=Moon NS, Premdas P, Truscott M, ''et al.'' |title=S phase-specific proteolytic cleavage is required to activate stable DNA binding by the CDP/Cut homeodomain protein. |journal=Mol. Cell. Biol. |volume=21 |issue= 18 |pages= 6332-45 |year= 2001 |pmid= 11509674 |doi= }}
*{{cite journal | author=Santaguida M, Ding Q, Bérubé G, ''et al.'' |title=Phosphorylation of the CCAAT displacement protein (CDP)/Cux transcription factor by cyclin A-Cdk1 modulates its DNA binding activity in G(2). |journal=J. Biol. Chem. |volume=276 |issue= 49 |pages= 45780-90 |year= 2002 |pmid= 11584018 |doi= 10.1074/jbc.M107978200 }}
*{{cite journal | author=Dintilhac A, Bernués J |title=HMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid sequences. |journal=J. Biol. Chem. |volume=277 |issue= 9 |pages= 7021-8 |year= 2002 |pmid= 11748221 |doi= 10.1074/jbc.M108417200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on F11R... {November 17, 2007 2:14:10 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 2:15:09 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_F11R_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1nbq.
| PDB = {{PDB2|1nbq}}
| Name = F11 receptor
| HGNCid = 14685
| Symbol = F11R
| AltSymbols =; KAT; CD321; JAM; JAM-1; JAM-A; JAM1; JAMA; JCAM; PAM-1
| OMIM = 605721
| ECnumber =
| Homologene = 14255
| MGIid = 1321398
| GeneAtlas_image1 = PBB_GE_F11R_221664_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_F11R_222354_at_tn.png
| Function = {{GNF_GO|id=GO:0004792 |text = thiosulfate sulfurtransferase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005923 |text = tight junction}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0030855 |text = epithelial cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 50848
| Hs_Ensembl = ENSG00000158769
| Hs_RefseqProtein = NP_058642
| Hs_RefseqmRNA = NM_016946
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 159231625
| Hs_GenLoc_end = 159275404
| Hs_Uniprot = Q9Y624
| Mm_EntrezGene = 16456
| Mm_Ensembl = ENSMUSG00000038235
| Mm_RefseqmRNA = NM_172647
| Mm_RefseqProtein = NP_766235
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 173274236
| Mm_GenLoc_end = 173301268
| Mm_Uniprot = Q8VC39
}}
}}
'''F11 receptor''', also known as '''F11R''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: F11R F11 receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=50848| 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 = Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. The protein encoded by this immunoglobulin superfamily gene member is an important regulator of tight junction assembly in epithelia. In addition, the encoded protein can act as (1) a receptor for reovirus, (2) a ligand for the integrin LFA1, involved in leukocyte transmigration, and (3) a platelet receptor. Multiple transcript variants encoding two different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: F11R F11 receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=50848| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Muller WA |title=Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response. |journal=Trends Immunol. |volume=24 |issue= 6 |pages= 327-34 |year= 2003 |pmid= 12810109 |doi= }}
*{{cite journal | author=Bazzoni G |title=The JAM family of junctional adhesion molecules. |journal=Curr. Opin. Cell Biol. |volume=15 |issue= 5 |pages= 525-30 |year= 2004 |pmid= 14519386 |doi= }}
*{{cite journal | author=Naik UP, Eckfeld K |title=Junctional adhesion molecule 1 (JAM-1). |journal=J. Biol. Regul. Homeost. Agents |volume=17 |issue= 4 |pages= 341-7 |year= 2004 |pmid= 15065765 |doi= }}
*{{cite journal | author=Kornecki E, Walkowiak B, Naik UP, Ehrlich YH |title=Activation of human platelets by a stimulatory monoclonal antibody. |journal=J. Biol. Chem. |volume=265 |issue= 17 |pages= 10042-8 |year= 1990 |pmid= 2351647 |doi= }}
*{{cite journal | author=Naik UP, Ehrlich YH, Kornecki E |title=Mechanisms of platelet activation by a stimulatory antibody: cross-linking of a novel platelet receptor for monoclonal antibody F11 with the Fc gamma RII receptor. |journal=Biochem. J. |volume=310 ( Pt 1) |issue= |pages= 155-62 |year= 1995 |pmid= 7646439 |doi= }}
*{{cite journal | author=Ozaki H, Ishii K, Horiuchi H, ''et al.'' |title=Cutting edge: combined treatment of TNF-alpha and IFN-gamma causes redistribution of junctional adhesion molecule in human endothelial cells. |journal=J. Immunol. |volume=163 |issue= 2 |pages= 553-7 |year= 1999 |pmid= 10395639 |doi= }}
*{{cite journal | author=Williams LA, Martin-Padura I, Dejana E, ''et al.'' |title=Identification and characterisation of human Junctional Adhesion Molecule (JAM). |journal=Mol. Immunol. |volume=36 |issue= 17 |pages= 1175-88 |year= 2000 |pmid= 10698320 |doi= }}
*{{cite journal | author=Sobocka MB, Sobocki T, Banerjee P, ''et al.'' |title=Cloning of the human platelet F11 receptor: a cell adhesion molecule member of the immunoglobulin superfamily involved in platelet aggregation. |journal=Blood |volume=95 |issue= 8 |pages= 2600-9 |year= 2000 |pmid= 10753840 |doi= }}
*{{cite journal | author=Liu Y, Nusrat A, Schnell FJ, ''et al.'' |title=Human junction adhesion molecule regulates tight junction resealing in epithelia. |journal=J. Cell. Sci. |volume=113 ( Pt 13) |issue= |pages= 2363-74 |year= 2000 |pmid= 10852816 |doi= }}
*{{cite journal | author=Ebnet K, Schulz CU, Meyer Zu Brickwedde MK, ''et al.'' |title=Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1. |journal=J. Biol. Chem. |volume=275 |issue= 36 |pages= 27979-88 |year= 2000 |pmid= 10856295 |doi= 10.1074/jbc.M002363200 }}
*{{cite journal | author=Bazzoni G, Martinez-Estrada OM, Orsenigo F, ''et al.'' |title=Interaction of junctional adhesion molecule with the tight junction components ZO-1, cingulin, and occludin. |journal=J. Biol. Chem. |volume=275 |issue= 27 |pages= 20520-6 |year= 2000 |pmid= 10877843 |doi= 10.1074/jbc.M905251199 }}
*{{cite journal | author=Gupta SK, Pillarisetti K, Ohlstein EH |title=Platelet agonist F11 receptor is a member of the immunoglobulin superfamily and identical with junctional adhesion molecule (JAM): regulation of expression in human endothelial cells and macrophages. |journal=IUBMB Life |volume=50 |issue= 1 |pages= 51-6 |year= 2001 |pmid= 11087121 |doi= }}
*{{cite journal | author=Martinez-Estrada OM, Villa A, Breviario F, ''et al.'' |title=Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells. |journal=J. Biol. Chem. |volume=276 |issue= 12 |pages= 9291-6 |year= 2001 |pmid= 11120739 |doi= 10.1074/jbc.M006991200 }}
*{{cite journal | author=Naik UP, Naik MU, Eckfeld K, ''et al.'' |title=Characterization and chromosomal localization of JAM-1, a platelet receptor for a stimulatory monoclonal antibody. |journal=J. Cell. Sci. |volume=114 |issue= Pt 3 |pages= 539-47 |year= 2001 |pmid= 11171323 |doi= }}
*{{cite journal | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
*{{cite journal | author=Barton ES, Forrest JC, Connolly JL, ''et al.'' |title=Junction adhesion molecule is a receptor for reovirus. |journal=Cell |volume=104 |issue= 3 |pages= 441-51 |year= 2001 |pmid= 11239401 |doi= }}
*{{cite journal | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
*{{cite journal | author=Ebnet K, Suzuki A, Horikoshi Y, ''et al.'' |title=The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM). |journal=EMBO J. |volume=20 |issue= 14 |pages= 3738-48 |year= 2001 |pmid= 11447115 |doi= 10.1093/emboj/20.14.3738 }}
*{{cite journal | author=Itoh M, Sasaki H, Furuse M, ''et al.'' |title=Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions. |journal=J. Cell Biol. |volume=154 |issue= 3 |pages= 491-7 |year= 2001 |pmid= 11489913 |doi= 10.1083/jcb.200103047 }}
*{{cite journal | author=Hamazaki Y, Itoh M, Sasaki H, ''et al.'' |title=Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule. |journal=J. Biol. Chem. |volume=277 |issue= 1 |pages= 455-61 |year= 2002 |pmid= 11689568 |doi= 10.1074/jbc.M109005200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GRM1... {November 17, 2007 2:05:36 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 2:06:13 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_GRM1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ewk.
| PDB = {{PDB2|1ewk}}, {{PDB2|1ewt}}, {{PDB2|1ewv}}, {{PDB2|1isr}}, {{PDB2|1iss}}
| Name = Glutamate receptor, metabotropic 1
| HGNCid = 4593
| Symbol = GRM1
| AltSymbols =; GPRC1A; GRM1A; MGLUR1; MGLUR1A; mGlu1
| OMIM = 604473
| ECnumber =
| Homologene = 649
| MGIid = 1351338
| GeneAtlas_image1 = PBB_GE_GRM1_207299_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_GRM1_210939_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_GRM1_210940_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008067 |text = metabotropic glutamate, GABA-B-like receptor activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0030425 |text = dendrite}}
| Process = {{GNF_GO|id=GO:0000186 |text = activation of MAPKK activity}} {{GNF_GO|id=GO:0000187 |text = activation of MAPK activity}} {{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:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007626 |text = locomotory behavior}} {{GNF_GO|id=GO:0043408 |text = regulation of MAPKKK cascade}} {{GNF_GO|id=GO:0051930 |text = regulation of sensory perception of pain}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2911
| Hs_Ensembl = ENSG00000152822
| Hs_RefseqProtein = NP_000829
| Hs_RefseqmRNA = NM_000838
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 146390611
| Hs_GenLoc_end = 146800427
| Hs_Uniprot = Q13255
| Mm_EntrezGene = 14816
| Mm_Ensembl = ENSMUSG00000019828
| Mm_RefseqmRNA = XM_976537
| Mm_RefseqProtein = XP_981631
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 10378793
| Mm_GenLoc_end = 10772495
| Mm_Uniprot = Q3V0U2
}}
}}
'''Glutamate receptor, metabotropic 1''', also known as '''GRM1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GRM1 glutamate receptor, metabotropic 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2911| 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 = L-glutamate is the major excitatory neurotransmitter in the central nervous system and activates both ionotropic and metabotropic glutamate receptors. Glutamatergic neurotransmission is involved in most aspects of normal brain function and can be perturbed in many neuropathologic conditions. The metabotropic glutamate receptors are a family of G protein-coupled receptors, that have been divided into 3 groups on the basis of sequence homology, putative signal transduction mechanisms, and pharmacologic properties. Group I includes GRM1 and GRM5 and these receptors have been shown to activate phospholipase C. Group II includes GRM2 and GRM3 while Group III includes GRM4, GRM6, GRM7 and GRM8. Group II and III receptors are linked to the inhibition of the cyclic AMP cascade but differ in their agonist selectivities. Alternative splice variants of the GRM1 gene have been described but their full-length nature has not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: GRM1 glutamate receptor, metabotropic 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2911| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bockaert J, Pin JP |title=Molecular tinkering of G protein-coupled receptors: an evolutionary success. |journal=EMBO J. |volume=18 |issue= 7 |pages= 1723-9 |year= 1999 |pmid= 10202136 |doi= 10.1093/emboj/18.7.1723 }}
*{{cite journal | author=King JE, Eugenin EA, Buckner CM, Berman JW |title=HIV tat and neurotoxicity. |journal=Microbes Infect. |volume=8 |issue= 5 |pages= 1347-57 |year= 2006 |pmid= 16697675 |doi= 10.1016/j.micinf.2005.11.014 }}
*{{cite journal | author=Desai MA, Burnett JP, Mayne NG, Schoepp DD |title=Cloning and expression of a human metabotropic glutamate receptor 1 alpha: enhanced coupling on co-transfection with a glutamate transporter. |journal=Mol. Pharmacol. |volume=48 |issue= 4 |pages= 648-57 |year= 1995 |pmid= 7476890 |doi= }}
*{{cite journal | author=Scherer SW, Duvoisin RM, Kuhn R, ''et al.'' |title=Localization of two metabotropic glutamate receptor genes, GRM3 and GRM8, to human chromosome 7q. |journal=Genomics |volume=31 |issue= 2 |pages= 230-3 |year= 1997 |pmid= 8824806 |doi= 10.1006/geno.1996.0036 }}
*{{cite journal | author=Brakeman PR, Lanahan AA, O'Brien R, ''et al.'' |title=Homer: a protein that selectively binds metabotropic glutamate receptors. |journal=Nature |volume=386 |issue= 6622 |pages= 284-8 |year= 1997 |pmid= 9069287 |doi= 10.1038/386284a0 }}
*{{cite journal | author=Stephan D, Bon C, Holzwarth JA, ''et al.'' |title=Human metabotropic glutamate receptor 1: mRNA distribution, chromosome localization and functional expression of two splice variants. |journal=Neuropharmacology |volume=35 |issue= 12 |pages= 1649-60 |year= 1997 |pmid= 9076744 |doi= }}
*{{cite journal | author=Makoff AJ, Phillips T, Pilling C, Emson P |title=Expression of a novel splice variant of human mGluR1 in the cerebellum. |journal=Neuroreport |volume=8 |issue= 13 |pages= 2943-7 |year= 1997 |pmid= 9376535 |doi= }}
*{{cite journal | author=Francesconi A, Duvoisin RM |title=Role of the second and third intracellular loops of metabotropic glutamate receptors in mediating dual signal transduction activation. |journal=J. Biol. Chem. |volume=273 |issue= 10 |pages= 5615-24 |year= 1998 |pmid= 9488690 |doi= }}
*{{cite journal | author=Okamoto T, Sekiyama N, Otsu M, ''et al.'' |title=Expression and purification of the extracellular ligand binding region of metabotropic glutamate receptor subtype 1. |journal=J. Biol. Chem. |volume=273 |issue= 21 |pages= 13089-96 |year= 1998 |pmid= 9582347 |doi= }}
*{{cite journal | author=Snow BE, Hall RA, Krumins AM, ''et al.'' |title=GTPase activating specificity of RGS12 and binding specificity of an alternatively spliced PDZ (PSD-95/Dlg/ZO-1) domain. |journal=J. Biol. Chem. |volume=273 |issue= 28 |pages= 17749-55 |year= 1998 |pmid= 9651375 |doi= }}
*{{cite journal | author=Xiao B, Tu JC, Petralia RS, ''et al.'' |title=Homer regulates the association of group 1 metabotropic glutamate receptors with multivalent complexes of homer-related, synaptic proteins. |journal=Neuron |volume=21 |issue= 4 |pages= 707-16 |year= 1998 |pmid= 9808458 |doi= }}
*{{cite journal | author=Tu JC, Xiao B, Yuan JP, ''et al.'' |title=Homer binds a novel proline-rich motif and links group 1 metabotropic glutamate receptors with IP3 receptors. |journal=Neuron |volume=21 |issue= 4 |pages= 717-26 |year= 1998 |pmid= 9808459 |doi= }}
*{{cite journal | author=Ciruela F, Robbins MJ, Willis AC, McIlhinney RA |title=Interactions of the C terminus of metabotropic glutamate receptor type 1alpha with rat brain proteins: evidence for a direct interaction with tubulin. |journal=J. Neurochem. |volume=72 |issue= 1 |pages= 346-54 |year= 1999 |pmid= 9886087 |doi= }}
*{{cite journal | author=Robbins MJ, Ciruela F, Rhodes A, McIlhinney RA |title=Characterization of the dimerization of metabotropic glutamate receptors using an N-terminal truncation of mGluR1alpha. |journal=J. Neurochem. |volume=72 |issue= 6 |pages= 2539-47 |year= 1999 |pmid= 10349865 |doi= }}
*{{cite journal | author=Mody N, Hermans E, Nahorski SR, Challiss RA |title=Inhibition of N-linked glycosylation of the human type 1alpha metabotropic glutamate receptor by tunicamycin: effects on cell-surface receptor expression and function. |journal=Neuropharmacology |volume=38 |issue= 10 |pages= 1485-92 |year= 1999 |pmid= 10530810 |doi= }}
*{{cite journal | author=Francesconi A, Duvoisin RM |title=Opposing effects of protein kinase C and protein kinase A on metabotropic glutamate receptor signaling: selective desensitization of the inositol trisphosphate/Ca2+ pathway by phosphorylation of the receptor-G protein-coupling domain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 11 |pages= 6185-90 |year= 2000 |pmid= 10823959 |doi= }}
*{{cite journal | author=Ganesh S, Amano K, Yamakawa K |title=Assignment of the gene GRM1 coding for metabotropic glutamate receptor 1 to human chromosome band 6q24 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=88 |issue= 3-4 |pages= 314-5 |year= 2000 |pmid= 10828618 |doi= }}
*{{cite journal | author=Ray K, Hauschild BC |title=Cys-140 is critical for metabotropic glutamate receptor-1 dimerization. |journal=J. Biol. Chem. |volume=275 |issue= 44 |pages= 34245-51 |year= 2000 |pmid= 10945991 |doi= 10.1074/jbc.M005581200 }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GUSB... {November 17, 2007 2:06:14 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 2:06:36 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_GUSB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bhg.
| PDB = {{PDB2|1bhg}}
| Name = Glucuronidase, beta
| HGNCid = 4696
| Symbol = GUSB
| AltSymbols =; FLJ39445; MPS7
| OMIM = 253220
| ECnumber =
| Homologene = 37271
| MGIid = 95872
| GeneAtlas_image1 = PBB_GE_GUSB_202605_at_tn.png
| Function = {{GNF_GO|id=GO:0004566 |text = beta-glucuronidase activity}} {{GNF_GO|id=GO:0043169 |text = cation binding}}
| Component = {{GNF_GO|id=GO:0005764 |text = lysosome}}
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006027 |text = glycosaminoglycan catabolic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2990
| Hs_Ensembl = ENSG00000169919
| Hs_RefseqProtein = NP_000172
| Hs_RefseqmRNA = NM_000181
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 65063110
| Hs_GenLoc_end = 65084635
| Hs_Uniprot = P08236
| Mm_EntrezGene = 110006
| Mm_Ensembl = ENSMUSG00000025534
| Mm_RefseqmRNA = NM_010368
| Mm_RefseqProtein = NP_034498
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 130273725
| Mm_GenLoc_end = 130287564
| Mm_Uniprot = Q3TW82
}}
}}
'''Glucuronidase, beta''', also known as '''GUSB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GUSB glucuronidase, beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2990| 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=Bell CE, Sly WS, Brot FE |title=Human beta-glucuronidase deficiency mucopolysaccharidosis: identification of cross-reactive antigen in cultured fibroblasts of deficient patients by enzyme immunoassay. |journal=J. Clin. Invest. |volume=59 |issue= 1 |pages= 97-105 |year= 1977 |pmid= 401508 |doi= }}
*{{cite journal | author=Tanaka J, Gasa S, Sakurada K, ''et al.'' |title=Characterization of the subunits and sugar moiety of human placental and leukemic beta-glucuronidase. |journal=Biol. Chem. Hoppe-Seyler |volume=373 |issue= 1 |pages= 57-62 |year= 1992 |pmid= 1311180 |doi= }}
*{{cite journal | author=Wolfe JH, Sands MS, Barker JE, ''et al.'' |title=Reversal of pathology in murine mucopolysaccharidosis type VII by somatic cell gene transfer. |journal=Nature |volume=360 |issue= 6406 |pages= 749-53 |year= 1993 |pmid= 1465145 |doi= 10.1038/360749a0 }}
*{{cite journal | author=Tomatsu S, Fukuda S, Sukegawa K, ''et al.'' |title=Mucopolysaccharidosis type VII: characterization of mutations and molecular heterogeneity. |journal=Am. J. Hum. Genet. |volume=48 |issue= 1 |pages= 89-96 |year= 1991 |pmid= 1702266 |doi= }}
*{{cite journal | author=Shipley JM, Miller RD, Wu BM, ''et al.'' |title=Analysis of the 5' flanking region of the human beta-glucuronidase gene. |journal=Genomics |volume=10 |issue= 4 |pages= 1009-18 |year= 1991 |pmid= 1916806 |doi= }}
*{{cite journal | author=Ono M, Taniguchi N, Makita A, ''et al.'' |title=Phosphorylation of beta-glucuronidases from human normal liver and hepatoma by cAMP-dependent protein kinase. |journal=J. Biol. Chem. |volume=263 |issue= 12 |pages= 5884-9 |year= 1988 |pmid= 2833520 |doi= }}
*{{cite journal | author=Oshima A, Kyle JW, Miller RD, ''et al.'' |title=Cloning, sequencing, and expression of cDNA for human beta-glucuronidase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 3 |pages= 685-9 |year= 1987 |pmid= 3468507 |doi= }}
*{{cite journal | author=Guise KS, Korneluk RG, Waye J, ''et al.'' |title=Isolation and expression in Escherichia coli of a cDNA clone encoding human beta-glucuronidase. |journal=Gene |volume=34 |issue= 1 |pages= 105-10 |year= 1985 |pmid= 3924735 |doi= }}
*{{cite journal | author=Ho YC, Ho LH, Ho KJ |title=Human hepatic beta-glucuronidase: an enzyme kinetic study. |journal=Enzyme |volume=33 |issue= 1 |pages= 9-17 |year= 1985 |pmid= 3987656 |doi= }}
*{{cite journal | author=Shipley JM, Klinkenberg M, Wu BM, ''et al.'' |title=Mutational analysis of a patient with mucopolysaccharidosis type VII, and identification of pseudogenes. |journal=Am. J. Hum. Genet. |volume=52 |issue= 3 |pages= 517-26 |year= 1993 |pmid= 7680524 |doi= }}
*{{cite journal | author=Vervoort R, Lissens W, Liebaers I |title=Molecular analysis of a patient with hydrops fetalis caused by beta-glucuronidase deficiency, and evidence for additional pseudogenes. |journal=Hum. Mutat. |volume=2 |issue= 6 |pages= 443-5 |year= 1994 |pmid= 8111412 |doi= 10.1002/humu.1380020604 }}
*{{cite journal | author=Wu BM, Sly WS |title=Mutational studies in a patient with the hydrops fetalis form of mucopolysaccharidosis type VII. |journal=Hum. Mutat. |volume=2 |issue= 6 |pages= 446-57 |year= 1994 |pmid= 8111413 |doi= 10.1002/humu.1380020605 }}
*{{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=Moullier P, Bohl D, Heard JM, Danos O |title=Correction of lysosomal storage in the liver and spleen of MPS VII mice by implantation of genetically modified skin fibroblasts. |journal=Nat. Genet. |volume=4 |issue= 2 |pages= 154-9 |year= 1993 |pmid= 8348154 |doi= 10.1038/ng0693-154 }}
*{{cite journal | author=Shipley JM, Grubb JH, Sly WS |title=The role of glycosylation and phosphorylation in the expression of active human beta-glucuronidase. |journal=J. Biol. Chem. |volume=268 |issue= 16 |pages= 12193-8 |year= 1993 |pmid= 8505339 |doi= }}
*{{cite journal | author=Nishimura Y, Kato K, Himeno M |title=Biochemical characterization of liver microsomal, Golgi, lysosomal, and serum beta-glucuronidases in dibutyl phosphate-treated rats. |journal=J. Biochem. |volume=118 |issue= 1 |pages= 56-66 |year= 1996 |pmid= 8537326 |doi= }}
*{{cite journal | author=Jain S, Drendel WB, Chen ZW, ''et al.'' |title=Structure of human beta-glucuronidase reveals candidate lysosomal targeting and active-site motifs. |journal=Nat. Struct. Biol. |volume=3 |issue= 4 |pages= 375-81 |year= 1996 |pmid= 8599764 |doi= }}
*{{cite journal | author=Vervoort R, Islam MR, Sly WS, ''et al.'' |title=Molecular analysis of patients with beta-glucuronidase deficiency presenting as hydrops fetalis or as early mucopolysaccharidosis VII. |journal=Am. J. Hum. Genet. |volume=58 |issue= 3 |pages= 457-71 |year= 1996 |pmid= 8644704 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Dentino AR, Raj PA, De Nardin E |title=Subtle differences between human and rabbit neutrophil receptors shown by the secretagogue activity of constrained formyl peptides. |journal=Arch. Biochem. Biophys. |volume=337 |issue= 2 |pages= 267-74 |year= 1997 |pmid= 9016822 |doi= 10.1006/abbi.1996.9791 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HIPK2... {November 17, 2007 2:13:23 PM PST}
- SEARCH REDIRECT: Control Box Found: HIPK2 {November 17, 2007 2:13:45 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 2:14:04 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 2:14:04 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 2:14:04 PM PST}
- UPDATED: Updated protein page: HIPK2 {November 17, 2007 2:14:10 PM PST}
- INFO: Beginning work on HNRPC... {November 17, 2007 2:06:36 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 2:07:10 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_HNRPC_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1wf2.
| PDB = {{PDB2|1wf2}}
| Name = Heterogeneous nuclear ribonucleoprotein C (C1/C2)
| HGNCid = 5035
| Symbol = HNRPC
| AltSymbols =; C1; C2; HNRNP; MGC104306; MGC105117; MGC117353; MGC131677; SNRPC; hnRNPC
| OMIM = 164020
| ECnumber =
| Homologene = 74524
| MGIid = 107795
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005681 |text = spliceosome}}
| Process = {{GNF_GO|id=GO:0000398 |text = nuclear mRNA splicing, via spliceosome}} {{GNF_GO|id=GO:0008380 |text = RNA splicing}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3183
| Hs_Ensembl =
| Hs_RefseqProtein = NP_001070910
| Hs_RefseqmRNA = NM_001077442
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 15381
| Mm_Ensembl = ENSMUSG00000060373
| Mm_RefseqmRNA = NM_016884
| Mm_RefseqProtein = NP_058580
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 50995502
| Mm_GenLoc_end = 51025955
| Mm_Uniprot = Q3U6P5
}}
}}
'''Heterogeneous nuclear ribonucleoprotein C (C1/C2)''', also known as '''HNRPC''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HNRPC heterogeneous nuclear ribonucleoprotein C (C1/C2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3183| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene can act as a tetramer and is involved in the assembly of 40S hnRNP particles. Multiple transcript variants encoding at least two different isoforms have been described for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: HNRPC heterogeneous nuclear ribonucleoprotein C (C1/C2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3183| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Görlach M, Wittekind M, Beckman RA, ''et al.'' |title=Interaction of the RNA-binding domain of the hnRNP C proteins with RNA. |journal=EMBO J. |volume=11 |issue= 9 |pages= 3289-95 |year= 1992 |pmid= 1380452 |doi= }}
*{{cite journal | author=Wittekind M, Görlach M, Friedrichs M, ''et al.'' |title=1H, 13C, and 15N NMR assignments and global folding pattern of the RNA-binding domain of the human hnRNP C proteins. |journal=Biochemistry |volume=31 |issue= 27 |pages= 6254-65 |year= 1992 |pmid= 1385725 |doi= }}
*{{cite journal | author=Burd CG, Swanson MS, Görlach M, Dreyfuss G |title=Primary structures of the heterogeneous nuclear ribonucleoprotein A2, B1, and C2 proteins: a diversity of RNA binding proteins is generated by small peptide inserts. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 24 |pages= 9788-92 |year= 1990 |pmid= 2557628 |doi= }}
*{{cite journal | author=Merrill BM, Barnett SF, LeStourgeon WM, Williams KR |title=Primary structure differences between proteins C1 and C2 of HeLa 40S nuclear ribonucleoprotein particles. |journal=Nucleic Acids Res. |volume=17 |issue= 21 |pages= 8441-9 |year= 1989 |pmid= 2587210 |doi= }}
*{{cite journal | author=Swanson MS, Nakagawa TY, LeVan K, Dreyfuss G |title=Primary structure of human nuclear ribonucleoprotein particle C proteins: conservation of sequence and domain structures in heterogeneous nuclear RNA, mRNA, and pre-rRNA-binding proteins. |journal=Mol. Cell. Biol. |volume=7 |issue= 5 |pages= 1731-9 |year= 1987 |pmid= 3110598 |doi= }}
*{{cite journal | author=Nakagawa TY, Swanson MS, Wold BJ, Dreyfuss G |title=Molecular cloning of cDNA for the nuclear ribonucleoprotein particle C proteins: a conserved gene family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 7 |pages= 2007-11 |year= 1986 |pmid= 3457372 |doi= }}
*{{cite journal | author=Sébillon P, Beldjord C, Kaplan JC, ''et al.'' |title=A T to G mutation in the polypyrimidine tract of the second intron of the human beta-globin gene reduces in vitro splicing efficiency: evidence for an increased hnRNP C interaction. |journal=Nucleic Acids Res. |volume=23 |issue= 17 |pages= 3419-25 |year= 1995 |pmid= 7567451 |doi= }}
*{{cite journal | author=Kato S, Sekine S, Oh SW, ''et al.'' |title=Construction of a human full-length cDNA bank. |journal=Gene |volume=150 |issue= 2 |pages= 243-50 |year= 1995 |pmid= 7821789 |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=Huang M, Rech JE, Northington SJ, ''et al.'' |title=The C-protein tetramer binds 230 to 240 nucleotides of pre-mRNA and nucleates the assembly of 40S heterogeneous nuclear ribonucleoprotein particles. |journal=Mol. Cell. Biol. |volume=14 |issue= 1 |pages= 518-33 |year= 1994 |pmid= 8264621 |doi= }}
*{{cite journal | author=Hamilton BJ, Nagy E, Malter JS, ''et al.'' |title=Association of heterogeneous nuclear ribonucleoprotein A1 and C proteins with reiterated AUUUA sequences. |journal=J. Biol. Chem. |volume=268 |issue= 12 |pages= 8881-7 |year= 1993 |pmid= 8473331 |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=Romero F, Ramos-Morales F, Domínguez A, ''et al.'' |title=Grb2 and its apoptotic isoform Grb3-3 associate with heterogeneous nuclear ribonucleoprotein C, and these interactions are modulated by poly(U) RNA. |journal=J. Biol. Chem. |volume=273 |issue= 13 |pages= 7776-81 |year= 1998 |pmid= 9516488 |doi= }}
*{{cite journal | author=Neubauer G, King A, Rappsilber J, ''et al.'' |title=Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex. |journal=Nat. Genet. |volume=20 |issue= 1 |pages= 46-50 |year= 1998 |pmid= 9731529 |doi= 10.1038/1700 }}
*{{cite journal | author=Sella O, Gerlitz G, Le SY, Elroy-Stein O |title=Differentiation-induced internal translation of c-sis mRNA: analysis of the cis elements and their differentiation-linked binding to the hnRNP C protein. |journal=Mol. Cell. Biol. |volume=19 |issue= 8 |pages= 5429-40 |year= 1999 |pmid= 10409733 |doi= }}
*{{cite journal | author=Wang W, Furneaux H, Cheng H, ''et al.'' |title=HuR regulates p21 mRNA stabilization by UV light. |journal=Mol. Cell. Biol. |volume=20 |issue= 3 |pages= 760-9 |year= 2000 |pmid= 10629032 |doi= }}
*{{cite journal | author=Spångberg K, Wiklund L, Schwartz S |title=HuR, a protein implicated in oncogene and growth factor mRNA decay, binds to the 3' ends of hepatitis C virus RNA of both polarities. |journal=Virology |volume=274 |issue= 2 |pages= 378-90 |year= 2000 |pmid= 10964780 |doi= 10.1006/viro.2000.0461 }}
*{{cite journal | author=Shahied L, Braswell EH, LeStourgeon WM, Krezel AM |title=An antiparallel four-helix bundle orients the high-affinity RNA binding sites in hnRNP C: a mechanism for RNA chaperonin activity. |journal=J. Mol. Biol. |volume=305 |issue= 4 |pages= 817-28 |year= 2001 |pmid= 11162094 |doi= 10.1006/jmbi.2000.4331 }}
*{{cite journal | author=Andersen JS, Lyon CE, Fox AH, ''et al.'' |title=Directed proteomic analysis of the human nucleolus. |journal=Curr. Biol. |volume=12 |issue= 1 |pages= 1-11 |year= 2002 |pmid= 11790298 |doi= }}
*{{cite journal | author=Stone JR, Collins T |title=Rapid phosphorylation of heterogeneous nuclear ribonucleoprotein C1/C2 in response to physiologic levels of hydrogen peroxide in human endothelial cells. |journal=J. Biol. Chem. |volume=277 |issue= 18 |pages= 15621-8 |year= 2002 |pmid= 11877401 |doi= 10.1074/jbc.M112153200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LAMA3... {November 17, 2007 2:07:10 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 2:07:46 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| 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 3
| HGNCid = 6483
| Symbol = LAMA3
| AltSymbols =; E170; LAMNA; LOCS; lama3a
| OMIM = 600805
| ECnumber =
| Homologene = 18279
| MGIid = 99909
| GeneAtlas_image1 = PBB_GE_LAMA3_203726_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_LAMA3_gnf1h02350_at_tn.png
| GeneAtlas_image3 = PBB_GE_LAMA3_gnf1h02351_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0005604 |text = basement membrane}} {{GNF_GO|id=GO:0005606 |text = laminin-1 complex}}
| Process = {{GNF_GO|id=GO:0008544 |text = epidermis development}} {{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 = 3909
| Hs_Ensembl = ENSG00000053747
| Hs_RefseqProtein = NP_000218
| Hs_RefseqmRNA = NM_000227
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 18
| Hs_GenLoc_start = 19523560
| Hs_GenLoc_end = 19789025
| Hs_Uniprot = Q16787
| Mm_EntrezGene = 16774
| Mm_Ensembl = ENSMUSG00000024421
| Mm_RefseqmRNA = XM_140451
| Mm_RefseqProtein = XP_140451
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 18
| Mm_GenLoc_start = 12477560
| Mm_GenLoc_end = 12725832
| Mm_Uniprot = Q3UU65
}}
}}
'''Laminin, alpha 3''', also known as '''LAMA3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LAMA3 laminin, alpha 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3909| 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 = Laminins are basement membrane components thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. The protein encoded by this gene is the alpha-3 chain of laminin 5, which is a complex glycoprotein composed of three subunits (alpha, beta, and gamma). Laminin 5 is thought to be involved in cell adhesion, signal transduction and differentiation of keratinocytes. Mutations in this gene have been identified as the cause of Herlitz type junctional epidermolysis bullosa. Alternatively spliced transcript variants encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: LAMA3 laminin, alpha 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3909| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Timpl R |title=Macromolecular organization of basement membranes. |journal=Curr. Opin. Cell Biol. |volume=8 |issue= 5 |pages= 618-24 |year= 1997 |pmid= 8939648 |doi= }}
*{{cite journal | author=Kivirikko S, McGrath JA, Baudoin C, ''et al.'' |title=A homozygous nonsense mutation in the alpha 3 chain gene of laminin 5 (LAMA3) in lethal (Herlitz) junctional epidermolysis bullosa. |journal=Hum. Mol. Genet. |volume=4 |issue= 5 |pages= 959-62 |year= 1995 |pmid= 7633458 |doi= }}
*{{cite journal | author=Rousselle P, Golbik R, van der Rest M, Aumailley M |title=Structural requirement for cell adhesion to kalinin (laminin-5). |journal=J. Biol. Chem. |volume=270 |issue= 23 |pages= 13766-70 |year= 1995 |pmid= 7775432 |doi= }}
*{{cite journal | author=Burgeson RE, Chiquet M, Deutzmann R, ''et al.'' |title=A new nomenclature for the laminins. |journal=Matrix Biol. |volume=14 |issue= 3 |pages= 209-11 |year= 1994 |pmid= 7921537 |doi= }}
*{{cite journal | author=Ryan MC, Tizard R, VanDevanter DR, Carter WG |title=Cloning of the LamA3 gene encoding the alpha 3 chain of the adhesive ligand epiligrin. Expression in wound repair. |journal=J. Biol. Chem. |volume=269 |issue= 36 |pages= 22779-87 |year= 1994 |pmid= 8077230 |doi= }}
*{{cite journal | author=Vidal F, Baudoin C, Miquel C, ''et al.'' |title=Cloning of the laminin alpha 3 chain gene (LAMA3) and identification of a homozygous deletion in a patient with Herlitz junctional epidermolysis bullosa. |journal=Genomics |volume=30 |issue= 2 |pages= 273-80 |year= 1996 |pmid= 8586427 |doi= 10.1006/geno.1995.9877 }}
*{{cite journal | author=McGrath JA, Kivirikko S, Ciatti S, ''et al.'' |title=A recurrent homozygous nonsense mutation within the LAMA3 gene as a cause of Herlitz junctional epidermolysis bullosa in patients of Pakistani ancestry: evidence for a founder effect. |journal=J. Invest. Dermatol. |volume=106 |issue= 4 |pages= 781-4 |year= 1996 |pmid= 8618022 |doi= }}
*{{cite journal | author=Mizushima H, Miyagi Y, Kikkawa Y, ''et al.'' |title=Differential expression of laminin-5/ladsin subunits in human tissues and cancer cell lines and their induction by tumor promoter and growth factors. |journal=J. Biochem. |volume=120 |issue= 6 |pages= 1196-202 |year= 1997 |pmid= 9010770 |doi= }}
*{{cite journal | author=Miner JH, Patton BL, Lentz SI, ''et al.'' |title=The laminin alpha chains: expression, developmental transitions, and chromosomal locations of alpha1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel alpha3 isoform. |journal=J. Cell Biol. |volume=137 |issue= 3 |pages= 685-701 |year= 1997 |pmid= 9151674 |doi= }}
*{{cite journal | author=Doliana R, Bellina I, Bucciotti F, ''et al.'' |title=The human alpha3b is a 'full-sized' laminin chain variant with a more widespread tissue expression than the truncated alpha3a. |journal=FEBS Lett. |volume=417 |issue= 1 |pages= 65-70 |year= 1998 |pmid= 9395076 |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=Pulkkinen L, Cserhalmi-Friedman PB, Tang M, ''et al.'' |title=Molecular analysis of the human laminin alpha3a chain gene (LAMA3a): a strategy for mutation identification and DNA-based prenatal diagnosis in Herlitz junctional epidermolysis bullosa. |journal=Lab. Invest. |volume=78 |issue= 9 |pages= 1067-76 |year= 1998 |pmid= 9759651 |doi= }}
*{{cite journal | author=Gonzales M, Haan K, Baker SE, ''et al.'' |title=A cell signal pathway involving laminin-5, alpha3beta1 integrin, and mitogen-activated protein kinase can regulate epithelial cell proliferation. |journal=Mol. Biol. Cell |volume=10 |issue= 2 |pages= 259-70 |year= 1999 |pmid= 9950675 |doi= }}
*{{cite journal | author=Hirosaki T, Mizushima H, Tsubota Y, ''et al.'' |title=Structural requirement of carboxyl-terminal globular domains of laminin alpha 3 chain for promotion of rapid cell adhesion and migration by laminin-5. |journal=J. Biol. Chem. |volume=275 |issue= 29 |pages= 22495-502 |year= 2000 |pmid= 10801807 |doi= 10.1074/jbc.M001326200 }}
*{{cite journal | author=Amano S, Scott IC, Takahara K, ''et al.'' |title=Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 gamma 2 chain. |journal=J. Biol. Chem. |volume=275 |issue= 30 |pages= 22728-35 |year= 2000 |pmid= 10806203 |doi= 10.1074/jbc.M002345200 }}
*{{cite journal | author=Goldfinger LE, Jiang L, Hopkinson SB, ''et al.'' |title=Spatial regulation and activity modulation of plasmin by high affinity binding to the G domain of the alpha 3 subunit of laminin-5. |journal=J. Biol. Chem. |volume=275 |issue= 45 |pages= 34887-93 |year= 2001 |pmid= 10956663 |doi= 10.1074/jbc.M006652200 }}
*{{cite journal | author=Fujiwara H, Kikkawa Y, Sanzen N, Sekiguchi K |title=Purification and characterization of human laminin-8. Laminin-8 stimulates cell adhesion and migration through alpha3beta1 and alpha6beta1 integrins. |journal=J. Biol. Chem. |volume=276 |issue= 20 |pages= 17550-8 |year= 2001 |pmid= 11278628 |doi= 10.1074/jbc.M010155200 }}
*{{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=Utani A, Nomizu M, Matsuura H, ''et al.'' |title=A unique sequence of the laminin alpha 3 G domain binds to heparin and promotes cell adhesion through syndecan-2 and -4. |journal=J. Biol. Chem. |volume=276 |issue= 31 |pages= 28779-88 |year= 2001 |pmid= 11373281 |doi= 10.1074/jbc.M101420200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LOX... {November 17, 2007 2:07:46 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 2:08:10 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- 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 = Lysyl oxidase
| HGNCid = 6664
| Symbol = LOX
| AltSymbols =; MGC105112
| OMIM = 153455
| ECnumber =
| Homologene = 1741
| MGIid = 96817
| GeneAtlas_image1 = PBB_GE_LOX_215446_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_LOX_204298_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_LOX_213640_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004720 |text = protein-lysine 6-oxidase activity}} {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005581 |text = collagen}}
| Process = {{GNF_GO|id=GO:0006464 |text = protein modification process}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4015
| Hs_Ensembl = ENSG00000113083
| Hs_RefseqProtein = NP_002308
| Hs_RefseqmRNA = NM_002317
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 121429918
| Hs_GenLoc_end = 121441853
| Hs_Uniprot = P28300
| Mm_EntrezGene = 16948
| Mm_Ensembl = ENSMUSG00000024529
| Mm_RefseqmRNA = NM_010728
| Mm_RefseqProtein = NP_034858
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 18
| Mm_GenLoc_start = 52646159
| Mm_GenLoc_end = 52654698
| Mm_Uniprot = Q3TLP7
}}
}}
'''Lysyl oxidase''', also known as '''LOX''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LOX lysyl oxidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4015| 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 an extracellular copper enzyme that initiates the crosslinking of collagens and elastin. The enzyme catalyzes oxidative deamination of the epsilon-amino group in certain lysine and hydroxylysine residues of collagens and lysine residues of elastin. In addition to crosslinking extracellular matrix proteins, the encoded protein may have a role in tumor suppression.<ref name="entrez">{{cite web | title = Entrez Gene: LOX lysyl oxidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4015| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Csiszar K |title=Lysyl oxidases: a novel multifunctional amine oxidase family. |journal=Prog. Nucleic Acid Res. Mol. Biol. |volume=70 |issue= |pages= 1-32 |year= 2001 |pmid= 11642359 |doi= }}
*{{cite journal | author=Kagan HM, Li W |title=Lysyl oxidase: properties, specificity, and biological roles inside and outside of the cell. |journal=J. Cell. Biochem. |volume=88 |issue= 4 |pages= 660-72 |year= 2003 |pmid= 12577300 |doi= 10.1002/jcb.10413 }}
*{{cite journal | author=Svinarich DM, Twomey TA, Macauley SP, ''et al.'' |title=Characterization of the human lysyl oxidase gene locus. |journal=J. Biol. Chem. |volume=267 |issue= 20 |pages= 14382-7 |year= 1992 |pmid= 1352776 |doi= }}
*{{cite journal | author=Mariani TJ, Trackman PC, Kagan HM, ''et al.'' |title=The complete derived amino acid sequence of human lysyl oxidase and assignment of the gene to chromosome 5 (extensive sequence homology with the murine ras recision gene). |journal=Matrix |volume=12 |issue= 3 |pages= 242-8 |year= 1992 |pmid= 1357535 |doi= }}
*{{cite journal | author=Murawaki Y, Kusakabe Y, Hirayama C |title=Serum lysyl oxidase activity in chronic liver disease in comparison with serum levels of prolyl hydroxylase and laminin. |journal=Hepatology |volume=14 |issue= 6 |pages= 1167-73 |year= 1992 |pmid= 1683640 |doi= }}
*{{cite journal | author=Hämäläinen ER, Jones TA, Sheer D, ''et al.'' |title=Molecular cloning of human lysyl oxidase and assignment of the gene to chromosome 5q23.3-31.2. |journal=Genomics |volume=11 |issue= 3 |pages= 508-16 |year= 1992 |pmid= 1685472 |doi= }}
*{{cite journal | author=Konishi A, Iguchi H, Ochi J, ''et al.'' |title=Increased lysyl oxidase activity in culture medium of nonparenchymal cells from fibrotic livers. |journal=Gastroenterology |volume=89 |issue= 4 |pages= 709-15 |year= 1985 |pmid= 2863189 |doi= }}
*{{cite journal | author=Kuivaniemi H, Ala-Kokko L, Kivirikko KI |title=Secretion of lysyl oxidase by cultured human skin fibroblasts and effects of monensin, nigericin, tunicamycin and colchicine. |journal=Biochim. Biophys. Acta |volume=883 |issue= 2 |pages= 326-34 |year= 1986 |pmid= 2874833 |doi= }}
*{{cite journal | author=Reiser KM, Hennessy SM, Last JA |title=Analysis of age-associated changes in collagen crosslinking in the skin and lung in monkeys and rats. |journal=Biochim. Biophys. Acta |volume=926 |issue= 3 |pages= 339-48 |year= 1988 |pmid= 3120785 |doi= }}
*{{cite journal | author=Järveläinen H, Halme T, Rönnemaa T |title=Effect of cortisol on the proliferation and protein synthesis of human aortic smooth muscle cells in culture. |journal=Acta Med. Scand. Suppl. |volume=660 |issue= |pages= 114-22 |year= 1982 |pmid= 6127904 |doi= }}
*{{cite journal | author=Kuivaniemi H, Savolainen ER, Kivirikko KI |title=Human placental lysyl oxidase. Purification, partial characterization, and preparation of two specific antisera to the enzyme. |journal=J. Biol. Chem. |volume=259 |issue= 11 |pages= 6996-7002 |year= 1984 |pmid= 6144680 |doi= }}
*{{cite journal | author=Lien YH, Stern R, Fu JC, Siegel RC |title=Inhibition of collagen fibril formation in vitro and subsequent cross-linking by glucose. |journal=Science |volume=225 |issue= 4669 |pages= 1489-91 |year= 1984 |pmid= 6147899 |doi= }}
*{{cite journal | author=Yasutake A, Powers JC |title=Reactivity of human leukocyte elastase and porcine pancreatic elastase toward peptide 4-nitroanilides containing model desmosine residues. Evidence that human leukocyte elastase is selective for cross-linked regions of elastin. |journal=Biochemistry |volume=20 |issue= 13 |pages= 3675-9 |year= 1981 |pmid= 6912069 |doi= }}
*{{cite journal | author=Kim Y, Boyd CD, Csiszar K |title=A new gene with sequence and structural similarity to the gene encoding human lysyl oxidase. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7176-82 |year= 1995 |pmid= 7706256 |doi= }}
*{{cite journal | author=Hämäläinen ER, Kemppainen R, Pihlajaniemi T, Kivirikko KI |title=Structure of the human lysyl oxidase gene. |journal=Genomics |volume=17 |issue= 3 |pages= 544-8 |year= 1993 |pmid= 7902322 |doi= 10.1006/geno.1993.1369 }}
*{{cite journal | author=Forbes EG, Cronshaw AD, MacBeath JR, Hulmes DJ |title=Tyrosine-rich acidic matrix protein (TRAMP) is a tyrosine-sulphated and widely distributed protein of the extracellular matrix. |journal=FEBS Lett. |volume=351 |issue= 3 |pages= 433-6 |year= 1994 |pmid= 8082810 |doi= }}
*{{cite journal | author=Csiszar K, Mariani TJ, Gosin JS, ''et al.'' |title=A restriction fragment length polymorphism results in a nonconservative amino acid substitution encoded within the first exon of the human lysyl oxidase gene. |journal=Genomics |volume=16 |issue= 2 |pages= 401-6 |year= 1993 |pmid= 8100215 |doi= 10.1006/geno.1993.1203 }}
*{{cite journal | author=Vetter U, Weis MA, Mörike M, ''et al.'' |title=Collagen crosslinks and mineral crystallinity in bone of patients with osteogenesis imperfecta. |journal=J. Bone Miner. Res. |volume=8 |issue= 2 |pages= 133-7 |year= 1993 |pmid= 8442432 |doi= }}
*{{cite journal | author=Panchenko MV, Stetler-Stevenson WG, Trubetskoy OV, ''et al.'' |title=Metalloproteinase activity secreted by fibrogenic cells in the processing of prolysyl oxidase. Potential role of procollagen C-proteinase. |journal=J. Biol. Chem. |volume=271 |issue= 12 |pages= 7113-9 |year= 1996 |pmid= 8636146 |doi= }}
*{{cite journal | author=Khakoo A, Thomas R, Trompeter R, ''et al.'' |title=Congenital cutis laxa and lysyl oxidase deficiency. |journal=Clin. Genet. |volume=51 |issue= 2 |pages= 109-14 |year= 1997 |pmid= 9111998 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MAP2K3... {November 17, 2007 2:12:00 PM PST}
- SEARCH REDIRECT: Control Box Found: MAP2K3 {November 17, 2007 2:12:27 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 2:12:29 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 2:12:29 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 2:12:29 PM PST}
- UPDATED: Updated protein page: MAP2K3 {November 17, 2007 2:12:35 PM PST}
- INFO: Beginning work on MLLT4... {November 17, 2007 2:08:10 PM PST}
- SEARCH REDIRECT: Control Box Found: MLLT4 {November 17, 2007 2:08:54 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 2:08:55 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 2:08:55 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 2:08:55 PM PST}
- UPDATED: Updated protein page: MLLT4 {November 17, 2007 2:09:01 PM PST}
- INFO: Beginning work on MPL... {November 17, 2007 2:09:01 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 2:09:35 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- 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 = Myeloproliferative leukemia virus oncogene
| HGNCid = 7217
| Symbol = MPL
| AltSymbols =; C-MPL; CD110; MPLV; TPOR
| OMIM = 159530
| ECnumber =
| Homologene = 7845
| MGIid = 97076
| GeneAtlas_image1 = PBB_GE_MPL_211903_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_MPL_207550_at_tn.png
| GeneAtlas_image3 = PBB_GE_MPL_216825_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004896 |text = hematopoietin/interferon-class (D200-domain) cytokine receptor activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4352
| Hs_Ensembl = ENSG00000117400
| Hs_RefseqProtein = NP_005364
| Hs_RefseqmRNA = NM_005373
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 43576065
| Hs_GenLoc_end = 43591030
| Hs_Uniprot = P40238
| Mm_EntrezGene = 17480
| Mm_Ensembl = ENSMUSG00000006389
| Mm_RefseqmRNA = NM_010823
| Mm_RefseqProtein = NP_034953
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 117940347
| Mm_GenLoc_end = 117955445
| Mm_Uniprot = Q3ZB69
}}
}}
'''Myeloproliferative leukemia virus oncogene''', also known as '''MPL''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MPL myeloproliferative leukemia virus oncogene| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4352| 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 = In 1990 an oncogene, v-mpl, was identified from the murine myeloproliferative leukemia virus that was capable of immortalizing bone marrow hematopoietic cells from different lineages. In 1992 the human homologue, named, c-mpl, was cloned. Sequence data revealed that c-mpl encoded a protein that was homologous with members of the hematopoietic receptor superfamily. Presence of anti-sense oligodeoxynucleotides of c-mpl inhibited megakaryocyte colony formation. The ligand for c-mpl, thrombopoietin, was cloned in 1994. Thrombopoietin was shown to be the major regulator of megakaryocytopoiesis and platelet formation. The protein encoded by the c-mpl gene, CD110, is a 635 amino acid transmembrane domain, with two extracellular cytokine receptor domains and two intracellular cytokine receptor box motifs . TPO-R deficient mice were severely thrombocytopenic, emphasizing the important role of CD110 and thrombopoietin in megakaryocyte and platelet formation. Upon binding of thrombopoietin CD110 is dimerized and the JAK family of non-receptor tyrosine kinases, as well as the STAT family, the MAPK family, the adaptor protein Shc and the receptors themselves become tyrosine phosphorylated.<ref name="entrez">{{cite web | title = Entrez Gene: MPL myeloproliferative leukemia virus oncogene| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4352| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kato T, Matsumoto A, Ogami K, ''et al.'' |title=Native thrombopoietin: structure and function. |journal=Stem Cells |volume=16 |issue= 5 |pages= 322-8 |year= 1999 |pmid= 9766811 |doi= }}
*{{cite journal | author=Vigon I, Mornon JP, Cocault L, ''et al.'' |title=Molecular cloning and characterization of MPL, the human homolog of the v-mpl oncogene: identification of a member of the hematopoietic growth factor receptor superfamily. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 12 |pages= 5640-4 |year= 1992 |pmid= 1608974 |doi= }}
*{{cite journal | author=Souyri M, Vigon I, Penciolelli JF, ''et al.'' |title=A putative truncated cytokine receptor gene transduced by the myeloproliferative leukemia virus immortalizes hematopoietic progenitors. |journal=Cell |volume=63 |issue= 6 |pages= 1137-47 |year= 1991 |pmid= 2175677 |doi= }}
*{{cite journal | author=Le Coniat M, Souyri M, Vigon I, ''et al.'' |title=The human homolog of the myeloproliferative virus maps to chromosome band 1p34. |journal=Hum. Genet. |volume=83 |issue= 2 |pages= 194-6 |year= 1989 |pmid= 2550356 |doi= }}
*{{cite journal | author=Drachman JG, Griffin JD, Kaushansky K |title=The c-Mpl ligand (thrombopoietin) stimulates tyrosine phosphorylation of Jak2, Shc, and c-Mpl. |journal=J. Biol. Chem. |volume=270 |issue= 10 |pages= 4979-82 |year= 1995 |pmid= 7534285 |doi= }}
*{{cite journal | author=Mignotte V, Vigon I, Boucher de Crèvecoeur E, ''et al.'' |title=Structure and transcription of the human c-mpl gene (MPL). |journal=Genomics |volume=20 |issue= 1 |pages= 5-12 |year= 1994 |pmid= 8020956 |doi= }}
*{{cite journal | author=Mu SX, Xia M, Elliott G, ''et al.'' |title=Megakaryocyte growth and development factor and interleukin-3 induce patterns of protein-tyrosine phosphorylation that correlate with dominant differentiation over proliferation of mpl-transfected 32D cells. |journal=Blood |volume=86 |issue= 12 |pages= 4532-43 |year= 1996 |pmid= 8541543 |doi= }}
*{{cite journal | author=Deveaux S, Filipe A, Lemarchandel V, ''et al.'' |title=Analysis of the thrombopoietin receptor (MPL) promoter implicates GATA and Ets proteins in the coregulation of megakaryocyte-specific genes. |journal=Blood |volume=87 |issue= 11 |pages= 4678-85 |year= 1996 |pmid= 8639837 |doi= }}
*{{cite journal | author=Drachman JG, Kaushansky K |title=Dissecting the thrombopoietin receptor: functional elements of the Mpl cytoplasmic domain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 6 |pages= 2350-5 |year= 1997 |pmid= 9122198 |doi= }}
*{{cite journal | author=Ihara K, Ishii E, Eguchi M, ''et al.'' |title=Identification of mutations in the c-mpl gene in congenital amegakaryocytic thrombocytopenia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 6 |pages= 3132-6 |year= 1999 |pmid= 10077649 |doi= }}
*{{cite journal | author=Drachman JG, Millett KM, Kaushansky K |title=Thrombopoietin signal transduction requires functional JAK2, not TYK2. |journal=J. Biol. Chem. |volume=274 |issue= 19 |pages= 13480-4 |year= 1999 |pmid= 10224114 |doi= }}
*{{cite journal | author=Cargill M, Altshuler D, Ireland J, ''et al.'' |title=Characterization of single-nucleotide polymorphisms in coding regions of human genes. |journal=Nat. Genet. |volume=22 |issue= 3 |pages= 231-8 |year= 1999 |pmid= 10391209 |doi= 10.1038/10290 }}
*{{cite journal | author=Okabe S, Tauchi T, Morita H, ''et al.'' |title=Thrombopoietin induces an SH2-containing protein, CIS1, which binds to Mpl: involvement of the ubiquitin proteosome pathway. |journal=Exp. Hematol. |volume=27 |issue= 10 |pages= 1542-7 |year= 1999 |pmid= 10517496 |doi= }}
*{{cite journal | author=Miyakawa Y, Drachman JG, Gallis B, ''et al.'' |title=A structure-function analysis of serine/threonine phosphorylation of the thrombopoietin receptor, c-Mpl. |journal=J. Biol. Chem. |volume=275 |issue= 41 |pages= 32214-9 |year= 2000 |pmid= 10918061 |doi= 10.1074/jbc.M005080200 }}
*{{cite journal | author=van den Oudenrijn S, Bruin M, Folman CC, ''et al.'' |title=Mutations in the thrombopoietin receptor, Mpl, in children with congenital amegakaryocytic thrombocytopenia. |journal=Br. J. Haematol. |volume=110 |issue= 2 |pages= 441-8 |year= 2000 |pmid= 10971406 |doi= }}
*{{cite journal | author=Wang Q, Miyakawa Y, Fox N, Kaushansky K |title=Interferon-alpha directly represses megakaryopoiesis by inhibiting thrombopoietin-induced signaling through induction of SOCS-1. |journal=Blood |volume=96 |issue= 6 |pages= 2093-9 |year= 2000 |pmid= 10979953 |doi= }}
*{{cite journal | author=Miyakawa Y, Rojnuckarin P, Habib T, Kaushansky K |title=Thrombopoietin induces phosphoinositol 3-kinase activation through SHP2, Gab, and insulin receptor substrate proteins in BAF3 cells and primary murine megakaryocytes. |journal=J. Biol. Chem. |volume=276 |issue= 4 |pages= 2494-502 |year= 2001 |pmid= 11054408 |doi= 10.1074/jbc.M002633200 }}
*{{cite journal | author=Tonelli R, Scardovi AL, Pession A, ''et al.'' |title=Compound heterozygosity for two different amino-acid substitution mutations in the thrombopoietin receptor (c-mpl gene) in congenital amegakaryocytic thrombocytopenia (CAMT). |journal=Hum. Genet. |volume=107 |issue= 3 |pages= 225-33 |year= 2000 |pmid= 11071383 |doi= }}
*{{cite journal | author=Ballmaier M, Germeshausen M, Schulze H, ''et al.'' |title=c-mpl mutations are the cause of congenital amegakaryocytic thrombocytopenia. |journal=Blood |volume=97 |issue= 1 |pages= 139-46 |year= 2001 |pmid= 11133753 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NOX1... {November 17, 2007 2:12:36 PM PST}
- SEARCH REDIRECT: Control Box Found: NOX1 {November 17, 2007 2:13:14 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 2:13:16 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 2:13:16 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 2:13:16 PM PST}
- UPDATED: Updated protein page: NOX1 {November 17, 2007 2:13:23 PM PST}
- INFO: Beginning work on NRF1... {November 17, 2007 2:09:35 PM PST}
- SEARCH REDIRECT: Control Box Found: NRF1 {November 17, 2007 2:10:05 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 2:10:07 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 2:10:07 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 2:10:07 PM PST}
- UPDATED: Updated protein page: NRF1 {November 17, 2007 2:10:14 PM PST}
- INFO: Beginning work on NTRK3... {November 17, 2007 2:10:14 PM PST}
- SEARCH REDIRECT: Control Box Found: NTRK3 {November 17, 2007 2:10:53 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 2:10:55 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 2:10:55 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 2:10:55 PM PST}
- UPDATED: Updated protein page: NTRK3 {November 17, 2007 2:11:02 PM PST}
- INFO: Beginning work on PKLR... {November 17, 2007 2:11:02 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 2:11:31 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_PKLR_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1liu.
| PDB = {{PDB2|1liu}}, {{PDB2|1liw}}, {{PDB2|1lix}}, {{PDB2|1liy}}
| Name = Pyruvate kinase, liver and RBC
| HGNCid = 9020
| Symbol = PKLR
| AltSymbols =; PK1; PKL; RPK
| OMIM = 609712
| ECnumber =
| Homologene = 37286
| MGIid = 97604
| GeneAtlas_image1 = PBB_GE_PKLR_207858_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PKLR_210451_at_tn.png
| GeneAtlas_image3 = PBB_GE_PKLR_222078_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004743 |text = pyruvate kinase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}}
| Process = {{GNF_GO|id=GO:0006096 |text = glycolysis}} {{GNF_GO|id=GO:0051707 |text = response to other organism}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5313
| Hs_Ensembl = ENSG00000143627
| Hs_RefseqProtein = NP_000289
| Hs_RefseqmRNA = NM_000298
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 153526254
| Hs_GenLoc_end = 153537849
| Hs_Uniprot = P30613
| Mm_EntrezGene = 18770
| Mm_Ensembl = ENSMUSG00000041237
| Mm_RefseqmRNA = NM_013631
| Mm_RefseqProtein = NP_038659
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 89222069
| Mm_GenLoc_end = 89231560
| Mm_Uniprot = Q3UEH4
}}
}}
'''Pyruvate kinase, liver and RBC''', also known as '''PKLR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PKLR pyruvate kinase, liver and RBC| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5313| 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 pyruvate kinase that catalyzes the production of phohsphoenolpyruvate from pyruvate and ATP. Defects in this enzyme, due to gene mutations or genetic variations, are the common cause of chronic hereditary nonspherocytic hemolytic anemia (CNSHA or HNSHA). Alternatively spliced transcript variants encoding distinct isoforms have been described.<ref name="entrez">{{cite web | title = Entrez Gene: PKLR pyruvate kinase, liver and RBC| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5313| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Beutler E, Baronciani L |title=Mutations in pyruvate kinase. |journal=Hum. Mutat. |volume=7 |issue= 1 |pages= 1-6 |year= 1996 |pmid= 8664896 |doi= 10.1002/(SICI)1098-1004(1996)7:1<1::AID-HUMU1>3.0.CO;2-H }}
*{{cite journal | author=Baronciani L, Bianchi P, Zanella A |title=Hematologically important mutations: red cell pyruvate kinase (2nd update). |journal=Blood Cells Mol. Dis. |volume=24 |issue= 3 |pages= 273-9 |year= 1999 |pmid= 10087985 |doi= 10.1006/bcmd.1998.0193 }}
*{{cite journal | author=Zanella A, Fermo E, Bianchi P, ''et al.'' |title=Pyruvate kinase deficiency: the genotype-phenotype association. |journal=Blood Rev. |volume=21 |issue= 4 |pages= 217-31 |year= 2007 |pmid= 17360088 |doi= 10.1016/j.blre.2007.01.001 }}
*{{cite journal | author=Kanno H, Fujii H, Miwa S |title=Structural analysis of human pyruvate kinase L-gene and identification of the promoter activity in erythroid cells. |journal=Biochem. Biophys. Res. Commun. |volume=188 |issue= 2 |pages= 516-23 |year= 1992 |pmid= 1445295 |doi= }}
*{{cite journal | author=Kanno H, Fujii H, Hirono A, ''et al.'' |title=Identical point mutations of the R-type pyruvate kinase (PK) cDNA found in unrelated PK variants associated with hereditary hemolytic anemia. |journal=Blood |volume=79 |issue= 5 |pages= 1347-50 |year= 1992 |pmid= 1536957 |doi= }}
*{{cite journal | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi= }}
*{{cite journal | author=Kanno H, Fujii H, Hirono A, Miwa S |title=cDNA cloning of human R-type pyruvate kinase and identification of a single amino acid substitution (Thr384----Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 18 |pages= 8218-21 |year= 1991 |pmid= 1896471 |doi= }}
*{{cite journal | author=Neubauer B, Lakomek M, Winkler H, ''et al.'' |title=Point mutations in the L-type pyruvate kinase gene of two children with hemolytic anemia caused by pyruvate kinase deficiency. |journal=Blood |volume=77 |issue= 9 |pages= 1871-5 |year= 1991 |pmid= 2018831 |doi= }}
*{{cite journal | author=Tani K, Fujii H, Nagata S, Miwa S |title=Human liver type pyruvate kinase: complete amino acid sequence and the expression in mammalian cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 6 |pages= 1792-5 |year= 1988 |pmid= 3126495 |doi= }}
*{{cite journal | author=Satoh H, Tani K, Yoshida MC, ''et al.'' |title=The human liver-type pyruvate kinase (PKL) gene is on chromosome 1 at band q21. |journal=Cytogenet. Cell Genet. |volume=47 |issue= 3 |pages= 132-3 |year= 1988 |pmid= 3378452 |doi= }}
*{{cite journal | author=Tani K, Fujii H, Tsutsumi H, ''et al.'' |title=Human liver type pyruvate kinase: cDNA cloning and chromosomal assignment. |journal=Biochem. Biophys. Res. Commun. |volume=143 |issue= 2 |pages= 431-8 |year= 1987 |pmid= 3566732 |doi= }}
*{{cite journal | author=Baronciani L, Beutler E |title=Molecular study of pyruvate kinase deficient patients with hereditary nonspherocytic hemolytic anemia. |journal=J. Clin. Invest. |volume=95 |issue= 4 |pages= 1702-9 |year= 1995 |pmid= 7706479 |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=Kanno H, Ballas SK, Miwa S, ''et al.'' |title=Molecular abnormality of erythrocyte pyruvate kinase deficiency in the Amish. |journal=Blood |volume=83 |issue= 8 |pages= 2311-6 |year= 1994 |pmid= 8161798 |doi= }}
*{{cite journal | author=Lenzner C, Nürnberg P, Thiele BJ, ''et al.'' |title=Mutations in the pyruvate kinase L gene in patients with hereditary hemolytic anemia. |journal=Blood |volume=83 |issue= 10 |pages= 2817-22 |year= 1994 |pmid= 8180378 |doi= }}
*{{cite journal | author=Kanno H, Fujii H, Tsujino G, Miwa S |title=Molecular basis of impaired pyruvate kinase isozyme conversion in erythroid cells: a single amino acid substitution near the active site and decreased mRNA content of the R-type PK. |journal=Biochem. Biophys. Res. Commun. |volume=192 |issue= 1 |pages= 46-52 |year= 1993 |pmid= 8476433 |doi= 10.1006/bbrc.1993.1379 }}
*{{cite journal | author=Kanno H, Fujii H, Miwa S |title=Low substrate affinity of pyruvate kinase variant (PK Sapporo) caused by a single amino acid substitution (426 Arg-->Gln) associated with hereditary hemolytic anemia. |journal=Blood |volume=81 |issue= 9 |pages= 2439-41 |year= 1993 |pmid= 8481523 |doi= }}
*{{cite journal | author=Baronciani L, Beutler E |title=Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 9 |pages= 4324-7 |year= 1993 |pmid= 8483951 |doi= }}
*{{cite journal | author=Baronciani L, Bianchi P, Zanella A |title=Hematologically important mutations: red cell pyruvate kinase. |journal=Blood Cells Mol. Dis. |volume=22 |issue= 1 |pages= 85-9 |year= 1996 |pmid= 8807089 |doi= 10.1006/bcmd.1996.0012 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PLEC1... {November 17, 2007 2:11:31 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 2:12:00 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_PLEC1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1mb8.
| PDB = {{PDB2|1mb8}}, {{PDB2|1sh5}}, {{PDB2|1sh6}}, {{PDB2|2odu}}, {{PDB2|2odv}}
| Name = Plectin 1, intermediate filament binding protein 500kDa
| HGNCid = 9069
| Symbol = PLEC1
| AltSymbols =; HD1; PCN; EBS1; EBSO; PLEC1b; PLTN
| OMIM = 601282
| ECnumber =
| Homologene = 384
| MGIid = 1277961
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0008307 |text = structural constituent of muscle}}
| Component = {{GNF_GO|id=GO:0005626 |text = insoluble fraction}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005882 |text = intermediate filament}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0043292 |text = contractile fiber}}
| Process = {{GNF_GO|id=GO:0007016 |text = cytoskeletal anchoring}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5339
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000436
| Hs_RefseqmRNA = NM_000445
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 18810
| Mm_Ensembl = ENSMUSG00000022565
| Mm_RefseqmRNA = XM_994758
| Mm_RefseqProtein = XP_999852
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 75998231
| Mm_GenLoc_end = 76058633
| Mm_Uniprot = Q6S390
}}
}}
'''Plectin 1, intermediate filament binding protein 500kDa''', also known as '''PLEC1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PLEC1 plectin 1, intermediate filament binding protein 500kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5339| 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 product of this gene belongs to the plakin or cytolinker family of genes. The encoded protein is involved in cytoskeleton-membrane attachment in epithelial cells, muscle, and other tissues. It also may regulate changes of lymphocyte cytoarchitecture during polarization and extravasation. This gene has alternative splicing of different 5' exons to the first constant exon, which generates transcript variants that encode distinct isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: PLEC1 plectin 1, intermediate filament binding protein 500kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5339| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Pfendner E, Rouan F, Uitto J |title=Progress in epidermolysis bullosa: the phenotypic spectrum of plectin mutations. |journal=Exp. Dermatol. |volume=14 |issue= 4 |pages= 241-9 |year= 2005 |pmid= 15810881 |doi= 10.1111/j.0906-6705.2005.00324.x }}
*{{cite journal | author=Foisner R, Traub P, Wiche G |title=Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 9 |pages= 3812-6 |year= 1991 |pmid= 2023931 |doi= }}
*{{cite journal | author=Herrmann H, Wiche G |title=Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin. |journal=J. Biol. Chem. |volume=262 |issue= 3 |pages= 1320-5 |year= 1987 |pmid= 3027087 |doi= }}
*{{cite journal | author=Malecz N, Foisner R, Stadler C, Wiche G |title=Identification of plectin as a substrate of p34cdc2 kinase and mapping of a single phosphorylation site. |journal=J. Biol. Chem. |volume=271 |issue= 14 |pages= 8203-8 |year= 1996 |pmid= 8626512 |doi= }}
*{{cite journal | author=Liu CG, Maercker C, Castañon MJ, ''et al.'' |title=Human plectin: organization of the gene, sequence analysis, and chromosome localization (8q24). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 9 |pages= 4278-83 |year= 1996 |pmid= 8633055 |doi= }}
*{{cite journal | author=Gache Y, Chavanas S, Lacour JP, ''et al.'' |title=Defective expression of plectin/HD1 in epidermolysis bullosa simplex with muscular dystrophy. |journal=J. Clin. Invest. |volume=97 |issue= 10 |pages= 2289-98 |year= 1996 |pmid= 8636409 |doi= }}
*{{cite journal | author=Smith FJ, Eady RA, Leigh IM, ''et al.'' |title=Plectin deficiency results in muscular dystrophy with epidermolysis bullosa. |journal=Nat. Genet. |volume=13 |issue= 4 |pages= 450-7 |year= 1996 |pmid= 8696340 |doi= 10.1038/ng0896-450 }}
*{{cite journal | author=McLean WH, Pulkkinen L, Smith FJ, ''et al.'' |title=Loss of plectin causes epidermolysis bullosa with muscular dystrophy: cDNA cloning and genomic organization. |journal=Genes Dev. |volume=10 |issue= 14 |pages= 1724-35 |year= 1996 |pmid= 8698233 |doi= }}
*{{cite journal | author=Nikolic B, Mac Nulty E, Mir B, Wiche G |title=Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions. |journal=J. Cell Biol. |volume=134 |issue= 6 |pages= 1455-67 |year= 1996 |pmid= 8830774 |doi= }}
*{{cite journal | author=Pulkkinen L, Smith FJ, Shimizu H, ''et al.'' |title=Homozygous deletion mutations in the plectin gene (PLEC1) in patients with epidermolysis bullosa simplex associated with late-onset muscular dystrophy. |journal=Hum. Mol. Genet. |volume=5 |issue= 10 |pages= 1539-46 |year= 1997 |pmid= 8894687 |doi= }}
*{{cite journal | author=Gress TM, Müller-Pillasch F, Geng M, ''et al.'' |title=A pancreatic cancer-specific expression profile. |journal=Oncogene |volume=13 |issue= 8 |pages= 1819-30 |year= 1996 |pmid= 8895530 |doi= }}
*{{cite journal | author=Andrä K, Nikolic B, Stöcher M, ''et al.'' |title=Not just scaffolding: plectin regulates actin dynamics in cultured cells. |journal=Genes Dev. |volume=12 |issue= 21 |pages= 3442-51 |year= 1998 |pmid= 9808630 |doi= }}
*{{cite journal | author=Banwell BL, Russel J, Fukudome T, ''et al.'' |title=Myopathy, myasthenic syndrome, and epidermolysis bullosa simplex due to plectin deficiency. |journal=J. Neuropathol. Exp. Neurol. |volume=58 |issue= 8 |pages= 832-46 |year= 1999 |pmid= 10446808 |doi= }}
*{{cite journal | author=Geerts D, Fontao L, Nievers MG, ''et al.'' |title=Binding of integrin alpha6beta4 to plectin prevents plectin association with F-actin but does not interfere with intermediate filament binding. |journal=J. Cell Biol. |volume=147 |issue= 2 |pages= 417-34 |year= 1999 |pmid= 10525545 |doi= }}
*{{cite journal | author=Stegh AH, Herrmann H, Lampel S, ''et al.'' |title=Identification of the cytolinker plectin as a major early in vivo substrate for caspase 8 during CD95- and tumor necrosis factor receptor-mediated apoptosis. |journal=Mol. Cell. Biol. |volume=20 |issue= 15 |pages= 5665-79 |year= 2000 |pmid= 10891503 |doi= }}
*{{cite journal | author=Bauer JW, Rouan F, Kofler B, ''et al.'' |title=A compound heterozygous one amino-acid insertion/nonsense mutation in the plectin gene causes epidermolysis bullosa simplex with plectin deficiency. |journal=Am. J. Pathol. |volume=158 |issue= 2 |pages= 617-25 |year= 2001 |pmid= 11159198 |doi= }}
*{{cite journal | author=Henzler T, Harmache A, Herrmann H, ''et al.'' |title=Fully functional, naturally occurring and C-terminally truncated variant human immunodeficiency virus (HIV) Vif does not bind to HIV Gag but influences intermediate filament structure. |journal=J. Gen. Virol. |volume=82 |issue= Pt 3 |pages= 561-73 |year= 2001 |pmid= 11172097 |doi= }}
*{{cite journal | author=Nakano A, Pulkkinen L, Murrell D, ''et al.'' |title=Epidermolysis bullosa with congenital pyloric atresia: novel mutations in the beta 4 integrin gene (ITGB4) and genotype/phenotype correlations. |journal=Pediatr. Res. |volume=49 |issue= 5 |pages= 618-26 |year= 2001 |pmid= 11328943 |doi= }}
*{{cite journal | author=Brown MJ, Hallam JA, Liu Y, ''et al.'' |title=Cutting edge: integration of human T lymphocyte cytoskeleton by the cytolinker plectin. |journal=J. Immunol. |volume=167 |issue= 2 |pages= 641-5 |year= 2001 |pmid= 11441066 |doi= }}
*{{cite journal | author=Koss-Harnes D, Høyheim B, Anton-Lamprecht I, ''et al.'' |title=A site-specific plectin mutation causes dominant epidermolysis bullosa simplex Ogna: two identical de novo mutations. |journal=J. Invest. Dermatol. |volume=118 |issue= 1 |pages= 87-93 |year= 2002 |pmid= 11851880 |doi= 10.1046/j.0022-202x.2001.01591.x }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SIRPA... {November 17, 2007 2:15:09 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 2:16:01 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Signal-regulatory protein alpha
| HGNCid = 9662
| Symbol = SIRPA
| AltSymbols =; P84; BIT; CD172A; MFR; MYD-1; PTPNS1; SHPS-1; SHPS1; SIRP; SIRP-ALPHA-1; SIRPalpha; SIRPalpha2
| OMIM = 602461
| ECnumber =
| Homologene = 7246
| MGIid = 108563
| GeneAtlas_image1 = PBB_GE_SIRPA_202896_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SIRPA_202895_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_SIRPA_202897_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 140885
| Hs_Ensembl = ENSG00000198053
| Hs_RefseqProtein = NP_001035111
| Hs_RefseqmRNA = NM_001040022
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 1823425
| Hs_GenLoc_end = 1868543
| Hs_Uniprot = P78324
| Mm_EntrezGene = 19261
| Mm_Ensembl = ENSMUSG00000037902
| Mm_RefseqmRNA = NM_007547
| Mm_RefseqProtein = NP_031573
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 129284355
| Mm_GenLoc_end = 129323669
| Mm_Uniprot = P97797
}}
}}
'''Signal-regulatory protein alpha''', also known as '''SIRPA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SIRPA signal-regulatory protein alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=140885| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the signal-regulatory-protein (SIRP) family, and also belongs to the immunoglobulin superfamily. SIRP family members are receptor-type transmembrane glycoproteins known to be involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. This protein can be phosphorylated by tyrosine kinases. The phospho-tyrosine residues of this PTP have been shown to recruit SH2 domain containing tyrosine phosphatases (PTP), and serve as substrates of PTPs. This protein was found to participate in signal transduction mediated by various growth factor receptors. CD47 has been demonstrated to be a ligand for this receptor protein. This gene and its product share very high similarity with several other members of the SIRP family. These related genes are located in close proximity to each other on chromosome 20p13. Multiple alternatively spliced transcript variants have been determined for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: SIRPA signal-regulatory protein alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=140885| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Oldenborg PA |title=Role of CD47 in erythroid cells and in autoimmunity. |journal=Leuk. Lymphoma |volume=45 |issue= 7 |pages= 1319-27 |year= 2004 |pmid= 15359629 |doi= 10.1080/1042819042000201989 }}
*{{cite journal | author=Margolis RL, Breschel TS, Li SH, ''et al.'' |title=Characterization of cDNA clones containing CCA trinucleotide repeats derived from human brain. |journal=Somat. Cell Mol. Genet. |volume=21 |issue= 4 |pages= 279-84 |year= 1996 |pmid= 8525433 |doi= }}
*{{cite journal | author=Ohnishi H, Kubota M, Ohtake A, ''et al.'' |title=Activation of protein-tyrosine phosphatase SH-PTP2 by a tyrosine-based activation motif of a novel brain molecule. |journal=J. Biol. Chem. |volume=271 |issue= 41 |pages= 25569-74 |year= 1996 |pmid= 8810330 |doi= }}
*{{cite journal | author=Fujioka Y, Matozaki T, Noguchi T, ''et al.'' |title=A novel membrane glycoprotein, SHPS-1, that binds the SH2-domain-containing protein tyrosine phosphatase SHP-2 in response to mitogens and cell adhesion. |journal=Mol. Cell. Biol. |volume=16 |issue= 12 |pages= 6887-99 |year= 1997 |pmid= 8943344 |doi= }}
*{{cite journal | author=Kharitonenkov A, Chen Z, Sures I, ''et al.'' |title=A family of proteins that inhibit signalling through tyrosine kinase receptors. |journal=Nature |volume=386 |issue= 6621 |pages= 181-6 |year= 1997 |pmid= 9062191 |doi= 10.1038/386181a0 }}
*{{cite journal | author=Yamao T, Matozaki T, Amano K, ''et al.'' |title=Mouse and human SHPS-1: molecular cloning of cDNAs and chromosomal localization of genes. |journal=Biochem. Biophys. Res. Commun. |volume=231 |issue= 1 |pages= 61-7 |year= 1997 |pmid= 9070220 |doi= 10.1006/bbrc.1996.6047 }}
*{{cite journal | author=Sano S, Ohnishi H, Omori A, ''et al.'' |title=BIT, an immune antigen receptor-like molecule in the brain. |journal=FEBS Lett. |volume=411 |issue= 2-3 |pages= 327-34 |year= 1997 |pmid= 9271230 |doi= }}
*{{cite journal | author=Brooke GP, Parsons KR, Howard CJ |title=Cloning of two members of the SIRP alpha family of protein tyrosine phosphatase binding proteins in cattle that are expressed on monocytes and a subpopulation of dendritic cells and which mediate binding to CD4 T cells. |journal=Eur. J. Immunol. |volume=28 |issue= 1 |pages= 1-11 |year= 1998 |pmid= 9485180 |doi= }}
*{{cite journal | author=Timms JF, Carlberg K, Gu H, ''et al.'' |title=Identification of major binding proteins and substrates for the SH2-containing protein tyrosine phosphatase SHP-1 in macrophages. |journal=Mol. Cell. Biol. |volume=18 |issue= 7 |pages= 3838-50 |year= 1998 |pmid= 9632768 |doi= }}
*{{cite journal | author=Veillette A, Thibaudeau E, Latour S |title=High expression of inhibitory receptor SHPS-1 and its association with protein-tyrosine phosphatase SHP-1 in macrophages. |journal=J. Biol. Chem. |volume=273 |issue= 35 |pages= 22719-28 |year= 1998 |pmid= 9712903 |doi= }}
*{{cite journal | author=Jiang P, Lagenaur CF, Narayanan V |title=Integrin-associated protein is a ligand for the P84 neural adhesion molecule. |journal=J. Biol. Chem. |volume=274 |issue= 2 |pages= 559-62 |year= 1999 |pmid= 9872987 |doi= }}
*{{cite journal | author=Ohnishi H, Yamada M, Kubota M, ''et al.'' |title=Tyrosine phosphorylation and association of BIT with SHP-2 induced by neurotrophins. |journal=J. Neurochem. |volume=72 |issue= 4 |pages= 1402-8 |year= 1999 |pmid= 10098842 |doi= }}
*{{cite journal | author=Timms JF, Swanson KD, Marie-Cardine A, ''et al.'' |title=SHPS-1 is a scaffold for assembling distinct adhesion-regulated multi-protein complexes in macrophages. |journal=Curr. Biol. |volume=9 |issue= 16 |pages= 927-30 |year= 1999 |pmid= 10469599 |doi= }}
*{{cite journal | author=Seiffert M, Cant C, Chen Z, ''et al.'' |title=Human signal-regulatory protein is expressed on normal, but not on subsets of leukemic myeloid cells and mediates cellular adhesion involving its counterreceptor CD47. |journal=Blood |volume=94 |issue= 11 |pages= 3633-43 |year= 1999 |pmid= 10572074 |doi= }}
*{{cite journal | author=Sano S, Ohnishi H, Kubota M |title=Gene structure of mouse BIT/SHPS-1. |journal=Biochem. J. |volume=344 Pt 3 |issue= |pages= 667-75 |year= 2000 |pmid= 10585853 |doi= }}
*{{cite journal | author=Yang J, Cheng Z, Niu T, ''et al.'' |title=Structural basis for substrate specificity of protein-tyrosine phosphatase SHP-1. |journal=J. Biol. Chem. |volume=275 |issue= 6 |pages= 4066-71 |year= 2000 |pmid= 10660565 |doi= }}
*{{cite journal | author=Stofega MR, Argetsinger LS, Wang H, ''et al.'' |title=Negative regulation of growth hormone receptor/JAK2 signaling by signal regulatory protein alpha. |journal=J. Biol. Chem. |volume=275 |issue= 36 |pages= 28222-9 |year= 2000 |pmid= 10842184 |doi= 10.1074/jbc.M004238200 }}
*{{cite journal | author=Wu CJ, Chen Z, Ullrich A, ''et al.'' |title=Inhibition of EGFR-mediated phosphoinositide-3-OH kinase (PI3-K) signaling and glioblastoma phenotype by signal-regulatory proteins (SIRPs). |journal=Oncogene |volume=19 |issue= 35 |pages= 3999-4010 |year= 2000 |pmid= 10962556 |doi= 10.1038/sj.onc.1203748 }}
*{{cite journal | author=Latour S, Tanaka H, Demeure C, ''et al.'' |title=Bidirectional negative regulation of human T and dendritic cells by CD47 and its cognate receptor signal-regulator protein-alpha: down-regulation of IL-12 responsiveness and inhibition of dendritic cell activation. |journal=J. Immunol. |volume=167 |issue= 5 |pages= 2547-54 |year= 2001 |pmid= 11509594 |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 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TPP1... {November 17, 2007 2:04:21 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 2:05:00 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 = Tripeptidyl peptidase I
| HGNCid = 2073
| Symbol = TPP1
| AltSymbols =; CLN2; GIG1; LPIC; MGC21297; TPP I
| OMIM = 607998
| ECnumber =
| Homologene = 335
| MGIid = 1336194
| GeneAtlas_image1 = PBB_GE_TPP1_200743_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_TPP1_200742_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_TPP1_214196_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004177 |text = aminopeptidase activity}} {{GNF_GO|id=GO:0004252 |text = serine-type endopeptidase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0019131 |text = tripeptidyl-peptidase I activity}}
| Component = {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005764 |text = lysosome}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0007040 |text = lysosome organization and biogenesis}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0030163 |text = protein catabolic process}} {{GNF_GO|id=GO:0043171 |text = peptide catabolic process}} {{GNF_GO|id=GO:0045453 |text = bone resorption}} {{GNF_GO|id=GO:0045862 |text = positive regulation of proteolysis}} {{GNF_GO|id=GO:0050885 |text = regulation of balance}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1200
| Hs_Ensembl = ENSG00000166340
| Hs_RefseqProtein = NP_000382
| Hs_RefseqmRNA = NM_000391
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 6590576
| Hs_GenLoc_end = 6597236
| Hs_Uniprot = O14773
| Mm_EntrezGene = 12751
| Mm_Ensembl = ENSMUSG00000030894
| Mm_RefseqmRNA = NM_009906
| Mm_RefseqProtein = NP_034036
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 105618668
| Mm_GenLoc_end = 105626028
| Mm_Uniprot = Q3TDY6
}}
}}
'''Tripeptidyl peptidase I''', also known as '''TPP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TPP1 tripeptidyl peptidase I| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1200| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the sedolisin family of serine proteases. The protease functions in the lysosome to cleave N-terminal tripeptides from substrates, and has weaker endopeptidase activity. It is synthesized as a catalytically-inactive enzyme which is activated and auto-proteolyzed upon acidification. Mutations in this gene result in late-infantile neuronal ceroid lipofuscinosis, which is associated with the failure to degrade specific neuropeptides and a subunit of ATP synthase in the lysosome.<ref name="entrez">{{cite web | title = Entrez Gene: TPP1 tripeptidyl peptidase I| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1200| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Mole SE, Mitchison HM, Munroe PB |title=Molecular basis of the neuronal ceroid lipofuscinoses: mutations in CLN1, CLN2, CLN3, and CLN5. |journal=Hum. Mutat. |volume=14 |issue= 3 |pages= 199-215 |year= 1999 |pmid= 10477428 |doi= 10.1002/(SICI)1098-1004(1999)14:3<199::AID-HUMU3>3.0.CO;2-A }}
*{{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=Hofmann SL, Atashband A, Cho SK, ''et al.'' |title=Neuronal ceroid lipofuscinoses caused by defects in soluble lysosomal enzymes (CLN1 and CLN2). |journal=Curr. Mol. Med. |volume=2 |issue= 5 |pages= 423-37 |year= 2003 |pmid= 12125808 |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=Page AE, Fuller K, Chambers TJ, Warburton MJ |title=Purification and characterization of a tripeptidyl peptidase I from human osteoclastomas: evidence for its role in bone resorption. |journal=Arch. Biochem. Biophys. |volume=306 |issue= 2 |pages= 354-9 |year= 1993 |pmid= 8215436 |doi= }}
*{{cite journal | author=Sleat DE, Donnelly RJ, Lackland H, ''et al.'' |title=Association of mutations in a lysosomal protein with classical late-infantile neuronal ceroid lipofuscinosis. |journal=Science |volume=277 |issue= 5333 |pages= 1802-5 |year= 1997 |pmid= 9295267 |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=Liu CG, Sleat DE, Donnelly RJ, Lobel P |title=Structural organization and sequence of CLN2, the defective gene in classical late infantile neuronal ceroid lipofuscinosis. |journal=Genomics |volume=50 |issue= 2 |pages= 206-12 |year= 1998 |pmid= 9653647 |doi= 10.1006/geno.1998.5328 }}
*{{cite journal | author=Rawlings ND, Barrett AJ |title=Tripeptidyl-peptidase I is apparently the CLN2 protein absent in classical late-infantile neuronal ceroid lipofuscinosis. |journal=Biochim. Biophys. Acta |volume=1429 |issue= 2 |pages= 496-500 |year= 1999 |pmid= 9989235 |doi= }}
*{{cite journal | author=Vines DJ, Warburton MJ |title=Classical late infantile neuronal ceroid lipofuscinosis fibroblasts are deficient in lysosomal tripeptidyl peptidase I. |journal=FEBS Lett. |volume=443 |issue= 2 |pages= 131-5 |year= 1999 |pmid= 9989590 |doi= }}
*{{cite journal | author=Sleat DE, Gin RM, Sohar I, ''et al.'' |title=Mutational analysis of the defective protease in classic late-infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder. |journal=Am. J. Hum. Genet. |volume=64 |issue= 6 |pages= 1511-23 |year= 1999 |pmid= 10330339 |doi= }}
*{{cite journal | author=Junaid MA, Wu G, Pullarkat RK |title=Purification and characterization of bovine brain lysosomal pepstatin-insensitive proteinase, the gene product deficient in the human late-infantile neuronal ceroid lipofuscinosis. |journal=J. Neurochem. |volume=74 |issue= 1 |pages= 287-94 |year= 2000 |pmid= 10617131 |doi= }}
*{{cite journal | author=Ezaki J, Takeda-Ezaki M, Oda K, Kominami E |title=Characterization of endopeptidase activity of tripeptidyl peptidase-I/CLN2 protein which is deficient in classical late infantile neuronal ceroid lipofuscinosis. |journal=Biochem. Biophys. Res. Commun. |volume=268 |issue= 3 |pages= 904-8 |year= 2000 |pmid= 10679303 |doi= 10.1006/bbrc.2000.2207 }}
*{{cite journal | author=Haines JL, Boustany RM, Alroy J, ''et al.'' |title=Chromosomal localization of two genes underlying late-infantile neuronal ceroid lipofuscinosis. |journal=Neurogenetics |volume=1 |issue= 3 |pages= 217-22 |year= 2000 |pmid= 10737126 |doi= }}
*{{cite journal | author=Ezaki J, Takeda-Ezaki M, Kominami E |title=Tripeptidyl peptidase I, the late infantile neuronal ceroid lipofuscinosis gene product, initiates the lysosomal degradation of subunit c of ATP synthase. |journal=J. Biochem. |volume=128 |issue= 3 |pages= 509-16 |year= 2000 |pmid= 10965052 |doi= }}
*{{cite journal | author=Lin L, Sohar I, Lackland H, Lobel P |title=The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH. |journal=J. Biol. Chem. |volume=276 |issue= 3 |pages= 2249-55 |year= 2001 |pmid= 11054422 |doi= 10.1074/jbc.M008562200 }}
*{{cite journal | author=Lam CW, Poon PM, Tong SF, Ko CH |title=Two novel CLN2 gene mutations in a Chinese patient with classical late-infantile neuronal ceroid lipofuscinosis. |journal=Am. J. Med. Genet. |volume=99 |issue= 2 |pages= 161-3 |year= 2001 |pmid= 11241479 |doi= }}
*{{cite journal | author=Zhong N, Moroziewicz DN, Ju W, ''et al.'' |title=Heterogeneity of late-infantile neuronal ceroid lipofuscinosis. |journal=Genet. Med. |volume=2 |issue= 6 |pages= 312-8 |year= 2001 |pmid= 11339651 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TUBB... {November 17, 2007 2:16:01 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 2:16:29 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_TUBB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ffx.
| PDB = {{PDB2|1ffx}}, {{PDB2|1ia0}}, {{PDB2|1jff}}, {{PDB2|1sa0}}, {{PDB2|1sa1}}, {{PDB2|1tub}}, {{PDB2|1tvk}}, {{PDB2|1z2b}}, {{PDB2|2hxf}}, {{PDB2|2hxh}}
| Name = Tubulin, beta
| HGNCid = 20778
| Symbol = TUBB
| AltSymbols =; TUBB5; TUBB1; M40; MGC117247; MGC16435; OK/SW-cl.56
| OMIM = 191130
| ECnumber =
| Homologene = 69099
| MGIid = 107812
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005525 |text = GTP binding}} {{GNF_GO|id=GO:0042288 |text = MHC class I protein binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005874 |text = microtubule}} {{GNF_GO|id=GO:0043234 |text = protein complex}}
| Process = {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0007018 |text = microtubule-based movement}} {{GNF_GO|id=GO:0042267 |text = natural killer cell mediated cytotoxicity}} {{GNF_GO|id=GO:0051227 |text = spindle assembly}} {{GNF_GO|id=GO:0051258 |text = protein polymerization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 203068
| Hs_Ensembl =
| Hs_RefseqProtein = NP_821133
| Hs_RefseqmRNA = NM_178014
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 22154
| Mm_Ensembl = ENSMUSG00000001525
| Mm_RefseqmRNA = NM_011655
| Mm_RefseqProtein = NP_035785
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 35442860
| Mm_GenLoc_end = 35446285
| Mm_Uniprot = Q3TFB6
}}
}}
'''Tubulin, beta''', also known as '''TUBB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TUBB tubulin, beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=203068| accessdate = }}</ref>
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==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Berrieman HK, Lind MJ, Cawkwell L |title=Do beta-tubulin mutations have a role in resistance to chemotherapy? |journal=Lancet Oncol. |volume=5 |issue= 3 |pages= 158-64 |year= 2004 |pmid= 15003198 |doi= 10.1016/S1470-2045(04)01411-1 }}
*{{cite journal | author=Horisberger MA |title=Interferon-induced human protein MxA is a GTPase which binds transiently to cellular proteins. |journal=J. Virol. |volume=66 |issue= 8 |pages= 4705-9 |year= 1992 |pmid= 1629950 |doi= }}
*{{cite journal | author=Wang D, Villasante A, Lewis SA, Cowan NJ |title=The mammalian beta-tubulin repertoire: hematopoietic expression of a novel, heterologous beta-tubulin isotype. |journal=J. Cell Biol. |volume=103 |issue= 5 |pages= 1903-10 |year= 1987 |pmid= 3782288 |doi= }}
*{{cite journal | author=Lee MG, Lewis SA, Wilde CD, Cowan NJ |title=Evolutionary history of a multigene family: an expressed human beta-tubulin gene and three processed pseudogenes. |journal=Cell |volume=33 |issue= 2 |pages= 477-87 |year= 1983 |pmid= 6688039 |doi= }}
*{{cite journal | author=Hall JL, Dudley L, Dobner PR, ''et al.'' |title=Identification of two human beta-tubulin isotypes. |journal=Mol. Cell. Biol. |volume=3 |issue= 5 |pages= 854-62 |year= 1983 |pmid= 6865944 |doi= }}
*{{cite journal | author=Volz A, Weiss E, Trowsdale J, Ziegler A |title=Presence of an expressed beta-tubulin gene (TUBB) in the HLA class I region may provide the genetic basis for HLA-linked microtubule dysfunction. |journal=Hum. Genet. |volume=93 |issue= 1 |pages= 42-6 |year= 1994 |pmid= 8270253 |doi= }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi= }}
*{{cite journal | author=Kinnunen T, Kaksonen M, Saarinen J, ''et al.'' |title=Cortactin-Src kinase signaling pathway is involved in N-syndecan-dependent neurite outgrowth. |journal=J. Biol. Chem. |volume=273 |issue= 17 |pages= 10702-8 |year= 1998 |pmid= 9553134 |doi= }}
*{{cite journal | author=Niethammer M, Valtschanoff JG, Kapoor TM, ''et al.'' |title=CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90. |journal=Neuron |volume=20 |issue= 4 |pages= 693-707 |year= 1998 |pmid= 9581762 |doi= }}
*{{cite journal | author=Rasmussen RK, Ji H, Eddes JS, ''et al.'' |title=Two-dimensional electrophoretic analysis of mixed lineage kinase 2 N-terminal domain binding proteins. |journal=Electrophoresis |volume=19 |issue= 5 |pages= 809-17 |year= 1998 |pmid= 9629920 |doi= 10.1002/elps.1150190535 }}
*{{cite journal | author=Ciruela F, Robbins MJ, Willis AC, McIlhinney RA |title=Interactions of the C terminus of metabotropic glutamate receptor type 1alpha with rat brain proteins: evidence for a direct interaction with tubulin. |journal=J. Neurochem. |volume=72 |issue= 1 |pages= 346-54 |year= 1999 |pmid= 9886087 |doi= }}
*{{cite journal | author=Chau MF, Radeke MJ, de Inés C, ''et al.'' |title=The microtubule-associated protein tau cross-links to two distinct sites on each alpha and beta tubulin monomer via separate domains. |journal=Biochemistry |volume=37 |issue= 51 |pages= 17692-703 |year= 1999 |pmid= 9922135 |doi= }}
*{{cite journal | author=Piredda L, Farrace MG, Lo Bello M, ''et al.'' |title=Identification of 'tissue' transglutaminase binding proteins in neural cells committed to apoptosis. |journal=FASEB J. |volume=13 |issue= 2 |pages= 355-64 |year= 1999 |pmid= 9973324 |doi= }}
*{{cite journal | author=Feng Y, Hodge DR, Palmieri G, ''et al.'' |title=Association of polo-like kinase with alpha-, beta- and gamma-tubulins in a stable complex. |journal=Biochem. J. |volume=339 ( Pt 2) |issue= |pages= 435-42 |year= 1999 |pmid= 10191277 |doi= }}
*{{cite journal | author=Martín L, Fanarraga ML, Aloria K, Zabala JC |title=Tubulin folding cofactor D is a microtubule destabilizing protein. |journal=FEBS Lett. |volume=470 |issue= 1 |pages= 93-5 |year= 2000 |pmid= 10722852 |doi= }}
*{{cite journal | author=Tarazona R, López-Lluch G, Galiani MD, ''et al.'' |title=HLA-B2702 (77-83/83-77) peptide binds to beta-tubulin on human NK cells and blocks their cytotoxic capacity. |journal=J. Immunol. |volume=165 |issue= 12 |pages= 6776-82 |year= 2001 |pmid= 11120798 |doi= }}
*{{cite journal | author=Bonnet C, Boucher D, Lazereg S, ''et al.'' |title=Differential binding regulation of microtubule-associated proteins MAP1A, MAP1B, and MAP2 by tubulin polyglutamylation. |journal=J. Biol. Chem. |volume=276 |issue= 16 |pages= 12839-48 |year= 2001 |pmid= 11278895 |doi= 10.1074/jbc.M011380200 }}
*{{cite journal | author=Crabtree DV, Ojima I, Geng X, Adler AJ |title=Tubulins in the primate retina: evidence that xanthophylls may be endogenous ligands for the paclitaxel-binding site. |journal=Bioorg. Med. Chem. |volume=9 |issue= 8 |pages= 1967-76 |year= 2001 |pmid= 11504633 |doi= }}
*{{cite journal | author=Ivings L, Pennington SR, Jenkins R, ''et al.'' |title=Identification of Ca2+-dependent binding partners for the neuronal calcium sensor protein neurocalcin delta: interaction with actin, clathrin and tubulin. |journal=Biochem. J. |volume=363 |issue= Pt 3 |pages= 599-608 |year= 2002 |pmid= 11964161 |doi= }}
}}
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